LOCUS       WP_010394775             294 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dienelactone hydrolase family protein [unclassified
            Janthinobacterium].
ACCESSION   WP_010394775
VERSION     WP_010394775.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..294
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30701
     Region          65..289
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 msdmitdces llgqsslsgp dgrrgflkva lgagfavavl pvaaqsvikt dsaglvtgsm
       61 svmvdgqavp vyaaqpegkt glpvvlvise ifgvhehiad marrfakqgy lalapdlfvr
      121 qgdptkvasi pellkgiiak tpdaqvmadl davvawakqn ggdtsrlait gfcwggritw
      181 lyaahnqavk agvawygrlv geptplqpsn pidiaatlkv pvlglyggkd tgisqesiak
      241 mqealakggk qsqfvvypda ghafnadyra syvaadakdg yarclawfkt hgva
//
LOCUS       WP_010394807             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Paracoccus].
ACCESSION   WP_010394807
VERSION     WP_010394807.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..268
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29153
     Region          1..258
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mkgrglraya liyllflyap illlpifafn sgtviafplr gittewfaqm wgnaslrral
       61 fnsltiavss svlatclgif aarastrfef pgkgpimgli mlplvlpeii vsisllvvll
      121 slgvklsvlt viightlicm pyatvilsta fnsldrslee aaydlgetrw safrlvilpl
      181 vmpgiissll msftisldef iiafflagne ptlptyifsq lrfpkqipai malgtvlvll
      241 svvlltiaey frrrgiartg akdtggfl
//
LOCUS       WP_010395022             103 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ETC complex I subunit [Paracoccus].
ACCESSION   WP_010395022
VERSION     WP_010395022.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10521567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..103
                     /product="ETC complex I subunit"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_process="GO:0001932 - regulation of protein
                     phosphorylation [Evidence IEA]"
                     /GO_process="GO:0006120 - mitochondrial electron
                     transport, NADH to ubiquinone [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /GO_process="GO:0032981 - mitochondrial respiratory chain
                     complex I assembly [Evidence IEA]"
                     /GO_process="GO:0042776 - proton motive force-driven
                     mitochondrial ATP synthesis [Evidence IEA]"
                     /GO_process="GO:0072593 - reactive oxygen species
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=11972
     Region          2..94
                     /region_name="NDUS4"
                     /note="NADH dehydrogenase ubiquinone Fe-S protein 4;
                     pfam04800"
                     /db_xref="CDD:461433"
ORIGIN      
        1 mrvriykpar namqsgtart kewllvfppa eareidplmg wtssddtqsq vrlrfetrkq
       61 aedyarengl eyevvephtr apnirprgyg enfanerrap wth
//
LOCUS       WP_010395238             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Paracoccus].
ACCESSION   WP_010395238
VERSION     WP_010395238.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..218
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23015
     Region          12..215
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mlrelkserk gpakadsvvv flhgygadga dllgladpla phlpgaafya pnapercvnn
       61 pmgyqwfpip wmdgsseeqa rssatqsfnd inafldkvlt deglpasrla vvgfsqgtmm
      121 alavapqree eiagvvgfsg rlldpenvaa rvrppillvh gdqdpvvpfe smsvagealq
      181 kagftvyghv mkgtghgisp dglsvalafl kerfaate
//
LOCUS       WP_010395242             211 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Paracoccus].
ACCESSION   WP_010395242
VERSION     WP_010395242.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..211
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23525
     Region          4..205
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mkdayslils aidngiyrpg drlveselae rfgvsrtpvr ealqrletqs mlkrdgrsli
       61 vatldhnqla elytvraele alaarlaarh atpeevrvla gmveedrail gdpqalvran
      121 rrfhhqihla shnrylvqql glvhrsmalm artslaaqgr dvvtldehqa ivdaiaahds
      181 araeealrhh ismafetrlk eearhleege g
//
LOCUS       WP_010395272             337 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Paracoccus].
ACCESSION   WP_010395272
VERSION     WP_010395272.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..337
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37058
     Region          28..337
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpdivpavtp apaaipppsq prpqrylfll ldrftmisfa aaieplrlan rlagrelydw
       61 rligedgkaa tcsngarlml dsgltetarg dtvlvcggld vpraasrqvl awlrrearrg
      121 trigalctga wvlaeaglld grrctihwen qdgfaekfpd vtlirtvfve dgnrltaagg
      181 taaidmilrq iardhgpela grvadqmiht airseedqqr lsipprlgar hprlaqvvar
      241 meaniedpis parlateagl sprqlerlfa rylgrspkrh ymelrlerar nlllqtemsv
      301 meialacgfa saahfskcyr atygctpyre rgaasgr
//
LOCUS       WP_010395302             493 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleobase:cation symporter-2 family protein
            [unclassified Paracoccus (in: a-proteobacteria)].
ACCESSION   WP_010395302
VERSION     WP_010395302.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paracoccus (in: a-proteobacteria)
  ORGANISM  unclassified Paracoccus (in: a-proteobacteria)
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="unclassified Paracoccus (in: a-proteobacteria)"
                     /db_xref="taxon:2688777"
     Protein         1..493
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51450
     Region          26..473
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mqnldtspgf dpveeriaap rlfalgfqhv lvmyagaiav plivgralql spqdvaflis
       61 adlfvcgivt iiqsfgatqw fgirlpvmmg vtfaavgpmv aiasanpgqe garmmfgaim
      121 aagvisiffa pivsrllrff psvvtgtvil vigvslmpvg inwifglpvg ptapqlvdpa
      181 aqawleaara agevpasvkl mptmpnpeya sveriiigit vlaailliar yargfvania
      241 vllgivigga laavmgmmhf dgiaeaawfa pikplhfgtp ifdpvmivtm llvmfvtmie
      301 stgmflalsd icgrrmtpqa lsaglrvdgl gtaigglfnt fpytsfsqnv glvgvtgvrs
      361 rfvcvaggai mivlglipkm galveslptt vlggaglvmf gmvaatgiri lstvdfkgnr
      421 hnlfivavsl glgmvpmiap dfnqwlphsl htlihsgill aavaavglnw ffngaphase
      481 eelaaaahas eah
//
LOCUS       WP_010395310             298 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Paracoccus (in: a-proteobacteria)].
ACCESSION   WP_010395310
VERSION     WP_010395310.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paracoccus (in: a-proteobacteria)
  ORGANISM  unclassified Paracoccus (in: a-proteobacteria)
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="unclassified Paracoccus (in: a-proteobacteria)"
                     /db_xref="taxon:2688777"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33350
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mpyleslrvf vrvvelgsit aggrdlrmsp avasnrikdl etrfgvrlln rttrklvpte
       61 vgrafydnar rvietldeae avvsgfsgnp hgalrvtapl glgrrliapl vpkfcdeypg
      121 velrlrlsdr nvdiiadgid lafflgepqd salkwrriae crralvatpe ylekhghper
      181 pedltshncl llryprspey ywvlqtpegp qkllvngkfd addgdvlsgw amagrgivnr
      241 pryevaehla agrlvevlpq fppipsqfgv ltphrrlqdp kvrlfadfia revrglfg
//
LOCUS       WP_010395323             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor [Paracoccus].
ACCESSION   WP_010395323
VERSION     WP_010395323.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..219
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24530
     Region          16..210
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mnrdnmpkds qqdqpvvfvv dddrsvrdal edllasvglg smlfassqef lqaerpdapa
       61 clvldvrmpg lsgldfqdel arqglhipiv fitahgdipm svramkggai efltkpfrdq
      121 dlldaiqqgi ardrirrqee avrqdlrrry aslnqgerav mdlvikglln kqiagmldvs
      181 eitvkvrrgr vmrkigaqsl adlvrfaeri headrgwrd
//
LOCUS       WP_010395418             336 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Paracoccus sp. TRP].
ACCESSION   WP_010395418
VERSION     WP_010395418.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..336
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36466
     Region          1..327
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtlkigvigt gaigqdhtrr inevlagarv talndvnran aetcqrqyap earifddpha
       61 lirdadvdav lvcswgqthe eyvlaavaag kpcfcekpla ttaegarriv eaeqaagkrl
      121 vqvgfmrryd pgyvalkkav sevtgaplmv haahrnprvg enyvtpmaih dtliheidvl
      181 rwlldddyts arvffprksp raheklrdpq vvvletaggv vidveifvnc hygydiqcei
      241 vgedgiarlp epmgiqtrsg avlgqpilmd wkdrfidsyd yeladflkaa aqgtaagpta
      301 wdgyvaavta dacvaaqeae gqavsidlpv rpslya
//
LOCUS       WP_010395506             226 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [unclassified Paracoccus (in: a-proteobacteria)].
ACCESSION   WP_010395506
VERSION     WP_010395506.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paracoccus (in: a-proteobacteria)
  ORGANISM  unclassified Paracoccus (in: a-proteobacteria)
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="unclassified Paracoccus (in: a-proteobacteria)"
                     /db_xref="taxon:2688777"
     Protein         1..226
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24978
     Region          13..220
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtktlglgdl ewfadltpqq laqiesmmrr rhfaqgqlif errdpgetvf fvlsgnvlav
       61 hwtstgreiv ysdigpgnac gelsvlsgep rslslyarna ctlyelpgaa llelmdsqps
      121 vrraitlhli rrvhaltdrv heltslsvee rlrawllrta ldrgglkpgr vlpdvpthae
      181 ianivganre aisrglakln regviesgrr tlrilrpeal fsnpae
//
LOCUS       WP_010395581             260 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Paracoccus].
ACCESSION   WP_010395581
VERSION     WP_010395581.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..260
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28274
     Region          1..251
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mkrvwswaal ilgglyfllp ligtiefslr mrrgeyslda yrsvlsdanf ratfsysvvm
       61 alltivlgvl ivvptaywvr lrlprlrpvi efitllplvi paivvvfgyi rlyntssvlp
      121 ltgtasgtnl lllcgyatla lpymyravdt glstldvrsl teaaqslgag wtriigrlil
      181 pnvlgavmsg aflsfaivig eftmaallnr pafgpymqll ganrayepaa laviafavtw
      241 gcmgvmqlis rlfgtripak
//
LOCUS       WP_010395663             417 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter permease [Paracoccus].
ACCESSION   WP_010395663
VERSION     WP_010395663.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 417)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..417
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=46180
     Region          1..417
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mvtytgadhp pfrlsmliyd rryrsltlqa ivfilvmvma swlidntlrn lsamgktlsf
       61 dflfrragyd ipqqlipyns ddthlrativ gllntllvsl lgciaatvlg vvvgvlrlss
      121 nwliarlmti yvevfrnipv llwilvclai ftevmpapna yrgenpaaqm ilfdliaptn
      181 rytaipslgm tnppgtialg reaiswalia yvvvivvawi awrrlrvwaq avqdrtgtrp
      241 ttwwislaif avplllltwy fglhlvppvl rgfnfadgin ldnalvvlwl altlytgafi
      301 aeivrggila vsrgqteaaf alglrprrtm slvvlpqalr vivpplisqy lnltknssla
      361 iavgymdlrg tlggttlnqt gremecmvlm mgiylalsli isggmnifns rvklker
//
LOCUS       WP_010395671             350 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RluA family pseudouridine synthase [Paracoccus].
ACCESSION   WP_010395671
VERSION     WP_010395671.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..350
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=37931
     Region          16..72
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(17,29..30,32..33,35..36,39..40,42,49..50,51..55,57)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          95..332
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 msgvqtirvs adegdqridr wlkkrfpqlt qgavekwcrt gqlrvdggrv kantrieagq
       61 evrvpplpva asgpvparpr aavkqsdaem iqscvlwrde hiialnkppg lpsqggsgqg
      121 drhvdgltaa lmfgykdrpk lvhrldkdts gvlllartdr iarslseafr hrltrkiywa
      181 avagvpsprm gsikyglvka pgrgrggege kmmtvhpsav astegakrah tdfavldalg
      241 srtawvamvp vtgrthqlra hmagighpiv gdgkyggsgq enpgdgwgaq lggeisrklh
      301 lharmirfeh pitkklitvt aplpdhmvrt wktlgwsend vpedpfaeat
//
LOCUS       WP_010395738             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SH3 domain-containing protein [Paracoccus].
ACCESSION   WP_010395738
VERSION     WP_010395738.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..231
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24963
     Region          91..231
                     /region_name="SH3"
                     /note="SH3-like domain [Function unknown]; COG3807"
                     /db_xref="CDD:443020"
ORIGIN      
        1 mvaplfqsra afgkvpamrg rhktpnkqdg qmkqgqawlg tailaagaif gtaalgqttn
       61 pgekldskei gglsadatis rnqdgerdpn rgpvtnlplp ryvslkgdeg narrgpslsh
      121 ridwvfrhag mplrvvaefg qwrrvedqdg aggwvhysll sgvrtaivtr dmldllsrpe
      181 pranviarae agaivrlhec nidwcrvsgg gekgwvpkta iwgvdadeir d
//
LOCUS       WP_010395789              58 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Trm112 family protein [Janthinobacterium].
ACCESSION   WP_010395789
VERSION     WP_010395789.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium
  ORGANISM  Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae.
REFERENCE   1  (residues 1 to 58)
  AUTHORS   van Tran,N., Muller,L., Ross,R.L., Lestini,R., Letoquart,J.,
            Ulryck,N., Limbach,P.A., de Crecy-Lagard,V., Cianferani,S. and
            Graille,M.
  TITLE     Evolutionary insights into Trm112-methyltransferase holoenzymes
            involved in translation between archaea and eukaryotes
  JOURNAL   Nucleic Acids Res 46 (16), 8483-8499 (2018)
   PUBMED   30010922
REFERENCE   2  (residues 1 to 58)
  AUTHORS   Bourgeois,G., Letoquart,J., van Tran,N. and Graille,M.
  TITLE     Trm112, a Protein Activator of Methyltransferases Modifying Actors
            of the Eukaryotic Translational Apparatus
  JOURNAL   Biomolecules 7 (1), 7 (2017)
   PUBMED   28134793
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006712
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..58
                     /organism="Janthinobacterium"
                     /db_xref="taxon:29580"
     Protein         1..58
                     /product="Trm112 family protein"
                     /calculated_mol_wt=6446
     Region          1..56
                     /region_name="Trm112"
                     /note="RNA methyltransferase activator Trm112/YbaR
                     [Translation, ribosomal structure and biogenesis];
                     COG2835"
                     /db_xref="CDD:442083"
ORIGIN      
        1 mdarlldilv cpvckgpleh dkkaqelicr adrlaypird gipimwadea rtlqdave
//
LOCUS       WP_010395790             248 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Paracoccus sp. TRP].
ACCESSION   WP_010395790
VERSION     WP_010395790.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..248
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25681
     Region          1..248
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mtdillmlaa gflggmlnav agggtfitfp alvasgvpvv sanatstvaa lpgylsaalg
       61 frreiaqidr slvlrltfwt viggiagscl llvssneafa vlvpflllaa tsvfiwgaqv
      121 rewagrhrna vapfgagtmv pvaiyggyfn gglgivllal falwgmtqln qmnglknwls
      181 falsvisfai faaggqvawk paavmsvgti lggylgapva rripipalra liaaigfgmt
      241 avffwrlf
//
LOCUS       WP_010395895             356 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Paracoccus].
ACCESSION   WP_010395895
VERSION     WP_010395895.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..356
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38523
     Region          11..331
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mnrrdsnlav rlqtgflgvi afglilfllv qarfiliclv laiiifslts daisafarlk
       61 vpnwlattla liaiaigllw aatavvaqvn evvsisitya draqvalarl sqewgpnvqe
      121 aigtfmgnid fagwlrsaaa qasnlisgsv liltfvgfmf seriwfpiki erltgdptra
      181 qqvletvhki mrrvnrylvv kaaisavtam liwaifrieg lelagavaml tfilnfiptl
      241 gsiiatvitf amvlaqtgdp attltvgglt vavqfiignv fdpmllgqtl rlssfgivls
      301 lafwgviwgi agtflavpim vaimivcaqi pwlrpvaiml sqeglpeqep ttrlrr
//
LOCUS       WP_010396135             369 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PhoH family protein [Paracoccus].
ACCESSION   WP_010396135
VERSION     WP_010396135.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..369
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=40472
     Region          15..326
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 mgltpthpat atpgetllef hdnrllidlc gphdrhlari eealkvhilr rgnllsvvgp
       61 adaqaeaaqv lgalyarleq grpvemaeve aalrmgsetm aesptpaeql emfqtgpiel
      121 rtrkktvepr tdaqkdyvra lfanelafgi gpagtgktyl avavgvtmli gghvdriils
      181 rpaveagerl gflpgdmkek vdpymqplyd alndflpakq vqklmeekri eiaplafmrg
      241 rtltnsfvvl deaqnattmq mkmfltrlge gsrmvitgdr tqidlprgvh sglvdaeril
      301 kdikgisfsy ftakdvvrhs lvariieayd aeaeaaqarg elfdergqri prrepriage
      361 gavrgtrdg
//
LOCUS       WP_010396137             245 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paracoccus sp. TRP].
ACCESSION   WP_010396137
VERSION     WP_010396137.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..245
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26402
     Region          1..232
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mlavrglska fgqkqvldsv dldlaegesl vviggsgtgk svllrcilgl evpdageilw
       61 rgrplaqhra dfmddfgmlf qnaalfdslp vwrnvafrql rhmpkarara iaieklarvg
      121 lgpevadlyp aelsggmrkr aglaraiaad prviffdept tgldpiraaa inalirgivd
      181 etgataitit hdmssvraia drvalldrgr lrwqgpvsei dragddylrd fiagrarpma
      241 rvpas
//
LOCUS       WP_010396178             227 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M48 family metallopeptidase [Paracoccus].
ACCESSION   WP_010396178
VERSION     WP_010396178.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..227
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=25058
     Region          1..222
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mdrilvggdi pvtlrrsara rrmtlrvtra ggevvltlps raslaagraf aesraewlrn
       61 tragmpplql aepgallpve grlrrivpaa trrielagda ilvpehrpag vvveaflkhl
      121 aqarlapacd rhaaalgrgf qalvlrdtrs rwgscthdgr lmfswrlama ppevldyvaa
      181 hevahlahmd hspafwaata rlrpdyarqr awlrahghel qawrfrg
//
LOCUS       WP_010396189             393 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Paracoccus].
ACCESSION   WP_010396189
VERSION     WP_010396189.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..393
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42264
     Region          43..391
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mttgempkpt satapnptaa lrqgqkqvgl rlhrpplltn isaarwllla ivaasvyffh
       61 gflvpvlaas vialaswplr draafqlnlg rtgaatllvl vlvcfllipi amaliyafre
      121 lrdwinwaim inssgaptpa wmvelpqigd wldenwqnyv grpggiseiv qlvsgsniga
      181 iyrgavtagt lafhlaltll fmlitlfvly rdgdrivaqi dqvgrrilpd rwerlsrvvp
      241 atisstvtgm tliaigegvv lglaywlagv pspvtfgvit gfmalipgga plcftlvsay
      301 laasgspvag aalflwgtce lfvvdktirp vlvggpvklp flptffglig gvktmgivgl
      361 fvgpvlmall vsiwrewqre laeeeqrqaa rie
//
LOCUS       WP_010396239             424 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein,
            partial [Paracoccus sp. TRP].
ACCESSION   WP_010396239
VERSION     WP_010396239.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..>424
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          9..424
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 marapllqlt disltfggnp vfselnmtvq qgdrlalvgr ngsgkstlmk vmaglvepds
       61 gevitpagtq vgymeqdpdl sgfatlgdfa ragldegegy rvemaaeglk fdpdrpvata
      121 sggerrraal armlaqapdl mlldeptnhl dieaigwlee qlsttraafv lishdraflr
      181 altratlwid rgevrrqdkg fehfedwret vwtaedearh kldrkiraea rwavegisar
      241 rkrnqgrlra laalreeras qirrqgtaam eldagqqsgk rvidakgisk afgervilkp
      301 fdlrvlrgdr vafvgpngag kttlikmltg eiptdsgeir hgtnleiavf dqaraaidds
      361 vtlwdalagd psmrvsgrsd qvmvrgnprh vvaylkdflf ddaqarapvg slsggekarl
      421 llar
//
LOCUS       WP_010396294             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Paracoccus].
ACCESSION   WP_010396294
VERSION     WP_010396294.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..157
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17248
     Region          10..149
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtapeqsdfe idpisarilr ilarngripn qqlaaevgls psaclrrvqe lerrgaiqgy
       61 raviapaara agftayvtvg larhsneaql aferaclaap qvrechnitg sveyllrvev
      121 rdldayrrfh tevlgafpqi atitthvvmr spkdera
//
LOCUS       WP_010396303             198 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Paracoccus].
ACCESSION   WP_010396303
VERSION     WP_010396303.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..198
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21342
     Region          9..164
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mfyrpenghg lphnplnaiv aprpigwist rgrmgdnlap ysffnltayv ppqvmfasts
       61 tksdrpgtkd svaqiaetrv fcvniadgpl kdqvnassap lpagvnefea agieaagcqt
      121 idcprvagaa aalecratri lrlageanfm vlgvvtgihl redclkdgrf dlhatgwlsr
      181 mgykdytitn etfemerp
//
LOCUS       WP_010396379             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Paracoccus].
ACCESSION   WP_010396379
VERSION     WP_010396379.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..224
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25280
     Region          10..220
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mqptidftls tapqvydwlr dailrgalpp gtrlseteig qqigvsrqpv reafirltad
       61 glaevrpqrg tyirrisisa vlsarlirea vesdlirmla eqaddklitq ldqeiaeqse
      121 avarddaetf vrlddrfhrl lavavgqeav wevleglksq mnrlryitar tfdiqkligq
      181 haeivdglrn hdpalaeaam rrhlrellnd lpeisrsrpe lfip
//
LOCUS       WP_010396385             426 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Paracoccus].
ACCESSION   WP_010396385
VERSION     WP_010396385.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..426
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44272
     Region          1..425
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mdlflllttf vvtlalgvpv avclglasla yilsaglpvv iipqrmyagm dvfvllcipg
       61 filagnlmnf ggiteriirl analvgwmrg glalanvads mmfggvsgta vadvaatggv
      121 mipgmkksgy pgdfaaaita asstvgpmlp psvpmiivga lsgisvgqlf lagavpgvlm
      181 giamgvtcyi lavrrnyprq ewkgfsella aflsafwala mtgliiggll tgiatpteta
      241 ivaclyafvv gafiyrelpi ravprivids aissagilal vgfanvfgsi laseripqml
      301 vnsvlaitdn pilvillini lllfvgmfme tiaaliilfv pllglatsvg ieplhfatfa
      361 vlnlmigltt ppvgvclfva cniareplar visavipfli sniivlllvs yyppfatwlp
      421 stlmgn
//
LOCUS       WP_010396445             278 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Paracoccus sp. TRP].
ACCESSION   WP_010396445
VERSION     WP_010396445.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..278
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29272
     Region          26..270
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mvarlglilg mivglaqhaa aqpprrvlsm nlctdqlalm laapgqlvsv salaadpsss
       61 amakeaaplp anhglteeiy lmqpdlvvag awsspetirl lqrlnipvev fpvendlagi
      121 ranilrmgkv lgrdaeaqrl iarfdadlsl lsdpapgprp raalyavngy ssghnslagq
      181 iialagfdni adelglpagg ilalerllia dpdllvegrr ypgaargqel lehpalkalg
      241 qdkstvvmsd pdwvcgtpyi lravaqmrea rlalqegp
//
LOCUS       WP_010396479             217 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paracoccus kondratievae].
ACCESSION   WP_010396479
VERSION     WP_010396479.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus kondratievae
  ORGANISM  Paracoccus kondratievae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Paracoccus kondratievae"
                     /db_xref="taxon:135740"
     Protein         1..217
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23974
     Region          5..206
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mlntraqval aealrhgelh agqflsmpql vdilklplaa vreaarhass sgwleiipkr
       61 gvqimdarpg tirdsldmrm vldqegarrr ildgdelapl galrqaheqm laaargaatp
      121 elspnaiavd lslhdflagg lnnpllrscy dsnririail qrvrpfvqer ilsameehla
      181 iidaverrdi saaveaiayh certqhwwgv payhrgr
//
LOCUS       WP_010396516             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy-coupling factor ABC transporter ATP-binding
            protein [unclassified Paracoccus (in: a-proteobacteria)].
ACCESSION   WP_010396516
VERSION     WP_010396516.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paracoccus (in: a-proteobacteria)
  ORGANISM  unclassified Paracoccus (in: a-proteobacteria)
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="unclassified Paracoccus (in: a-proteobacteria)"
                     /db_xref="taxon:2688777"
     Protein         1..249
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27378
     Region          14..230
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mqkrpeddsa dlaihldevg hevagrpvls gltlystarr igvvgrngsg kstlarllag
       61 liapssgtir igghdifrdr realatvgil fqnpehqiif prvseeiafg lrqqgldkha
      121 aaaraeavlh sfdklhwkda pisalsqgqk hlvcmmavla mrprllilde pyagldiptr
      181 rqlarylrrv ntrslhishe psdledckel fwldrgriva qgtpaevlpr ftaemirlgd
      241 lddiadlag
//
LOCUS       WP_010396565             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FAD:protein FMN transferase [Paracoccus].
ACCESSION   WP_010396565
VERSION     WP_010396565.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..304
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=31472
     Region          35..275
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mslsrrrflt isaaaallpa tlqarparhw vgqalgaraa ihidhpdaga itarclaeie
       61 rlenilslyr pesalsrlnr dgaldappfe lieclslags vhrasgglfd psvqplwslw
      121 aeaatqgrrp akaerravla rigwqgvnld sgritlapgm altlngigqg yvadriaall
      181 eaeglsnili dtgelralga rpdgadwpvq ladggstalr gralatsapl gtcfdaggqd
      241 ghiidphsgm parpvwravs vsapgaalad alstagcltp drlaldglls afpaarleaa
      301 hmag
//
LOCUS       WP_010396586             404 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome-c peroxidase [Paracoccus sp. TRP].
ACCESSION   WP_010396586
VERSION     WP_010396586.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..404
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=44392
     Region          44..385
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 msfprslspf llvlaligav vtvgaatgrt prptsgqvqh dltelgqrlf hdpalsrngt
       61 qscatchdpe yaftdpregv agravslgdd gvsygdrntp tlsyaalsps fhrdakgryk
      121 ggqfwdgrad dledqagqpm lnpvemamtd kaavvarlrd eqgyqesfaa lfgpgalddv
      181 drafkgasaa laayqrsqef mpfdsrfdrw qrgeegltpq eefgytvfit wncrlchqlq
      241 kqgvveretf tsfeyhnigv pvnpgaraas glgpdhvdlg llarpgiddp aqagrikvpt
      301 lrnvavtgpy mhngvfedlr tavlfynkyt srrpesrinp etgrdwgqpe vaenlslpel
      361 qsglmlndar vdalvaflet ltdrryepll aeqkrirket aptd
//
LOCUS       WP_010396556             299 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paracoccus sp. TRP].
ACCESSION   WP_010396556
VERSION     WP_010396556.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..299
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31430
     Region          5..220
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnstltisrl tkrfqgvsal sevslslgpg mrvallghng agkstmmkii lglipfdggq
       61 vqvcgaapgs araraqvayl penaafhpal tgeeqirhyl slrgesprra selpervgla
      121 raagrrigty skgmrqrvgl aqaligrpgl lvldeptsgl dpvsrrdfya lldglaaega
      181 aillsshalt eveartdril ilsqgrlvae gtlsdlrrra alpvalivtp apdaaaalaa
      241 alpqarqadd gtlhltcaqt eklallahia tlgpqvadle vippslediy shfsrrdgq
//
LOCUS       WP_010396558             274 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Paracoccus].
ACCESSION   WP_010396558
VERSION     WP_010396558.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 274)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..274
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27664
     Region          5..187
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mirrilstaa lefrialrnr wvaiaiglmv vfalvlaaag aaptgdigad rlsvtvvslt
       61 slavylvpll allmsfdaia gevergtlpl lltypvarae vlagklvahm ailalavgag
      121 ygaaalaavw vdpastaglp alwrlmwsst llgatflgvg yalsclarrp sgaaglavgl
      181 wlglvvlydl gllamivadg ggpltgrvlp vallanpada frlfnlaaae aanaaagmgg
      241 aaatiplwqs alsvvlwpla alglaiaafr kvtp
//
LOCUS       WP_010396600             322 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paracoccus sp. TRP].
ACCESSION   WP_010396600
VERSION     WP_010396600.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..322
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33565
     Region          5..322
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mkidlhtlgp lvalialvil gaalnssfla panitnvlar safigliavg mtfvitaggl
       61 dlsvgsmaaf lagvaiiamn valpglgsnw gtillgmava vlggivagyl ngalitkari
      121 epfivtlgtm gifrslvtwl adggtlsldy glrtlyrpvy yggigwitwp iiafamvavl
      181 gewimrhsrf grhveaigsn drvarysaid vnrvrlltyv llgalvgiav vlyvprlgsa
      241 sgstgvlwel eaiaaviigg talkggrgrv wgtvvgvlil slidnilnla dlvspylnga
      301 iqgviivlav vlqrekraae er
//
LOCUS       WP_010396638             433 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Paracoccus sp.
            TRP].
ACCESSION   WP_010396638
VERSION     WP_010396638.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..433
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45315
     Region          6..432
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgiyairmpd igegiaeaei aewlvkpgdv lreddpmvav mtdkatveip spvtgtviwq
       61 agqpgdviav gaelvrlevd gpgnvaeeae tpatsagtks atpekpaaap vpepepaprq
      121 eaaaevqkap asaapapaap aaplrpegek piaspavrar areagvdlrl vrgsgpggri
      181 shddldafia sggvpapsgp rpdtsveeir viglrrkiae rmeaansipq itiveevdat
      241 aledlrgrmn aqgkgtrltm lpfiaramvr alreqpllnv hydagagvir rfggihigia
      301 aqtptglmvp vlrhaealdl rstaaeiarl ataakegtar rdeltgstit itslgplgai
      361 astpilnvpe vaivgvnrla vrpfwngtaf eprkmmnlsc sfdhrvidgw daavfvarlk
      421 elletpalif veg
//
LOCUS       WP_010396667             370 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paracoccus sp. TRP].
ACCESSION   WP_010396667
VERSION     WP_010396667.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..370
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40717
     Region          1..368
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mgfleirntt ksygsveilh didisveege flvlvgpsgc gkstllnmia gleditsgei
       61 sikgrvmngv hpskrniamv fqsyalypnm tvgqnitfgl emhgtpraer ekalaevarl
      121 lqidhlldrk pgqlsggqrq rvamgralvr dpdvflfdep lsnldaklrv dmrteikklh
      181 qklkttivyv thdqieamtl striavmyqg yvqqlgtpke iydtpanvfv atfmgspamn
      241 iipahvvmre dvphakitda dgnevllrfs qpnlaewdgr eillgirpea mtdpegadrq
      301 saniqtltnr vsvtepagsd tfvtmvlggk evvarmrada lvrpgqsfdf aanmekaiaf
      361 dpktekriap
//
LOCUS       WP_010396751             261 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RlmE family RNA methyltransferase [Paracoccus].
ACCESSION   WP_010396751
VERSION     WP_010396751.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Hirata,A., Okada,K., Yoshii,K., Shiraishi,H., Saijo,S.,
            Yonezawa,K., Shimizu,N. and Hori,H.
  TITLE     Structure of tRNA methyltransferase complex of Trm7 and Trm734
            reveals a novel binding interface for tRNA recognition
  JOURNAL   Nucleic Acids Res 47 (20), 10942-10955 (2019)
   PUBMED   31586407
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Caldas,T., Binet,E., Bouloc,P., Costa,A., Desgres,J. and
            Richarme,G.
  TITLE     The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S
            ribosomal RNA methyltransferase
  JOURNAL   J Biol Chem 275 (22), 16414-16419 (2000)
   PUBMED   10748051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..261
                     /product="RlmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=27900
     Region          28..241
                     /region_name="RlmE"
                     /note="23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ
                     [Translation, ribosomal structure and biogenesis];
                     COG0293"
                     /db_xref="CDD:440062"
ORIGIN      
        1 maqdkkpgeg rkssgrgqre lrvrvksakg rklsstlwle rqlndpyvar akregyrgra
       61 aykiielddk fgflvpgarv vdlgcapggw cqvavsrvna lgdrsgkkvg rvlgvdlqev
      121 dpipgaeihq ldflsdgadd lvkawlggra dvvmsdmaaa ssghkatdhl rivalveaaa
      181 qlafdvlepg gtfvakvlag gaeaemqvml krnfskvanv kppasrsdss ekfvvaqgfr
      241 grdeterand edegdalsdq g
//
LOCUS       WP_010396993             382 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Paracoccus].
ACCESSION   WP_010396993
VERSION     WP_010396993.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..382
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40442
     Region          16..381
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mgtrkmdksf ldwpffearh relaaaledw svkhlpadhg dtdaackglv aalgqagflr
       61 hsganegerl dvrslclire tlarhdplad fafamqglgm gavtlfgtpd qrkwlertra
      121 gqaisafalt epgagsdvas tattaertpg gwrlsgekty isnggiadly vifartgeap
      181 garglsaflm padstglsva erieviaphp larlklagve lpeaaligqp gegfkiamsv
      241 ldvfrptvga aalgmarral dealarvarp ragggtlady qivqghladm alkvdaaall
      301 iyraawtkdq gatritreaa maklyateaa qevidtalql hggdgvrcgs tvealyrdir
      361 alriyegasd vqrvviarsv la
//
LOCUS       WP_010396966             244 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Paracoccus].
ACCESSION   WP_010396966
VERSION     WP_010396966.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..244
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27043
     Region          6..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mteaaiimrs vnkyygayha lvdinltvar gerivicgps gsgkstlirt inqlepiesg
       61 tivvdgvelt aggenvarvr qdvgmvfqsf nlfphmtvle ncvlapmktr kipraeaeat
      121 arkylervri peqadkypaq lsggqqqrva iaralcmkpr imlfdeptsa ldpemvkevl
      181 dtmidlareg mtmlcvthem dfaravadrv ifmdkgvive enapeeffnn pknerlqnfl
      241 gqia
//
LOCUS       WP_010396906             295 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paracoccus sp. TRP].
ACCESSION   WP_010396906
VERSION     WP_010396906.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32503
     Region          8..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..283
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(110..111,113..114,117,121,123..129,213..218,
                     224..225,227..228)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176173"
ORIGIN      
        1 mdrpqlplna lrafevasrh lnltraaiel cvtqaalshq irgleerlgv tlfrrvprgl
       61 vlteegimla pvltrifdem sgaldrfssg hyhetinlgv vssfatewli priedfqrlh
      121 psvdlrihtn nnrvdlageg ldlairfgdg swhgvaatrl msgammlvcs petagrlrwi
      181 edlpsipllr syrasewerw fasqglpapl lrgpvfdssl aiaemaarsy gaglvpvvlf
      241 apwlqngrlv rpfdtvlaag dywltrlhas petagqaafr ewltaacaed esgai
//
LOCUS       WP_010397007             330 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Paracoccus].
ACCESSION   WP_010397007
VERSION     WP_010397007.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..330
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34294
     Region          31..328
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mgellnrdai inlvifallv avalgahlag dgftvtlatk aaifglagvg lnlalgyggl
       61 isfghaaffg iggyvtgila shassgmpvv tlpftimgsn emlgiwpvam laggvaalai
      121 galslrtsgv yfimvtlafa qmlyyfaisw sryggedgls fyvrntfpgl ntfapiqyfa
      181 icavllalal vftavvtqsr fglalqaarq nsqravavgi rpyairltaf vlsgmivgla
      241 gslyadlnrf vspamlswhm sgeimvfvil ggvgrlcgpv agaaiyille hvlggisdyw
      301 qallgllllg ivlfapggli givtrrgrha
//
LOCUS       WP_010397013             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Paracoccus].
ACCESSION   WP_010397013
VERSION     WP_010397013.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..267
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28951
     Region          65..265
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 maiyrgmnrq qldaaynnsa rvadfpglmr elrarsevfy stqdcrrdlr ygtsarqtyd
       61 wiscgkpnap vfvfihggyw qncvkedfay saagplahgy dvilaeytla peasmtrivt
      121 eigqlldhlv pqiagrplcl sghsagghla ashrshpavt rvmpisglyd lepislgqln
      181 dnlrltpeei aayspqhhig pgapmlitvg ggelpelirq sdeyaaacqq ageqagllhv
      241 kdcdhfqvld dladpagaql taltarp
//
LOCUS       WP_010397074             526 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Paracoccus sp. TRP].
ACCESSION   WP_010397074
VERSION     WP_010397074.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..526
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57440
     Region          28..524
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 madnvakfeh ddasvvvvvg tgagggvlan elaqrgikvv aleaggrylp edyindewds
       61 faqlswgdmr ttsgdwriar dfanlpawiv kavggtsihw agaslrfqeh efralstygr
      121 vdganlldwp itlsdlepyy dlaekklgvt rtndwpglpg nnnylvlekg akaagyskvs
      181 tgrmainsvd nddrmacqqt gfcfqgckwg akwsaaytdi prgeatgnle vrdhchatri
      241 ehdddgkvtg vryidkdgte qlqrarivav agnsiesprl llasaseryp dglanssgqv
      301 grnymrhttg svyaiferpv rmwrgttmag ivqdeahhdp srgfvggyel etlslgvpfm
      361 aafmdpggwg reftsaldsy enmagmwivg edlpqetnri tlnpgekdrf glpvanvhyd
      421 dhpndiamrn hayaageriy raagatrvlp tppypsthnl gtnrmsenpr dgvvnkwgqs
      481 hdipnlfvsd gsvfttsaae nptltivala irqaehiaae mekgtl
//
LOCUS       WP_010397203             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Paracoccus].
ACCESSION   WP_010397203
VERSION     WP_010397203.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..143
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15484
     Region          1..135
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdeldrgila hlaqdarmsv avlarrlkva rstvqarler letsgaiagy tlrlgdtare
       61 hriratcllt iepraqaail arlrslpeve rihttsgrvd lllqlaavst sqlddvldqi
      121 ggltgvrsse slihlstkld rat
//
LOCUS       WP_010397374             320 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Paracoccus sp. TRP].
ACCESSION   WP_010397374
VERSION     WP_010397374.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..320
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=34167
     Region          137..303
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mligagaatd lapfepdrlq ivqgfypdhr alvaqgyevv teasgdfdga vvflprarae
       61 arariaeavs wlapgaslwi dgqktdgida vmkemrglvp vdevhsrahg kifrvilpap
      121 gwlpdgwaaa dheaapgmvt rpgvfsadgp dpasqallah lpeklptriv dlgagwgwla
      181 agilthpgve vlhlveadat alacarrnvc dpraqfhwad aldfrlpepv ngvimnppfh
      241 egraadpklg agfiraaagl ltgagrlwmv anrhlpyeqv lrecfadvse lggdsrfkil
      301 tatgarrpgs krpqpkgrkr
//
LOCUS       WP_010397380             152 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Paracoccus sp. TRP].
ACCESSION   WP_010397380
VERSION     WP_010397380.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..152
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16825
     Region          6..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 msvqpdatdl ailrllgeda trgaaeigrm lgltqpatwr rirrltetgv iagrrivvne
       61 aalgfgvtvf lgirlavkgr vsledferav maipevqvvq hvlgqfdyrl rirardiadf
      121 erilrrrimt lpgvgqvean vmlseerrpg pl
//
LOCUS       WP_010397392             356 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Paracoccus
            (in: a-proteobacteria)].
ACCESSION   WP_010397392
VERSION     WP_010397392.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paracoccus (in: a-proteobacteria)
  ORGANISM  unclassified Paracoccus (in: a-proteobacteria)
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="unclassified Paracoccus (in: a-proteobacteria)"
                     /db_xref="taxon:2688777"
     Protein         1..356
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37572
     Region          1..356
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mfrleprasa pllwqvvtpl lavlatiivg galfaamgfd pvasirtifw dplfgpasgy
       61 srpqllvkag pliliasgla lgfragiwni gaegqyiiga isgaavalaa ypleahwifp
      121 amilagaagg wawgmipaml rnwfgaseil vslmlvyvaq riaawmafgp mknpegfnfp
      181 gsrnlqqyes asnpelians glhwggvaav lalaatwfim srhilgfhir tagaapraar
      241 fagvrperlv alclgvsgal aglaglfeva gpggqitesf gsgygftaii vaflgrlhpl
      301 gillagllla ltyiggelaq mmlnlpaatv qvfqgmllff llgfdiltry rirrra
//
LOCUS       WP_010397407             288 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Paracoccus].
ACCESSION   WP_010397407
VERSION     WP_010397407.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14427476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..288
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30070
     Region          8..206
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16278"
                     /db_xref="CDD:293836"
     Site            order(66,68,70..71,146..147,163,202)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293836"
     Region          237..274
                     /region_name="BLACT_WH"
                     /note="Beta-lactamase associated winged helix domain;
                     pfam17778"
                     /db_xref="CDD:407650"
ORIGIN      
        1 mtsvekalrv itannpsplt gpgtntfllg heriavidpg pdlpehreai laaagagris
       61 hilvthahld hsegaralaq ttgapilgfg paesgrsavm erlaregaid ggegldrdfa
      121 pdipladgav ietdewrlta ihtpghfagh lafrhdetif cgdvvmgwss tiisppdgdl
      181 adyfrtlarl asagasqllp ahgeaihdpa arlaelaahr rertaqilaa lsrspataen
      241 laqqiyeipp allpaatrnv lahlialhel gavstpglia sdaifsar
//
LOCUS       WP_010397569             476 aa            linear   BCT 01-JAN-2025
DEFINITION  alkaline phosphatase D family protein [Paracoccus sp. TRP].
ACCESSION   WP_010397569
VERSION     WP_010397569.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..476
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=52921
     Region          95..402
                     /region_name="MPP_PhoD"
                     /note="Bacillus subtilis PhoD and related proteins,
                     metallophosphatase domain; cd07389"
                     /db_xref="CDD:277335"
     Site            order(101,140,143,208..210,214..215,376,378)
                     /site_type="active"
                     /db_xref="CDD:277335"
     Site            order(101,140,143,208..209,214..215,376,378)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277335"
ORIGIN      
        1 mmdeaqesgh agpilhfrgm agggirlati iirplnapap pslrvstagv apvriaeian
       61 vaiwrhdftl tpadrgyefa dcfyevvtdl sgdlrlafvs cngeengdle rdddernlmw
      121 trlaqdhasa pfalllqggd qiyadeatqg hplsedwpdh vpevddsaal qdlarhlrdr
      181 fverylhvlr apgyswmaar vptlaiwddh dicdgwgslp ekrarsavgq alfqaarety
      241 llfqhgaves dipelfldat gaslgwkrel pgltiaapdl rserdrhrim gpagwqsvea
      301 lapqgehifl vssvpllgpr lsliervmma iprmqhyedd lrdqwqsrah raewrrmlgq
      361 vlqwrdharv talsgeihla traemgpqaq kihqlvasgi shrappraya rllglfaglg
      421 eaplpghpir ilplpgqrhr yvaernyltl trsaghwqav whledsgktp plelsa
//
LOCUS       WP_010397587             332 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Paracoccus].
ACCESSION   WP_010397587
VERSION     WP_010397587.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..332
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36135
     Region          1..332
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mgsitleqvc ksfgevevip gvdlqiedge fvvfvgpsgc gkstllrlia gledvtsgri
       61 vidgqdvtva ppsrrklamv fqsyalyphm svrkniafpl kmaglsadeq errvqhaagi
      121 lnltdyldrr pgqlsggqrq rvaigraivr epsaflfdep lsnldaalrv nmrveiselh
      181 kklattmiyv thdqveamtm adkivvlrag rieqvgsple lyrrpanrfv agfigspnmn
      241 flegeaaarl gahaigvrpe hfrlsmsega fagrvgvaeh lgsdtflhvd lddgthvvar
      301 aegefpashg drihltpqdg rlyrfdqngs al
//
LOCUS       WP_010397821             317 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Paracoccus].
ACCESSION   WP_010397821
VERSION     WP_010397821.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34662
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,192,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mrydlndlet fltvmelgtv taaaarlnls ksvvskritd legtlgaalf rrnagritpt
       61 eaalrlaerl rpalteliaa aestawdmdg laplrgslsi aapmtfgvmh lgpiiarfaa
      121 lnpeleisvd yddrardlar egfdigirig kmrdkalmqr klcedesvvc aspaylerkg
      181 rprtladlrd hevigyshlp nsqlwqfqdr drfvspvvqg rlsmnngeai rdmaigglgl
      241 ailpgfiaap aladgrlerv legfdtrplp vvavwppvsp mpaklrrfvd hlaaelhrpp
      301 wqaplsqhpp atteatp
//
LOCUS       WP_010397919             598 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-binding protein, partial [Paracoccus sp.
            TRP].
ACCESSION   WP_010397919
VERSION     WP_010397919.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..>598
                     /product="thiamine pyrophosphate-binding protein"
                     /GO_component="GO:0005948 - acetolactate synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0009097 - isoleucine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009099 - L-valine biosynthetic process
                     [Evidence IEA]"
     Region          1..572
                     /region_name="IlvB"
                     /note="Acetolactate synthase large subunit or other
                     thiamine pyrophosphate-requiring enzyme [Amino acid
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0028"
                     /db_xref="CDD:439799"
ORIGIN      
        1 mkltggqvva ralkeygvey vagvpghgiw slfdaflqeg seipfiqvmh eqsavhmadg
       61 yyracgkpma cstsvgpgaa ntiiglatay tdstavfyvs gspqtymqgh gtmqeierqq
      121 dnafpriteq vtkrawqahs vrtlpsimhr afsemltgrp gpvhvevpmd vqveaeevti
      181 hpldkrlpvg vaypdpkaie aaakvllsar rpvivaggga itadasaelt alaeklgaav
      241 sitwngkgai aednelfiga vgqtgttcgn qitasadvvv svgcrftdws assyakgvsf
      301 sfppgklihi dldpreigkn yptevgivsd akialgqlle aisdadatal rdrnadfhae
      361 vqkakadwha qveprensre tpftsqrplv alrkvlprdg ivvvgsgntq gsvkqsfpvy
      421 eprthltsgs yspmgwavpa amgaklacpe kkvvaivgdg dfmmslpemg tavmnginvv
      481 flvlnnqgym sirggqrkfm grhiasefnh hagngepysa dltatakafg leawkvvkde
      541 dlestlekal ntdgptlvev ivsrdaagpf atgwwdfpsp ayyekeqeay aemrakeq
//
LOCUS       WP_010397934             303 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Paracoccus sp. TRP].
ACCESSION   WP_010397934
VERSION     WP_010397934.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..303
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32326
     Region          5..299
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 msfaiegvyc aaatplkadg tpdlplfgah aralikegch giamlgstge ansfsvrerm
       61 dlleaaitgg trpdqllpgt sscavtdave ltrhavqagv kgvvllppfy ytafsdeslf
      121 rfyasiiekv addrlkvily hipmltgvpi sheliamlvq afpdtvagik dsdgkienmh
      181 amaarfpgfa vlagadplll pvlqgggagc itassnlvar elrlvwdhwn dpakaaevka
      241 aqevivawrk ltnsytqlpt vktmlakrrg dmgwmnvhpp fsplsegeaa kvwavmdele
      301 gka
//
LOCUS       WP_010397948             540 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paracoccus sp. TRP].
ACCESSION   WP_010397948
VERSION     WP_010397948.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..540
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58845
     Region          1..523
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 maepmlqvrn lsvefhtaag tvravrnvsf dldrgetlai lgesgsgksv sssaimdlid
       61 mppgmitsgq iifegrdllk lsaserrkvn ghkiamifqd plshlnpvyt igwqivetmt
      121 vhgmarpqar aealrllgrv gipdpegsme kyphqfsggq rqrlmiamal alkpdlliad
      181 epttaldvtv qaevlallee lqqetgmgvl iithdlgvva eiadrvvvmn agevvetgdt
      241 rqvyrnpahp ytrkligaap gkgamheplp paepvlsvrn arkvygdfaa vedvsfdlma
      301 getlaivges gsgkstvakm llrleeptgg eahwkgqdlf amserqlfal rrdlqmvfqd
      361 ptqslnprmt vwqlitegwv ihpgilprsk wkarvaellh qvglkpemag ryphqfsggq
      421 rqriaiaral alepeliicd eavsaldvsv qaqvielldg lrnslgiafi fiahdlpvvr
      481 dfadhvmvmq kgrvveagtv rqifdnprqp ytqallaagl dpdpdvqaer raarlamaag
//
LOCUS       WP_010398002             335 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Paracoccus sp. TRP].
ACCESSION   WP_010398002
VERSION     WP_010398002.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..335
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35580
     Region          12..321
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mndmiirkdr ragrltfnrp qalnalshem alaidaalre wrddpevalv iidaegeraf
       61 csggdiaavy raglagdhrv grkffrdeyi mnariaeypk pivafmqgfv mgggvgvggh
      121 ashrivgdtt qiampecgig lipdvggswl lghapgrcge ylgltaarmg agdaiftgfa
      181 dsyipeaewp alierlaesg dvtaigahpa peaplatvdl safagetvae ivaaletagn
      241 eaalkplrrn splsmaatla lvraarkdat lrdslarelr ftaratagsd flegvraqii
      301 dkdrnprwsa daspahvaem laplgadeli weesk
//
LOCUS       WP_010398105             141 aa            linear   BCT 01-JAN-2025
DEFINITION  EVE domain-containing protein [Paracoccus sp. TRP].
ACCESSION   WP_010398105
VERSION     WP_010398105.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Bertonati,C., Punta,M., Fischer,M., Yachdav,G., Forouhar,F.,
            Zhou,W., Kuzin,A.P., Seetharaman,J., Abashidze,M., Ramelot,T.A.,
            Kennedy,M.A., Cort,J.R., Belachew,A., Hunt,J.F., Tong,L.,
            Montelione,G.T. and Rost,B.
  TITLE     Structural genomics reveals EVE as a new ASCH/PUA-related domain
  JOURNAL   Proteins 75 (3), 760-773 (2009)
   PUBMED   19191354
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..141
                     /product="EVE domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=15916
     Region          2..136
                     /region_name="EVE"
                     /note="Predicted RNA-binding protein, contains EVE domain
                     [General function prediction only]; COG2947"
                     /db_xref="CDD:442190"
ORIGIN      
        1 macwlfksep dvfsfddlia rgekgeewdg vrnyqarnnm rtmkkgergf fyhsnvgkei
       61 vgicevvtea hpdstaddpk wecvdvrava wlerpisldm akteprlkdm vlvnnsrlsv
      121 qpvsdaewqv ilelaggtrt l
//
LOCUS       WP_010398153             337 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Paracoccus].
ACCESSION   WP_010398153
VERSION     WP_010398153.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..337
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36984
     Region          15..333
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msehasspdp nqprlrigfl ltprftlsaf atfvdvlrla addgdgsrpi rcrwrvlspd
       61 mapvqsscgm riepderlgd parfdyivtv gglidggpgl speqvtflrr aaaarvalgg
      121 lctgvfalar iglmdgyrcc vswfhhqdfl aefekmrpvs dqifvvdrdr lscsggvsaa
      181 hlaaflvdrh lgraaarkal silmidepme gdrpqpglpl elnahdplvr rallamqqnl
      241 haplpiaria rdlgvgrrkl erhfnadlgi ppadasirir laqarmllar tdrtvtriae
      301 etgfcdashl irvfreaegt tpdlwrqnrs maaeega
//
LOCUS       WP_010398164             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Paracoccus].
ACCESSION   WP_010398164
VERSION     WP_010398164.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..219
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24434
     Region          3..212
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 mpelifpgpe grlegryhaq pnpdapiaiv lhphpqyggt mnnrvvynlh yafhrmgftv
       61 mrfnfrgvgr sqgefdqgvg elsdaaaald ylqamnpnsk hcwvagfsfg awigmqllmr
      121 rpeitgfisv appanmydfs flapcpssgl iingtvdrva ppkdvhalvg klreqkgiti
      181 theeiegadh ffrddevhmk pmietvqayv rrrltettr
//
LOCUS       WP_010398290             148 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Paracoccus].
ACCESSION   WP_010398290
VERSION     WP_010398290.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 148)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..148
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15762
     Region          6..139
                     /region_name="NUDIX_ADPRase"
                     /note="ADP-ribose pyrophosphatase; cd04673"
                     /db_xref="CDD:467557"
ORIGIN      
        1 mahfprlaal avtldgvgdt arallvqrrn ppdaglwgfp gghvepgeta leaaarelae
       61 etgvigrpls ylenidvier nddgslrfhf lltavlcdyi sgeplaadda adarwvpvad
      121 ilsaqlplsa svpevvrkal alwsertr
//
LOCUS       WP_010398336             368 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide biosynthesis/export family protein
            [Paracoccus].
ACCESSION   WP_010398336
VERSION     WP_010398336.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..368
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39040
     Region          4..348
                     /region_name="PRK15175"
                     /note="Vi polysaccharide ABC transporter protein VexA"
                     /db_xref="CDD:185097"
     Region          75..244
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 maqvalvgam llvsacglpr sgptkgeils gsvekggsth iinvdnrvnr aanftpaygf
       61 sadfraagtv gadeirpgdv lglsiwenvd dgllasmgqs stqltelqvd sqgyifvpya
      121 grvraagnsp eelrrlitqk letqtpdpqv mvtrvagdga tvsvmgkvna qgvypierpt
      181 rtlssmlsra ggvaiepeia vvtvkrgnss gkvwlrdlys narndialrp gdvilveedq
      241 rsftalgalg gqtkvplgne qisaieavam vgglstqlad pkgvfilrde pqsvaravlg
      301 rndiygtqrf ayvldltkpd gmflardfvi rdgdtvyvte apfvqwrktl qsilgtatev
      361 gsvdnafn
//
LOCUS       WP_010398443             258 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Paracoccus sp. TRP].
ACCESSION   WP_010398443
VERSION     WP_010398443.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..258
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27529
     Region          30..253
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 msaqaelaas phlspeqsra lqrspaqcvr hgflqalpfi lvlmpfgmlf gvvaseagld
       61 laqtvgftvl vlagasqfta vqlltdhapv lviivsaiav nlrmamysas lvpwlgaarp
      121 rdrawiayal idqsyalsiq hyekhprlsi dqrvgyflgs vlatcpvwvv amllgfwlgk
      181 sipedwaldf ampitflali spmlrtpahv aaalvavvgs lifaflpsgl glfvaaplam
      241 itgavvealm errngarl
//
LOCUS       WP_010398494             198 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Paracoccus sp. TRP].
ACCESSION   WP_010398494
VERSION     WP_010398494.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..198
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21770
     Region          1..198
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltlyhapks rsssvvvlle elgvldkvdv rrvtiprqdg sgardpanph pegkvpylvn
       61 gqdhvrerga imlyltdtfp eaglgplpgd prrgqylswl swyqgvlepv ailhfcginh
      121 palaaslrdy dtavarldev ltkqpyllgk dfsaadllva gpfmffgpeq mprtpavddw
      181 vqriqsrpsm arvaelda
//
LOCUS       WP_010398538             299 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [Paracoccus].
ACCESSION   WP_010398538
VERSION     WP_010398538.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..299
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32144
     Region          85..290
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 mkkpvlliaa mavlalggwg tlrgspsdtp evqgmailda egnavgryav padkdilaqs
       61 nadeilygkr lladtarllp dnvgaamncn schlgdgkie gangyintvn fyprvmprag
      121 knvdlemrin gcfqrsmngk pldpdgpemk amiaymdwlr qdvpkgqtvd ivnagpides
      181 llpdpengkr iyaakcaach gangegmrdq sgdilfpplw geesfnigag martykaaqf
      241 vkwamppamh ltgqlgqggv lsdqeavdva effthmprpd fpgkvndwpn gnrpkdary
//
LOCUS       WP_010398557             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Paracoccus].
ACCESSION   WP_010398557
VERSION     WP_010398557.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..220
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24497
     Region          14..214
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mddwtayfke mdqlpapmrk sllrdsrklq fpagsrlfgp gqpagyllll vsgkvrvtqv
       61 sdtgrelvly rvgagescvl tsacmlaydd lateglaetd ieaigiprat fdemmalspd
      121 frgfvmraws rrvtdllsli ddiafqridl rlanrllala tgdtvhathq qlaaelgsar
      181 evisrtlsef qrrgwieqar gevrlmnrpa lekltrepel
//
LOCUS       WP_010398645             400 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Paracoccus sp. TRP].
ACCESSION   WP_010398645
VERSION     WP_010398645.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..400
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44512
     Region          18..373
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mietpgriep cffeehipas ladlsveiqr eaaglgqglh sdsaaeladl vrvmncyysn
       61 lieghntrpr dieralagae leaetrplal earahvivqr sidkmhregs lprptsvafl
      121 twvhktfyee mpdefrrieh pdgtiepiip grmrqegdse vavgrhlpps sgrvaafmdh
      181 fdkrfqiaar sasgriiaia sahhrlnyvh pfpdgngrvs rlmshamale agiggqglws
      241 vsrglargla drgeykrmmd madtprrgdr dgrgnlseaa lktycewflk vtldqitfsa
      301 klfdlgglek ryrrlvedti ddkrapdlis avlrygtler geapivlkts ertarntlsk
      361 ltsagylssa spktpvrlaf pldyrerlfp nlfadgdipe
//
LOCUS       WP_010398657             730 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParB/RepB/Spo0J family partition protein
            [Paracoccaceae].
ACCESSION   WP_010398657
VERSION     WP_010398657.1
KEYWORDS    RefSeq.
SOURCE      Paracoccaceae
  ORGANISM  Paracoccaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 730)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Paracoccaceae"
                     /db_xref="taxon:31989"
     Protein         1..730
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=79092
     Region          14..267
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 maqaaqkitl sssrdipfdk lvlsqsnvrr ikagvsveel aediarrgll qglsvrpvld
       61 adgietgkfe ipaggrrfqa lsllvkqkrl aktapvpcvl rdvtsdvlae ddslaenmqr
      121 valhpldqfr afvalrdkgq geeaiaaaff vtpqivkqrl rlasvapall dvyaedgmtl
      181 eqlmaftvnp dpgrqvqvwd avknswnkep ysirrmltet svrasdrrav fvgvdvyeaa
      241 ggvvlrdlfq gddggwledp alldrlvtdk lqagaqaiaa egwkwievst dlpygyshgl
      301 rrlvgdpspl sadeaadhar llaeyralee eysgqdeype eidtrlgele atmeafeqrp
      361 lifdaaevvr agvfvtldrd gnlavyrgyv rpedepreet vanfgdelsa egqgadgsvs
      421 ayqlpvgasa atvitfgsqp fsaglpdded dgalkplper lvmeltahrt lalreaigrs
      481 pdvaltlllm klvndtfrss gasgscleas vrtvymsaqa pdlkdspvak avddrhsawe
      541 adlplgddav lwdylsaldq asrlsllahc lsfginalhe kvnpygagis asglnrrmaq
      601 seivaeavdl dmvaagwept adnylnrvpk arileavrea mgegtaqlld hlkkgemate
      661 aerllkgsrw lpevlrrsdl agldddgaae gqgalseevl gdqdnveeid lpaflmadlp
      721 mesaammaae
//
LOCUS       WP_010398804             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Paracoccus].
ACCESSION   WP_010398804
VERSION     WP_010398804.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..222
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24213
     Region          1..205
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msagseetla vrisrvladr ivsgeigpge rlrqdriaee fgashvpvre afrrleaqgl
       61 aiseprrgvr vaafdlpevk evaemraale elalrhaaph ltpailnaae eatkagdasr
      121 dvrsweaanr rfhkliltpc amprllaaid dlhaasarfl faawqsnwet rtdhdhrail
      181 aalrkgdvds acatlarhvr wigrrpatgg gdkqreafai vg
//
LOCUS       WP_010398806             185 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: 2'-5' RNA ligase family protein [unclassified
            Paracoccus (in: a-proteobacteria)].
ACCESSION   WP_010398806
VERSION     WP_010398806.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paracoccus (in: a-proteobacteria)
  ORGANISM  unclassified Paracoccus (in: a-proteobacteria)
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="unclassified Paracoccus (in: a-proteobacteria)"
                     /db_xref="taxon:2688777"
     Protein         1..185
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=20441
     Region          17..185
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 mpdapksqet arehfllfva ipppdaaaem etvwhlaerr drfrrstlhm tilpvlrspq
       61 fepclakgla havegldfpa fdlvldlltt fgpprrrdrp lvlagrqinp apdalcqqlw
      121 qrlagaglav arhqvtphvt laygkplppa giavppvrwr vnelvlidsl qglgrhvpla
      181 rwplt
//
LOCUS       WP_010398962             266 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Paracoccus sp. TRP].
ACCESSION   WP_010398962
VERSION     WP_010398962.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 266)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..266
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28707
     Region          1..247
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mklvtfafaa alslvglsas aealkigvvp gaygdavnva aeeakekgle vevvefsnwt
       61 tpnvalaagd idlnffqhrp flenaekerg ydfevvgqgi lanlglyslk hksfdeipeg
      121 gsvaiandpv nqgrglllle kagliklked vgflgtlddi venprnlkft evegpqlvri
      181 tgdvdlaqgy phfivasgaf dptsgliysg iedkqfsvsf vsrsdnkddp rikqfielfq
      241 qsqavkdqvh asfassdkly ilawqs
//
LOCUS       WP_010399203             134 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [unclassified
            Janthinobacterium].
ACCESSION   WP_010399203
VERSION     WP_010399203.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..134
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15483
     Region          22..133
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(23..25,39,56..58)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mnerisktel ialppipakr yftigevsel cgvkphvlry weqefsqlkp vkrrgnrryy
       61 qhhevllirr irellyeqgf tisgarnkld srgashgivn elplppamav vsqeepldra
      121 wirnelmail nllk
//
LOCUS       WP_010399226             354 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkene reductase [unclassified Janthinobacterium].
ACCESSION   WP_010399226
VERSION     WP_010399226.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..354
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37880
     Region          3..333
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,226,287,307,309..311)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,101,108,174,177,179,226,233,287,307,
                     309..310)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,101,174,177,179,310)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            179
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mttlfdpiti gslqlknrii mapltrsrad npgrvpnalm aeyytqrasa gmiiseatav
       61 tpqgvgyaat pgiwseeqve gwkhitkavh dagglivlql whvgrisapa fldgdlpvap
      121 savkpaghvs llrpkqefvt praldaqeip givaayrlga enakkagfdg veihgangyl
      181 ldqflqdstn lrtdnyggsi enrarlmlev tdaciavwga dkvgmhlapr rdahdmgdsd
      241 pkatfgyvar elgkrgiafi carealgedr lgpylkqefg gvyianekmd kpaalallak
      301 geadavafgl wfianpdlpi rlhsdaplnq lnpdtlyapd aagytdypal aaqa
//
LOCUS       WP_010399298             549 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type IV secretory system conjugative DNA transfer
            family protein [Alphaproteobacteria].
ACCESSION   WP_010399298
VERSION     WP_010399298.1
KEYWORDS    RefSeq.
SOURCE      Alphaproteobacteria (a-proteobacteria)
  ORGANISM  Alphaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Alphaproteobacteria"
                     /db_xref="taxon:28211"
     Protein         1..549
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59166
     Region          144..541
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mnqatlawaa fknmlraaar dpvwaissil mspfragryl lqvgffvflv tlmlavaang
       61 ipqewwiart iaglllllff lvlvfrvltn pliehfgdme gethgsarfa tdketaalar
      121 adtglligrd gktgkllryd gpahlltmap trtgkgvgti ipnlltadrs vicidpkgen
      181 ariagrarqt fgpvhvldpf gvtgqpsaaf npldqldpag ldvaedastl adalvfdepg
      241 mageahwnee akaliaglil hiaaseprdr rnlatlreal tlapeafaal lkdmqastaa
      301 ggliaraanr hlgksdreaa gvlsaaqrht hfldsprmva vlggsdfrfa dlkrrnasvf
      361 lvlppdrlat ysrwlrllvs qslidmardp vkpaapvlyl ldefaalghl apveramglm
      421 agygvqlwpi lqdvhqlrat ygqragtfls nagvlqvfgv ndhdsarlvs dllgqgtvvf
      481 qtmsraldse ksglsygeqh tarplltpde vrnlpahael lflagqrpiv agklayyada
      541 efrglydap
//
LOCUS       WP_010399393             350 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: permease [Paracoccus].
ACCESSION   WP_010399393
VERSION     WP_010399393.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..350
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=35717
     Region          39..346
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mtdttlptpg lrsalrhlwq dqrvwlasal ilgalavfdt pqaadsalfa gtallntapf
       61 lilsiaiaaw anatgadnli akaftgapil miglgalagg vspfcscgvi pliaallamg
      121 vplsavmafw laspimdpsm faltagvldl efavaktlaa iglgvfggtv vhlmmkggaf
      181 adplrdgign ggcggakira pkpvvwqfwt dadrrakfgk taltttlfla kwltlafile
      241 slmlawipae tvtaalggeg llpivtatlv gvpaylngya alplvsglie qgmapgagma
      301 flvaggvtsi paamavwala rpqvfavyig lsligafasg llfqlwtqva
//
LOCUS       WP_010399559             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: trimeric intracellular cation channel family protein
            [Campylobacter].
ACCESSION   WP_010399559
VERSION     WP_010399559.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter
  ORGANISM  Campylobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Campylobacter"
                     /db_xref="taxon:194"
     Protein         1..207
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23083
     Region          4..204
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 meafllaeyi giasaalsgf lfgikrgcdw lgvflaaflt alggglmrdv ivgrpaysft
       61 hhmpvlivig vmfiaiflkf hrenrndlek kfifimtdav dvisfsivga ivsleyglnv
      121 fgvvmvafcn gvgggilrdv llnevpwflk tglygtisms igliyyfmsl ygltniywim
      181 alfalgvifr lcayyrkwnl pqiyyke
//
LOCUS       WP_010399566             266 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Paracoccus sp. TRP].
ACCESSION   WP_010399566
VERSION     WP_010399566.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..266
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28442
     Region          7..252
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msedqrldlr ieadiarlti rrpdklnald aemvdgllpl crriersdar vviltgeggr
       61 sfcaggdiaa wsqlspedfs rrwlrdghaa fdalarlmqp viavlnghcl ggglelaaca
      121 dyrlaeahvr iglpetslgv ipgwsgtqra vrrfgasavr rmalfgevfg aeeaqrlglv
      181 dqvvptgagm aaaealaarv iarapratei tkmlvnaaeg eerervleal agsvaaasgd
      241 lreglaafre krsarfeatg rgekme
//
LOCUS       WP_010399572             380 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Paracoccus].
ACCESSION   WP_010399572
VERSION     WP_010399572.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..380
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40799
     Region          3..378
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mylndtqlqv rdmarafade virpaaeald rderfpaeiy demaklglfg igvpesmggp
       61 gfdtltyavv meelsrgyas vadqcgllel istllvrhgt eaqrkllpgi lamqqkvayc
      121 itepeagtdv sgirttavrd gdgwvlnggk iwihnapvad lgfvlartdk eagnrgmsif
      181 ivdlhaagve rgpkehkmgq rasqvgaltf tdvrlgadam lgepgrgfhm mmsvldkgrv
      241 giaalavgig qagleaaley agtrmqfgkq iaefqgvqwl ladmakdiea arllvhsaas
      301 kidngqdatk acsiakcfag dmavartada vqvfggsgyi rgfeverlyr dakitqiyeg
      361 tnqiqrmiia rellkkgaqa
//
LOCUS       WP_010399580             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HDOD domain-containing protein [unclassified
            Janthinobacterium].
ACCESSION   WP_010399580
VERSION     WP_010399580.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..279
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=30291
     Region          7..252
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mirlsfehil rqvhelpslp vvvlellssm eqddtdvhvl ahkieldqal aaktlrians
       61 sfygmqskvt siaqavsvlg fhsirtvvta cvltdsfapv rgdfdfpafw rhslataiaa
      121 rllaphlhvd petaftagll hdlgilvlvt rfpaehalvr syrqahdcqm adaemavigi
      181 dhaqvgsala aywkfpeaiq qavaehhatd rleagglpla vhmanavala ldlagiddal
      241 vpplspavwh klaldepawl allrqtqhsf demsqimla
//
LOCUS       WP_010399591             434 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Paracoccus].
ACCESSION   WP_010399591
VERSION     WP_010399591.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..434
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45669
     Region          4..434
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mgaivaslfg llfgtlaiga wigiallata iglammftgl pvdrlfpqyl fnilttpdlv
       61 alplfilmge flfrtrlset lfsglapwag llpgrllhvn vvgcsifaai sgssaattqv
      121 vgrmtlkell argyspdlai gslagagtlg flippstvmi mygvlanesi lrlftagfip
      181 gvllalvfaa yimirasakp dlvpeneral rhmpfrqrla alrdlgpvmf lilcvlgsmy
      241 gglatpseaa algvvgaflv slsqgalnlr alrdiilgtv qtcsvmgiii lgasvlgnit
      301 stlgipaava nvvtdwnlsp mllivalivl ylvlgtaleg fsmiattlpv vlplveaagf
      361 dkiwfgifmv lvvemaqitp pvafnfaviq nitarstayi arvtfpflli migfaimlal
      421 fpgivtflpd lllg
//
LOCUS       WP_010399973             219 aa            linear   BCT 01-JAN-2025
DEFINITION  DsbA family oxidoreductase [Paracoccus sp. TRP].
ACCESSION   WP_010399973
VERSION     WP_010399973.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..219
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24378
     Region          11..211
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(19,22)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mteplpgqir ldifadpvcp wcmigkaeld lalesrpdhp ftiswhpfrl dpqmpqagmd
       61 yvaymkmkfg gekgilqamk pvmeaserlg lwinpslier vpntldahrl lhwaglegaq
      121 tpvmsglmra hwregrnisn pdvlveigek agmdgrmirr llataedrde vatreiharq
      181 rginsvptfi vadshvvtga qpaslwqnvi deltglqsq
//
LOCUS       WP_010400068             332 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Paracoccus].
ACCESSION   WP_010400068
VERSION     WP_010400068.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..332
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36451
     Region          1..250
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtikigwigc grhatwmlmp qlarsgfeis avcdrdeaaa rnaarqfgak avysdyddmi
       61 anadidavgm avgpeihfra tlsslrrglp vfmekppaat aaqarellda seaakvpvtv
      121 gfmkrystgn kiaknilngg dfgqvlgihg symtaptyfa gqvdytgfyl hhcvhymdli
      181 twfagsefad lrlrknvpda gkmllhmnfe cdngvignii mgtvqsrgtp meyiqimgdh
      241 nrieveniin vawhrnppfk aedpdavldp acdslvwtpn ftaaanedhk gyhallldva
      301 atmrgesdta pqirdgwlam rrleqmiali ea
//
LOCUS       WP_010400077             547 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Paracoccus sp. TRP].
ACCESSION   WP_010400077
VERSION     WP_010400077.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..547
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=60182
     Region          5..361
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
     Region          <308..>478
                     /region_name="DUF3584"
                     /note="Protein of unknown function (DUF3584); pfam12128"
                     /db_xref="CDD:432349"
ORIGIN      
        1 mtkqklrvai yarfstdkqr dakagkfdiv laealdrlsr kladiakfhe rmehqgieih
       61 tltegkvdam ligmkgtmnq illrdigikt hrgqkgrvkd gklaggnayg ydvlpgievn
      121 gksehgdrai nraeaevvqr ifydyaqgms agkiaealni eripgprggw wgsssilgnr
      181 ergtgilnne lyvgrlvwnr lhfskdpdtg krnsrlnpqd rvtsvavphl riiddalwdq
      241 vkarqgamkt kntdvpiwdr rrpkflfsgl mtcgccgggf skvskdgfgc starkkgaaa
      301 ctnmavikqk dlearvlsal ehhlmdeeav rifceeyaae rnrlqatraa gradlekelk
      361 qvstdhkklv daiiagvpae qvkdrmield arrkdlerkl saspapdpir ihpgmtrtyr
      421 arigqlitsl qdaermdeak ealraliekv elvpapaeeg etckpglaih lhgaltsllr
      481 lacglpvhev veaaeqmqka prkaghggsn sahqgdsqdq htdnigelvl vagasnrrnl
      541 pelkcav
//
LOCUS       WP_010400094             374 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Paracoccus].
ACCESSION   WP_010400094
VERSION     WP_010400094.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..374
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40147
     Region          7..273
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msdkpvlrig ligtgfmgka hvfgfasaqk vfdlpyqlel htvadvteda aaraaadfgf
       61 ahatadwrsm vadpqidvid itapnalhke malaaisagk hvycekplap lasdarqmad
      121 aaaakgvktq vgfnylcnpm lrlaremiaa gelgeirgyr glhaedymad adgpwtfrhd
      181 pagggaladi gshalataef llgpiaevmg dcitmigqrp dgqgnmravt vddvgraflr
      241 fangaqgsie gnwiatgrkm qhdfevygtk galafsqerf nelhfystad apgrrgfrri
      301 easpdhppyg rfcvapghqi gfndlkaiei egylraiage ipepfgfaag lriqrlveti
      361 qrssaarqwm avta
//
LOCUS       WP_010400118             318 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Paracoccus sp. TRP].
ACCESSION   WP_010400118
VERSION     WP_010400118.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..318
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33990
     Region          5..235
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mslaigviga gvmggfharl faeeisgarl vavsdpdpgr agasaygaqv faeglelies
       61 dlveavlvaa pdaahhelvm aairlgkpvl cekplastva qcreiveada grnlvsvgfm
      121 rrfdpayrem kaaldagrig apllmhcvhr nleaprwfdg smivtnamvh eidicrwlld
      181 teytsasltq vgdagdmlla elhtdrgavv svemfmnaay gyhvhaeivg regtvamaep
      241 aqvrlrrgga mqagyssdwi grfadsyrlq dqawvracrs grpckdmata rdgllatgyc
      301 qqlvehlpag ggpltprm
//
LOCUS       WP_010400121             398 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Paracoccus].
ACCESSION   WP_010400121
VERSION     WP_010400121.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..398
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42642
     Region          30..286
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msknanfaga fpamgrklrl gvvgggagaf igqvhargar lsdrwqivag alssrpeval
       61 asgrdwglep drsytdwrem araeaarpdg idavaitvpn hlhfavamaf mdagidvicd
      121 kplvntlvea ralidrqret glifgvtysf aahamvrqar qmvregaigr vmqihveyfq
      181 emallpadaa wsgtpwrqdp akvggaatta digshahhla efvsglrmtd lraefhrlga
      241 dqpledtafm scrfeggvpg tllisqaaag ascglriris gtegtlewdq enpeylqhrp
      301 fnaphirisr ghgagmlsda arfvhmprgh pealsdawgn lyeefaiaie arregrdlpd
      361 gllaypglee gaagvafiqa airsnaegga wvscacda
//
LOCUS       WP_010400266             360 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sterol desaturase family protein [Paracoccus].
ACCESSION   WP_010400266
VERSION     WP_010400266.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10513792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..360
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41611
     Region          198..323
                     /region_name="FA_hydroxylase"
                     /note="Fatty acid hydroxylase; pfam04116"
                     /db_xref="CDD:397991"
ORIGIN      
        1 mahdalrpip iaeesvmddl qygtrnkrgd wtpnrpvepa plfdfpprik ailkwlphyf
       61 lpwnvifavs avaywawiip pvesmqsirl gwigwlyavn alcvllfyga felhlyvlrr
      121 qenrfkyngk fpaeqrskaf wfesqnidni lrtflsgvti wtgvevvmlw ayanghapwl
      181 sfaerpwtla lvalavpvih efhffcihrl ihtpllykwv hsvhhnsvnp spwsslsmhp
      241 vehllyfatv fyhlilpsnp vvmlyqlhya gfgaipghvg fdkvevgeng lvdshayahy
      301 lhhkyfevny gdalipldkw fgtwhdgspe gearmqqryr krkeklaark armeaggatk
//
LOCUS       WP_010400286             294 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Paracoccus sp. TRP].
ACCESSION   WP_010400286
VERSION     WP_010400286.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..294
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=32651
     Region          3..127
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,65..66,69)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(64,108..109,111..112,116)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(70,75..76,104,107..108,111..112,115,118)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93..95,104..105,108..109,112,116,119,123)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93,109,112,116,119,123)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(117,123..124)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mpligyarvs tedqtplpqs qalksagcie iheeqasggn rarpvlarvl eriskgdtlv
       61 vvridrlars lshlleview leakgaffrs lhdpidtssp qgkftlqvlg aaaeferali
      121 rertkaglas aktkgrvggn pglragdpaa lrkvrlarqd gymerlneta qdwvphvrrl
      181 rpdmawedvl rivngplpre rqwtqsrllr avnayvrdgf lpetvlgrag rretddrlpa
      241 ivaaikgadp ditlqaicsr leamrertpr grtswqpssv kmlleraerl glle
//
LOCUS       WP_010400325             787 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase [Paracoccus].
ACCESSION   WP_010400325
VERSION     WP_010400325.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 787)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 787)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 787)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 787)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17596983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..787
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82510
     Region          25..78
                     /region_name="YHS"
                     /note="Heavy metal-bindng TRASH/YHS domain, predicted
                     Cu/Ag metallochaperone [Inorganic ion transport and
                     metabolism]; COG3350"
                     /db_xref="CDD:442578"
     Region          90..115
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          131..784
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(432,434,739)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(476..478,541,557..559,588,628..630,650,653,656,675,
                     678)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(740,768,772)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mdhnhdhshg hhdhgthgga paqadpgkai dpvcgmqvti kpearhrdye gqtfyfcsdg
       61 cqskfdgdpw fyasgaaakv eksapagtqw tcpmhpeivr depgacpicg malepmipsd
      121 epsheltdft rrlwvsvaaa vplliltmge mvgipvrdwi ghrtavwlef llatpivlwa
      181 arpffqrgld sfknrspnmw tlislgvgaa ylyslfatfl pgifpeeyrm ggivgtyyea
      241 avvivalvfv gqvlelrare rtgdairalm dlapktarri lpdgteydap lenitagdll
      301 rvrpgdsvpv dsevvegrss vdesmitgep vpvekvqgdr vtggtinkng tlairatdvg
      361 adtvlsqivq mvagarrska piqgladrvs aifvpavvvi ailafvvwli fgpspsyvfa
      421 iasavsvlii acpcalglat pisittaagr gaqagvlvkn aealelmadv dtlivdktgt
      481 ltegkpaltd vtsfgdvaed ellaaaaale rasehplaea ivegakargl slgngeefea
      541 vtgkgvigkv dgrdvalgnn ammtslgidc dtgeetadrl rgdgktamfv aldgrlaglv
      601 avadpiksta eaaihdlhdl gikvimatgd nertaqavas rlgidevrag mlpegkkdlv
      661 dglrangrkv amagdgvnda palaaadvgi amgtgadvav esagltllgg dltgivrark
      721 lavatmrnir qnlffafiyn aagipvaagl lypvfgllls pmiaaaamsl ssvsvianal
      781 rlkrvkl
//
LOCUS       WP_010400437              68 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Paracoccus sp. TRP].
ACCESSION   WP_010400437
VERSION     WP_010400437.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..68
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7358
     Region          1..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mangtvkwfn snkgfgfiap eagskdvfih isaleragih hlndgqaiay dierdrngre
       61 satnlvlf
//
LOCUS       WP_010400476             604 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Paracoccus sp. TRP].
ACCESSION   WP_010400476
VERSION     WP_010400476.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..604
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=66613
     Region          5..244
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mqaivenvpf adlylselnp rtvldpagie alaanirelg liqnlgglrd esgkvgvifg
       61 grryralaml qddprfttvp vriapdasta elwatsenhq reqphpadei reygamsrkg
      121 asvpaialaf gvteahiyrr lklaslpapv ldalkdnelt laqaaaftvs ddeartlavl
      181 advrgrgiea egikrrlkse ailstdrrav fvgrdayeaa ggrlttdlfg ddvyfedeal
      241 ldelfaakla etvealcadg wkwaeasptr widysnvdnr kfgrvyaetp elteeqaery
      301 delaelaeng vlddageeel aaldalmqpv mlpeqkalsg vifcvdyngr letvtglvkp
      361 edhaaaieag ymrqpvqraq saseagkspi sqtlrddltr vltgarqhaa lrdpdllldl
      421 layqltgrmg yrsafgirtd dvpnfpttga egyeldarlt tpaerpddpf gsdlakgfra
      481 frkkgrdyvm geltrhlaal ltgadsklrs lidkevnahv revwtptaan fwtrvsgayr
      541 qkiwcdllnl kddhptattf aklkkaeqae rleklfsdpa freahgvtdk qaeriakwfp
      601 eevk
//
LOCUS       WP_010400602             232 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase, partial [Paracoccus sp. TRP].
ACCESSION   WP_010400602
VERSION     WP_010400602.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..>232
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          5..>227
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mfnfaptkei clrpyqadai enlrkgirag krrlllvagt gagktltsah llqeadrkgs
       61 yalfivdrva lvdqtsavfd eygishgivq ginsrwtpre nvqvcsaqtl arrslprdpd
      121 livvdeahcq ykatldfmar ypnavkiglt atpftkgmge hwddvvnvip trqlindgfl
      181 iepkiyvaks pddadlglns ygefsdasat magiqivgdv vqewiaktne hf
//
LOCUS       WP_010400661              99 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Paracoccus sp. TRP].
ACCESSION   WP_010400661
VERSION     WP_010400661.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..99
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11075
     Region          15..79
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 msrkpwadkg srhkrgygaa wdrirlqalr rdcylcqpcm ragriteara vdhitpkaqg
       61 gsddlanlqs icdechkdkt ardegwkrpp tigvdgwpt
//
LOCUS       WP_010400693             554 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BCCT family transporter [Paracoccus].
ACCESSION   WP_010400693
VERSION     WP_010400693.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..554
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58546
     Region          39..554
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 msqisspeps tpdasiealp ppegptqviv tdyeigqdni egvkpvafdi hnpvfmisgv
       61 avvlftaatl lfpsvlgpff gglrevvtsn fdwffliagn vfvllclgli lsplgsvrlg
      121 gpeatadfsl tgwfsmlfaa gmgiglmfyg vseplghfta alggpvveng vrtdwapldg
      181 apgdelgarr lamaatifhw glhpwaiyav valalalfay nkglpltlrs vfypilgerv
      241 wgwpghvvdv lavmatlfgl atslgigaeq asagfhflfg wstaitakiv liviitgvat
      301 asvvlgvekg vkrlseinmv lavllllfvi lagptgqilt gffgnlaayg akilplsnpf
      361 grsddnfrhg wtafywawwi swspfvgmfi arvsrgrtvr qfltavlivp slisvlwmta
      421 fggtaisetl agftgvtdaa lelqlfqmls qlpltaissf igivlvivff vtssdsgslv
      481 idtiaaggki hapvpqrifw csfeglvaia lllgggltal qamavstglp ftlvllgacw
      541 aivkgllgek rela
//
LOCUS       WP_010400793             320 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Paracoccus].
ACCESSION   WP_010400793
VERSION     WP_010400793.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Grant Pearce,F., Hudson,A.O., Loomes,K. and Dobson,R.C.J.
  TITLE     Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and
            Evolution
  JOURNAL   Subcell Biochem 83, 271-289 (2017)
   PUBMED   28271480
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Laber,B., Gomis-Ruth,F.X., Romao,M.J. and Huber,R.
  TITLE     Escherichia coli dihydrodipicolinate synthase. Identification of
            the active site and crystallization
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 691-695 (1992)
   PUBMED   1463470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..320
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0009436 - glyoxylate catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=34324
     Region          9..272
                     /region_name="DHDPS-like"
                     /note="Dihydrodipicolinate synthase family; cd00408"
                     /db_xref="CDD:188630"
     Site            order(12,44,47..49,136,164)
                     /site_type="inhibition"
                     /note="inhibitor site"
                     /db_xref="CDD:188630"
     Site            order(44,47..49,136,164,209)
                     /site_type="active"
                     /db_xref="CDD:188630"
     Site            order(48,53..54,82..83,107..108,116,120)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188630"
     Site            164
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188630"
ORIGIN      
        1 mntqiftgvi palmtpctae rqpdydalvr kgqeliaagm savvycgsmg dwplltdaqr
       61 megverlvka gipvivgtga vnsasavaha ahaqkvgaag lmviprvlsr gasvtaqrnh
      121 fkailaaapd lpaviynspy ygfetkadlf falraehpnl vgfkefggak amtyaaehit
      181 saddsvilma gvdtgvfhgy vkcgatgtit gignvlprei lhfvalskaa aagdlearqr
      241 aqelsealev lsswdegtdl vlyykhlmvl qgdkeytlhf netdeltpsq rawaeqqynq
      301 fktwyagwsk qpgavqkyaa
//
LOCUS       WP_010400978             175 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein,
            partial [Paracoccus sp. TRP].
ACCESSION   WP_010400978
VERSION     WP_010400978.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         <1..175
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
     Region          <1..175
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mgadrailvv aaddvhqdie plavarilak vaqeegagli iagkqaidnd mnatgqmlaa
       61 llgwaqatfa sklevdggka rvtrevdggl qtievslpav vtadlrlnep ryaslpnimk
      121 akkkpldekt agdygvdvsp rlevlktrep egrkagirvg svdelvgklk eagvi
//
LOCUS       WP_010400141             386 aa            linear   BCT 01-JAN-2025
DEFINITION  phage portal protein [Paracoccus sp. TRP].
ACCESSION   WP_010400141
VERSION     WP_010400141.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Dedeo,C.L., Cingolani,G. and Teschke,C.M.
  TITLE     Portal Protein: The Orchestrator of Capsid Assembly for the dsDNA
            Tailed Bacteriophages and Herpesviruses
  JOURNAL   Annu Rev Virol 6 (1), 141-160 (2019)
   PUBMED   31337287
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Prevelige,P.E. Jr. and Cortines,J.R.
  TITLE     Phage assembly and the special role of the portal protein
  JOURNAL   Curr Opin Virol 31, 66-73 (2018)
   PUBMED   30274853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..386
                     /product="phage portal protein"
                     /GO_component="GO:0019028 - viral capsid [Evidence IEA]"
                     /GO_component="GO:0044423 - virion component [Evidence
                     IEA]"
                     /GO_function="GO:0005198 - structural molecule activity
                     [Evidence IEA]"
                     /GO_process="GO:0019068 - virion assembly [Evidence IEA]"
                     /calculated_mol_wt=42448
     Region          1..356
                     /region_name="BeeE"
                     /note="Phage portal protein BeeE [Mobilome: prophages,
                     transposons]; COG4695"
                     /db_xref="CDD:443730"
ORIGIN      
        1 mnlfkrmfgp revkgynpen kedrvffkgi gdfgsrefts vaaalragft iasgmgllpl
       61 qaegrggdnl aalindepnd lltgvefkel mtlhavfaga grafirrdpl gkpveliplh
      121 pswcgpwvyk dgehvlpvsi eeggiwgdft rkdilevtsp rwnmlsgldv thacchvlgl
      181 srklqqkqaq yadtnapygv lfvkegeskd gvrrlkesws kqfgrsgiav vdmdgkfqql
      241 aqsstdqqln ealkfqveei ariygvhpyf lmqtagsgaq gavadvmlfh qaytmapwin
      301 rwegalrrsl fkgsqsmpnf denalmrttp qvraeiysra lggggnapwm tadevrsgas
      361 pfnlaakgdn fwkagnkqeg qdeapv
//
LOCUS       WP_010401261             309 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Wolbachia endosymbiont of Nasonia
            vitripennis].
ACCESSION   WP_010401261
VERSION     WP_010401261.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..309
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34440
     Region          2..302
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mfftlflkil piyitiligy lagrylkidr ntisqilfyi anpivilygv shtevnlkvi
       61 slpiliwfig stmslsvyyl ssflfkdntr nilafssgst smgyfglpia ialfdedsvs
      121 vyvvcyigma lfenslgfyi aangiytake cvlkllklps lyamilgffl siydiqiptf
      181 ltdvminirs tfitlgmvll gvsiaqitnf kvdwklaltt ivakyifwps fvlgivlldk
      241 hvtgiydesi ykalmllaii pisgssiila nilnyqpdka tllllistav glfyvpliis
      301 lfftklvpf
//
LOCUS       WP_010401464             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter ATP-binding protein
            [unclassified Wolbachia].
ACCESSION   WP_010401464
VERSION     WP_010401464.1
KEYWORDS    RefSeq.
SOURCE      unclassified Wolbachia
  ORGANISM  unclassified Wolbachia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="unclassified Wolbachia"
                     /db_xref="taxon:2640676"
     Protein         1..243
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26578
     Region          20..238
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mshiniekks ifakklsnvn ncilkienlt lsygnkkvld ninisvqrgd ivtilgpngg
       61 gktslvkava ginkgyigsi lfadnvkisy mpqnfsignl mpitvesflf nssskrfkkn
      121 qsivteaiel vgignilknq vleisagqtq llllarclis esdliildep vsamdinara
      181 kfydiinkia kersvsilmt shdlnsalps sdyiicinnt iyyqgkpdei meineifgsy
      241 aak
//
LOCUS       WP_010401701             544 aa            linear   BCT 01-JAN-2025
DEFINITION  ribonuclease J [Wolbachia endosymbiont of Nasonia vitripennis].
ACCESSION   WP_010401701
VERSION     WP_010401701.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..544
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=60404
     Region          4..544
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mninkneflf lplggvgrig mnvslyhyqg kwimidlgig fadetmpgve lliadvdfia
       61 qrkkdllgii ithahedhcg avphlwedlq cpiyttkftv nflkeklkef rlegvvpvke
      121 vdingsinlg pftvefinvt hsipeansil isteagsalh tgdwkfdpkp vvglisnier
      181 lkeigdkgdl laaicdstni lskhdpeses eiydniynii krskkliavs lfasnvarie
      241 tiakaaqaln rkvvllgrsl wrivkvaqds gyltdspefl eakeavnfpr eklvllctgc
      301 qgeplaatsr lankshqafk mqqgdtmifs skiipgnetr ahnmlnafie mgvevitekt
      361 envhasghpv kaelremysl ikpkiaipvh geyihtdahv kfakecgvkk aimiapgdiv
      421 nlengekvss idvdyfgidg mllrhpecsv ikmrermrda gvivvtaivn kknkllakpk
      481 vfapgvfeaq edaaimqkii ekvesafspq pikkirnkie ssifsilkey llkrpiievq
      541 ieqv
//
LOCUS       WP_010401966             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [Wolbachia].
ACCESSION   WP_010401966
VERSION     WP_010401966.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia
  ORGANISM  Wolbachia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 268)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Wolbachia"
                     /db_xref="taxon:953"
     Protein         1..268
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30684
     Region          28..>248
                     /region_name="RepA"
                     /note="RecA-family ATPase [Replication, recombination and
                     repair]; COG3598"
                     /db_xref="CDD:442817"
ORIGIN      
        1 mlqdfftitq kipffsvkey lddqspiped ivspriltkr gllvfggppk igksdflisw
       61 lvhmaagrsf lgmmpsrplk ifymqteiey dymkerlqql qldkelldia annliitprv
      121 qlslsseeid eikntvkerf kpdiiaidpl rnifnsseyg nendnsamlf flqktleklr
      181 nvinpdasvv lthhtkklsk kmleedpfqg lsgagslrgf ystgmvmfah deessvrqvv
      241 felrngervp nklvdkingh welvdqws
//
LOCUS       WP_010402073             323 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified
            Janthinobacterium].
ACCESSION   WP_010402073
VERSION     WP_010402073.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..323
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33326
     Region          21..323
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtihsspsyl qrsladlkny agligallam cvlfsfasen fftlatlstl snniptlvvm
       61 avgmtfvlii ggidlsvgsv malaasvlsl avvhwgwpvw saallgmfva avcgattgli
      121 svgwripsfi vslgvlemar glayqvtnsr teyigsavdg isspiafgls pafiaaiaiv
      181 vighlvltrt vlgrhwigig tneeavrlsg intkpskvlv falmgflagv galfqvsrle
      241 aadpnggvgm elqviaavvi ggtslmggrg svistfigvl iisvleagla qvgvsepvkr
      301 ivtglvivaa vvldtyrrrg era
//
LOCUS       WP_010402136             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Janthinobacterium].
ACCESSION   WP_010402136
VERSION     WP_010402136.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..305
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33622
     Region          4..224
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtaiqitnve ksykslkalg gvslaieege ffgllgpnga gkttlisiia glirpdagsv
       61 kihghdvvsd frnarrnlgv vpqelvfdpf ftvretlrlq sgyfglpnnd kwidevmenl
      121 dltgkadtnm ralsggmkrr vlvaqalvhk ppvivldept agvdvelrqt lwkfisrlnr
      181 egghtvvltt hyleeaqamc qrvamlkagk vvaldtmsal irriagsqlq lhlkhgglpa
      241 dlqhlllhpq eqqapnkfsl rineysevek ilahlreagv eidemqlqqa dlediflqim
      301 dkgtv
//
LOCUS       WP_010402231             314 aa            linear   BCT 01-JAN-2025
DEFINITION  FecR family protein [Sphingomonas echinoides].
ACCESSION   WP_010402231
VERSION     WP_010402231.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..314
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32850
     Region          75..312
                     /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"
ORIGIN      
        1 msglsespqq hadltdeaaa wlaaldagsa dvaafeawre adirhavafv evastwrdld
       61 alrlangela regraepivp erpgrrhilr aaasvavavv vgggfayraa arasattavg
      121 qrktvaaapg lsldlntdtr vswkagmpar vwleqgeiav rlaalhrlel ltpggkflle
      181 pgaynarlrg agcelailsg ggtfegttrr igagdvalan agqmalrdap dlgsigawqh
      241 dtlvlngqsl dyalaemnry lpdkivigdp dlsrlrlggt fsttnpaefl qalrtsfgvr
      301 attganggiv ltri
//
LOCUS       WP_010402321             213 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Sphingomonas sp. PL20].
ACCESSION   WP_010402321
VERSION     WP_010402321.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PL20
  ORGANISM  Sphingomonas sp. PL20
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Sphingomonas sp. PL20"
                     /db_xref="taxon:2760712"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23570
ORIGIN      
        1 mptpqksadk lmkkrdsrae drrarilsaa rqlfiqygfh asgvariaad sgvkvgqlyr
       61 dfaskediva elvradvvef ldepalraav eardfalvra wiarfleedp ndpgsyalfa
      121 emfaeatrnd rvgdilrgid alvrdnilsa lgalapgeer aarrseladf ilaighgvlf
      181 rrisdpdvhh aelsryigql idselakimq dpr
//
LOCUS       WP_010402285             303 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Sphingomonas echinoides].
ACCESSION   WP_010402285
VERSION     WP_010402285.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..303
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32106
     Region          2..183
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          215..297
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdplsdilsl lkpnsygfrg ldaggawals fgaddsircy avqsgacwla ldgtaepvrl
       61 aagdfvllpg gkgyrlysta eapvtdafrf fpavpageta vlnggggvlg vggyfgfegm
      121 haelllgmlp sivhvraean kaalrssidr lmgelrepkp gsallaehlv qalliealrl
      181 hlaehsrhrs gwlfaladrq msavigamha epgrkwtles lakvaglsrs sfavrfkatv
      241 gepamdyltr wrmmiasdrl anggmpialv aptvgyeses afgaafkrvm gysprqfara
      301 aap
//
LOCUS       WP_010402537             414 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Sphingomonas
            echinoides].
ACCESSION   WP_010402537
VERSION     WP_010402537.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..414
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=46251
     Region          15..144
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          226..375
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meapdtippe edtstkrfra krdailaaaa eaineqsakg mtfadvarrv glnttsvtyy
       61 fkrkedlaaa cfehtldrll gmleeslaep tprarvakyl slnmarlari qrgeetsfai
      121 lsdlrameep vlgrlmagwr evfrktrslw gpttnraqtd lhggrahvll entfwlpvwl
      181 nrydldqypr veerlmdvfa hgiagpnerw spelidlahd epepgreafl laatrlinql
      241 gyrgasvqki aselnvtkgs fyhhldakdd lvlacykrsl dtvadaqrla derggshwdr
      301 lsgtiatlld vqfsergpll rttalsglps qarlamvdrs nriarrfagt msdgiaegsi
      361 rpvdpliaaq almamqnaaf dmrkwahtms reraigyyas tlafglfddr ildt
//
LOCUS       WP_010402576             223 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Sphingomonas echinoides].
ACCESSION   WP_010402576
VERSION     WP_010402576.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..223
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23227
     Region          43..221
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 msgaawdavd gyivdhllgd davldaalaa naaaglpqid vspaqgkmlh lfarmvgarr
       61 ileigtlggy stiwlaralp eggrvvtlei dphhaavagd niaraglgdr veirvgaalq
      121 sleamiaqge apfdlvfvda dkencvpyvr aamalarpgt tivvdnvvre gevldpastd
      181 srvhgvralf dmiaseprls atavqtvgak kwdgfvlavv eti
//
LOCUS       WP_010402649             333 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Sphingomonas
            echinoides].
ACCESSION   WP_010402649
VERSION     WP_010402649.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..333
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34596
     Region          1..329
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,223,
                     245..246,248..249,269..271,321,323,325)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mrallskaag gpetlviddl pdpvagpgqv vvavkacsin ypdvliiedk yqfkpprpfa
       61 pgseiagvid svgagvtewk pgdrviamtg sgglvekial pvaslyrlpe grsfaegasl
      121 lltygttiha lldrghlaeg qtllvlgaag gvglaavelg kafgarvvaa vsseekaeaa
      181 rqagaddtiv yarapfdkdq skalaeqfka aggkggydvi ydpvggdyae palrsigweg
      241 rylvvgfpag ipklplnltl lkscdvcgvf wgafaardpe anrahierlf llwrdgqiap
      301 rvtetfafed ggkaiakmaa rgaigklvvs vse
//
LOCUS       WP_010402659             122 aa            linear   BCT 01-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Sphingomonas
            echinoides].
ACCESSION   WP_010402659
VERSION     WP_010402659.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..122
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=13635
     Region          3..121
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 maerisdaeh tvmevlwdes pltaqdvaer ipagrewsan tvktllgrll aknviaheed
       61 grrylyrplv qreeyvages rklmdrlfgg klsplvahla erdaltaqdi aeieallkel
      121 ka
//
LOCUS       WP_010402689             308 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Sphingomonas echinoides].
ACCESSION   WP_010402689
VERSION     WP_010402689.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..308
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33319
     Region          1..241
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mspiriaivg lgkiahdqhl paiagspefe lvaaatlagt ladvpvfasv eamldadiai
       61 davamcqppq vrfdaavqai ragkhvllek ppgatlseve altrlseaag atlfaawhsr
      121 fapavhdara wlterrinhv eitwkedvrr whpgqqwiwe pgglgvfdpg inalsiatri
      181 lprhfylhdg tldfpanraa piaaelnmig msgapvhavf dwrqtgpqtw divvdtddgt
      241 lalthggsrl aingvvresa peaeyaalyh hfaaliakge sdvdrtplrl vadaflrcrr
      301 rdtdpfdd
//
LOCUS       WP_010402721             390 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Sphingomonas echinoides].
ACCESSION   WP_010402721
VERSION     WP_010402721.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..390
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=40915
     Region          19..388
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mtpsartqaa ielldqiiag ardsgaaadt ivaryfatrr yagskdrrav relvyaaira
       61 lgerpasgra avlalakadp elaatfdgvg hgpavigpse tpaktgiapn wildrlrqsg
      121 lddaefpali drapldarin raiheaieie gaepiaglad glrlpsgtqv eqlpaynhga
      181 ievqdagsqf vtlaaraqag qrivdlcaga ggktlalaaa mggqgvvlat dtdrarlsrl
      241 apraerarag iietrllnpg revemlddwv gsadcvlida pcsgtgtwrr npearwrltp
      301 drierlvetq rhllevgatl vkpggalvyi vcslldeega gqvatflaan pgwraqpldl
      361 gagraqgagt rltpahdatd gffvarlqha
//
LOCUS       WP_010402752             179 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CinA family protein [Sphingomonas].
ACCESSION   WP_010402752
VERSION     WP_010402752.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..179
                     /product="CinA family protein"
                     /calculated_mol_wt=17825
     Region          9..153
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mdtilpaqlv eaarkvvaan laagrrvala esctgglvaa aiteiagsse mfesgfvtys
       61 ndaklemlgv sadvletfga vsvatawsma qgaleasgad vavaitgvag pgggtekkpv
      121 gtvvfaraer gadpghvvad rkdfgdlgrg gvrlqaalca lelllpsedd tapeaeeap
//
LOCUS       WP_010402770             258 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Sphingomonas echinoides].
ACCESSION   WP_010402770
VERSION     WP_010402770.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..258
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28071
     Region          2..253
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mfadshchln ykglgeqqda vlararargv hamlniatre sewdavlata erepdvwatv
       61 gihpneadeh pdigtarlve raqhprvvgi gesgldyfye hsdrerqras frahiaaare
      121 tqlpivvhtr daeddtaail reemgkgayp gvihcftasg afadialelg fyisisgivt
      181 fknakdlqdt aarlpldrll ietdapflap vphrgktgep afvadtaafl aklrgeplet
      241 laaataenfh alftktra
//
LOCUS       WP_010402802              90 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HPr family phosphocarrier protein [Sphingomonas].
ACCESSION   WP_010402802
VERSION     WP_010402802.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..90
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=9042
     Region          2..90
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 mavsrsvlit nkrglharas akfvtlaatq pcevlvekdg agsvtgtsim glmmlgaamg
       61 dtivisadge daetavsalc dlveakfged
//
LOCUS       WP_010402812             174 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: gamma carbonic anhydrase family protein
            [Sphingomonas].
ACCESSION   WP_010402812
VERSION     WP_010402812.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..174
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17779
     Region          1..170
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mplyeidgfr ptlgynawva psadligdvq lgpdvsiwfg avirgdntpi vvgarsniqe
       61 gamchsdpga pltigedcti ghhailhgct vgdgvligmg avvlnraeig agsivgagal
      121 vtegkvfppg slivgspara vraldedaqa mlrvsaehyv angrkyaagl krvd
//
LOCUS       WP_010402878             287 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Sphingomonas echinoides].
ACCESSION   WP_010402878
VERSION     WP_010402878.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..287
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29606
     Region          52..267
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mrrigptqkg faaivltill lagatpvlsq sihdriypap ttpiatatlp agaervavht
       61 sdglsitgaa iaaapgkptl lvfhgngssa mstldwfapa iakgygvvaa eyrgysgnpg
      121 radeaglard adafyaearr ragggrlivv ghslsggval glasrqklda lvtigtftsl
      181 ramvpkiara fvsdrydnla tvptldepyf lihgladdtv paamgqelhk aayaakrtgf
      241 slviqganhh pdgallaail emivahldhp daaplalpdt vkmygfg
//
LOCUS       WP_010402951             327 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Sphingomonas echinoides].
ACCESSION   WP_010402951
VERSION     WP_010402951.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..327
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34336
     Region          82..309
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mldrrlvlag avgatlgmps valaqsgdtt atptwppaes fplwpgkapg apatlpipap
       61 sfdgyqgkel wlrgiavptv gvfrperpdg ravlsipggg ygfvsvsneg idvarvlnar
      121 gitvfvlayr lpgegwakre dvplqdaqra mrliranatr ygidparlgt igfsagghla
      181 gmlavghadp vytpvdhadh lsarpdfagl iyavtsfqta gfdptapvng llgpkpsaal
      241 ldrydparrl dssapplfla hamddgvvpi aqsllmldra riervpveah lfqhgghgfg
      301 alhlaagspg ldwpelfsrw saalprp
//
LOCUS       WP_010402972             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter, partial [Wolbachia endosymbiont of Nasonia
            vitripennis].
ACCESSION   WP_010402972
VERSION     WP_010402972.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12081071
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..>290
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          3..>280
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 menkawfiwl isnlivvfsn mqiiytfisv nlekelglti aqvalansay twtfaisqff
       61 sgamfnvfss kkiyffslsi mlfgffvlik sdnfahlils qfliaigasf gfigaahvss
      121 tyfpltqfgl mfslvqtiss lsalmiqmcf ssllaegadw knlivcvilf gvsifvlmff
      181 ypkglskknl geytikssik tvicsvltvl klrdiwitsi vgaitfgtfl alnmlwaprl
      241 lsnlelntme lgvatailwl glavgapiad lisnlfknrr hvicnsldli
//
LOCUS       WP_010403008             619 aa            linear   BCT 01-JAN-2025
DEFINITION  terminase large subunit [Sphingomonas echinoides].
ACCESSION   WP_010403008
VERSION     WP_010403008.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..619
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67720
ORIGIN      
        1 mpssapvrad apgeidpttr waqaavrgdf pvgdfvrgaa erhlrdlrea skrgyffrpe
       61 laqraldffp svftitdgpa agkpfhllpy qvfavgslmg wvnadgrwrf rsawietgkg
      121 qaksplmggl glyamgwcgf prsqiyaigg dkntanvlfq davamcraqv pgydegetle
      181 glghvkiggi gknahtiehp asqsfflpla sgenqsgprp rmvladeihe fktdaqieiw
      241 rraitkvags ammvlgtnta aisshvgngy seiyqdiatg kkrddtafsl vfrvdkkdre
      301 nvftneacwq kslpalgity piqnireevq tattsklsaa ssvkrlyfgi ptgaadfwid
      361 eekfaavlgp vddaaiaalk gcrcwlsldl skkndltalt atwldgagvl wqktwywttk
      421 dgladraktd napyeewveg chlvavpgat idksfiaaqv aricaehnvv elvfdpaqfa
      481 dfetaceeig fpawkfegpd kpegtglkmv rhaqgvkvmf edrqhcmprs ierfedrilk
      541 qtividdspv tyscaanaam vtdgqanraf dkkrsrgkid givtcamgag aadnielegt
      601 kydgkffvdl dddddedpl
//
LOCUS       WP_010403049             129 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator [Sphingomonas].
ACCESSION   WP_010403049
VERSION     WP_010403049.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..129
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=13785
     Region          1..124
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mnilfieddp mnrrvvkdml dvagatmtga esgeiglali daqdfeivll dlrmpgmdgf
       61 etlrhirars dakahlpviv vtadtavdlr erciaqgade vlfkpvamds lfdaigrmla
      121 kgagdgmig
//
LOCUS       WP_010403064             222 aa            linear   BCT 01-JAN-2025
DEFINITION  YoaK family protein [Sphingomonas echinoides].
ACCESSION   WP_010403064
VERSION     WP_010403064.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..222
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22968
     Region          3..208
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mirydarqrs favclsalag fvdaigfiat ggffvsfmsg nstrlavgva qhhaaallal
       61 qliatfvggv vigsmigria gryrhplila wmavllalag tagesgavwa aaslmalamg
      121 aentvfeedg evrlgltymt gtlvklgqrl alalqggprw awlphfylwi glvggaitga
      181 atfpllgfgg lwiasavlva lavftifrge vlfgvatakd pa
//
LOCUS       WP_010403120             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fasciclin domain-containing protein [Sphingomonas].
ACCESSION   WP_010403120
VERSION     WP_010403120.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Clout,N.J., Tisi,D. and Hohenester,E.
  TITLE     Novel fold revealed by the structure of a FAS1 domain pair from the
            insect cell adhesion molecule fasciclin I
  JOURNAL   Structure 11 (2), 197-203 (2003)
   PUBMED   12575939
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..204
                     /product="fasciclin domain-containing protein"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=19864
     Region          47..188
                     /region_name="FAS1"
                     /note="Uncaracterized surface protein containing fasciclin
                     (FAS1) repeats [General function prediction only];
                     COG2335"
                     /db_xref="CDD:441906"
ORIGIN      
        1 mtfktnlyla tvagalafga aataqtapaa paapaapaaa papnptvgga vmdatkpiat
       61 naaaapnltt lvsavkaagl attlagpgpf tvfaptndaf srlapgtvdt llkpehkatl
      121 akvltyhvvp gtltladiqa kvtagggkav lttvegeplt ielvgggvql tdvngnksyi
      181 etpdvaqsng vvhvvngvls pklg
//
LOCUS       WP_010403126             108 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Sphingomonas].
ACCESSION   WP_010403126
VERSION     WP_010403126.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..108
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11708
     Region          13..100
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 miaaefepvv qtdrrrspra pisldaklgr ggldralckv tnvslhgakl htyspmkkga
       61 riwltlprig qviativwad dfeagcqfqe plddttfaal tganvefv
//
LOCUS       WP_010403157             687 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M13 family metallopeptidase [Sphingomonas].
ACCESSION   WP_010403157
VERSION     WP_010403157.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..687
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74501
     Region          43..687
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mrrsfvmvsl lasaalvgvt hanpapkakv aakaepapka tgaeigafgl dlagmdtsvq
       61 pgddfvkfag gkweaateip adkatygmfn rladrsleqt rtildaaakr pgdkigdfya
      121 sfmdeaaina kgidpikpwi aeiraagdkt alaaemaklq rtgvgglfrm gvgqddkapd
      181 tyivglsqsg iglpdrdyyl kddpkladtr akyqayqvqm lglagvddaa argaavyafe
      241 kalatahwdr iksrdsdlty nkwsaadfat kapgfpwevy mktagtagqa nylvgmpsal
      301 tdeakafada pvqvvqdfli lrllrsyagv lakpindanf afygtvlsga pqqpvrwkrg
      361 vgivsgamge qvgqayveqy fppatkaaad qlvkniiaam svrldnltwm apetkvkaha
      421 klaaftpkig ypskwrdysa ltvkrddiva nvaaanafey erdlhklgqp idrtewgmtp
      481 mtvnayanpp mneivfpaai lqppffdaka dpavnyggig vvighelshh fddqgrkydp
      541 tgkltdwwta edvkrftamt dklvkqyday eplpglhikg gltlgenmad laglalayda
      601 yhrslggkpa pvidgltgdq rfflgyaqvw rikfrepalr sqvisnehsp gpfrtvevrn
      661 vdawykafgv kageklylap adrvkvw
//
LOCUS       WP_010403201             139 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein, partial [Wolbachia
            endosymbiont of Nasonia vitripennis].
ACCESSION   WP_010403201
VERSION     WP_010403201.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12158766
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         <1..>139
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <6..49
                     /region_name="Ank_5"
                     /note="Ankyrin repeats (many copies); pfam13857"
                     /db_xref="CDD:433530"
     Region          8..39
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 ddvqderhgr talhwaayhd kfeivkllvn kgadwnikdr dgktaldlvg tkslylvree
       61 nreksssesk itkflegldd ktplhlnikk dpesknidnq rpqrsivdke enimnnkkvs
      121 ieetidnnny rrgkmpkni
//
LOCUS       WP_010403248             209 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YceI family protein [Sphingomonas].
ACCESSION   WP_010403248
VERSION     WP_010403248.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..209
                     /product="YceI family protein"
                     /calculated_mol_wt=21894
     Region          32..209
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mrlthlytat aavllfgapv vaqmappeml rgagtvtdvk agtyavephh tqvtfsvshf
       61 gispyagtfs dasgtlkldp akpaetqldv tlpiasvqtt ssvltgelks adwfdaakfp
      121 tatfhstkvt qisgdavavd gtltlhgvtk pvtfraklfg aatnpmskka sigflgrmvi
      181 hrsdfgvsky vpvvsdetvl vinaafelq
//
LOCUS       WP_010403257             498 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA recombination protein RmuC [Sphingomonas echinoides].
ACCESSION   WP_010403257
VERSION     WP_010403257.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..498
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=54486
     Region          <26..>243
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          163..453
                     /region_name="RmuC"
                     /note="RmuC family; pfam02646"
                     /db_xref="CDD:460637"
ORIGIN      
        1 mtgvtmalfg vaallvglai gfllgirgta qaraerdarn edfkraivdl asaeeraret
       61 aqlrtelaai rderdvarle ntalkthssa fesrlaemre adearlqmvr etheariael
      121 lhakellaaq faevsnklln eaqevflkra derfrqseet agqnlksmlq pvsdrllkye
      181 eavtkveser lsafdqlkgq leglrvgqek vsseaaklvn slrnapksrg rwgeqqlknv
      241 lescglseht dfqtevsvsg gdeggrlrpd aivtvpggrs lvidakvsln ayqdafgavd
      301 eaerarglal haaamrahvn glgnkaywsq fadapdyvim fvpgehflsa aleqdptlwd
      361 fafdkrvlla tptnliaiar tvaavwrqer lakeaaeigr lgkemhdrla kvaddlrkvg
      421 aglnsavnnf nsfsnsfngr lmvtgrkfrd lnietgarel edvapveala rysdseplql
      481 aepgvvsvge aeaevakp
//
LOCUS       WP_010403256              93 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SWIB/MDM2 domain-containing protein [Pseudomonadota].
ACCESSION   WP_010403256
VERSION     WP_010403256.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadota (proteobacteria)
  ORGANISM  Pseudomonadota
            Bacteria; Pseudomonadati.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12970643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     Protein         1..93
                     /product="SWIB/MDM2 domain-containing protein"
                     /GO_component="GO:0016514 - SWI/SNF complex [Evidence
                     IEA]"
                     /GO_function="GO:0061629 - RNA polymerase II-specific
                     DNA-binding transcription factor binding [Evidence IEA]"
                     /GO_process="GO:0006338 - chromatin remodeling [Evidence
                     IEA]"
                     /GO_process="GO:0006361 - transcription initiation at RNA
                     polymerase I promoter [Evidence IEA]"
                     /GO_process="GO:2000819 - regulation of
                     nucleotide-excision repair [Evidence IEA]"
                     /calculated_mol_wt=10042
     Region          22..91
                     /region_name="SWIB-MDM2_like"
                     /note="SWIB/MDM2 domain found in SWIB/MDM2 homologous
                     proteins; cd10567"
                     /db_xref="CDD:349489"
     Site            order(39,42..43,45..46,49..50,55,60..61,63,83..84)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349489"
ORIGIN      
        1 maktptaksd apktggifap itpsaelgai vgtdklprse viskvwayik ahnlqnpenk
       61 reivadeklk kvfgkdkvtm femnkhlagh mka
//
LOCUS       WP_010403307             224 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sphingomonas echinoides].
ACCESSION   WP_010403307
VERSION     WP_010403307.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..224
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23580
     Region          3..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msepvlsvag ltrafsqgge tievlrgvdl hvgageival lgpsgsgkst llqavglleg
       61 gfggsiriag eqvakldsdg rtrvrrdslg fvyqfhhllp dfnatenvvl pqlirdrtha
      121 eanaratall salglghrlt hrpsqlsgge qqrvavaral anqpalvlad eptgnldeat
      181 advvlaeflr lvrgegsaal vathnermal kmdrvvrlhe grla
//
LOCUS       WP_010403369             207 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Sphingomonas
            echinoides].
ACCESSION   WP_010403369
VERSION     WP_010403369.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21904
     Region          11..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mlqnatrsrg rprsfdekqa lekailvfra kgydgvtidd lvagmgvgrp slysvfgdkr
       61 tiflralkty aeaygalaak alfspptvra slvgflrhav esataegtap gclfacvapl
      121 vddaevrqfv qdvaaasaaq verrfqdgmv tgevppdfpa saraiqvmdl arglvmraqm
      181 gtprktllkd aedavglvlp pspkpaa
//
LOCUS       WP_010403382             309 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Sphingomonas echinoides].
ACCESSION   WP_010403382
VERSION     WP_010403382.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32702
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,216..221,
                     227..228,230..231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdrleelrtf vavadlasfa eaarqmrisp taasravasl easlgtallr rttrsvrlte
       61 egaaylercr aalvelddaa lslrgdgatp ggtlvitapv tfgrlhilpl vnhllrahpa
      121 lrvsltlidr vvrlvdegid vavrigdlsd sslhalkvae vrrilvaspa ylaargmpan
      181 ipalhdhdli sfaeidrape wrfgpagkpa irieprlivn tadaaiaaav dgmgiarvls
      241 yqaidaiaag tlvslhddaa pppvpvhlvy qanrrgsvnv rafveaardh fggldltara
      301 ptgrpgprs
//
LOCUS       WP_010403453              50 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2256 domain-containing protein [Sphingomonas echinoides].
ACCESSION   WP_010403453
VERSION     WP_010403453.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..50
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..50
                     /product="DUF2256 domain-containing protein"
                     /calculated_mol_wt=5709
     Region          7..49
                     /region_name="COG4338"
                     /note="Uncharacterized conserved protein, DUF2256 family
                     [Function unknown]"
                     /db_xref="CDD:443479"
ORIGIN      
        1 mpngvaktnl pektcpvcqr pfawrkkwar dwdsvvycse rckrarisav
//
LOCUS       WP_010403471             436 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A [Sphingomonas
            echinoides].
ACCESSION   WP_010403471
VERSION     WP_010403471.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..436
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47239
     Region          9..433
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mpdlfatfdp paadqpsata pladrlrptt laevvgqdhi tgpegaigrm vaagrlssmi
       61 lwgppgtgkt tiarlladav glrfmaisav fsgvadlkka faeardharm gkrtllfvde
      121 ihrfnraqqd gflpyvedgt vtlvgatten psfelnaavl sraqvlilhr ldhaalgkll
      181 draeqveerp lpltpearda miasadgdgr fllnqaetlf avhlpepldp aglsaflqrr
      241 vavydkdreg hynlisalhk avrgsdpqaa lyylarmlta geeplyllrr mvrmavedig
      301 ladsnaltlc laakdaydfl gspegelaia qaclylatap ksnaaytaqk aawksaretg
      361 slmppeniln aptklmkdig ygkgyaydhd taegfsgany wpaemapqtf yvptergmek
      421 riaermawwa slkgde
//
LOCUS       WP_010403488             303 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Sphingomonas].
ACCESSION   WP_010403488
VERSION     WP_010403488.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32294
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,147,161,163,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,190,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mrlpdleawa ifasvvehrs fsgaadaigv skatvskavt rlethlgqsl fhrtsrrlsl
       61 tengkalaeh aarilaeana aeeaahaaat aptglvrvaa pmslgliaia pviadflklh
      121 pgiaidlhls darvdivaeg fdialriasl pdsslrarkl adirinlvas pdylarygrp
      181 thpgqlgehr cfaytnitap wrfvgpdgte vsvrlqgpla tnsgeamlpa lrqglgiaml
      241 pdfiigedla tgrletilen wtpyggalhl mtppgtlrpa rvevliayls ehlrtlcsvk
      301 tpk
//
LOCUS       WP_010403506             327 aa            linear   BCT 01-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Sphingomonas echinoides].
ACCESSION   WP_010403506
VERSION     WP_010403506.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..327
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36277
     Region          107..318
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mdtrtaelak irdldrywae atfrapkrlp wmqtrillds lglgleqtvs ylgrqpdyqt
       61 flawvlatag ppaadriary hawldaaqsp pataerlaai aaapdvldad dlaqwdalgf
      121 vilrgalspd eakacedllw qqvggtpddp atwytrrpng imvqyfqhpa ldvartaprv
      181 hkafaqlwgt adlwmtvdrm sfnpperpgy tfpgphlhwd vslaqpipfa tqgilyltdt
      241 radqgalqlv pgfhhrlpdw ldalgdadpr rvdlsaeait ipaaagdlii wrqdlphgas
      301 pnasdrprma hyvnmyaptl tahsvwr
//
LOCUS       WP_010403513             397 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Wolbachia
            endosymbiont of Nasonia vitripennis].
ACCESSION   WP_010403513
VERSION     WP_010403513.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..397
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43802
     Region          1..397
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,173,205,233,235..236,244)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,198,242..244,273,276)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            236
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 msdlakrmsl ikpsptiavt dkanrlkseg kkicvlaage pdfdtpdhik kaaiqsineg
       61 ktkytavdgt helkeaiink lkrdnnleyt lnqicvgaga kqvlfnlfma tidpgdeaii
      121 papywvsyvd mvnlfgglpv vveckqnfkl tpellkskit kktkwlilns pnnpagivyt
      181 ydelksiaqv lleyphvniv tddiyehivy dekfftiaqv epklydrvfv vngvskayam
      241 tgwrigyiag rsdivkaist lqsqstsnpn siaqaaavea lngdhsflke rtkifkdrrd
      301 fvvkklnsas vlsvsipqga fylfvscegl lgkstksdkv insdldfaey lledhlvavv
      361 pgiafglknf irisyatsqe qleigcdsit kacemls
//
LOCUS       WP_010403563             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [unclassified Wolbachia].
ACCESSION   WP_010403563
VERSION     WP_010403563.1
KEYWORDS    RefSeq.
SOURCE      unclassified Wolbachia
  ORGANISM  unclassified Wolbachia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="unclassified Wolbachia"
                     /db_xref="taxon:2640676"
     Protein         1..262
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29439
     Region          2..255
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mivdshchli yfsddeipkv israeqngvr ilhnicisin dipkllkiss sydqvycsvg
       61 ihpldtnvek gecinadeli eftkgkkvis igetgldfyk sdnksnqkks fashieaakv
      121 tglplvihtr nadsemidml nsemkkdafs gvmhcfassk elaykamdlg lyisfsgiit
      181 fknanllrei aqnvprervl vetdapylsp epyrgrknep amvkyvvncl aelwnespeq
      241 vakittnnff rlfsklelke il
//
LOCUS       WP_010403577             131 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Sphingomonas echinoides].
ACCESSION   WP_010403577
VERSION     WP_010403577.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..131
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=13524
     Region          13..126
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 matatarigt afyrteittg hhtliadepa srggadagpa pydlllsalg actaitlrly
       61 adrkgwsiet ldvalrlvgs adgnriervl tivgpdaaaq arlaeiaert pvtltlksgi
      121 aihttlstta l
//
LOCUS       WP_010403587             138 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Sphingomonas echinoides].
ACCESSION   WP_010403587
VERSION     WP_010403587.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..138
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14917
     Region          17..137
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtghetprfv saildwpptw fvvrlallsa yliggvaklg dwpsavaeqv hfgvhppelt
       61 aaltllvelv gsvlilwgrf vwlaagalgv ftlltafias pfwamqgqar fiatndffeh
      121 lglvaafvmv amvaarrr
//
LOCUS       WP_010403590             233 aa            linear   BCT 01-JAN-2025
DEFINITION  YoaK family protein [Sphingomonas echinoides].
ACCESSION   WP_010403590
VERSION     WP_010403590.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10536473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..233
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23817
     Region          20..220
                     /region_name="DUF1275"
                     /note="Protein of unknown function (DUF1275); pfam06912"
                     /db_xref="CDD:462038"
ORIGIN      
        1 matptppqpa llppllllls vttglvdats vlglgkvfta nmtgnivflg faavgtpgft
       61 iapyviaiat fmlgafvagr tgrfhtnrpl rhwllwsali eavllwaaai laigfdpaal
      121 tpewtlfaii altavamgyr natirqlkvp dltttvltlt itglaadstl aggsnpnwar
      181 riaavvaill gaalgavlvr fglavplava galilggtia ctlhpdatrp lag
//
LOCUS       WP_010403204             576 aa            linear   BCT 01-JAN-2025
DEFINITION  M1 family metallopeptidase [Sphingomonas echinoides].
ACCESSION   WP_010403204
VERSION     WP_010403204.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..576
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63710
     Region          53..483
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(165,167..168,302..306,327,330..331,334,349,353,414)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 miasrlafac gclaltgatt lpkkgepeit aqtarsggvi dpdqaklgfd aadlsfevlp
       61 etetlrgvat lsftakapld rlaidldrnl pvdaiaidga alapaawsnp egrlvitlpq
      121 rvakgghvta rityggqphv avkapwdsgm vwattpggap wfattaegyg cdlfwpcldf
      181 ptgepgvvtl hitvpkglka psngkllgvd tlpdgrtvwn wrikhpntyg ialnvgpyee
      241 isgvyksryg nsipmfywfl pgeedkaral faefaptldf fesevgpypf gdekvgvvet
      301 phkgmehqti naygndyaka pegfdwlfqh efaheyfgnq ltaanwddyw lhegygtymq
      361 plygrwrege aryatmlsde rnkianlrpi isgkvrteee vyevdkggpg qdiyykgawm
      421 lhtlrtligd rafrdvtrla vygrtdprpg nfaprygssa eyqrfvrrvt gkdygwffdv
      481 ylreaalpdl ietrsatrla lrwqvpggrv fpmpvevqid grivtlpmag gvgslpvpkr
      541 ahvvidpkak llrrsvaieq yqawrdaqar rprpan
//
LOCUS       WP_010403664             416 aa            linear   BCT 01-JAN-2025
DEFINITION  PstA family ABC transporter permease [Wolbachia endosymbiont of
            Nasonia vitripennis].
ACCESSION   WP_010403664
VERSION     WP_010403664.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 416)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11672565
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..416
                     /product="PstA family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46143
     Region          18..151
                     /region_name="DUF3333"
                     /note="Domain of unknown function (DUF3333); pfam11812"
                     /db_xref="CDD:463357"
     Region          174..378
                     /region_name="PstA"
                     /note="ABC-type phosphate transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG0581"
                     /db_xref="CDD:440346"
ORIGIN      
        1 msikkkflkl lqsrrvhari krknkknral rfcsftalvi slgcpvcill silvnsysal
       61 tvtkillpve inadliltnn psdlryksis llnnslhkvf egidfkdsde ilsrnsykel
      121 erfflkrvkn sgeyeiwfta ssvinslykn kclndhyakl ldwlkekgrv rkffnkslfl
      181 ksdsrepena gilgafigsl mtiivclala lpigimsgic lyefmprnrl itsiveismn
      241 nlaavpsiif gvvgltlylg ifglprsspl vggmtlsfmm lpniiiatkn aftnvpiaik
      301 daafalgaph ikvildhslp ialpriihga vlaiarilge sspllmigmv afiadtptsf
      361 fdpatvlpvq iyiwssspei afielaaiai ialllmlfal nlianfvkrk feffds
//
LOCUS       WP_010403830             149 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA (cytidine(34)-2'-O)-methyltransferase [Sphingomonas
            echinoides].
ACCESSION   WP_010403830
VERSION     WP_010403830.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..149
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=15797
     Region          1..149
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 mrialyqpei agnvgailrl gaclgtpvdv ieptgftwse kalarsgmdy agvvdvhrhl
       61 dwatferqvp grivllttrg rvrldaatfq pndvllmgse gsgvpdavha radmavripl
      121 aegmrslnia vatgialaea lrqtngwpa
//
LOCUS       WP_010403942             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Sphingomonas].
ACCESSION   WP_010403942
VERSION     WP_010403942.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..397
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41774
     Region          <255..370
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mnsisiasgv rlvsrlkayf ktrdfifhdg rdlkrfslga raqatmagva gvtlcfsayg
       61 vaqaavgava mtgivgapls peakvaqmqv rvrkmqadva sikaaaqaha krveqrqall
      121 vavvsgkgdv aalsqptpti dpkadalaad vvaplkkveq qqvavaaraq rvaeqrfvra
      181 vahvrslgla perlmprqpa mggpfeaads aaaeadlrad tqfrslfmtw kkldtlehgv
      241 iaipsaqpve hlaftsnygi rsdpfrgtaa mhagvdipgp vgtpvyatad gmvdraersg
      301 gygnlveldh gkgiqtrygh lskilveagt rvhrgqlial mgstgrstgp hlhyevridg
      361 havnpvpflq tadyllaaqd rsihtipvav ggpaaad
//
LOCUS       WP_010403943             156 aa            linear   BCT 01-JAN-2025
DEFINITION  peroxiredoxin [Sphingomonas echinoides].
ACCESSION   WP_010403943
VERSION     WP_010403943.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..156
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17106
     Region          9..150
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(43,46,121)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mtiieeggal paidlatptg drlnlrdyvg kifvlyfypk ddtsgctrea qdfsshyaef
       61 qalgaavlgv srdtpakhqk fidkydltvp latddtdaam qafgvwvekk lygktymgid
      121 rstflfdaag ilvrdwrkvk vpghvvdvle avralg
//
LOCUS       WP_010403997             320 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Sphingomonas echinoides].
ACCESSION   WP_010403997
VERSION     WP_010403997.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..320
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=33941
     Region          42..285
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 msatikrgta rrpvqpkrrp ppkvstidrv iamlpvseat lrriatwtim gvvgavglat
       61 asyfgvpgav gsalgeaige agfrvtniqi tglnrmdhnv iykiaanqps mamplvslek
      121 irqdlvahsg wiedahvsrr lpdtlivhvv erepsaiwqk dgqlaliaan gtwlepvdpq
      181 ampdlplvig ahaneqeaay rqlldvapal rgqvkaatwv gnrrwtltfe tgetlalpeg
      241 dvaagkalvk faeldgvkpl lgkgwlgfdm rdptrlvark pgtvtnrait dpaaplagat
      301 gaatqpvrie akqsgpageg
//
LOCUS       WP_010404029             241 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Sphingomonas].
ACCESSION   WP_010404029
VERSION     WP_010404029.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..241
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26345
     Region          1..240
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mstiaiyslk ggvgkttlav nlswasatls srrtllwdld pqaastflls qraengklkd
       61 qaqsvfakdv epdkliekta tprldligad aslrgldllf heldkkkrlq kllvglrkdy
      121 drilldcppg ltetsdqvmr aadlivvpvi psplserala evikhlgtka qimpvhsmvd
      181 rrrklhaeal arhpdwpvvp maslieqvta rrapvgsfaa rsagaqafah lwqaierrla
      241 a
//
LOCUS       WP_010404074              68 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Sphingomonas].
ACCESSION   WP_010404074
VERSION     WP_010404074.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..68
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7306
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mtigtvkffn adkgygfiap egggedafvh itaveragmg tldkdqrvqy eleqdkrgkm
       61 savnlqqa
//
LOCUS       WP_010404041             197 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Sphingomonas echinoides].
ACCESSION   WP_010404041
VERSION     WP_010404041.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..197
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21560
     Region          34..98
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
     Region          134..194
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mlnetillpd rskcaeqakt eptssgalsr vysgvlkwfd itrgfgflva ddpsvgdili
       61 hfsvlrphgr rslpegarle ciatlrdrgl qaieilsidl seatepldrl rlsatvpqdr
      121 edgldkagpf epvtvkwfnr lkgygflvrn edsadvfvhv etlrrsglve vepgqlllar
      181 miagdkgppa vvvqqeg
//
LOCUS       WP_010404123             390 aa            linear   BCT 01-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Sphingomonas echinoides].
ACCESSION   WP_010404123
VERSION     WP_010404123.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 390)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..390
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40049
     Region          1..390
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mqdivitaak rtpvgsflga faatpahelg riaieaalaq agvagadvse vilgqvltaa
       61 qgqnparqas maagvpkeip awgvnqvcgs glravalaaq aiatgdstiv vaggqesmsm
      121 sahaqllrag qkmgdlslid tmvkdgltda fnsyhmgita enlaeqyqit raaqddfavr
      181 sqnladaars sgrfraeivp vtikgrkget ivaddeyira gvtvesvsgl rpafkkdgsv
      241 taanasglnd gaaalvlmsr aeaerrrspi lariaswasa gvdpsimgig pvpatrralq
      301 kagwniadld lieaneafaa qalsvgkele wdadrvnvng gaiaighpig asgarilttl
      361 lyemakrdvt kglatlcigg gmgialcver
//
LOCUS       WP_010404168             249 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Sphingomonas echinoides].
ACCESSION   WP_010404168
VERSION     WP_010404168.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..249
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=26382
     Region          45..206
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mrfvttllvf llafvagpaf aakkkvdpks avvttvgrpa ipsatdpenl lyldlstggr
       61 vviwlrpdaa pkmvervktl trqhfydgll fhrviegfma qtgdpkgdgt ggstlpnvpa
      121 efnwlphvrg avsaaregsa egatveevtk aensansqff ivfnptmkld kkytvfgrvi
      181 sgmdyvdaia rgeppvhpsr ilhayiaadn ppayappppp apvaapatla psqpvlkpap
      241 kaapkkkaa
//
LOCUS       WP_010404291             452 aa            linear   BCT 01-JAN-2025
DEFINITION  TldD/PmbA family protein [Sphingomonas echinoides].
ACCESSION   WP_010404291
VERSION     WP_010404291.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..452
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46366
     Region          34..450
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mltpdqgrdr aaaivsrara agadaadavy aadtsldisv rlgaledvgr sesaelglrv
       61 fvgkrsasvs tsdlsddalt alvdraiama reapedawag lapaerlmhg dpplldlddl
      121 akggsepspe alrdaaraae daaravagvt nseggsasas rsiwalatsh gfaaayaatg
      181 yglsasvlag eggamvrdya yssarhrral eapeligtra geravarvnp grlasgpmtv
      241 vfdprvgssl lghligaisg qaitrktsfl lealgtqvfa sgvtvlddph rphglrsrpf
      301 dgeglpvspt aiieagmler wlldsasarq lgleptghaa rgvsgapgvs tsnlhmaagh
      361 vppetliadi tdgvfvteli gmgvngvtgd ysrgaagfri ergeitgpva eftiagnlkd
      421 mflnltpand lefrygtnvp tlriegmtva sg
//
LOCUS       WP_010404281             789 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Sphingomonas echinoides].
ACCESSION   WP_010404281
VERSION     WP_010404281.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..789
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83266
     Region          39..767
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mrrsfslafa gvllgcssta alaqsataae tpeaqggdii vtaqkreqkl qdvpitvsal
       61 tgaqmqtlgv nslaevamyv pglriqeqsd nnpgfvirgi tsdsgsaqqg arvslyyngv
      121 disrtrgayq dlfdleriev vkgpqatlfg tasavgavni isarpkagts agiiasygny
      181 nrgqvsgfvn vgndtlaarl afaykyhdgf vrniagdpnv pnqnqgktkq ddlngqdqrg
      241 lrgslrwapt daltatlvlt ydgqrnpgta frsraqaptg gnggdysyae lsgspysaqv
      301 lggsklglkr dvydanftlt aelapgvsft tvngyrkfns nevfdadggp awylefaeda
      361 rgdqyshegr fnftgttyra sfgwnaffen nlqrvpfste egtyltcaga lpaatraall
      421 aagipsgpgc vlpngtvaaa gatalltrga ataipyssvf tnygtndtys vfadgtwlpt
      481 prleltagar iliekrksgy ssvqpnsvla gvpllptvst ggvkftaqrs fsailprfna
      541 lyrltdginl yatiskgrrs pvvqlsaats ggvavpslqv vpdevvwnye ggikakigaf
      601 sgslgvfyqd yngfqvtvtd gagktttqsa gkaqnpgvel egnwrvnsll qlfgnfayvd
      661 gkiannpayg vysgaqfrlq pkysasggat lrvparnmtf yatpsatyqs keyfelpnse
      721 pisqgayalv nvragvelag gryqiggfar naldrkylid agntgggfgi ptyirgeprv
      781 ygvevsgkf
//
LOCUS       WP_010404301             194 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Sphingomonas echinoides].
ACCESSION   WP_010404301
VERSION     WP_010404301.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..194
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21016
     Region          8..164
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mihtsptlvi agsvrprris phiaqwvatl graqsddaye vvdlrdwplp mddeaempqr
       61 asyasaltle wsrkiasaaa fvfvtpqynw gypaalknai dhlyrewadk pvmivsyggh
      121 gggkaaaqlq evcegiglrp iatrpalrls rtqieansge idpaeafagh ieevraalae
      181 lsqsrdatiq ptta
//
LOCUS       WP_010404318              83 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Wolbachia endosymbiont of Nasonia vitripennis].
ACCESSION   WP_010404318
VERSION     WP_010404318.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..83
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9210
     Region          1..81
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mefgnikwfn vekgygfikp egkgedvflh vstlersgir pdalrgedkk ggxkgervsy
       61 elkeergrng enkksainlr led
//
LOCUS       WP_010404425             345 aa            linear   BCT 01-JAN-2025
DEFINITION  COX15/CtaA family protein [Sphingomonas echinoides].
ACCESSION   WP_010404425
VERSION     WP_010404425.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..345
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=37171
     Region          18..325
                     /region_name="COX15-CtaA"
                     /note="Cytochrome oxidase assembly protein; pfam02628"
                     /db_xref="CDD:460629"
ORIGIN      
        1 mlqasslpqq vrprtlsnwl fgvaalvvam vviggitrlt esglsitqwk pisgiippln
       61 aaqwqaefdn ykkipeyqql hrgmsmagfq aiffweylhr llgrvvgaay llpllwfwar
      121 grvprgyvpr lfalvalvaf qgaigwwmvs sglvkrtdvs hvrlavhlvt altllagtvw
      181 taldlralaq dsrarparlr pvavialgll fgqilfgaft agldagyafs swplmgdeif
      241 paatpltdpl wrnavdnpvv vqfihrwfaf vaaaglvmla lramragapr tatvviglva
      301 cqialgiatl lsgveivvav ahqanaaltl iaataaahav grrfa
//
LOCUS       WP_010404480             200 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Sphingomonas echinoides].
ACCESSION   WP_010404480
VERSION     WP_010404480.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..200
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22717
     Region          3..189
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtikaimvdv dgvlivhpdq rgwtvnlerd lgipstqlqs affeqhwddv vhgraplrer
       61 ltpvlqehwp eircdalidy wftndahlnh allaelvsir negtevhlat vqeheraryi
      121 wdalglrtrf dglhyaaelg cskpaaafyk sieartgfrp ndlfliddkl anvqgaierg
      181 wrsalwtgdv tlrsliaqqe
//
LOCUS       WP_010404603             566 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Sphingomonas echinoides].
ACCESSION   WP_010404603
VERSION     WP_010404603.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..566
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=63563
     Region          8..420
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mtdpiplrac ayvrvstkrq aehetslneq etgiarsaae rgyeivetyi eagksgmtdr
       61 rpalqrmiad acarpqryda vfvynfsrff rdeyecegyr rklekagvkl isatqdvgeg
      121 pharlirsif tsldaassei naeqvkvvms anaeagfhng sapplgyrty vaerrgkkdk
      181 kkleidpael plvelifrly legdgtsepl gigsmvkwlr ergythrsqh fhtgliyail
      241 tretyagrhy ygcrdsrtgk vrprdqwiev rvpailsees fqavqqrlka rnphitaprs
      301 htspvllsgl grcgcngcts tmmlmtgkgg ryryyacsnr rkkgdlscgg nnvpmdqvdd
      361 avvsalehrl fqpgrlkall gemldasdva dadrrkrlav lrteetevna siralfmmve
      421 sgattpddpf lkerlatlkl rlssigeema alerqigarg gritpekver faaamrtklr
      481 dtddmqvrrr yvrafvgevv msrkriiirg pnralelaaa gdmpaddkvr tfmgnwrtrl
      541 dsnqwplpse gkagnerrqp qanekh
//
LOCUS       WP_010404666             168 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheW [Sphingomonas].
ACCESSION   WP_010404666
VERSION     WP_010404666.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..168
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=18252
     Region          12..137
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mssldhrtan kqadrkivtf slghqtfgid mhslieirew eeptplptvp sfikgvtnlr
       61 gnvvpvigla erlgwepski harscvlvvs igekqagflv devsdivsig dqeiqpapdv
      121 eigepsvilg lvrvesrtme argddtgqmi llldldglsl trhlelva
//
LOCUS       WP_010404677             213 aa            linear   BCT 01-JAN-2025
DEFINITION  PilZ domain-containing protein [Sphingomonas echinoides].
ACCESSION   WP_010404677
VERSION     WP_010404677.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..213
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22604
     Region          19..98
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
     Region          122..208
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mapierhfpa dppinpterf qpraqrtvtt liaaklelgp gkealcrlrn vsttgmlvet
       61 gqpltpddav vielrsgerl satvvwtdeg rvgiqldrei dvastlrpqv vkakghvpav
      121 graprfavaa pgrlsslgrs cpvtvenlsq sgarltlssd iplgapvtlt iaglspracs
      181 vrwrndlhvg vafidlisya elsawlagas hnn
//
LOCUS       WP_010404921             214 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Sphingomonas echinoides].
ACCESSION   WP_010404921
VERSION     WP_010404921.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..214
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23703
     Region          32..202
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mfdevsardd adtpvdgdsa srqpdvdplg llllrvrhgd qrafkrvydm taprllskal
       61 silstrdtae dvlqetyvri wrniaqfdpa rgsaatwilr ilrnaaidrl rhdrtiaryq
      121 tttdalpdlp iapepvtdri dldralaris peqrasicrv vvhgwthdev gkldgvptpt
      181 akarvqrglr rlhaaltdlp pdarvanaae kala
//
LOCUS       WP_010405024             276 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Sphingomonas echinoides].
ACCESSION   WP_010405024
VERSION     WP_010405024.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..276
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=28876
     Region          9..274
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 msrilrfvag lvliglalli gsyaasradp ivrrltvalp dwpqgaapvt lalltdihlg
       61 nasmdrarld rivdqvnalk pdlvllggdf laeydkakap vrsrlvaesl arlqaplgtv
      121 avlgnhdynt dpqavtrafa rvgipvlqnt alqrgpivig glgdfdtgha dvaamsvama
      181 klrgadvvlt htpdiptplp gtiglllagh lhcgqivlpl lgpisvsptq rrylcgvvhd
      241 gnrtvvvsag lgtstlplrv happdlwlvt vgpakr
//
LOCUS       WP_010405036             234 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ComF family protein [Wolbachia].
ACCESSION   WP_010405036
VERSION     WP_010405036.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia
  ORGANISM  Wolbachia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Wolbachia"
                     /db_xref="taxon:953"
     Protein         1..234
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=26598
     Region          5..234
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
     Region          26..>76
                     /region_name="FYVE_like_SF"
                     /note="FYVE domain like superfamily; cl28890"
                     /db_xref="CDD:333710"
ORIGIN      
        1 mnllllkkat dlifpnvcvs ceriidksyd lcsecnkkin fltkhycnvc gvvipdnidt
       61 cgkcisnpsp fkvlrsvfay dehsknmiin fkffdnlnyv kvyakwmyka nkdmfqnaev
      121 ivpiplhkir lfkrkynqaa llakelskls nlsytpfaik rirhtkpqag lslkqreknl
      181 kntfkvsnse iiknkivilv ddvvttgata rscsqeilns garevrvlsl artv
//
LOCUS       WP_010405060             317 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Sphingomonas echinoides].
ACCESSION   WP_010405060
VERSION     WP_010405060.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..317
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32390
     Region          36..281
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mirsgllava alaaspalaa ppapveltap gpegplagtl ldpdgkaplv llipgsgptd
       61 rdgnnplgva ggpyrqlaea laakgiatlr idkrglfgsk aaqadpnavt taayaadvqa
      121 wskvarartg raciwllghs egglvalqaa qtpagicgli lvssigrpmg avlreqlran
      181 panapllpaa eaaiasleag kridtaqlpa plqtlfpdrl qgywidllsh dparliaavk
      241 lpvlilqgtr dlqvsvadae alhraqpkar ltllpginhv lrpvgsddra anlatyrdat
      301 qpispsiaea vatfvgr
//
LOCUS       WP_010405152             363 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Sphingomonas echinoides].
ACCESSION   WP_010405152
VERSION     WP_010405152.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..363
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39272
     Region          4..360
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mlgeqvrygl vgtgmmgveh itnlaitpga vvtaladpva esigwatsal gdragaatvf
       61 dsvealaasg lcdavivasp nythrrvlep lfdaglhilc ekpvattldd crwiveraaq
      121 tdrvfwtame yrymppaaaf ieeirsgaig rlqmlsireh rfpflvkvad wnrfnrntgg
      181 tmvekcchff dlmrlitgse avrvycsgam dvnhrderyg getpdiidns yttvdfangv
      241 ralldlsmfa dgaenqeeit avgdkarldv lipegalvha prvgfrnakq vtrrvvevdq
      301 aalaagshhg stfyehqrfn aavrgagpve vtatdgmmav aigtaaeisa rehrvvemae
      361 lgf
//
LOCUS       WP_010405150             793 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Sphingomonas echinoides].
ACCESSION   WP_010405150
VERSION     WP_010405150.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..793
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83626
     Region          38..775
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkalyltgaa alalvsaaps faqtapapaa sedapgdiiv taqkrserlq dvplavtvvs
       61 gdaiaaqgkt slegaqylvp slnflksgtt lnqslflrgv gtstfsiage psistvvdgv
      121 vysrageafg dlvdvdqiev lrgpqgtlfg knasagvini iskkptstfg gyvedgffsd
      181 seyraraain vplgehvrsr ltgfytnydg nirnvttgkl vngfehyggr lqvdadagpn
      241 vklafiadyh rnnddccgev iatgpintat gavttnasta alptprgtdt relaqnlttr
      301 tketgygfsl qadiqagtqt vtsitayrny knteirdgdf lpaayigfnq lhdfgpqtgd
      361 tfsqeirlts pghqfltyvl gayysraase rvftrndqvc taavtpapta ltpcssasan
      421 pstfptgtad fgsvfknval fgqgtlnisd rfrligglry tvdqldvfhs rattlagpgi
      481 nanfdqgvyn eyvrliglgv sattaasqav sasngvpfra katnenlsgk agvqfdishg
      541 stayatyarg ykgpafnvfy nltatgtnvi apetsdsyei glkntllggk ltlnlaafya
      601 kyknfqannp dlvagvvvtr ftnagdvstr gveldatlrp vrdlsitgga aytdahvdkf
      661 napagsatip agtplgfapk wkgnvsvdyr vrtggfadvl lgaqgsyqss elglfsadav
      721 qrqlgtigay slvnlsaglv skddrykltf qvrnlfdksf aasiinggpg qayryqiprd
      781 adryfgvtgr vtf
//
LOCUS       WP_010405165             522 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Sphingomonas echinoides].
ACCESSION   WP_010405165
VERSION     WP_010405165.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..522
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=55721
     Region          32..512
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 msgaeltrra llgsgaaala aaatplraal appvacsagr ffgtaeangi rayrgirygr
       61 aerfrapapf vygpaphpad tfgpvapqag gtyglqsedc lflniwtarp draaklpvml
      121 yihggaysgg svtdplndga alaargdvvv vtvnhrlnaf gylylarlnp rfpdsgnagq
      181 ldlilalqwv rdniaafggd pgrvmvfgqs gggakiatml gmpaakglfh raatmsgqqv
      241 tasgplnata raraylarlg vdagdlspll tmpqdrlvaa ldaidpilgg gvyfgpvldm
      301 kwltrhpfwp danpqglgip milgnvrdet rgflspdsdk vrgltwdnva ariapelrid
      361 ilpewvvaqy rahfpdwspt evfygattag rswrgqviea esraqagapa fvyqvdftsr
      421 ldprrgafht idiplvfgti gakgshtgtg adaqaasqam qnsfvafaqt gdpnhtglpq
      481 wprydlprra tmvfdtvahr eddprrwqre lfarvpyiqp gt
//
LOCUS       WP_010405176             403 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA recombination protein RmuC, partial [Wolbachia endosymbiont of
            Nasonia vitripennis].
ACCESSION   WP_010405176
VERSION     WP_010405176.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         <1..403
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          93..375
                     /region_name="RmuC"
                     /note="RmuC family; pfam02646"
                     /db_xref="CDD:460637"
ORIGIN      
        1 lqeakqslvd knkeivdlkv rnaelxvilq kereekkkei elltkaeerl tntfkalsld
       61 alqvnnnnfl nlakevidnk lketesdfkk rqatinevit pikeklekfd seireleker
      121 vgayeglreq igalmsqtsn lanalrkphi rgkwgemqlk rvvemagmve ycdfftqasv
      181 vdknednllr pdliikmpsg kqiiidakvp ldsymdamsq ndlqiqrekl knhslaikkh
      241 indlgrkeyw nqfentpefv vlfltgegvf saalecepal ieigiekkvi iatpitlial
      301 lravaygwkq emiaenakki selghilyer ictmgenfdn lrrslksavd hynktagsle
      361 arvfpaaref nklgihaknk eltaakeles lprslhaerl kvd
//
LOCUS       WP_010405254             187 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein, partial [Wolbachia
            endosymbiont of Nasonia vitripennis].
ACCESSION   WP_010405254
VERSION     WP_010405254.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..>187
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          1..187
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          5..31
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(33,35,39..40,43..45,47..48,52,55,64,66,68,72..73,
                     76..78,80..81,85,88,97,99,101,105..106,110..112,114..115,
                     119,122,131)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          33..64
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          66..97
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          99..131
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          133..164
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 minelfaavr sgdanqvadl inkgddvnar dnrgntplhl avladklqvv ekliergadi
       61 naknnhgatp lhwaalnqnv sivekliekg anvneknkyd nvplhyaaff ngclgtaekl
      121 iekganvnak nndgatplhw aalhdnlqva glfinkranv nakdengwtp lhtaaargnl
      181 gvvklil
//
LOCUS       WP_010405291             307 aa            linear   BCT 01-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Wolbachia endosymbiont of
            Nasonia vitripennis].
ACCESSION   WP_010405291
VERSION     WP_010405291.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..307
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=34309
     Region          15..>64
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(16,28..29,31..32,34..35,38..39,41,48..49,50..54,56)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          90..302
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 msegiktilv ednnvrldry irrifpnlkq saiekslrkg likvdnctak ssdrvnsgqt
       61 itiryldyie ntnsdrkyne klvnllrdni lyedeyilai nksagiivqg gikvkisisx
      121 xldqirxgev fkivhrldrd tsgviifarn asvarylmee fkgrrikkty laltsgipsk
      181 dngiidyplv kkyisgqekv videdspqna tthfsiisrl khnvaylklq pitgrthqlr
      241 ahlahincpi lgdgkyggkk afidgvvnqi hlhshslslk lpnnkeitit apiprhieks
      301 ievlsfn
//
LOCUS       WP_010405332             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Wolbachia].
ACCESSION   WP_010405332
VERSION     WP_010405332.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia
  ORGANISM  Wolbachia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Wolbachia"
                     /db_xref="taxon:953"
     Protein         1..233
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25849
     Region          4..230
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 myspiisiln lslsfddrti lnnisfnisk geslvilggs gsgksvltki iigllkpdsg
       61 sikinseskn kfgvlfqnsa lfdyvtvwen isfnykkrfn isekeakqla ieklndvgle
      121 esiadmfpie lsggmkkrva laraiahnpe iivldeptsg ldpimsdmvn eiiiklskdf
      181 nptiitithd ihsafkiadk iavlyegnii yhgtvqeiqn tnneyikkfi hyi
//
LOCUS       WP_010405351             193 aa            linear   BCT 01-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Sphingomonas
            echinoides].
ACCESSION   WP_010405351
VERSION     WP_010405351.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..193
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=19753
     Region          37..187
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mlehlpewlg aslsgvraga ehltivhpal gigfvpivls spafadwtem plrftadgag
       61 vspplawddv ppatqslali vedadsptpa plvhailwgl pagmrtlaeg aivadaatge
      121 tgknsylsqs wlapdppkgh gehryvfqlf aldcpaadlg dapgrgavln amaghvigag
      181 mltglyarge vvg
//
LOCUS       WP_010405092             510 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease/substrate-binding protein [Sphingomonas
            echinoides].
ACCESSION   WP_010405092
VERSION     WP_010405092.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 510)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..510
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53543
     Region          29..220
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          246..505
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
ORIGIN      
        1 mspfldamtr vppllaahll laaaalalgl tislplaiws arrpgvarva lgfaslvqti
       61 pslallalfy plllfvsgla gggipalgfl psllaltlya llpilrngvt gmagidpavi
      121 eaadgmgmta wqklrlveap lvapvlmagv rtaavwtiga atlsttvgqp slgdlifagl
      181 qtqnwalvla gcvsaaglal avdallglie rgiatrrrgr vygagavlll avlaalapla
      241 vpraptivig sknfseqyil arvighrler agyrveyreg lgsaviygal ssgaidvyvd
      301 yagtlwtnam rrrdtparpa mvaaignwsa rtsgvrllga lgfenayafa mrgdaarakg
      361 ivslddlvra apgltlgsdl eflerpewaa vqraypirfa athaysptfm yralesgqad
      421 visafssdgr iaaehltvlt dprraipgyd ailllapkra kdarlaaalt plvgripvaa
      481 mreanylvdr drnkvspega arwlerrlgl
//
LOCUS       WP_010405399              95 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein, partial [Wolbachia
            endosymbiont of Nasonia vitripennis].
ACCESSION   WP_010405399
VERSION     WP_010405399.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12120816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..>95
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <37..95
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          41..69
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mdklgqdtkn klhfwwlitv ivciiatysy mkakaadnyk tilriasqnc nletvkflve
       61 nlldinvqip kltalhyaae egcaevvkfl vekgv
//
LOCUS       WP_010405469             530 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Sphingomonas echinoides].
ACCESSION   WP_010405469
VERSION     WP_010405469.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..530
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=58640
     Region          1..409
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mrtviyarfs sdnqnprsae dqialcrera dregwsviav fqdvatsgaa gigddqrpgl
       61 ssmlrlveag gidqvlaest drvsrhvada hmirerlefa garlftlfdg avtpiiglik
      121 gftdaqfrtd laarsrrghi aniqrgrass gvaygyrian rldergqlva glreidaera
      181 evvrrifrdy aagispraia talnaegvrp prggaiwqts tilghnktgf gilrnrvylg
      241 klvygrsksa mnpvtrrklm rpnpdqtaiv eqdvphlqii detlwqrvhd rieankgvpv
      301 drqrrpkhll sglgecgvcg gpwikvstln wgcsrhrlgn actnnrsiat rqyerrvlad
      361 lkanmlapdv vaayvreyhr dfarqsadli rdrtrierql geaerkvkrm ldafadggse
      421 fseirgmlat akadkerltr elasidaipt vltfhprlee eyrrqvesle aalaepqaal
      481 eavpqargmi akiivspaek rgvqiqvvrq vdqvlaiamq gredgaslag
//
LOCUS       WP_010405472             589 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Sphingomonas echinoides].
ACCESSION   WP_010405472
VERSION     WP_010405472.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18540890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..589
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=63060
     Region          1..>190
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
     Region          <7..567
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
ORIGIN      
        1 melkhidiah lsvssanmrv kgnpvdlasi lpsvrargvl vplivrakps tepgedgspd
       61 tyeivagkrr yhaalvvaqe sgeaeplpca vmaagddada leaslienia rvdpdevtrw
      121 esftrlvreg rtpeeialtf gltevqvkrt lalgnllpri rglyrkgeid aatirhltlv
      181 skarqqewla lfddpaaycp tghhvkawaf ggasipvraa lfdldrytgd ivsdlfgedr
      241 yfadpqafwa sqeaaiaerv eayvqsgwsd vvvlptgepf hawehertpk rkggkvfvav
      301 gprgdvafhe gylttkeark larsetpmaq pvrpeigaai qnyidlhrha avrsavaanp
      361 svalrlmvah aiagsslwrv svepqrsand aiaesvenca setafdarrr avlallgfdp
      421 dmptvtggcd gdhglaglfa rlleltdsav rdvlaivmae tleagsalie llgvhlgvem
      481 rgvweaddal ldlirdreva gcilsdvaga gvatanagat gkvkrqiird cltgangrak
      541 aegwvprwma fppaaytlrg gvqttsrsta lgglveavtp hitplahaa
//
LOCUS       WP_010405489             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: crossover junction endodeoxyribonuclease RuvC
            [Wolbachia].
ACCESSION   WP_010405489
VERSION     WP_010405489.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia
  ORGANISM  Wolbachia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002778
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Wolbachia"
                     /db_xref="taxon:953"
     Protein         1..155
                     /product="crossover junction endodeoxyribonuclease RuvC"
                     /EC_number="3.1.21.10"
                     /GO_component="GO:0048476 - Holliday junction resolvase
                     complex [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008821 - crossover junction DNA
                     endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=17149
     Region          3..141
                     /region_name="RuvC"
                     /note="Holliday junction resolvasome RuvABC endonuclease
                     subunit RuvC [Replication, recombination and repair];
                     COG0817"
                     /db_xref="CDD:440579"
ORIGIN      
        1 msiltldlgk qtgwailtdg viesgsksfh gsrfsgggmh flkfrswlne mkekfsniea
       61 vyfeevrrhl gtdaahcygg flavlsawce ehhvpyqgvn vktikrfitg kgnasksevi
      121 eavkkkgvsp rddnegdala lmfylskdfn slkmp
//
LOCUS       WP_010405811             699 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParB/RepB/Spo0J family partition protein
            [Sphingomonas].
ACCESSION   WP_010405811
VERSION     WP_010405811.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..699
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=76973
     Region          2..>186
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 miqtmklnkl rlspinvrrl peeklqipqm aadieargvl qnllvtpakk prgtfevfdg
       61 grrlralqrl adagtikadd ydvpvmvlqa deatlsetst atnfqqlkmt paeecrafqh
      121 figtsgdida vakrfgvtrr fvegrlrlaa laepifeals sgeitldvak ayastenqek
      181 qllvwnnyqn syvnadtirr vianetlkan dpiailvget ryidaggkid gdlftdgndr
      241 wvdpeiahrl ageimeaeak rvgeetglaw irpiasnyah naahglyrai lrqpdlteeq
      301 alrltaider rseletemqd eslleedfkl ldqeddrliq eaeaienrap vlpdelkahv
      361 gafllltpqg amvldtqyys eqqilseepa ddegsegedg erssggfrig gpkpsepshr
      421 peavapggkp lssrlydela mqrrdilasc llaqpalald yglfvmvdar tktssrytyn
      481 stkygttira sgpqdpntgd mptsrardyl aeahesldag wtehenever fegfralddd
      541 skanwlayiv aisleakpgi sneqiplhnr lasileidva swwrptsenf fdrvnkgsil
      601 slldevggpa lsgrhaslkk teisascekl fagdtiveae vkeaalawvp namrfldrqp
      661 edvvieadea ehdeddsggv adaaadssqa gdevlepaa
//
LOCUS       WP_010405814             230 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Sphingomonas sp. Ant H11].
ACCESSION   WP_010405814
VERSION     WP_010405814.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. Ant H11
  ORGANISM  Sphingomonas sp. Ant H11
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Sphingomonas sp. Ant H11"
                     /db_xref="taxon:1564113"
     Protein         1..230
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24480
     Region          1..226
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 msvdlftadd gtpapaiify mdagsirpat lamaarlsea gfvvllpdlf yrygpygpld
       61 pkevfkgdvk ailgplmatt gnarsaedtd allafldsrt evagvkvgav gfcmgggmai
      121 aaagtrpdrf aavasfhggn lateapdsph syatrldael yiavaendgs yppamaeqfe
      181 halneagvsy rsetypaahg wmkpdfpvyd etaaehgwre mlaffrrtlr
//
LOCUS       WP_010405845             155 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Sphingomonas echinoides].
ACCESSION   WP_010405845
VERSION     WP_010405845.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..155
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16579
     Region          9..138
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 msdsgssdgg crcgeirfkv fgdplitmac hcrgcqrmta saysvsafyp adrfevlage
       61 pvagalrgpq rhlycpscls wvftrpegmd dfvnvrstll dsppsdapfi etvtaealpw
      121 arigaahafe gfppreqfpa ligefiaara natsv
//
LOCUS       WP_010405876             178 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YdcF family protein [Sphingomonas].
ACCESSION   WP_010405876
VERSION     WP_010405876.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..178
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18994
     Region          5..>134
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 miarvlgvla llwmlgfavf latmpvplag prtdaivvlt gsagridrgl allqghmakr
       61 mlisgvapev rpaelaheyr vspalfaccv dlgheavdtr snadetadwv rthgyktvrl
      121 vtsdwhlara rlelvnaldg datvfgdgvp sspryavlig eynklilrka alligavt
//
LOCUS       WP_010405888             229 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Sphingomonas
            echinoides].
ACCESSION   WP_010405888
VERSION     WP_010405888.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..229
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24456
     Region          40..193
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maakrgavat adpaqsgapa aggyavrldd sasagkaprt ergrktlrai ldaaaiefge
       61 rgfheasvsg itrragvalg sfytyfdskd avfralvrdm sdqvrervap airaapdqia
      121 aeragllefi afvrghkeiy riideaefvd pesfhlhyat taeriavrlk agaargeirs
      181 dvsevhawav mgmnvflglr ygvwtddlap eavadviadm lvnglaarp
//
LOCUS       WP_010405912             323 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent glycerol-3-phosphate dehydrogenase [Sphingomonas
            echinoides].
ACCESSION   WP_010405912
VERSION     WP_010405912.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..323
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=32188
     Region          1..321
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
ORIGIN      
        1 mkigviggga wgtalaqvaa rsgdpvllwa repevvasin qthensrfla gialprsira
       61 tgaladlagc dallvvapaq hvravlaetp vattplvlca kgieagtqll vgevaqqlyp
      121 dapiavlsgp tfahevaagq ptavtlacad aalgaaladr laspsfrpya stdvigaeig
      181 gavknvlaia cgvvegaglg qnaraaliar gfaemtrfgl argaraetls glsglgdlvl
      241 tcsstssrnf slgvglgqgk raadlladrl tvaegaftap vlqaaaaeag vdmpvvdavc
      301 alldgrdvaa vvgallarpl rre
//
LOCUS       WP_010405925             767 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA translocase FtsK [Sphingomonas].
ACCESSION   WP_010405925
VERSION     WP_010405925.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12144184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..767
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=82474
     Region          25..181
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          118..763
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 masraqpplw retvragavr sgaliaaitl valvalivva lasyhasdps lntasagpar
       61 nwlgrggavv adaafwllgp gialvlptvl lialrlwrdv pvgrwqrmll salggigllg
      121 tafalvsgaa vawlpagwgg viglavsdll raaialigns aavlwttrga aaiiglagva
      181 lwaysftidm aerpvrapra pkrltdrrat aeieperfvp esprklpmpr avatpdvrpg
      241 pviserqmtp vttakprekq tsldfgdksh lpsvdllkpt ppsvggpidk valdrnarll
      301 etvlsdfhvk gsiinvrpgp vvtmyelepa agikasrviq laddiarnms avsarvatip
      361 grtvigielp narretvglr elidslddqp galslvlgkn iagdpviadl apmphllvag
      421 ttgsgksvgl ncmilsllyr lkpeecrmim idpkmlelsm yediphlyap vvtdpakavr
      481 alkwtveqme dryrqmsslg vrslasfndk vraakakgqp lgrkvqtgye pvtgapiyee
      541 etldyqvlpq ivvivdelad lmmtagkeve fliqrlaqka raagihlima tqrpsvdvit
      601 gvikanlptr isfhvtskid srtilgeqga eqllgkgdml ympggkgivr vhgpfvsdde
      661 vravadhwra qgrpdynnav teepedgfal dgapigedsa edqqyraaiq lvvesqkast
      721 swlqrqlrvg ynsaarlier mekdnivgrp dhvgrrevlr drdgnpv
//
LOCUS       WP_010405930             413 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation:proton antiporter [Pseudomonas].
ACCESSION   WP_010405930
VERSION     WP_010405930.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..413
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43696
     Region          1..403
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mthwmlslfv vlitalivgs iaervgqsrv igeiasglll gasvlggvsp elfnylfvgs
       61 pgqhlkelae lgviilmfev awhapaslen iakkhapivi avagivfsfs igcvlayvak
      121 pvmapekpff sfilfcglal sitalpvlvr iirentfink ssgsialasa vcsdmvawag
      181 vavisamyas gytstkqiti ngilfltfiv tslyvvspii rkfkwldgdr fpafaqitia
      241 fsycllcsei sdslgfnrvt gaivagytls rvpglegnwk kivggfssla ltpvffaysg
      301 iqaslslsgs lvvwlllffv gsligklggc ylgarivglp kstsvevgvl mntkglvelv
      361 vlnigleigv vnqatysvll ilalvstgmt ipvlnwwykr agksqsapae avt
//
LOCUS       WP_010405944             263 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Sphingomonas].
ACCESSION   WP_010405944
VERSION     WP_010405944.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..263
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28205
     Region          1..252
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mnviavanqk ggvgktttai nlgtalaatg lrvllldldp qgnastglgi aradrhhsty
       61 dillgettie aaalptivpk ldivpatvdl sgaeielvey eerthrlsra larsdhrwdv
      121 vlidcppslg lltlnamvas nsllvplqce ffaleglsql lstverirer fnpglsimgv
      181 altmhdrrnr ltdqvsndvr avlggvvfdt viprnvrlse apshglpali ydyrcpgsea
      241 yialarelia rlpniepqpa raa
//
LOCUS       WP_010405970             197 aa            linear   BCT 01-JAN-2025
DEFINITION  SCO family protein [Sphingomonas echinoides].
ACCESSION   WP_010405970
VERSION     WP_010405970.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11133300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..197
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21054
ORIGIN      
        1 mnqiaralsa lflavlpvac sgpatparap ldgvalggpf tltdqdgrvr tdrdfagryr
       61 imyfgytfcp dvcptdmqti gaglrvfegk dakrgakvvp ifvtvdpkrd tpavlkafvs
      121 afhprmvglt gspqaiaava keygayfeae kpnaeggylv aharlaylmd pagkpvallp
      181 qdktpqdvat eldrwvr
//
LOCUS       WP_010405978             357 aa            linear   BCT 01-JAN-2025
DEFINITION  type III polyketide synthase [Sphingomonas echinoides].
ACCESSION   WP_010405978
VERSION     WP_010405978.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..357
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36812
     Region          4..354
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 msstahiaai gtavpaqdih aafiewarar lpdgravrif drmagraaia hrwsvlplga
       61 qggspvdpdg fyaksvlpgt aermrlyaqa apelsiaaie alraqvaleg ithlvvasct
      121 gfiapgidqi iaariglaps verllvgfmg cyaavaalrs arhivrsdad arvlvvcvel
      181 stlhlqdnpa lepllamlqf gdgaaaalvt aepagfaldh pfattlpdsa alirwditdq
      241 gfamhlsgev pariaaglsd pvfaaaatgg rprleidgwa vhaggrsild avehslglpa
      301 daldasravl seygnmssat lmfvlarmld gppvtngval afgpglaaeg fgfrsva
//
LOCUS       WP_010405994             360 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Sphingomonas echinoides].
ACCESSION   WP_010405994
VERSION     WP_010405994.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869916
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..360
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37365
     Region          55..254
                     /region_name="arylsulfatase_AtsA-like_MBL-fold"
                     /note="Pseudoalteromonas carrageenovora arylsulfatase AtsA
                     and related proteins; MBL-fold metallo-hydrolase domain;
                     cd07719"
                     /db_xref="CDD:293805"
     Site            order(113,115,117..118,212..213,235,254)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293805"
ORIGIN      
        1 mrtygkwvsa ialiglaggi lvgvfqaqia tallvwivda rvgrdttatl pdglhvalcg
       61 tgsplpdptr agpcsvviag krlfvvdige ggartivamg lpigriegvf lthfhsdhid
      121 glgplmlqsw iassatsplp vhgptgveav vagfdaayat dwgyrtahhg ggvappggag
      181 avavpfvvpq gnarqvvyrq dgltitafcv dhgpvrpavg yrfdykgrsv vfsgdtgpsa
      241 slvaaakgad llvhealqph lvgllttale rnhrynlaqv trdirnyhtt peqaadaaka
      301 agvkrlvlnh ivpplplrfa ypaflgdsah hftgpitvge dgmlfslpag tatisqskle
//
LOCUS       WP_010406016             338 aa            linear   BCT 01-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Sphingomonas echinoides].
ACCESSION   WP_010406016
VERSION     WP_010406016.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..338
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34117
     Region          71..248
                     /region_name="Ferritin_2"
                     /note="Ferritin-like domain; pfam13668"
                     /db_xref="CDD:433392"
ORIGIN      
        1 mndsdilvpa pdpkerrrag rrhflrsasv atlafggsal lsacggsgts tpsatdsstp
       61 tpspsstdtl ndqdsfnfll nlaylqaqfy tvavtgaglp taliakgdgn qtvqgavtgg
      121 rqvtftdplv aqyareiaad kvahvaflrs algaatvaqp ainidgsasg afsalaqaat
      181 vvaagaafdp yasdenflla afmledvvvt aytgrqstia ttllidaaag ihattsyhag
      241 lirtvlyakg svstpslltn aglisnarda fdgstdldqg ivgdsvtsni spldsnglal
      301 artagqvlnv lylnknavvg ggffpggvng niktsaan
//
LOCUS       WP_010406017             337 aa            linear   BCT 01-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Sphingomonas echinoides].
ACCESSION   WP_010406017
VERSION     WP_010406017.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..337
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34394
     Region          59..213
                     /region_name="Ferritin_2"
                     /note="Ferritin-like domain; pfam13668"
                     /db_xref="CDD:433392"
ORIGIN      
        1 mtdlpqdsga qlherleaga eqrserreff rtalgagaia avgaaavtlg sramadstsd
       61 tnllnvllnf eyleaqfyaf avtgaglpsa qltpgsastt tvgavtggkq vsftdplvak
      121 yareianeka aqvaflrttl gtavvaqpai dlgstatsaf slamraaniv asgvafdpfa
      181 sdenfllsaf fledvvvtay kaaaqlistp ayrdagagll aahahhaali rtvlytkgat
      241 tatlrtqada isavrdtldg ttkddvgisp aviansqlaa lngltasniv pagtdgiayg
      301 rlvanvlnif ylnslavtkg gfypnglnat vvtsaan
//
LOCUS       WP_010406039             528 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Sphingomonas echinoides].
ACCESSION   WP_010406039
VERSION     WP_010406039.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..528
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56932
     Region          21..528
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 meeadivvvg ggsggaaaag rlseggkfsv alleaggrnt glrtripafl afqtdktnwn
       61 yetvpqagln grrghqprgk glggssaina miyirgnrwd ydnwaamgcp gwsydevlpw
      121 fkrsehnvrr gdayhggdgp lwvsdqkfan pgsldfieag aslqiprnmd fngerqegig
      181 lyqvtqknge rwtsaraylg drpanpdlhi ltgvtaervl fdegrvwgva ylqdgqskvi
      241 rarrgvilag gvfgtaqllm lsgigpgahl rekgvavrvd rpavgsnlqd hidyvaafet
      301 pgtdfvgssl kgtlamgsaf fqwlrkrqgm mttpfaeaga fltvtpdapa pdvqlhfvia
      361 aledhgrtkv pghgfschvc vlrpeshgtv rlasvdaraa plidpaffsd srdmevmkrg
      421 vramyrilet aplsnhkgrd rypidlsddd alerlirara dtvyhpvgta rmgsddaavc
      481 dprlrvrgve glyvadasvm pklisgntna psimigerca dfvtadla
//
LOCUS       WP_010406084             225 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: outer membrane protein [Sphingomonas].
ACCESSION   WP_010406084
VERSION     WP_010406084.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..225
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23461
     Region          72..225
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mrklaltata aafglglaap afaqdgpppa rddatftgpr vgvilgydkl qpgrgpnssi
       61 ssdrkadglt yggdfgydva lnrfvigaeg evtgstgdvs naptsaaalg ygrvkqgrdl
      121 yagarigyvv apktliyakg gytndrldlt anngttttga hynldgyrvg agveqkigrt
      181 tyakleyrys nygdarleya nggntnnfsv dtdrhqvvag lgvrf
//
LOCUS       WP_010406090             188 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Sphingomonas
            echinoides].
ACCESSION   WP_010406090
VERSION     WP_010406090.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..188
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20563
     Region          53..186
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mrlplitpad lteqqkplye dmkagiasnf nvfktvdadg aligpwnpwl hepvigkavw
       61 eltkamtaqa tlddkprqia ilvcgahfda ayeiyahiav aeheqmspqr lselcanikp
      121 rdlsaqesva ydvafalvng gvlpepcyrl avdtfgqhgt neliylvgly alvsmtlngf
      181 nvpvpere
//
LOCUS       WP_010406199             603 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Sphingomonas echinoides].
ACCESSION   WP_010406199
VERSION     WP_010406199.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..603
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=65210
     Region          19..603
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mvdtptadtp repdishvnp adgktwfghp kplfwlfgte mwerfgyygm ralltiyltk
       61 hfvlgdrast glyggytalv yltplvggfl adqylgskra vrfgalimai gyftlafggq
      121 pakpyavidg qryevvverf rdapssdpke aryvvdgtrk lkirgnddgs lallaadgsv
      181 arsvaaghys dgadrdpvlt mvllialsli smgngffkpn istmvgelya qgdrrrdsgf
      241 tifymgintg sflgqilcpi ladmfgwpig lgfagvvmlv swamisfhgg rlsdvgnppa
      301 rtgrdpalli yccallavpv fyllfvnlma aeppvagsgf igyleslsvm gkllfgtflv
      361 svpgiilwsw fagnrtefqm mmaamvlvtf nvifwtlfeq agssltlfad rntnlsvfgl
      421 fslsapqtqn fnsiaimlla pvmsvlwgal akrnlepsip lkfaialmgv gagflflvlg
      481 trfvgpdfkv glwwlaglyv ihslaelcis pvglsmitkl siarvvglmm gvwflsisva
      541 qyvagviaqf asvdtvggqv tnlkvsldty vgvfttiaev aiglgvllll lswplkkwmn
      601 gvk
//
LOCUS       WP_010406205             428 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dicarboxylate/amino acid:cation symporter
            [Sphingomonas].
ACCESSION   WP_010406205
VERSION     WP_010406205.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..428
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42872
     Region          6..410
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 msatlnspst rilvslgagl llgiafatwl paavpgatav aqpigsawln alqmtviplv
       61 fsllvtgias taeaarsgav aaraisiilv vmvssavaaa lltplflglv pmpaasaaal
      121 rgalvnvgpp gavpplgefl agmvpnnvia aaanggflsl ilfalifafa ltridatgrt
      181 alltffsair damlvmigwi iwiapigvfa laltvaaktg taavgalfhy ivtvssvgiv
      241 vslfavpvav wgggialgrf vraslpvlav alstqsslas lpamlrssee mdvpvatsgv
      301 vlplavammr atgpamnlav aiyvaawfgv pltfatlaaa tvvavltslg svslpgqisf
      361 isaiapiavt lgvpvaplgl lvavetmpdi frtlgnvifd lavtltvaar gdkvplsaad
      421 tllqehhs
//
LOCUS       WP_010406218             294 aa            linear   BCT 01-JAN-2025
DEFINITION  bestrophin family protein [Sphingomonas echinoides].
ACCESSION   WP_010406218
VERSION     WP_010406218.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..294
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32876
     Region          1..294
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 miidsgprlr qifaevwrpl lvlfvwdvvv tggyyllpfh apslpltlfg salalflgfr
       61 stsayqrwwe grvlwgamin asrslsrtvr sylpdaegrd lqraiilrqi tyvnvlrcql
      121 rrqdpkpeve rflspdeakp slartntang ildgtgrrid haralgwidt vqqaaierll
      181 vditnaqggm erlkntplpn qyrffpelft rlfcvllpig lvetlefatp igstvagamf
      241 lavlrigddl vdpfantvhd vplsamcrti eidllqalgd papepmrpvk gilw
//
LOCUS       WP_010406227             375 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P) transhydrogenase subunit alpha [Sphingomonas].
ACCESSION   WP_010406227
VERSION     WP_010406227.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Bhakta,T., Whitehead,S.J., Snaith,J.S., Dafforn,T.R., Wilkie,J.,
            Rajesh,S., White,S.A. and Jackson,J.B.
  TITLE     Structures of the dI2dIII1 complex of proton-translocating
            transhydrogenase with bound, inactive analogues of NADH and NADPH
            reveal active site geometries
  JOURNAL   Biochemistry 46 (11), 3304-3318 (2007)
   PUBMED   17323922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..375
                     /product="NAD(P) transhydrogenase subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37815
     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 mkiavlreta egerrvaatp etvkkfvglg asvavesgag ltasiadady aaagasvadr
       61 aatlagaeiv lgvqgpaadt lsgvapgawl aaalnpfadr ariegyaaag lealamefmp
      121 ritraqsmdi lssqsnlagy kavldaasvy grafpmmmta agtvsaarvf vmgvgvaglq
      181 aiatarrlga qvsatdvrsa tkeqilslga kpvfvesvag iegegsggya gemspeyqaa
      241 qaelvsshia kqdivittal ipgrpaprli saaqvasmrp gsvivdlave sggnvegava
      301 getvvvngvs ivghrnvasr laadasalfs rnlfnflsaf wdkeagkpvl daeigdairl
      361 tqggkivnar llpaa
//
LOCUS       WP_010406326             275 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Sphingomonas].
ACCESSION   WP_010406326
VERSION     WP_010406326.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..275
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27870
     Region          30..273
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mslliawgpa iiallaaglf agfaaglfgi gggfvvvpam iallpllggs haeythvaig
       61 tsfativita lrstlshakr gavdfeilks wapwiiggvg igvmlarvlt gqalsiifav
      121 gitlmsinfl vpklarrqvs dtmptgvvra giagslgifs sllgigggtv avivmtlcgr
      181 sihkaiataa gfgfiiavpg tigwmliglg kpglpigsig yvnflgaaii tsmsiltapl
      241 gvasahalpa eplkrvfgvy llfiagvmfn ramhm
//
LOCUS       WP_010406372             189 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pseudomonas syringae].
ACCESSION   WP_010406372
VERSION     WP_010406372.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12134272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..189
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21698
     Region          11..151
                     /region_name="Acetyltransf_3"
                     /note="Acetyltransferase (GNAT) domain; pfam13302"
                     /db_xref="CDD:379112"
ORIGIN      
        1 mtitptlhte rllltplqle dapavqqrfp lwdivrylnn rvpwpypqdg alryiqdval
       61 paiangtewh wmirlqsaph diigsitlmt hpgnnrgfwl hpdwqgrgym keacrvinrq
      121 wfdvmgkplm qvpkaapnea srrisinegm rkvstqegef vggrfevevw emtreewlar
      181 alqagtsnv
//
LOCUS       WP_010406391             670 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Sphingomonas].
ACCESSION   WP_010406391
VERSION     WP_010406391.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..670
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70017
     Region          33..656
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mrcpsllpll tlavpfsala qqgpvppagq adivvlgqpl plppgvpayg svtigrarlt
       61 gdatgrvedv lldvagfqqf rrsdsrsanp saqgvtlral ggnassralv lldgvpladp
      121 ffgyipfnal avdrlagvrv trgggagafg agavagtiel asatradlpp vagelfygsn
      181 aavvasgsvs pdagggfvsl sgkfergdgf yttppgqftp atvraryrdg saslravvpi
      241 daqteiqarg llyrdarslr fagadsssag edasvrlihr gawaidalay vqarnfsnrv
      301 isatsfrltl dqrntpatgv ggkielrppv gpdhvlriga darlgdgqly enayaasgav
      361 ttrrnagght sttglfvedd wtlgrlvlta gvrgdrwtit rgffrettaa gatttdtryp
      421 drdgfegtgr agalfhasda valraagytg frlptlnely rpfvvfpitt qanaalgler
      481 lrgaeggldl kpvagvtfgv tafynrldga ianvtiapnl rqrrnvdtiv akgieltaha
      541 argrfsfdgs yafsdsrvha sgasrqldgf vpaqsprhsg satlawasph gfaaaltarh
      601 vgkqyeddlq tdvlppattl dgvltlpvgq rvgvvlrgen lfdetvitrn sagsidfgtp
      661 rtlwigvrlr
//
LOCUS       WP_010406502             445 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S41 family peptidase [Sphingomonas].
ACCESSION   WP_010406502
VERSION     WP_010406502.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..445
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47417
     Region          40..375
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 msrfttslfq asaiaavlai vpigtsamaa vdtgtyrems vfldvfnrvk aeyvdkvddk
       61 vlvkgaiqgm laaldphsay etgldydnlk iqtmgsyggl gltvtmedga vkvmspqpda
      121 pgaragiksg dyithidgkl ifgdsldesi qkmrgapgtk valtllrpgr dkpiqvtlvr
      181 ekivqkpvkw svkdgvgvit itafsehtge avtgairgiv kqlghdplgy iidlrdnggg
      241 lrdesiavad nflssgeivs qrgrdkadie pfyaesyvkg dlahgvpiiv ltnagtasas
      301 eivagalqdh hralvmgers fgkgsvqtvi dlgdnaalrl ttsryytpsg rsvqeggiep
      361 diavpqlsdp dyksrpvfre ddlrrhline vkanngalee dgkvdprfaa tadelkakgv
      421 ddfqlsyalk tlarlsstqs vtaak
//
LOCUS       WP_010405652             436 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein, partial [Wolbachia
            endosymbiont of Nasonia vitripennis].
ACCESSION   WP_010405652
VERSION     WP_010405652.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..>436
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          33..62
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          45..342
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(64,66,70..71,74..76,78..79,83,86,95,97,99,103..104,
                     107..109,111..112,116,119,128,130,132,136..137,140..142,
                     144..145,149,152,161)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          64..95
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          97..128
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          130..161
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          163..192
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          207..235
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(210..211,214..216,218..219,223,226,235,237,239,
                     243..244,247..249,251..252,256,259,268,270,272,276..277,
                     280..282,284..285,290,293,302)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          237..268
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          270..302
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          304..335
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          309..401
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Site            order(337,339,343..344,347..349,351..352,356,359,368,370,
                     372,376..377,380..382,385..386,390,393,402,404,406,
                     410..411,414..416,418..419,423,426,435)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          337..368
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          370..402
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          375..>436
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          404..435
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mftnrisnnl dqlqffvefl nenyetqkhl sltplhlaag ngqldlvntl lgegldinse
       61 ikydgftply faiaknrlem vnfliahgad vnhktilgft plsfasqqgy ldivntlian
      121 gadlstktdk lntplhlaae nghldivnvf iengldvnav nndrarplhs avqngnlevv
      181 kalisqgsdi nagssgignr kvdanitplh lgtqtgrldi vkvlleagan vnaktddkit
      241 plhlasqngf lelvdillka ksnvnakdye nltplhlaae rnhfgvvksl llvrgidvna
      301 kdhdnstalh igsqnghlev vklliekkan vnakknegft plhlamqqsh fevsdflikn
      361 ganintvddq nwtplhnaay ngfslkives liakganina kmddgrralh laaehnhlei
      421 mnfliengad inaldn
//
LOCUS       WP_010406541             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Sphingomonas].
ACCESSION   WP_010406541
VERSION     WP_010406541.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..214
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23665
     Region          33..79
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          101..211
                     /region_name="TetR_C_24"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17932"
                     /db_xref="CDD:465574"
ORIGIN      
        1 mtkssaaakn pagyesslre ikpgvvaykr arilaeasal fyekgyesat lemladrlsa
       61 tkpflytyfk gksailsaic eagvkeslaa ldrieeierr pidklkaslr evaeiivarh
      121 eylviyqrem mnldradaqr ilrlrhefdl rigkliddcv qdgavtvana agmsiwiggl
      181 lswiihcyrp gskrsaemvv dqavaaclrl iavd
//
LOCUS       WP_010406582             768 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Sphingomonas echinoides].
ACCESSION   WP_010406582
VERSION     WP_010406582.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 768)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..768
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82612
     Region          51..750
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mriisvtsrl lgctaafals safasaacaq sttapttasa apdknapdgd ivvtatrrdt
       61 slqktplait vltgqtltna gvtniadyak fvpslriqdn gpgqrrvslr gvqtsgeatv
      121 gvyyddtpvt gsvgvssdaa grtadftlfd vnrievlrgp qgtlygassm ggairvllnk
      181 ptqdyegkie sqvagtnggg lnyfvqgmvn vplvkdllav ravlyrrdsd gyidntylkr
      241 qnvndytatg grlmarltps snltidgmam ientdafssn wnpavgtyks atkvmlpytd
      301 rsqlynltgk ldlgpatvts itsyqhrrsa yaaddsyyia syrtaakcag yvnastgaac
      361 ssdqltnyyg yidslspaai yypgstkdft qevrissdgt hlfdwtiggf yqnrknnvts
      421 edaradattg diitpnqify rreifdkleq yagfgegtfh ptrtigltag iryfsynktv
      481 sgftdiawtl igaparplst vnssengtll kfnaswqanp dilfyatasq gyrpgganqv
      541 iglsadltpy ksdslwnyei gtklglldrk ltlnlaayqi dwsniqvsgr ttngafsfls
      601 nagaarirgv eaeafvrptr glqftfsgny idprltqdqv nasvvaagra gdripyipnw
      661 tgaagaeyta pisptldffa radfnyvgss ysefrptnvy rvkigayslt nlrvgidlkh
      721 ndagvylfvn nlfdavainr asqsstansy satsaaprti ginvrksf
//
LOCUS       WP_010406564             210 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010406564
VERSION     WP_010406564.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..210
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23301
     Region          11..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtraatprkp qarsqarids ildaartlla eqgvaslsiy svaeragipp ssvyhffasv
       61 pallealtad ihaafraslq apidhdqltt wrdlsrivel rmlaiynada aarqlilaqh
      121 glteinqadr qhdielgqlm levfdrhfql palpddvdvf alamelgdrv yarsvqlhde
      181 itprmaeegm rvfdaylgly lpvflvkrad
//
LOCUS       WP_010406603             768 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Sphingomonas echinoides].
ACCESSION   WP_010406603
VERSION     WP_010406603.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..768
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80790
     Region          <65..>182
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          198..765
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrlastaea trnalsrrgf lvasgaagia fgfshvlaai dpavpggtpa aptgpqfeps
       61 iwfgidaaai vtvniiraem gqhvgtalar iladeleadw dkvrivhvdt dpkwglmvtg
      121 gswsvwqtfp vfsqagaagr ialieagakl lgtsaancta rggavhaggr sisygdiakr
      181 ggvarqftpe elkalpikpa kdrrligkqv aaldiatktd gtalygidak vpnmvyarpk
      241 lpptrfgskv vsvddskakt vrgylrylvi edpsdtvpgw vmviaqnypa airaadllqv
      301 twtagpgatt sekdlqahaa dlagkaesgv aldivnagak ptnaastler vyttstvlhf
      361 qleplnalaf ekdgrfeiht gnqwqslilp tlakalgvpe tkiilrtyml gggfgrrlng
      421 dyavpaalaa kalgrpvkmv ltrqddalfd svrspsvqrv rmsfdkdnav iamehhaaag
      481 wptqmnapal laktksggay dpfaisgadh wyevghqtvh aipndlantt frsgwlrsvg
      541 pgwtnwales fideaalqvk sdpvafrlkl ltgagrnags apsaiggalr qaevvrraaa
      601 ragwgeklpp dtalgiatsf gqerdmptwv acvarvhvdr ktgvvrvekl tlvtdagtiv
      661 dpdgalaqtq gaalwglsma lhegtefang lvkdtnldty lplrmadvpe lditfveseh
      721 vpvglgepat tvvapaigna ifaavgarvr hlpitpaavl dalagrsa
//
LOCUS       WP_010406612             464 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [Pseudomonas].
ACCESSION   WP_010406612
VERSION     WP_010406612.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..464
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=51305
     Region          1..463
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mtdrvlidel qtlvdpgkvl tdagsletyg kdwtkqftpa plaivfpktt eqvqaivrwa
       61 nerlvalvps ggrtglsaaa vaangevvvs fdymnqvldl nltdrtavcq pgvitrqlqa
      121 laeenglyyp vdfassgssq iggnigtnag gikvirygmt rnwvaglkvv tgkgdlleln
      181 kdliknatgy dlrqlfigae gtlgfvveat mrldrapknl tamvlgtsdf nsimpvlhaf
      241 hgkldltafe ffsdksfarv margdvpspf dtpcpfyvll efeattedla dqalatfehc
      301 veqgwvldgv msqseqqlrn lwklreyise tishftpykn disvtvskvp eflaeidaiv
      361 aehypdfevl wyghigdgnl hlnilkpegl dkdeffvkca rvnkwvfetv ekyngsisae
      421 hgvgmtkrdy ltysrspvei eymkalkavf dpnwimnpgk ifai
//
LOCUS       WP_010406699             139 aa            linear   BCT 01-JAN-2025
DEFINITION  dephospho-CoA kinase, partial [Wolbachia endosymbiont of Nasonia
            vitripennis].
ACCESSION   WP_010406699
VERSION     WP_010406699.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         <1..139
                     /product="dephospho-CoA kinase"
                     /EC_number="2.7.1.24"
                     /GO_function="GO:0004140 - dephospho-CoA kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015937 - coenzyme A biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
     Region          <1..135
                     /region_name="CoaE"
                     /note="Dephospho-CoA kinase [Coenzyme transport and
                     metabolism]; COG0237"
                     /db_xref="CDD:440007"
ORIGIN      
        1 ngkidravls eyflaydenw kqfqslvhsv vrneleifia qekkndrksl vldiplllep
       61 kqdsvyiail lflslihads avqaqrlser nmdkeklnlm ssiqlpieek rqmsdfiidt
      121 sanvfsqvkk ivdslnlnt
//
LOCUS       WP_010406763             772 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Sphingomonas echinoides].
ACCESSION   WP_010406763
VERSION     WP_010406763.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..772
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=83951
     Region          5..768
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mtidrrtlls sstlalfasa lpwrldarap aaapnlfvgt ggdghtypgp slpfgmvqlg
       61 pdtdverwat csgyhhgdgs imgfshthls gtgigdmldv lvvpttgpvt ltpgpldnpd
      121 agyrqrysne iaepgsyrvt lesgvhaelt ttdrtgwhry sypkgpghvl idlshlildt
      181 sdhaplvdea slaidtdgti tgsrrvfrwa kgrrihfalq csrrpdrvtf ygdgdaeqpa
      241 gtthvsgkrl kmalhwndag aapillrcgi sgvdvagara nlaaeaphwd fdrtlraarq
      301 rwaealgvvq veggsadqrt imasalyhaq laptlfsdvd gryvgldgqi htvppggaay
      361 styslwdtyr alhplltlia partkslidd lirqtqqspy gplvwplqgk etgtmigwhg
      421 vvplaeaqak gipadyaaaw paiakrsfdf kapeqdnsla reaydklgyv padqvfesvs
      481 rtqeyayddw asshlaraag asadadrllk rsghwrnvid rdtgfarprf adgtwwtpyd
      541 pvqlghmpkp wwrdyteang wqatflnqhd iygriahvgg daafaaklda ffsapstlpd
      601 nappdisglv gqyahgnepd qhaaylyayv gqpwktqamv rrlctemyrn apdgiigndd
      661 cgqmsawfvf salgfypvdp veaayvfgsp lferatvrvg tgrtltieap gnradtpyvt
      721 avswngqpwt kswidhrtls sggtlrftms atpnpnfgaa radrppsfgh sa
//
LOCUS       WP_010406773             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Sphingomonas].
ACCESSION   WP_010406773
VERSION     WP_010406773.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..245
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26680
     Region          14..243
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mafsqqigqf regnpaplyl qlqhlireai ahdvlaqdda ipaerdlave ydisritvrk
       61 aigglveegl ltrrrgagtf vtgrveksfs klssfsedma argktasssw israagtvdp
      121 deamslglsp gtpvyrfhri ryaddqpmal efstiagycl pgisavedsl ytaldkagsr
      181 pvralqrlra vpfgpehakm lgvsaghpgl lierrgflkd graaeftrsy yrgdaydfva
      241 elsdl
//
LOCUS       WP_010406902             588 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Wolbachia endosymbiont of
            Nasonia vitripennis].
ACCESSION   WP_010406902
VERSION     WP_010406902.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..588
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=65548
     Region          66..277
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     Region          206..386
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     Region          408..578
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mqkiirllil ilvghlcygd daindflsal hdvkyvsynt kdfakflvqc nkasipqdfk
       61 kgfgpnlnga nfsqlylsks ifdgvsliga dfsntdlsdv sfidvdlrga nfsnanlhgv
      121 kikgtnlsfs kfastnltdi ifdqsnisya dfinsnlnkv smrniiglht kflnvkmnfs
      181 nlsnssasyi nfsdseindt vmqknnfdna sffgvdahkl kvqfsslkna niygaeikks
      241 dftgsnlsna yfnasiivds nfekanlsns qisyvkgdns nfiksilngs kikhayvfea
      301 dlqdadlsni dfsfselykv naydanichg kfhntkvvns dmngsffdhs lftsakieds
      361 dlsttsmykt kikdsqiyns tlshhnmdss eiensiffkl ladnsswsks kvtnsnfies
      421 dfkssvfydn afrktsffls nlsnstvsdv sflsssiyks siadihltdc kfdnsilidn
      481 qgqtkitnle naitsikdlq ekisqgkkfd vnysyfefkd mnlenanfsn silsrakfvn
      541 vnlnkanlek adlrytvfdn sslidanlsn snlegsslln fdskntks
//
LOCUS       WP_010406985             278 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Sphingomonas
            echinoides].
ACCESSION   WP_010406985
VERSION     WP_010406985.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..278
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29923
     Region          17..267
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mqtpfspldd apgprviqss riaailklle arsslsiael aarfdcseet irrdirqleq
       61 tgrvlkvhgg vrmpdadfea pyrlrfreqa dakqqigraa aelvepgmtl lidsgttsfw
      121 lvralarvpd ltivtnsiev asevlgrpkq rlflaggiin hdyraafgpe aiaycggfip
      181 dltifsmgai dvergfldfe pdeatfkral iesarrivvl adstkfgrkg ttrvagfgdv
      241 adlvtdappp hpfvtaaaat gmavhvarpa saaeaqpl
//
LOCUS       WP_010407064             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: trimeric intracellular cation channel family protein
            [Sphingomonas].
ACCESSION   WP_010407064
VERSION     WP_010407064.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..214
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21590
     Region          11..211
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mlplapwqfg silpwldlfg iavfaitgal aaagrgqtfv taaffalitg vgggsvrdll
       61 igapvfwvhd plvaaiclav avlvwttprg wwqgahapts aldwldgvgl aayavfgaak
      121 alafgippvp aalmgvvtac vggiirdvla gepsilmrpe lyvtaaalaa glhvalvelg
      181 isptvaagva ascgfalraa airwrlglpa ygak
//
LOCUS       WP_010407067             268 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Sphingomonas echinoides].
ACCESSION   WP_010407067
VERSION     WP_010407067.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..268
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28363
     Region          191..267
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mktiaivall gqvlatstda plvpsgkwtv dyanagcils rdygtvpavt sigfnpfplg
       61 dtlevitvsp gipakryqkl kgtltlqpsg etfqsevtvy giaarnntlt tlnaegdiaa
      121 kllrstsisi aladgtrksf avpgmpgaaa alracqddll kswgidpter drvptpkprt
      181 evatwlstdd ypseamashs egtsvivwti qpngligdcr ivqssgskpl ddtacrafkk
      241 kgryaavidr dgkpataham hkvvwrlp
//
LOCUS       WP_010407070             404 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Sphingomonas echinoides].
ACCESSION   WP_010407070
VERSION     WP_010407070.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..404
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=43864
     Region          25..392
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 maspvgidkq gactgqaigh gesmnerpgf yeffagggma raglggtwqc lfandfdpkk
       61 akayadnwgt nelwlgdvge vtlgqlpgqa dlvwasfpcq dlslagagag ltgarsgafw
      121 pfwklirdls kqgrkpraiv lenvcgllts rngadfaalc qtvgdagywl gamvidaqhf
      181 vpqsrprlfv ialdrdvemp arvfspwavd rwhperlrqa qaalpeklra qwlwftapap
      241 aprqarlidv iedhpgdvaw hsaadtkkll ammskgnrak vdlvagnarr aigavykrtr
      301 feggkkvqra evrfdlagcl rtpgggssrq tilvvergkv rtrlisaret arlmglpeay
      361 rlperynday hltgdgvvvp vvrhiaewvl epaltqsgia lasa
//
LOCUS       WP_010406704             439 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydroorotase [Wolbachia endosymbiont of Nasonia vitripennis].
ACCESSION   WP_010406704
VERSION     WP_010406704.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Gojkovic,Z., Rislund,L., Andersen,B., Sandrini,M.P., Cook,P.F.,
            Schnackerz,K.D. and Piskur,J.
  TITLE     Dihydropyrimidine amidohydrolases and dihydroorotases share the
            same origin and several enzymatic properties
  JOURNAL   Nucleic Acids Res 31 (6), 1683-1692 (2003)
   PUBMED   12626710
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..439
                     /product="dihydroorotase"
                     /EC_number="3.5.2.3"
                     /GO_function="GO:0004151 - dihydroorotase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006221 - pyrimidine nucleotide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=47871
     Region          19..436
                     /region_name="pyrC"
                     /note="dihydroorotase; Validated; PRK09357"
                     /db_xref="CDD:236479"
     Site            order(75,77,192,246,319)
                     /site_type="active"
                     /db_xref="CDD:238642"
ORIGIN      
        1 miwnllqtgq kegykiaytn ariidpetkl dikgsllteg gkivdfgesl fstsgvdeii
       61 dckglvlmpg lidihvhfre pgqehketih tgsksaaagg vttvvcqpnt vpaidsvvla
      121 kylkyrafet shvnvqfyak ittseeklte mallkeagav gftddgmpvm npmimrqall
      181 yssmlgvpia qhaedlnlsa ggvinegkis eelgvkgils asesvmvtrd illmknienv
      241 hyhilhvssk dsldaikrak dlglnvtcev tphhftlted ivkqhgaiak mnpplrteed
      301 rlamieglkt gvidciatdh aphdlsskdl plenaafgii gletmlplsl elyhsgqmgl
      361 ldvlakltyk padiihmprg riqknlvadl ilvdldhewe ikvdnfasks knspfggrkv
      421 kghvvrtvvs gktvylqks
//
LOCUS       WP_010406765             476 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 125 protein [Sphingomonas echinoides].
ACCESSION   WP_010406765
VERSION     WP_010406765.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..476
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52317
     Region          32..472
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 miltrretll ggaagaalva spalaaapla skrppvterl ftsraverei vhvsakigdp
       61 klrwmfancy pntldttvrm stvdgapdaf vitgdipclw lrdssaqlap ylhlvrddpa
      121 lrtlfhglia rqarsilidp yanafmqdps artnlgwakd dktemkpgva erkweidslc
      181 ypmrlahdyw qttrdpapfd arwaaaarls iatfreqqrk dgpgpyrflr esdrntetqp
      241 ldgygnpsrp vglihcgfrp sddaclypyl ipanlfavsa lrelavvaqg argdaalaqd
      301 atalaaeveq allehgrmrl rdgrevwaye vdgfgnaifm ddanvpslsg laylgcvaqs
      361 dplwqrtqaa awgpdnpyff kgkagegigg phaglrqiwp mslivralss ddpaviracl
      421 ktlretdadt gfihetfdqd darkftrpwf awanglfgel ivrlantrpa llegtl
//
LOCUS       WP_010407086             137 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Sphingomonas].
ACCESSION   WP_010407086
VERSION     WP_010407086.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..137
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15441
     Region          1..120
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mkylhtmirv tdpvatidff kllgleevrr fdnekgrftl iflaapgdhs aqvelthnwd
       61 pepytggrnf ghlayqvdni yetcqrlmdg gvtinrpprd ghmafvrtpd nisiellqdg
      121 vlapaepwas mpntgew
//
LOCUS       WP_010407093              69 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Sphingomonas].
ACCESSION   WP_010407093
VERSION     WP_010407093.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..69
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7511
     Region          1..60
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 minrlkvlra ergwsqgdla erlevsrqsv naietgrydp slplafriae lfalpieaif
       61 vspskgdaa
//
LOCUS       WP_010407204             126 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF423 domain-containing protein [Pseudomonas].
ACCESSION   WP_010407204
VERSION     WP_010407204.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..126
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13208
     Region          1..122
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mlrsflmlaa ffgftgvalg afaahglker lsaeylavfh tgvlyqliha lallgvaila
       61 tqipgrlitw agfsfavgil lfsgslyalt ltgfsklgii tpfgglaflf gwsmlglaaw
      121 rlgspp
//
LOCUS       WP_010407276             300 aa            linear   BCT 01-JAN-2025
DEFINITION  pirin family protein [Sphingomonas echinoides].
ACCESSION   WP_010407276
VERSION     WP_010407276.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..300
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32188
     Region          15..272
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtnddlilqt iipsthdlgg fkvhrtlpsr prtmvgpfif fdqmgparle vgtgidvrph
       61 phinlatvty lfagalghrd sigsdvviep gavnlmtagh givhsersps aeretgpels
      121 giqtwlalpe adeerdpafe hvakadlpti datnararvv mgslwgqsap tttyastiya
      181 divldaggsi pidaeadera iyialgeatl dgmtlepmtl yvlkpgvaat lrsatgaram
      241 lcggeafttp rhvwwnfvss srdrieeakr awtagefpkv pgddkewipi pgvpktvsyp
//
LOCUS       WP_010407295             216 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Sphingomonas echinoides].
ACCESSION   WP_010407295
VERSION     WP_010407295.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..216
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23915
     Region          20..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtptittfaw vppfargqvr dlrarwafee igqpyaldli rdaktpehrr fqpfgqvpcy
       61 rdedvalfes gaivlhiarr gtgllpddaa gqaiaeqwvi aalnsvepfv mdlvrcdlfe
      121 adkpwstqrr psvidtvrdr lggvaaalgd qpylggerft vgdlvmasvl rigrtkdild
      181 dfptlaayle rctarpafrk aladqlalyt eetvpa
//
LOCUS       WP_010407365             142 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Sphingomonas].
ACCESSION   WP_010407365
VERSION     WP_010407365.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..142
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14411
     Region          4..137
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mttrsgsasy dgfgkdgkgh vstqsgvlsd tqygfgsrfe dgigtnpeel iaaahascft
       61 malsfalaga gftagklett akvtldkdgd gfsitksald lkatiadisp eqfetiaaga
      121 kancpvskvl naeitlthsl na
//
LOCUS       WP_010407392             308 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sphingomonas echinoides].
ACCESSION   WP_010407392
VERSION     WP_010407392.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..308
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33838
     Region          5..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mdvvlsvagv skvyasgqra lepvnldirr geifallgpn gagkttlisi icgivtpstg
       61 tvtvlghdaq rdfrsarrai glvpqelsvd mfetvlatvk fsrrlfgrap dnayveqvlr
      121 dlslwdkrda kirelsggmk rrvliakals hepdilflde ptvgvdvalr rdmwklvhrl
      181 rakgttiilt thyieeaeem adrvgvidkg riilvedkaa lmkklgkrrm aitlqtpmaa
      241 vpsalegwsv alddegktlv ytfdsenehi pillaklgel gigysdleth kssledifvd
      301 lverkdaa
//
LOCUS       WP_010407395             408 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Pseudomonas syringae].
ACCESSION   WP_010407395
VERSION     WP_010407395.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..408
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44235
     Region          25..402
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrvaalclvl lplvapgiaa aqgislaqal eaafarnpel aaaqweigva egdrqqagli
       61 pnptvsweve dtrretsttt vmlsqalelg gkrgarieaa skgqdaarle lerrgnelra
      121 evvqafyaaa raqaglelar qsrtlaergl evaegrvrag kvspveatra qvqlaetdll
      181 vrraetlkin snrelarttg splasferld ysdlspgklp psaklltaln qsaelrlaqt
      241 qieqreaalg serakripdl tvsvgsqysr eerervnvvg lsmplplfdr nqgnvlaasr
      301 sadqsrdlrn avelklrtqt qsaldqwnta aqevesfdrv ilpaaqravd tatrgfemgk
      361 fgflevldaq rtlisarsqy leslatatda rvaierihgd lnrfslnp
//
LOCUS       WP_010407437              83 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein, partial [Wolbachia
            endosymbiont of Nasonia vitripennis].
ACCESSION   WP_010407437
VERSION     WP_010407437.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         <1..>83
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <2..>83
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          7..39
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          41..72
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 tnvkdnksrt slelavshgh lqvvkmllqy kkvdmnakgn ddwtilhias qesnlemvkc
       61 lvdegsnina knasgskpih iaa
//
LOCUS       WP_010407560             102 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein, partial [Wolbachia
            endosymbiont of Nasonia vitripennis].
ACCESSION   WP_010407560
VERSION     WP_010407560.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         <1..>102
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <1..>101
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(1,3,7..8,11..13,15..16,20,23,32,34,36,40..41,44..46,
                     48..49,53,56,65,67,69,73..74,77..79,81..82,86,89,98)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1..32
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          34..65
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          67..98
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 eggeplllav lagyrdivei llrnkayvnt kgpenttllh laakrghkei vnalitkgan
       61 vdamtingtt plylaaqegh geiaetlian radvnivnve ga
//
LOCUS       WP_010407443             424 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Sphingomonas echinoides].
ACCESSION   WP_010407443
VERSION     WP_010407443.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45114
     Region          11..416
                     /region_name="MFS_KgtP"
                     /note="Alpha-ketoglutarate permease of the Major
                     Facilitator Superfamily of transporters; cd17367"
                     /db_xref="CDD:340925"
     Site            order(21..22,25..26,29,67,125..126,128..130,133,153,
                     156..157,160,241,244..245,248..250,253,281,285,338..339,
                     343,347,363,366..367,370..371,374)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340925"
ORIGIN      
        1 maleakrlra iiggsagnlv ewydwyaysa lslyfsasff pkgdptaqll ntsavfavgf
       61 fmrpigayvm gryadrhgrk aglavsvalm cagslmiaft ptyatiglaa pilllvarll
      121 qglsvggeyg asatylsema trrhrgfwss fqyvtliggm lsalavtlll qavftkaqmd
      181 sfgwriafvl aavlalgvyl lrrglaetas fqalsadrpa sgmaalwrah prefllvgai
      241 taggslafya yttymqkfla ntvgfsvqsa taimtaalvv fmlvqplfga ladrvgrkpm
      301 lllfgiggai vsvpvfsale svrtpgaafa ivlvplllla aytsisalvk aelfpahira
      361 lgvafpyaig naafggtaey valslkgwhi esafywyvsa mlaltsvcfw llpetraasl
      421 ived
//
LOCUS       WP_010407668             381 aa            linear   BCT 01-JAN-2025
DEFINITION  SET domain-containing protein [Sphingomonas echinoides].
ACCESSION   WP_010407668
VERSION     WP_010407668.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Qian,C. and Zhou,M.M.
  TITLE     SET domain protein lysine methyltransferases: Structure,
            specificity and catalysis
  JOURNAL   Cell Mol Life Sci 63 (23), 2755-2763 (2006)
   PUBMED   17013555
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Dillon,S.C., Zhang,X., Trievel,R.C. and Cheng,X.
  TITLE     The SET-domain protein superfamily: protein lysine
            methyltransferases
  JOURNAL   Genome Biol 6 (8), 227 (2005)
   PUBMED   16086857
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Yeates,T.O.
  TITLE     Structures of SET domain proteins: protein lysine
            methyltransferases make their mark
  JOURNAL   Cell 111 (1), 5-7 (2002)
   PUBMED   12372294
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459262
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..381
                     /product="SET domain-containing protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42081
     Region          226..340
                     /region_name="SET"
                     /note="SET domain-containing protein (function unknown)
                     [General function prediction only]; COG2940"
                     /db_xref="CDD:442183"
ORIGIN      
        1 maidpwfpia ilcslagygs ylaglrrqlv qpnraswliw taataveaat yaavnpaalq
       61 gwvfalstla clvvtigiwr rstwsapsrg evactaacla alvvwivard afwahmlvva
      121 avpvsfwptw qsvaedrtre rspawglwti gdlatllvat rhgdqhagey vyilvellch
      181 asvwfmvgla tinplrslgf rngrfyvlda yaptanlfav gethlgkavy aaqgfaegde
      241 iirftgrrfr adrvpslmrg ssdrfvqvtp ehymgpsgri ddlinhscap naglrfggns
      301 vvlvairdia pgeeiawdys ttlaesnwhm icqcrspecr rvignfstls perqewfrar
      361 nlvapylrrk deialprera a
//
LOCUS       WP_010406899             324 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Wolbachia endosymbiont of
            Nasonia vitripennis].
ACCESSION   WP_010406899
VERSION     WP_010406899.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Nasonia vitripennis
  ORGANISM  Wolbachia endosymbiont of Nasonia vitripennis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12120816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Wolbachia endosymbiont of Nasonia vitripennis"
                     /db_xref="taxon:180837"
     Protein         1..324
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=37243
     Region          <230..288
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          234..264
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          266..304
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mkykaffill ivisnllaae qpeenkness inqedvsksn tdaektspll selkeitdpt
       61 nvineevpss nqtnlqseee tnikdtkalt splseekkee peekkishnn qtnlqpeeei
      121 skkdtelsts qltekkkeeq pdnitpvnke neesekwtkl nkeikkhksk siykrqydsl
      181 nehlpktift ddyskqffyc ikkgnliclr gvinklekig ltiqeilrfr nklgdtpliy
      241 avkqgeidtv rflllqgadp rvvdnnfksp ieiaiernqi niinaiaemm pylledkein
      301 nqensemynf aiktkentcd akdn
//
LOCUS       WP_010407809             356 aa            linear   BCT 01-JAN-2025
DEFINITION  COX15/CtaA family protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010407809
VERSION     WP_010407809.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..356
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=38429
     Region          23..331
                     /region_name="COX15-CtaA"
                     /note="Cytochrome oxidase assembly protein; pfam02628"
                     /db_xref="CDD:460629"
ORIGIN      
        1 mastpldqss dlahdrsrpg wlawwllava amvvlivavg gitrltesgl sitewnvasg
       61 vlpplsdaqw qaefakyrat peyryeagpa gmtladfkai ffwewfhrll grviglafal
      121 plafawirgw ipigyaprll allalgglqg vfgwlmvrsg lggtmtdvsh fwlsihlcta
      181 lvtlaglvwt aldlqaldrd raarparfrp iamlagavlf lqillgawva glnaghasnt
      241 wplmqerivp eadlsqglff avthdpfllh flhrwfawaa fgallwlglr alsrednagk
      301 aliglamgqv llgivtvvtg vslwiavahq vtgallvaat ataahavgrr pqghge
//
LOCUS       WP_010407861             768 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Sphingomonas echinoides].
ACCESSION   WP_010407861
VERSION     WP_010407861.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 768)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..768
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83017
     Region          56..730
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msirtearsr llgvsafalv asfcataaaa etapaaateq ktepaaktdi aegsdivvta
       61 tkanelapvt aslkttqpqa ivsrsfieds lpatvdfnqi alitpsvsny ggnngiglse
      121 skaqirgfqd geynitydgv pfgdtndpth hsttffpsnt ietlivdrgp gnasnlgqat
      181 fggtfnlfsr atrddfggqi vgsygsfnty largllqtgt fangaqavfs gqyvhsdgrt
      241 syskyqnynl fgkvvvpvgp dvkltfiaty nknrfnqads dgstlyqqsl ygkyfglnnd
      301 pktsqyygyn htdkttdfei ikleanlapg avfenrayty yydnetlsan dvttlpgaay
      361 tttgadgkai agdipgytkt nkyrvfgdia kvridlasfa titagawlef shtyrqqtdv
      421 dlttggfnyi ekvvkapatg lnpgaltpqy ikfdqksrgn hteefvelel rpieglkitp
      481 gfkhvdfgrk idalynqttr yaqrnannys adlpfvtiny qptsnfsiyg qyakgflapp
      541 lsqlyvantt fsnavpqkst nyqagavyhg shlsldadvy vinftnkfys ytdtsgqglg
      601 tiftniggal ykgvegqvty afgnglavfa nasrnyaktn vytdpvtgkv vprtiigkap
      661 mstaaggily kngpikfslt dkwtgpqyad lantyrispy ntvnlatsyd fgrirvgvdv
      721 tdllnsqkvt qigtgkntag igvvstsnfd qyyyqpgrai tgqmtltf
//
LOCUS       WP_010407944             210 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Sphingomonas echinoides].
ACCESSION   WP_010407944
VERSION     WP_010407944.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..210
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22805
     Region          1..199
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mklydaawap sprrvriyla ekgievdrvp vdlrsdehlg aaflainprg vvpaleldsg
       61 evlcessaic ryfealqpap slfgesaldi arieswtrri eqegyaavvy vlrnqreafr
      121 drgvagkwpa ipqipelaer ggilwaafst aldaqlatra wiatdaysfa ditalvtidf
      181 akaarlavpe glgnlrrwha aasarssaaa
//
LOCUS       WP_010407952             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Sphingomonas].
ACCESSION   WP_010407952
VERSION     WP_010407952.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..222
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23248
     Region          144..220
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mayadrntsg srvvsivivs iivalfawgf vngltfkyik kvteklntfd vveppppppd
       61 kppppppeqp qlqtppvvsp ppivrvtapp ppvvsvavpp palvitpraa apapvpvaap
      121 paptinkqag pkgdpsqwvt tddypsdals aeaqgtskik weintagrve ncvvvassgn
      181 asldraacsn itrrgrytpa ldsagnpirs sssrnvvwrl pq
//
LOCUS       WP_010407969            1270 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010407969
VERSION     WP_010407969.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 1270)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1270)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1270
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..1270
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=140531
     Region          283..961
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mvttkfiatq nedggetial lreqpgglfr rasseivpvp ewprvapeag qaalalaral
       61 dddgqiseea egivlppqiv arldeadafa lglppatsmt lqlnsggsla egtikvdtkw
      121 vrrgglpvra diagarlrdg grvgripepi ysafqsalav naagdpdqrr affaelrskl
      181 gddigtgiea dgfldrvria yaanfslnak tdhgrfdfdp vlfsknases aegdlvdeee
      241 aslltpqdnq hfqrrfrgqe ggrrsyllsd gtllfldpml gkaldivrak qvgtsrekre
      301 flrspqrvlr eelkldasgd deaadclfie tqqfservsg ievwqkpvlp wikpkpnswl
      361 pegfglrigd ppnarhvqla pgeaekladd vemaidacke tvswaaeeip atpatlqaar
      421 aianledeis wvreeraefe lpptetaeif flqvgenfeq ldyarlprps tgvtsfeppe
      481 lpngmrsnpk phqvqafawf aeawerrlpg vlladdmglg ktfqalmfll wvrqrssqrk
      541 pvliiapagl lrnwqaeisq hidsgllgpv veafganlrn frleagsdir ggtsrldase
      601 wtdagivltt yetmrdyhms faripfaaiv ydeiqklknp asqmtraaka lngriqvamt
      661 gtpvenrlqd lwsiadtvyp gflgssrefe nsfppndldr lrdlqsrlte rdgelppfml
      721 rrmkdeiltg lpekssrkys vkmpvaqaqa ydlvlarara lresgeqgam lkvlhmlrgt
      781 slhpspprgv tdideyigqs arlqktfdil eevkergeka llfcedlemq aflataiqer
      841 fslsqrpmci sgkvaghkrq emvtrfqssp apfdvlilsp kaggvgltit aannvihlsr
      901 wwnpavedqa tdrayrigqt rpvtihipma vhpdeaigps sfderldelm erkrslsrgl
      961 lmppesdcdv edllsgvlng rssgqqdass lpgipreiea dgendrqevg dqepeassds
     1021 pmaseinepa gygkipdple npteddeaea atndtdkksp sshsseeaap sappkaaenv
     1081 rpidageqtr rpilslgtpv eaaearatsv qrvvfeqygq rdwtifeqya rdaridwlei
     1141 qdpyccanel argrlinfis rfeclaselt avqiiafdad svqsrtpest peqrrdleer
     1201 wnrmfpsvsl hlaqksrrst gdlhdrfvra klengdrvvw dlgrgvdgvm sarwscvvna
     1261 fyetsagvtk
//
LOCUS       WP_010408020             590 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptide MFS transporter [Citromicrobium].
ACCESSION   WP_010408020
VERSION     WP_010408020.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..590
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62866
     Region          12..554
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mandvsglph gdsagtilgh pkglfvlffa emwerfsyyg mrallifylt khwlfsdses
       61 gviygaytal vyiapvvggy ladkalgqrk avlfgavllt lghffmafeg spgagnennp
      121 iifvfwlala liivgsgflk anisvmvgql yprtdvrrdg aytifymgin igaaagsllc
      181 gfigetygwa ygfglagigm laglvvfiwg kplllgrgep prllgkttel gvyglgllfv
      241 alcwvaiqyq davgiflgtf gaalvcyvls iaifqlpygr ysaapkaall syvllsvvla
      301 vsmffvsqge gyeswqlpat igfggvvtim ilqmiaktdh drdrivsamf liivsiifwa
      361 lfeqagssln lftdrhvdrg gvpastfqsi naiyiillap vfaitwqflg rrgmepstpm
      421 kfglgviqvg lgflvlvwga qsvgvdvptp vififliyll httgelclsp vglsamnrla
      481 pvqiaslimg twffasatgn faagliaaat gaegsgeeag kqvvldvyss vgwyavavgv
      541 avivvspfvk klmhldtlad ddvgddlegq segpgepqga gihpttrpth
//
LOCUS       WP_010408044             410 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Citromicrobium sp. JLT1363].
ACCESSION   WP_010408044
VERSION     WP_010408044.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 410)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..410
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43166
     Region          10..397
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
ORIGIN      
        1 msrsarlslw qaalviarrd ftaivfskvf llfligplff laisagggyv gamaadsadd
       61 pqlgialpae ataaildaqe rldplvgmpe vaavdpadaq dprallqaed snlfavlsgt
      121 ldeplltgpk ddierwsget allvgaargt tipeadiaid ttdtgiinqr taqdatarag
      181 ivmlflltml lagmvlsnlv eekgnkiiei laaaipmdav fvgklfamlg vslvglvvwg
      241 svggaivflg asalpvippp avgwplffal fviyfamayl ligsvfltvg smaptvrdvq
      301 tislpatilq llifflanfa vgqtgswiev aaaifplssp ymmlaraake gvlwwhlaal
      361 awqvlwvaif vkigatlfkr tvlksgtagr ekgagrkgll amlrlttnqs
//
LOCUS       WP_010408053             296 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Sphingomonas echinoides].
ACCESSION   WP_010408053
VERSION     WP_010408053.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..296
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32694
     Region          81..238
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 metlitgspi ilvvgvamvl teivwrvgag rgydrstamt tiglvagnip aaalnaavlg
       61 vvysvawkia pihlplgdwr twaagflfve fayywfhras hrvrwmwath avhhsaeemt
      121 llsslrlgwt nvfsggwlfy vplilvgfdp rlivvlltan lryqfflhte aplslgrlew
      181 vlnapshhra hhgrneayld cnyggvlilf drvfgtfrpe radepvefgl kgraaeanpv
      241 kvvwrewadl ftairksgsv laavrvalap pgvdpnkgdd hlldatvala qarnvq
//
LOCUS       WP_010408063             834 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010408063
VERSION     WP_010408063.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 834)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..834
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94144
     Region          79..>129
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 meqhitdtrq anrrfgkhap dqhdlsvlfl srvgarrrka llaeyreavy dkafpdsdla
       61 enpedwaqyi dgklppplph tevilllreg kviggatvey yrqadagllt ylaiaedyre
      121 kglsrrlvda ahkalaaias kstllfaete kfddnaeede raalirrhrr ldalgayaid
      181 fdyvmpplrp gaepralhll vldppdpgra prvsahtvra llqelaqslq trledhaptr
      241 ameaflagrk tltvsrlpgt rfdrrfretp viplhgpaaf tfafelgftg prgeeqppai
      301 vlksimdtll rdkkvrekli eparsylddv ttgppghngr pllflaagdy rgspnrrvml
      361 krperwlyka enegremhaa prttafelrd cfcvfesgrv fylptlvlpe daeegideyt
      421 vlqlqalamk pedpdevrry gdleftwqpf ehdgplggsi fdfvearlaw lernepatqp
      481 gafrdlihay girrpgferr avrpadlrnl cisieseelv qtaeranaif dhdgngapdl
      541 srlksadrsw iapggtldlp phddpendid rkllalagla tgvpdfpwqd ksevhdstrp
      601 ggasvdsvly vhprfileva rewrsftnsl dslgncpyll lmwiaavqde ltvttiedri
      661 edmiydpgre parfraiamr dvdsvrrnak rmsgrsgari leknlqrrld lfrfhtihrt
      721 gkifrypkek aalemllhek giddrferal amidrieglv edttsmksay tekrtnqala
      781 viallglvsv gndialalek sdsvgivtfw vlitaalvli ayfiwneita rrdr
//
LOCUS       WP_010408078             247 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010408078
VERSION     WP_010408078.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..247
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25510
     Region          9..234
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; cl46157"
                     /db_xref="CDD:480497"
ORIGIN      
        1 mellagftwl qlavalgtgl vaafirglag fglaillvpv lalalspvea vlttnvvall
       61 igglelprll reaersvwii iglvllttlp glallaatpp dlarllialv alsafaailf
      121 pvreperpgm lttgltgaat giltgfagmp gppvvpyyvg raiprqvaks smiliftfaa
      181 ligigsgval grmewrlall galllpvvli gtwlgrradg yvsdrawrif vgvvlaaaal
      241 aalaklf
//
LOCUS       WP_010408064              63 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citromicrobium].
ACCESSION   WP_010408064
VERSION     WP_010408064.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..63
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7036
     Region          1..63
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mknrlkvlra ernwsqqala delgvsrqsv naietgrydp slplafqiae vfgmaieeif
       61 srd
//
LOCUS       WP_010408114             272 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010408114
VERSION     WP_010408114.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..272
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28966
     Region          30..242
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mfrlflaaca vsligtaaap ahagpvsdrv yqpvplsqte vefrgepplp iqaktrdgle
       61 legafwppee gidqivvvfh gngynhlvsa yraeplrigg rgvlvasyrg ygdnpgtpse
      121 gglysdaeaw iakarelrpd ariylfgfsl ggavalqmaa rddfagvatm gaftrlrdaa
      181 pllarpfike rydnlasial vtepalllhg trdgtvdpkm verleeaggp nitrinlkgg
      241 ghwvpldsia ggiwqqweaa ealapgdtpm ap
//
LOCUS       WP_010408167             724 aa            linear   BCT 01-JAN-2025
DEFINITION  M13 family metallopeptidase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010408167
VERSION     WP_010408167.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..724
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=79348
     Region          35..724
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mirtilatta svaalamaap avahegddqg giemllqdsg asegatetpt msfgewgvdt
       61 sllsdeidpg ddffayvnqe wldanplpae ysrfgafnll rekstsdvkt lvdsllakpe
      121 aqltgdekri vdaynayfdt saidaaglsh aqpyldkirg astlaelatl wgqpgysspl
      181 gggvsvdske ptrysvyvgs gglglpdrdy yldesekgre iqskyrdylt flmdeagyed
      241 paamaqsiyd fedtiartvs wdratsrnrd ltynalspse lgelaegfpl aalltasgfa
      301 etdrfivgdl ppsleeaeel gldqdtldki gggtpammal avntpvevlq awtikeflen
      361 nasvlpsrfd eadfafygqt lqgtpeqrpr wkraigeteg llgellgksy vaeyfpaenk
      421 aameelvanl rvalresige igwmgedtke qalakldsfd pkigyrdnle tyeglairpg
      481 dpianrmaaa rwnaeenlak lggpidrtew fmlpqtvnay ynstkneivf paailqqpff
      541 alsndpavny ggiggvighe mghgfddqgs ksdstgmlrn wwtdadraaf delgdalveq
      601 ynsycplddg etcvngrltl genigdlggl slayraykls lggkedkvid gltgdqrffl
      661 awaqvwrsqq reeaarsrll tdphspeefr vngivrnmda wyeafnvspq ddlylppeer
      721 isiw
//
LOCUS       WP_010408282             230 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Sphingomonas
            echinoides].
ACCESSION   WP_010408282
VERSION     WP_010408282.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..230
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25394
     Region          1..228
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mikvvsynmh kgigldrrrd prrildvlre idgdvialqe adrrfgtkaq viphaliedh
       61 spwhavsfgh dgasmgwhgn amlvrkgsei raatslhlpa leprgairad viighhairv
      121 lgmhldlsgl wrrrqarail ahidacpapl ptvlmgdlne wtarggclhd fgrdypsvpt
      181 gpsfharrpv grldrimtrg frvlgcgvhd salarrasdh lpiwailepl
//
LOCUS       WP_010408288             339 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010408288
VERSION     WP_010408288.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..339
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=35758
     Region          8..338
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mgesnahyya ardplgapre adggdfvtap eisqmfgelv glwladiwsr agappdpiyc
       61 elgpgrgtla kdalrsmarf glspqvhfve gspvlralqa eavpgaqfhe dvaslpedrp
      121 lllvaneffd alpvrqlvrt dagwrermig lddgalddgg qgegafrfva gdqpmdsavp
      181 egwadrpagt iietcpaata vmgeiarrla eqggvalivd yghlrhrtgs slqavaqhkk
      241 vdplvrpgma dltahvdfaa lataaridgv rvlgtatqge fleslgigar aaalaraape
      301 raleveeare rlvsaeqmge lfkvmafaaa dwpagaglh
//
LOCUS       WP_010408321             527 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudomonas syringae].
ACCESSION   WP_010408321
VERSION     WP_010408321.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 527)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..527
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58357
     Region          1..525
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mhdnlieird lrvafngrev vhgvsldirr geclalvges gsgksvtahs ilrllpaktv
       61 stqgsirydg ldlvsasdkq lrslrgnrva mifqepmssl nplhtvekqi geilvthkgl
      121 kgkaaltrtl ellelvgird plsrlkayph qlsggqrqri miamalanep dlliadeptt
      181 aldvtvqvki lellkslqqr lnmslllish dlnlvrriaq rvcvmregei veqadcqtlf
      241 dspqhpysrl linaepdgep apsthsntll svqdlkvwfp lgkawfkrep qyvkavdgvs
      301 fellkgktlg ivgesgsgks tlgqailrlv dsegsirfgt kelslhsqhl mrplrrqlqv
      361 vfqdpfgsls prmtveqiia eglvthnigt pkereqtvir vlqevgldpa trhryphefs
      421 ggqrqrisia ralvlepdli lldeptsald rtvqkqival lrdlqirhgl tylfishdla
      481 vvhalahdli vikdgkvveq gpsreifaap qqaytqellr ssglvfa
//
LOCUS       WP_010408355             791 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Sphingomonas echinoides].
ACCESSION   WP_010408355
VERSION     WP_010408355.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..791
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84527
     Region          44..769
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mrssiftatv savavlalmp cvadaqptpd qpkadaaidp nsdivvtarq raenlekvpl
       61 avsvvggali drsytvntsq lsllvpalny ssanprntaf tirglgssvv avsqandgle
      121 pgvgfyvdqv yharpataaf dfsdiqqiev lrgpqgtlfg knttagaiti ttraptftpe
      181 aseelsvgsy nfvqakasas gpligdtvaf rlsglvtrrd gvidnvrtga kengignqav
      241 raqilfkptt dfqlrvtgdf tnfesecctq vylrvgqslr sparqypala alfnysppst
      301 npydrvtdid aalgvntneg gvsaiadwnv gfatltsvsa wrfwnwdaan drdytgipvq
      361 lsqhipsrqd qysqelrlas ngdhrlgyva glyffdqkit gepisiygpa aayyligqtt
      421 gtpavavpan lldgygtdgh trlkedsyaa faelnykilp rltltgglry tyevkdgtyd
      481 ttvfggpatt nttlinarlg vlrpqsyvah dresnvsgra nlawqatdtv mlyggyargf
      541 ksgginlsgl plntanqpvl ttavirpeln ttyeggikaa lfdrrlvani agyytdvrdf
      601 qativdssqt valrgylsni pkvtvkgfea ditanvtraf qlrgnvayah gtyatypagp
      661 cplevqtaat aacnltgrpl aglpkwstti ggdytlplgs aalilhadss wrtsyygdps
      721 lskytlidgy nvtnaslglr sksglevavf vrnlfnakyi qnltiqagns glilgtpsdp
      781 rvigvtlrar q
//
LOCUS       WP_010408385             797 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Sphingomonas echinoides].
ACCESSION   WP_010408385
VERSION     WP_010408385.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..797
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85259
     Region          53..781
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msfhtvsrva lalgllagls nvanaatsda apapgepvaa paaqpddaaq tdilvtarrs
       61 trsvtqldst eiqkilpgin plkaiqtlpg vtyltadpwg nneqnislfi hgfnqqqlgy
      121 tldgiplgdq nygnynglsp qraiisenvg kvtlasgagd lgtastsnlg gtidtfssdp
      181 khsfggtvaq tvgsysalrt yvrldsgdlg ggnafyvsgv rqdarawdfn ghqggyqang
      241 kfvhdsgsik ltgyfaysdk tepnedatvv niskgevpgs vpytrpflyp dfktavaylt
      301 saeyaaakdn yrnyysdaqr tdylgyvamt aklssavtyd akvyyhhddg vgvvagpitv
      361 aglpqlfsvy ypgqnlstvf ggsgfatrtt eyridrggii qtlklslgnh diefggwfer
      421 qsssafrrwy aldvnnpstp yqrprdtlnp litqyysevr vdqlqshvqd awhvlptlti
      481 lggfkstyqf atqrikvqpl lgsfagtval pngalettkv flpevgavwe vtpndqlfvn
      541 aqknirqfqt saaaglspfa lgsqgafdlf sstvqpetsw tyeggvrshh qlggglsieg
      601 qlsvyhvdfs nrllgispnp ivnsitsgaa iiqnvggvkt ngvdfaftlh agprvslyna
      661 lsyntskyka dyisgtttip tkdknvpgsp dwlnktvlsv ghgifdgqli gdyigrryat
      721 ytndlsvggy ftlagqigat ipldqrmvak alhvsvnvtn itdrkaassl sigsatntys
      781 vfplaprqvf gtvsisf
//
LOCUS       WP_010408409             159 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Citromicrobium].
ACCESSION   WP_010408409
VERSION     WP_010408409.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..159
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16837
     Region          4..121
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 maflasvlgr illalifiva gitklvnlga tqtfleqttt lptgialpvg ifevvfgmfl
       61 aigfmtrvss illcgftlat ifffhnalad haqlqvalkn laiaggllmv faygqargsv
      121 dvwrerdrar raelraarag gtengaeear qkapdgtav
//
LOCUS       WP_010408431             243 aa            linear   BCT 01-JAN-2025
DEFINITION  TlyA family RNA methyltransferase [Sphingomonas echinoides].
ACCESSION   WP_010408431
VERSION     WP_010408431.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..243
                     /product="TlyA family RNA methyltransferase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25915
     Region          5..243
                     /region_name="YqxC"
                     /note="Predicted rRNA methylase YqxC, contains S4 and FtsJ
                     domains [Translation, ribosomal structure and biogenesis];
                     COG1189"
                     /db_xref="CDD:440802"
ORIGIN      
        1 msktradqll vdrglaesrt raqalimagl vfagerkidk pgqavaddvv ldvrgrdhpw
       61 vsrggiklah gldavgwdvt gavaidvgss tggftdvllq rgaarvyavd sgtnqlawkl
      121 rqddrvivhe qtsariltea hipepvdliv cdasfigltk vlevplrfak pqarllalik
      181 pqfeagrnev gkggvvrdpa vharvctevs awvvahgwsv vtlvespitg pegnveflia
      241 atr
//
LOCUS       WP_010408449             318 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Sphingomonas
            echinoides].
ACCESSION   WP_010408449
VERSION     WP_010408449.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181037
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..318
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35818
     Region          30..269
                     /region_name="CE4_NodB_like_1"
                     /note="Catalytic NodB homology domain of uncharacterized
                     bacterial polysaccharide deacetylases; cd10960"
                     /db_xref="CDD:200583"
     Site            order(33..36,101..106,142,144..145,172,178..179,232,234)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:200583"
     Site            order(35..36,101,105,144..146,172,232,234)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:200583"
ORIGIN      
        1 mtmlrlillg liaiplgcsp vaarskhaki altfddlpal tmakeqpyvn glnadilegl
       61 rkhripatgf vnesklneld rpqqiavleh wldagmdlgn htfshespnr lgaaayiadi
      121 argepvtrgl leerhrrigw frhpyletgt peavkheina wltahgyria pvtidaddwe
      181 faepydaati ardeatrari rhlylahtat tirwyrsaah alfgrdiayv mllhatrlna
      241 dsiddlaail qrehlrpvtl aqamkdpayr tpdpyagkeg iewierwsma lhkplpwssf
      301 tdvpkeieaa ydrvdhdr
//
LOCUS       WP_010408458             538 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010408458
VERSION     WP_010408458.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..538
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=57075
     Region          26..532
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mqrhlfaplv slaalaigga asaqeptlad atpvveteag pvqgleqggi daflgvryaa
       61 pplgdlrfqp pakpeawegi adatgygapc mqlysasgpn esemtrriqa ifptsteakm
      121 dnedclflnv wtpeagdggk rpvmvwfhgg gyaygsgnwp ayngrnlaek gdvvvvtvnh
      181 rlnafgylnl aekfgedfaa sgnvgnldlv rslewvrdni aafggdpenv timgesgggs
      241 kvshlmampa adglfdkavi qsgpgvfsgk paeaadyaak ilkaagvetl ddlrnvrsde
      301 iveavrkatp sgamgsgpqf gpiadgtiip rdpflpaape qssdipvlig ynkdemtlfv
      361 aaqpwfgrlt egtlnamtga mgeqavaava ayrkrypdys pthlaaiamg trfvrgtyll
      421 adqqaktasa pvyvyrltwe tpigggmlrt phtldiplmf dnavesaalv gtgedaqtma
      481 dmmsdawiaf aktgtpssel lpewkaytpa nrnvmelnve pqlvddpekd irelpsel
//
LOCUS       WP_010408484             737 aa            linear   BCT 01-JAN-2025
DEFINITION  spermidine synthase [Sphingomonas echinoides].
ACCESSION   WP_010408484
VERSION     WP_010408484.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..737
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78165
     Region          539..664
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mssrlarplf vltifagsfl lflvqpmvar malprlggap avwnsamlvy qalllagygy
       61 ahwlgrlsqr aqgmthlgvl llaglwlpig lialqpgpta lpalwvpwll tlsigplffa
      121 isaqapllqr wfslsrdgen pyalyaasnf gsfagliayp llvepgmalv gqrvlwssgy
      181 ivvgllvalc aatlpkagsg avglaepspq sapptrgrva hwialafvas glmlatstyi
      241 stdivampll wvvplglyll sftvafatdr ttadmqtria pvaillfggi lvggmggmpy
      301 lgaimalall flgcvalnta lyrlrpepdr ltgfylamav ggalgglfaa viapivfdwt
      361 yeypilvlaa allvpqhpll gplgvlwhrs aqrrhvltgv valavlalvv lilanpgpad
      421 gpgplqqaal lamvaiglva igarwafala vlgaliafgg yravqislep hartrsyfgv
      481 ytvhsmatqr qlahgttvhg tqllgspare rtptayyvag sgvgramqal ptlygaharv
      541 gvvglgagtl acyavagqaw rfyeidpavv riardtgqft flslclphpt ivlgdarlnl
      601 drarptsldl laldafssds vpmhlmtrea fasyarvlap rglllvhisn rfldlepvva
      661 aaargggwhs aqlfyrpgan nrdaatmsqw ialsrdpgvi qtlksrdsaw epvklrpgfa
      721 pwtddystil pllkagr
//
LOCUS       WP_010408493             796 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Sphingomonas echinoides].
ACCESSION   WP_010408493
VERSION     WP_010408493.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..796
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84937
     Region          49..782
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mftnhhtvmv rllaatafcs tiaispafaa tapetaptap aaasegdqlg divvtaekrp
       61 qtaqktpisi svlsgadlan rhvvsladlt dgsipslkva pfysrnsali vnirgvgvls
      121 dgnqpardqg vgvyvngvyl graqglgtal fdidslevlk gpqgtlfgrn teggainitt
      181 kkptgefhan llagvgnfgs ykaeghidlp svagialkid gvvsrrdplv kntltgasgf
      241 naydkrgvrv ealwkptsdf sadyafdtsy dastslylql lglgtnkqaa lgtvqatrad
      301 vanvgvpeqp svgkvhghel nleyhparnl tiksitsyra ltqsqydngs aattmsnssg
      361 vftnvafsry slaqfrqnqf sqefqaigel grlkyvagal yyrenvqdna qafatnqftd
      421 aagsaytils lnydaqridr ashvsttsvg afgqatytpa llddaihvtg glrwtrdakh
      481 gqlftvngaa pkvfdvigtr yldahwsrvd pmvnvlvdvs rdihvygkws tgyksggans
      541 rslqylafnp etvsvfeagl kteffnrhar fnvsayagty knvqvdfsgl yetivggtlt
      601 rsnrtttetl napgtggihg veadfkltpv phltlgasya ytyvripsta npfpataggt
      661 vnntpvpiyq tytpkhgasg tidyevplqg atirahldgn ydsgfyangn dvlylgagnp
      721 gnvyqpkgds afivngtlal adidmgrgda rvtvsvwarn lfnehhvfyr alsltsgyng
      781 ffneartfgg qvqvkf
//
LOCUS       WP_010408517             241 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Citromicrobium].
ACCESSION   WP_010408517
VERSION     WP_010408517.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..241
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26213
     Region          8..232
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnapsppepl ielegitkvf gtgsaafqal kgvdlkidrg qfvaimgpsg sgksttmnil
       61 gcldvptdgi frfkgvevqk ldrdqrsllr rkylgfvfqg fnllarttal envelpllyr
      121 gekksvrqea amrsldavgl gpwashtpae lsggqqqrva iaralvtdpd vlladeptgn
      181 ldsersveim ellrrlnaeg itvlmvthee emaafaktiv hfrdglveri ergarsmevp
      241 a
//
LOCUS       WP_010408561             175 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TadE/TadG family type IV pilus assembly protein
            [Sphingomonas].
ACCESSION   WP_010408561
VERSION     WP_010408561.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..175
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=18562
     Region          3..143
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mtrrfwadqr gvsavefaic lpfivllylg gyqlsdsisa yrkvtaatrt vadltsqsts
       61 vtasdldtil nastqilspy kisaakltvs qiytdpngvs tvdwsrglni naltkgtsft
      121 lpgtikqngt yvivasidyt ytpvaglall gaipmrdqii msprasnsvt gvnvs
//
LOCUS       WP_010408574             181 aa            linear   BCT 01-JAN-2025
DEFINITION  GbsR/MarR family transcriptional regulator [Sphingomonas
            echinoides].
ACCESSION   WP_010408574
VERSION     WP_010408574.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..181
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20355
     Region          1..160
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mtlldhpdak afilhwgemg thwgvnrsva qvhallylse kpvdaeaive alglarsnvs
       61 talkelqtya ivrrvhvegd rrdhfvaegd lwemlmriva erkrreidpt iallaeladr
      121 lrsddtapah lrdrvvrmhe flstlggwye qvrtlpkstl vtlmklgskv arflpgskak
      181 d
//
LOCUS       WP_010408660             379 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010408660
VERSION     WP_010408660.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..379
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40485
     Region          1..375
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mplyydddqa mladsasdfm reegaiakql rhwrdrdckd gfghglweqf gemgftgill
       61 peedgglgmg qveanivlee iganltpspf lsssvlaata lkhgsddtrg rwlpdlvagk
      121 nvyavaideg pkhrperiac kaeksgngfk lsgkkdfvvy gasaemivva artsgsdsdt
      181 dgitlfavpq dasgmshdsv rlvdssmash itfdgvdldg davigevdgg revlnamlra
      241 grvgaaaegv gvargamdmt vdylkqrkqf gtligtfqal qhraahlyse veiaravvlk
      301 aaqlvdgese kaelmtsvak akvakaagla vregvqmhgg igmtdeydig lymkreralq
      361 eflgdmyyha grvaelsgy
//
LOCUS       WP_010408701             640 aa            linear   BCT 01-JAN-2025
DEFINITION  M1 family metallopeptidase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010408701
VERSION     WP_010408701.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Evnouchidou,I., Koumantou,D., Nugue,M. and Saveanu,L.
  TITLE     M1-aminopeptidase family - beyond antigen-trimming activities
  JOURNAL   Curr Opin Immunol 83, 102337 (2023)
   PUBMED   37216842
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Peer,W.A.
  TITLE     The role of multifunctional M1 metallopeptidases in cell cycle
            progression
  JOURNAL   Ann Bot 107 (7), 1171-1181 (2011)
   PUBMED   21258033
REFERENCE   4  (residues 1 to 640)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   5  (residues 1 to 640)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..640
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=70123
     Region          45..482
                     /region_name="M1_LTA4H"
                     /note="Peptidase M1 family including Leukotriene A4
                     hydrolase catalytic domain; cd09599"
                     /db_xref="CDD:341062"
     Site            order(169,171..172,301..305,326,329..330,333,348,352,359,
                     416)
                     /site_type="active"
                     /db_xref="CDD:341062"
     Region          523..634
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
ORIGIN      
        1 mriaaaalal sftatacttp daasqsasmt qpmvspiltt aqafddqtya qpqvarvthv
       61 dldldldfeg qqvggkatld vlaapgakei vldsnglqia svtdgagrrl sysvgamsdd
      121 ggkgapltiq ldgaelivid yraapnaaal qwlmpeqtag geypylfsqg qailnrtwip
      181 tqdspgirqt wearitapkp ldvvmsgvrq gepedlgngr rafrfvmdkp vppyliaiaa
      241 gdidfraigp rsgvwaepvm ldrawrevnd teqlieaaee lygdyrwgry dmivlppafp
      301 yggmenpvmt fltptfiagd ksnngliahe lahswsgnla tysswrdgwl negvtsyfen
      361 riteqvygeq raeqeyalsy aslvegieea gadspttamr spdsispfet egvaiydkgt
      421 vflrtvenmv grdrfdawlt qwfdnhafep vtsemfladl rekligndaq learlmldew
      481 vygtglpsna lkpdpqtfaa vdnavaayaa dgtlptantw tgwtaaeqrr flermpeert
      541 deqlaaldar lglseagnne vlflwleaal rnqydpavpq aerflsqvgr nkfvsplfta
      601 lsesdwgkpi arriyaetrd syhsytrgrv datlgmtage
//
LOCUS       WP_010408724             140 aa            linear   BCT 01-JAN-2025
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010408724
VERSION     WP_010408724.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..140
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15579
     Region          18..138
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mtdyakplpk vtdesapfwe gcraqelriq rcdscarfrf ppqkmcrhcn sveftwapvs
       61 gkgtvysftv ptntspgelp argfdypyav alvelegtdg vriasnivdc pvdeiaidmp
      121 vevtfdqvtd eitlpkfrrv
//
LOCUS       WP_010408762             134 aa            linear   BCT 01-JAN-2025
DEFINITION  RidA family protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010408762
VERSION     WP_010408762.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..134
                     /product="RidA family protein"
                     /calculated_mol_wt=14064
     Region          1..134
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mpnkpinpgq lynavefgfs havesrgqrt lhlagqvawd pecnvvgadd laaqtrqala
       61 nlkavlaeag agpehvvrlr tyivdhkpek lgvvlpeiga fydgatpaan tligvaalam
      121 peflieieat avld
//
LOCUS       WP_010408771             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Citromicrobium].
ACCESSION   WP_010408771
VERSION     WP_010408771.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..308
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33143
     Region          9..304
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mdkrsivewr gyipaittpf aadgaidfgg latlldwlhg egmhglvvag ttgewtsmsd
       61 aercsvfaav gdqlsgklpl lagcsaftae rviamateah kagfsgilvt pppyicpsst
      121 eisnfyrsva kgsplpvciy nwppgtgidc eldllerltd idniiavkqs tsrldrfvat
      181 ffalrekvlv fghamdehgl allearggdg tmgaggvlgr yqpdfynhlw ageiekarqc
      241 grmdrvlmke wytpdlvgkf gsgpailkaa ldarglpggh vraplldice edrekvrrtl
      301 delgclsv
//
LOCUS       WP_010408774             391 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: zinc-dependent alcohol dehydrogenase [Sphingomonas].
ACCESSION   WP_010408774
VERSION     WP_010408774.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..391
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41469
     Region          1..389
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,169,173,192..193,195..197,216..218,222,
                     236,260..262,291,308..310,333..335,375)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,169)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mralcwhgkg dvrvdtvadp eikhprdaii kitacaicgs dlhlldgyqp tmeagdilgh
       61 enmgevvalg sevtnlkigd rvvvpftisc gdcwfckkgl faacdrtnpn admaakamgh
      121 spaglfgfsh mlggycggqa eylrvpmadv gpikipdnvt deqalflsdi fptgymaaen
      181 aqiehgdtva iwgcgpvgqf airsalmmga grviaidevp erlamaeagg aetinfaetd
      241 vydelqartk grgpdscida vgceaaahga adavmdkvka smmlatdrvh vlrqaimscr
      301 kggtvsvpgv yvgmgdklpi gaamnkglti klgqthvqry trpllekiva gaidpsfvit
      361 hpasledape myakfrdkee gvikvvmrph g
//
LOCUS       WP_010408932             379 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010408932
VERSION     WP_010408932.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..379
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40669
     Region          1..>44
                     /region_name="DUF5930"
                     /note="Family of unknown function (DUF5930); pfam19353"
                     /db_xref="CDD:466052"
     Region          158..348
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mehwfperef fmrsqgqvrf ikissglqkr taalaltasv afvgsmgvms vlqyqssler
       61 aalmereasv ataeerlday qadigavthd lekrqdfiee mmkvmpadai qhgsseeget
      121 selvqkvsaa vpeaealari earqiafveg ltnyadlrsq qamwalrelg ldpqkmlasa
      181 eqgarggple tvfadgeidp rferlglslt rlaalestla gvpqikptda paanssyglr
      241 rdpftgraam hkgldfpgam gapiyatarg kvtfvgrrgg ygnvveishg qglltryahm
      301 srfeaqvgdr veagavigai gstgrstgph lhfevrvngt avnprtflel apdvlkkarr
      361 npgpsstrta gntqgdagv
//
LOCUS       WP_010408968             199 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma carbonic anhydrase family protein [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010408968
VERSION     WP_010408968.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..199
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20393
     Region          18..192
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 msdtitgdta hgrpgvrlip ihgkaprihe tafiapgtvi vgdvtigags siwyncvlra
       61 dvssitiger tnvqdgsvlh cdgpspqypd gcplvigddv lighmamvhg ctihdrgfvg
      121 lgaiamnkav igsdamlaag amltetkqmg arelwggrpa rkmrdlddaa iagmqlgvah
      181 yaenakhhaa aiagsgnga
//
LOCUS       WP_010408943             339 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010408943
VERSION     WP_010408943.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..339
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35477
     Region          1..324
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(41..42,123,127,130,148,151..153,172..173,177,192,
                     216..217,238..239,241,263..265,313,318)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mratgyaetg gpevlglred aavprpgage vllkvayagv nrpdciqrag hyppppgasp
       61 ilgleasgei vavgegvdvs wlgeqvcalt pggayaeycv vpeghmlpvp dvltmaeaaa
      121 lpetlftvwh nvfqrgmard gemllvhggt sgigtmaiml akafglgviv tagseekcda
      181 aravgadhai dykttdfvea vglitggdgv dvvldmvsgd yvsrnlkclk pdgrhvtiav
      241 lgglkaqinm alvmskrlvl tgstlrprsd afktalrdei areawplved gtirpvmdei
      301 faladadkah armengdhig kivlaidedl srsglssdr
//
LOCUS       WP_010409003             326 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010409003
VERSION     WP_010409003.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..326
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35313
     Region          58..321
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mstkpvpaea tpdrskrklg rglgallget qreesiapse ggttlgtgtg ganepgpsta
       61 sglasipvar ieplpgqprk ifeedaleel aksiarrgvi qpiivrpler kgryqlvage
      121 rrwraaqran lheipaivrd ldrrevmaia lieniqredl npieearayq hlseeeemsq
      181 adiaelvdks rshvanlqrl lalpepviql velgklsmgh aralighdra eelaqeavsk
      241 nlsvrevekk vrakpagkks aaaggngapq qtnadieave rhleeflgms lsikpdadpr
      301 sgaitirykt ldqldllcqr ltggei
//
LOCUS       WP_010409174             275 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Sphingomonas echinoides].
ACCESSION   WP_010409174
VERSION     WP_010409174.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10084616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..275
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=29709
     Region          154..274
                     /region_name="USP-like"
                     /note="universal stress protein (USP) and similar
                     proteins; cd00293"
                     /db_xref="CDD:467483"
ORIGIN      
        1 mikdllavid dadraqsfln svvtlsqshd avlevaaltp apmampamap fgelyvpewv
       61 lmgddaanve rtrshlaaag stadvfglhn evgwlagdlk rsrqvadliv lgaretwttp
      121 wlrrrvaetl irasgtplll lpegqnlapv rkailgwkpg peatramhvl ahlaqpgati
      181 dvitvgttlg scekekdsha evkrhltrhg faaeghwivn derieadtlt lyaqetqadl
      241 lviggfahsr irdiilggtt rdlierqdlp vlivg
//
LOCUS       WP_010409195             216 aa            linear   BCT 01-JAN-2025
DEFINITION  BON domain-containing protein [Sphingomonas echinoides].
ACCESSION   WP_010409195
VERSION     WP_010409195.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..216
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=23139
     Region          2..144
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
     Region          152..213
                     /region_name="BON"
                     /note="BON domain; pfam04972"
                     /db_xref="CDD:428229"
ORIGIN      
        1 mrtdqeiqgd vqaelaweps vahehigvsv qagvvtlsgl vssyaeklaa ekavrrvagv
       61 kaiaedvevr rpgdarttdt eiaericslf awdavipeek itvkvengrv tlggtvdwry
      121 evdaarkaag riggvtsvvd lisirqvpvt hdvkerieqa fkrnavldas sisviadggt
      181 itlggkvhaw rereiaeraa wsapgvtaih dnifva
//
LOCUS       WP_010409203             268 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Sphingomonas echinoides].
ACCESSION   WP_010409203
VERSION     WP_010409203.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10084616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..268
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=29222
     Region          1..>108
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          148..265
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mknilllihd degqearyqa aldvtralgg hltcvdltii pevmgdyvdm gtgvllaeeq
       61 adetrnavrm rarleredvp fdwsettgfl srtleersrl adlivlstdm dgeifprmtd
      121 vigellvgtg kpvlaippna kplaldgrvm vawdgsedae aalaaavpll traktvvlyy
      181 addrsmgapi edaarylsrh giepvikkdp lgidrvssal lceaemghhd lvvmggyghs
      241 rtletifgga trsmlrkskv plllvhhr
//
LOCUS       WP_010409302             278 aa            linear   BCT 01-JAN-2025
DEFINITION  pirin family protein [Pseudomonas syringae].
ACCESSION   WP_010409302
VERSION     WP_010409302.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..278
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29540
     Region          30..234
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mnsivsirpr aivhrttgrt rgpitrlvsp gdlgqllkpf vfldricfts epgktgfgmh
       61 phsgiatlty miegelayed ttgksgvlls ggvewmsagn gvwhdaqpvn gsavrgfqlw
      121 valpaaqens paqsvylsaa qvaqqgpvnv llgrygsaks slpapegmny lavqlkdgeh
      181 wrytppaghs vgwlavntgq ldagspvgag elvifeesdr pidivakgdt hfvlgsavkh
      241 phdlvtgyys vhtskaaliq geleieriga llreegrl
//
LOCUS       WP_010409472              99 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira inadai].
ACCESSION   WP_010409472
VERSION     WP_010409472.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..99
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11263
     Region          21..>89
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 mklktkdfnl llnkelknkd fkkeydafsn eftlakeiik lrkkrnltqk dlaekigtsq
       61 paiariesgn yrnlslsfin rlakaldaep vihlksksa
//
LOCUS       WP_010409477             123 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Leptospira inadai].
ACCESSION   WP_010409477
VERSION     WP_010409477.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..123
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13845
     Region          61..123
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mlavvktplt evtvkgeist tflkalkkef gkklliekse esvpwkdtif fkenkeflqp
       61 gsklkyyrkq aglslselge klggiprqnl samelgkrpi srdlakqlsk lfkkpvevfl
      121 yae
//
LOCUS       WP_010409483              98 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Leptospira inadai].
ACCESSION   WP_010409483
VERSION     WP_010409483.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..98
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10810
     Region          3..93
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mafvrigkfk akqervveic ltyekeaipm irkaegnisa allqektapd sflaisvwqt
       61 eedavayers glaqemvnki rsdfaapptl itynafgi
//
LOCUS       WP_010409496             268 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010409496
VERSION     WP_010409496.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..268
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=28715
     Region          4..247
                     /region_name="SDR_a4"
                     /note="atypical (a) SDRs, subgroup 4; cd05266"
                     /db_xref="CDD:187576"
     Site            order(8,10..12,57..59,85..87,111,117,134..137)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187576"
ORIGIN      
        1 maklfifglg ysakriarea qslgwevvat gsdgklsfad egevraelal adavlssvpp
       61 drettsdpvl erygdalsqd wlgylsstgv ygdrqgawvd eatptiaqgg egrrnaraqa
      121 drawleqgar vfrlpgiygp grsifdriea gkahridmpg qvfsrvhvdd iasgavaalt
      181 anvppgaynl gddlpasqna vveeacallg vepppllsle eadlspmarg fyaenrrvan
      241 gkakrllgwq pkyptyregl rallpprp
//
LOCUS       WP_010409511             289 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome c1 [Citromicrobium sp. JLT1363].
ACCESSION   WP_010409511
VERSION     WP_010409511.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10490041
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..289
                     /product="cytochrome c1"
                     /EC_number="7.1.1.8"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31744
     Region          52..284
                     /region_name="Cytochrom_C1"
                     /note="Cytochrome C1 family; pfam02167"
                     /db_xref="CDD:426633"
ORIGIN      
        1 mirilaalag lvfagvalls fgfgayafft eeplhsaehe fhlqahgpes gfsfdgplgt
       61 wdiaqlqrgy kvykevcsac hslnyvafrd ladldyseeq vkaeaaswqv pgidpntgea
      121 ttrpgtdtdy fpspypnkva aaaannnavp pdlslmtkar hhgtdyvysl ltgytdpvtf
      181 endgkrlmee fpdyatpegl yfnpyfanln lamappltsa gqvtfddgke atisqmskdv
      241 aafltwtaep klierkqtgw pvlvfllfat vlayfakrqi wssvkpkkd
//
LOCUS       WP_010409520             216 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010409520
VERSION     WP_010409520.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..216
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22648
     Region          62..173
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(69..70,103..104,107,111..112,115,163,167)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mrgpmmmlal gallagcngd epapapeptp tpvatedgae qasiirpeme verppialep
       61 lratipfgdg gsdlsemala elnamletdq wqqvervilr ghsdaggpdr vnmrvseera
      121 qavadwlmeq gldeeairvi pfgaqnpvqp nllpngepne rgraanrrve vtllvpegat
      181 ipdpgptvtp epegppsspa sgappkprat ggsitq
//
LOCUS       WP_010409594             189 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Leptospira inadai].
ACCESSION   WP_010409594
VERSION     WP_010409594.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..189
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21096
     Region          2..184
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrriivsefl tldgvmedpg gaekskyggw shrffneefg nykfdelfsc dalllgrlty
       61 qgfaaawpsm tdergfserm ngipkfvvst tltnadwnns tlikenvvas vrklkeqpgk
      121 dilvtgsgvl artllqndli delrlmihpi lvgggrklfd eaprralelv esrkletgvg
      181 iltyrpvkn
//
LOCUS       WP_010409599             193 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Citromicrobium
            sp. JLT1363].
ACCESSION   WP_010409599
VERSION     WP_010409599.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..193
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21091
     Region          1..>137
                     /region_name="COG3576"
                     /note="Predicted flavin-nucleotide-binding protein,
                     pyridoxine 5'-phosphate oxidase superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442796"
ORIGIN      
        1 madffdtltd khiamiakqp vffvataapd arinlspkgy nafrvlapdr vayldlagsg
       61 nethahlvad anenggritl mfcnfdrpal ilriygrgra vlpqdagwed laqhftllpg
      121 trqifdiave svqtscgwgv pfmayeaerp tlkkahaqsd pvqweakmae rttsidglpt
      181 rptdryiage dag
//
LOCUS       WP_010409603             530 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010409603
VERSION     WP_010409603.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..530
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57426
     Region          1..526
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mkqydyivig ggsagcavtg rlavggtrsv clveaggrnn tmriktpgmm pflgsrpnyl
       61 yetvpqkgln grighqprgk glggssaina mvyirgnawd ydnwaamgcd gwsfadvlpw
      121 frkseanerg esnyhgaggp lfvsdqkwpn easrafvqsa aalqltetdd fnderqagfg
      181 ifqvtqrdge rwsasrayve pirnqdnldi rtntlverli veggrvtgva irqgrrseki
      241 yarrgvilsa gafnspqilm lsgigpgrhl nalgvpvlld rpavgsnlqd hidyvscwes
      301 esrvpigrsa egtlrmarav lehrrsrsgp mttpyaeagg fwtvsadapa pdvqwhfvpa
      361 mledhgrekl sghgvslhac vlrpesrgtv rlasreasda paidpnfldd erdiavlreg
      421 vrlshriaea ppladygltd rhpidlsdda aldalirara dtvyhpvgtc rmgsdedavv
      481 dpklkargld glwiadasim pkivsgntna psimigerca dfvieaekat
//
LOCUS       WP_010409787             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Leptospira].
ACCESSION   WP_010409787
VERSION     WP_010409787.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..204
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22052
     Region          31..199
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mnfeilvevg esaifiimii asiiavavav ergivffknt kdsknllpei vqtirngdis
       61 kaakftevhp envyarfasf saehsksgke sleelmegka igervefetr lsilntlgnn
      121 apfigllgtv fgvinafyrl gtlgntgaev vmrsistall ataaglavai pvvmannyft
      181 rklkiiqsnl dilskeflan lsrk
//
LOCUS       WP_010409832             267 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Leptospira inadai].
ACCESSION   WP_010409832
VERSION     WP_010409832.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..267
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29234
     Region          3..217
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mkilitgasg glgkklaeds fargheiflt dinekalnaf askwkgeknr vitskldiss
       61 aadwkkvmdl lykkwerldi lmnvagyllp gyiyetqpkd idrhidinsk glmygtreas
      121 lrmidqgggh iiniaslagv apisgltlys askfavrgfs laaaeelrpk nvfvttvcpd
      181 aiktpmldlq kdyesasltf sgnryltvee vsdiifrnvi pkkplevlvp gsrgflaklg
      241 gffpflglll gpalrskgmr kqatytv
//
LOCUS       WP_010409945             434 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Leptospira inadai].
ACCESSION   WP_010409945
VERSION     WP_010409945.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..434
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48053
     Region          14..399
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mplnkktkkk vvvigagfgg lqaikklskh edlditvidk knhhlfqpll yqvatavlsp
       61 adiaiptrsl vgneenvtvy lgevdrvdlk erkvyfqdhs edydflilaa gartsyfgnd
      121 hwkkyttglk slkdaleirt klllsferae leedkeiaks llnyviiggg ptgvelagsi
      181 aelsheivrn efhtidpals kitlieaspr llmafhpnls gfaknrlekr gvevlvgtkv
      241 inideegvhl egrtircsni iwaagvqana isqalgvpld rtgrvivdef cnieghpevf
      301 vigdianftk nserplpgvs pvamqqgryv aslilgdlkg kkrsafkyvd kgsmatigrq
      361 davaqvgpwr mkgffgwaaw lfvhlfyqvg fknkvsilit wfwsyltfra earliqdevg
      421 sggipnptak ekrs
//
LOCUS       WP_010409960             233 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Leptospira inadai].
ACCESSION   WP_010409960
VERSION     WP_010409960.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..233
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26131
     Region          24..>173
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makraefagm dlltafgged ssrkeipiqd ilpnpeqprv fgkeevgdlt esmrrlgmie
       61 pivvrkigkk fqivagerry qaakalgwks maavetdase drcyemalae nekrkslnpw
      121 evgraiqylr kekkktadev akllgytery vkqlssiarl dqksvadllr sgkdasvknl
      181 esllkrkegr ggetisprkt iekvtldlks lpsktrdsfl rdlavlkkky gls
//
LOCUS       WP_010409998             397 aa            linear   BCT 01-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010409998
VERSION     WP_010409998.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..397
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42578
     Region          1..389
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,85,170,174,193..194,196..198,217..219,223,
                     237,261..263,291,308..310,333..335,375)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,170)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(89..90,92,95,103)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mraltwhgth dvrvdtvddp eiinsrdaii evtstaicgs dlhlydgvip gvlpgdvlgh
       61 efmgrvvetg sdstlekgqr vvvpftiscg gcfhcqiqqf sacensnpae kqdmsaklyg
      121 hsmaalfgys hmtggysggq aeyvrvpysd vgpivipdhl dddkvlflsd ilptgwmaae
      181 naeiqpddtv avwgcgpvgl faiqsaivmg askviaidhy pnrlalakql gaevidfrkt
      241 nvrealmems ggigvdavid avgmeshgfa idnivdvvkq kvgmgadras alkqailavr
      301 pggrvsipgv yggitdkfpl galmekglqi rsgqthvqry tkdllekied gtldttflis
      361 hrlpledaac gyecfrteqd swtkvvlkpg mdmpaan
//
LOCUS       WP_010410010             314 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010410010
VERSION     WP_010410010.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..314
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34022
     Region          21..293
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 msnhhthggh gghnhgeenl sdrqlifava invlltlaqi vggivsgsla liadalhnfs
       61 daaslglawf arrigrrpad rrmtfgyaqg evvaalinlt tlliigfyll veainrfadp
      121 qpiegwtvia vagvalvidl vtafithrga kdsinmkaaf lhnvsdamas vgvivagili
      181 llydlyvadl vitviiaayv iwqglslmpr tvrllmgavp ddvelreimd eleaidgves
      241 ihhlhvwnlg ehrralevhi vpsspslerf edlkrtvrqh vssrfnieha tleaclaadc
      301 degliaqagh sgrf
//
LOCUS       WP_010410113             243 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010410113
VERSION     WP_010410113.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..243
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26226
     Region          1..241
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mavvavysvk ggvgkttfaa nlawcaatqs srrtllwdld aaggagfllg vdprkkkrat
       61 sviskeldpa klirktgypr ldllpadesi raldvqlaei gkknriarlt adlvkdydrl
      121 vldcppvlne lssqivraad lvivpippsp lsaralemvq eeveaagkka ppimpvfsmv
      181 drrrtlhrea vanhpdwpvi paasaieqca sqqapvgafa prspalrafk klwtdverrl
      241 akg
//
LOCUS       WP_010410162             226 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Citromicrobium].
ACCESSION   WP_010410162
VERSION     WP_010410162.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..226
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25261
     Region          2..82
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(13,15..16,18..19,22..23,75,78..79)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(13,56..58,73..74)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(56,72..73,75..76,79)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          107..209
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(109..110,113..114,175,178)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mkliignkny sswslrgwla ckqaglsfee ilvplfgedw dalkkgegdl tpssgkvpvl
       61 wdgdddagav vwdslailey ladkvgrdrf wpkddaaram aramvaemhs sylslrrecp
      121 mnirvrhenv kiseatrqdv vrilglwaea rarfgsggpf lfgtfgaadi fyapvvsrfi
      181 tygfgvpgfa esymqavwth dwlqqwvaaa edeqwvieqy esvpts
//
LOCUS       WP_010410236             147 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Leptospira
            inadai].
ACCESSION   WP_010410236
VERSION     WP_010410236.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..147
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16728
     Region          12..141
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mnlrfdyaka ypaalqamls leeftksggi dsnlreliki rasqingcaf clhmhtkdar
       61 sageeekriy llnawrespy ytekeraale iteyvtkisq eglpdrvyen arayfdekef
      121 valimlinti nswnriaitt gkqapvv
//
LOCUS       WP_010410346             598 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Pseudomonas].
ACCESSION   WP_010410346
VERSION     WP_010410346.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..598
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=65728
     Region          <1..426
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mqtlkalyes vekqffntlt kklsslfllv lvsallywva lnirsdimlq lrgtqtdpaa
       61 lgviqsqldl lsnaillstl ftlvmvsfmv wyfrhlivrp vmsmtralee vasgegdlsk
      121 dlpllthdei rglastcnlf lakqreiiss iqgltvqiav esarslknis dssdsatdqa
      181 rfarevmdqs nmavgsiedv sqqtqgisst taqnlsmard syaellevtg nisqisssln
      241 efgglvsgln ersssiksiv gliqqissqt nllalnaaie aaragesgrg favvadevrt
      301 laqnvskatd disrnidaml qevsstheqt iqishsaret qlvverasgh fesmigdfes
      361 tndkladiaa hiqqfastnt ginervtriy sdsqaidqrm qhsatatrdl ssvaeqvqal
      421 lgrfvlghge ldaaitrasq crdilqarlv elhkqgvnlf dqsyklipgt dpkqyttgyt
      481 erfaqicqee cdkltkgtrg gkvtfivdsk gycpvnnswv sqkptgnrev dlpvcrnkrm
      541 fsdpiglraa gnkqrfllqt ylrdtgeimt eidvpfffeg rhwgnlrmgf daalllgk
//
LOCUS       WP_010410352             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Citromicrobium].
ACCESSION   WP_010410352
VERSION     WP_010410352.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..146
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16437
     Region          1..130
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 meylhtmirv sdlddsldff cnklglvevr rvdveagrft lvflsapgde traradqapl
       61 veltynwdpe eydggrnfgh layrvddiya acqrlmdkgv tinrpprdgh mafvrspdgi
      121 siellqkges lpakepwasm entgtw
//
LOCUS       WP_010410395             195 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Leptospira inadai].
ACCESSION   WP_010410395
VERSION     WP_010410395.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..195
                     /product="YceI family protein"
                     /calculated_mol_wt=21105
     Region          1..195
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mnkknilfal llsafsfsgt eaenfkldns htsvgfkvrh laisnvpgtf reysgkfafd
       61 ektnsvtgle vtiqsasist sdadrdkhlk gkdffdasnf atisfkaika vikkggvskv
      121 dgeltikgit kpvvlevkyv gsakdpwgnt hlafeaetki nrkdfgltwn ktletggvlv
      181 geevsirieg eavpe
//
LOCUS       WP_010410407             230 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010410407
VERSION     WP_010410407.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..230
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24488
     Region          <58..216
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 mcaaalvsas qtatglvrql sqavselpaq gddpavdvrf vtsrgwptrh pmltpnrdlt
       61 elerariaqa iadipgvggv hwtdgtmlaa gdtdieslrc esdlldvlae rtirfeessa
      121 efipgseell delatvlrpc vgaivaisgh tdtsgspqvn lalsqdraqm vrreliergi
      181 paqnlratgy gssrpvsgid padpanrrie frvvsteitk ptpidtpaar
//
LOCUS       WP_010410427             444 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010410427
VERSION     WP_010410427.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..444
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=50644
     Region          <278..404
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mewrgfqfwk eefwswrhpr rfrfriwarv rwlkfrqwlr epkfralrrh wprpaiiilt
       61 aalvawvvft ffgnqsggll mkldrllsye tvkmnwreat qlllvlvglp iafllwlfrd
      121 ihtnavlenq rkdvnlkefq eiqmraagam deklpasare tsqiaathql agflrgeygv
      181 sfqrpawell rarllasser mgyrailaqi edwrradpge rqsakqlggn vrkaakqitq
      241 dntgksqrda vrdewrtifs srlplpdtvf dgialppgal latcdlsrcs figvhlwdah
      301 legaelwgah legsslgnah legaslrgah legaflgnah lkcaslfaah leganlfaah
      361 legadlgrah legadlryah legadladph lddkteldra ifddrtrfaf dwsgltkdek
      421 drarapwier glihvndrna ndpk
//
LOCUS       WP_010410643             251 aa            linear   BCT 01-JAN-2025
DEFINITION  siderophore-interacting protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010410643
VERSION     WP_010410643.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..251
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=26947
     Region          1..236
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 msqrpeprql tvlrrdritp slqrvtlggp glagfpadqe ggylklflge aengkpiirt
       61 ytirhqrdge ldidfalhgg eaagpatkws ltaepgspit vggpgaakpl psghdfylia
      121 gdmtalpais vnlaalppga rgvaaieiqn eadkldldkp dgveirwlvn repgsqpdll
      181 vdalrnvelp egqlaawaac efssmrnlra flrddlglrg eslyissywk agliedehkl
      241 akredaeaqa a
//
LOCUS       WP_010410797             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Citromicrobium].
ACCESSION   WP_010410797
VERSION     WP_010410797.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..300
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31954
     Region          15..290
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 mktisnttka afvcgiaala lpaslsaqeq wgeastetta entltvtgti padiselpeg
       61 peidgfisaq gedriqitse dgsqtvvfvg dateiksrgg flglgrttld deqlfngvpv
      121 svrtvqwaqg liaqrismke sdlktaamiq rgteqgfaeq taatealrgr vadidnynvk
      181 gttnvyfdtg eytlsgqaqa elcsaaaqad qmdnalllvv gytdstgsye inqelsekra
      241 ervvnylqqq cgwkpyrmlt ptgmaqadpv adnstdygkq qnrrvavnil vskavdgmgg
//
LOCUS       WP_010410813              86 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Leptospira inadai].
ACCESSION   WP_010410813
VERSION     WP_010410813.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..86
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9749
     Region          30..83
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 meneellewe ennstrfsrd taswkpgivv rilrkihgys rkdlaeklgg veveyvtsie
       61 kgkltigknl arklaeifqi saeifv
//
LOCUS       WP_010410842             235 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Leptospira inadai].
ACCESSION   WP_010410842
VERSION     WP_010410842.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..235
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26833
     Region          23..232
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 masdlayqvt eerspfsaiw stfpacskdl yesflhprfg krtfkfpkks ilfnegkptt
       61 gfylilqgtv rtfkdspngq rqqtlkiysp eswvglrdai sedyynktae cledtvsvyi
      121 dkeemkkafs qdlafqtait kyiatecraa enriysmgtr qvhsklaefl lslkekygse
      181 invkfsrevm atmigsktet lvraltdlkg kgwieidknm isirneeall klmet
//
LOCUS       WP_010410892             173 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Leptospira
            inadai].
ACCESSION   WP_010410892
VERSION     WP_010410892.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..173
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=19539
     Region          <3..173
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mrilffdird fthssekmsp kdnfdfsnsy trrmgpfirk nkgfvdkylg dgimalfpns
       61 pddalqaame mlkelanlnl swkerkyepi pigiglhtgt rmlgeigeee rmygtaisda
      121 vnlasriegl skelyatill segkykklhd kkkysfnklg kvtvkgksks sqv
//
LOCUS       WP_010410933             563 aa            linear   BCT 01-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010410933
VERSION     WP_010410933.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..563
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=61965
     Region          55..562
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 myltpearia dyeskgwwrg itvdellket lagdhaelav idpsnreald gvapgrltwe
       61 efderidrla asfhqlglrk ddrivaqlpn tidamltlfa sarlglilsp vvmqyrkhel
      121 ghvfekvepa afvtipsfhd fdqaalgtql ckahgaqllm fgdapdgats lddamqdadr
      181 dalaryraen pvsagevfti cwtsgtesqp kgvprnhnhw vlngdvmvea tamksgdtil
      241 npfplvnigs igglmmpwlr cggtvvlhhp fdvgvfltql qqekvsytia ppavlgallk
      301 qpellekfdl salrtvgsgs aplspwlieg wkdrygieia nifgsnegas lfsnlqsvpd
      361 pveraryfpr fgardadwdg mtatimdsrl vdpateeeit epgkvgelrl ggamifdgyw
      421 rapemnataf dsegyyrtgd lfeiagpgnr fyqfqgrske iimrggvnis paelddlivg
      481 qpqikeaatv gvpderlger iavavvpheg eepkledita wleardiaif krpeflvivd
      541 alprnamnkv vrdelremvv akl
//
LOCUS       WP_010410680             140 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Leptospira inadai].
ACCESSION   WP_010410680
VERSION     WP_010410680.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14436104
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..140
                     /product="response regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=15935
     Region          18..131
                     /region_name="REC_hyHK_CKI1_RcsC-like"
                     /note="phosphoacceptor receiver (REC) domain of hybrid
                     sensor histidine kinases/response regulators similar to
                     Arabidopsis thaliana CKI1 and Escherichia coli RcsC;
                     cd17546"
                     /db_xref="CDD:381099"
     Site            order(24,26..27,29..30,33..34,37,99,121,123..124)
                     /site_type="other"
                     /note="Hpt domain binding site [polypeptide binding]"
                     /db_xref="CDD:381099"
ORIGIN      
        1 mnptqgngtp ttirtlrilv aeddhinqvi akrmfqksgy eveivnnglg vlnairrsky
       61 diiyldlimp elggfetarr lreefkksae spwivaltai sladeleeyl esgmnsfisk
      121 pykfedirds indyferksv
//
LOCUS       WP_010411075             194 aa            linear   BCT 01-JAN-2025
DEFINITION  SCO family protein [Leptospira inadai].
ACCESSION   WP_010411075
VERSION     WP_010411075.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..194
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22345
     Region          57..171
                     /region_name="SCO"
                     /note="SCO (an acronym for Synthesis of Cytochrome c
                     Oxidase) family; composed of proteins similar to Sco1, a
                     membrane-anchored protein possessing a soluble domain with
                     a TRX fold. Members of this family are required for the
                     proper assembly of cytochrome c...; cd02968"
                     /db_xref="CDD:239266"
     Site            order(71,75,153)
                     /site_type="other"
                     /note="Cu(I) binding site [ion binding]"
                     /db_xref="CDD:239266"
ORIGIN      
        1 mkmelwkitv agtaiilalf yflsvmpkrm levdrtvpsf plmlagetaa tdirdiligk
       61 enlvyfgyln cksvchgtla klkstltgre dlrlvfisld pkndsqkrfr eyfreaakqs
      121 vlirmesteq afelarrfgi rafpseqsdd idhsdsalwi nskgrikgff gefnrwwnle
      181 sedefirtir nsqd
//
LOCUS       WP_010411252             243 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010411252
VERSION     WP_010411252.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..243
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25865
     Region          1..241
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mlvarklrld erlrgvdtqv rsgqvtaicg pngagkstli rlfagvlsps ngevlldger
       61 tadihprvra ralgylpqep qiawdmsvrn lvslgrlahg dthaepveaa lqamdlhdfa
      121 rrpvstlsgg erarallarv lageprfila depfasldlg yqsalarhlr aqaadhgrgv
      181 vvvvhdlsla hnladrvill negvvhaega padalspgnl ldvfgiearw lgdpgaqvla
      241 vrk
//
LOCUS       WP_010411353             282 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Leptospira inadai].
ACCESSION   WP_010411353
VERSION     WP_010411353.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..282
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31724
     Region          7..256
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 msnwsflksd lsdqdllidc rsqaqyqeat lkgayyfpfv kkafasdpes fkkmlgplde
       61 ilalakkegk srivvfdegm gmfaarltll lrsagfvhty vldkrwpvee gtekgsreld
      121 fgpaskirkl egiidkafle knltrlqifd trtpeeyegk lprltapepg slcgrlpgaf
      181 lwdwrmlydp tgdlvdktff nkklrgfpfm perttviydy ngarssllal mlkevgyndv
      241 nvyigswfew rksslpkqav niygqaggag aaprvggaer kn
//
LOCUS       WP_010411436             132 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Pseudomonas].
ACCESSION   WP_010411436
VERSION     WP_010411436.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 132)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..132
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14262
     Region          3..117
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mkqratvick rdgqvlyvrk pksrwalpgg kieagetpfq aavrelceet gladldllyl
       61 dvyekdqvah yvftaqvpas sepspqneia ackwlapqkl gdlkassatk tivksyates
      121 egvpgtrshv tg
//
LOCUS       WP_010411553             447 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Leptospira inadai].
ACCESSION   WP_010411553
VERSION     WP_010411553.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..447
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=50543
     Region          10..442
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mdnieptgvi tierlgrnlr gsgklggksv eipyslvgdv yrvfkfgkrk ffykwqadsl
       61 ekrdvvpkca hfgqcggcsg qhleyakqfe lkfepirqgl lergienfsv qpaveqyhyr
      121 nrmdfavfpd kivglrmagn frkiilldnc eiqsdwanee lsrikiflse fpgieydrkk
      181 eigflkyvtl rksvftddsm tiftftedfk enpllekvaa aakrisigkn lvfcfnrkkg
      241 eisasgeslv vrgkdslvdi vldhsflipf dgffqpnpke flhildfvkr rlagkktlid
      301 lfcgsgffsl lfgrefpnll gidvipssva aglsvlqref pdkksemlsv dlfhkkglek
      361 leatgllqsd svliadpprs glspelcall nrsrvgqffy vscnpeklle dlrilsesye
      421 iedllicdpf phtphleava llipkns
//
LOCUS       WP_010411611             398 aa            linear   BCT 01-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010411611
VERSION     WP_010411611.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20165749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..398
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=43435
     Region          29..>85
                     /region_name="HslR"
                     /note="Ribosomal 50S subunit-recycling heat shock protein,
                     contains S4 domain [Translation, ribosomal structure and
                     biogenesis]; COG1188"
                     /db_xref="CDD:440801"
     Region          118..325
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 madnnptpdq tptraperge vrqytvgadd ddirldrwfk rhlpqvgfat varwartgqi
       61 rvdgarakpd drlktgqtlr ippgnpaktk apprrrelta deraqahamv iketktaial
      121 nkppglatqg gsktyshvdg lldafvegde prprlvhrld kdtsgvllia rtpgsaaafs
      181 krfsgrsakk vywalvvgvp eqhvgeidap lakqpgtgge kmhvdmeggq paktryrvve
      241 ragnkaawle lepltgrthq lrvhlaaigh pilgdgkygg qdafltgsvs rkmhlharrl
      301 iisqpgggql dvtadlpehf astmehmgfd lslsdaeplr ddpgpkskae kkqdakqhak
      361 qyrkarrger rsrtvskpaa kkkarakgkp kgkpggkr
//
LOCUS       WP_010411645             326 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Leptospira
            inadai].
ACCESSION   WP_010411645
VERSION     WP_010411645.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..326
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=37104
     Region          <14..269
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mstsqnpskp aseisrlrse lrdlrilykn tiehatllen eledkrwkie rllqnmqkyl
       61 pmklyervtd gelsissgyq rkkltvffsd lvgfteltds vepeviascl ncymndmsrl
      121 avkyggkidk figdammiff eesdsdsgka yalncihmal emqkrlrlir lawkefgise
      181 svqvrigint gfctmgnfgs dirmdytiig ntvnvaarle qlarpgsili svstyelikd
      241 efrarslgkv qikgihvpve ifeligtren kispylekng dtfklkeiim plkspisdqe
      301 alsimealee trdtiekslr gwaqie
//
LOCUS       WP_010411802             692 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S9 family peptidase [Citromicrobium].
ACCESSION   WP_010411802
VERSION     WP_010411802.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..692
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=74582
     Region          <55..148
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          <111..>266
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          397..657
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mfdrqklsla lgcataalal aavpsiaqtp tatdtsmtat spatsaplip realfgnpsr
       61 asaqispdge wlswlapsng vlnvwmapas npddakvmts aterpireyf wapdsaslly
      121 vqdkggdenf llyginietg kettltpfen trvqlvgasd tikdkvlvgl nnrdprfhdv
      181 hlldlntgel tqlienngya gfvaddnldv rlalrpnaag gmdffrvedn vvaeeafsst
      241 dledalttsp agftrdgetl ywldsrgrdt aalvamdwdt aetrviaend kadiggtird
      301 netgeveays vyylkrewta tdpeieaalt flennlegef gigsrtdddr kwivgndpvt
      361 gpsasylfdr dagtltklyv trpelegapl qpmhpveias rdgltlpsyl tlppgsdsda
      421 dgvpdapvpm vllvhggpwa rdgygynsyh qwlanrgyav lstnfrgstg fgknfisagn
      481 lewgrkmhdd lidavnwave rgvtsqdsva imggsyggya tlaglaftpe efacgvdivg
      541 psnletllst ippywepvva qfhermgnpn teeglallke rsplysadki tkplligqga
      601 ndprvnqaes dqivaamkqn eipvtyvlfp deghgfarpv nniafnaite nflatcldgr
      661 aepmgdtvea staeivegad fvqglaeavs ae
//
LOCUS       WP_010411837             413 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FtsW/RodA/SpoVE family cell cycle protein
            [Citromicrobium].
ACCESSION   WP_010411837
VERSION     WP_010411837.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..413
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=44661
     Region          21..372
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mniapataia telpgrgsqk mtlrarlkiw wreldhvllg livllmavgc aaiaaaspag
       61 anrlssdtvt ldplfflwah lrwlalgitv mlglsmlnre tarrfaills lamvgalllv
      121 pfigsevnga rrwldvgftf qpseflkpgf avtlawimsw rlkdpqmpvf glvtgalgfv
      181 ivllmvqpnl gaailfsgvw fvlvvlggvs frniaglivg gflglslaya fydnarhrid
      241 swlsggtdfd qvdlaqrtll aggwdgvgfw vgtqkmrlpe aqtdyifsvv geefgllacg
      301 givllflaiv wrvlsrvsse enffallaaa gltaqiggqa finilvnlsl fpskgmtlpl
      361 vsyggsstia vclslgllla ltrrnpfltr etaglrktlf ekdrglfgke rdr
//
LOCUS       WP_010411914             282 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010411914
VERSION     WP_010411914.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..282
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30152
     Region          10..277
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mdmlvstdwl vaeldapdla vldaslhlpa aqrdaraefe dghipgahfm dlaglhdpas
       61 ampgkvpdga riarwlgdrg igpqtrivly ddsmlrsaar awvlldlagi anvavldggl
      121 akwkeqdrpl dsgmpspspa drpptairlt dirdkaamla nvqsgaeqvv dardaarftg
      181 seedsvhdlp gghipaarhl ffrdllredg tfrdtdalra lfaqaqidie qpvvttcgsg
      241 itasvllfgl rlvgaprtal ydgswsewga dpdtpketgd pr
//
LOCUS       WP_010411682             174 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Leptospira inadai].
ACCESSION   WP_010411682
VERSION     WP_010411682.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..174
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20640
     Region          1..169
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdiheieery fqlrpdvfrf ivsqtydpel aedvlqetim eilrifrkgv eiregtfrsf
       61 lytiaytqvk nhrrkaarqp vtyfesdsfi eakphekdqs sliyksvqva lsdpkipert
      121 revlrlrlie elsikeimri ldisrqtfyr dlrigmkilq etlsekgitp eslk
//
LOCUS       WP_010411939             366 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Leptospira inadai].
ACCESSION   WP_010411939
VERSION     WP_010411939.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..366
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39938
     Region          94..363
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mrfslppvvv vnaglavlli lililpgegg lssffrgdkp ldygeqkagi elqnafrnvy
       61 rlakdsvvsi rtkksdlivs pyhyfdyrne rlasfgsgfl ihekgyiatn fhviegaesi
      121 evitsdgsvf pakfvgsher adisllkire gsglkpvrfg nsddievgdw aiaigspfgl
      181 ersfsvgvvs akyredldet gqthiqidsm inpgssggpl lniygevigi nrlirsdtgr
      241 ntgigfaipm nyakkiiqli qenkgriirp atlgvmatvp ladhrkalgi pddwtgvlvy
      301 dieagssaes sglkrydfll eanglpvkni ndlreqvgiv glggrlklri yrekslqelv
      361 vrlvqk
//
LOCUS       WP_010411990             162 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Fur family transcriptional regulator [Leptospira].
ACCESSION   WP_010411990
VERSION     WP_010411990.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..162
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18811
     Region          19..158
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mnkdkeaeil ktvdesvrme mktfsdylqk kglkitnqrm lvaerifslh nhftaeslle
       61 efkdqrdkis katiyrilsi mveakllqeh nfgqdykyye hiighthhdh iicvdcgriv
      121 efvderieql qeqaalgngf kitghslniy gscldpncpr kk
//
LOCUS       WP_010411966             358 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Leptospira inadai].
ACCESSION   WP_010411966
VERSION     WP_010411966.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..358
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40991
     Region          131..356
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          262..349
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 miseitnilh yfclsnlifl iglfawryhy dlririaagf sfgiicyiil sldpnmlipl
       61 pirvglfggl lslpfffwil ssaifvdnfh pklwhwsilv gkilisallv ypvldeinmr
      121 gpiesetvla hiivptllsl afvlaailqt ysgrkddlie trrrlrevhi lvtgsvitfs
      181 ifshlilrgk alseildlln vvlawglila fmhlvlelkd glvdpepdge ieeeerviqa
      241 dpalkrklvl afeeeklyrk egltigqlae dlevqeyklr rlinqamgfr nfpdflnryr
      301 iqeaceilld sgkdefpiir iamdlgyqsl gpfnrafkel tgvtptefrk nrerqpqv
//
LOCUS       WP_010412070             341 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HEAT repeat domain-containing protein
            [Citromicrobium].
ACCESSION   WP_010412070
VERSION     WP_010412070.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..341
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=37727
     Region          188..317
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          199..226
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          229..258
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          292..317
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mkifssglye tvvlgsaama gvvvviflll vlrrhlaerq vdankridaa itrsylrrva
       61 ghrpetddtg wtderrlaav sqiqallrgg erdrlmqiae ldgllaatvr rsrrwrrser
      121 vnairllqrf gselciarlr elmardrspl vrveaafala aahalpppre tmrilrmtdr
      181 apsrldsall rasvpdyreq fvllleddlp pvwraqlida lgwsgdvavi pvlekaagde
      241 dpevrgaalr aaaklghpga rewimaalrd pdanvrvqav kasealglrd avpqirdlre
      301 dsqlwvrlra eqalealdpg ydttarppla pnpapdlsnc a
//
LOCUS       WP_010412173             624 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Citromicrobium].
ACCESSION   WP_010412173
VERSION     WP_010412173.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..624
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67419
     Region          4..515
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mltidgvtvr lggrpilera satvpvgarv gligrngagk stlmkalige iepddgevtk
       61 psrsrigyia qeapsgdltp eevvlasate raalleelet ctdmdrmgdv hdrllaiday
      121 saparaakil nglgfdeemq qrpvdsfsgg wkmrialgal lfsepdilll depsnhldle
      181 atlwlenflk sypatlvvis herdllnkvv dhilhlqggq ltlypggyda fekqraeraa
      241 qlaaakasqd aqrarlqdyv arnsarasta kqaqsrakml akmqpiaalm edpslsfdfp
      301 dpeemkspmi tleqaavgyg eappilkrln frieaddria llgrngngkt tlarllasql
      361 daaegdvnap grlkvgyftq yqveelaged tpldlmnram egaaqsavra qlgrfgfsgp
      421 raqqrvdkls ggerarlala litrdaphll ildeptnhld vdarealiqa indysgavil
      481 ishdrhmvel tadrlilvdg gtareyagsm qdyidlvlgr nqprkergds apkvrgsraa
      541 nsegkarfak selskaekav erltadvarl dgliversgq qtgqdsasam qdllrkrada
      601 adslaeaeea wlaagaalee ieqg
//
LOCUS       WP_010412197             183 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Leptospira].
ACCESSION   WP_010412197
VERSION     WP_010412197.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..183
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21483
     Region          1..128
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 makdtrdlil ktslrlfseq gyhgttmrqi aqraglslgl ayryfeskes ilvgiiqshd
       61 kilkkylpen ltspddrkel ieflagqiik lvkeneeylr lywnlmlqpk ihrlkrrnih
      121 lvnlifyens kkvilalkpn ytefevknls sstigyminy ltnrkefsle dfrayivyal
      181 ent
//
LOCUS       WP_010412217             207 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010412217
VERSION     WP_010412217.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..207
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22623
     Region          7..191
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 msdrlgliep ddalrrqmlg elgdagfhae pfeglreflq yrsrgdyavl vndetvdvla
       61 vreslcregd wlaviaycpa pnlrrivavm rgggydyfsl pldtatlars lsqlrqaksp
      121 faaarqraaq ariklaalsp reaevlanma egrsnktigi dlgisprtve ihranmlskl
      181 gvhsstealr mfyehalleg eaavpge
//
LOCUS       WP_010412222             354 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein
            [Citromicrobium].
ACCESSION   WP_010412222
VERSION     WP_010412222.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..354
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38161
     Region          4..351
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mavlndeqem lrdmarewtk nehpvdawrk vrdagqpfda dawgamaemg wagiiipeeh
       61 ggsdfgwlsl glvieelgks laasplvasa laasaivlgg seeqkaeflp rlaageligt
      121 lafdegprht glnastsvhd grltgtkafv heasraglfv vlaqdgvylv ekgkgisvsk
      181 rmladmrdha eidfndapaq klaaggddla qkildrarvl taaemlgmcq avfdttldyl
      241 kqrvqfnqvl ssfqalqhrm adlyteielt rsaveaglqa idsgfavsea atlakarand
      301 tlhlvskegi qlhggigmtd eysvgfylkr arvleaawgs sshlrdayar mksy
//
LOCUS       WP_010412228              97 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010412228
VERSION     WP_010412228.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 97)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..97
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10279
     Region          11..95
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mstitinrvg ndtkglyvaq vegfdevgel tfsrasptlv ivdhtgvpds lrgkgvgaal
       61 aekvvadara egfrivplcp ffkaqaqrhp dwadvvq
//
LOCUS       WP_010412262             241 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SIMPL domain-containing protein [Citromicrobium].
ACCESSION   WP_010412262
VERSION     WP_010412262.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..241
                     /product="SIMPL domain-containing protein"
                     /note="The SIMPL domain is named for its presence in mouse
                     protein SIMPL (signalling molecule that associates with
                     mouse pelle-like kinase). Bacterial member BP26, from
                     Brucella, was shown to assemble into a channel-like
                     structure, while YggE from E. coli has been associated
                     with resistance to oxidative stress.; The SIMPL domain is
                     named for its presence in mouse protein SIMPL (signalling
                     molecule that associates with mouse pelle-like kinase).
                     Bacterial member BP26, from Brucella, was shown to
                     assemble into a channel-like structure, while YggE from E.
                     coli has been associated with resistance to oxidative
                     stress."
                     /calculated_mol_wt=25747
     Region          27..238
                     /region_name="YggE"
                     /note="Uncharacterized conserved protein YggE, contains
                     kinase-interacting SIMPL domain [Function unknown];
                     COG2968"
                     /db_xref="CDD:442208"
ORIGIN      
        1 mirtaivpta ialaalatap asaadiqvqa tgpvielvvn eqvevepdtv tisagvttqa
       61 mtasdalrqn stqmqsvidr lrslgiperd iqttrinlna rfdydqqtrd qvfrgyeasn
      121 qvsvklrdte evgnvldalv qaganningp rfsvsddtqp kaearrrale rarsmamdya
      181 rvagysnvrv lkiaesvqgn areyaadaim vtaqrsagap pvqpgmvetg vtvsvtyeav
      241 n
//
LOCUS       WP_010412271             134 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Leptospira].
ACCESSION   WP_010412271
VERSION     WP_010412271.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..134
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14934
     Region          1..130
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mkstvrenls fgsspdnpdg lqlkitfded tktaygdytv pekfqgspdv ihpgiiatil
       61 deimakinea mnfktttgel tirflqpaqi nqplhlrgwf vkknkkvien raeieneigk
      121 ivargkgkyi elds
//
LOCUS       WP_010412276             299 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Leptospira inadai].
ACCESSION   WP_010412276
VERSION     WP_010412276.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..299
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=32954
     Region          42..288
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mkikifllll llltypahta sakekkqigk swflsasdal slerqgaivv daregfkfts
       61 ysgsiplvwk eisrkdpprr gyllteseai eilngkglrk gniilvfadp tsgwgeegri
      121 vwsfrtlgfl hayiidggiq alrkareskh lsdskietft anpagppvdl avdsgfvksh
      181 lsdkkfifld sreerefaga tpygesrggh lpgarslyyk nllnsdgyll seselrrkfs
      241 svgiesektv vsyctggirs awlvavlvsl gyeaknyags mrewssldpn kfplvkgpn
//
LOCUS       WP_010412356             323 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Leptospira inadai].
ACCESSION   WP_010412356
VERSION     WP_010412356.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..323
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37792
     Region          132..297
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mdlnfsniys allspiriif lpsvkiywly llssviitaf filwqkirvk dfnvgnylsk
       61 ilsreywlhk salidykyyf lntilfsfyy gyfvlsgatv safvnnglvr lfgvlayeip
      121 fdssvlivly silfwlmndf grflahwllh knsffwefhr lhhsaevlnp ltvyrvhpve
      181 ailvnslgaf fsgivtgvam fafpmtitmi sffgvnvgif ifnlyanlrh sniaihfpkw
      241 lshiflspaq hqihhsvdvr lqnknigvtf afwdlflgsl yipdrhetee itfglqdakq
      301 edfenffsiy flpfkrifdi lkr
//
LOCUS       WP_010412386             234 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010412386
VERSION     WP_010412386.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..234
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24366
     Region          <97..203
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
ORIGIN      
        1 migtwiavgg lalvalgaal lvaresrrvw tlfatalvfa lagyawqgap dlagsphqav
       61 rdvsptsdal idarrrfynv egilpsrfvv tadgfsrrgq hqdaagllrn avseqpddge
      121 awlalalala ehtrgtitpp vayafqrare tspanvapgy fqgllalrtg alaeardlwa
      181 dalagapeda rgrdfvaqql erldgvigvl gdrasqagpq ggpmmpppgg apap
//
LOCUS       WP_010412407              56 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CsbD family protein [Citromicrobium].
ACCESSION   WP_010412407
VERSION     WP_010412407.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..56
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..56
                     /product="CsbD family protein"
                     /calculated_mol_wt=5752
     Region          7..56
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mgelkskveg nvneaigeak qksndpetra egrgqeakgk aqqtkgevqg algddi
//
LOCUS       WP_010412424             306 aa            linear   BCT 01-JAN-2025
DEFINITION  hydrogen peroxide-inducible genes activator [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010412424
VERSION     WP_010412424.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Jo,I., Chung,I.Y., Bae,H.W., Kim,J.S., Song,S., Cho,Y.H. and
            Ha,N.C.
  TITLE     Structural details of the OxyR peroxide-sensing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 112 (20), 6443-6448 (2015)
   PUBMED   25931525
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..306
                     /product="hydrogen peroxide-inducible genes activator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33722
     Region          8..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..295
                     /region_name="PBP2_OxyR"
                     /note="The C-terminal substrate-binding domain of the
                     LysR-type transcriptional regulator OxyR, a member of the
                     type 2 periplasmic binding fold protein superfamily;
                     cd08411"
                     /db_xref="CDD:176103"
     Site            order(108,111..112,115,119,127..131,224,227..228,231,
                     234..235,237..238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176103"
ORIGIN      
        1 mstylptirq lqylvalheh ghfgraadas fvsqstlsag ireletlldv tlversrrvv
       61 rftplghqvv ekahallrqa edlsdlvraa gqpltgtlrm sviptiapfl lprllprlrk
      121 drpelelflr eetssdaves lhhgrvdcvl lalpfstgev eqaligkdrf fvaypgdepr
      181 dlpeeirpet iedgrlllle dghclkehal aacnrpelra atsmigtslh tlvqmvdngl
      241 gvtmlpemal eagilkgtkv iarpldapaa trdialiwrk nspreadfll ladelragqa
      301 qirrga
//
LOCUS       WP_010412578             211 aa            linear   BCT 01-JAN-2025
DEFINITION  leucine-rich repeat domain-containing protein [Leptospira inadai].
ACCESSION   WP_010412578
VERSION     WP_010412578.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..211
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23634
     Region          <37..>187
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          61..83
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          84..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          129..154
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 mirllvlpil sglllfgnsc krsaedilsv asqtplkvek ldiglqklgt fpqvlftfpn
       61 lkwldirlnr letlpenlgd lqqleylnvy gndlkrlpas caklgklhvl fagnndferi
      121 ppelkglslk aiyldqnkli lnesdidllg nlqqlqildl sknrnivafp knlnlladhp
      181 klrvlilkds glrtadvnaa rkllpkvrie f
//
LOCUS       WP_010412615             470 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Leptospira inadai].
ACCESSION   WP_010412615
VERSION     WP_010412615.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..470
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=51956
     Region          29..463
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mrsdfrydpe tvrrilssps kvaflkesei lsittssgmc esdslfvplr gnrdghdfip
       61 dalskgatyf lceyehpile klseadreka ifvkdtligl gklaafhrsr fkpiviavtg
      121 ssgktttkei lgsclsplee slvvternyn neigvpftlf rigpktryvi cemgmntkde
      181 isrlssmakp qlsiittigt ahieffrsrk giakakaevm dgmpksgivf ypatgeykrv
      241 lskkarksgv kftlvpltsr iktletlreg frleifstal nwnlpgskll enlslciaal
      301 eeigtpedwi legirnfktk dkrldlqegt yrilndtyna nresmlssle acsqlsgteg
      361 fyailgdmke vgsysskfha evgkfaasls nckgiftfgs gshfifkgfq skakppqiaa
      421 sfsgdeeglh slleevkknv qpgsyilaka srgmklervv ealnsnskmd
//
LOCUS       WP_010412641             665 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Leptospira inadai].
ACCESSION   WP_010412641
VERSION     WP_010412641.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12036995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..665
                     /product="methyl-accepting chemotaxis protein"
                     /calculated_mol_wt=71510
     Region          35..263
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          170..665
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkhqslifil laysisiiav lvltisgval gvgkdqiekt yftqmrsvsq saaseienfy
       61 dthlriaeil aedprtketi rtgkpiaqal ykevlqkfga yenvfvttme kdplvitdal
      121 gkgtglrlgv reqnvpnika avegkfhlgk plrspvtklp vslltvpvmd agkvvgivaf
      181 alsleslsek viknykigqq gylaatttdg ilyahpkkdm ilnldvaket tygkkllala
      241 sgemmefefr gqeryatlfr lknwdtlafv ilpkdeiwss fkgllltila vsvltaiial
      301 silyfllkrr lgplrdaslv fqsmaqgdlt tnveaaynde igtmsremnt figslrsslh
      361 diqrialelg aaaeqltgss qafasgaqst aasseemsat ieemsagmes issitetqyk
      421 nilafhskik elsagvrkig seiqgtlgaa ksisaqarkg eeslngmsgm ignilkssge
      481 mtaiigiind isdqtqllal naaieaarag eagkgfavva eeisklsvkt assiksigdm
      541 inknnseldi gakgirssve iihsiiqsvd svadamnhly eitsaqegin rivddqadkv
      601 gseaesvkla tgeqkravre iaqvitqine htlntasgse qmsasaqnla ttaetlrsit
      661 dkfki
//
LOCUS       WP_010412683             417 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Alphaproteobacteria].
ACCESSION   WP_010412683
VERSION     WP_010412683.1
KEYWORDS    RefSeq.
SOURCE      Alphaproteobacteria (a-proteobacteria)
  ORGANISM  Alphaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Alphaproteobacteria"
                     /db_xref="taxon:28211"
     Protein         1..417
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44691
     Region          32..411
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mfaiiwrgal faglslavlp gavraqerav ltldealara gvdesaqvqs dnprligpqa
       61 etdaaralid qarlrpnpel afeaeniags gafsglqate ytlslsqrle lggkrgarir
      121 saeaearvam lsgelsvael srmvreryie avasaarlel ardvvernre lariagllve
      181 vgrepplrsl raeaalaeae aefeaarase iaarsalval wgetspppdv psafpgiepp
      241 amllaspsal rlqvaraere aadaaidrer slgvpdpais agvrrfeesr dqaflvgvsi
      301 plpfrnrnqg niaaaearfr aasareavar adfelevtqa rgrflaaear vetlsqtslp
      361 qaeealrlvr igyrngrfpl ievlaaaear dairealiqa qedrgrlaaq liwlgaq
//
LOCUS       WP_010412754             234 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [Sphingomonadales].
ACCESSION   WP_010412754
VERSION     WP_010412754.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonadales
  ORGANISM  Sphingomonadales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Sphingomonadales"
                     /db_xref="taxon:204457"
     Protein         1..234
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25215
     Region          7..214
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mtdtrpiavf gaggktgtel lrhalardip irafehtvpg pdervgdfey iecdvlsddf
       61 agdldgcrav istlgvafgp gnaidppply tdgtrnllga maqtkidria visaafvehq
      121 ssvpawfelt akpalfnile qmrameamls daqgikwtaa rpgwlldepy tgdavitder
      181 laegcfrcrh adlaasllef vcedtwinak paigrpeaer fespaaikae lgid
//
LOCUS       WP_010412733             776 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase
            [Sphingomonadales].
ACCESSION   WP_010412733
VERSION     WP_010412733.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonadales
  ORGANISM  Sphingomonadales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17596983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Sphingomonadales"
                     /db_xref="taxon:204457"
     Protein         1..776
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81399
     Region          9..60
                     /region_name="YHS"
                     /note="Heavy metal-bindng TRASH/YHS domain, predicted
                     Cu/Ag metallochaperone [Inorganic ion transport and
                     metabolism]; COG3350"
                     /db_xref="CDD:442578"
     Region          73..99
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          116..771
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(419,421,726)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(463..465,528,544..546,575,615..617,637,640,643,662,
                     665)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(727,755,759)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mskdqsvieg taidpvcgms vaidgaqhia thegathyfc sprchdkfvt dpelylsgah
       61 ldavedvpeg tiytcpmhpe irqpgpgscp icgmalepet vslgdgpdpe lvdmlrrfww
      121 salltlplfv yamsdmapgl sfdrliepaw aqwaqfalat pvvlwgawpf fvraiqslkt
      181 rnlnmftlig fgvaiaylfs vvatvapdlf paafrdhsgr vgvyfeaaav ittlvllgqv
      241 lelkargsts salrallela ppsavkifgs gderevpldq lttgdrlrvr pgdkvpvdge
      301 ieegssaide smisgeplpv akqagdivig gtvnqtggfv mratgvgkdt mlskivqmva
      361 daqrsrapiq rladqvagwf vpavvviaia tfvvwaiwgp apalayalvn aiavliiacp
      421 calglatpms imtgtgkgaq hgilirnaea letlekidtl vvdktgtlti gkpdlvavkp
      481 adgidetefl aavagvemgs ehplahaive gakargvspa natdlasttg egveanvqgg
      541 rvaignekmm rrvgiddeaw lgsaengrkq gqtvmfvafd grpagliava dpikptsaaa
      601 iaalhkrdir vvmltgdsrg taeavaremg idevhanvsp edkhrkieel kaqgrrvgma
      661 gdgindapal aaadvgiamg tgtdvaiesa gvtlvrgdlt gvvqatvlsr gtmrnirqnl
      721 ffafayntlg ipvaagvlfp ffgvllspmi aaaamslssv svignalrlr glsfar
//
LOCUS       WP_010412776             152 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Leptospira inadai].
ACCESSION   WP_010412776
VERSION     WP_010412776.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..152
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16527
     Region          10..120
                     /region_name="Glyoxalase_4"
                     /note="Glyoxalase/Bleomycin resistance protein/Dioxygenase
                     superfamily; pfam13669"
                     /db_xref="CDD:463951"
ORIGIN      
        1 mrpfkilgiq qvavggdskd klknfwvdil glestgtyrs ekenvnedil rmgkgpyave
       61 vdimepvdps kspkvndpkl nhiglwvddi hkavewltsk gvrftpggir kgagghdvtf
      121 ihpkgneefp lcgegvliel vqaptdvika lg
//
LOCUS       WP_010412832             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Citromicrobium].
ACCESSION   WP_010412832
VERSION     WP_010412832.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..158
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=17626
     Region          1..148
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mnnalsdrva dllvklgalg llattaiigw qvfgryvlqs spswteqasl llmiwyvfla
       61 aaagvwerfh irieilelrf nednrrrlri gihalvavmg lvllvygvml awdvrvhvip
      121 slgisraway vvipfaglli slfslarirv rmsergan
//
LOCUS       WP_010412906             403 aa            linear   BCT 01-JAN-2025
DEFINITION  saccharopine dehydrogenase family protein [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010412906
VERSION     WP_010412906.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..403
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44732
     Region          28..396
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mskvlvigag gvssvcvhkm amnkdifsei hlasrtkskc daiaasvkdr tgvdvatyei
       61 daeevpamin lirkigpslv vnlalpyqdl pimdacleag vdyldtanye pkdeakfeyh
      121 wqwayhdrfk ekgltallgs gfdpgvtsvf tmwlkkhklk tirqldildc nggdhgqafa
      181 tnfnpeinir evtaparhwe ngewvetpam qvktefdfee vgpknaymmy heeleslakf
      241 vpelerarfw mtfgdeyikh ltvlqavgmt siepvkyqgr diiplqflaa vlpkpeslge
      301 ttkgktnigv iatgealdgs gektfyinni csheaayeet gnqavsyttg vpamigsamm
      361 lqgkwdgegv fnmeqfdpdp fmdmlnqhgl pwnvkeldgp vgf
//
LOCUS       WP_010412978             510 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Citromicrobium sp. JLT1363].
ACCESSION   WP_010412978
VERSION     WP_010412978.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..510
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55748
     Region          1..508
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 msaniaemek rreaarmggg qkridaqhak gkltarerld vlldegsfee ldtyvvhdct
       61 dfgmedqqim gdgvvtgsgt ingrlvyvfs qdftvfggsl skrhaekick vmdtamkvga
      121 pviglndsgg ariqegvasl ggyaevfqrn vlasgvipqi svimgpcagg avyspamtdf
      181 ifmvkdssym fvtgpdvvkt vtnevvtqee lggavthttk tsvaddafen dietlmatrr
      241 ffdflplsnr epvpdmpssd pwdrredsld tlipdnanqp ydmheviskt lddgdffevq
      301 pkhaaniicg fgrvegrtvg vvanqpmvla gvldinsskk aarfvrfcda fdipivtfvd
      361 vpgflpgtsq elggiikhga kllfayaeat vpkitvitrk ayggaydvma skhlrgdlny
      421 awptaeiavm gakgaveiif rqdrddpeki aektkeyedr fanpfvaasr gyideviyph
      481 strrrialgl rklrgkelsn pwkkhdnipl
//
LOCUS       WP_010413030             107 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF1476 domain-containing protein [Sphingomonadales].
ACCESSION   WP_010413030
VERSION     WP_010413030.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonadales
  ORGANISM  Sphingomonadales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Sphingomonadales"
                     /db_xref="taxon:204457"
     Protein         1..107
                     /product="DUF1476 domain-containing protein"
                     /calculated_mol_wt=11827
     Region          1..106
                     /region_name="COG5467"
                     /note="Uncharacterized conserved protein, DUF1476 domain
                     [Function unknown]"
                     /db_xref="CDD:444218"
ORIGIN      
        1 mtdfndrrrg eeakyamdee tafkvaarrn rllgewaadl mnlteeetds yrkavvqadf
       61 eeagdedvir kvlgdltaas cdvdeaavra klaecevear rqligga
//
LOCUS       WP_010413092             323 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010413092
VERSION     WP_010413092.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..323
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34239
     Region          92..295
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 madapnsqas tepfvradvr glldmlkamn rppaeevgaq aareamrama qigeaaprel
       61 avikdvacpg pagdipcrfy daresreagp avlflhgggf vlgdlevyha lctefaarld
      121 lpvlsvdyrl apenpfpaap ddceaaarwl asspaelgre itglvisgds aggnltivtt
      181 nalrdepadv pvlvqapiyp vadeagqyds yrqfkdgyfl tgdtmawftk syaadpqspr
      241 nlpllgdcsn apatvlctag ldplrdsgrn yaacmvkqgt eitylefpgi ihgfftmrka
      301 ipsgqadvea fidavgaavg rrt
//
LOCUS       WP_010412400             391 aa            linear   BCT 01-JAN-2025
DEFINITION  MiaB/RimO family radical SAM methylthiotransferase [Citromicrobium
            sp. JLT1363].
ACCESSION   WP_010412400
VERSION     WP_010412400.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Wang,S.C. and Frey,P.A.
  TITLE     S-adenosylmethionine as an oxidant: the radical SAM superfamily
  JOURNAL   Trends Biochem Sci 32 (3), 101-110 (2007)
   PUBMED   17291766
  REMARK    Erratum:[Trends Biochem Sci. 2007 May;32(5):209]
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Layer,G., Heinz,D.W., Jahn,D. and Schubert,W.D.
  TITLE     Structure and function of radical SAM enzymes
  JOURNAL   Curr Opin Chem Biol 8 (5), 468-476 (2004)
   PUBMED   15450488
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..391
                     /product="MiaB/RimO family radical SAM
                     methylthiotransferase"
                     /EC_number="2.8.4.-"
                     /GO_function="GO:0035596 - methylthiotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42501
     Region          6..385
                     /region_name="MiaB"
                     /note="tRNA A37 methylthiotransferase MiaB [Translation,
                     ribosomal structure and biogenesis]; COG0621"
                     /db_xref="CDD:440386"
ORIGIN      
        1 msaervislg crlnhaeser iaalvererd lvvvnscsvt reavrhtrqa irrarkanpq
       61 arllvtgcaa etdreglanm aevdgfvang akldarswnv peppvalrqq gtrafigvqn
      121 gcdhactfcs ipqgrgasrs dsiadvlrav dtrlaegake ivltgvdlts wghdlpgepg
      181 lgtlvaailr efpqlprlrl ssvdgieide alfnliatep rvmphlhlsl qhgsdlilkr
      241 mkrrhsrtqa idlvarlkqq rpeiaigadl iagfpteada hhadnlsiia ecgivhghvf
      301 pyspregtpa armpqiepat ikrraaelrs avrqtrdiwl etlvgaeyev laekdgsgyt
      361 phfarvalpe gtvpgqlvti rptriiegml a
//
LOCUS       WP_010413218             325 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010413218
VERSION     WP_010413218.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..325
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35204
     Region          13..293
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mrsgaasdra ilgrsaafas ivtalflvgl klwavwqtes mallgslads aldliaslat
       61 ltgviiaarp adrthrfghg kaealaaifq vmlialsaag iamqsaeala egqrvaaaqe
      121 givvsmiail atfallayqr fviartgsla istdhlhyqs dlllnlavia alvldryvgl
      181 agadplfglg iagwllwgaw ragseaidhl mdrewpeekr rrfvavaarh pelsrlhdlr
      241 trtsggidfv qfhvdlpgdy tveqahdiie rvekdlhaef pdaevlihid peghvdeprn
      301 tlveedqfsr fgerrmtgph detpt
//
LOCUS       WP_010413223            1036 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Leptospira inadai].
ACCESSION   WP_010413223
VERSION     WP_010413223.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..1036
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115881
     Region          4..1028
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mraiiesfik nrlffylgts fvflagivsl lglrrdtfpn vdmkqlvitt kfpgaapadv
       61 elrvtypiee kikeidgide irsfsrnsas didvrvslee kdpekildei rravdnaise
      121 fppqvtekpk iierksssyp vlefsvfggk deielhttae flerelekis gvarvdvfgk
      181 rdrewqilvn anrlkqyqld lsdittairn rnvnlpagsv dsetafdlri dgefrnpsdi
      241 ykipirtndl fskvelgsla rvedtfeypr flaiangkqg lilsvvkker adaidvadhv
      301 rkrlaelkkt appeiktvtl sdeakrtskr ldivsnnali gfcivfgilf lfldfrtati
      361 tslslpisml mtfavlpffd vsfnmismmg liialgmlvd nsiviseniy tylgknmdsf
      421 tasvkgtlem lvpifgsylt tvaaflpmlf msgimgkfvw qiplvvival tasliesflf
      481 lparitafak tpdqlkrttg frktldaffh rmeerfsdfv aftlhhkyss fviililila
      541 sfvalsrmkf ilfpkediei ftvkaefpss friyqtrekm kymetiiqsi ppdelvsysi
      601 kigvqqtdpe dplsrygenl gvilvyltpe serkrkagei laslesdfrk tpslvdvyme
      661 efgaappiga pitvsilgkd ykdltkvsge lqtflktipg vhsvrddyry grkqlqvrld
      721 eglesftgvs tfaaanmlrt aydgeragtv rkgrtkiylr vvydkdfrkn pdeikhiplr
      781 nkagnithls kiskmelvds pellshrefe raitvnaeik idqitahean skiievfkpl
      841 ierqypgvsl vfggeekdtq rsmeslgkag llalfgifai laltmqnfwk pflilstipl
      901 gimgivlgfp lsgksisfla migiiglagv lvnasivlvd cidsiqkgss dsmdeillea
      961 srrrfrpill ttlttvagil ptayglggtd pvlvpmtlal gwglgfgtfg sllyvpvtls
     1021 vfhrfaskqs rrktgh
//
LOCUS       WP_010413240             498 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Leptospira inadai].
ACCESSION   WP_010413240
VERSION     WP_010413240.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..498
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56008
     Region          4..490
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mikisnlqkt ynsktlfedl nlslnrgekl glvgrnghgk stlfqmilgs vepdsgtitv
       61 pkgykighlq qhlkftkptv leecalglpe geeyetwqve kvlsglgfse admerhpdef
      121 sggyqirmnl akllvsgpdl lmldepnnyl divtirwlee flrewegeii lvthdrsfmd
      181 svvshtaaih rskaikvqgd tdklynqinq aeeiyertrl neakkrkqee ifiarfkaka
      241 sfasraqsrv krlekqgemk aleaiqdlel yfnsapfaan qmlsvedlsf sytgkepyli
      301 edfslsvgkr driciigkng kgkstllkll agelsptrgk vqkhptlkeg yfgqtnklnl
      361 nenatvveei mnadkscsew lartiagglm fsddealkki kvlsggeksr vllgkilvtp
      421 cnllyldept nhldmqscds lieaidefdg svimvthnem hlkavatkli vfdnntirtf
      481 dgsyedflsd vgwadedy
//
LOCUS       WP_010413269             397 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010413269
VERSION     WP_010413269.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..397
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=41859
     Region          5..394
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 msdpvtriaa kgdglteggq hvaggvpgdv laadgtlvrg phhvdppcrh fpqcggcqlq
       61 haddaalaqf vshrvsfaae sqglvpgtla pphlspprtr rratlhaarl gkklvigfre
      121 ggshrivdmt echilhprlf alvdplrkll aswggklaad iqltlvdtgi aaeikgisae
      181 nlaqtealld farehslarl svdegfgpep vwepepatvt lggtpvafph gaflqptadg
      241 eaallsaare wcsghgivad lfaglgtfaf alagpakvla aeadrgahla cqaaarasgk
      301 pvhalhrdlf rdpltadeis kfgcvlldpp ragarnqvda iaqstasrva yiscnpqswa
      361 rdarrladag frlaelrpvg qfrwsthvel aslflrd
//
LOCUS       WP_010413333             830 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [Citromicrobium].
ACCESSION   WP_010413333
VERSION     WP_010413333.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..830
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91326
     Region          32..799
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mteinvehir yrlqrgssda faefrqtwrd nwavrwivyg taallvlfai awfligrdlp
       61 naaalqdyet plptvvrgnd geivgsyard rrvqldfvdf prplinafla aedetfwshn
      121 gvditgtana vidyarkagt deravggsti tqqvaknvll sdeysitrkl remlvarrie
      181 qtlskqeilt lylneiplgr rsfgvqaaar ayfgkdvgdl dlhemaflai lpkaperygr
      241 eryedmaitr rnyvldkmae newaseaava aakaeplglt sgatsirnad agyfieevrr
      301 qlldrfgeta ddgpnsvyag glwvrssvdl elqdaartal rrgmqryhgn rgwsgpvatl
      361 dpdngdltsq lasaniginy ddwrvavftg sgtigfsdge tatlngapns lragdvlavr
      421 psgnawrvav ipdasggivv edpqtgrila mqggwdsrle sfnratqakr qpgstvkpfv
      481 yatgldqglt pasqvdnssf cayqgarygr kcirggragt ytlryglens qnvmtanian
      541 eagmanvikt yervgigsyd pyisfalgag ettvekmtna fstlanhgry ndptvidyvq
      601 drrgkviwra dkrecaecnk peydgaampr pgplgrqmmd artafqishi legvitrgta
      661 kvlrgtglpl fgktgtttgp kdvwfvggtq qmmvgtylgf dqprnmggya qggtiaapiv
      721 ktfieetrdr wratppvapa gvrmvridrr tggrvfdqwp gtdenaaiiw eafkpdtepp
      781 rstraseiaa qrqelldlir rarraqaegq ravereeppe dfveeqggiy
//
LOCUS       WP_010413044             399 aa            linear   BCT 01-JAN-2025
DEFINITION  NHL repeat-containing protein [Leptospira inadai].
ACCESSION   WP_010413044
VERSION     WP_010413044.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chaudhuri,I., Soding,J. and Lupas,A.N.
  TITLE     Evolution of the beta-propeller fold
  JOURNAL   Proteins 71 (2), 795-803 (2008)
   PUBMED   17979191
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10146633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..399
                     /product="NHL repeat-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=40306
     Region          71..398
                     /region_name="NHL"
                     /note="NHL repeat unit of beta-propeller proteins;
                     cd05819"
                     /db_xref="CDD:271320"
     Region          80..130
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          138..188
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          196..245
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          252..305
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          314..355
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          364..398
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
ORIGIN      
        1 mnqfkprsvi lvaltislsc kpkhnnngal liallaasak qsnctttpvl tlgesatlvl
       61 gqssfttsas gttqnqlkqp sgiavdsrgg ewvsdatnnr vlhfpngvas ggnadivlgq
      121 snftassagt tqstlttpqg lavdsngglw vvdsgnhrvl hfpsgvatgg nadlvlgqan
      181 ytngtaattq srlssphava vdstggiwvs dggnnralhf psgivsggna dlvlgqsnyt
      241 tgtggvtaqn alndprglav dsnggiwiae yannrvlhfp sgvssggnad rvlgqtnyts
      301 sagqftrtqi slyqpqgiav dssggiwvgd agnvrvlhya sgvangggad kvlgqsdytt
      361 igktgptads vgavaalams scgqlwvgdt tntrvlyfp
//
LOCUS       WP_010413338             432 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Citromicrobium sp. JLT1363].
ACCESSION   WP_010413338
VERSION     WP_010413338.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..432
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44494
     Region          30..429
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mtrfvsalll aaliaapasa qdigaivand tgdtawilta salvllmtlp glalfygglv
       61 rsrnflsval qtgavasivs vlwivvgytf afgdvssgwv gngrawmlie ltnvrlgtti
      121 pestfvlfqm tfaiiapalm igawvdrarf swvvvfcalw slvvyapvah wiwgggwlas
      181 sgtldfaggl vvhttagvsa lvvavmmgar rgfpdkpmlp hapgltmvga allwvgwfgf
      241 nggsalaatd dastaiinth vaastaalvw llierigfgk ttmvgwatga iaglatitpa
      301 aafispgaai lfgalaavvc yfavlqirkw giddsldvfa vhgvggimgs lllglfvssa
      361 lggvgyaqgm tpgaqlgaqa lgvgvvalws avmtailalg igiiapmrvr kkdeiegldi
      421 tshgerawhl gd
//
LOCUS       WP_010413491             210 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SCO family protein [Pseudomonas].
ACCESSION   WP_010413491
VERSION     WP_010413491.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..210
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22698
     Region          56..209
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mnrtqkavfi aaaivalllg vilsqvlpgr ssqdqaalnd agivllpksr qlpalsmtdq
       61 ngaavaldgl kdqwtlmflg ytfcpdicpt tlaqikqira elpeeavkhm rvvlvsvdpn
      121 rdtpqqlkqy lgyfdpqyig ltapvadiqt lanavsipfi padtskpnyf vdhsgnlali
      181 gpdgtqrgfi raplnnqklv kqlpgllerd
//
LOCUS       WP_010413510             368 aa            linear   BCT 01-JAN-2025
DEFINITION  alanine racemase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010413510
VERSION     WP_010413510.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Hayashi,H., Wada,H., Yoshimura,T., Esaki,N. and Soda,K.
  TITLE     Recent topics in pyridoxal 5'-phosphate enzyme studies
  JOURNAL   Annu Rev Biochem 59, 87-110 (1990)
   PUBMED   2197992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..368
                     /product="alanine racemase"
                     /EC_number="5.1.1.1"
                     /GO_function="GO:0008784 - alanine racemase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0006522 - alanine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=38813
     Region          13..348
                     /region_name="Alr"
                     /note="Alanine racemase [Cell wall/membrane/envelope
                     biogenesis]; COG0787"
                     /db_xref="CDD:440550"
ORIGIN      
        1 mntlpdpppp tlrlaidtda laanwralnd lssparagaa vkadcyglga dicvpvlrda
       61 gcrdffvahw sevapalrhv apgrlsvlhg pvnaaeadya ralgvrpvin slhqarvwte
      121 ggggpcdlmv dtginrlgva psqlgeddir aldvhvllsh lssadedapa naqqlaifge
      181 akrriahret slsnsagial gsayhcdltr pgialyggvp spalaqhirq vaylqasiih
      241 iaeigagdtv gynreftasg pmrvgtvslg yadgflrswg ggfllhdgrr lrllgkvsmd
      301 mvvvdltdap eigigdwldv pyhlpdaarh tglsqyellt llghrfgrsv kadclanaad
      361 akpnaaqh
//
LOCUS       WP_010413583             293 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010413583
VERSION     WP_010413583.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..293
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=32380
     Region          22..278
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mnavaqghta ststqpqpaa qptaeallqv rgvsleyrtp ervvrathqv sfevdpadrf
       61 vllgpsgcgk stllkavagf iapsegeirl aghqvtepgp drivvfqefd qlppwktvie
      121 nvmfpllasr tlkrpealer aryylekvgl safadaypht lsggmkarva iaralamqpk
      181 illmdepfaa ldaltrrkmq eellelweev rftllfvths ieealvvgnr illlsphpgr
      241 vraeinshqy dlkslggvgf qqtaqrihrl lfdegeagpv eqdlnfqdir iay
//
LOCUS       WP_010413611              86 aa            linear   BCT 01-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Leptospira inadai].
ACCESSION   WP_010413611
VERSION     WP_010413611.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..86
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9106
     Region          1..>58
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mptyeyrcrn cgqtfeffqs mkdeplkdci lckngkvdrl isngggiifk gsgfyvtdnk
       61 spgsssdkss sdsgsstaap sdsssk
//
LOCUS       WP_010413630             332 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [Citromicrobium].
ACCESSION   WP_010413630
VERSION     WP_010413630.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..332
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34739
     Region          40..298
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(46,48..51,71,97..99,126..129,149,176..178,191,195,
                     224,226,233..234)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(150,178,191,195)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(178..180,185,191,222..223,235,251,253)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mpqlsrrtll agaaatgvlt ataaraqrdl aattpnlfgk svlitgsssg fgrlgaehya
       61 rlgakvfatm rnlprpeaee lralaaddgl ditvieidvl sdaqvaagva eaerlngggi
      121 dvlvnnagig isgpievqdm qatelifgtn vlgahrmara vlpgmrkkgg glivpissql
      181 grvivpysgh ysptkfalea mseamayelv phnievsiie pggyptqvwv nrniytsalk
      241 eraaqvhtag ypqvvanmge edgsgrsadp mdvpraiaqi iampggtrpl rtevhpgskp
      301 qmrinevtaq vqvgwlggsg ygplikavhn vd
//
LOCUS       WP_010413631             411 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Leptospira inadai].
ACCESSION   WP_010413631
VERSION     WP_010413631.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..411
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45569
     Region          131..368
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mgiveekdil isysnspvwa aivsagkncl pfytrsvqvn dminarqaai fslfliitgc
       61 fpldpdrvss psykdgryrn lapdeelvgk sffsvlkwkl fgphdpptvk glsnelplvl
      121 ersagdliaa egriravwlg hstiwisvtq kgktiniltd pifesptpil vdrwvplpip
      181 keslpavdfa ivshahrdhl drdslrflrs knpnlkillp sgmkafsede klglaqvqei
      241 gqvthhdfvk ivflpayhws rmgvndtnqy fwgsyaieaa gkliyfagdt gysvhfkeia
      301 kllgkpidla flpigaykpr wfmkhahigp dealaasidl daksfapihw gtfplgddlp
      361 qepvldlkgk lnfpeipdik glnplytgis wgnkngvrvv pwtigsgidl e
//
LOCUS       WP_010413693             191 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010413693
VERSION     WP_010413693.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..191
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=21138
     Region          2..191
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mrvliidghp dpeparfvha ladayadgce agghslrrlr ladmdfpllr svqdwmegep
       61 cpviaaaqkd iswaehvvlf yplwlgdvpa lvkafleqva rpgfahryrg sglpeklltg
      121 rsarvvvtmg mpsafyrlfy fahslkslkr nifgfvgfap vrhtiigave ssakdrqkhl
      181 samrelgqsa r
//
LOCUS       WP_010413698             286 aa            linear   BCT 01-JAN-2025
DEFINITION  prohibitin family protein [Leptospira inadai].
ACCESSION   WP_010413698
VERSION     WP_010413698.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Yoshinaka,T., Kosako,H., Yoshizumi,T., Furukawa,R., Hirano,Y.,
            Kuge,O., Tamada,T. and Koshiba,T.
  TITLE     Structural Basis of Mitochondrial Scaffolds by Prohibitin
            Complexes: Insight into a Role of the Coiled-Coil Region
  JOURNAL   iScience 19, 1065-1078 (2019)
   PUBMED   31522117
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..286
                     /product="prohibitin family protein"
                     /GO_component="GO:0005743 - mitochondrial inner membrane
                     [Evidence IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0035632 - mitochondrial prohibitin
                     complex [Evidence IEA]"
                     /calculated_mol_wt=32296
     Region          32..225
                     /region_name="SPFH_prohibitin"
                     /note="Prohibitin family; SPFH (stomatin, prohibitin,
                     flotillin, and HflK/C) superfamily; cd03401"
                     /db_xref="CDD:259799"
ORIGIN      
        1 mqtnlnpnkl lrvkktafvt lllsilasyg cftnirpgea glrwhpltsg lqkdlltnal
       61 ylyapwndiy lypiqwtsyk ekvdvltrdd ltinvvaavi lrpvaseiyn lqieigpdyy
      121 ekvvrpqfrt svrnalsays mirisketpk vsqdirqals eklrgkhiei ddviiddiey
      181 srpiltaieg kltkeqeqeq mkfeiniakk daeitiihae akakatviea egkakaqkli
      241 asqltkqylq lkafenpnsk lmivpsgkds lplilntpqe naksee
//
LOCUS       WP_010413723             315 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010413723
VERSION     WP_010413723.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..315
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34247
     Region          6..226
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msdpilelsg ltkvypgglk alddvdltir kgeifallgp ngagkttlig avcglvrpts
       61 gsmrafgqdl qgdwrqarar iglvpqelst dmfepvkhav eysrglfgla pdparieeil
      121 rslslwdkrd nrimelsggm krrvliakam ahepdllfld eptagvdvel rkdmwhqida
      181 mrargvtvil tthyieeaee madrvgiirk grilmvdekd ammarlgrte ahimlaeplg
      241 alppaiaqfp veleeggrsi cyrggdgtgk greevadltk aliasgidyv gidvressle
      301 difvsllgde egeaa
//
LOCUS       WP_010413753             161 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010413753
VERSION     WP_010413753.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..161
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=17136
     Region          <39..158
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mtqqplliaw hsrtgaseam araaakgagd aarilaaedv tpddllaaqg ylfvcpenla
       61 tmsgmmkemy drcyypvlgk iegrafatii aagsdgegaq aqidriaqgw rlkrvadrii
      121 icmeaqtpee ilaektvpqg rldecealge amaeglamgv f
//
LOCUS       WP_010413832             189 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein, partial [Citromicrobium
            sp. JLT1363].
ACCESSION   WP_010413832
VERSION     WP_010413832.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         <1..189
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
     Region          5..183
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 qtrlapatyk alsplgtapv itddnglvla esnavidyil dshpdsplrp apgdssrtdy
       61 lfwfhagvgs lmpmqffngl ltmmkdrspa lvrpvigkat dtvremlvap rlktlfdkle
      121 idlarnrwia gdhltaadis mcysiasada qgrlkdrpnc qrwmeqmret psfqramekd
      181 gretfvfsf
//
LOCUS       WP_010413853             395 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Citromicrobium sp. JLT1363].
ACCESSION   WP_010413853
VERSION     WP_010413853.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..395
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39997
     Region          2..389
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msgskssdge lglaavwaia vggmvgggif stlgvvissa ghwaalsfvl gglvayatgh
       61 slaaltvekd eaggvysflr dlgftglarf sawvllagyv ltcavyaytf gaylgqaigg
      121 pswlppamaa tailtmtgin lrgagqaagv eitivvvklt ilaglaafgl sqfeaeklsi
      181 aqqpgligiv igaasvfmay egfelvaydy demkdrkrim rrimplaigs aaliyvlval
      241 avpmltgtqa viedgevals ragqaalgtp gliavtiaaa fstasainat lfssarlare
      301 vaqdgglpqg lgrknshgsp qwavltlaal alalavmggl dglvsgasiv fllvfgtlna
      361 lavkenvgkr witlpgavla fgalavlvlh mlgvi
//
LOCUS       WP_010413890             819 aa            linear   BCT 01-JAN-2025
DEFINITION  penicillin-binding protein 1A [Leptospira inadai].
ACCESSION   WP_010413890
VERSION     WP_010413890.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..819
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=90499
     Region          14..709
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtlfsdgihr ttkillgial agglffgyil sevdeggela mlasyqpttp trlydnngiv
       61 faelyrhkqq llkyqdipph vvqaflsved nnffnhfgid fmaisraaiv nvlsgrikqg
      121 gstltqqlak tvlqnrkrsf irkfvealft lqieqeyske eileiyfnli ylghgttgla
      181 saadvyfhkd vtdldvaeaa llarlpkapv dyspyknpaa akrahlevlk lmagqgfipa
      241 dkvqfihdef wekywpvvit qspsqstwgt klnraphfte fvrqkllkvl gedrlynggl
      301 kiyttldvrk qeiaqeelrk alkkhddlvs gvtvnyagga drglvglygl lgsvfpvgvp
      361 fvsklddkan frvalekeli daadlltlft peadnesasf tefqkrsavf gknlhvegaa
      421 itidhtngyi qtmvggyeft pknqfnravq arrqtgssfk pfvygaaiae rvvgsgtgim
      481 daplttltee gegwspqdfd gdfqgmvpls ralslslniv svqvflrtga davidfasrl
      541 tkadksrfps spalalgiae ltpyemavgy siiankgrnv ipfavryvid qsgnviynee
      601 ekvrqelere redgsiqvis egtsyilrrm lmmvamagta tdglrnpekg nykgfaagkt
      661 gstssftnaw ycgfdpkltt viwmgfdkss islgrgqaas vlavpiwgrm ynrfyggegy
      721 pnfgnehged lppdevqggg tcayngltpk pgvcpmtqnl tlkpitvagv tksvqgnrqc
      781 dgdrdhhrsi dfreflqqey qisdeeigkt erkfkpktd
//
LOCUS       WP_010413948             194 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmD family RNA methyltransferase [Leptospira inadai].
ACCESSION   WP_010413948
VERSION     WP_010413948.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002368
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..194
                     /product="RsmD family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0031167 - rRNA methylation [Evidence IEA]"
                     /calculated_mol_wt=21691
     Region          10..188
                     /region_name="RsmD"
                     /note="16S rRNA G966 N2-methylase RsmD [Translation,
                     ribosomal structure and biogenesis]; COG0742"
                     /db_xref="CDD:440505"
ORIGIN      
        1 mkpakkgkgl riqtgdlkgr vipspvspeg ksnftpailk kslfdilesl qlqgrlnlsd
       61 aafldlfags gqmgiealsr gfakavflel awdryeslkg vlsrldrehl vlrkdafrfh
      121 kdfdltqthk vyfidppysf wekkepkika mvediiaeep gaaviaiqsp tplnwdgfep
      181 rpfgrnvlnv rvlv
//
LOCUS       WP_010413958             133 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Citromicrobium].
ACCESSION   WP_010413958
VERSION     WP_010413958.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..133
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14459
     Region          14..133
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 msetsgeagg tpgerisdae haimevlwdr hplsaaevcd evcetrgwsm ptvktllsrl
       61 vgkgalatep agrkflyspl iersdyvgge srrlvdrlfg graaslfahl aesealtded
      121 lgeierllke mrk
//
LOCUS       WP_010413980             217 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Leptospira inadai].
ACCESSION   WP_010413980
VERSION     WP_010413980.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..217
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23382
     Region          4..217
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          33..61
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          62..89
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(91,93,97..98,101..103,105..106,110,113,122,128,130,
                     134..135,138..140,142..143,147,150,160,162,164,168..169,
                     173..175,177..178,182,185)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          91..122
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          128..160
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          162..193
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msdifhlias gqkaqviyal renpslgsla npegitpllf alyygkddii qaylaleipl
       61 nlfeaaalgn qarvqallek dseavhsfsp dgwtplhlaa hfgrtslvtf lldhgaelqa
      121 kskskfsfgn tplhsavasg kdetvkllie rgadpnygqe eggytplhia asrqgngqiv
      181 alllkhganp elktkdgqta reiamqrgnw keaeile
//
LOCUS       WP_010414029             343 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010414029
VERSION     WP_010414029.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..343
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37422
     Region          15..196
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(18,20,100)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(45,99..100)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            98..100
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 msrlapirld qtlavvipsy kvlahvldvi grigsevami fvvddacpeg sgnhveencs
       61 dprvrvirha qnkgvggavm tgyqaalaag advivkldgd gqmdpaligr iarpvlegra
      121 dyakgnrfhs iwnvrkmpal rlwgnaalsf vtklssgyws lfdptngyta ihasalemle
      181 paniseryff etdmlinlgn aravvadvpm eavygeeisn lnirresgqf likhlremvk
      241 rifynyllrd fslasvqlla gsamllfgvv fgmvhwydsl asghiastgt vmvavlpiil
      301 gfqlllnfla fdmanepkhp lqpapsltel lsgtrrreat nva
//
LOCUS       WP_010414036             467 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA recombination protein RmuC [Leptospira inadai].
ACCESSION   WP_010414036
VERSION     WP_010414036.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13487459
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..467
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=52631
     Region          15..>201
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          120..460
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mdfpknrsih kggkmeyaiv llvgilvgfs lafflakrvy ggeskvspae heklklelag
       61 iratelrske rtaqletdlk clsdkntqai gawqsmkkes dllkerlenq kkefeemisr
      121 lkdefknlan qvlldnsqkf nqqtheklgd llkplkenie ifgkkvesst qetkisaatl
      181 kehisslvkm neslqaeakn laealrgdkk aqgdwgeeil egilersglr egeeffrqns
      241 fkdeegekrp dvvvrlpgnr cvildskvsl nayvsfyste dekekdlfle qhanalrkhv
      301 kdlsrknyqy leglnspdfv lmflhnepal fwalqkdpal aleayqqnil ivtpsslmis
      361 lkmvsniwrl edqdrnakei arqsglllek lgnfvgdlek vggsltatqg hydnamkklk
      421 tgkgnvlkka geimelgatv skdetkkrla tflneedgde psllspd
//
LOCUS       WP_010414047             120 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PH domain-containing protein [Sphingomonadales].
ACCESSION   WP_010414047
VERSION     WP_010414047.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonadales
  ORGANISM  Sphingomonadales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10547098
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Sphingomonadales"
                     /db_xref="taxon:204457"
     Protein         1..120
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13321
     Region          <22..115
                     /region_name="bPH_1"
                     /note="Bacterial PH domain; pfam08000"
                     /db_xref="CDD:462337"
ORIGIN      
        1 mgllnqtqtt pqgfvdnhgh alvegeevyf afrtirdwia ftdwrliyvd vqgilgnkke
       61 yltvpyrsit afsitsagti didaeiavfl sghppiefkv gkftntealq kllasrmnan
//
LOCUS       WP_010414123             345 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010414123
VERSION     WP_010414123.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..345
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37887
     Region          18..344
                     /region_name="BcsL"
                     /note="Acetyltransferase involved in cellulose
                     biosynthesis, CelD/BcsL family [Cell motility]; COG5653"
                     /db_xref="CDD:444374"
ORIGIN      
        1 mnalshpteg datgsaidal ahaddprraf lrerwfsavd dpsfrthive gsegrpllgl
       61 glvsrsfgpl siaqaagayw pfrglpmpgd tsaktlaeal rqrgarealg hawrlgpvia
      121 ddpavgilrq aavdagwhcv erpvgslfcl dlvalrasgt wpstkgkqkd rwrvrqlekt
      181 gpvnittysg ldwsaedrda iaqieaaswv gqleqggdtk fhdpdlrryw ervsedpala
      241 amirghilwv getpaaftfg letgdtryci annfdrqfnk fspgrvllyh dfedaadrgf
      301 aridwglgdg gyksqmgahe datvvdllfv rnpllariaa llwrr
//
LOCUS       WP_010414175             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: J domain-containing protein [Citromicrobium].
ACCESSION   WP_010414175
VERSION     WP_010414175.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..197
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=22151
     Region          141..>191
                     /region_name="DnaJ"
                     /note="DnaJ-class molecular chaperone with C-terminal Zn
                     finger domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0484"
                     /db_xref="CDD:440252"
ORIGIN      
        1 mrqtrfhgrh eangrlcshp acdepgefra pgaygnsfdg pgqwrwfcle hirefnagyd
       61 wfdgmsadei lraqspaagw qtespafrpt ggvdgmprwa dfddpldais araggirsra
      121 erearmameg rfskeearal etlglgektd akrlrqryse lvrryhpdrn ggdrsyetrl
      181 grvveayqvl rksaaig
//
LOCUS       WP_010414185             713 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010414185
VERSION     WP_010414185.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..713
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=77457
     Region          86..627
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mwghkakprl gheaagssag hsgyysltes maddpwendp dfaedrrsgp tlwdlayeil
       61 tahgtrywgv riaagllllv iltviwlaft aplskslepi appqvtllaa dgtpiarnga
      121 vydepvdvdr lpdhvvqafl atedrrfysh wgvdprglar atlnnisggp tqggstitqq
      181 lakftfltpe qslsrkarem liafwlegwl tkdeileryl snayfgdnty glraaslhyf
      241 yrqperlepn qaamlagllk apsayapsqh yeraatrmqa vkaslvsagf lsseqaermr
      301 apeldmrlsn dlptgtyfad walpeardrt qpgyalqalt ttldarlqgi ardviadapl
      361 gdaqaalvam rrngevvami ggtdysksaf nrvtqarrqp gstfktivyl aalqngfgpe
      421 dpvsnrpftq gsyrpenydd qysdfltleq afarssnvaa vrmfnevgsa dvielardlg
      481 isspiprgdp svalgtagms lmdltaayag iagnsypvrp taflreprgl wdrifnaprs
      541 fsgsthndie rllrtaindg tgraaqlpgl nfgktgttqn nrdalfvgya gdlvvgvwvg
      601 nddntpldgv sggglpariw ksfmlraqgi rsegparrqd prapvqpldv pnasdipdpv
      661 eeegaeittd srgitireea prdeapplda pqdgprsape lppvreeeaa tan
//
LOCUS       WP_010414202             198 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira inadai].
ACCESSION   WP_010414202
VERSION     WP_010414202.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23052
     Region          16..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mekrkvpian hegpyerlvg tairliysqg yagtsvnqvi gesdshkasf yryfqtkedl
       61 greylkiqat nfrnswerlm arsatpvefi nrwmallnkq vrekkyfgcp larfmgsldq
      121 pdqawvnqga evleswihcl etyfeenitr gllprtfpar kkaerlmklf qansqfymit
      181 gnskffkelq eemigelt
//
LOCUS       WP_010414331             165 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF427 domain-containing protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010414331
VERSION     WP_010414331.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..165
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=18148
     Region          14..135
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 mqrpdpippg pgqesvwdyp rpaiaeptsa hiviehrgit iadtrravrv letshppqyy
       61 lppeditpgv lehapgkslc ewkgqarywd vvaggdrlak vgwsyaepta pfriladyva
      121 fypapfdrit ldgevvqpqp gefyggwits avvgpfkgvp gsrfw
//
LOCUS       WP_010414418             247 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Citromicrobium
            sp. JLT1363].
ACCESSION   WP_010414418
VERSION     WP_010414418.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..247
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27426
     Region          4..240
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mndsapaptf klasynihka vgtdrqrdpl rilkvlaevd adivvlqead rrfgtrdrtl
       61 pdflveqhsd yvpvpfdvqh dsmgwhgnsi mvrrdisvid hdvlhipyle prgvvtatlr
      121 lpggaelsvf gmhldlsglw rvrqaraiae laqaaqrerp tllagdlnew rpnggclkef
      181 arhftlldcg rsfhsqrplg rldrimhgps leavdfgvhh splasrasdh lpvwadlrap
      241 akqaaat
//
LOCUS       WP_010414045             374 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P) transhydrogenase subunit alpha [Citromicrobium sp. JLT1363].
ACCESSION   WP_010414045
VERSION     WP_010414045.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Bhakta,T., Whitehead,S.J., Snaith,J.S., Dafforn,T.R., Wilkie,J.,
            Rajesh,S., White,S.A. and Jackson,J.B.
  TITLE     Structures of the dI2dIII1 complex of proton-translocating
            transhydrogenase with bound, inactive analogues of NADH and NADPH
            reveal active site geometries
  JOURNAL   Biochemistry 46 (11), 3304-3318 (2007)
   PUBMED   17323922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..374
                     /product="NAD(P) transhydrogenase subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38652
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,289,315,317)
                     /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..188,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,229,240,
                     257..259,266,268)
                     /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 mkiavlkera egetrvaltp etakkfialg advaieagag eaaaisdaay tdvgatvgpa
       61 qealkdagiv lgvqapdpat lggakegafv aalfdpfrer ervdayakag lealsmefmp
      121 ritraqsmdv lssqsnlsgy kaviaaadqy grafpmmmta agtvqparvf vmgvgvaglq
      181 aiatakrmga qvsatdvrsa treqieslga kaifvaeggi egegsggyas emsdeykaaq
      241 aklvsehiak qdivittali pgrpaprlis ddqiatmkpg svifdiavpq ggnvegavad
      301 qlvtrhgvti mgyantpahl apdasalfar nlynflsafw daeegrpvld eeigdavrlt
      361 qggqvvsarl leag
//
LOCUS       WP_010414520             419 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Citromicrobium sp. JLT1363].
ACCESSION   WP_010414520
VERSION     WP_010414520.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..419
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=44512
     Region          10..417
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mtkagkpkgg advpglparr aalrmldgvl rrgetleqne taalhglpap daglaraiaa
       61 etlrwlvdfd alidsatren lpedakprtv lrlmlaqwlr ldtpphavva talpllsggp
      121 krlahgvfga lakrgvelpg aptlppavag rwgeragaia aglaepppld ltlrdpshtp
      181 ewavklgads lmpshlrlsr gqavhglegf edgawwvqdl aaslparllg dgqgrrvldl
      241 caapggktlq latqgwqvta ldisakrlkl leenlkrtgl eaeviaadaf kwepeapfda
      301 ilidapctat gtarrhpdvl hrigprqiad laevqarlie rasgwltpgg alvyavcsle
      361 seegeeqaek vwlprepisa eelpaglspt skgtvrtdpg mlpehggldg ffiarwrns
//
LOCUS       WP_010414548            1094 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010414548
VERSION     WP_010414548.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..1094
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=117805
     Region          29..1053
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msdsqaksaa vdrygneatd rardrtgpia fmarngvasn lllllmlmag yfsyttivqe
       61 vfpensldti tvsvtypgat peeieesill kveeaveaid gvdqisstas egggsvnvel
      121 dlgtdiaral devksevdqi qtfpeeaeep direlttrqv alrialfgdv nertlketay
      181 rledaaaalp eisyvetsav rnyeiyadvp qsrlralgls lpqlaqtvgq ssldspagai
      241 etdseevrvr tigqnydqqd fenivvltts dgatlrlgdi aevrdefeda dlitrfndep
      301 vafvdiyrts dervldvags aktliaedfd lppgvsyaiw edsselledr lslllrnaal
      361 glvlvlaalt lfldlrlaaw tavgigatfv gaifildwag ssinmfslfg filalglvvd
      421 davvvgeniy aerergrtgi gaaiagaqrv kipvffavat tvtaflplla vggvigkila
      481 diplvviavl slsliealyv lphhlstlpd pehkpgnpvt rffarvqawv darfqtfvng
      541 pldralrfvv ampylivasg vallvvfmam ipgglikfsf fpeiegdivv aalempsgtt
      601 vertaevter ieaaadrama rfadqdtptd aaeadgtagp tfleavytti gqarstngpg
      661 gpqttlrpnl anvqlslvps aerdvsavqi eeawreelge vpearslsis ssllgvgapi
      721 nvqlnhpdda vldqagdrlm aelgrvsgvf dlesdqdagq qevelrlkps artlgvtlqd
      781 vagqvraaff gaeavrvqrg redvrvyirl peeerdsiad ieryrvrvpg gevalssiad
      841 vsfgeapsvi rredghriat itgdvdddti tgqevaqlld ekimpdlqad ypalqyefgg
      901 eqeeqqesfg dlgrafllal lviyallavp frsyiqplii maaipfgmig alighlllgi
      961 plgilsmfgi ialsgviing slvmidflne nldngmeped amieaaksrf rpvmltaitt
     1021 flgvapitfe tslqaqflip msaslgfgvl fgtallilli palaiiqmra aarvqqwrgk
     1081 draqidhgge pmap
//
LOCUS       WP_010414611             504 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tripartite tricarboxylate transporter permease
            [Pseudomonas].
ACCESSION   WP_010414611
VERSION     WP_010414611.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..504
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=52772
     Region          1..491
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mdtfgylgqg fgvaltpynl italcgtlig tvvgllpglg pingvallip iafalglppe
       61 salillaavy lgceyggris sillnipgea stvmttldgy pmarqglagv alslsawssf
      121 igafiatcgm vlfapllakw aiafgpaeyf vlmvfaivcl ggmagdrplk tfiaaliglf
      181 lsavgidans gvyrftgdni hltdgiqfvv lvlglfsise illllekthr gqeavkatgr
      241 mmfnvkeaas vfvvnircgl lgfilgvlpg agatlasava ymtekriaga sgkfgqgdmr
      301 glaapetaig atacgalvpm ltlgvpgsgt tavmigalsl ynitpgpmlf qqqpdivwgl
      361 iaslfianim lvilnipmir iftrilavpn walvpviaii tgigvyavha ttfdlflmvg
      421 igifgyilrk ldfplspill gfilgglmeq nlrralsisn gelgilwssp itlgvwvvtv
      481 fmllfpllri wrkrakqkaa aahg
//
LOCUS       WP_010414686             396 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010414686
VERSION     WP_010414686.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 396)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..396
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42249
     Region          100..370
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 msaadrlgig rllrsapspg adiqgrlyaq lggspaaalm gslcalvvla vaiyrssapv
       61 fvvfvaleiv lafariaesr wrtrrkaecl sidvswsalf sllwcslqga vafvimsgdd
      121 pvlqvlsatl vtaalglica rnyaapnfat lllllmdvpf aagavladap llsviviltp
      181 pfmfgarqii ttfhgtllks lkaekenlyl ayhdsltgil nrqgmdhhla klanepthtm
      241 aivsldldgf kaindeyghg agdtvlveva rrieavvgtr gvvarmggde fmvlvrdcgi
      301 ehvralgekl verisegaip vatdvpvrvg asagfacipq daltthelri radmalydak
      361 dagkhtcrrf rqpdrpigdl naklrrafsr gsrvag
//
LOCUS       WP_010414752             184 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010414752
VERSION     WP_010414752.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..184
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=19084
     Region          1..151
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mtkmtvnnrp veylldpdtp llwalrdasn ltgtkygcgt gdcgacmvlv dgvalrsclv
       61 tiaeaegrlv ttieglsrdr shpvqqalva eqaiqcgfct pgiaiaaaal iednpspsre
      121 didaaipnlc rcgvyprlar aikraseaas gaapieaapp paiepaeaar dvpalrptsa
      181 pprd
//
LOCUS       WP_010414790              96 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Leptospira inadai].
ACCESSION   WP_010414790
VERSION     WP_010414790.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..96
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11049
     Region          21..87
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 msgesflpde pilwvseeei rkqrqiakdl rktpwwkkkk adgicyycrk kfppeeltmd
       61 hliplakggk svkanlvpac kecnnakknk lpfedf
//
LOCUS       WP_010414800             110 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Leptospira inadai].
ACCESSION   WP_010414800
VERSION     WP_010414800.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..110
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12317
     Region          3..98
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(19,21..23,29,52,54..56,58..60,63..64,86,90..91,93)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            55
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 meisirksge tnviglsgsl diytsidlkn ffeqnidrin nnvvinlekl nyidssgigm
       61 likqlnyvqe lngkffianm kpaiekvfkv agltsyfqtl sesefiakyp
//
LOCUS       WP_010414854             164 aa            linear   BCT 01-JAN-2025
DEFINITION  GAF domain-containing protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010414854
VERSION     WP_010414854.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10482064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..164
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18344
     Region          21..151
                     /region_name="GAF"
                     /note="GAF domain; pfam01590"
                     /db_xref="CDD:460259"
ORIGIN      
        1 medrekrrlq tlhgyrlldt ppepefddiv rraaerfdtp ialmslvdad rqwfkakvgl
       61 dvdetprsva fcaytiqgsd vmvvedared erfsrnplvl ddpsirfyag apvtaeggdk
      121 lgticiidrk prhdfseadr ealanlaaev srmlgstkem arsg
//
LOCUS       WP_010414869             329 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010414869
VERSION     WP_010414869.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..329
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36363
     Region          3..205
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mtnpkmsivm pvynvqdyva eaiqsvlaqt ftdfeliivd dggqdgsmei vhsfyderir
       61 ivtqanrgla garnsgiaaa rapyiallds ddrwhpeklr lhyvhleadk sigvsfsgsr
      121 midqvgnela vamrpkltgi rpqdilrrnp vgngsaavlr rsaidaamft hpeeswrkcw
      181 fdesfrqsed ielwvrlsaa hgvrfegiag elteyrivgg alsanivkqy lswtemldka
      241 mryapdlvak hgvaarayql rylarravql gnaelaadlf aqavrleprm lvaeprksat
      301 tagavvaakv lgpqrfrais qhylkqaaa
//
LOCUS       WP_010414997             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Sphingomonadales].
ACCESSION   WP_010414997
VERSION     WP_010414997.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonadales
  ORGANISM  Sphingomonadales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Sphingomonadales"
                     /db_xref="taxon:204457"
     Protein         1..304
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=31742
     Region          15..291
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mdvylpianl svnglvival galtgilsgl fgvgggfltt pllifygipp tvaaasaatq
       61 vtgasvsgvl ahnrrggvdy rmggvlvvgg ifgaligall frffqaigqi dvvisilyvf
      121 mlgsigslmm realsalnir qskglkraak rrhhplvagl pyrwrfyasg lyisplapli
      181 lgtgvgiltm lmgvgggfml vpamlyilgm sgkvvvgtsl fnilfvtmat tmthalttka
      241 vdlvlaglll vgsvlgaqfg trialklkpd wlrlalativ llvalrmlfg lsiqpdevys
      301 vvnl
//
LOCUS       WP_010415085             226 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010415085
VERSION     WP_010415085.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24274
     Region          1..220
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 miklenierr yvsdevetta lvdvnlevae geflaimgps gcgkstllnt lgtidrptsg
       61 hywfgdtdla amdekalakf rgaqlgfvfq sfnlidelti eenvalglay rkdvsgnkge
      121 rvaaamdtvg iahrgrhfph qlsggqqqra aiaraivgqp kliladeptg nldtangeqv
      181 mniltalndd gativmvths pshadmakrr idmldgriva samrai
//
LOCUS       WP_010415105             265 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010415105
VERSION     WP_010415105.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..265
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26806
     Region          16..265
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mprrsrracr sgrigfaall aafcvtally asvgfgggst ysallalsgm dyrllpvvsl
       61 lcnlvvvsgg tirfararit pwrgallltg iaapaallgg ltpiaerafl mllgaslcva
      121 gallllprrk vtdgpgggag arggramlla aaplgylagl vgigggifla pllhlvrwdg
      181 praiaatasl filvnslfgl tgqlakngtg llgeaagtgl plmlavvigg qigslfavrl
      241 fkpqliawlt aaltlfvgvr lllgl
//
LOCUS       WP_010415193              88 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Pseudomonas].
ACCESSION   WP_010415193
VERSION     WP_010415193.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..88
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9702
     Region          9..>73
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
ORIGIN      
        1 mekeaflqll aaegfgtvve vereafgtld shahnfeama lvlygslvir ksdgdftyns
       61 gdifhlecnq phsevfgehg vrylvgrk
//
LOCUS       WP_010415114             270 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010415114
VERSION     WP_010415114.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..270
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=29018
     Region          5..263
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 msaldrevla lmrdvserii mprhraleat eiiekadddl vtiadreaev alaeglaklh
       61 peaaivgees vhadpavmdr lsgtcwiidp idgtsnfasg kghfgimval aengfaqagw
      121 iydperdrlc aahlgqgati dgeqvlarps ganpphlaam tkfmapaqrk rfeteiapny
      181 tlvqppgaac eqypltvlge hdvaiyertl pwdhaagnlf lneaggtclr ldgtpyrvdd
      241 grrgmigaan relfdqliar laaagyqpaa
//
LOCUS       WP_010415218             219 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010415218
VERSION     WP_010415218.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..219
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23503
     Region          3..194
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mktvfvidak aerraevcrv llqgerhaep fetaadflaf areeslalvh dadgaaaglc
       61 drlrdapqlv pvvgysesps fsravtamqa gaasylawpf tvdefsdeid riepamretl
      121 drkrrvaear rllagltare revlvnlish gtnkaiakel eisprtveky raailvrlgv
      181 antaqairva veagavegdf tdsarkgaaa spaqaglmg
//
LOCUS       WP_010415220             247 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Citromicrobium sp.
            JLT1363].
ACCESSION   WP_010415220
VERSION     WP_010415220.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..247
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28027
     Region          18..227
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mefpntgdfl agrlrdklsq ddlefieslv aetrqgetgd vllergavte qstilisgyi
       61 frtiesgdrr fivgvhvpgd fvdlhgfalk rldhsivaag pitygiaphe rlrdalehrp
      121 rvaralwfat lldaaihrkw iqmleqldap rriahiycel hrrfelvgqa narslrtpft
      181 qidladmcgv saihanravg klrelelaei rrgdlytsdw dalrtyaqfq adylygdgpl
      241 rfdqdwl
//
LOCUS       WP_010415235             895 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Citromicrobium sp. JLT1363].
ACCESSION   WP_010415235
VERSION     WP_010415235.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..895
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=96638
     Region          54..878
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mnrlltgiss galsfvlstg ayaqvatpad asaaaataqq eqavqadrpk rggvntivvt
       61 aqrrsedlqd vpvavnaiga eeldelnint fddyleqlps vtaggsgpaq stiyirglas
      121 ttpnlttagv aglapnvsly ldeqplaqpg rnldvyaadl erievlkgpq gtlfgassqa
      181 gvvrlitnkp slagfdasft agtsftkgge qsykaeamin vpvtnnlalr gvvylddqgg
      241 yidnvqgtrs lrdsamfrpv gtvrdngvav sadragfksd aaslayidnn vtfieannat
      301 lveddfndtq ysgfrataly evtpdwritv ahtrqgldsd gvffadpdlg lddleiqrfs
      361 qdklqddfsn tswsvegrlg mldviyngay tdretqqsvg ysdylfvgqy ipyyscdtaa
      421 iypgsvaaap adptcyapdf svgsntdttv ftqelrfstp senrlratag gfysnlilke
      481 rndyfygreq srgsdgvtrg fapiypftnt evtgitgnaf pgyfsdpgpl penaafrndv
      541 krtdeqigif gevsfdivpd tltvtggary ydvkvdlega atsafckrns piyganvgvd
      601 padqtnipgc ggtnlsliyg edntfgnpdk araegvifkg tvtwtptsdl lfyatysegf
      661 rpgllnrpgg aqgpgnftvp felqtddvkn yelgwktelf drqlrlngsa fyvdvsdlqt
      721 tifdpgitnl ffsdnaadae ikgveaefty apysisgltv agaisildte itdkltptdd
      781 ivvgselaya psfqgnlrvr yewdlsdtle afiqpqvshs askftdiiqi nrleldsytl
      841 fdlsvgvsta nykfelygen ltderaqvsg nfnfdrarit vnrpltvgvr atyny
//
LOCUS       WP_010415293             213 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Leptospira inadai].
ACCESSION   WP_010415293
VERSION     WP_010415293.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..213
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24117
     Region          14..206
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mdlmlesmfs kfgktydpnq iifcenepgn dfyliqtgkv kitktvgtsi ktldileqgd
       61 ifgemailee qprsataiai sdvkvlnfnr anfellltkn ptlalkilti fsvriydakr
      121 rllilllddi tgkvadvflm lyekmhthtd fkevvlnitv edvadwcaqp vgevqkvvnq
      181 faksgkieiy sdkivihnin dfqrivsqkr kps
//
LOCUS       WP_010415363             127 aa            linear   BCT 01-JAN-2025
DEFINITION  PilZ domain-containing protein [Leptospira inadai].
ACCESSION   WP_010415363
VERSION     WP_010415363.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..127
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14267
     Region          20..114
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 magthslfdd kyeyrdpsqq krknarvkit idadfsvkgk sqrfpahlvd igtggaglet
       61 rtsvfegdri flfapingkn melesevirv sgkkanvifv nlldedrdli qdlihkkffd
      121 kdkkpla
//
LOCUS       WP_010415367              68 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Leptospira
            inadai].
ACCESSION   WP_010415367
VERSION     WP_010415367.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..68
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7424
     Region          1..66
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mrelkidgmt cdhcmstikk aiqkmdpkak ieidlktgia kiesastead lsnaireegy
       61 tllsikni
//
LOCUS       WP_010415372             403 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Citromicrobium sp. JLT1363].
ACCESSION   WP_010415372
VERSION     WP_010415372.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..403
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42831
     Region          41..375
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 msdpgagpna apkpkggsak krnllaeqel rllstlvlll giglflalpf vlsigsvvfl
       61 plttavilsv llapladrls awgvpntlas vlsllifvai vvlafsailq pafslfdrlp
      121 elieqigary eelqaefawi anandrladl vgssggnevv lagpsvfqqv aisapvllle
      181 vmltflmaff mveargrlrr nilfgrtsfg tsvkaarvlr evqdrvaayi ltvawinlgv
      241 givvalgawa mdlpapimwg glatllnfip yigplamtal ltlfglgtad tvflglippv
      301 ayvvlhvfea naitpailgr rftmnpvmil lafsyftwiw gavgallsvp illmltaffd
      361 higrpnllgf ifgeplfqtp lieldaegdt gadaatasea rpg
//
LOCUS       WP_010415377             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: superoxide dismutase [Citromicrobium].
ACCESSION   WP_010415377
VERSION     WP_010415377.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..204
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22323
     Region          7..193
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mafevtplpy pddvlspavs aetlsyhhgk hhkayidktn aaiegtdhag kpleaiiaaa
       61 rgsdqglfnn saqswnhgfy wnsmagqesa psdelksmie safgsvdalk eklqergagh
      121 fasgwvwlae kggklsieet hdgdtladqd gvnpllvidl wehayyldhq narpaylkal
      181 tteklnwafa senlargktw typq
//
LOCUS       WP_010415380             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dicarboxylate/amino acid:cation symporter
            [Citromicrobium].
ACCESSION   WP_010415380
VERSION     WP_010415380.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..429
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43971
     Region          20..416
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 msapetqrpa klvtlrlpiw wtfgglvtgl iagsliagqp vaerilpvvq pvgtlwlral
       61 qmtiiplvaa llvlgitqla saaragatar rmltlvaatl vfsglatiia lpllldaipp
      121 ppgaqsllae nvdpqqvpgl aefflslvap nivaaaaeta mlpltiffal favaitrlpe
      181 dqsvilrsff eavanamlmv igwvlwlapv gvfalalgva vraggdaafl tlihyilsva
      241 amggivlvaa favgavrhgp vafaramlpa qavaistqss laslpamlas arrldvsenv
      301 adfvlplsva ifratspamn lgvaiyvahl fgielglpam laglavafvi sigsvslpgs
      361 isfvvsigpi alamgvpvep lallvavemi pdimrtlanv tadvalasat drengentpd
      421 datdgapar
//
LOCUS       WP_010415396             225 aa            linear   BCT 01-JAN-2025
DEFINITION  RlmE family RNA methyltransferase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010415396
VERSION     WP_010415396.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Hirata,A., Okada,K., Yoshii,K., Shiraishi,H., Saijo,S.,
            Yonezawa,K., Shimizu,N. and Hori,H.
  TITLE     Structure of tRNA methyltransferase complex of Trm7 and Trm734
            reveals a novel binding interface for tRNA recognition
  JOURNAL   Nucleic Acids Res 47 (20), 10942-10955 (2019)
   PUBMED   31586407
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Caldas,T., Binet,E., Bouloc,P., Costa,A., Desgres,J. and
            Richarme,G.
  TITLE     The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S
            ribosomal RNA methyltransferase
  JOURNAL   J Biol Chem 275 (22), 16414-16419 (2000)
   PUBMED   10748051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..225
                     /product="RlmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=24360
     Region          21..219
                     /region_name="RlmE"
                     /note="23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ
                     [Translation, ribosomal structure and biogenesis];
                     COG0293"
                     /db_xref="CDD:440062"
ORIGIN      
        1 mgrsrgdpdk rvrtarrrta sstrwlerql ndpyvreaka agyrsraafk lieldekfgi
       61 lrgserivdl giapggwaqv aikkrpqari vgidllptep iegvtilemd fmadeapdai
      121 mehlggapdl vmsdmaantv ghkqtdhlrt mglvetaadf aiqtlapggq flakvlaggt
      181 daellkllkq nfktvkhakp pasrkgssew yvvaqgfkgg rsage
//
LOCUS       WP_010415527             111 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: STAS domain-containing protein [Leptospira].
ACCESSION   WP_010415527
VERSION     WP_010415527.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..111
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12353
     Region          3..101
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(19,21..23,29,52,54..56,58..60,63..64,86,90..91,93)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            55
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 meiktkkigk htlvqldgrl dithsdevea kllddvqagl gdiiinlqni syisssgiri
       61 fvgmvrelek qgrklklcci tpnvkkvfdv velldlfevf eteqeavatl k
//
LOCUS       WP_010415607             179 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheW [Pseudomonas].
ACCESSION   WP_010415607
VERSION     WP_010415607.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..179
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=18979
     Region          11..166
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mgslvttrqa aatveeeaqy ltfmlggemf aigilgikei ieygsltvvp mmpafvrgvi
       61 nlrgavvpvv dlsarfgrqn saitrrscvi iieansedgq pqdigllvdn vsavleipas
      121 qiepppnfga riradfisgm akvdgkfviv levdrvlsid emsslaeasq slptdvdat
//
LOCUS       WP_010415634             319 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Leptospira inadai].
ACCESSION   WP_010415634
VERSION     WP_010415634.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..319
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35546
     Region          5..314
                     /region_name="UDP-GlcNAcDh_Arch"
                     /note="UDP-N-acetylglucosamine 3-dehydrogenase; NF040723"
                     /db_xref="CDD:468687"
ORIGIN      
        1 mtdrvkigvi gtghmgqyhv nvaktlgdav lvgiydadte rakqmaekhk tsafsslddl
       61 iknvesviva vptflhheia kkallagkhv lvekpiaetl eqakelvels tkndlvllvg
      121 hverfngavl elgkiatdpl lvesrrlapf nprikdvgvv ldmmihdidi vlnlvkspvk
      181 hlsavgskvv sehediaavi lhfengtian isasrctqsk irtlnvtqqd vyitldfsdq
      241 eielhrqats dillrtgeik yrqesiveki fvhkdnplkq eqehfvkcir ketepivygq
      301 sdiqtleiay rilkeihnn
//
LOCUS       WP_010415650             721 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Leptospira inadai].
ACCESSION   WP_010415650
VERSION     WP_010415650.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..721
                     /product="cation:proton antiporter"
                     /calculated_mol_wt=79152
     Region          65..464
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
     Region          508..607
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
ORIGIN      
        1 mnrkavrsvl vyafflivfg lgifvsldlg ksletyvtps vnggterlvp pleilselgk
       61 nlkqpvamli lqllvilgta rvlgsllafl gqpsvigeii agillgpsfl gtfwpeasgf
      121 lfpkeslkii qalsnvglll flfligmeln lsilgkkahd avvvshasil fpfflgtays
      181 ltlygdlapk gisflvfglf mgiamsitaf pvlarivqer gltktplgtl vitcaaaddi
      241 tawcilagvv aiaqagtfag giitlglavi yviimifivr plmrkissiy pskealrrpv
      301 tafvfmiwll sayateaigi halfgaflag vimppqqefr rmlsekiedi slllllplff
      361 vstglktqig llnsgnlwwi cfgvigiaia gkflgstvaa rlvgqnwkds laigalmntr
      421 glmelvvlni gydlgilske ifammvlmal vttfmtgpil dildlkffsr vaepptakrk
      481 illsfaapss gvrllelvsy lfpeakkknp dteitalhvt ssgdltpiea etiekevfss
      541 leekgrelgw sfkriyknts lvakeilnqt rqvrpnllli grahsifskk dtvgrvrfiv
      601 ensqfpvgil idrgfkgark llflfsgnrd aflreyfeff snlsgkesti lwtdglapkw
      661 atslpkkssr hrvrllqkpe seltqedwnp ydlilaswdy yreiestela srlpsililt
      721 s
//
LOCUS       WP_010415680             240 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira inadai].
ACCESSION   WP_010415680
VERSION     WP_010415680.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..240
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27508
     Region          41..192
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mndknlaevy hcyidnesae ketsssvrgr enligrdlpl rkskeriiaa alqlfsekgf
       61 fethipdial rakigvgtiy rnfrnkdhlf nesfrkclfe flsflekevg ersdrrekff
      121 llwtgigsff kerpseflfl nrffcsahld aesqrdflgl klklavyfrs dyaedfsdic
      181 aslvigsflg lvrlqsnesg gpdqriirra aeilwggfsq mnglnesqit rsedvdktlg
//
LOCUS       WP_010416009             444 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Anaerophaga thermohalophila].
ACCESSION   WP_010416009
VERSION     WP_010416009.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..444
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48381
     Region          11..437
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mrdltygpeg rlifrfaipl iignifqqly nvvdsiivgk ilgeqalaav gasfpviytl
       61 iafvigigsg atvvisqyfg arsyeevkra igtfyififf asivlsaagi ifsheiftll
      121 kigsdimpea isyfsvyllg lfiyfgfyst asilrglgds ktplifftis tlanigfdll
      181 fiivfewgie gaalatiaaq ggafmsaili lnrrqhlihf srksmvfdwe ifkksvrigl
      241 ptgfqqvfia lgmmalirii nnfdttvlaa ytaasridal tsmpatnlas alaafvgqnl
      301 gagqlkrirk gvratlfmsw glslgvmliv ilageglmsl ftdnkeviky gkdylviiss
      361 fypvfatmft mhgtlrgagd tlipmfitmi slwivripla aylsaqigvv giwwaipcgw
      421 sigligtisy ylsgkwknkg vagk
//
LOCUS       WP_010415883             290 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Anaerophaga thermohalophila].
ACCESSION   WP_010415883
VERSION     WP_010415883.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..290
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31686
     Region          4..289
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mglniivlak qvpdtrnvgk damkadgtvn raalpaifnp edlnaleqal rlkdkypgtk
       61 vtlltmgpgr aadiireglf rgadggvllt drafagsdtl atsyalscti raikdydlil
      121 agrqaidgdt aqvgpqvaek lglpqvtyce eiysaekgki slkrrlergv etiecpmpav
      181 vtingsaapc rprnaklvmk fkhaqtvter qnrsedyidl tndrpylnid ewsvddiesd
      241 reklglsgsp tkvkkienvv fqakesrhiq andeeieelv kelianhtlg
//
LOCUS       WP_010416011             297 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Anaerophaga
            thermohalophila].
ACCESSION   WP_010416011
VERSION     WP_010416011.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18916493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..297
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34251
     Region          4..69
                     /region_name="HTH_MlrA-CarA"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators MlrA and CarA; cd01104"
                     /db_xref="CDD:133379"
     Site            order(5..7,21,38..40)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133379"
     Region          92..261
                     /region_name="MtbC1"
                     /note="Methanogenic corrinoid protein MtbC1 [Energy
                     production and conversion]; COG5012"
                     /db_xref="CDD:444036"
ORIGIN      
        1 mavysikdle kisgikahti riwerrygli hpkrtstnir yysdeelkkl lnisilnqng
       61 fkiskiagld ehqlrdrvld lcidarnnnv qietlmvsml elderkflnv lsgavikygf
      121 edtveqilfp flerigmlwq agtinpaqeh fisnlirqki ivaidnemqn iavkgpriif
      181 flpedelhei gilfysllar kegldvvylg msvpladlkl vhqvrpaday ftsfvtarek
      241 nelegllqql rdyfpevpfm vtgmqikelh prlpndfsvi ssiktfkeni rllmfsd
//
LOCUS       WP_010416192             304 aa            linear   BCT 01-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010416192
VERSION     WP_010416192.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..304
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33701
     Region          42..286
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mglfdwfkkh nekpeeekee ksseveedii pasnenkynh eigialsggs argfahigvl
       61 kaldengmsp diisgtsmga lvgvlyaagh spdhilqlvk kdkiynmvsl rfgqngffel
      121 davrrilkee ipqddfsalk kpfylsvani sdgqnevkge sgplydyvia scsvpvmlvp
      181 qvidgktyid gglfdnlpag aikdkcqtli gvhvnyngpm ekldgmrdia qrtfslgieq
      241 nvvesrkmcd fmiepeemkk ftfldfdkad elfevgynaa lklikeelap vlrkdkieee
      301 eagi
//
LOCUS       WP_010416200             212 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira inadai].
ACCESSION   WP_010416200
VERSION     WP_010416200.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23642
     Region          13..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpakkktkkp erayhhgnla etlkalalkr leeskdsaft vreiareagv shaaayrhfp
       61 srrdllaeis kdgfigitka fleaeakaip gdsidrleki giayvsfcve npgyyramwh
      121 tdlgpkddll elqeagrkaf lrlwetvlac yeeqvsdyqp veiasaawsi vhgfstline
      181 qqltnnlglt rnsakdaakt lvrllmsgir kr
//
LOCUS       WP_010416208             128 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF423 domain-containing protein [Leptospira inadai].
ACCESSION   WP_010416208
VERSION     WP_010416208.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..128
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13754
     Region          22..128
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mefknsknlp lffaaffgft gvafgafgah glkailspdl liifetgary qlihsvvlvi
       61 lalsnkwses kelrigywli fsgilifsgs lytlsitgik vlgaitpfgg iafllgwgfl
      121 gysgikgr
//
LOCUS       WP_010416219             601 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010416219
VERSION     WP_010416219.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..601
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=69346
     Region          3..589
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mnnlnygivg ngksaalisd kgsvdwlclp kfdspsvfas lldkekgghf siisvagaei
       61 tqryefhsni lvtrfecadg tfeihdfmpr yktdngsyyi ppdliryikw iegkpkikiq
      121 fdprleyakf gtnitfngky vkaytskgsy dslylytsmd klsvvgqlpi tiekdefili
      181 synqkllaqt israylklqr tkvywlnwae rttrfkkynd eimrsalllk llsyqksgai
      241 laavttsipe tigeernwdy rfcwirdasm vikvmtklgh fnvahrylnf iidllpdkge
      301 kiqimyging ekklteyelp hlsgyedskp vrignaaykq kqndiygilv dviyqlfhlf
      361 atslehseel wtitrniikv vetnwqkpdk giweirhstk hftfskvlcw vaadrgikia
      421 ellhqkeyiq swsrlrnkik ndilknawse kkqsftqayg iedldasall mesfgfldgn
      481 dpkfrstvka iqkeleykgl mfryknrddf gqpssaftic sfwlirslyi igekeeaqrk
      541 fdellkysnh lglfsedldf eskrllgnfp qayshlalid vamllaggem sseekilgni
      601 g
//
LOCUS       WP_010416273             345 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Anaerophaga thermohalophila].
ACCESSION   WP_010416273
VERSION     WP_010416273.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..345
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37538
     Region          <4..345
                     /region_name="trifunc_aldol"
                     /note="KHG/KDPG aldolase/sugar kinase fusion protein;
                     NF041633"
                     /db_xref="CDD:469516"
ORIGIN      
        1 mskkrvvtfg eimlrlstpg flrfsqatsy nanfgggean vavslanygi esrfvtrlpn
       61 ndlgracrme lekygvdtsk ishggerlgi yfletgavar pgkviydrah ssfatvgsgl
      121 fdwdeifrda dwfhwtgitp avsqgaadac leavktankk gitvscdlny rknlwkygkk
      181 anevmpelvs gcdivlgnee daemvlgikp egvditsgqv eaeayrsvsq qimkqfprvk
      241 kvittlrgsi sashnswsgv lydgknlyta ptyqithivd rvgggdsfmg gliyglltyn
      301 ddekalrfat aasclkhtih gdfnqvtvee veklaggdas grvsr
//
LOCUS       WP_010416281             360 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Anaerophaga thermohalophila].
ACCESSION   WP_010416281
VERSION     WP_010416281.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..360
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39713
     Region          20..334
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(44..45,48,101,120,122,154,187,299,302)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(264,275,290,299..301,304,326,330)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mniiqlrkdc kyamvvptsm gvritpengq pvhssdiykm qatsaetnva sissylglpv
       61 kvlttfvkgs pvaafiksnl rsrhmdyegv eveqggpwgy rhqfniadsg yggrgprvhn
      121 dragevgrtl nakdfdleri fgkegvqivh lsgliaalsp dtgnfclela raakkhgtvi
      181 sfdlnyrasf wegrekelrd ifseiasvsd vligneedfq lclgiegpea ggkeiadkid
      241 sfkemikrvk qtfpnasvfa ttlrqvisan ehlwgaimlq gndweviepr pirvldrigg
      301 gdgfvgglly gilrgwepek wvqfgwatga lattfltdya qpadeemvws lwsgnarvkr
//
LOCUS       WP_010416317             614 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Anaerophaga thermohalophila].
ACCESSION   WP_010416317
VERSION     WP_010416317.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 614)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   5  (residues 1 to 614)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 614)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..614
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70973
     Region          49..496
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
     Region          <352..545
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mrnivtyfli tvfgififtg ceddlletet kssyttdvvf snpaftlnal ygiyslmtld
       61 emysqkipfy aslnsdievv afgtgdyadn grrgignyla tpgnneiarp wnalyraier
      121 anilieevpk spvmegdnee akrkmwtyyg ealtlralfy fdlvriwgdv pfkveptqpd
      181 gsnfflgktd rdeilesiie dlqeaeqyvp widqsdagtp eriskgfvkg lmarvalyrg
      241 gysvraesnt mergsnwehy yqiardqcke imdegvhsln psfkdvfirq nqlepdrqyy
      301 eslfevghgm trsgeagyys gvryetssky grrnqggelt lphylysfep edarryvsva
      361 fysyneqpqm eiytdpsqfr fakwnikwmt dayiaanrna gnklltginw clmrysdvll
      421 mfaeaenaln gptaeakeal kevrrrafpt evhaekvday vdglsspedf feaivderal
      481 efggesirkf dlvrwnmlye kitearelnr kivygeapyd yvpqylyyqy reddpedlnf
      541 etlnldeelg dinmpdfdrv ewmsgrseee kqefidwlnl mssgldqypn rhllpiaqpv
      601 iddangaftn eygy
//
LOCUS       WP_010416348             123 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Leptospira].
ACCESSION   WP_010416348
VERSION     WP_010416348.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..123
                     /product="VOC family protein"
                     /calculated_mol_wt=13439
     Region          6..118
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 miivegidyi viptgdldss vkfyselfdf etieertgef aiigldsvni kllhtngtkg
       61 alseakspvl sfvldvddft eaivelesks vqivrgpear dggeflhfld psgnileiny
      121 kes
//
LOCUS       WP_010416487             146 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010416487
VERSION     WP_010416487.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..146
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=16735
     Region          39..146
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 maivrrfnnq vpdianifdd ffggdffdtp arrtstpavn vkenddeyvi evaapgmkkd
       61 dfkveidngv lsisaeveek deqkdedkgy trreffyssf nrsfaipkde vdeskidaky
      121 kdgllritlq krdevkpkpa rmieik
//
LOCUS       WP_010416578             331 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Leptospira inadai].
ACCESSION   WP_010416578
VERSION     WP_010416578.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..331
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37364
     Region          <198..328
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mnlksyfali yyrlrykyqd lklkldlkva nwnkkgrerl tvmviphseq ktinfhisyr
       61 aitifvgtil vlllissvnv lshsgsihql telnlsnqdf irqsakmkee inslhehvey
      121 yhthvgalyg rltgdsskva kgiggaeklt sngsskdgsp lppgaevfrl kedvhnlkva
      181 neltqeiisi lkkrksvirq tpsiwpvrgy vlypygeyln pitarremnn gidigafpgs
      241 evvaaapgti yeigytrhtg yfvkvahkfg wktiysnldr ikvkqnqqvs kaevigfvgk
      301 senspqyslh yeihvgtrai npfaflnqiq d
//
LOCUS       WP_010416580             270 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Leptospira inadai].
ACCESSION   WP_010416580
VERSION     WP_010416580.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..270
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30639
     Region          4..259
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mysiidthch ldivleqgqt idqslrnake sgikkivqig idlessvrak glseeysdsd
       61 idifytigch ptetnefpkk eeilsyiten lddsrlsaig eigldyyhda sskneqievl
      121 hsfldashry rlpvvihsrd agedtiailk ehrdkafgvi hcftydysia krlvdlgyyi
      181 sfsgilafkn ardiqeaaek lplealliet dapflapppf rgkrnepaft kfvlekmfsl
      241 rkesnievek ilfansekfi qrkpfyhags
//
LOCUS       WP_010416568             253 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Leptospira inadai].
ACCESSION   WP_010416568
VERSION     WP_010416568.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..253
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27469
     Region          3..252
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgkivsisnq kggvgkttts inlaanlaai gkkvlivdfd pqgnsgsglg leintlpkts
       61 yelligecsa necirrtdle nlhiipsnin lsgaeadlla eenrefrlkd airllrmeyd
      121 yilidcppsl gvltinalca adsvmitlqt eyfalegltq lmkiislvqe klnpsleleg
      181 vlltmydkrt nlaqqvaedv kayfkdkvyt tviprnikls eapsfgksil sydpegvgaq
      241 syrnlaleva gkn
//
LOCUS       WP_010416830             190 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Anaerophaga thermohalophila].
ACCESSION   WP_010416830
VERSION     WP_010416830.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..190
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22178
     Region          3..177
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mqeeklftel skgnkrvlde iynryhqkif gfalsylkne ddaydivqev finlwnsrss
       61 lkkdtriepf iftatknavi slfrkrateq kyleylgntv isnnmgtneq idynfleely
      121 eslisqlpek rreifilsrk kgltnkdiaa nlkisektve nqltralafl kehfsaagfl
      181 gllffhlfil
//
LOCUS       WP_010416860             759 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Anaerophaga thermohalophila].
ACCESSION   WP_010416860
VERSION     WP_010416860.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..759
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=86765
     Region          25..757
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mrpskillma lvvmlmlllp gnvfpgekep vdyvnpymgn ishllvptyp tihlpnsmlr
       61 vyperndytg drlgglplvi tshrgssafn lspyqgdese mkpvidfsyd feevtpysys
      121 vyfdeqetfi dfglshqsai ydvrfqndap syliinstng alkwdghllt ghqivsseig
      181 gnqtniylsm qpenlpetvy vlddgellek teaegedacl vlkypkgtnn lkirygisli
      241 dtdqalqnme revagnsisq lhkegrkiwn ealgkidikg gsdddktvfy tslyrtyerp
      301 vkiseegryy safdgkvhdd ngtpfytddw iwdtyrathp lrviiepele tdiinsflrm
      361 aeqmnhfwlp tfpeitgdsr rmnsnhgvat iidsyrkgld gfdlerayea srraitektl
      421 apwsgapage ldefykehgy ipalrpgeke yipevqehek rqpvpvtlgt aydewclaqi
      481 aqelekeddy krflsdayny rnlfhpethf fhpkdsagef iqpfdyrfsg glgareyyge
      541 nngwvyrwdv phniadlvdl mggpekfean mdsmfaeplg vdlkfqfysq lpdhsgnvgq
      601 fsmanepsfh ipylynyarv pwktqkrirk lldqwfrndl mglpgdedgg gmsafvvfsq
      661 mgfypvtpgl pmynigsptf eeatvnlpng ktfkviarny spenkyiqfa klngetwnkp
      721 wfrhqdiaeg gtlelfmgky pnkewgvspe dvppsfsmd
//
LOCUS       WP_010417087             460 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Leptospira inadai].
ACCESSION   WP_010417087
VERSION     WP_010417087.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 460)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..460
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51130
     Region          39..253
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          156..460
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnflfsrtpl vllltsryir gsraagllsl ksrvsfvvma vgvsllivvl sifngfqrqv
       61 keslwqggsh itiesnsgag eitdyqkiis wiektpelkq rivsveggiq shgliqnynt
      121 fypviiravp vsnvddlllt rlpnfprvvh ynrdelaqmn renyivigke meglynfslg
      181 rqltlavpgg rfslgkgvev svenfrvsgf fktgnyqfds ryvymslpia qrffklrnsv
      241 nqitlkvksl ddlsyckrkl lrlfgepdfe revevsssls vrtiaeeqen flaalklekt
      301 iisiivflfi ilaalgmvas vyslvrakrk sigvlkalgl pssdillift lnamlvgila
      361 sliggvtgif lansleniin gieeimnmlg pdisvlfgae wspvelvpkr iyyfdkipvd
      421 idiafifmvt taatilsgia gyfparwaas lnpvdtirnd
//
LOCUS       WP_010417101             106 aa            linear   BCT 01-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Anaerophaga thermohalophila].
ACCESSION   WP_010417101
VERSION     WP_010417101.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..106
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=11628
     Region          1..106
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 mlkmivsgal gqdaeirevg kkkainfdva vsmdykdqqg nkvertewvk aviwkndgqs
       61 tkvadflkkg rkvllegvps segfkskdgd iksalnlnvk dlefls
//
LOCUS       WP_010417138              96 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Leptospira inadai].
ACCESSION   WP_010417138
VERSION     WP_010417138.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..96
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11060
     Region          2..94
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(13,15..17,25,48,50..52,54..56,59..60,82,86..87,89)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            51
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mrdnseviei kpeltalfnd yyafrnqlmd aiakkpkriv lnlgkipvmn sisisslvwf
       61 cknaksdgie iqiqeihpdl mktfevlkid eyfqqi
//
LOCUS       WP_010417208             262 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Leptospira inadai].
ACCESSION   WP_010417208
VERSION     WP_010417208.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..262
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28506
     Region          5..236
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mpirsdllpl fesisreage kilnyfdgks eyslkdpmqv ltdadiashe vlfeslhref
       61 sgipivleeq enseplptsy ivcdeldgta lfsrgmsefs vimayvedgk pvagciyfpa
      121 masivlserg kgttvddhki vfreksdlsh svvsleinnt ltnedfswia nvvknslasr
      181 slaatgagfr elllgktdlf lnfngakvwd faagavaiee aggillnkeg kplewdkirm
      241 sgvickdssl assvfrlkpg gs
//
LOCUS       WP_010417183             111 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Leptospira inadai].
ACCESSION   WP_010417183
VERSION     WP_010417183.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..111
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=12180
     Region          3..111
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mipkelktrl darksgdddf ylldvrnpne qeicliegtd llipvtdlpa hiaelepwkq
       61 sgkdiivycr sggrsgsaca flksagyakv fnleggilry sddvdstlak y
//
LOCUS       WP_010417187             205 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira inadai].
ACCESSION   WP_010417187
VERSION     WP_010417187.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23518
     Region          11..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtlvatrpkr rtrnslnkqt ivqaameilt edgidglsmr riaekldcsv aspyshfksq
       61 qdiikilisq geaqltetlr eaklqgknay ekltriarty yefsgnnqel hkvmfntvhg
      121 hmhrkafpkl ptsyrvflet iregcrsgef iiteeeypsl artmyswmyg iivldmtgml
      181 kkrgmgdpld egflffrkil lgdei
//
LOCUS       WP_010417216             113 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Leptospira inadai].
ACCESSION   WP_010417216
VERSION     WP_010417216.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..113
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12255
     Region          6..104
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(22,24..26,32,55,57..59,61..63,66..67,89,93..94,96)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            58
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 manltfnekl egsrlilkva geidaktapd lklklesavg ngvktivcdc taltyiasag
       61 igvlnsiqkf lkeksgeivf cslkkevkdt melmyftkkv rifpnleeal siv
//
LOCUS       WP_010417218             143 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Leptospira inadai].
ACCESSION   WP_010417218
VERSION     WP_010417218.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..143
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16646
     Region          11..136
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mnshkekvyl frndfdelak vrneirsflg edcpdlikgr ivfcldeavt nviehglpen
       61 ekstielkmr knkgswrfsv tdegiffdpt kvkseswkel yesgadggfg lrsikkimiv
      121 ryqrlknppr nrltlihtre rnd
//
LOCUS       WP_010417225             138 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Leptospira inadai].
ACCESSION   WP_010417225
VERSION     WP_010417225.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..138
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=15377
     Region          1..>88
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mkplilvvdd ndryadnlkt ylenlncdvl ravdaaqgwe yytknkdkls avitditmet
       61 qtsglwlirr ihkdgfkgvk viattgfdvf gvmtvsrlll ptfagigfmi pkvplkvgkv
      121 lmlptgliqe tfelsirk
//
LOCUS       WP_010417313             219 aa            linear   BCT 01-JAN-2025
DEFINITION  precorrin-8X methylmutase [Leptospira inadai].
ACCESSION   WP_010417313
VERSION     WP_010417313.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..219
                     /product="precorrin-8X methylmutase"
                     /calculated_mol_wt=23494
     Region          6..212
                     /region_name="CobH"
                     /note="Precorrin-8X methylmutase CbiC/CobH [Coenzyme
                     transport and metabolism]; COG2082"
                     /db_xref="CDD:441685"
ORIGIN      
        1 mndmrqmtsl grniedrsfq iideeagmhs yppadweivr riihatadfe fkdltkihpe
       61 aassgiaalk rgcsiicdvq milaglnrer ldaygckths fisdadviqk akeknstrai
      121 esirkaselg lldgsilaig naptalleiv rliesneakp sliigvpvgf vsaseskesv
      181 malqgsipyi itrgrkggst iavailhall llsakgspv
//
LOCUS       WP_010417425             795 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Leptospira inadai].
ACCESSION   WP_010417425
VERSION     WP_010417425.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..795
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=88277
     Region          21..679
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mnkerifrti ssllnsaken wksilkygtv igliiaafli ggsyvvwltk qddvirnlet
       61 fqkevsnayd pnqskpiril dkngkligef srrkfkpirt dnlnnhgnii wallssedqd
      121 fydhggvnyt sliraiivnl ttfrkqggst itqqlakltl dlgarnifnk ltefyctfyl
      181 enrfdkktil amylnriflg egntgveeas ryyfnkpaye ltpaeaallv gtipapsnyn
      241 avrnpkiafk rqrmvlflma enkslhpnpn aiekdferki dsnirkfktf ykveetkeed
      301 dklsvtseig kygfdkdfni nlapdfnfsv rqfvienfse mdletrglnv yttldydkqe
      361 aaekalregi egvrkklsde kaaylkagkn eeaaiqkkiv enmngslisi npsngyveal
      421 vgsykisnif rmnravsavr qpgsvikalv yllafekrvi tptsvvtdee ikirgyspkn
      481 wyagyrgemq arvafaqsvn tvavkllnev gvgifletlg kilsldksel dkrfqpnlsl
      541 algsgelspk elatiyatia nlgkkvkpie ilritdyegs elfsippvna seaeqildpv
      601 acamvlnlle avvseegtmk iglkgedrfp mggktgtvqs pkearkrwgn rkgvrdawfa
      661 gvnpnlvttv wigndagapf pgsgsgisgs vwykyvsyva rtigfgetli ppfngdfvkv
      721 dicadtggll ageadclhpl hgqyfyigdq pastaaipik eggeitgths sealsgedsv
      781 elempeaked rtddp
//
LOCUS       WP_010417441             112 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: STAS domain-containing protein [Leptospira].
ACCESSION   WP_010417441
VERSION     WP_010417441.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..112
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12434
     Region          1..99
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(17,19..21,27,50,52..54,56..58,61..62,84,88..89,91)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            53
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 meitvqddih iikisgsilq sdseeldrnl sdhnfdpspk viidltevsh icstalgilv
       61 sykkkfnsae gdiiivvnde dllqlfeitm ldkvfkvvpt iddafdefkl gn
//
LOCUS       WP_010417510             199 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Leptospira inadai].
ACCESSION   WP_010417510
VERSION     WP_010417510.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   6  (residues 1 to 199)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   7  (residues 1 to 199)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   8  (residues 1 to 199)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..199
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21609
     Region          24..198
                     /region_name="PRX_like1"
                     /note="Peroxiredoxin (PRX)-like 1 family; hypothetical
                     proteins that show sequence similarity to PRXs. Members of
                     this group contain a conserved cysteine that aligns to the
                     first cysteine in the CXXC motif of TRX. This does not
                     correspond to the peroxidatic...; cd02969"
                     /db_xref="CDD:239267"
     Site            59
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239267"
ORIGIN      
        1 mkrafflfsi lsifvyslsa mkpgdmapdf sekdisgklr nlsefkgkfl vlewhnqgcp
       61 fvkkhygsgn mqklqkevta kgivwlsvis sapgkqgyvt peeekeylkk sqaspsavlf
      121 dsdgtmgkay gakttpqmvl ispqgkilyn gaiddkpstd qsdipsakny isaaideala
      181 gklisvstsq pygcsvkye
//
LOCUS       WP_010417542             276 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010417542
VERSION     WP_010417542.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..276
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30652
     Region          12..274
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 menvknwfsn pelimtfvik yggqllfaii tliiglwiis llmkgmkkmf iardvepglq
       61 sfllsvsria lkimlfisvi smlgirmtsf iavlgaagla igmalsgslq nfaggvmili
      121 fkpfkvgdyi taqgesgtvk eiqifhtiln spdkktiilp ngalstgslt nysteprrrv
      181 dftfsigygd didkakevim giinrderil kepepfigvi nlgnssvdlv vrvwanatdy
      241 wgiffdmqet vkkefdkqgi sipfpqqdvh lyqtrq
//
LOCUS       WP_010417629             119 aa            linear   BCT 01-JAN-2025
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Leptospira inadai].
ACCESSION   WP_010417629
VERSION     WP_010417629.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..119
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12800
     Region          2..108
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 metleinvlk gkkcascgfe mtepavactr cgsdslqekv fsgkgkiyty tvvhvgfghl
       61 asrapyvlav idleegpktm gilegrsegk pvtesvridm pvtfdrtepk tgsifkpte
//
LOCUS       WP_010417712            1073 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Leptospira inadai].
ACCESSION   WP_010417712
VERSION     WP_010417712.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..1073
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=116385
     Region          40..1068
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msqknkniqt lpirsesssp ndvapdsyae avqqvnqagi aafsvknphl mivsciivlv
       61 lgvlalfqmp rdllppskqp avqildvywg mptsstetil twkferytgq apglihqesk
      121 sypgvsvvnn ffdedstsrp eamastvgyi msvlrrlppg amppivlpfd pmgstpvclv
      181 avsgdfevne lydrgqydvr ralqgtpgti aptvmggaek qviieldplk lkqydmsaae
      241 amdkigrlnt fipagdvkig dfdypiytng vadsiqafdd fplrsregvs vfvknvgktk
      301 essivqtemv tlngkeivyv pvlrqqgant lavvdaarea mkslekeikg lklnivadtt
      361 vfirkavetv geeamfgggl aalmvflflg npratfatll slpfstlfvl mglkatgsti
      421 nimtlggmal sigllvdnsi vaienimrhl aedkdpnrir vvvraaqevt ppiiavtlcn
      481 vvvlfpillt kgvvnvlfga iaktvmlait gsllsetaii plfasrfltg eppklpkffq
      541 viqdliaglt eiygralekv mtktravvig icilfaigaa alpfigtelf pradagsfvl
      601 hlrlpsglri eetsekakqv eaklkewiks dlemvlsdsg lyqgfpaafs qnggtqdvtm
      661 tvelkenrkk tsqyyariir eklpqefpnv digvelggll ssslnggaqa pinvqvkgsn
      721 agkayeiaks llpdikavkg atdvrilenf dtpaievnin rkkadaqgvl tdeivqnivs
      781 alagsivykp tiwvdpksgi dyalgvrfpe ekfqtmkdfe nipvtgkfqe raiplsqlsd
      841 ieqtqgptvl srvnmkrtvn imldsqdrdv gsvsseieki iksvkvpdgy kiaitgeiek
      901 mrdalsqlgg gfflsaflvy milvvqfrsf llpgimmltv plgmigialm fsitgtyysl
      961 qagigtifli giavsngvll iefilhmieh ekmnldegii agakarlrpi mmtslasmlg
     1021 ltpmaigfgk gaeaniplgr aviggqflat lltlfvlptv frylyrkfyl kgn
//
LOCUS       WP_010417875             214 aa            linear   BCT 01-JAN-2025
DEFINITION  class II aldolase/adducin family protein [Leptospira inadai].
ACCESSION   WP_010417875
VERSION     WP_010417875.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..214
                     /product="class II aldolase/adducin family protein"
                     /calculated_mol_wt=22927
     Region          6..183
                     /region_name="AraD"
                     /note="5-methylthioribulose/5-deoxyribulose/Fuculose
                     1-phosphate aldolase (methionine salvage, sugar
                     degradation) [Amino acid transport and metabolism,
                     Carbohydrate transport and metabolism]; COG0235"
                     /db_xref="CDD:440005"
ORIGIN      
        1 mknlgfkavr dsvvtasrkl adlgffagig gnlavrvdpe lmavtpsasd yysmknedic
       61 ivrmkdlklv egdkqpttes gmhaafltlr pdlqvslhth qplasavtll gidmpiegae
      121 araslgaslr lvsyapsgti flvnafkkkv rkdtngyllr nhgivcgaks ieqaienvll
      181 aekqsahflr sriknnagvs gisplvirqa lsil
//
LOCUS       WP_010417920             188 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010417920
VERSION     WP_010417920.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..188
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=21260
     Region          <1..188
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; cl46157"
                     /db_xref="CDD:480497"
ORIGIN      
        1 mfairyyykn lkwehikkly pyaltgivla livggmisdn qfrniigisv llclalifyr
       61 dfsggpngft rkswfartlg ftggfatmig naagpifnly llsmrlpkks fiatgavfyi
      121 slnllkiplh ffvwksisld tlqlnfvmlp avwigsmtgk ylvrfipere frifvtvvia
      181 isavllff
//
LOCUS       WP_010417945             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Pseudomonas syringae group].
ACCESSION   WP_010417945
VERSION     WP_010417945.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 181)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..181
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20135
     Region          19..175
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04697"
                     /db_xref="CDD:467578"
ORIGIN      
        1 msipaneaah raasdaeqia wvdeqdrllg slvradlrer gligrgtyil lfnsqgelcv
       61 hrrtlskaiy pgywdvaagg mvqadesyaa saareleeel gvngvplqah eqfffdqpgn
      121 rlwcavfsav wdgplklqpe evlearfmpi aevlqeaehn pwcpdslaal krylkqiene
      181 q
//
LOCUS       WP_010417992             248 aa            linear   BCT 01-JAN-2025
DEFINITION  uroporphyrinogen-III synthase [Anaerophaga thermohalophila].
ACCESSION   WP_010417992
VERSION     WP_010417992.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schubert,H.L., Raux,E., Matthews,M.A., Phillips,J.D., Wilson,K.S.,
            Hill,C.P. and Warren,M.J.
  TITLE     Structural diversity in metal ion chelation and the structure of
            uroporphyrinogen III synthase
  JOURNAL   Biochem Soc Trans 30 (4), 595-600 (2002)
   PUBMED   12196144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..248
                     /product="uroporphyrinogen-III synthase"
                     /EC_number="4.2.1.75"
                     /GO_function="GO:0004852 - uroporphyrinogen-III synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006780 - uroporphyrinogen III
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0033014 - tetrapyrrole biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28389
     Region          1..224
                     /region_name="HemD"
                     /note="Uroporphyrinogen-III synthase [Coenzyme transport
                     and metabolism]; COG1587"
                     /db_xref="CDD:441195"
ORIGIN      
        1 mkikkilvsq pkpstpkspy fdlseknnvk idfrpfiqve gvsskefrqq kinildhnav
       61 iftsrtaidh ffriceetrv tvpddmkyfc iseatafylq kyivyrkrki fhstgkfpdl
      121 vevikkhkqe kflvplsdih kpeipnlltk akvkftkail yrtvssdlsd lkdidydvlv
      181 ffspsgiksl lqnfpdfkqn dtliasfgpa takavkeagl rldiqapmpq apsmtaalem
      241 yikkhnkk
//
LOCUS       WP_010418027             338 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010418027
VERSION     WP_010418027.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..338
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38070
     Region          6..257
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mhtelirfgi igcgrianrh akhianngql aatcdidiek agnladeygc kawsdtekfl
       61 tenkgkmdvv svcspnglha dhtiaalrhg yhvlcekpma isvedcgnmi neaehanrrl
      121 fivkqnrfnp pvealkkaie edrlgkifnv qlscfwnrne syykesnwkg skemdggtlf
      181 tqfshfidll ywligdvksv rsftrnfthq niidfedtgv vamefyngai gtinytvssh
      241 qqnmegsitv fgdkgtvkig gqylnkleyq nikdfrienl vesrqpndyg tyqgsmsnhd
      301 kvyenlvsvl tregviatng feglktveii dkiyskak
//
LOCUS       WP_010418030             487 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010418030
VERSION     WP_010418030.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..487
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56038
     Region          8..407
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mqsqtrfifk qgiiygigni vvklsgvili plylryines eygvvtlfet ifqfililss
       61 wgvkggfmrw yhdmdgdrek kklffttysf nfittlltvl vvgfvifrfs deifhyelsp
      121 siilyfisas ffrlmfempq yllkieqkav aqtwwvflnv vlligatfyf levkkmgleg
      181 iylaqlvahl vtflmfiplt irnidlgfnr svlkemlhyg lplavsnilt tvltlsdrhm
      241 inqyqnlgev agygmafkvs nlvqmvivas fitgytnyyf ktmnepdsrr fyekivryfm
      301 vvisfgglgi vlfspeiiyv vtmgseffqt svvivpvlmv gmifsamrqi ftlplnkhkr
      361 trrislilil savinlignf ilvpsigkmg asvstvvaqf favawffiev rktepfrfsl
      421 psnfallviw gvlvytgmhl phwpffslvl lkvtlllffa galfatghik reeftelkri
      481 yrkvrgh
//
LOCUS       WP_010418058             242 aa            linear   BCT 01-JAN-2025
DEFINITION  M48 family metallopeptidase [Anaerophaga thermohalophila].
ACCESSION   WP_010418058
VERSION     WP_010418058.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..242
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27951
     Region          1..242
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mpvktslihi dgigpvlfks drrckrlsir ikpfegvvvm fppgysphka lafveakksw
       61 irknkariee qekavtifde ttnfrtrsfq lkiekaprdd vrlilnsgvl kvlypqhinv
      121 adapvqnair ygieevmrie akmvlpikvr tfarqyhfkf nkvfiknmks rwgscssvnn
      181 inlnlhlmrl pehlvdyvvl helchtvekn hgpgfwrlln eltggkaktl aaemrqyrtt
      241 ly
//
LOCUS       WP_010418083             304 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Leptospira inadai].
ACCESSION   WP_010418083
VERSION     WP_010418083.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..304
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33536
     Region          98..296
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mgetpkrils aavlvvlylf mifyrdfyyl qtlillgvgg vigltefyrl sdrqqdgrpf
       61 kgtgiffflv illlyyfrfv aaqnkfeapm vfqrnfkffv ppfdavifaf vllfitsfvl
      121 qilrrpldga ifsvsstvlg vfyagvplgh lllllgmndg iyyiflvsva tfltdvggyf
      181 ggrwfgrnpa glaispkktw egyvsgiiia alsvfllnyi wekntgvptp vggaevllis
      241 lilsivgvig dllesamkrd akvkdsgnli pghggildra dallltvpml yfylqikgal
      301 gfpv
//
LOCUS       WP_010418212             372 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Leptospira inadai].
ACCESSION   WP_010418212
VERSION     WP_010418212.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..372
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41773
     Region          10..369
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 msqstleyal anrirglnss airkafelag tlkdpinlsi gqphfpcpen iieagvkalr
       61 dgktaytlta gipqlreals lkyrkensip yatpervlvt sgissaflll fnallnegde
      121 clvvspyflm ypeyikiygg rmhtisenfs pedlspfkdk rlkiiifssp snptgtilsk
      181 dqltsladla ertgaylisd eiyekfdydk qfhsvgsfye kaitlsgfsk tysmtglrla
      241 silapepiik tlttlqqytl vcapsvtqwm giealktdmn syiadyrekr dfvyenlkdf
      301 yevkksqgaf yfflkikdrd edfigravke kglilvpgyi fvdspnyiri sfasewdnlk
      361 rgitalrela ga
//
LOCUS       WP_010418230             161 aa            linear   BCT 01-JAN-2025
DEFINITION  CAP domain-containing protein [Anaerophaga thermohalophila].
ACCESSION   WP_010418230
VERSION     WP_010418230.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..161
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=17926
     Region          9..160
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
ORIGIN      
        1 mkkalisvlv fslgvlgiaq sidysdvkid kremlklvne armtrrfcgg krqeavpplq
       61 wnaklakaaq khaddmadnd ffdhigsdks tvvmriehed ylwmavgeni amgprsvkev
      121 vegwlespgh csnimngeft emgaalshdg kywvqvfatp r
//
LOCUS       WP_010418409             231 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Leptospira inadai].
ACCESSION   WP_010418409
VERSION     WP_010418409.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..231
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25775
     Region          6..224
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mknkiiltva ahpddeilgc ggamarfaee gheihilila egltsrdlkr drdakigels
       61 elsrcasnag kilgvksvel ldlpdnrmds mdrldiikiv ekkiedvrpg vifthfyndl
      121 nvdhrlanea vvtacrafpg qtvkelyffe vqsstewqir nsagnftpny fvslserqlq
      181 kklsalaeyr semrefphar sleavealak wrgasigfps aesfvlgrki v
//
LOCUS       WP_010418423             208 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Anaerophaga thermohalophila].
ACCESSION   WP_010418423
VERSION     WP_010418423.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..208
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23441
     Region          53..131
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
     Region          152..>204
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkhfistf fallvlaman itfaqsvqvv qndidkapkf rgnpkqvgrf lekymsypde
       61 arigmiegvv evsaiitdqg klmepqisks vdalldseal rlvslmqewk pakkdgqnvd
      121 ckvvikvpfy lseeekelmq tlnehgltek mplfvidnki vkeylevphy nvksirvmkg
      181 qkaierygdd akngvviitt krgtppvr
//
LOCUS       WP_010418528             211 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Anaerophaga thermohalophila].
ACCESSION   WP_010418528
VERSION     WP_010418528.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23375
     Region          1..203
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mywktlfdgi ivgfsasvpl gpigvliiqr tlqngrlsgf csglgavmsd viyaiiagfs
       61 lsyivsfvea qmlwlqlggv ivltalgiki yrtnpavglr rqkkgkhnli kdfvstfflt
      121 lsnplaiflf iaffaifnvf kpqygladhm iiisgvfmga slwwlmltsl vglfrskinl
      181 rrlywinkia gsliislvla afivwlvkey v
//
LOCUS       WP_010418537             146 aa            linear   BCT 01-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Leptospira inadai].
ACCESSION   WP_010418537
VERSION     WP_010418537.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..146
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=15827
     Region          5..114
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 mandinrvtl vgrltrdpef ktvngtslvn fslangrtyv sngekkeeth ffdceawgkg
       61 adiiqqyckk gkqlvvegrl kqdtwetmeg kkasririvv enfqmigake sgggdygssa
      121 atggssyatt sheefgssgt dddipf
//
LOCUS       WP_010418610             493 aa            linear   BCT 01-JAN-2025
DEFINITION  HDOD domain-containing protein [Leptospira inadai].
ACCESSION   WP_010418610
VERSION     WP_010418610.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12095900
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..493
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=55625
     Region          231..425
                     /region_name="HDOD"
                     /note="HDOD domain; pfam08668"
                     /db_xref="CDD:430141"
ORIGIN      
        1 mlnvseyads lssgkeidie yrfisdedhq qiyllllqil ghldrlflte vvstilkell
       61 mnankanakr ifflseglni sdaaqyqrgi krfqeeiihr wdeqepvlkg snfsvrlrak
      121 ilnqnliflv endcpllaqe serikarles askfndlsea fltmsdsqes aglgivliql
      181 llknsgigmd kfkiesdgki tratlvipkq ivplevttkl kdrifteveg lpplpntltk
      241 iislcnnads dlgvianeie rnpalgadll klsnsagfas rnkvntivqa vkvvglknvr
      301 nllyvsgvrk imegrytklq evwnhsnlts ylarqvsqra glvklgdiaa agallhdlgk
      361 fvllaldpnl frklsafqky rdlnnstife eisigishpt lggmlarkwd fppdlvnmie
      421 fhhrpfmayg tiyadlvetv ylanmmsdyt erkvtyyavd snilrkfeld dkqkfeetce
      481 rltkayeian een
//
LOCUS       WP_010418669             319 aa            linear   BCT 01-JAN-2025
DEFINITION  transketolase family protein [Leptospira inadai].
ACCESSION   WP_010418669
VERSION     WP_010418669.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..319
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34477
     Region          9..316
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mgapsvsttd qkatrdgygd alhelgaerk divvldadls gstktnkfak aypdrffnig
       61 vaeqnlvgha aglalagyvp fassfamfls grawevvrns iaypflnvkl vashggitvg
      121 edgashqcie dfgtmrvipe mvvicpsdyn etkqvirait eykgpvyvrv grpnvplier
      181 enykfeigka eviregkdvl iiangvlvne amiavkeles sgiqatllnm atikpidkda
      241 ilkyakvcgv vvtceehnvv gglgsavsef lseeypvril klgmkdtfgk sgtwsglldy
      301 fglrsknive larkaiqlk
//
LOCUS       WP_010418690             399 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Leptospira inadai].
ACCESSION   WP_010418690
VERSION     WP_010418690.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..399
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46246
     Region          100..254
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mgesiidlav pfflililae ayigrkrnvy rwndtitdlg tgilfsltgv fvttgslwiy
       61 eqvrahfsvq hlwgfselpv gppilrevdg wkfrwaetls wlsillavdf iyywfhrath
      121 evhflwachv thhsseefnl svalrqssfq rifeyafnlp laiagvpwwa lllcqgilki
      181 yqfwvhtrli gklgwierif ltpshhrvhh grdpqyldkn hggililwdk wfgtyaeets
      241 epvyglttql gtfnpltanl hvyrdlwnli rlaqnwkdkf llliqkpdwr psllggtkei
      301 plvsrerlqv ydprissgqk iyaivqfiil aaitlfalrf fkkgildvei fllaslwiif
      361 sffslgille grtkailwes lrfaslpilv gyvivksgf
//
LOCUS       WP_010418820             575 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Anaerophaga thermohalophila].
ACCESSION   WP_010418820
VERSION     WP_010418820.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..575
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64107
     Region          <20..179
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mhrihylils svlsviqffn laaqkapsqw hyhfpldevt nvsgsfgeir snhfhsgvdf
       61 ttkgktgwpv yaadngylsr iavspggfgk alyishpngl ttvyghldaf sepidslvta
      121 lqyeresfsi neyftseqid vskgeiigfs gnsgssggph lhfevretag qrpvdplmfp
      181 npvkddirph iagvkiypls adaaingkhe aryfpavfyd gafhlkhnpd ipasgtigig
      241 idvvdyytgs wrecgvhrid lkvddrevys fvidgfffhn trfvnshidy aekvtsgrti
      301 qksfvdpynh ndvyvtdesr geiqmipgdt khlsyvvkdi sgnesllnfk ihaekaltts
      361 gsldkngniy idasqpftfr qngyvvgfdk esfyrdvrgd inirksfvsl tgavitvldk
      421 tipvhktfei kipldsinnk tglcgakfgn nhrleyaggr iedahfvisa recgeylltr
      481 dtvppeisvi nppqsmdyss rneivvkikd efsgiasyda tidgrwslfe ydakndriic
      541 nlkkvpflek gthrlviait dgagnpgkie trfry
//
LOCUS       WP_010418842            1159 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Anaerophaga thermohalophila].
ACCESSION   WP_010418842
VERSION     WP_010418842.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 1159)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1159)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 1159)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 1159)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 1159)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 1159)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 1159)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1159
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..1159
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=132667
     Region          <102..325
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          241..913
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
ORIGIN      
        1 mnklpyiikr ldirkmpgfp gglrpfddls sdinivsgpn asgksstarl iqqliwhkht
       61 igleanasil ldnqewdiki dhgkiqvlhe greesitglp aaegshryfl alqdmvaeed
      121 qnaaetiare siggynldla keelgysdai ftknigefka ldkaiqkyha tlsnqerikr
      181 eensldklyk ekeeaeldrq rssffktlae flnarnaynq intkleqfyp smdkltgnep
      241 eqiekleqqi rhskniieqs nadieektrk lgqltipksg vasavieele nrtenikelt
      301 rtindneeki etlkiqsqea lknidvninp sewegldlnd vgqldrflqr ahnllgrkaf
      361 lnnqmelltq eltnlgeles dgekissgin ilnnwltgqq agketpnwlv pllivlgavt
      421 aiatfffgwp glsgiilmag awifsnlktt kqdtlqireq dyrktglkqp gqwhpddvve
      481 llndlvkdlq kahhrddiir kqkdiekqlr dtnselkqle etrnqlieki ktaphipeis
      541 endytslvwf ienlkkwqks hlellslqtk trhlkselqt elakcnqifs etgsssandi
      601 sqikatlsel krqendrrel vrqiqqseke idnqdkllke arqelseiys rldidegkkg
      661 iirqmteqlk nykslkdnli gakagyqeke rllknhplys dykqetehlt aeealdksee
      721 yarhagnwet iieqikeien avrqiknghe ledvltrken altdledvyh nnisgftghl
      781 iveelkaqtr dqnrpqvfka agelfnritt gryelrldnk eqavftaydt vlkleqplsq
      841 lstgtrvqll lavrlafiek qeetiklpll adellansdd erasaiiqal ieisregrqi
      901 fyftaqddev kkwfsflkse ndihfthval tgdsgisysd nisqispedi kfsysaprpe
      961 eknhakygea lavspfsllt dditslhlwy liddvnllyr clqkgirqwg qlqsfvqnng
     1021 risgldddtw qiicnkaell erfkelytig rpkpvgrdvl mqsglisdtf idavtekave
     1081 lngnpeqlll alkngevprf yktkteelad yftannyide nepmpmddil lklqafises
     1141 gidakdaeef lrmiidnrs
//
LOCUS       WP_010418907             319 aa            linear   BCT 01-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010418907
VERSION     WP_010418907.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..319
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=35723
     Region          24..310
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 maeivvepie ryalsakrrv ktlfskigvv gcgkegqniv riaawhgiev vfielseeki
       61 qnsldnisre ldnrieswgl tsgekraimg rikgsldfqd lagsdfviea iradektglr
      121 sidvrkdvfh kieqvvdrda iiatnsttii itelaseley pdrcvslhff vtspeariie
      181 vvkglyttde vykkvctfvk linrevipve esaglisirl fvtllneace almegvatae
      241 nidktmiigm gmrygafqma diiglnkvek wmenlyeefg gpkykaspli krlvrakrlg
      301 vrtghgffky dangnkiee
//
LOCUS       WP_010419006             433 aa            linear   BCT 01-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010419006
VERSION     WP_010419006.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..433
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=47171
     Region          1..432
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 msdfkfetlq lhagqevdpv tnsravpiyq ttsyvfndse haanlfglke fgniytrmmn
       61 pttdvfekri aaleggvaav avgsglaaqf iainnflqag dnfistsnly ggtfnqfkvq
      121 fkrlgiqvkf vetddpadye aridentrai yvetignprf nipdfeklgq iaakhgipli
      181 vdntfgaggy lfrplehgan vvvesatkwi gghgtsiggv ivdggnfnwg ngkfpaftep
      241 sesyhglkfw evfgadspfg niafairarv eglrdfgpal spfnaflllq gletlslrve
      301 rtvqnalela kwlekqpqve yvnypglpss pyhelakkyl krgfggvfsf kikgpqgtgd
      361 kfinnlslvs hlanvgdakt liihpsstth eqlspeeqka agvepgllrv svgiehiddl
      421 kadfsaafek agk
//
LOCUS       WP_010419105             286 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Anaerophaga thermohalophila].
ACCESSION   WP_010419105
VERSION     WP_010419105.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..286
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=32795
     Region          3..149
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          163..285
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
ORIGIN      
        1 minilvpvtf tdysvnalty altlagkfps kitilhsfpe yedleeeaap dmpnseesir
       61 rreqdardrl talcqatink mttlqdrnve lqnrfefgyp edviiqvcke mnsdvvimgt
      121 kskgetikel lgsitadvmk raespvlavp anskvdldkl skvlfitdfs dsdyisihkl
      181 vrlitpfhte ihairfvnhk pdkaeirkqe qfrdyckaty rnhrmkfgfe kgepfipale
      241 kyvgdnnidl iamtkrkrnm iaqlfspeit rkilfhtdip llvfhp
//
LOCUS       WP_010419166             254 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Leptospira inadai].
ACCESSION   WP_010419166
VERSION     WP_010419166.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..254
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27813
     Region          2..249
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mieveknghi lelyiktnet nslgtdffrk lretmesaes dpsikaills grndkffsng
       61 fnpeifigke lseikvvlke aleacgkvlf ssrpivcaln ghsmgvgavl aifsdyrilv
      121 ekkgrigfpe aliglnfpst sgyvlkelvg iktaqdllys grglksdeal avglveesat
      181 aeelipkark wcdqfasmal esvigikial rdsqrlvadr leardidlla tavhakngqe
      241 glrsilerrr paft
//
LOCUS       WP_010419234             376 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Pseudomonas syringae].
ACCESSION   WP_010419234
VERSION     WP_010419234.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..376
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42215
     Region          21..369
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 msehfwiwqq pnwprfhwre erlaplirac akaqgrllgm sgavggdaqm ceglnallqn
       61 ivtssaiege rlnadsvrss larrlgiadn gkhsprsegl aelmldatrg hdqpldlqrl
      121 ctwhrwlfpe edsfvsaril vgqlrsdepm qvvsgrldrp ivhfeappra gleqqledfl
      181 dwfassqsdp tldpfvragi ahfwfvtlhp fddgngrltr aitdlaltqg dqqairlfam
      241 sasiladrag yyhvletsqk sttditewle wflrtllksi enalvhierv lgktrfwqlh
      301 rdndlsaeqi kvlnrlldgg ergfenglsa aqyqavakvs katatrhlsd llaknclvrl
      361 pgggrstryq inlplp
//
LOCUS       WP_010419323             213 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Leptospira inadai].
ACCESSION   WP_010419323
VERSION     WP_010419323.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..213
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24019
     Region          11..213
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 magfestley lldwvanlpp slvwlfftls nltenvfppw pgdtvtafgg fllargkigf
       61 wslftstlvg nllgawlmys fghhllawlk hrdfpfktel ydeeaiqktl nwfsrnsviv
      121 vifsrfsagi rffvsivagm vemnpilffs cfslavsiwc giliyaghyl gshwevvvef
      181 lavyneiisi vlvsagigfl iyrhknkskt kap
//
LOCUS       WP_010419329             371 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Leptospira inadai].
ACCESSION   WP_010419329
VERSION     WP_010419329.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..371
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41876
     Region          16..367
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 miaregtgdp nrtafnilla ilflgagall ffvlrpyfys slvalilyla trkqykqlrk
       61 liglkldfla pwimigfvcm ivllpsyfvi rtlideslsi lfkirislse dkiietlmsl
      121 nmltdlvtdn pffwvklpei ygdfarnyid ilnldslyav lsnasslilg sidlpagiim
      181 nlffsllllf flyqdgkkve rfisdnlpfs releeqvgrk iasavqtvfr gnlivsimqg
      241 aavyvllvfa risnpflyas laaffsiipv igtsvvwlpi glyimfienn ivgaslfmia
      301 gltfylvlen vvkpkmldkk lrihpllvfl sliggiqqfg imglvlgpva vtlivilwdf
      361 wklyrkdffv r
//
LOCUS       WP_010419338             243 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Anaerophaga thermohalophila].
ACCESSION   WP_010419338
VERSION     WP_010419338.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..243
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=28357
     Region          <46..240
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mkrvkqillw sllllyfpvm lglveshhqe vvcsevevnv ldslqtrfin heairnavlm
       61 kfegilgepv nslklneiea fvekhpavrn cevyntiegh lkidllqhyp lfrvfednrs
      121 yyidedgnem plfdnftarv mvvsgaiegq mehliyiarl frndpfwsaq meqlyikqng
      181 dyvlvprvgd hlillgqper ideklrnlra lykqglspre wnnyqvinlk ykgqvlcskn
      241 rni
//
LOCUS       WP_010419375             394 aa            linear   BCT 01-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Leptospira inadai].
ACCESSION   WP_010419375
VERSION     WP_010419375.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12112208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..394
                     /product="HD-GYP domain-containing protein"
                     /calculated_mol_wt=44619
     Region          2..>50
                     /region_name="DUF3391"
                     /note="Domain of unknown function (DUF3391); pfam11871"
                     /db_xref="CDD:432148"
     Region          34..327
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mkkvsvaelk pgmrfskpvy ldkenlfits ntpitdsdle rlkrfgitev lthgdplqli
       61 tdpdfletqi ediivstivd edllplkgiy dnlnrikiqf sslykstfnv vqdvyrkaae
      121 dknfefgpir dqaeslsdfv rlhsnlsyli lgmnnpgyyl ynqitnstfy aliigklldy
      181 srpkmvdlai sclvadvgmt kvpatvsekt dqlndeeyks ilkhtiigyq iltqrikmkn
      241 nlavvalqhh erydgkgypq klaataieea ariyaiadnf salitnrphr krilpheaik
      301 smismdvgkf dlkivrtfln hvslypvgsc velsdkrvgl vlssnpdkpl rpsirivkde
      361 ygtfvrnlil vdlvkenhlf ivkaldlqea tnah
//
LOCUS       WP_010418956             229 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine phosphate synthase [Leptospira inadai].
ACCESSION   WP_010418956
VERSION     WP_010418956.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Begley,T.P., Downs,D.M., Ealick,S.E., McLafferty,F.W., Van
            Loon,A.P., Taylor,S., Campobasso,N., Chiu,H.J., Kinsland,C.,
            Reddick,J.J. and Xi,J.
  TITLE     Thiamin biosynthesis in prokaryotes
  JOURNAL   Arch Microbiol 171 (5), 293-300 (1999)
   PUBMED   10382260
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..229
                     /product="thiamine phosphate synthase"
                     /EC_number="2.5.1.3"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004789 - thiamine-phosphate
                     diphosphorylase activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=25671
     Region          54..225
                     /region_name="TMP_TenI"
                     /note="Thiamine monophosphate synthase (TMP
                     synthase)/TenI. TMP synthase catalyzes an important step
                     in the thiamine biosynthesis pathway, the substitution of
                     the pyrophosphate of 2-methyl-4-amino-5-
                     hydroxymethylpyrimidine pyrophosphate by 4-methyl-5-...;
                     cd00564"
                     /db_xref="CDD:238317"
     Site            order(58,60,62,88..89,108,130,156,158..159,187,207..208)
                     /site_type="active"
                     /db_xref="CDD:238317"
     Site            order(58,60,103,130,147,149,156,158,183,187,205..208)
                     /site_type="other"
                     /note="thiamine phosphate binding site [chemical binding]"
                     /db_xref="CDD:238317"
     Site            order(60,62,88..89,105,108,130,159)
                     /site_type="other"
                     /note="pyrophosphate binding site [ion binding]"
                     /db_xref="CDD:238317"
ORIGIN      
        1 mnpnrknlss tirprvelwk apglypildl eycskfqknp felvslwaky rdyipffqlr
       61 akketveqit ilyrslretf pdfpvilndh wklaldlgsf glhigkedye nldqearnri
      121 raselflgts shcladlsni etgawdytgf gpifdtsske kihpvlgiae lsealrlssv
      181 pvtpiggigs etlprilskg nflvamisga aetedvlksl rllqesgtv
//
LOCUS       WP_010419406              88 aa            linear   BCT 01-JAN-2025
DEFINITION  HPr family phosphocarrier protein [Leptospira inadai].
ACCESSION   WP_010419406
VERSION     WP_010419406.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..88
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=9292
     Region          1..86
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 mreihlkine nstgmharpa svfvncaskf pcevlvskeg vevngksimg lmmlalapgq
       61 efsikatgek egeaidalsk lvaddfai
//
LOCUS       WP_010419439            1139 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Leptospira inadai].
ACCESSION   WP_010419439
VERSION     WP_010419439.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 1139)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1139
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..1139
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=127379
     Region          1..1077
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miqniirfsa hnkflillft lgilvasyvs mktipldaip dlsdtqvivy srwdrspdii
       61 edqvtypiit sllgapkikv vrgfsdfgfs yvyvifqdgt diywarsrvl eylsriqsql
      121 pagvktelgp dasavgwvfq yalvdttgnn sladlrtyqd fhlryllnsv pgvsevagig
      181 gfkkqyqiti npnalrsyni gfetlvqkir esnqetggrl leisgaeymv rgrgylkslt
      241 dieniplstd ingtpvllrn iasvqfgpdi rrgiadlnge gdvvggtivm rhgenalsvi
      301 ervkakindi kaslpvgaei vttydrseli dhaisnlkfk lmeemlivsl vilvflwhfp
      361 saiipiltip isvivafipm nlldvnanim slagmaisig vlvdgaivev enaykkleew
      421 esggrkgdyh mvrleallev gpsvffsllv iavaffpift lvdqegrlfr playskniam
      481 avaallaitl dpafrmlftr mepfrfksal lskvatalfv gkyypeekhp vskilfrlyg
      541 pachwvlerp ktviasalal vfltipvyls lgsefmpqly eesllymptt lpgisvaeae
      601 klmvamdkki ksfpevkrvf gkagrsdtat dsapfsmmet villkpqdew rtanrfysdw
      661 prilqlpflp fvnerlskde lielmnremq fpgatnawtm piktridmls tgmrtpigik
      721 vlgssldeie kigiqietll ktnqdvrsvf aertaggyfl dlelkrekla rynisvdaaq
      781 qiivaaigge qvtqtvegre rfsvnvrypr elrdsvekir silvptqefg hipigeiadi
      841 ktktgpsmir dengflagyv yvdpstsdig gfvdqakrkv sesirlppgy silwsgqyen
      901 mlrvrermky ilpltifiif lllyfntksy aktiivllav pfsligavgl lyvldyhvsv
      961 avwvgmialm gldaetgvfm llyldlsyes aerkgmvrtr edrinaiihg avhrvrpkim
     1021 tvlaammgll pimwsngtgs dvmkriaapm vgglatsfll ellvyppiyl lwkegklvfg
     1081 qslpivskff drteskkkdv litqvksese tlneadsyed eirktaqirg kklkkktls
//
LOCUS       WP_010419516             149 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Leptospira inadai].
ACCESSION   WP_010419516
VERSION     WP_010419516.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..149
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16398
     Region          1..149
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslqakintd lkeaikskqe pllstlrllk adiqyeltkt gaqelvdeqi ialikrsyvk
       61 rtdaiqmyek anrsdladke kaeaevlksy lppevseeqi igvldkivae lkptgpkdig
      121 kvmgrvmaef kglnidgskv saivkskls
//
LOCUS       WP_010419586             427 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Leptospira inadai].
ACCESSION   WP_010419586
VERSION     WP_010419586.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..427
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48896
     Region          33..421
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkhrilyilv lfpiislfsq sdlmkeapvr eidfqtylne vldnnyelas rkynvditks
       61 eidvarkfpn pnlvlgnqsa disskhlpqq wyagfqgtve lggkrgarid yqtavadqsr
      121 aqfadfllql radatityvn tlaimlvtkr keesykslfq laesnaiklk fgditeldvt
      181 qsqveanlmk ndlissesdl raaalnmilf mckkdrsrlf yprgdlniqp keydleklia
      241 famenrpdvi aarydkvssr ynlklteanr vpnfnfevan nfytrstnat gpspsyyalt
      301 yffgitmpls nmytgdlema kyrisksevd leatklkvev qvktaylqyq lakeqlkiyk
      361 ssiladaekv fqgrmynykr gnttltdvla aqrtlnsvyf ayyqdlrnyv tkvvelqras
      421 giweisi
//
LOCUS       WP_010419591            1027 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Leptospira inadai].
ACCESSION   WP_010419591
VERSION     WP_010419591.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..1027
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=113003
     Region          1..1017
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mihqyilksi ekrilifvlf illcvfgyys wtqlsieayp diadvtsqvi tqfpgraaee
       61 ieeqitiple ralngmpgls iirskstfgl svitlvfqeg vedywsrqri keriegvqlp
      121 gdtkpeldpl tspigeifry tlessskdar elrelqrwvv ipklkqvigv advanfggit
      181 tqfqleidpn klnqfnisla qvidtiqknn tnsggsilrm gdlayvvrgi glirsledlg
      241 hivvdtrkgi piflkdlgdl klgelgrkgi lgrdfkndev sgivlllryq npsavlkgvh
      301 akvdelnngl lpsgvkvvpy mdridlvntt lntvsktlle giglvivvli lflgnvrgal
      361 lvaltipisl liafilmnft nipanllslg aidfgiivdg sivmmesilk lkeekeadtl
      421 qipdvakvas avaspiffat liiitayipl faferierkl ftpmaytvgy alagalfial
      481 tlipaisyia ykrpqrlyhn kwleritvly qkkitdlieh plrilkfaag alllcfalfi
      541 vigkdflpel degsiwlqvq lppgislakg aemaddlrke tlkfeevshv itqtgrnddg
      601 tdswtpshie csiglkpydt wksgrtkrel vgalrdhylk mpgytisfsq pmidnvndki
      661 sgahselvik vfgddfretr eltkkiaevl kstpgssdvg idqepplpqi qvkidrataa
      721 ryslnvsdis dlieaaiggq aisnlflgek kyditvryge afrntpeais nlmltspnga
      781 kipvsqvanv klttgestit resnqrhltv kvnlhgrdls sfvseakeni shkikydskk
      841 yrivwggqle nqeranrrls iilplilcvm ftllyvafgn lrhaflllsi vpaallggli
      901 alivrgmtln vsssvgfial fgvaiqngvi mvshlnelia nkvplklavi sgatnrlrpi
      961 lmtatvaalg llpasvatgi gsdvqrplat vivyglisgt gitlfalpvl yymlekrvsn
     1021 gkfnksg
//
LOCUS       WP_010416918             504 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Anaerophaga thermohalophila].
ACCESSION   WP_010416918
VERSION     WP_010416918.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..504
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58062
     Region          97..466
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkskiyliii ltlgviitsv tsctdldeel fsqveskdyg ktadeietiv ggaysslrgf
       61 sddisisypt ceyvfflsec tsdeaciptr gtdwydggry qeaqkhtwta dnamilsawr
      121 ycfqglakvn aiiyqvnqse ltedekfvin aelrgirayy yyllldmfgd vpvvtdfedk
      181 elpakssrqe vfdfvesell eirdvlpsev iygrftqnva ntllarlyln aevytgnprw
      241 qdcidacekv sgyslepdyf tnfltenqvs revifaipyd seagtvgnyl hsmtfhykqp
      301 yafsptgdyp wcgngicgqp gvyssfddad rrkdamlege qinlatgsvi nmdngepliy
      361 teeienfena kqnegvrlfk yevkageswe rdhdwvvmry aevlmmqaec yvrmgtpdla
      421 rpfiepirer agmdtpetit ldflndewlr efifeghrrt hnirfgdffe pwwekgetpr
      481 yrevfpipqs eldknknlvq npny
//
LOCUS       WP_010419667             665 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Leptospira inadai].
ACCESSION   WP_010419667
VERSION     WP_010419667.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..665
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75377
     Region          1..622
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mtvlenlnek qkeavetteg pvlliagagt gktntlvhrl aklvsngvsa enillltftk
       61 kaaremltra vsvldkrcsk vnggtfhsfa ghilrkyapa lgissqfsvl desdsidvfq
      121 lirtegnyaa qklrfpsnet llslystsvn tgkdlsellk tespkfldqe tsirkifsdy
      181 ksykrersll dyddlllfsr elltdhdgir kklseqykyv mvdefqdtnk lqahiaclla
      241 sehenifvvg ddaqsiysfr ganvkgifdf pkifpnakti flernyrstp silnlangvl
      301 lnfsekyeky lytknedfhk prllgfpdel deaegvadri lerreegial gnmavlfrsg
      361 wnsnqlelvl narnipyqkf ggkkfvesah akdflsllri renrldsvsw lrillllpgi
      421 gaakakliln eltrsggdlq avrllqkgta aadlqllsdl ldrsdssltl tlenflefyk
      481 pllerkyddp krrmedlnsf ltlskryetl heflvemsle gpnrsldklv peeeeedvlv
      541 lstihsskgl efdtvillnv tegsfpsgrg eknieeerrl fyvgitrarr sltltypqts
      601 ssrgghnfnr lsrfieelke sdkilernff pkahtaatks lseipsedlk tetearkrir
      661 dffgs
//
LOCUS       WP_010419673             184 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Leptospira inadai].
ACCESSION   WP_010419673
VERSION     WP_010419673.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..184
                     /product="YceI family protein"
                     /calculated_mol_wt=20087
     Region          1..181
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mkrifgiasi flvfglifpi slrsedlkis qktlkftvih pfktvngvcg evnitpttys
       61 tgangiqlpk avkieaplke frsgdenrds hileslgfpe iqsvsfssts idvteggwfv
      121 sgnltvngvt kpvktranis ssngqievsg kfqikmgeyr isppsllfak akeeveiefs
      181 fllr
//
LOCUS       WP_010419684             460 aa            linear   BCT 01-JAN-2025
DEFINITION  TldD/PmbA family protein [Leptospira inadai].
ACCESSION   WP_010419684
VERSION     WP_010419684.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..460
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49331
     Region          6..459
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mdlkkaeali eagknrkadf veiyeeesrn ssvalrdkki eqslaatdyg igirliygtd
       61 vlyaytsnde ishlislinl ladsrgeasl lggrfifsps pvkpqfpaaf ldprqvspsr
      121 klellqsads aarqvsskvv qvgasasdiv tnvlianseg lwvedlrvrs rfslsvtaek
      181 egerfvates pgairgfeff dglpvkdlaq naaeralfml dagyiegkkl pvlmgngfgg
      241 vifheacghp letesirkns spfvgklgea igqscltayd dgtlenyygs lkvddegmpt
      301 qktlliengi lkaylsdrig smetgsprtg sgrresyqya pvsrmrntfi apgkdsfdem
      361 lssveyglya krmgggsvnp atgefnfave egyvirngkv aepvrgatli gkgheilpki
      421 smvgndlela agtcgassgs ipvtvgqpsl kvdeilvggr
//
LOCUS       WP_010419710             352 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Leptospira inadai].
ACCESSION   WP_010419710
VERSION     WP_010419710.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..352
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40135
     Region          1..342
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mnllvlrfsa mgdvalmapa liavvakytn iqltvvtrgn yapffynipn vhviginlkk
       61 yrgimglyrl frelnklgpy ekivdlhssv rsrfislffr lrgvpifqiv kgrreklrqi
      121 rrnrkvlrkl phtvdrylkv fdkagypasv rkgpwinvdp eskifakdfl lsrkidkkeg
      181 lwvgyapfag hklkewphek siallkllke efpniriflf gssqeasime ewrngdqsmt
      241 ivsggklgir gelgimermd viigmdssni hiaallkrpv valfgtthpy sgfapfgqed
      301 tgvlqiedlt crpcsiygnt tcfrkdfacm ewitpedvik rinviinint lf
//
LOCUS       WP_010419860             705 aa            linear   BCT 01-JAN-2025
DEFINITION  M3 family metallopeptidase [Anaerophaga thermohalophila].
ACCESSION   WP_010419860
VERSION     WP_010419860.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..705
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=81484
     Region          25..705
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 mrkffllpma lmfltacqsg tedktnpfft vydtpfetpp fneikeshyl pafkegikqh
       61 eaeintivnn setptfenti lpfdqsgkll ykisrvffnl rsadtsdsiq aiarevspml
      121 sehsdnimmn mklfervksv yenlessdld dsqkrvvtky yedfvrngal fkgddqkrlk
      181 eintrlstlt lefgenllae tnenfeliie deadlaglpe gvreaaaeaa teagyegkwl
      241 ftvqkpsmlp fltyaenrdl reklyrgyfm rcdrgdgfdn kdiikeival raeraqllgf
      301 enhadyviev nmakepqtvy eflmelwvpa lkkskeereq mqtiidsegg dfnlapwdww
      361 yyaeklrkek ydldesqlkp yfqlenvrdg mfwvanqlyg itfeksdnvp vyhedvevfe
      421 vkendgshig llyldyfpre skrvgawcts frgagwdhek neriaplssi vcnftkptgt
      481 tpsllswdev ntlfhefgha lhglftkgky drtagdvprd yvelpsqime nwaaepevir
      541 hyakhyetge tipdeliekl ensslfnqgf anveylaasl ldmdwhtlqh pvnvedvnaf
      601 edesmneigl ipeilpryrs tyfshifsgg ysagyyvykw aevldadafy afrqtgdifn
      661 kelaakfrky claevgegeg meqykkfrgq epsiepllek lgfed
//
LOCUS       WP_010419901             277 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Anaerophaga thermohalophila].
ACCESSION   WP_010419901
VERSION     WP_010419901.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..277
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31593
     Region          5..127
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          136..262
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 meslmhsilv pydfsdtvfn avqhavnlsr vlntnitllh ivkkeseisp aeenlrkeak
       61 diekklnvkp eilvkegtif ktinevseel ecamvvmvth gmrgmqkltg swalkvivgs
      121 rvpflvvqep pqkddytkiv fpvdfksenk eklrwaeyms ryfktkiylf sdtardgsvd
      181 srtkanvvfc knfleeknid yelvlakhka pfseetiefa kennadliii mttrdiafhd
      241 yilgaheqyi iansakvpvm vinprtdlmk ygyggsf
//
LOCUS       WP_010419960             149 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Anaerophaga thermohalophila].
ACCESSION   WP_010419960
VERSION     WP_010419960.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..149
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=16692
     Region          2..149
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mseqqnntll sfrvndeffa ldamkvnhil eipeitripn tpgfmkgvin lhgniipvvd
       61 lrvlmgfset eydndtaiiv itpddeqdss lglivdmvke vieadgiemk ptvvdmeksq
      121 lknfhgtfsf dnqfvhvidi eelvktaei
//
LOCUS       WP_010419965             434 aa            linear   BCT 01-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Leptospira inadai].
ACCESSION   WP_010419965
VERSION     WP_010419965.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..434
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46991
     Region          3..434
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 marhyksetl alhagqtpdp tttsravpiy qttsyvfndt dhaarlfglq efgniytrig
       61 npttdvleqr vaaleggvag latasgqsae tlallnives gqeivasssl yggtynllhy
      121 tfpklgikvh fvdqsdpenf rkaanektra ffaetlgnpk ldtldiegva kvahelgvpl
      181 vidntlpspy lvqpiehgad ivihsltkfl gghgssiggi ivdsgkfnwg ngkfknftep
      241 dpsyhglkfw evfgkfepfg giniafiika rvqglrdlgp aispfnawni iqgietlplr
      301 vtqhsinaqk vaeflskhpk vswvnypglp gdtnfalakk yhkrnlfgai lgfgikggis
      361 eakkfidnle lfsllanvgd akslaihpas tthqqlspae qvtagvtpef irlsvglehi
      421 ddiitdldea lkkv
//
LOCUS       WP_010420021             352 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Leptospira inadai].
ACCESSION   WP_010420021
VERSION     WP_010420021.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..352
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38498
     Region          <201..331
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 msyfvpehap mseaerekaa esarnnllnn ilggigyvag rvgdfakgiw dgmfgeedge
       61 flahgsdiaf dgkivsgwle giqsktlsaq dkaafweewk tqsrdqtdat isilkslgyd
      121 vselenkvka lraakdgvpg gydkdgfmyt nqegaaiqvv gsreksfler vssffgfian
      181 ginsawnglf gsssltenrf etapvtilnn garlpvgaeg srygmrtfid qdgnekthfh
      241 tgldqpipag tpipavadgk vvivieiykn gidqgygaqv miehengvrt nyghnsailv
      301 kvgdivkqgq visfsgnsgh stgphmhfev rtyneerktw efndprtfdw rr
//
LOCUS       WP_010419738             258 aa            linear   BCT 01-JAN-2025
DEFINITION  LOG family protein [Leptospira inadai].
ACCESSION   WP_010419738
VERSION     WP_010419738.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..258
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29451
     Region          41..255
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mgraafenee flhsvdafhl rvlaeinypq alfrdakird ticifgsari lsteeyaard
       61 klrekltpke lrihekqgel vryyeearet arlitlwgke iskdvrrmav ctgggpgime
      121 aanrgavegg gpslglnirl pfeqtintfa dpkisiefhy ffmrklwflr lskgivvfpg
      181 gfgtvdelfe tltliqtgrn nlkipvimyg kkywdqvfhi gpmkeyglid pddinlityc
      241 depnevlevl kkkvpfed
//
LOCUS       WP_010420039             405 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 27 protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010420039
VERSION     WP_010420039.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Kitaoka,M.
  TITLE     Diversity of phosphorylases in glycoside hydrolase families
  JOURNAL   Appl Microbiol Biotechnol 99 (20), 8377-8390 (2015)
   PUBMED   26293338
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Naumov,D.G.
  TITLE     [Phylogenetic analysis of alpha-galactosidases of the GH27 family]
  JOURNAL   Mol Biol (Mosk) 38 (3), 463-476 (2004)
   PUBMED   15285616
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14423446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..405
                     /product="glycoside hydrolase family 27 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46338
     Region          31..303
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(38,73..74,114,148,150,182,201,205)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          315..401
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
ORIGIN      
        1 miikkgllvf fvllfgfriq aqkfeelalt pplgwnswnk facnineeii rdiadamves
       61 gmkdagyeyi viddcwhggr dslgfiypdf trfpngmkal adyvhskglk lgiysdagtk
      121 tcggypgsrg yeyqdalqya kwgidylkyd wcnteninpv gayttmrdal ykagrpvlfs
      181 mcewgnnepw kwaadiahmw rttgdificw dckhqheggw yswgvmkild mqeglrkyag
      241 pghwndpdml evgngltvne drahfsmwam laapliagnd lrnmseetie iltneeviai
      301 dqdslgvqgf kysskdslet wfkplkngew avcflnrrae pavvefdwkn envmdeifgy
      361 vtkfdevtys irnlwnrkni gktkkafiat vpshdvvmlr lkplk
//
LOCUS       WP_010420117             137 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Anaerophaga thermohalophila].
ACCESSION   WP_010420117
VERSION     WP_010420117.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..137
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15481
     Region          4..136
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 menneiekkl esknvkptam rtlvykalae sgkalslsdl eqrfekvers tifralksfq
       61 dnfivhpvdd gtgsvkyavc dddctcnihd lhvhfyctrc gktrcmkelp ipdvklpdgy
      121 tyenaqfiin gvcprcd
//
LOCUS       WP_010420135             115 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Anaerophaga thermohalophila].
ACCESSION   WP_010420135
VERSION     WP_010420135.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..115
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12818
     Region          2..113
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mlqvltehks aislpeleqk fekadkatly rtlktfqgnk lihsidddsg svkyalcqea
       61 cecqpedlhv hflcsncnqt fclndipvpt inlpnrfsle cvnmvvkgic ancdk
//
LOCUS       WP_010420165             201 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010420165
VERSION     WP_010420165.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Stukey,J. and Carman,G.M.
  TITLE     Identification of a novel phosphatase sequence motif
  JOURNAL   Protein Sci 6 (2), 469-472 (1997)
   PUBMED   9041652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10107962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..201
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0042577 - lipid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0046839 - phospholipid dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=22270
     Region          <130..194
                     /region_name="PAP2_like"
                     /note="PAP2_like proteins, a super-family of histidine
                     phosphatases and vanadium haloperoxidases, includes type 2
                     phosphatidic acid phosphatase or lipid phosphate
                     phosphatase (LPP), Glucose-6-phosphatase,
                     Phosphatidylglycerophosphatase B and bacterial acid...;
                     cd01610"
                     /db_xref="CDD:238813"
ORIGIN      
        1 mklfskilsf lfhpmlmptl giffilnsgn hhaflpfeik rlvyiivfts tcllpvsllp
       61 lflqikliks femetarerv ypaltsaaff llgyflltrl nvsvlietfl lsslvailis
      121 vaisffwkis lhtlavggvs glivalmfky gidllsllsl mivisglvam arlylnahsp
      181 fqiyagyflg liivgsgiml i
//
LOCUS       WP_010420293             266 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010420293
VERSION     WP_010420293.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..266
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29233
     Region          2..254
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 makiialanq kggvgkttta inlaaslavl eydvlvidad pqanatsglg feirdvetsi
       61 yecivdgedp kkailkgeid hlyvlpshid lvgaeiemln mperekvlkg vinkikddyd
      121 filidcspsl glitvnalta adsvmipvqc eyfaleglgk llntikiiqt rlnpdleieg
      181 flltmydsrl rlsnqvveev qkhfqdmvfe tlitrnikls eapsygkavv mydaaskgam
      241 nylnlarell qknnmtkidn knkvan
//
LOCUS       WP_010419739             287 aa            linear   BCT 01-JAN-2025
DEFINITION  VIT1/CCC1 transporter family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010419739
VERSION     WP_010419739.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Kato,T., Kumazaki,K., Wada,M., Taniguchi,R., Nakane,T.,
            Yamashita,K., Hirata,K., Ishitani,R., Ito,K., Nishizawa,T. and
            Nureki,O.
  TITLE     Crystal structure of plant vacuolar iron transporter VIT1
  JOURNAL   Nat Plants 5 (3), 308-315 (2019)
   PUBMED   30742036
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Li,L., Chen,O.S., McVey Ward,D. and Kaplan,J.
  TITLE     CCC1 is a transporter that mediates vacuolar iron storage in yeast
  JOURNAL   J Biol Chem 276 (31), 29515-29519 (2001)
   PUBMED   11390404
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..287
                     /product="VIT1/CCC1 transporter family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006873 - intracellular monoatomic ion
                     homeostasis [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31447
     Region          7..127
                     /region_name="Ferritin_CCC1_N"
                     /note="Ferritin-CCC1, N-terminal ferritin-like
                     diiron-binding domain; cd01044"
                     /db_xref="CDD:153103"
     Site            order(16,46,49,91,115,118)
                     /site_type="other"
                     /note="diiron binding motif [ion binding]"
                     /db_xref="CDD:153103"
     Region          134..279
                     /region_name="Ferritin_CCC1_C"
                     /note="CCC1-related domain of ferritin; cd02431"
                     /db_xref="CDD:153122"
ORIGIN      
        1 mdaqarkyal aaqrteitey hiykrlagkt knsknaevln riagqekqha afwesktgqq
       61 vkpdkwrlyr tlllarflgl sfalklmeek egtgadnyvr qaryfpeaad fareegehek
      121 eilkmleggn ltfvgsvvlg lndalveltg alagftlalg etkiisiagl vtgisaalsm
      181 aaseflstkt egdprakeaa lytgisylat villilpffl vdnkfvalgi vlvlalliiw
      241 gfnyyvsvvk dldfkkrfwe masismgvaa fsflvgfgln allgvdv
//
LOCUS       WP_010420410             202 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Anaerophaga
            thermohalophila].
ACCESSION   WP_010420410
VERSION     WP_010420410.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23075
     Region          19..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 menrgldier ianlyykfgv knitmdeian elgiskrtiy qqvatkyelv qmvlneefdk
       61 fkeavlkvvs enrggiqkly glysvvlmhf kpitpvfvys lvkmssvlad nireqygsfi
      121 ketlsqiiee gknegvfltr fkddfatlft gflfqtgdiy vdgkernvdl nnmfylqisg
      181 ictakgekil eqfienpqil sa
//
LOCUS       WP_010420432             356 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Pseudomonas syringae].
ACCESSION   WP_010420432
VERSION     WP_010420432.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..356
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39186
     Region          18..347
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mfnvlrnwvq ryfsdeeavv lavllflaft lvltlggmla pviaglvlaf lmhglvsvle
       61 rlrmpevaav glvftlfigv llvfllvlvp llwhqlitlf neapgmlakw qsvllllper
      121 yphlvsdeqv llaievarge vgkigqlalt fsisslpllv nlmiylvlvp ilvffflkdr
      181 hmigrwargy lpreralinr vademkrqia nyirgkviei ficggvtyia faalglnyaa
      241 llamlvgisv vvpyvgavvv tvpvaliglf qwgwgdqfiy lmiahgiiqa ldgnvlvpll
      301 fseavnlhpv aiicavllfg glwgvwgiff aiplatlfka vldawprnep tvapll
//
LOCUS       WP_010420433             157 aa            linear   BCT 01-JAN-2025
DEFINITION  peroxiredoxin [Pseudomonas syringae].
ACCESSION   WP_010420433
VERSION     WP_010420433.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..157
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17295
     Region          8..149
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(42,45,120)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mtvtvdhpvp dfqapatsgq tvelsalkgq qvviyfypkd ntpgcttqgq dfrdhiaqfq
       61 aantvvlgvs rdsvkthenf kakqsfpfel isdkdeavcq lfdviklkkl ygkeylgvdr
      121 stflidkegv lrqewrgvkv pghvaevlaq aealnkg
//
LOCUS       WP_010420507             286 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Rickettsia helvetica].
ACCESSION   WP_010420507
VERSION     WP_010420507.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..286
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32676
     Region          36..212
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 maknkglgrg lssllgeevi sieseiiqii nidkirpnen qprknfeydk ikeladsiln
       61 ngllqpiivd nnfqiiager rwracklakv leipviiknl daresmeial ieniqrtdlt
      121 vmeeargfky lvenfnytae klaerlgksr shianllrln nlpqsiqdkv nenilsmgqa
      181 rclinhehae viadhiinnd lnvrqteelv rqwykneytk spnnnnkvgk rclkdnatdn
      241 dlallvkals ekfgikitie nyplggklif hykdleeldl illkln
//
LOCUS       WP_010420633             395 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA desaturase [Rickettsia helvetica].
ACCESSION   WP_010420633
VERSION     WP_010420633.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Los,D.A. and Murata,N.
  TITLE     Structure and expression of fatty acid desaturases
  JOURNAL   Biochim Biophys Acta 1394 (1), 3-15 (1998)
   PUBMED   9767077
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..395
                     /product="acyl-CoA desaturase"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0006636 - unsaturated fatty acid
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=45607
     Region          3..287
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
     Region          <282..>394
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
ORIGIN      
        1 mlsklnkpal falifypifi islvvkysfd ygigltevif iiasyyinni tvgiglhrlw
       61 shnaytinky aefvlvmlsa gtlqgpalsw asnhykhhry tdedqdphtp lkfdnkflgf
      121 mwshigwmlv gsgsyksidr itwakhgkns llkwqlkyyw qiaafmnivv plfigylvgg
      181 tmqsayagfl fmglgrflqq qatfcvnslc hfagskkyyk gtagdiwwma lfllgenwhn
      241 yhhafpsdyr ngakwyhfdv hkwiiflmsk iglaselert tkvriqakmq etlsylsekq
      301 kqkltlmqak idhllenlcl kikeleessi tikkqfkksf veiqeslknl aeqvssatqi
      361 tekpsekllk ivnkkiidae qsiyklynkl nalkv
//
LOCUS       WP_010420663             119 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Rickettsia
            helvetica].
ACCESSION   WP_010420663
VERSION     WP_010420663.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..119
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=13316
     Region          10..118
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mveqkeiltr ggiylagldp akineigttr piiilnsqti ldsippiifi cplssqsqpe
       61 fsnlhfeldv rdnlevksya liehcrsvsi triiyprlaq atsyevnril lilqqlvdv
//
LOCUS       WP_010420673             783 aa            linear   BCT 01-JAN-2025
DEFINITION  penicillin-binding protein 1A [Anaerophaga thermohalophila].
ACCESSION   WP_010420673
VERSION     WP_010420673.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..783
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=89426
     Region          25..751
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mekkllqkyi rwlyglflgl lgfsillffl isigglgfmp sfeelenpkt nlatilyssd
       61 hevlgkyfre nrtnvtydel npyvinalis tedirfyrhs gidahglgrv llrtiimgek
      121 ssgggstitq qlakllfhdp atnvwqrslq klkewviavk lersytkqei ltmylnkapf
      181 iygaygiesa ahtffsksld siqveeaatl igmlknpsly npirrpeltq arrnvvlgqm
      241 rkaghitsee fdslkmlplg lnfqrddhih glapyfreyl rlvltaekpe renyaswqeq
      301 qfiedstawi edplfgwvnk nlqsdgtkyd iyedglriyt tidsrlqqya ekamtqhlge
      361 elqptffrek kgrprapftk nitqeqyesi inrsirnsdr yrylrqegve wdsimaifkq
      421 pvemevfswk gdidtimspl dsihyyksfl rasllsmnpq sghvkayigg pnykhfkydm
      481 vsmgkrqvgs tikpfvytla mqegltpcdm vpnipqtfhl ptgktwtpgn sgsaragemv
      541 slkwglansn nnitawvlkq fnpeavvnii helgidspmd pvpsivlgvp efglnemvsa
      601 yctyankgvh veplmvtrie drygnvisnf tprkkevlse etaflmlnll egvvnqgtai
      661 rlrlrynfea qiggktgttq nhsdgwfmgv tpnlvsgiwv ggedrdihfd nlyygqganm
      721 alpiwalymk qvyedeeipi tpedtfeepa nfnidlecpd ehipaneeql eggdttmyee
      781 eff
//
LOCUS       WP_010420791             249 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rickettsia helvetica].
ACCESSION   WP_010420791
VERSION     WP_010420791.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..249
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27633
     Region          23..245
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mslshskvfi eitdgyvegi dthkraqglk hfflkkgvsl spnipilnni nfscyegeki
       61 afigsngsgk ssllkliagi yplksgtvrv hgdiaaiidm gvgfeqeqtg renikmlmly
      121 nnmldkyskk iekeiidfse lgskidlpik iyssgmlsrl afsvsifqnp qillldevfa
      181 agdsyfieks lnlmknkfkn tpisiivshq eeiikdncdr cillrdgnii gdgspseifk
      241 iynqqqgns
//
LOCUS       WP_010420906             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: siderophore-interacting protein [Pseudomonas].
ACCESSION   WP_010420906
VERSION     WP_010420906.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..255
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=28410
     Region          3..255
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mnspqsihrv mheikrrklq vvrvteltpl mrritlqgpe lagfislgtd dhvklffpqt
       61 aeeqaalenl npagdkdtpr ppmrdytprr ydektgeldi dfvlhgegpa atwaaqaapg
      121 qflhiagpkg smvvpdmfds ylligdetai paiarrlesl panraalvvv evanpqeqqv
      181 fdsaaqvdvi wivrgeqnll dvtrrlempe gklyawvate salsrklrrv lldefgleed
      241 fvkaagywkl dstae
//
LOCUS       WP_010420984             187 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmD family RNA methyltransferase [Anaerophaga thermohalophila].
ACCESSION   WP_010420984
VERSION     WP_010420984.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002368
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..187
                     /product="RsmD family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0031167 - rRNA methylation [Evidence IEA]"
                     /calculated_mol_wt=21203
     Region          1..181
                     /region_name="RsmD"
                     /note="16S rRNA G966 N2-methylase RsmD [Translation,
                     ribosomal structure and biogenesis]; COG0742"
                     /db_xref="CDD:440505"
ORIGIN      
        1 mrivsgqlkg rrfsppssfk arpttdqare slfnilnnli dfeseevldl fsgtgaisye
       61 fasrgcssvt aieknyanfs fikktaagfn iennlkvika dvfkfieknn kkytfifadp
      121 pfdlpqteel pgmvmnseil tkdglfvleh gpdknfennp ffwqnrhygk vnfsffkvkk
      181 dkkgpsd
//
LOCUS       WP_010421031             744 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK [Rickettsia helvetica].
ACCESSION   WP_010421031
VERSION     WP_010421031.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12144184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..744
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=82763
     Region          14..173
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          118..743
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mlyyinkill nnkvqavilg iiglgivtvl tsyniddpsf nsvtteyssn lvgifgsyls
       61 dclyqcfgla afiiplacfv wgrncwygry rgsfirmfvm flalissstl lsklklefip
      121 anaggaigii asnfferftn qlylllifft fiilvvllei kftslnnfii klgkfltywi
      181 qsflhnvfsr lssirlfptk nndkinitss yqrpvsekvk cteearpvpa npikffskpv
      241 spkisqseia elppisllrd penhhvkgas sselkqkaee lltvlndfgv kgqiininqg
      301 pvvtqyefep aagtktsrvv glsddiarsl salstriavi pgknvlgiel pnkqreffcl
      361 kelietpeyr dkstllplvl gkdlagkpli adlakmphll vagttgsgks vginamivsl
      421 lyryapeecr fimidpkmle lsaydgiphl ltpvvtepsk avvalkwavk emenryrmms
      481 nigvkniagy nakileavke nrviersiqt gfdpetgkpi yetvtmnmek lpyivvivde
      541 madlmlvagk diemliqrla qmaraagihi imatqrpsvd vitgvikanf psrisfkvts
      601 kidsrtilge qgseqllgmg dmlfmgntsk isrvhgpfvn eaeiekitey lketgtpeyi
      661 savteqpeed dssidigdgt sdellykkav qvvrderkss isyiqrslri gynkaanlve
      721 kmekegivsp pnhtgkreil lper
//
LOCUS       WP_010421033             203 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Anaerophaga thermohalophila].
ACCESSION   WP_010421033
VERSION     WP_010421033.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..203
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23894
     Region          14..200
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mevnpnlsdk arydlelver avkgdqkaya elmaryrdai yfmllkminn ktdaedltie
       61 afgkafknls qyspnyafst wlfkiasnnc idylrkkrnn hisidgnyss eekdsepqvh
      121 lkdetpdpee fmireqkvvl mrtvvkklkp ryrtlielry fkeysyeeis eeldlplgtv
      181 kaqlfrarel lfntlknsev kkh
//
LOCUS       WP_010421085             394 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Rickettsia helvetica].
ACCESSION   WP_010421085
VERSION     WP_010421085.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..394
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=44995
     Region          1..386
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 mierflakdi ksflnefsav ailgprqvgk ttlakeiaeq isptplyldl ekpsdlakls
       61 dpelyfqths nylviideiq rmpqlfqvlr sviderrqqg qkvkqflllg saskellkhs
      121 seslagriiy tqlygfniqe vrkagyidnn llwlrgnfpd sflsasdnss mnwrqsfimt
      181 ylereipqlg ynisteilrr twtifahcqg dllnaskiaa slgisvptim ryidlfedlf
      241 lirllrpwss nvkkrlvkap klyirdsgil hallniksyd ellghyilgg sfegfvieni
      301 lsivknqmns wfyrtaggae vdlilessin nltaieikrs ltpsiskgfy nalqdlkpkk
      361 ayivypgkdk yylnsqvevv plhyllnllk telq
//
LOCUS       WP_010421096             143 aa            linear   BCT 01-JAN-2025
DEFINITION  Dps family protein [Rickettsia helvetica].
ACCESSION   WP_010421096
VERSION     WP_010421096.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..143
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=16040
     Region          1..141
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mqvvkaleqi ladsyalyfk tqnyhwnveg aefrslhllf egqyedlaes ldelaerirs
       61 lsakvpalsd liklasidea npnatademl ksltkdqdii rdtlykglka aqaesdegta
      121 dmiigrikvh eknrwmlkss ilv
//
LOCUS       WP_010421181             474 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010421181
VERSION     WP_010421181.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..474
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53513
     Region          368..470
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(370..371,404..405,408,412..413,416,460,464)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 meankamlha klvqadllvp teynkgvesy keaqkhyadk kgvkkieesl veavnhfnrs
       61 adfsvsaklv fansldarsd alsagadkfa ketwseaeev fnratkelek gdrdnsykys
      121 teaielyrka elasiktnll detrallera ddmkvdrnap ktikkaesll aetereletn
      181 rydmdypril akqakyeash aiflnktisd mddrdmemed vilkyetpli riaeqlgfva
      241 qfhegienpe nqiikhisgl qkdnkmlmae nldnenairh lkstvdllkk enlalssevn
      301 neinkrtddm iaqsrefeke kaklaakiak qtklnqqfee vylifdssea svfrsedeiv
      361 irmhgfgfet gkseitpknf dlltkvqnai kifpkcnviv egytdsfggd asnlvlsqkr
      421 sdavtqylna nsdapgiski ssvgygennp vannetaegr kqnrridiki qpvm
//
LOCUS       WP_010421394             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010421394
VERSION     WP_010421394.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..277
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=29733
     Region          76..268
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mkklfaflav fgmlsigass vyaqgeeqsv aeettteqvt eqeaaaeeev veedaaaeaa
       61 eseepqglhk qikakfiegg amfmsfvlla lifglaivie riiylnlstt ntkkllqnve
      121 ealneggvea akevcrntrg pvasifyqgl drfdegievv eksvvsygsv qmgllekglt
      181 wislfiaiap mlgfmgtvig midafdsiqa mgdvsatava ggikvalitt vsglivaiil
      241 qvfynylvsk idsivnsmed asitlmdilv kynmknk
//
LOCUS       WP_010421411             111 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Rickettsia helvetica].
ACCESSION   WP_010421411
VERSION     WP_010421411.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..111
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=12772
     Region          <2..>102
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          25..52
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          54..86
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mlkileiffe nkarikierf kqlpplhvaa aegnisdvri ylhrkcdvnk qdingntplh
       61 hayekgnkev ikilfqshgi dkniqdnkny ipadystefe nkvdklgevi e
//
LOCUS       WP_010421465             393 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010421465
VERSION     WP_010421465.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..393
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45079
     Region          1..348
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlllplfylt edigvffvfs alglllgslv swrsfnaili sdtdevansn lgisfllggv
       61 tslileilil afspfwgnwq snvewiyflp vyalftsvfi sfenflnykk ryiqigygkl
      121 ikasatllit lllgiltpsa eslifalitg llavivfqiw isgitwhifq iskrkfkiff
      181 fkyrdiltfn sslaiiseln shlptillsi fygenvvafy gmaqrffstp vsvwsnsias
      241 vfgkesvery iksrnisgyf vstvkkvimi iipfgviafl lapwifdtfl gkeweasggi
      301 sriiipliia qnivmpttil ytilnhqkri lifylvsffv riillfilpy llfdinyiyl
      361 lmmfsftgvl hyilyyrelr sqienyetqi ehk
//
LOCUS       WP_010421479             185 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Anaerophaga thermohalophila].
ACCESSION   WP_010421479
VERSION     WP_010421479.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..185
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20675
     Region          2..163
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mlktgiiigs trpgrnaeqv akwvydfask rndaeyelvd lkdynlplld eaypasfgqy
       61 snehtkvwae kiksldafif vngeynhsip galknaldyl yaewnnkaag fvtygsagga
      121 raveqlrlvl selqvahvra qvllslytdf enfsvfkpap lhadnlktml dqlnswgnal
      181 ktlre
//
LOCUS       WP_010421495             109 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Anaerophaga
            thermohalophila].
ACCESSION   WP_010421495
VERSION     WP_010421495.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..109
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12417
     Region          4..>87
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msidstkdsi lrvanqlfsr fgfhktsmde iakvarkakg slyyhfvske dlfrevilke
       61 ithlksqlgi itnssdldas qklrsylvkr meilnsaasy hetlradff
//
LOCUS       WP_010421509             152 aa            linear   BCT 01-JAN-2025
DEFINITION  GtrA family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010421509
VERSION     WP_010421509.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..152
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17461
     Region          6..136
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 maikyikfva srligtlvdt lvlwglssyi fssyighyiv aptisfefav fsnfllsyyw
       61 iwrkristkn iktfiarfai fniscvlgfi vkmaflllfe klfgwdvvfc nlaallisgi
      121 vnfvlaefvv fkkrppiiep lnemeslkni ny
//
LOCUS       WP_010421595             312 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Anaerophaga thermohalophila].
ACCESSION   WP_010421595
VERSION     WP_010421595.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..312
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35415
     Region          66..312
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 miiqlallta vilqlgaffk tlglirktrf nvswitisia fflmairrvs elldftqnae
       61 lsridlfntw vavfisllmf vasfyirrif nlqeeidkmr kqnearvlsa iidteekerq
      121 lfarelhdgl gpilssvkma fsainkeeig dknkvimert eksvdhavma vreisnnlsp
      181 hlldtfgllk airsfynaia itkkpeldve ncfippklpk nievilyril celinntlkh
      241 adaskinivi feqsgileln ysddgcgfdl kqkkhqgngl dnissrvksl ngkvqmhsks
      301 nngffikini pl
//
LOCUS       WP_010421650             394 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu [Rickettsia helvetica].
ACCESSION   WP_010421650
VERSION     WP_010421650.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     gene            1..394
                     /gene="tuf"
     Protein         1..394
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=42718
     Region          1..392
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makakfertk phvnigtigh vdhgktslta aitivlaktg gakataydqi daapeekerg
       61 itistahvey etknrhyahv dcpghadyvk nmitgaaqmd gailvvsaad gpmpqtrehi
      121 llakqvgvpa mvvflnkvdm vddpdllelv emevrellsk ygfpgdeipv ikgsalqale
      181 gkpegekain elmdavdsyi pqpvratdkp flmpiedvfs isgrgtvvtg rvesgiikvg
      241 eeieivglkd tqkttctgve mfrklldegq agdnvgillr gtkreeverg qvlakpgsik
      301 phdkfkaevy vlskeeggrh tpftndyrpq fyfrttdvtg tiklpadkqm vmpgdnatft
      361 velikpiamq eglkfsireg grtvgagvvt kinn
//
LOCUS       WP_010421684              92 aa            linear   BCT 01-JAN-2025
DEFINITION  co-chaperone GroES [Anaerophaga thermohalophila].
ACCESSION   WP_010421684
VERSION     WP_010421684.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF001531.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK00364
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     gene            1..92
                     /gene="groES"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
     Protein         1..92
                     /product="co-chaperone GroES"
                     /calculated_mol_wt=9742
     Region          7..91
                     /region_name="GroES"
                     /note="Co-chaperonin GroES (HSP10) [Posttranslational
                     modification, protein turnover, chaperones]; COG0234"
                     /db_xref="CDD:440004"
ORIGIN      
        1 mstlkgkila gkvlvkpqaa eektssgiii pdsakekpqk gevvlvgadk kdepmqvkpg
       61 dvvlygkyag telnidgedy llisqndily ia
//
LOCUS       WP_010421720             406 aa            linear   BCT 01-JAN-2025
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme [Anaerophaga
            thermohalophila].
ACCESSION   WP_010421720
VERSION     WP_010421720.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 406)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..406
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=44951
     Region          4..401
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mglniqeirn dfpilaekvy gkplvyfdna attqkplsvi eaeadvyrri nsnihrsvhh
       61 lgnlcteafe evrkkvagfi nagsneeiif tkgttesinl latslgehlf segdevilte
      121 mehhsnivpw qllqkrkgih ikvvpvtddg eldmdafgkl fsgktkivsv thisnvmgti
      181 npvgkmieka hafdvpviid gaqaihhlpv dvqkldcdfy vfsahkmygp tgvgilygkr
      241 ewlekmepyq gggemidkvs fsgttfnelp ykfeagtpnf agvialgaal eylesknlnd
      301 iwdyehdlfe ygmkkmkavp girligqasd htsvisfllg kahpfdvgtl ldklgfalrt
      361 ghhcaqplmd rfgipgtvra sfafyntrde idrlvgalnr vgtmle
//
LOCUS       WP_010421847              80 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Anaerophaga thermohalophila].
ACCESSION   WP_010421847
VERSION     WP_010421847.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..80
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=8836
     Region          1..>73
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdktqlskwv ndftddlyqr arhktgdphl asdlvqdtfm aaaesledfr nesspktwlf
       61 aihcvangik hrspsgsgmg
//
LOCUS       WP_010421859             120 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010421859
VERSION     WP_010421859.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..120
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13176
     Region          40..>116
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 menykihtpe tapegakeil ssvqkqngfl pnlygimans pavikayqql gklfgqttfs
       61 rveqnlvwlt vsktnnchyc lpihtmtakm skvpddvida irnntpiksd pklealslcg
//
LOCUS       WP_010421996             805 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Anaerophaga thermohalophila].
ACCESSION   WP_010421996
VERSION     WP_010421996.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 805)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 805)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12785913
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..805
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91730
     Region          6..421
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
     Region          <286..786
                     /region_name="ADOP"
                     /note="Acidobacterial duplicated orphan permease;
                     TIGR03434"
                     /db_xref="CDD:274576"
ORIGIN      
        1 mriwsyints frtlflhrgf sllilfglsv giamsifvle yvyyqfsydk hyrdsdniyr
       61 vvskgklene yvdvaltpmv laselqkypg vsaltriidt sekpvqsdys kayesdiifa
      121 dssffsvffr pfvlgdakdc fsdstgiais rsaasrlfan hnpigeiiri netdtfvvrg
      181 vyqdvpdnsh fkydivlpyr ivekqlkehy gqsyqeiees wfslityvyv ktkpgteadl
      241 ladrfnseiq temeeqrdel fdplsqtyln yhfqklediy lfsncdfeig ettsplyvyi
      301 flgiaffill vtafnfmnlt tsraldrvre agvrrifgar rgslvarfis esvlfsfial
      361 flglvlvell lpyfsdlfrm dfldqnyreq inmswvlvgt llvgvlsgly palvfsgirp
      421 vhlytgqntf ssypgiwfrg alvfiqvfva vvlcavaigm wrqmnfvkny dlgfdpqnlv
      481 lierarylge dvdsvisels kidgvshvsk mysnpgepvs imsfnlaeds trtyflsvfy
      541 vdctvfetlq akiksgkvhc ndtsriline eaasmmnisk ldgqklqtma sgggdikeyp
      601 itgiienvym gslkntlrpa mfvpvqshei prsllvrysd idyssvyrri kevwdrsgtg
      661 apflggliae rldnfyredy rysslatafa vlvvimaslg mtglvsflia trrhgfflrk
      721 ltgfpdfhii lslfrgylrf vlagvvlalp vsqillniwl etfsvhyysd ylcfvvsavl
      781 ltgiaagivy ygvrklrkqm slhqf
//
LOCUS       WP_010422013             205 aa            linear   BCT 01-JAN-2025
DEFINITION  SCO family protein [Rickettsia helvetica].
ACCESSION   WP_010422013
VERSION     WP_010422013.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11133300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..205
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23271
     Region          50..185
                     /region_name="SCO1-SenC"
                     /note="SCO1/SenC; pfam02630"
                     /db_xref="CDD:460630"
ORIGIN      
        1 mkmqsniiki iivislligv galylllslr tpekplagqv niyednvkig gdfelidqng
       61 eifnsdelkg nlsliyfgft scpdicptsl nkmteiveil nkhkidilpv fitidpkrdt
      121 pivlkeylkh fhpkfigltg neqqikdvtn kfkvfyarvn gddddpnyml dhssftylid
      181 ahgkylkhfy ldsspkeime flkgn
//
LOCUS       WP_010422047            2772 aa            linear   BCT 01-JAN-2025
DEFINITION  T9SS type A sorting domain-containing protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010422047
VERSION     WP_010422047.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 2772)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2772
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..2772
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=298378
     Region          346..2076
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          2712..2771
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 mkkfyivlvg lilglitgvd afaqqtwyal nsgewnnpdn wtldpaaaiy vtedegyple
       61 gddvviksgr titmptegds fsahcnvltv dgrldlknts ghnfseirgs griimegdnf
      121 psgdasnfvg egkgtvvykg sgydisdhtf ynveidlegt dpkvnlagdl tvngnfsvln
      181 gnfqfgnnnt trtltvkgni tvnngasmtv nsanaahnly srgnitnngs iqftnlsnpd
      241 ydstptdgyv iltvkgesnt vltannttfl qrlildkgsd rtyrftvnps qreyfrlfgq
      301 ndtvseekal yikngtlelt gatyihslte ggddfyvpet ggfwinggav evnstavsnn
      361 adgftstgve vnavgsqsfs vlgkfritdg tlnththgfv awdsgnalvq ieggtvktpg
      421 frsagnqegr wtynqsgghv fmkggiesdl npqgkatfsi egvnnvfimt ggtmeiqdaa
      481 tgndlaidiq sgegkfnvtg gtikinriag tsgefnisst apffnleiag vsntatalln
      541 seltvlndli vrengildvt snnyalnigr dltlesgssi dlrsnitsfi gsqnsvitva
      601 eglslnfnnv dvnkeisyng yfevsssgsg vniegdlnvt rgnfvvsasg iniggsiylf
      661 dgnisggsit lngntqqtly skyrkeksig dfnfdnsgsk pqiilasdll inslsfnrdq
      721 vvmlgnynle lansqlsttg wgnsrmfatn grasnggltl pvvldgsynd diaqyfpigy
      781 tvdgeyyftp atvrvdgaln dsgsinvkhv aanhptvdnp ndvapyywkt sysglstvgs
      841 snmryiftyf enisnvpsgk gmiftannew ydagndvrdg snlyfdygdp lltdytygkn
      901 nafnnvrtly sltsgpfnqs stwtesadhq gsstsraprs ydmvviggan gvnhtvtisg
      961 derasqvyik gksetgigvg ddnvdpptfe vtsgasgaat ynyslwggwg yvsgnefssi
     1021 kgkgrflihg dnmpsadfse fcngneaife ytgigaysip essyvtlklf gvidygqeli
     1081 felnqypnlh itesgtktag didltvngnl fvedatfnis nqnngdidiv gnleintgnl
     1141 vlpntesrvl nvdgdfffsg dgdfyvsggg saiehsvnly gnlmqesgai dlsgntakan
     1201 iyfigsnsve fsksgtditn fnrvyinkpi geqvlfsgnf nlnsnlnndn tktlvlqsgn
     1261 ayldnsalni elssgggmyk ipavselivn qgtislggsd pngaglwldg kltindggka
     1321 qfdegtnnyi eytssgksei evngsgelyv gsqirrspyt eagilkfsqn sdastieigt
     1381 kdagestrgv feilntgssf tqaagaklti knskaggftd fyfdpesvsl gegstieiaa
     1441 gneasepfdm yvnqplenlt fsgnvegklk tvpveilgnl sigtnsvfnt ngldvtihgd
     1501 mtnegsynan enttyfsgla gqsitgntef ynlvknegtd tlrigessav tiandltlnt
     1561 gifdtgendv svkgdfyiag gaytvsgser ngvvlngtss qelsgggtia rlmvdnaagv
     1621 vvptqssait fsdvlklnng ildigrnllv ltenaviegd dsdsfsssnm vqtnlsftda
     1681 gikkyfpadv vsnfvypiga sgkytpvvme nttngneggs irvkaaneph itipvedldn
     1741 vlqynwtlda egisnftanv amhgypadvr gdtasyitar ildeeegiwn kysvddfdgi
     1801 ntilnfsfeg tndagidgdy tagtdeaipd kvqtfvteqd gfwndpdvws vvgggvvpag
     1861 gprgaivqin hevnlqvngh aaykteises gvvnvgntln hrlgkvsgtg tvvvesgslp
     1921 ageyteffse nggtleysgs snysvlaelp qvnnlvfsgs gqrilpnldv dilgdfvieg
     1981 gnvineesrp ltihgnmsrt ggsfdvrqgt iklqgdevqt ingsftdena lynievnnva
     2041 gltlngpvdv gnvitftkgi istsetallt vlnsdnaavn nashlryvng pmqkkinagt
     2101 mfdfpvgddy rygnigvkpa ttglwtaqyf dhaasedgys engvtyvsqn eywsvkaana
     2161 dnaeiklrwd sesgvnpdsp dflvisyeps awgevnfnnk tgdvsggsvm tetlyhnter
     2221 lftfgsgsma eytwlgtist dwfdggnwvg glapsaansv ivdnlnssnn pvigegmday
     2281 csnltietgk tvtlkpgasl eiknnidnng tiilestnsk lsslmlpdsp tktgsvnvkl
     2341 eldakkkfyl sspikyaqln wfypdgdinn dfvyvfredp kwkwirvdda yisenpdlne
     2401 leavygkylq gkelnfsgev nnsdvtktyg rgyylvgnpf ptaidwenpa gwvregfsnt
     2461 iwswvtigee rviqtynngg dnlpgawtle pegydesnis hiapyqsvqm kiettnadlt
     2521 ikrtarvrns daplksasne tfsynliriq tnnnllfdgt viyfneafse gigeedsekq
     2581 fnssenvpei ytrinnsaya inglpalnds efsisisvrn rveadvtmaf dlkefgagys
     2641 vyledketgs winllqqsey vytpaqmgdd hdrfvlhfek aaeiptnvee peqnditgid
     2701 ilgqkefalv risevllqss gaaievmdin grlmnsvtts etetevdlpd nsgvyiirvn
     2761 tgevvktgkv vr
//
LOCUS       WP_010422170             381 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Rickettsia helvetica].
ACCESSION   WP_010422170
VERSION     WP_010422170.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..381
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=43629
     Region          1..362
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 mfqrsieevv eqyaqffpvv gitgprqsgk ttlakmlfph lpyvsledld irmqakedmr
       61 vflskyydga ifdevqhvpe llsylqgvvd dspqkgryvi tgsqnfalnh kitqslagrv
      121 gmvtllplsl aeiqkidnpl tsifkggyps lhslniptir fyqsyiqtyi erdvrqlkni
      181 gdlnqfhnfl klcagrigqi isfsslaqdc gishttarqw lnileascii fflqpfyknf
      241 nkrlikmpkl yfydtglacn llgleqdkql ethylkgaly enlvilellk grlnlglpan
      301 fyfwrdktgh eidcigewgg kikaieikfn stlqkdfikn ltyfskfdpn ienylvyngt
      361 qdgsflntnl iplerisqil k
//
LOCUS       WP_010422200             229 aa            linear   BCT 01-JAN-2025
DEFINITION  pseudouridine synthase [Rickettsia helvetica].
ACCESSION   WP_010422200
VERSION     WP_010422200.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..229
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26077
     Region          3..223
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mhrlakiisn agvcsrrdae kliaegqvkv dgitilspat nvdisnhiev sdilinqsqk
       61 prlwiyykpv glitthkdpl srktvfedlt glprvisigr ldlnseglll ltnsgdlarq
      121 felpssrlkr vyhvraygnp nillksnykn lemdgifynp hsvkllkqnk snswfeivlf
      181 egknreirri feyfglkvnk lirvqygsft ignlkpgdyk einnkilek
//
LOCUS       WP_010422201             337 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010422201
VERSION     WP_010422201.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..337
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38129
     Region          3..257
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mttgkvkfai vgmghigkrh akmiednpda eliavcdvrp aeetgwnnsk vpyfkdftem
       61 lsgmddcdvv nictpnglha sqaiaalerk khvviekpma lsradgekii fkalqvsrhv
      121 fvvmqnrysp psawlkevie kniagkiyfv qlncfwnrdd ryyldngwhg taemdggtlf
      181 tqfshfidml ywlfgditdi kagfndfahq hstdfedsgs vifrfvnggm gninfstavw
      241 drnlestmti igekgtikvs gqymnevtec nimdykmpei ppsnppndyg yykgsaanhq
      301 yvidnviqtl rertyvttna leglkvvdii eriyqqk
//
LOCUS       WP_010422281             256 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide biosynthesis/export family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010422281
VERSION     WP_010422281.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..256
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29049
     Region          <87..227
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mwriiifsli lallsgcmtr rrmvyvqdeg kkkdlgvefl neqeralvqt fdelyvhvss
       61 fseenpemls ggegriggrt stdyslisyq vdengdidlp llgkthvagk nvdevaaqir
      121 eelksyfysp svkvsfvnkn vtvigmvenp gryfysgeni nifqalglag diqeygdrek
      181 vvilresngr irknsvdltd krlfisdfyy lksgdivyve plnrriwgid qvpfslilsa
      241 attsllifdy irrndl
//
LOCUS       WP_010422333              83 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl carrier protein [Anaerophaga thermohalophila].
ACCESSION   WP_010422333
VERSION     WP_010422333.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..83
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9430
     Region          8..83
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 metmvlnkee ikafiaetsf tdpkeikddt mlfeegifds mgllnllsfl eenygvqtdd
       61 tdlveenfqn lkaiedyvar kkg
//
LOCUS       WP_010422362             315 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Anaerophaga thermohalophila].
ACCESSION   WP_010422362
VERSION     WP_010422362.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..315
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35882
     Region          5..186
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(8,10,94)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(41,93..94)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            92..94
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mdlsiviply neeeslpeli awidevlqkm rvsfevvlvd dgssdkswet ilnlksrfgy
       61 lrgirfrrny gksaalntgf kaakgdvvit mdadlqdnpd eipelyrlir kegfdlvsgw
      121 kkkrrdplnk tlpsklfnlt arlvsgiklh dfncglkayk sevvknievy gemhryipil
      181 vkragfnnit ekivnhherk ygvskfgmdr flkgfldlls vmfiskfgnr pmhlfgalgt
      241 lmfligfala iwlgahklyc vahgveaqlv tnnpffyigl vcmilgtqlf vtgflaelvt
      301 rnqpdrnvys ikeef
//
LOCUS       WP_010422490             264 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010422490
VERSION     WP_010422490.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..264
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=29542
     Region          12..260
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mtdykeicer tvdiaretgl fvknyrmqnk pdveskgrnd fvtqidkase kklvealgrl
       61 lpeagfiaee ntsdkqgety nwiidpidgt tnfihgvfpy aisialqekd rivagviyep
      121 vmdecfyswt ggpallngke ihvsetskva dsliatgfpy snyslinnfm dtldffmkns
      181 hglrrmgsaa vdlayvacgr fdafyeynlk pwdvaagafl vqqaggrvsd fkggdnylfg
      241 keivcanskm feemqkvieq imtk
//
LOCUS       WP_010422496             432 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Anaerophaga thermohalophila].
ACCESSION   WP_010422496
VERSION     WP_010422496.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..432
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=47552
     Region          12..432
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mnniarlyef flesgkvstd trniipgslf falkgkrfdg nsfakdalna gcrlavvddk
       61 nlkgekdcfw vpdvlkalqe larlhrrkmn ipvigitgsn gktttkelia avlakkynvw
      121 ytqgnlnnhi gvpltllsmp patriaviem ganhvgeiag lceialpdhg litnvgkahl
      181 egfgsfegvk kakgelydfl kknggeifin vdnpdllkma ghypwigygs gkdavvkaen
      241 vsadpmlsfe lttsrvsrmt ittrltglyn kdnvlaaasv ahyfgveeel vkealeryep
      301 knnrsqlfht krnqillday nanpmsmkaa ldnframnhh rkvliiggmk elgndslaeh
      361 rnliaeisel dfticfltgp efkdvvpagd rfvwydntas lkdalrkaei sgalilikgs
      421 ransledvve vl
//
LOCUS       WP_010422540             322 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudomonas syringae].
ACCESSION   WP_010422540
VERSION     WP_010422540.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35603
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,147,162,164,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 melrnlndia afvssvnags ftaaakqlgl trsavgksiv rlearlqvrl lnrttrslsm
       61 tdegqilyer cvgvlqdldd vedalafrrs tpsgrlrisl pvalgrlhvl qhiecclndw
      121 pslsvditfs drlvdlideg fdlamrigpp kedsrlltrt vayqqmitca spkylaehde
      181 pktpedlseh qclhfvsggr llpwnfrvng ssvpvthggr lqmdsaeslh qsaiaglgia
      241 tlpsyvvndd lrsgklvqll agyaeaaepi rviypskrhl spkirlfidk lveawsprpp
      301 weqqpvkdtt sraknpngmk fs
//
LOCUS       WP_010422610             106 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Anaerophaga thermohalophila].
ACCESSION   WP_010422610
VERSION     WP_010422610.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..106
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11876
     Region          5..105
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(23,25..27,33,56,58..60,62..64,67..68,90,94..95,97)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            59
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mdtrlkvtrq ndmligtled tdrlnatiap evkaqlnsnl nkpevnfiln lqkikfidst
       61 gigvlisalk tarqnngnfy ltnvnkevmd llslmkldkv fdfyeg
//
LOCUS       WP_010422420             239 aa            linear   BCT 01-JAN-2025
DEFINITION  (Fe-S)-binding protein [Anaerophaga thermohalophila].
ACCESSION   WP_010422420
VERSION     WP_010422420.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..239
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26892
     Region          <5..238
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mvvdlfipcf idqlypgtgw nvvkilekag ievnynprqt ccgqatfnsg ywdgsrksae
       61 kflkdfpndr pivipaasca gyvrnhypel fkehpdkked vdrvcknvve ltdflvnhlk
      121 ienfeacfph kvtyhdacsa lreygikdep rrllsnvegl elrelpdntt ccgfggtfmv
      181 kyvpvstamv eqkvenalst gaeyivstea scllniesyi kknelpikti hiadvlarf
//
LOCUS       WP_010422624              79 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl carrier protein [Anaerophaga thermohalophila].
ACCESSION   WP_010422624
VERSION     WP_010422624.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..79
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9202
     Region          1..79
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mdakeirrnl ykvfrqtgip rdviderasl kddlfmddvd macflfylet rfkvevknee
       61 lpklnsvgst inylqqhca
//
LOCUS       WP_010422643             450 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010422643
VERSION     WP_010422643.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..450
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=50929
     Region          173..446
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 midslisgvp gykegwllsl gtmqyfqliv ilvlliagwl ltrpgqikgd tnfkrilfrt
       61 lfwvvrafli iglsiwtlsv vglnireffg tpvvtiagev pispyfvltf vlgvyflvif
      121 nkfikhliar aaeslkfdrs igrqlhrfam lllfvligni wlklagtfil dffnnqlfsv
      181 neanitigti iyallilygv siaisiieii ytrhilsrgl dmgqsktvfq llkyvlwvia
      241 iillldsigi nitvlvassa allvglgfgi qglfndyisg lvvlfeglik vgdvveiese
      301 lvgrvmdvgl rtskiltrdn iimivpnhnf vservinwsy nepktrfhvd vgvaygsdvr
      361 lveklliesa leqnevipdp apfvlfrdfg nssldfrvyf wveevfyvel lkskirfsid
      421 ekfrankiqi pfpqrdlhlk sgweqlntnr
//
LOCUS       WP_010422841             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas
            syringae group].
ACCESSION   WP_010422841
VERSION     WP_010422841.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..259
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28404
     Region          1..255
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mlaleslawa peqtsvcthe hfalkdidlq iaagefvgli gpngsgktsl lrcafrysrp
       61 hsgkvainar diwscsprwc arhvavvaqe fpdafgltll dvanmgraph qgffaadsdh
      121 draivqnaln avglagyeqh rfdtlsggek qrcllaralv qeprlmvlde ptnhldprhq
      181 lellglvkql gmatlasihd lnlaaafcdr lcvihhgrli aqgtprevlt pemlfnvfga
      241 kalvdshplr dypritwip
//
LOCUS       WP_010422852             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Pseudomonas].
ACCESSION   WP_010422852
VERSION     WP_010422852.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..247
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27278
     Region          9..189
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(12,14,97)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(43,96..97)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            95..97
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mttptflsvv ipakneadnl pclikeicta ldgeryeilv vddgstddtl kvlthlkdsg
       61 ltllrilrhe rslgqstsvy haalaangtw latldgdgqn dpadipgmla lvrahangsg
      121 aiqlvaghrv nrrdtaskrw asrfanglrs rllkdatpdt gcglkliera aflrlpyfdh
      181 mhrfipaliq rhngrmvthp vnhrhrqagv skygnldral vgildlvgvw wlirrtrldv
      241 qaqelrp
//
LOCUS       WP_010422893             204 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Anaerophaga thermohalophila].
ACCESSION   WP_010422893
VERSION     WP_010422893.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..204
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=22946
     Region          3..185
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mqhliisahp nensfsnala ealakrsrhn didavirnly evdfnpiltk kdlskikegt
       61 vpediareqe ilndsevisl iyplwwgsfp ailkgyfdrv ltngfafkit tdgpegllkg
      121 kkaflhttmg nsieeyenkg ilkafrqihg qevfgfcgie vaghlfyphi sdsstdmknk
      181 yieealgfyk tvlpdeevvn svkr
//
LOCUS       WP_010422897             303 aa            linear   BCT 01-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010422897
VERSION     WP_010422897.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..303
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33263
     Region          40..293
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 makltslltt filsavytgt maqtplyksf dvtpdsvftk laegpavspd gtlyavnygh
       61 kgtigyvrpd gshglfvdlp egstgngirl wnnekllvad ytghnileid inskaisvla
      121 hneqmsqpnd iaissegtvy asdpdwenns griwmtdqkg nmklleegmg tvngielspd
      181 ekllyvnesn qrniwvfdvl edgtpdnkrl likfedygld gmrcdekgnl yvtriqkgtv
      241 aivapegkii reivlkgdlp tnvafggedg ktvyvtvadr gaieafrtef rgrsfvltel
      301 wkn
//
LOCUS       WP_010422898             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: host attachment protein [spotted fever group].
ACCESSION   WP_010422898
VERSION     WP_010422898.1
KEYWORDS    RefSeq.
SOURCE      spotted fever group
  ORGANISM  spotted fever group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10562447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="spotted fever group"
                     /db_xref="taxon:114277"
     Protein         1..146
                     /product="host attachment protein"
                     /calculated_mol_wt=16429
     Region          9..143
                     /region_name="Host_attach"
                     /note="Protein required for attachment to host cells;
                     pfam10116"
                     /db_xref="CDD:431066"
ORIGIN      
        1 mvstaplkli avidskqmml ydaqgvkitt nkplklsldl eehhhhrekr qslyqnkstp
       61 gslfephtsl kdiehkeaar siikhlekia gndqakykel iivaepqmlg cvrqelkngl
      121 kkmitkeiak dlvqhsvdav eravfs
//
LOCUS       WP_010422902             239 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Rickettsia helvetica].
ACCESSION   WP_010422902
VERSION     WP_010422902.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..239
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26775
     Region          4..211
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 mpqiyfngpe griegryaka tspnapialv lhphplyegn mnnkvvynay kiladngytv
       61 lrinfrgvgg sqgkfdngvg evvdagaafd wlqqnnlnaq snlilgfsfg awiamqlvmr
      121 rpainhfiai sppvntihky dfsflspcpi pgfilqgdnd sivsaddvkd lanrlskqqs
      181 hikvdykiin gadhffrykt eefskaindy litiqsnyhh hnnnvneeis ksqkklfly
//
LOCUS       WP_010422977             209 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Rickettsia helvetica].
ACCESSION   WP_010422977
VERSION     WP_010422977.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..209
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24385
     Region          16..206
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mtycdksnqt shpfilsdlp yekesfkphf tpetfdyhhg khhnayvqnl nnllkdkeel
       61 qkkdleeiie wssqnsnaai fnnaaqiwnh tffwhsikpq gggkpsgkil eqinkdfssf
      121 egfceqfkqe avgqfgsgwv wlvyhdnrlq iiktanagtp iangmkplla cdvwehayyi
      181 dyrnkrpdyv difikhminw kfvednlik
//
LOCUS       WP_010422981             183 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA-3-methyladenine glycosylase I [Pseudomonas].
ACCESSION   WP_010422981
VERSION     WP_010422981.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..183
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=20807
     Region          1..179
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mtrcfwcned plyiayhdqe wgvplrdaqk lfellllegf qaglswitil krraryrevl
       61 hgfdverlaq lsdaeiealm ldpsiirnrl klkavrtnar awlaledpva llwsfvggtp
      121 kinhfkdrse vpaitaeaea mskalrkagf tfvgpticya ymqasgmvmd htvdcdryai
      181 lsr
//
LOCUS       WP_010422990             201 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010422990
VERSION     WP_010422990.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..201
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23225
     Region          3..166
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mkkesiftip nllsfyrlla fpwilylvvs enevlfslfl iinlitdild gllarilrqr
       61 telgarldsa addltytlai igifvfkyee lephlqsfiv fivflilpiv lslikfgrlp
      121 sfhlystkag gyiegiffiv lfsghfivsy yyfmvvwgil asiehiaiqa lipemrsnvk
      181 glywvlmeel rqkkefrdtg r
//
LOCUS       WP_010423041             955 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Rickettsia helvetica].
ACCESSION   WP_010423041
VERSION     WP_010423041.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..955
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=108175
     Region          <605..675
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mavtnnknyq kvignvlsss kankvlksvi kdlsssksis lrtillgarf vltnpvntyn
       61 lvklakssni yldpefqksl lekspiwefl kkhsddlpki gqilakagfr efqdksaldq
      121 kgleilkecf knekvlkklq eiavevkqel pdwnkvasrs ldmlvtdknf kkffneksed
      181 ithyirtgat ailpsdyikt fdnilqkpqs kdiyakviki fneypdfkqe laeninntns
      241 lkrfnklspe kqiiiesfla eakeqakpfl keyfesykid lkildiiptl lnkipetkei
      301 fdtlnapnqg vmisleqsle mvagddklks ffannktilp nialgiient psvqsiikey
      361 nfdkqmlsiv gevmskpeia heiiadlnkg dymsltgnii salndpsfkl kdilveqske
      421 glfdnlitgv leqdeknsqt ikqqlinygl easdvtklts impilldkpe slktvfrdfi
      481 kgdytgmake lialtkdnpe ikeylnnnre vftsildktl vdipginnld kkelynvlps
      541 mlnhpdelvk vieeveksny rgaasaiynl aqktnyfegq lpniikagfs yatekvkdvf
      601 spsqdfkdkt ideitlrnnl nkiqngkfnl egailvgnls nidfsgvslk nadltkvtsl
      661 kdcnfkntnl adaklpdnlm lltdtynldk aipplvpeli keqqaklidk aidkvfiqiq
      721 aegkrnllsk kefvqqvqil yeenqtvkdy iieklnslpm nmvtnlatpk tnqykhitnh
      781 insplqilnp lyeniankqd iksnllanil seqisqklfd kgdnrgkdfy minqmlkpiv
      841 seyskenpdn innflepknl eklasniast lnskskytwa gtitggiylp keifneqlkd
      901 nfknefenin klnvlkeaqs ivsnlnskin ivgsktnals itpisnnkkk eeihr
//
LOCUS       WP_010423047             567 aa            linear   BCT 01-JAN-2025
DEFINITION  S41 family peptidase [Anaerophaga thermohalophila].
ACCESSION   WP_010423047
VERSION     WP_010423047.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..567
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=62885
     Region          52..371
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 makqikntsr hiylpiilav vlvtgmfvgr itaplgqgds srrllmypes gklqtiinli
       61 deqyvdsvdt dklvdnvipe ilekldphsv yipprnleaa nqelegnfgg igvefsmqnd
      121 tvmvisvvsg gpsekvgilp gdriitvndt viagvgmptn dvvgmlrgdi gtkvnvgikr
      181 rnrdklidfe itrgniplys vdvaymidds igyikvnrfa rntyqellsg larlkadncr
      241 hiimdlrgns ggyldiaism vnefldkgdm ivytegvhsp rqevhangsg sckntditvl
      301 idefsasase ifagamqdnd rgvvvgrrsf gkglvqqqfp lpaggalrlt varyytpsgr
      361 ciqkpydngv edyyrdiiyr yehgeffnrd sinindslvy ktiggrkvyg gggimpdvfv
      421 ardtsnhtdy yynlresgvi yqfaldysdk nrnelsefet veqleayldr qpigdmlvsf
      481 anrkdvkyna seyqiskeli vnetkayiar nildnegfyp iirkhdevln kalevirsga
      541 adsilhvdsa qasevsesta datepni
//
LOCUS       WP_010423133             317 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Anaerophaga thermohalophila].
ACCESSION   WP_010423133
VERSION     WP_010423133.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..317
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34734
     Region          5..228
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 meniieiegl tktygqykav nnlnltierg evfgllgpng agksttllml lgltepdegs
       61 akvcgidpvq fpirvkkkvg ylpedvgfyd dlsgfdnlvf tarlnnipqd iaekkahell
      121 gkvglerekd kmagkysrgm rqrlgladvl ikepeviild eptlgidpag vktflqlivk
      181 lsredgitvl fsshllyqvq qvcdrvgifv egkllaqgni gelsrqlfss nshvieggve
      241 plngnsskal svedlanrvk eipgvakvsf edrrfvleae sdiahlvsav ivesgyglsy
      301 lskkeygldd iysryfq
//
LOCUS       WP_010423080             175 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma carbonic anhydrase family protein [Rickettsia helvetica].
ACCESSION   WP_010423080
VERSION     WP_010423080.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..175
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19372
     Region          1..168
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mliipykgvt pridksvyia esssligdve igsnssiwfn tvlrgdvesi kignntnvqd
       61 gsvihtsrfn gpveigdnit ighlslihac tihnnafigm rttimdyavi eeyafiaags
      121 lippkkiiks kelwmgspak fvryltdqdl eymqdnvrny vklanvykir chpva
//
LOCUS       WP_010423545             156 aa            linear   BCT 01-JAN-2025
DEFINITION  NfeD family protein [Rickettsia helvetica].
ACCESSION   WP_010423545
VERSION     WP_010423545.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..156
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=17581
     Region          17..153
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mfminnylte iwliigiici vveffaipsi gflffglgal sntlvvynyt lvgltnqitf
       61 fgilsliwfc ilyyplkkyv ynktdkteny sdmigktvev ysatvssdti gqvrwsgtim
      121 naylapneid aktgdrlfii evkgnvlics khrpkt
//
LOCUS       WP_010423580             443 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010423580
VERSION     WP_010423580.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..443
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50680
     Region          177..437
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 mrhsitvlfv iflyagnsal taqqidfynl eeeqlynpdr kyntwsvtag igpviyytdv
       61 nnyallpssh wrfgpsvlvs kqfgrpwsld aqfltadmyg ekniryfsgs fydlslnlnf
      121 sinqlvlfgp irdklniygk lglgvnyfrs rqrsletgdw itvgevhsgt pgyprpygwa
      181 dtdylaigyd rqnpedktsr gsevivpigv gidyrinknf dvgfeltlrn vtqdnldvnl
      241 tgadndsyma alltftykig kknkrhslwt ykdfnlayqr eretdplare ldslrrrldy
      301 iaandssvtd tsfvykesvi qkddltasvf fefdkarita ashktlavva rfmkengder
      361 vlvqgycder gsddynvkls qrrcdavidv lvndygidrn rfetepmget dllsdtkela
      421 prgvhrvnrr vdifllkgqk tee
//
LOCUS       WP_010423598             248 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010423598
VERSION     WP_010423598.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..248
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27021
     Region          7..245
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mgeltvlliv vsgvvilmss llkgmtgfgf allaipflsl iypvkvlvpa mtifnlitsv
       61 illlkireri swyyfipmfv aslggiplgi ylldyldeev lriiigvtli flslkmlsgi
      121 plarrfrdkp vffagflsgi lsgsvslggp plviamsrkn ynkdlfrgif awfsvfssff
      181 alagfyakgm ipgdslrlsl yytpllflgs slgnklaalv naekfkrviv vvnvftgvit
      241 visaiisl
//
LOCUS       WP_010423629             219 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Rickettsia helvetica].
ACCESSION   WP_010423629
VERSION     WP_010423629.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..219
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=25022
     Region          <72..216
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(94..96,98..99,103,106,120,122,124,128..129,132..134,
                     136..137,141,144,153,155,157,161..162,165..167,169..170,
                     174,177)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          122..153
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          155..183
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          188..214
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mkkqveqiei tddiirnkfy eilsgkdiee qqtmgfnnid eikryqffre sfvkeftafi
       61 edpnkdvdsv hygayiniak iarnprdfta kaiqqgdydl vdtlltalsi dpnkvayisd
      121 aaagsllyfa cinnqkeiar llikkganik faddfgmipl ynaiearhld mvefllenga
      181 dpnymgrkif scleivtfry kdiamvtkll aygaliwkl
//
LOCUS       WP_010423718             399 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Rickettsia helvetica].
ACCESSION   WP_010423718
VERSION     WP_010423718.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..399
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42986
     Region          1..397
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mklwqkvtlg lilgiifgiy lpqyvnyikp igdiflrlik miitpliffs lvsgitsmnd
       61 tsalgrvgmk avaaflgttf fatvfgltva lvlkpgvdih idftssgtts rtsfniidff
      121 vnivpdnavg afangdvlqv vffaifvgit lnkmksigep itdlihvmsk lilkmisfvi
      181 qlspygafal tgwivgmqgv evmislsklv vavvvamtfq ylvfglliyv fcrvspipfy
      241 kksfeyqila fstssskatl attmqvcrek lgisesstsf vlpigasinm dgfainlslt
      301 tiffaqmmgv tlaphdylvi iltstlgsig gagipgasli mlpmvlsavh lpiegvaiia
      361 gidrildmlr ttinitgdat itmiidnsed tldkevyls
//
LOCUS       WP_010423814             160 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Rickettsia helvetica].
ACCESSION   WP_010423814
VERSION     WP_010423814.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..160
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=17757
     Region          14..156
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 magtviesqf kdamsrfpqg vtiittncnn epfgftassf tsvslkppli lfclnknsfs
       61 insfqksdkf avsmladnqi diskyfaksq pnkftkidye lgnktdcpli ngatchiecn
      121 kyasydagdh vifigevint aikndlkpll yfhksytrli
//
LOCUS       WP_010423820             853 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [Pseudomonas].
ACCESSION   WP_010423820
VERSION     WP_010423820.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..853
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=93366
     Region          10..777
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mlkdltalfa pqnrrliklt tvardeqell lerfsgtesl selfsfelsm isrdaglelk
       61 sqigqpaqla ielatgesrf ingyistfsl egsdgglary satlspwlwm lsrrvdsrif
      121 qeqtieavir tvfaaygalp dfefqlsqpl kthsyitqyr esdltfvlrl leheglffyf
      181 dhnqekhtli ildhsrdlsp lpqqptiryh sasvtetads itewrshrrl qsgrmsiqtf
      241 dykqprnslp vgmpslneqg nvdsyevydv ldhyshgtfn dgerlvrqrl eaievqgktf
      301 tgnsncramy pghtfeltqh fdhdrgsaed rsfllitvkh egsnnylsde sagytnefvc
      361 irhkipyrhp itvprpsiag plsaivvgpe geevftdela riqvrfhwqr gdslpqgttw
      421 lrvampsags gfghqfmpri gqevlvtfla gdidrplvts vlynninlpp rfskasglpg
      481 nrtlsgirtq ehkgsgfnel lfddtpgslr armgtthqat alnlgkltdp rtdgtaqprg
      541 ngaelrtdaa ialraaqgml lttyartdak gsqldreell kllaecgelf kslgetaaar
      601 ggqavdvkgi ealrqsldqw papdnnglgd pvlamtaaag iasatprsqa hyagenhdtt
      661 aqdnlqltsg aamhlqagkg lsafaqdagi saianrgkvl vqaqeddial naqknlhvsa
      721 vegevvitap tirlvaddgs yikigggvei gsqgkvtvha sehdwigpkt dsaaipsfgr
      781 dpaaqqvtfh ypghseqspr aaadhsyeik ledgslvkgm tnadglterv eremmhqaqv
      841 salrsgtpkg gaq
//
LOCUS       WP_010423886             368 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010423886
VERSION     WP_010423886.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..368
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42409
     Region          18..364
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mkvyiyenef wpnftwndqe iieilgkvrn lqgrivgkme slgfnlkqqa eletlkteil
       61 rsseiegeil npeqvrssia rklgmdisgl ipsdrnvegi vdmmldatqn fsqpltkerl
      121 fdwhyalfpt grsgmykviv gnwrndstgp mqvisgpmgk ekvhfqapaa trieeemntf
      181 ldwfnnyeki dlvlkagiah lwfvtihpfe dgngriarti sdmllaradg isqrfysmsa
      241 qirqerkeyy eilektqkgd lnitkwltwf lscllnalne sniilekvis khnfwienal
      301 kiqnerqklm lnkildgdff gkltsskwak itkcspdtal rdiqdlidkg ilkktekggr
      361 stnyelie
//
LOCUS       WP_010423988             252 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [spotted fever
            group].
ACCESSION   WP_010423988
VERSION     WP_010423988.1
KEYWORDS    RefSeq.
SOURCE      spotted fever group
  ORGANISM  spotted fever group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="spotted fever group"
                     /db_xref="taxon:114277"
     Protein         1..252
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27528
     Region          9..242
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 msekeefkik iqslyksfan hkvldgidld vkkgsslvil ggsgsgksvl iknivglikp
       61 dkgkifidnv eiqdisskqk feimdgigfl fqggalfdsl nicdnitfet kklskkeknd
      121 lagaklnsvg lsprildlyp selsggmqkr valaraicst psilfldept tgldpimanv
      181 ineliikiqe elgattitit hdmisaekia kevamiyqgk ikwygskdem rnsdnpylkq
      241 finglttgpi ev
//
LOCUS       WP_010424097              79 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF433 domain-containing protein [Anaerophaga thermohalophila].
ACCESSION   WP_010424097
VERSION     WP_010424097.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Sala,A., Bordes,P. and Genevaux,P.
  TITLE     Multiple toxin-antitoxin systems in Mycobacterium tuberculosis
  JOURNAL   Toxins (Basel) 6 (3), 1002-1020 (2014)
   PUBMED   24662523
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..79
                     /product="DUF433 domain-containing protein"
                     /calculated_mol_wt=8871
     Region          7..66
                     /region_name="COG2442"
                     /note="Predicted antitoxin component of a toxin-antitoxin
                     system, DUF433 family [Defense mechanisms]"
                     /db_xref="CDD:441983"
ORIGIN      
        1 mgknnfldri tinpeichgk pcirnmrwpv eviidmlgse msideiiedh pelekedila
       61 slnfaklyms gisvnqdva
//
LOCUS       WP_010424562             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Pseudomonas].
ACCESSION   WP_010424562
VERSION     WP_010424562.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..219
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24081
     Region          10..219
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 msdsliieps spadacviwl hglgadrydf lpvaealqes lrstrfvlpq aptravtvng
       61 gyampswydi ksmssearai dhdqmeasaq kvldlieqqr dsgidparif lagfsqggav
      121 vlhagyrrwq gplggvlals tyaptfssem tlsasqqrip ayclhgkhda vvpypmgrav
      181 ydhltaqgvt vewqeypmeh qvlpeeirdi gvwlaerlr
//
LOCUS       WP_010424612             419 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphoglycerate kinase [Anaerophaga thermohalophila].
ACCESSION   WP_010424612
VERSION     WP_010424612.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..419
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=45226
     Region          4..418
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mskiesynfs gkkaivrvdf nvplnekfei tddtrikaal ptlkkiisdg gsvivmshlg
       61 rpngkanpdl smkhvqgrla elldtevlfa kdcvgpdake kaaalqpgqv lmlenlrfhl
      121 eeegkpklae daseeekkaa kaemkekqqt fskelaslad vyvndafgta hrahastavi
      181 adffdsdkkm fgflieqelq sldkvlkspd rpftaimgga kvstkitiie nlldkvnnli
      241 lgggmtytfi karggqigds icedeylela rkiekmakek gvnlylpvdv vaadafenna
      301 ntrivpvdqi pdgwqgldag petikiyqdv iensktilwn gpvgvfeldt fakgsravad
      361 aiaaatkkga fsligggdsv acinkfglad evsyistagg alleylegke lpgikairg
//
LOCUS       WP_010424586             197 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010424586
VERSION     WP_010424586.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..197
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22591
     Region          9..>121
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mkpltikgek vlnvpnllsl yrllvfpvil fmaltgrenw fvillcislv sdildgniar
       61 ffnqqthfga aldnladivt yamallglfi fkwneiepha wilylflgvf ilsyiisflr
      121 fgkipglhly savsagylqg ifffilfvfg fwpwlyylav gwgaiayiek ilvllklddi
      181 kigvkglywl lkdernr
//
LOCUS       WP_010425093             234 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Anaerophaga thermohalophila].
ACCESSION   WP_010425093
VERSION     WP_010425093.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..234
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25796
     Region          3..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnsnvilied lhkhyhlgtq vvkalngvtl sidkgeyvai mgpsgsgkst lmnligaldt
       61 pskgryvlng tdvshlsdde laeirnreig fvfqtfnlls rysalenvvl pliyagvpre
      121 erykrgeeal rnvgladrml hkpnelsggq rqrvavaral vnhpslilad eptgnldskt
      181 svdimrlfdr ihaegntivl vtheediakh aerivrlrdg vvesdvmnee kvqa
//
LOCUS       WP_010425176             273 aa            linear   BCT 01-JAN-2025
DEFINITION  acyltransferase [Pseudomonas syringae].
ACCESSION   WP_010425176
VERSION     WP_010425176.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..273
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=30505
     Region          124..255
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mkhrmmhshn lrealpdyar kmavplnele aayqwmldne vcfetrlrer tlsficylni
       61 epriehplar rfykllaiet kgpliplygi nwptlrdrml rtweqaynil ickipshtlr
      121 llwlrigrak igkgstvwrn tevlgvdslr igndstvgwh cqldargglv igdhvtiash
      181 vliiagghdl nepefwavgg pvfigdyawi csrallsfga digegavvgg nsvvskpvpp
      241 yaivsgpnae ikgerargln ykvggkglft lfh
//
LOCUS       WP_010425219             314 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pseudomonas syringae].
ACCESSION   WP_010425219
VERSION     WP_010425219.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..314
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34564
     Region          58..296
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 msisplarfk arplrwismi avilglpvgc avlehkerel vfriepgtas wysglpadvq
       61 eielstpafg tsqnihawww paadknapav lylhgsrwnl tgqlfriqql kaqgysilai
      121 dyrgfgqsmg qlpsersvye dariawerlk qlqpdpqrrl iyghslggav avdlaaelge
      181 naekdnvpiq argliiestf tnladvatal antslpvrwl lsqkfdsldk iadihmpvli
      241 vhgtedryvp srfseqlfaa arepkklllv pggthnnsmq lgqpaysrai ralldtpasl
      301 pqvtkqgkds knag
//
LOCUS       WP_010425560             318 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010425560
VERSION     WP_010425560.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13797492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..318
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34002
     Region          7..196
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          <210..313
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mptcsndpis elllgmrlfg vqfrrlevvq plgigfsnai graqfhfvgr gpvwlrsaen
       61 vlcrldsgda vliprgghha ilpaedtaas diplfdpspg ivdgvhngay deeggvsdha
      121 iifsccmele lggmqplvaa mpdvmqvstl letcpelrpm laameretlm lqaghagila
      181 rlaevvaall vrgwvaggcg naagwlgalq dprlsraivm mhqrpgrrwt vatlarearh
      241 srsvfaqrfl eatgmpplqy ltelrmrlal hslsrehcsl eavasqlgyg slaafsrafk
      301 rtvglspgav raakgvav
//
LOCUS       WP_010425884             219 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Pseudomonas syringae].
ACCESSION   WP_010425884
VERSION     WP_010425884.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..219
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24701
     Region          5..218
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtfkapdsla eqiahhlaer iirgelkpge riqeqkvtqa lnvsrgsvre allilerrhl
       61 vvilprrgaq vtvlnahnvt slccmmrely illanavver wtteedlapf mqiqqrlqas
      121 feqqdvnafv eesfnvmraa ypfannpyle etvenlqpsm srsyfialeq rkadmgdyla
      181 lfdellsavv ardipkirvv lvsycqrscq lvlaalaag
//
LOCUS       WP_010423508             167 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Rickettsia helvetica].
ACCESSION   WP_010423508
VERSION     WP_010423508.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Stamler,R., Kappe,G., Boelens,W. and Slingsby,C.
  TITLE     Wrapping the alpha-crystallin domain fold in a chaperone assembly
  JOURNAL   J Mol Biol 353 (1), 68-79 (2005)
   PUBMED   16165157
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Narberhaus,F.
  TITLE     Alpha-crystallin-type heat shock proteins: socializing
            minichaperones in the context of a multichaperone network
  JOURNAL   Microbiol Mol Biol Rev 66 (1), 64-93 (2002)
   PUBMED   11875128
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Haslbeck,M. and Buchner,J.
  TITLE     Chaperone function of sHsps
  JOURNAL   Prog Mol Subcell Biol 28, 37-59 (2002)
   PUBMED   11908065
REFERENCE   4  (residues 1 to 167)
  AUTHORS   MacRae,T.H.
  TITLE     Structure and function of small heat shock/alpha-crystallin
            proteins: established concepts and emerging ideas
  JOURNAL   Cell Mol Life Sci 57 (6), 899-913 (2000)
   PUBMED   10950306
REFERENCE   5  (residues 1 to 167)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10157978
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..167
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_process="GO:0006950 - response to stress [Evidence
                     IEA]"
                     /calculated_mol_wt=18949
     Region          69..153
                     /region_name="ACD_sHsps-like"
                     /note="Alpha-crystallin domain (ACD) of
                     alpha-crystallin-type small(s) heat shock proteins (Hsps).
                     sHsps are small stress induced proteins with monomeric
                     masses between 12 -43 kDa, whose common feature is the
                     Alpha-crystallin domain (ACD). sHsps are generally...;
                     cd06464"
                     /db_xref="CDD:107221"
     Site            order(69..73,80,82,84..85,145..146)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:107221"
ORIGIN      
        1 mlksvrlyip siaaiilssn iaianknyds ghamplrqvv dlidnqitni dnlfknrlpl
       61 yefnsiksnf itkdkhyiii mevpgfdksq ikvkvngnkl fitgnieekn kgddsdnymn
      121 knfnyvmsly edvdqaniss slkngiltii lprieikeqe areipin
//
LOCUS       WP_010426022             299 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Enterobacter].
ACCESSION   WP_010426022
VERSION     WP_010426022.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33383
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdkihamqlf irvaelesfs raaetlslpk gsvsrqiqal enqlgtqllh rttrrvsltq
       61 dgmvyyertk dllanldeld smflhdpssi sgrlrvdmpv gvarnlvipk lpaflqqypg
      121 ielelsssdr lvdviregfd cvvrvgtlkd sgliarplgk lsvincaspa yltrfgypet
      181 ledlashavi hyaatlgtrp qgfefyngst tqwvktggvl tvnstetyqa aclaglgiiq
      241 vprvgvrdll rtkklveilp qyraepmpvs liyphrrnls rrvhlfmewl teltkayvd
//
LOCUS       WP_010426386             191 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas].
ACCESSION   WP_010426386
VERSION     WP_010426386.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12134272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..191
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22206
     Region          19..159
                     /region_name="Acetyltransf_3"
                     /note="Acetyltransferase (GNAT) domain; pfam13302"
                     /db_xref="CDD:379112"
ORIGIN      
        1 mpdithlsai ltptlytprl vlrplqleda aamqhlfnqw evvrylthhv pwpypdgetl
       61 rylredalpa mqdgeewhws irlcgeqdhl igaacmmdep dnnrgfwlsp pyqglglmse
      121 vcvaidrfwf etlkrpvlrv aksalneasc rlsrregmrl vtvqeaqfvc gttqeqiwel
      181 trqewqmnnn r
//
LOCUS       WP_010426396             302 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterobacter mori].
ACCESSION   WP_010426396
VERSION     WP_010426396.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..302
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34910
     Region          1..218
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 maflsviiaa hnaedtlhat leslhaamdn agdaveviif ndssddatqd iiekwlpafp
       61 haqsryveyr nvghvrnsav slasgdyitm ldsddrlkpc slrdavaflk aqrpdmlltr
      121 lletrdirki tafwqgftpv sfsqneaikr flqhkefqah ligqffhrkl yesnpipsmv
      181 cyedfavfpa mlmqaekicy qrqghyyyik rseslssrld askittlvec tlkmektfpq
      241 afknlinchw fdiysnhrqh ltdqqlkfvk srvnalysls fflssdvrfs ykkrviealw
      301 kk
//
LOCUS       WP_010426631             285 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Pseudomonas congelans].
ACCESSION   WP_010426631
VERSION     WP_010426631.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..285
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29784
     Region          9..259
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 msialkqptl tgqcvaeflg talmiffgtg cvaalkvaga tfglweisii wgiavsmgiy
       61 lsagisgahl npavsialsl fagfekrklp fyisaqiaga fcgaglvyll yislffdfeh
      121 ahhiirgseq slelasvfst ypnpaisvgq aflvelvitt ilmgvimalg ddsnglprgp
      181 laplligllv avigssmgpl tgfamnpard fgpklmtffa gwgemaftgg rdipyflvpi
      241 fapilgaclg aagyraliar hlpsavpven ekeapvvrgk vqvss
//
LOCUS       WP_010426775             195 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudomonas].
ACCESSION   WP_010426775
VERSION     WP_010426775.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..195
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21564
     Region          79..176
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mstldeagrr eyyriddsva leinplsaad qasqdamqdt stlfdllsel hvsefesqhl
       61 mrqlderdrv lnsflkslsk ridllgevva htalgklgap qpvklseggi qfnsqqaftv
      121 geqlsikmvl mpqaaglmlr arvcqcdtla dgnfdistef vnlpdaqrql larhvlqrqa
      181 qqrrqaleqg qpsgn
//
LOCUS       WP_010426813             529 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Pseudomonas syringae].
ACCESSION   WP_010426813
VERSION     WP_010426813.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..529
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=60476
     Region          6..521
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mssffpfqiv dlfsgpggls egfasfkdgk qfkiivsaem dpiahktlml rayfrllnse
       61 apdhkkdyyd ycngiskkpy snvtehlwnk akkeancltl gdekdnfkld tmikdrllsn
      121 qpwvliggpp cqayslagrs rnmgktdyka eedhrhflyl eylriiqknr ptvfvmenvk
      181 gilssqvnge kifpkilkdl eapdlalnka dtglrynifs lvadeeqdfe lipndvdpkk
      241 yiiraehygi pqarhrvill gvlenkntpv iklkklekrr evtvsevigt lpklrsklsk
      301 skdspekwcl eildqieaie tpavargrse itervrfire klgeiletgd lryiknkneg
      361 ktgtselddw fldsqlnvwl nhetrghmps dlrrylyasv yadannrspr ghlefnlpgl
      421 spdhknwetg kfcdrfkvqv khapsttits hiskdghyfi hpdphqcrsl tvreaarlqt
      481 fpdnyffegn rtqqyhqvgn avppllasqi aaivsdaleq ntkvvstqr
//
LOCUS       WP_010426836             159 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010426836
VERSION     WP_010426836.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..159
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17884
     Region          3..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mqieldnydr rilallqeda slssaqiaeq vglsqspcwr riqrlkdegv irrqvalldr
       61 kkiglntqif aevklnahgr snfteftdai rgfpevlecy vlmgsvdfll rivtpdieay
      121 erfffeklsl vpgiqevnst valseikstt slpllrqgg
//
LOCUS       WP_010426899             415 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Enterobacter mori].
ACCESSION   WP_010426899
VERSION     WP_010426899.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..415
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46886
     Region          236..405
                     /region_name="CE4_yadE_5s"
                     /note="Putative catalytic polysaccharide deacetylase
                     domain of uncharacterized protein yadE and similar
                     proteins; cd10966"
                     /db_xref="CDD:213024"
     Site            order(245..246,307,312,354..356)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213024"
ORIGIN      
        1 mlmrviflll llfsggtsas lisqqglpar ymqttedaai waqvgsnvin vgnvragqil
       61 avvptsadyy efrfgfgtgf idkghleevq gkqrvedslg dlnkplsnqn litwkdtpvy
      121 napnsgsapf gtmspnlryp ilsklkdrln qtwfqirign rlawvsslda hednglpvlt
      181 yhhilrdeen trfrhtsttt svrafnnqma wlrdqgyatl tmyqlegyvr nkmnlpakav
      241 vitfddglks vsryaypilk eygfnatafi issrikghaq kwdpkslqfm svheikgiqd
      301 vfdiqshthf lhrvdgykhp illsrsyhvt lfdfersrra laqfnprvly lsypfggydn
      361 kaikaandag fhlavttvkg kvkpgdnpfl lkrlyilrtd sletmsrlis nqpqg
//
LOCUS       WP_010427083             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010427083
VERSION     WP_010427083.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..181
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=19032
     Region          <25..175
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          53..83
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(54,58..59,62..64,66..67,71,74,83,85,87,91..92,
                     95..97,99..100,104,107,116,118,120,124..125,128..130,
                     132..133,137,140,149)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          85..116
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          118..149
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          151..175
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mtdtdisask tmtedeaaef aeqvfdvarq gnavmlerll ekglpadlrn hkgdtllmla
       61 syhchadavr vllnhkadpe irndngqspi agaafkgdla vvrllveaga didgasadgr
      121 talmmaamfn rneivdylis qgadphatda kgitalgaaq amgatvtieq ltkmgvqpar
      181 s
//
LOCUS       WP_010426935             123 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Pseudomonas congelans].
ACCESSION   WP_010426935
VERSION     WP_010426935.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..123
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=13092
     Region          1..>67
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mktsqsgftl lemlaaltvm avcsgvllva fgqsarslqq vsrsdrlsha artimdqesa
       61 galengtrrg kiagidwtld irqlpgangq armfrldlll sehqrkaqfs tfklrgavsg
      121 ags
//
LOCUS       WP_010427158             219 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Pseudomonas congelans].
ACCESSION   WP_010427158
VERSION     WP_010427158.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..219
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24609
     Region          5..218
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtfkapdsla eqiahhlaer iirgelkpge riqeqkvtqa lnvsrgsvre allilerrhl
       61 vvilprrgaq vtvlnahnvt slcslmsely illanavver wkteddlapf vqiqqrlqas
      121 feqqdvkafv eesfnvmraa ypfannpyle etvenlqpsm srsyflaleq rkadmgdyla
      181 lfdellgavm vrdvpkirvv lvsycqrscq lvlaalaag
//
LOCUS       WP_010427202             308 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Pseudomonas congelans].
ACCESSION   WP_010427202
VERSION     WP_010427202.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..308
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33379
     Region          1..241
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mqpirlglvg ygkiaqdqhv paihanpafe lvavatqgqp cagvenfksl gellasglqi
       61 daiafctppq grfalvqeal aagkhvlvek ppcatlgeam alvaqvseqg vsglfawhsr
      121 yaqgieaare wlstrtlqsv qidwkedvrk whpgqawiwq pgglgvfdpg inalsivthl
      181 lplplfvesa elrvpsncqs piaasikmsd trhldiraef dfdhghdelw sieircaegi
      241 lrldnggavl sidgvrqavs eegeyaavyr hfqqligdsa sdldlqplrl vadsffvgsr
      301 asvepfyd
//
LOCUS       WP_010427271             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Enterobacter].
ACCESSION   WP_010427271
VERSION     WP_010427271.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..135
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14847
     Region          28..135
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mkntiapprv dlglfflrlt gsllllyvhg lpkvlhfsee ltriedpfgf gpwaslipai
       61 vaevicplfi iagvytrlac lpiiavllva mlavhpnwsi aegqfgwlll iifttlaltg
      121 pgqwrlqrka terfa
//
LOCUS       WP_010427364             378 aa            linear   BCT 01-JAN-2025
DEFINITION  lactonase family protein [Enterobacter mori].
ACCESSION   WP_010427364
VERSION     WP_010427364.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..378
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40341
     Region          17..376
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mhtrtllvas lsmlattaia qtqyawvgty npngeglyrf tvdpqsgala nktlvstlpn
       61 aaqltvshdg ktlylaseve qgvvqalrvg dngelsklnq vasggagpvy lsltpngrhl
      121 lvanyvsgsi avlpvkadgs lgdamdqyqd qgepgaakpe aaaegsfais dhngphahmi
      181 aadpsgkyvf stdlgldrly qyrfddrsgk ltpndpqfis asskgagprh fvltpkgdal
      241 wlineeastl thytvnangt lkegktlsal pegykgtsfa aglalsadgk qlyvanrlhn
      301 sighftvtae gtlthqddvw trgdyprtlt ldkqgrwlyv mnqrsdnitr frvaqdgkls
      361 fepdytpvgs psqmvisp
//
LOCUS       WP_010427385             114 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pentapeptide repeat-containing protein [Pseudomonas].
ACCESSION   WP_010427385
VERSION     WP_010427385.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..114
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=12669
     Region          <34..88
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mshpkqidsp lymllrkddv egfnqekprt gtidmaggdf rgldlreldt agidftdayf
       61 rsadlrgldl rntpmegasi ahaqisgvff paelsadeil msvnfgtrlr yrtr
//
LOCUS       WP_010427412             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Enterobacter].
ACCESSION   WP_010427412
VERSION     WP_010427412.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..389
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42749
     Region          1..346
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mlnvaivgtg nishnhiqgy lqfgqrcriv alvdiypeka eekkarygle darvyeshqq
       61 mlesesnvdi vdvctppyvh aeisidalna gchvlcekpm aasleecdam iaaqqasgkt
      121 lsiiaqnrft dafwrlkaal dsglagkvch aqvdsfwwrg hcyydlwwrg twekegggct
      181 lnhavhhida iqwmlgfpse vvammtnvah dnaevedlsa aifkypsgal tqltasvvhh
      241 gedqkmiiqg dkarisapwq afasvsadng fpqethdqqr eaqlnavfqe tpklewtlht
      301 gqindllyai ehgtaplvdg vqgkrsleli taiyksaitr avvslpigrd dpfyrtggtn
      361 alaprfyeks asvanfsevg aiplgkdld
//
LOCUS       WP_010427416             340 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterobacter mori].
ACCESSION   WP_010427416
VERSION     WP_010427416.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..340
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37806
     Region          1..338
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtilntaiig ggaihrchvn alrqipdval ralvdidsvk glklamgyqc rfyqdyreml
       61 lddsidvvhi ctphfehksm ilaalaagkh vfcekpvgmn gselvdiara veqakgqfgv
      121 cyqnrlnpts lrvrqelahg glgkmlsika vltwsrfgty ytdslwrgrl ateggsllin
      181 qaihtldlmq wfgggvtrlk gvvdsgelad vtegedsama tlhfangarg lfyatnchtt
      241 dspllmeihc ehsslllehn vlwritpger lrlttddspd gsvksywglg hqqairrfyh
      301 alihpenrdy tdiheagksl tlveaiyrss qlrqwieinn
//
LOCUS       WP_010427480             258 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterobacter mori].
ACCESSION   WP_010427480
VERSION     WP_010427480.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..258
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28686
     Region          1..256
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msaitlenvs lsfaakpqpf tvledinlsl nsgefvvllg psgcgkstil nlvagfnkpd
       61 rgrvaaggke igrpgpdrgm ifqqpnlfpw lsvlenvtfg prlgkyrkde tnalaqtwle
      121 rvglkgfehh apwqlsggmk qrvalarawl pgpevlllde pfgaldaqtr lmmqellrea
      181 wlstgttllf vthdveealf ladrilimsa kpgkivdeiv lpfgrerdie tlaehpfyse
      241 ikhhvlhrvr qeakrhlr
//
LOCUS       WP_010427515             287 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterobacter mori].
ACCESSION   WP_010427515
VERSION     WP_010427515.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..287
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31611
     Region          1..262
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mqvisiistk ggvgkttiaa nlggfiadag lrvllldldi qptlsshsql ahrapggiye
       61 llafnerdia qlasrtaver ldiilsndqh hqlntlllha pdgrlrlrnl lpafephydl
      121 vlidtqgsrs vllemavlas rlavspvtpe ilaaremrrg tvqliqdiap yrhlgieppp
      181 lqllinrvpa vssnarlvrq tlrrvfreqt gvqvldtevp aieafpraat qsmpahrveh
      241 rrptgriapa aldivralat elcpqwherf slvtgkigrr hphverp
//
LOCUS       WP_010427633             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Pseudomonas].
ACCESSION   WP_010427633
VERSION     WP_010427633.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..181
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20563
     Region          31..177
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mnamnqsllp tpsgtscfaq ltqqqlqklq nfirkrvihq edaedilqqt fvealhaegk
       61 flqqskpetw lcgialnlir nhfrkvyrrp mhvefeeqla haeptqdifg hiesyrdlqq
      121 tvqaisvlpa vmrhtleitv etegsyqeaa dalgvpigti rsrlsrarsq lrdclpegfr
      181 a
//
LOCUS       WP_010427663            1028 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Enterobacter mori].
ACCESSION   WP_010427663
VERSION     WP_010427663.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..1028
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=110157
     Region          1..1010
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnisswsirn pvpsillfil lmifgligfs klqiqdfpdm dlptvqisat legaapsqle
       61 tevarkiedk ltslvlldhi tttitdgtvs iivtfkidkd sevavnevrn avdsarsdlp
      121 asmneptvsk qtaaassllt yivesnklde qelswlidnq itkrlmsvdg vasvervggv
      181 drevlveldp vlmsgigvtp sdvsnrlkav qkessggqgd iggqrqsart iatvgtvael
      241 sgitvslsdg rwvrldqiar itdghadpis yalhngkpvv gfkvtrsrgf sdvdvaqkvr
      301 asvldlapkn vhikevsnsv npvednysgs mllliegafl avivvwlflr dwratliaav
      361 alplsiiptf aymwlagysl nmvtllslal vvgilvddai veienierhl rmgktpyqaa
      421 meaadeigla viattltlva vflptafmsg iagqffrqfg vtasvavlas llvarlltpm
      481 maaymmkpgh pecdqsdanr plmtkylnla kaalrkrktt vgasmvffal amalipfist
      541 afipaqdksq ssislqlaqg stledtaeaa rqaakmlael pevkgvfasv gtantgggpd
      601 astmadvtsa tltvelvsrg erkskqsave armrevlrsl pgvrvsvggs engnkfeltl
      661 tgdesdllml taakveaqlr tlkgignvts saalqrpevq vrpdyaraam lgvtsealad
      721 avrfatygdy stslpklnlp erqinirvrm dpalrsdlda isqlriqghn gpgtlgsvad
      781 ismgsapsqi dridrsrnvt lrvelngrai gdvqrealsl aamkhlpagv kridqgeaqr
      841 mselfesfgl amvvgifciy avlvvlfhdf mqpatilsal plalagaiva lwmtgqsfsm
      901 svvigvlmlm givtknsill veyaivarrh gmnrlealid acnkrarpvv mttiamgagm
      961 mpnalglgae psfrqpmaiv vigglltsti lslvvvpvvf tyvddflqwi rkstrvvlgf
     1021 dapqkssp
//
LOCUS       WP_010427691             375 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Enterobacteriaceae].
ACCESSION   WP_010427691
VERSION     WP_010427691.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..375
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39373
     Region          4..360
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(14..15,18..19,22,54,104..105,107..109,112,131,
                     134..135,138,203,206..207,210..212,215,243,247,296..297,
                     301,305,321,324..325,328..329,332)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mneristrii ffvagmataa wavivpfakl ntevndgvlg tlllclgfga maampltgal
       61 tsrhgcrrii tvsifimvat lpllavinna illgiflftf gigvgttdca mnvqailveq
      121 kankplmsgf hgmfsvggia gagimtgmls gglsvlqaal iviimivvll flsfrhllpy
      181 anpsegpafa fpkgivltlg licfiifmae gtvldwsavy lidsrdiaes mgglgfvffs
      241 tamtagrltg dyivgrfgal rivltgsvla llgfsaviwg tqlsvillgy lfiglgcsni
      301 vpimfslvgk qdampqmvav pavttlgyig ilagpaiigy ishhsslmng fifvmglvll
      361 sgflsytirg lllqk
//
LOCUS       WP_010427825             234 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudomonas congelans].
ACCESSION   WP_010427825
VERSION     WP_010427825.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..234
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26109
     Region          1..232
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 msrvvikaen ltkqfvlrhn rgglkkkflg lfdaryrera etftavsdvs ftlhkgesla
       61 lvghngsgks tllqlvsril vptsgrltsv grvaplieig vgfhpeltge eniylnaslf
      121 glsnkevrsr fneivdfsgl gnfidtpvkn yssgmymrlg fsvavhvepq tlladevlav
      181 gdeefkrkch erirvmqddg malilvthav eegkefcqry ltlergrmte hgyy
//
LOCUS       WP_010427857             436 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterobacterales].
ACCESSION   WP_010427857
VERSION     WP_010427857.1
KEYWORDS    RefSeq.
SOURCE      Enterobacterales
  ORGANISM  Enterobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Enterobacterales"
                     /db_xref="taxon:91347"
     Protein         1..436
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47840
     Region          44..267
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          175..434
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 msgemvlans vvllillfvl wcvvfrsrdv kfaflnlfrh krrsfstmaa imlggvsifl
       61 yggfidysfw ilkeqtirtn ighvqiynkn yfetsnknks liddypalkk ailndpalae
      121 distlsgqle ftgvisqyes etssyfsalg veplpalklg sfdklitgsd lsrirtdeit
      181 lgsglaktln ahyddwldvl vvntqggqga lsmklrgife sgikdyddva mkiplgtaqr
      241 imgtnsvskv lillkeddta aftaklrgfi aehnlplivk dwkdasifyq qvegllsgiy
      301 ffiklivgli vifmignsmt mniiertrei ttlraiglkp lhvtrlflle gifigiigai
      361 gslaigyaia svinlygiam ppspgqsqgy tafiktdsva lnwitlvlpi ltatgasvlp
      421 alrasrlnis dafkfs
//
LOCUS       WP_010427907             498 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Pseudomonas].
ACCESSION   WP_010427907
VERSION     WP_010427907.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..498
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=53636
     Region          <205..496
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mpvaprfldh yrkadrimlg liwllfvyal glafwfdtft qavvvgggta lvltglyrai
       61 ggtrlmrccf gvglmvmtal hinqthgqve ihfgifvlla vltfyrdwlp ilvaavtial
      121 hhigfhalqh sgfpvyvmhh gfgwsmvlvh avyvvvesai lvylavqnqa eavenqdmld
      181 rmlattnkfs pdsqtsersa krvplaqrfe qflaqitglv dgvvrdtrgl gelghdlaka
      241 sstletgaqh qlseiarmtg amqrmgdamn disshvaqav qragdasdqv ahgrdsvdra
      301 qseitqlaar itttdetvqa lanqseqigk vldvigsiae qtnllalnaa ieaarageqg
      361 rgfavvadev rnlaqrtass tkeiqtiied lqrgsrqaat amndslqgvg rcvedsqras
      421 eslravgegi ghitqlngli attteqqsav sreiadqlrs vqtiaehtaa nigvlatssq
      481 slsplairle algqsfha
//
LOCUS       WP_010427929             127 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Enterobacter mori].
ACCESSION   WP_010427929
VERSION     WP_010427929.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..127
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13673
     Region          3..120
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mekilsggcl cgavrftaan ggnvhtcscd icqkhtgaqt vvwiefpaed vqwtgpggrp
       61 atwrssdyss rafcptcgss igaiddsptv alftgvfddp dqpefapenh sfddmmpaww
      121 rhtmrea
//
LOCUS       WP_010427997             115 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: STAS domain-containing protein [Pseudomonas].
ACCESSION   WP_010427997
VERSION     WP_010427997.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..115
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12657
     Region          10..99
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(21,23..25,31,52,54..56,58..60,63..64,86,90..91,93)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            55
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mtvtsersad gqtltlyieg rfdfnshqaf rtayedypqs lsyvvdlrgt hyldssalgm
       61 llllrdhagg dkalvrlvnc tpdvlkilai snfsklfels ipsaaspekt vhshr
//
LOCUS       WP_010428344             134 aa            linear   BCT 01-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Enterobacter mori].
ACCESSION   WP_010428344
VERSION     WP_010428344.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..134
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=15071
     Region          14..131
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 myltdsenkl tvyeinafnt ifdnqlpasf ldfylknngg hphknkdgnp fmlggfnpvk
       61 ygnlpieqly rdlvesfgel snmvpfaydd ggnsfllslk sddslgkvfv ffmddkeval
      121 vsgtfsefle elfh
//
LOCUS       WP_010428393             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter permease [Enterobacter].
ACCESSION   WP_010428393
VERSION     WP_010428393.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 279)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..279
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29658
     Region          11..269
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mmallldpfq fafmnnalli sllvavpcal lsvflvlkgw almgdamsha vfpgvvlawm
       61 mglplalgaf vaglfcavat gylkdnsrik qdtvmgivfs gmfgaglily iavkpevhld
      121 hilfgdmlgi ngmdilqsgi vaglialvig lkwrdfllfc fdyqqaqvsg lrtrwlhygl
      181 lcmvsltiva tlkavgiils islliapgav avlitrrfhm allvavavsa lvsvsgvyas
      241 fyldsapapt ivvlfamvfi vtfgvtsvka rrqesvtag
//
LOCUS       WP_010428448             200 aa            linear   BCT 01-JAN-2025
DEFINITION  2OG-Fe(II) oxygenase [Vibrio cyclitrophicus].
ACCESSION   WP_010428448
VERSION     WP_010428448.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Chowdhury,R., Leung,I.K., Tian,Y.M., Abboud,M.I., Ge,W., Domene,C.,
            Cantrelle,F.X., Landrieu,I., Hardy,A.P., Pugh,C.W., Ratcliffe,P.J.,
            Claridge,T.D. and Schofield,C.J.
  TITLE     Structural basis for oxygen degradation domain selectivity of the
            HIF prolyl hydroxylases
  JOURNAL   Nat Commun 7, 12673 (2016)
   PUBMED   27561929
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..200
                     /product="2OG-Fe(II) oxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=23326
     Region          3..189
                     /region_name="EGL9"
                     /note="Proline 4-hydroxylase (includes Rps23 Pro-64
                     3,4-dihydroxylase Tpa1), contains SM-20 domain
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG3751"
                     /db_xref="CDD:442965"
ORIGIN      
        1 mnqlidalst qgyfvwddfl theevvalrd cipenwkkar igrnddvare atirsdkiqw
       61 vrrdmgqpas lfldkmeqir laanqafflg lfeyeahfak yekgdfyqkh ldcfkgnenr
      121 rlttvfymnd ewteddagel vvydlkdnhi atippksgrl fvflseqfph evlptnterf
      181 siagwfring vkdnqldiah
//
LOCUS       WP_010428421             326 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Vibrio].
ACCESSION   WP_010428421
VERSION     WP_010428421.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..326
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35755
     Region          1..266
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mikfavigtn witqkfvqaa hetqsmklaa vysrniesas qfaqefnvnt tydsldalas
       61 dstieavyia spnslhctqs ilmmkhgkhv icekpvasni deatqmfeva eqngvvlfea
      121 yksqflpnfk qvqlglekig kvhkahinyc qyssryqkyl ngdnpntfnp afsngslvdi
      181 gfycvaatva lfgkpesaha saklldsgvd ahgcavfqyp efdvtlahsk vsdsyapsei
      241 qgecgaiiid hiaectdvki ryrdgrienl tqtqsensms yeaqafanci ggdkttqaea
      301 ekraltvakl itemrqqvgv vypadk
//
LOCUS       WP_010428506             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Enterobacter].
ACCESSION   WP_010428506
VERSION     WP_010428506.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..205
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22326
     Region          10..189
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 myfyqpsqgh glphdplnai igprpigwis scdtngmlnl apysffncfn yrppiigfss
       61 ngwkdsvrni hetgefvwnl atrdlaaamn ktsamlphde deftfagltp vasqlvkapr
      121 vaespvnfec rlsqciqltg adgtpvdtwl vlgevvgihi adtlleegiy qtakaqpilr
      181 aggptayygi sdehrfdmvr pgagq
//
LOCUS       WP_010428515             284 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Vibrio].
ACCESSION   WP_010428515
VERSION     WP_010428515.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..284
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31754
     Region          5..223
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mstllsvknv tktysnqvgv enisfelkpg qvlgllghng agkstliksl lgghnyqgei
       61 evngyhpihq haalmqhlsy isdvnvlpew mtvkqllryt qgvhpsfnrq kaeqvlsstn
      121 inlsstikql skgmkvqlhl aviiatdtqv lildeptlgl dllyrdtfyr hllewfydge
      181 ramiiashev seiehlltdv lilkqghcvl qksmediend yfiievanny sseiqrfnpl
      241 tsqsglgttk wllegqykaq veslgntynv gladlflatq meka
//
LOCUS       WP_010428533             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Pseudomonas].
ACCESSION   WP_010428533
VERSION     WP_010428533.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..145
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15917
     Region          7..>108
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mdtsdgtlqg tchcgavrfq vrltdgfktv rrcncsycrm rgaiavsaal edieitsgea
       61 mlklyqfntl qakhyfcsqc giythhqrrs dpaqygvnva clegvspfdf eevpvnegrt
      121 hpkdrsagsg sniagylryl pntnp
//
LOCUS       WP_010428549             477 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Vibrio].
ACCESSION   WP_010428549
VERSION     WP_010428549.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..477
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51510
     Region          80..476
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mklnlplkhs lislaligli gctttsqtdy vslaeqstnq tqqsllaeli qlassdqast
       61 qqdldaknlq ltdlvnapel dlyieralkn spslqqnita lkiayaqqgv tsgdrlptvd
      121 asfsgqadeg tngssttety ttdvtvgwel dlwqkladtn naalkdiats qanlqgaqdl
      181 lvasvmrgwl dislkqqlvd ietqrlvile nneelvlery raglgsledl dnaktssast
      241 qatladyqeq laqsrrglvl ltglwsgesd easltdlgsf ptiinpldni ptqdlagrpd
      301 lqaaffniea etlradaayk amlpsislsa sltdmaesps ealltgplws algqvsaplf
      361 qggklkaqae iadlttetsy wayqetllna vnevenamgq essltlqqqh lanalvsaqr
      421 sfasyeekyr qglvdifdll svqqqtydle aqlaqtiynr lvnridlgla lglgvss
//
LOCUS       WP_010428582             392 aa            linear   BCT 01-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Pseudomonas congelans].
ACCESSION   WP_010428582
VERSION     WP_010428582.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 392)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..392
                     /product="acetyl-CoA C-acetyltransferase"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40369
     Region          1..392
                     /region_name="PRK05656"
                     /note="acetyl-CoA C-acetyltransferase"
                     /db_xref="CDD:168156"
ORIGIN      
        1 mhdvvivaat rtavgsfqgs latvsavdlg aavirqllar tgidgaqvde vimgqvltag
       61 agqnparqaa ikaglpfsvp amtlnkvcgs glkalhlatq aircgdaeii iaggqenmsl
      121 snyvlpgart glrmghasmv dtmitdglwd afndyhmgit aenlaqqydi sreaqdqfaa
      181 lsqqkamaai eagrfvdeit pilipqrkgd plsfatdeqp ragttaetla klkpafkkdg
      241 tvtagnassl ndgaaavmlm saakaeqlgl pvlariaaya nagvdpaimg igpvsatrrc
      301 ldkagwslae ldlieaneaf aaqslsvgke lgldpqklnv nggaialghp igasgcrvlv
      361 tllhemirrd vkkglatlci gggqgvalal er
//
LOCUS       WP_010428606             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Vibrio].
ACCESSION   WP_010428606
VERSION     WP_010428606.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21620
     Region          1..203
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtvtiwfsll aicllgamsp gpslamiakh slaggrmngl vaawshaagi giyafativg
       61 lavlleqspm lfkgisiaga ayllylgvna lrskggvaak leageqmsym qsareaflis
      121 ilspkialff ialfsqfval gneltnkvii vstplivdgl wytfitlvls spliverirs
      181 kaqlidrlsg vvlillavrv vwti
//
LOCUS       WP_010428801             492 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptide MFS transporter [Vibrio].
ACCESSION   WP_010428801
VERSION     WP_010428801.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..492
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53249
     Region          9..479
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mwnrlnksmm fcqmmfglsf ygvmviltrf fledlnynea dtmmvvgafs aigplfaiag
       61 gfiadkflga yrsltiaflg fasgyallvl gaaatnvpma lcgialasya rglmspsyps
      121 lykrtfktqe dfencypiny svnnigallg qylfpmlvli vgfnggflls ailagaallm
      181 mifvrkglve asaeidqtpv stknwaaflg lsaamiglvf fmfsnmdigq nivyaiggaa
      241 iiyfvslmik skksdmlkmg tiliitfltt cffvyygqmm tsmtmvaint mrgdlfgfip
      301 vapeasmamn plwcmvagpi itgifsklek knihfstatk vgfsfiltai afgiltmavt
      361 tvgddilirp evflaihffl afgevivgsm vvafilsvap khienfsvsl fsvaialsgi
      421 vgavfstsia lekgqqitqe ivqtvygdyf qmltvlavvm vgiamaasfi irkmleaakt
      481 aeetieleqa ns
//
LOCUS       WP_010428812             172 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Vibrio].
ACCESSION   WP_010428812
VERSION     WP_010428812.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 172)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..172
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19748
     Region          25..114
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cd02883"
                     /db_xref="CDD:467528"
ORIGIN      
        1 mrhlkttihp didhldnktv ykrnaaraiv ldgedilmly teryhdytip gggldegedv
       61 iagmvrelee etgaknihsi kpfgifeefr pwykddadiv hmisycysck idselgetay
      121 edyevkngmk pvwmniheai ahnektmaes pkkgmsiere tfllhliake ml
//
LOCUS       WP_010428961             374 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF917 domain-containing protein [Vibrio cyclitrophicus].
ACCESSION   WP_010428961
VERSION     WP_010428961.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..374
                     /product="DUF917 domain-containing protein"
                     /calculated_mol_wt=40134
     Region          1..368
                     /region_name="COG3535"
                     /note="Uncharacterized conserved protein, DUF917 family
                     [Function unknown]"
                     /db_xref="CDD:442756"
ORIGIN      
        1 miiteqmidd ialgatvlgt ggggdpysga lmakvaiata khpvriisle dvqddwmtvp
       61 ssmigaptva veklnskdqm liafeameka ldtevaatfp ievggfnsli pilvaaqkni
      121 pvidcdamgr afpeaqmvtf fldglpsapn tladergnvv tlypidgiws ekfarpvteq
      181 mggsaamcdy pmngknlkrs alpatltqam kigeairlan dnnqsgtqav lnivgghtii
      241 rgkivdiqre tgggfatggv vieklaqfed tgidnvfvqf qnelllvhkg tsradmnqdn
      301 llastpdlis vldhetgkpi tteqlrygqr idliaypcds kwrtdkgiev agpgyfgytv
      361 eyqtieqlks alkr
//
LOCUS       WP_010428998             206 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Pseudomonas congelans].
ACCESSION   WP_010428998
VERSION     WP_010428998.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..206
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21635
     Region          2..191
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mldltqvlty saalgiaaai pgpgmaalva rsvsggavsg fcllsglilg dltylsfavf
       61 glamiaehfn alfqvvrwga aiylcylawq fwfadhqaid igksarkkel lsaaasglti
      121 tlgnpktiaf ylallplvin letvslqtwg lvlvpltvlv llavgavfif aalrirhlls
      181 sesaqrklfr gaaaimvaaa asmlvr
//
LOCUS       WP_010429013             369 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas congelans].
ACCESSION   WP_010429013
VERSION     WP_010429013.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..369
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37979
     Region          3..343
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 msssislrrl asallpglpt vlavfsscvl fglflavqgk pawqalhlvg egafgswfal
       61 entlqraapl mltalcvalp aragliiigg egalvlggla aavtplwlsh lpaglmlacm
      121 avaamtvgal wiglsgwmrq rrgvnetiss lllsyialal frqlvegplr dpaslnkpst
      181 pplddaymig tisdsfevhw glvagvvacv layvlvrhsv kgfalavvgg nvrtalmigl
      241 pvdrlimlsc llggaaagla gmfevtavqg sanaaliagy gtsgilvafa arhhplaiiv
      301 caillgglea sggllqrrlg lpdattlile gllftnlllw ealggriaaw kirltaspap
      361 ldkgalqhg
//
LOCUS       WP_010429046             314 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RDD family protein [Vibrio].
ACCESSION   WP_010429046
VERSION     WP_010429046.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..314
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=34864
     Region          11..163
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 meevqqkwic gfwtrigalf idtiflgvlg yvvglfledv fvqlgewgrl igfvvsityf
       61 gvmnssllng qtigkkllni rvvdscnsti slpksflrys flavpfslng aqitneavip
      121 ylmyllsfiv fgglcsityl yifnrvtrqs lhdlavgtyv vnaeassekl psvwrphlvv
      181 vtglfvtavl vpvltsdltq sesfkgllvt qkainnnesv kyagvtegat tftssnsgsk
      241 tttyvkaqaf lykdsvrdse iakqlvqtii ytypeslnkn likvtltygy digiaskwns
      301 ynykfnpqel kile
//
LOCUS       WP_010429300             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Pseudomonas].
ACCESSION   WP_010429300
VERSION     WP_010429300.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..397
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42934
     Region          17..390
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtlstlrptp rqlhdapepa edfgkrlael taalaetaeq ydvsaqfpha nfqllhahgl
       61 lgltvptelg gggadlprar qvisavarge pstalilvmq ylqhsrlqen rnwpshlrvq
      121 vaeqavrega linalrvepd lgtpargglp gtiarrtaqg wrisgskiys tgshgltwfa
      181 vwarsddddp lvgswlvhkd tpgitiiedw dhlgmratss hevrfdnvlv pldhavsvsp
      241 wsapqseldg sgllwmsvll ssvydgiaqs ardwlvhwle qrtpsnlgaa lstlprfqet
      301 vgqidtllfa nrsllhsaah ghtpaqhagq ikylvtgnai ravelaieas gnpglsrsnp
      361 lqrhyrnvlc grvhtpqnda vlagvgkaaf aarskdq
//
LOCUS       WP_010429350              95 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas].
ACCESSION   WP_010429350
VERSION     WP_010429350.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..95
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10621
     Region          5..86
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 msealsihhd evghhfeiiv dghrayltym dlgkqtldfy rtfvpdalrg rgiaaaltke
       61 aldyadsmgy svipscsyve rymelhdlqs qaakl
//
LOCUS       WP_010429360             527 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Vibrio cyclitrophicus].
ACCESSION   WP_010429360
VERSION     WP_010429360.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..527
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=59307
     Region          7..129
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mtlspdlrvl ivddsksati likqqlvglg iphrnvfiat nyqqaikave shsfhvllid
       61 yhleqsftgf ellgilyrnr lidhtvaiil lsgdmrqetv ltalsgeahh fiskpintla
      121 lgkkiqtavf eakqisqltn lypinnqval nsalnipgkd tkvqfeatli ehliarkkwe
      181 llsyllnksg tnmhptklva ealildglgk pksaidklhn ylvaqplsln vidclsciye
      241 khqmlipalk lairafeltp sishrairai dlaenvdntq vliklgeiya nsisladldv
      301 ihsistyfna lratyeremh vtnkkllieh agqfttqvnl klpnhsqnqi lsnlaifhch
      361 ilifeknekl ahhklvkatt llshrlydgp tdllnqllpl ldhfgeysmy ravtkcilsr
      421 gdpvlhqiqp vtlspstlin lesvdsvndl knyihnypys vaakldylya vnktqiqeql
      481 sddfvqeitq lelpekwktw vsdlslkgfi tkppcpfpti srresic
//
LOCUS       WP_010429380             177 aa            linear   BCT 01-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Vibrio
            cyclitrophicus].
ACCESSION   WP_010429380
VERSION     WP_010429380.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..177
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=18970
     Region          22..176
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mktliksvla lsiltagsaq afeltsndiq dghpmaktfe ysswgcngdn lspqlmwkda
       61 pagtksfait aydpdaptes gfwhwvafdi patvselprg vdiskmggke gridygtvgf
      121 ggacppekgg mhryqftvwa lptdklnlde ntpsavvgft lnsmaldkak ltatytr
//
LOCUS       WP_010429408             208 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Vibrio].
ACCESSION   WP_010429408
VERSION     WP_010429408.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22241
     Region          1..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslegavtff iamfifgitp gpgvfailar gmvqgwrkci tlslgmicsd liylalacfg
       61 latiaenwsf afeviryvga ayliylgykm fkslpevqgs aelaakqsqk selasfaqgf
      121 lisasnpkvi lfyisflptf vdltvlrsqd ivlvsvlasv almsglmlia mgagrmasll
      181 ktprahkrln qsaggimiaa gsylainr
//
LOCUS       WP_010429436             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Enterobacterales].
ACCESSION   WP_010429436
VERSION     WP_010429436.1
KEYWORDS    RefSeq.
SOURCE      Enterobacterales
  ORGANISM  Enterobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterobacterales"
                     /db_xref="taxon:91347"
     Protein         1..245
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26912
     Region          3..241
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mplitinqvq kyygenhvlk gvdldidmgq visiigrsgs gkstllrcin glegyqdgsi
       61 klggmtitdr dsqareisrs vgmvfqsfnl fphmtalenv mlaprrvlkk saaecrelaq
      121 rmlekvglgd rldyypssls ggqqqrvaia ralamspkvl lcdeitsald pelvgevlkv
      181 leqlaaegmt lilvthemnf arevgdrvvf mhqgkvweqg dsktlfanpq ttelkqfiss
      241 vrgln
//
LOCUS       WP_010429504             423 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Vibrio].
ACCESSION   WP_010429504
VERSION     WP_010429504.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..423
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46700
     Region          5..423
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msestksfnq lglsehllat laelnftapt svqeqaiplv legkdvlaga qtgtgktaaf
       61 glpiiqrlie tkdniipnpk lvralvlvpt relaqqvfdn vteyakgtdi kvvvayggvs
      121 mkvqtdnlrg gadilvatpg rlidhmftkn imlshtevlv ldeadrmldm gfmpdikril
      181 srmnevrqtl ffsatfdnki kaiahrmmqs pseiqvtpkn staetvtqmv ypvdksrkse
      241 llayligskn wqqvlvftkt kqgtdalvke lkldgikaas ingdksqgar qkalddfksg
      301 kvraliatdv aargidiqql eqvvnydlpf kaedyvhrig rtgragnsgl aislmsqdea
      361 yllgdierll dtrlpqewle gfepslekdv aperggrsks rssekrkmka klkihqnrgk
      421 arr
//
LOCUS       WP_010429447             283 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar ABC transporter permease [Enterobacter mori].
ACCESSION   WP_010429447
VERSION     WP_010429447.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..283
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31194
     Region          1..283
                     /region_name="MalG"
                     /note="ABC-type maltose transport system, permease
                     component MalG [Carbohydrate transport and metabolism];
                     COG3833"
                     /db_xref="CDD:443045"
ORIGIN      
        1 maqsqsikre kwvrlslswl vivlvstiii yplvwtvgas fnagnsllss siipenfsvq
       61 hyadlfngqv nymtwywnsm kisfltmvlt lisvsftaya fsrfrfkgrq nglmlflllq
      121 mipqfsalia ifvlsqllgl inshlalvli yvggmipmnt ylmkgyldai pkdldesarm
      181 dgasnfrifi eiimplskpi vaavalfsft gplgdfilss tilrtpdkyt lpiglynlva
      241 qkmgasytty aagavliavp vailylalqk yfvsgltsgs tkg
//
LOCUS       WP_010429613             563 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SgrR family transcriptional regulator [Vibrio].
ACCESSION   WP_010429613
VERSION     WP_010429613.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10579933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..563
                     /product="SgrR family transcriptional regulator"
                     /calculated_mol_wt=64331
     Region          5..119
                     /region_name="SgrR_N"
                     /note="Sugar transport-related sRNA regulator N-term;
                     pfam12793"
                     /db_xref="CDD:432788"
     Region          117..559
                     /region_name="PBP2_SgrR_like"
                     /note="The C-terminal solute-binding domain of DNA-binding
                     transcriptional regulator SgrR is related to the ABC-type
                     oligopeptide-binding proteins and contains the type 2
                     periplasmic-binding fold; cd08507"
                     /db_xref="CDD:173872"
ORIGIN      
        1 mssprlrvqf etlfehfdgk dsdvqlddit dvlcctrrna rmvlnkleee gwvewlpaag
       61 rgklsqlifk qnrcdvsenl atrylqegki gqalsvldhn aakltqviqn ylgvqyqege
      121 qvirlpyyrp lsmlnptksm rrseqhiacq vfsgltrlde ndqlqpdlah swqkindyqw
      181 rfflrpgvrf hngeplltnh vvdtllqlep lnmfshikdv sspancvvdv fltrpdrhfp
      241 laltesvakv tlpmtlrged ydirpigtgp yrvekndekq lvlnafngyf gfrplidrve
      301 vwvvdeayss mvypslskpv madrgdsdev eldpgctyll lnrkkgiakd pawaeflsnt
      361 lnaadlfvhi pketvidlgv lhaygikpgw ydiklktpvc ppanskptir layqcqhpmf
      421 ptlakaivtv lkqynvdvel hgykteppha ddvdiwinpm giannrddal agwlmdysfl
      481 desspaddfd qwchmidrwr sgefeqfpar qlgkqlvqsn qlipmfhcwl gvnkdqcgtl
      541 qnakcnalgw fdfsqvwvkp evd
//
LOCUS       WP_010429732             394 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid aminotransferase [Vibrio].
ACCESSION   WP_010429732
VERSION     WP_010429732.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..394
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43267
     Region          1..392
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(99..101,127,180,211,240,242..243,251)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,137,204,249..251,287,290)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            243
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mfshlpkptl dpilslsvay rgdprtdkvd lgigvykndq getpimkavs maqdivvetq
       61 ktkayvglag ceefnqsmvd lllkgtsamg rvaaiqtpga sgalrmlgdl mkvsqpdttv
      121 wisnpsyvnh kpvmeaaglk vryynyfspq tkqvdtakml edlskagpsd vvllhgcchn
      181 ptgadidfea wqeitklsqk ngflpfvdia yqgfgdglee dakglqhman nveemlitts
      241 csknfglyre rtgaaivigk nsehvgnakg klltlarsty tmppdhgaal vktilqnqel
      301 ttiwkqelse mqqrllnlrq slcdelrnty ntsqfdfies hkgmftvlgf ketqmnqlre
      361 eygiygvgdg riniaglses hipyvakaia nvsk
//
LOCUS       WP_010429543             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Pseudomonas].
ACCESSION   WP_010429543
VERSION     WP_010429543.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..207
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23543
     Region          1..198
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mlrilgktss invrkvlwtc eelkipftqe dwgsgfkpad tdefvalnpn amvpvivddd
       61 fvlwesnsiv rylanryagd svypldprgr aqtdqwidwq gsdlnrswsy afmslvrrst
      121 ehqdpaaiaa scaqwarhmq ildrqlektg ayvcgerftl adipiglsvn rwfetplehp
      181 dlpavnayye rlshrsgyll ygrngtp
//
LOCUS       WP_010429743            1033 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Pseudomonas].
ACCESSION   WP_010429743
VERSION     WP_010429743.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..1033
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113728
     Region          6..990
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mkgnfnlsew aikhqsfvwy lmfvallmgv fsymklgree dpsftiktmi iqtrwpgatv
       61 detleqvtdr iekkleelds ldyvksytrp gestvfvylr dttsakaipe iwyqvrkkvd
      121 dirgqfpqgl qgpsfndefg dvygsiyaft adgfsmrqlr dyvekvradi revpglgkve
      181 migqqdevly lnfstrklaa lgidqsqvvq slqsqnavtp agvieagper isvrtsgqfa
      241 sekdlaavnl rindrfyrls diaditrgyt dppkplfrfd gkpaiglaia mqkggniqsf
      301 gkalhermda ttaelpvgig vhkvsdqaev vnkavggfts alfeaviivl lvsfvslgfr
      361 aglvvacsip lvlamvfvfm eysgitmqri slgaliialg llvddamitv emmvtrlemg
      421 etkeqaatya ytstafpmlt gtlvtvagfv piglnnssag eytftlfavi avamlvswvv
      481 avlfapvigv hilsanikpk seepgrigra fngsmlwamr hrwlaiaitv glfaaslfsm
      541 qfvqnqffps sdrpeilvdl nlpqnasine trkvvdrfea slkddpdier wstyigqgal
      601 rfylpldqql enpfyaqlvi vskgleerga ltarlqkrlr defvgigsyv qalemgppvg
      661 rplqyrvsge nidkvrqhai elatlldhnp hvgeviydwn epgkvlridi nqdkarqlgl
      721 ssedvaklmn svvsgstvtq vrddiylinv igraedaerg tpetlqnlqi vtptgtsipl
      781 lafatvgyel eqplvwrrdr kptitvkgav rdaiqptdlv kqlqpeidkf saglpvgykv
      841 atggtveess kaqgpiasva plmlflmatf lmiqlhsiqk mflvasvapl gligvvlali
      901 ptgtplgfva ilgvlaligi iirnsvilvt qidayeksgy lpwdavveat ehrrrpillt
      961 aaaaslgmip iarevfwgpm ayamiggiii atlltllflp alyvawyrik eptdeqrqea
     1021 edknedenaq pah
//
LOCUS       WP_010429769             383 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Vibrio].
ACCESSION   WP_010429769
VERSION     WP_010429769.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..383
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40672
     Region          13..368
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,137,
                     140..141,144,211,214..215,218..220,223,247,251,300..301,
                     305,309,325,328..329,332..333,336)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mdniqpttri tvpvialsfy aiasgylmss lplmlseygl dsnlsswlas afyagllagt
       61 lliertiarv ghkdafvmal svfiatilvl pllphqavwl larfvagvsv agifvivesw
      121 lmsgdesqra krlgvymcsl yggsavgqlg igylgitggv pfiamftllf gavivlmygq
      181 atppqihdak slslkqiskl shsaligciv sgltlgaiyg lmpvelaqrn iahedigglm
      241 alvimggmav qpmvtwlshh igqvllmalf cllgvasiav ltlnrdfyvl gmslfvlgma
      301 tfalypiain lgcrnldpsy lvsvtqimll cysigsvagp liadtfmssq aglftylfas
      361 llattiymli aslkrsplqi age
//
LOCUS       WP_010429797             291 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter permease [Vibrio].
ACCESSION   WP_010429797
VERSION     WP_010429797.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..291
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30906
     Region          47..289
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mdwlrqlais gveagwlsds fmyafmvnal vaalllgpll gglgtlviak rlaffseavg
       61 haaltgiaig vllgeppenp iiglfsfcmi falllhfvrn rtnvpydtlv gvflalalav
      121 gaallmyvar kinihmlenv lfgsiltvtd qdlvilagsc aliilllipt fnrilltcis
      181 pdiakvrgyn tsfydylfvm mitlvtiaav kivgavlvga lllipgatar lltkrmgsfv
      241 llsallatia clvgtvlpme lklpvpsgas iiivsatffl aatlyrivrk a
//
LOCUS       WP_010429845             458 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Vibrio].
ACCESSION   WP_010429845
VERSION     WP_010429845.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..458
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48701
     Region          <48..>181
                     /region_name="CALCOCO1"
                     /note="Calcium binding and coiled-coil domain (CALCOCO1)
                     like; pfam07888"
                     /db_xref="CDD:462303"
     Region          258..438
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mnlkplaall citslsfsaf sasdstaqlv nkaksenrtq ashnvvread fkkteqelka
       61 ikaeleakrt svqnatdvlt qtfsdnenkl arleeklrle tgslgelfgv vrqnakelga
      121 elsstvnsvd raehtatvdq iidakslpsm pqlsglwmsm veqiqassel sksqiafing
      181 egntqsvday rlgsiglvtd qgyvswntqr edaiaylkqp sngptlasls slangdisnv
      241 vvdpsrgfml eqlaltpslt drlqaggvvg kvilgllaig liialvrgis lviarqkira
      301 qlknpeqagd nplgrvlavy nkeqnqtvea lelrlleavv deqthlekgl smlkllaala
      361 pmlgllgtvt gmietfqvit qfgngdpkvm aggismalvt tvlglvaamp lllahnilss
      421 qaenirnile kqgiglvaeq aektvesnav vspvgtaa
//
LOCUS       WP_010430012             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Vibrio].
ACCESSION   WP_010430012
VERSION     WP_010430012.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20260227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..181
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20652
     Region          1..111
                     /region_name="Spm_actase_Thplmales"
                     /note="spermidine N(1)-acetyltransferase; NF041158"
                     /db_xref="CDD:469070"
     Region          74..>145
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 meikvaeykd yeriaqlhad swklyyrgil addylendvl edrsviwqtr linppfnqhv
       61 llleeggllv gfvcafgnhn fergtfidal hvdnayrgrg vgkrllsels kwlqqyysds
      121 glylevmsen hqaiafyqai ggkeeleqvw napcgsqvte kviswespve leqktasavy
      181 s
//
LOCUS       WP_010430179             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Vibrio].
ACCESSION   WP_010430179
VERSION     WP_010430179.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..262
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29009
     Region          2..257
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mkkdkyfymq lfftltvcaf livpvfmsvv agltnnyfvg vksgftfrwv eqvwalysdt
       61 iwltlqiaia ttlinvvigv pcayvlaksk srwasifdel ltlpiaipgm aislglilay
      121 ggftdfrssw mfilvghvif tlpfmvksvl silqsinfrv leegaaslga tfwqrffdvi
      181 vpnckagiva gmlmtltlsi gefnltwmlh tpltktlpvg ladsyasmrl eissaytlif
      241 lclilpllvl aqalnkkpvv nn
//
LOCUS       WP_010430310             257 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Enterobacter mori].
ACCESSION   WP_010430310
VERSION     WP_010430310.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..257
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28566
     Region          <124..250
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 marinkisit lcallftslt ftpaanaseq arhsavqksh lvksterkkk ttsktvkkkt
       61 ptqtkktass ktktspihta hssrrkasqt aanlvtekct trkghkakct kvtklaevhk
      121 vrmqkaqkta mnklmgqigk pyhwggtspr tgfdcsglvy yaykdlvkfr iprtanemyh
      181 lrdaapvnrg dlengdlvff rtqgrgtadh vgvyvgngkf iqsprsgqdi qitslsedyw
      241 vrhyvgarrv mtpetir
//
LOCUS       WP_010430334             677 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Enterobacter mori].
ACCESSION   WP_010430334
VERSION     WP_010430334.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..677
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76231
     Region          21..664
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mnlrvlswqn lpwvkasrpq wryalrngia mclaltvayy lnldepywam tsaavvsfpt
       61 vggviskslg rvagsllgat aaliiaghtl ndpwlfllsm aawlgfctwa cahftnnvay
      121 afqragytaa iiafpvvnvl dttelwdiaq arvcevivgi lsggfmmmil pstsdgtali
      181 talktmharl lehasllwqp dtndesrlah ekvigqiltm nllriqafws hyrfrrqnkl
      241 lnyllhqqlr mtsaisslrr mllnwpappa ntravidtll aalarpdtdi ytvariiapl
      301 apvdeydyrh rafwqrlnyf crlylrssrw inavenatpi teftvpsspa larhtgymea
      361 lwsgfrtfca ltlvgawsit tqwesgsaal tlaaiscvly svaaspfnsl tlllrtllll
      421 slfsfvvkfg lmvqisdlwq fllflfpllt tmqllklqmp rlaglwgqli vfmgsfisvt
      481 nppvydyadf lndnlakilg vglawlafav lrpgsdarks rrhirelrrg fvdqlsrkph
      541 lresgyeslv yhhvsqlnns qdslsrrwll rwgvvllncs hvvwqlrawe trsdplsqvr
      601 dvclsllrdv msergvqqrp lettlaelqr icdtlarhhl paardlasii wrlhcslsql
      661 eqapppgtig dqitpqa
//
LOCUS       WP_010430400             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Enterobacter mori].
ACCESSION   WP_010430400
VERSION     WP_010430400.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32549
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..285
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,219,236,264)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     213..217,224..225,228)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mrledievfv eavragslag aarrlsmsam aasralthle aelgvrlvhr ttrslsptsd
       61 gdiflphala lledksnala dlfpdgthls grlritasag fgrkivapml trfmqqhpal
      121 qvdllgadeq vdivgkgidv alriaplrdn rlvahrlchn prdlcasaey latngypksf
      181 ndlaahsclt tsdtvhwsfe qgelrykqkv sgrfsansve aifeaclggm gianlsrwyv
      241 epafregklv rivledaqpe slavwavypt srlipakvrk fvealeaell lnpltqqt
//
LOCUS       WP_010430447             154 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator [Vibrio].
ACCESSION   WP_010430447
VERSION     WP_010430447.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..154
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17525
     Region          1..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mvidridrni lvelqknnri pnltlaelvg lsppaclkrv krlreegviv gdvsiinpel
       61 tgskmtlvvs vemerdrgdi yqifrhsisk aeevtqcyqi sgsfdfmliv tvkdiqayed
      121 fvervlrkdl nirkfhtsvs mrtvkfstav nlde
//
LOCUS       WP_010430582             294 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Enterobacter mori].
ACCESSION   WP_010430582
VERSION     WP_010430582.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33043
     Region          8..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..292
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(105,109,148,162,165,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(106..107,111..112,114..115,118,122,124..130,192,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 makrenynel ylfmqvvreg sftaaalrlg laqsgisrsi releerlgvq llvrttrkls
       61 lthageqlyq taesafdtld tglatlahyr qtpsgtvrin asqhaidkcl lpklaifkqr
      121 ypdirlelmn esrfvdiiae rfdagvrlgp evgqgmiavr itpdmemaav aapehfrryg
      181 fpqtpadlvd hpciayqfad gsdyqwelvq dgkkithrpe gqwalsdsym eaeaarlglg
      241 layvpvelva ddlergtlir vlqryslrmd glylyyphrn vspalravid tlki
//
LOCUS       WP_010430636             194 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterobacter mori].
ACCESSION   WP_010430636
VERSION     WP_010430636.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21026
     Region          3..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mierspkare imantrqllt tggyksfsya dlaervgirk asihhhfpgk edlvkavvqe
       61 yraearsgme amdrqtndpl ikvkgyadfw sacikegasp fcicvmlave lptlpadiaa
      121 evtghfndls dwltavlsag eaqgvftlse saevearalm agmhgamlaa rafnnphvfe
      181 qiayplidkv ltaa
//
LOCUS       WP_010430660             310 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Vibrio].
ACCESSION   WP_010430660
VERSION     WP_010430660.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34656
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mlledlqvil kvaefrsita aatnldmrta tasaavkrve valgaelfvr ttrhlrlssa
       61 gerylpeceq alkileqakl nmreelgild geirialssd lgrnlitpwl deflleypka
      121 tlrtsisdsn idfyrdsvdm alrygsptda smygfkicdv prilcaapey laemgtpsqp
      181 snlaehngll yqlhdmlqde wvfndgkqdh kvklkgnrts ndadlvrrwc vagkgvaiks
      241 cldmsshlls gevvkimpef kptptelwlv cpsrqsitpt vrllrdlfre ktaeilsqls
      301 eqdiiatqks
//
LOCUS       WP_010430815             192 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterobacter mori].
ACCESSION   WP_010430815
VERSION     WP_010430815.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21627
     Region          15..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mktepagndt kisvrdkill tahdlfystg fratgvdtli kaskvtkvtf yrhfpsksll
       61 ilaylhyrhe iwiswfettl rrhfdegeip sdavsatlye wfispefhgc afinasaeak
      121 sedieseike icrdhksetk ktivtltgin deetvndmmm lidgaiihaq mgmdpervvk
      181 alttgleklt gq
//
LOCUS       WP_010430888             273 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase [Pseudomonas].
ACCESSION   WP_010430888
VERSION     WP_010430888.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..273
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=30306
     Region          124..255
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mkhrmmhshn lrealpdyar kmavpleele aayqwmldne vcfetriker tlsficylni
       61 epriehplar rfykllaset qgaliplygi nwptlrdrml rtweqaynil ickipshtlr
      121 llwlriggak igkgstvwrn tevlgvdslr igndstvgwh cqldargglv igdhvtiash
      181 vliiagghdl nepefwavgg pvligdyawi csrallsfga digegavvgg nsvvskpvpp
      241 yaivsgpnae ikgerargln ykvggkglft lfh
//
LOCUS       WP_010430961             268 aa            linear   BCT 01-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Vibrio cyclitrophicus].
ACCESSION   WP_010430961
VERSION     WP_010430961.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..268
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29941
     Region          <13..187
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mnnsairqsl remmllawev eardpytsgh lwrvskfahl tatalnwstl eiakatlgaf
       61 lhdvgklhtp leilnkpgpl tdseyqviqh hpvqgyelik enpfshfvad ailyhherad
      121 gqgypkglds navskhvklv slcdafdamt sqrpyrapms keraldilqa hlgtqfdiev
      181 gsafihlgrd gkfdhiilhs degiplqhcp mcgptievtr hqnkgdltrc rvcgtqytvs
      241 daavsldske knkhmvdhfi dvtidhlp
//
LOCUS       WP_010431200             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YoaK family protein [Vibrio].
ACCESSION   WP_010431200
VERSION     WP_010431200.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..224
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23968
     Region          23..213
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 misklprwve ygalllagla gsvnaigllg fqhqaishis gtmsllgssl ltptsasihl
       61 llvvmsfmlg aafsgffien qalklgrryg valcieggll flslwallqg ytsgqyfasa
      121 acglqnamit tysgaiirtt hmsgiitdlg imigaglkgv pfdrrkgkll mfivvgflfg
      181 gltgaclfqr feilalafpa sfafiiafiy wlyltyrtet qanl
//
LOCUS       WP_010431210             304 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterobacter mori].
ACCESSION   WP_010431210
VERSION     WP_010431210.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..304
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33930
     Region          31..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <180..290
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 misnksvekr ldelsrniaq rtpdtgdfpt aveglelfrr nepappvscm vppsivlvad
       61 gekimwvgge pytynakkfl itsldlpass evlsasatrp cvgiaykldq rvlmelitqg
      121 glppvkkrda gtgvgigtmt dvllepfcrl lslldepeai pvlspliqre ihyrllmsdr
      181 sdhlrqiaav dghgyrigka idwlkthias plrieelasr vqmstpsfhr hfrqlagmsp
      241 lqyqkwlrln easrlmlneh ydvttaayav gyeslshfsr eytrmfgesp krditglrks
      301 adnl
//
LOCUS       WP_010431226             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Vibrio
            cyclitrophicus].
ACCESSION   WP_010431226
VERSION     WP_010431226.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..231
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=24725
     Region          10..194
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mqqisylqdq lglmtwplli csaltamiia ervfqvmlsi gvgkrairre lnqisptnnk
       61 eiealaqsis gkrpllykgv smllahhsfs kglredaagi wlqekrhqlh aglrllglig
      121 vispligllg tvlgliemfk gvaattgsit pndladglgl amrttaaglm ialpaisgaq
      181 llglwadrvl aqlehtlnyv nvwlegmsiq tnhsdetkgs svnkvgdvsq a
//
LOCUS       WP_010431230             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Enterobacter].
ACCESSION   WP_010431230
VERSION     WP_010431230.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32968
     Region          <26..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..297
                     /region_name="PBP2_DntR_like_1"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     similar to DntR, which is involved in the catabolism of
                     dinitrotoluene; contains the type 2 periplasmic binding
                     fold; cd08460"
                     /db_xref="CDD:176149"
     Site            order(103,105..106,110,167,205,272)
                     /site_type="other"
                     /note="putative substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:176149"
     Site            order(104,107..108,111..112,115..116,118..119,122..123,
                     125..129,131,194,222..226,229..230,233..234,237,251)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176149"
ORIGIN      
        1 mtdpdfnllv aldvllaeas vaaaarrlnl stsamsrtls rlrevtgdpi lvragrhmvl
       61 tpwaeatrdr arnavheara vlqpstetln vqtlarlfti randgfvvaf gpaliaavaa
      121 aapevcirfa pkpektsryl reglvdleig vqsnmgpeir lqrlfqdrfv gavrkghpla
      181 alsaisindy vswghvvasp dgslhgfvdd vlaeqsmkrk vasvvpgfpt alsvalasdl
      241 iamvpalylr nqtmtenlhv felpfkarti tvsqmwhprm eqdpghrwlr ekvrevcqva
      301 q
//
LOCUS       WP_010431233             461 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterobacter mori].
ACCESSION   WP_010431233
VERSION     WP_010431233.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..461
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48202
     Region          25..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,278,281..282,285..287,290,318,322,374..375,
                     379,383,399,402..403,406..407,410)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlfsnqpgd eglpgherar vmvalmtptl mgvfdgtmin valppmasam qvsanvavwf
       61 angyllsaam tlaifaalaa rmgyrpvfla glatftltsl gcalattpdm ligmrvlqgi
      121 ggaatlsiap ailrsvfpgr llgrvlglha lliaastala pvlggtilea lrwewlfain
      181 mvpgsvalll awkalprgsa ssktpfdtag avlsamllgs mimtansfqh vsheaafwag
      241 iallsatafi whirrvhspl lppvifrngr ftlaalisla sfvsqgitfi alpflfqsvy
      301 gysplesall ftpwpigivl iaphagrwad tisaplisti glmifavgli llatlpaspp
      361 twdiclrslv cgigfgcfqs pnnremlanv arenasyasg vlsivrtfgq clgaavvgvw
      421 laattgsdqa vhyalwtavv asagsvlfsl srlraavras a
//
LOCUS       WP_010431285             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Pseudomonas].
ACCESSION   WP_010431285
VERSION     WP_010431285.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..220
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24563
     Region          2..161
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mlqnflnefg yfalflgtff egetilvlag flafrgymdl nivilvafcg syagdqlwyf
       61 mgrkhgrkll arkprwqlmg dkalrlvrkh pdiwvlsfrf vyglrtvmpv aiglsgyppg
      121 rylllngiga avwaaalgsa ayhfgavleg llgnvkkyel wvlgalvllg lalwirrrik
      181 nariareere eksrfcasaa asdletpvtv pvdltkksde
//
LOCUS       WP_010431324             328 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterobacter mori].
ACCESSION   WP_010431324
VERSION     WP_010431324.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35924
     Region          5..326
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msdavlaied vhlsfpifrg dvhalnhvsl eikrgeivgv vgesgsgksv tamlamrllp
       61 egsyrvhhgk vtllgedvln atekqlrqwr gakvamifqe pmtalnptrr igkqmvevir
      121 qhqplsrrea qqkaisllee mqipdaarvm erypfelsgg mrqrvmiala fscepeliva
      181 depttaldvt vqlqvlrllk hkarasgtsv lfishdmavv sqlsdrmyvm yagsviesga
      241 tqtlihhpvh pysigllqca pengqprdvl paipgtvpnl sqlprgcafr ercfaagakc
      301 getprlmphg aegqqaacwy pqqgahhv
//
LOCUS       WP_010431348             570 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterobacter mori].
ACCESSION   WP_010431348
VERSION     WP_010431348.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..570
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63038
     Region          15..492
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mstlltaqsl rvdtafgtlf dslsftlkkg drigllgdng cgkstllkvl dgtdspaagt
       61 valaghclma rveqplpdai fpltmldavl aqlafaerds lrwkaetlla smgftpqdmm
      121 lqsatlsggq htrlllaral ihdpdlllld epsnhldlpt llwleqflqn wpgsfvlvsh
      181 drqlldavtn gswilrdkml hyfalpctaa rkaleakdes daqrhkaeqk eidrvtasar
      241 rlatwgkvyd nedlarkakq mekqverlre sqtaltagsq wtltlrgdal radrllelen
      301 ldvppapglp alfniemarl ksgdrvaivg rngcgksslm rliwqqfade pagsglkihp
      361 rvspgyydqt lnqlsdsatl ldalepfapd pqnrkmalis agfpwarhgq tvstlsgger
      421 srllfvgltl arysllmlde ptnhldmegk aalaqtlqqf eggvllvshd rqlisqscnr
      481 fwlieegtls ewhdaeavfe rmresaglvt ptapviaaet vqpspyddll erlvaletll
      541 eddlarkpkh qkpqlqaqwr keieeieaql
//
LOCUS       WP_010431333             142 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Enterobacter].
ACCESSION   WP_010431333
VERSION     WP_010431333.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..142
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14697
     Region          5..138
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mtihkhgsah wsgdiksgkg tvstesgvln qqpygfntrf egakgtnpee ligaahaacf
       61 smalslmige agftadsidt tadvsldkad ggfaitkial tskvtvpgid pqkfdgiiqk
      121 akagcpvsqv lkaeitldyk ln
//
LOCUS       WP_010431388             261 aa            linear   BCT 01-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Vibrio cyclitrophicus].
ACCESSION   WP_010431388
VERSION     WP_010431388.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..261
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30240
     Region          11..207
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mlennqqlsn qydeqgyfvl rnyfdeaqia slrkvvlkfh eswkadneef yqeeafnssl
       61 itgsqylptd drtalfdfis skkvmdvvda vipnnpafmn tqlffnpvnp eqkdfwhrdc
      121 qydydiddqm rviletqvlh lrvplfdelg melipgthkr wdneeeynvr qevngkessd
      181 disggkqipl aagdllvfsa dmihrgrygl drlaldilif dsaadyvdyv dddclptpsm
      241 lnkfndprlf mntlqlksml c
//
LOCUS       WP_010431407             368 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Enterobacter
            mori].
ACCESSION   WP_010431407
VERSION     WP_010431407.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..368
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39917
     Region          38..364
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mttvqlqtpt atrkfwsgmt lfrlalliap vvasqiggny wvrvidfall yimlalglni
       61 vvgytglldm gfiafyavga ylaallasph lsevfpiltv wfpeglhtsw lliipiaalv
      121 aavcgillga ptlklrgdyl aivtlgfgei irilmrnldr pvnitngakg itgvdtlnlf
      181 glkfsgvyhw fgfkvpalwl wyyllmlviv aivfaclrlq hsrigrawha irededvara
      241 mginvrnykl lafamgasfg gvagalfgaf qgfvspesft lqesiavlam vvlggmghip
      301 gvilgavllt alpellrsqa apvqqalfgt vlvdpeilrq lfyglalvlv mlvrpsgiwp
      361 vrhkevka
//
LOCUS       WP_010431178             430 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 28 protein [Enterobacter mori].
ACCESSION   WP_010431178
VERSION     WP_010431178.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Abbott,D.W. and Boraston,A.B.
  TITLE     The structural basis for exopolygalacturonase activity in a family
            28 glycoside hydrolase
  JOURNAL   J Mol Biol 368 (5), 1215-1222 (2007)
   PUBMED   17397864
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..430
                     /product="glycoside hydrolase family 28 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47134
     Region          2..402
                     /region_name="Pgu1"
                     /note="Polygalacturonase [Carbohydrate transport and
                     metabolism]; COG5434"
                     /db_xref="CDD:444185"
ORIGIN      
        1 madisiltfg adpsaerist taiqqaiaka kpgdsvvipa gryltgaifl ksditlhlvq
       61 gsvllgsqhl edyplidtrv agidmrwpag iinvinaqnv sltgtgtldg qgriwwqrfw
      121 gddehggmvg dysanglrwv vdydcqrprn vlvyesknil lkdftscesg fwnvhlcysr
      181 dvavenlsii nsagpstdgi didsceqvri erctvscndd nicikagrgr eaapkartar
      241 aivirecvln kgsgitlgse tsggiehvli ennrfngtgv gfriksarnr ggfirhitvr
      301 nlllqnvrfp vliqlnwfpq ysygdsgnlq dkpehwrkla dgvegeaglt evshptlsni
      361 tarrsdsnlf sraffiegyp drpvcgltld nisvdatefg kisgveglrf nnvlvtanel
      421 tqdindsyer
//
LOCUS       WP_010431531             268 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterobacter mori].
ACCESSION   WP_010431531
VERSION     WP_010431531.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..268
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28766
     Region          3..261
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mhsdraplfl kvaawggvif lhfplliiai yafntedaaf sfppqgltlk wfsvaagrgd
       61 ilesvtlslk iaslstgisl vlgtlaaaal wrseffgkna islllllpia lpgiitglal
      121 ltafktinle pgfftivvgh atfcvvvvfn nviarfrrts wslveasmdl gadgwqtfry
      181 vvlpnlgsal laggmlafal sfdeiivttf taghertlpl wllnqlgrpr dvpvtnvval
      241 lvmlvttipi lgawwltrdg engaesgk
//
LOCUS       WP_010431576             526 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Vibrio].
ACCESSION   WP_010431576
VERSION     WP_010431576.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..526
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60074
     Region          370..524
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(403,447)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(408,411..412,416,420,443,445..448)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(439,467)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 metllskitd agldpssvsg eeaiifwnhi rqhvsttkte qahcyiisse yraelqqnqt
       61 sieelrhaln llhlpvdied iltvktslsd rlveigdyts alnefvssss iavehgyide
      121 yvmailgmgn lcdaygdhsr alryyqkins idhaissrsl rlkfklhmva sllllnrita
      181 asdllnecde lsilvsdkql taqillyqak vlrakkkhhd alrcltkiqy pvnntqanwl
      241 atmtrletay clsaigkqey asmilsstdk rvneysspvl akrfydslsd vcmnqgrfqe
      301 alnyekkgyr ietdlmkqip iselgssqlr rlsrfelqlk lilseqenre lketteqhkn
      361 avaqlqqdvf tdpltglhnr rwldvklkdl llhetpfalm vvdidhfksi ndelshlvgd
      421 kaivsvsqel rsyfkfrgas cvrfggeefl vilentnldk aemhsenyre rifqfgwhei
      481 lgergltvsi gitihregen tqrtfyradk alyrakangr nqtcte
//
LOCUS       WP_010431598             564 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Vibrio].
ACCESSION   WP_010431598
VERSION     WP_010431598.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 564)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..564
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62749
     Region          1..532
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mtiafsnfsf ryesldkptl kninlriekg ekiviigpsg sgkstlgqcl ngliphaikg
       61 evtgsleing knisefsmhd yteqvgtvlq dtdsqfvgls igediafale nqlmsnidmy
      121 plvkstakmv dladmlersp hdlsggqkqr vslagilvdd vdillfdepl asldpktgka
      181 tieiidqlhk etnktiviie hrledvlhrd idrvilmerg eivadttpde ilaselldth
      241 gireplylsa lkaakapltc edklsnlkal dykrfrpavq awfaerpapv adkqypplle
      301 vhgltysydg eknaledvsf kigkgefvsi lgkngsgkst itklimgvid adsgssylng
      361 edlselsife rsqkvgvvmq npnhmishhm ifdeiafglr nrniaeelit ekvehvlelc
      421 glskfrhwpi ealsygqkkr vtiasilvle pellildept agqdyrnyts mlafiqklnr
      481 dlgitvviis hdmhlvleyt trsiviadsr lianaamtev fsqpsllera nlcttsiyel
      541 atmmkiddtn afmqyfidye rsaq
//
LOCUS       WP_010431658             540 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [Pseudomonas].
ACCESSION   WP_010431658
VERSION     WP_010431658.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..540
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=60547
     Region          19..>535
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mrkdlqvpim laitdcqpdl hvisfaghea lnetyrfdiw migsnphldv gsllhreafl
       61 sfgkpgsgrh griehavrlh ngarlslyhl tlvpdlqrla qhqqhrtyqd laipqlivql
      121 leahgigana yrfehvngly parplhiqyg esdlhllqrl ceeegmhfrf ehrqsghrlv
      181 fsddpasfpa qplpvrfkrp easgasretl lhlaerlafp yvsrlpvehp qpahaasslh
      241 dehpltiaan hafqppgfrg aishqealsr qrgsrrlerl rcerrdvrgq gtdtalqcge
      301 viqvldhpep llndqwllte vmhagrqlqv lrgaaahdal ailrilveaq rsspeseqlq
      361 gngycnsfrv ipwatpfrps inhprppvtg ehfatlqrnd irpdppgyrs irfdwhvqgl
      421 eddpaqrwpv aevacpeihr lppgtrvlvr fldnhperpv icavlspshg ldgmtahpan
      481 girlasgqhl hisahdgllv rgqaaalhvd aqrilivghg dqqslksgwr lsinarmpsf
//
LOCUS       WP_010431659             309 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Vibrio cyclitrophicus].
ACCESSION   WP_010431659
VERSION     WP_010431659.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##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="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34460
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..282
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,227,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mpntnqlllf ldvvqqgsft kaatlhdmdn sslskqikkl eqdlgvqlln rstrsfslts
       61 agedilaqty vlkdtinqvq giadsyqsep kgvlritspi yfgqqylqpi itqfmrkypd
      121 vqivlslddk ianiiagqfd iafrfsklve snliakkiad snfmlvasnd fvkeygepkt
      181 pqdllalpav iytngdmtvd hlriseepgg ntfqsltirg nykvsdvrtm vscvkdglgy
      241 gfldqsnlya smkelglvtl lpdypistid taiyavyphr kqtklvkefi ttvqdyigsp
      301 tiwekmqqg
//
LOCUS       WP_010431692             172 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Pseudomonas congelans].
ACCESSION   WP_010431692
VERSION     WP_010431692.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..172
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19143
     Region          6..155
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mshsdfnkvf laqrpvllrt lqrmvgnqsa aedllqetwl rvsraltehp vdhlepfvfq
       61 tarnlaldhl rarrihgrtm ledvsparle svvaqlgspe daahakrlle slsaslstls
      121 prqqkiftls rldgrsylei aeqlqvsast vqkelklima vcvgvlsrld ps
//
LOCUS       WP_010431754             324 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Vibrio cyclitrophicus].
ACCESSION   WP_010431754
VERSION     WP_010431754.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..324
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35591
     Region          1..248
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkwgilgtsf isgvmadaik gdaqselyav agrtektlne faaqyqptrt fnsyealied
       61 esvdiiyial pnhvhheyvi kaaqkgkail cekslsvdme kteqalqavk eagvffaegl
      121 mylnhpliak lhqelatgei gevrsiqgsy vaaidqfvnp askgalynlg cypmslihsv
      181 aqqqfgesvf ddvqisaigr rgqdgnices sammhfndrf taqihtaedh glkhgftilg
      241 skgcitldtn pwlpteensf tveiyetstr evkvaaqgdg fhyqvrnirq avergdtqla
      301 apmathqdsr vimklltdwd laas
//
LOCUS       WP_010431777             190 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Vibrio cyclitrophicus].
ACCESSION   WP_010431777
VERSION     WP_010431777.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21622
     Region          3..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mskkelildv aeslfnqfgy tavgvdrird eaevsktsmy rhfgsktkli eavlerrhqr
       61 fesslevala sasgsqsqln tlldwhfawf eqpdfkgcmf mhafaefkes eddiamlsrq
      121 hkvwlknsir dvlrgneevd tailelrses vmtfiegliv rgefgqldsk sdsnrqayrk
      181 alhslailai
//
LOCUS       WP_010431784             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MIP/aquaporin family protein [Vibrio].
ACCESSION   WP_010431784
VERSION     WP_010431784.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..283
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29695
     Region          8..257
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mttnkhpslf gqclaefigt glliffgvgc vaalvltgat fgqwevsiiw gfgvaiaiyc
       61 tagvsgahin pavtialamf hgfdkakvvp yiisqllgaf csaalvysly snlftdyeia
      121 hnfvrssqda lstagifsty phaslsffga favefvitav lmfailalgd enngasrgam
      181 nplligvlia viggslgplt gfamnpardf gpklfayfag wdfaltgard ipyfivpila
      241 piagacfggw lyprvigayl piegqgctip nqcdteeaeq aqa
//
LOCUS       WP_010431830             252 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator [Vibrio].
ACCESSION   WP_010431830
VERSION     WP_010431830.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..252
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28461
     Region          <119..242
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mqiselkipl englnkspse feeairnglt tlgiehvtlv isskpdfpaf kyidglsdgv
       61 sltevitdnl ddylmlisks rkgkihhkld dimdnrilgh dklpvaqdyl nfysisenll
      121 yehgisimfh svdelridel rqlksicdia iawanswvah rtmvshwrky sepktantsp
      181 sltkseldvl dlltkglngt eiaqtrdvsk etvrsqiksi lhktqcknqn qlisrfgqgq
      241 wlisppirsa yt
//
LOCUS       WP_010431832             844 aa            linear   BCT 01-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Enterobacter mori].
ACCESSION   WP_010431832
VERSION     WP_010431832.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 844)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 844)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 844)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 844)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..844
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..844
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=91679
     Region          10..843
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mrknkqerlf kparlaflia falgatteva hardyfnpel ieldnpgmkg adlsafesgs
       61 qlpgtyrvdi vlgdqvvdtr evkfdavkda ngeeslqpcl svaqlkswgv ktelfpelas
      121 ggecakldai pqasaeflfs aqrlvisipq aalspqargy vppemwdegi taamlnysls
      181 gsnnrarngn dsdtnsqyan lrpginigpw rlrnyttwtr dsngkdkwdt vytygqraii
      241 plkaqltagd ssspadvfds ipfrgaqlas dddmmpdslk gyapvvrgia rtnaqviirq
      301 ngyqiyqsyv apgafeitdm yptggagdld vtvkesdgse qhftvafasl pvlqregrfk
      361 yavtggqyrs ynsdvdktpf sqltgiyglp ygltmyggfq esskyqslaa gigknmgdlg
      421 afstdvtqsw gtpkdmpksq gqswrirysk nfvetgtnfa iagyrystsg yygmqevlds
      481 ygdssalqdr rrnraeltms qnigqnfgsl mlsavredyw nsgktmesys tgynnswnsv
      541 sygitytysk ngstdsyght tsydkdqqia ltvsvplekf lprtwanysm nhsknngtth
      601 svglngtale nnalswnvqq gygtdnvgyt gnanadykgt ygevtagygy dkdsdrlnyg
      661 lqggiiahad gvtfsqplge tnvlvkapga kgvsiqnqsg aktdwrgyta vsnltpyrkn
      721 dvalmtdtlp ddveleltnk tviptrgavv radyvanvgi rvlmtlnhss gqpvpfgaia
      781 tvkgqgansf ivgdkgqvyl tglnpsgtll vkwgndtseq cnanyslsek nltsgvlvis
      841 arcn
//
LOCUS       WP_010431932             351 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Vibrio].
ACCESSION   WP_010431932
VERSION     WP_010431932.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..351
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39215
     Region          15..345
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mtskkysilr qrsvlqtsfm llavlmmsif tlhiakpfll piifgafisl lcsplvnylt
       61 rfgiprvinv mavligfigf vvislnmlse paqqwwsklp mlvenvsnev sevtqnsrlt
      121 datgfsmsst vtndgltnnt afsiiesvlt ttptivtqll vaflmayfmm nygrkiysqs
      181 lslfecfsdk rravelvkvv qkdlsryiga itiinvclgl tvgfafymmg lqdpflwgaf
      241 aglmnfipyl gpmvsvtcfa lvsfiqfesf syaltvaaif lainliesql vtptllgkrf
      301 slnplilfvw lvfwgwlwgs mgmlvgvpll vcvnvffeql rhprlnahkg q
//
LOCUS       WP_010432054             382 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Pseudomonas].
ACCESSION   WP_010432054
VERSION     WP_010432054.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..382
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40026
     Region          2..366
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 msapvviigt glagynlare frkldadtpl llitaddgrs yskpmlstgf gknkeadgls
       61 maeagamadq lkaeirthtr isgidaghkr lwigeeavyy rdlvlawgae tirvpvegda
      121 gdaifpindl qdyarfraaa agkrrvlilg agligcefan dlilggyevd lvapceqvmp
      181 tllppeaaaa vksgleslga rfhlgpvltr lnrngeglqa hlsdgqvmdc dlvvsaiglr
      241 prtelaaaag lqtgrgilvd rllqtshani halgdcaevd glnllyvmpl mscaralaqt
      301 lagnptsvky gpmpitvktp acplvvsppp rgsdghwsve gqgadikalc hdadgnllgy
      361 altgaavmek lalnkvlpal la
//
LOCUS       WP_010432065             446 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [Pseudomonas].
ACCESSION   WP_010432065
VERSION     WP_010432065.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..446
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49897
     Region          18..446
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mdpspsfnls slfadfgmil falflvllng ffvaaefamv klrstkveai adkngwrghi
       61 lrkvhgqlda ylsacqlgit laslglgwvg epafahllep llaamgvdtp elikgvsfft
      121 affiisylhi vigelapksw airkpellsl wtaaplyffy wlmypaiyll nasanailri
      181 agqgepgphh ehsysrdelk lilhssrgqd psdqgmrvla savemgelev vdwansredm
      241 vsldfnaplk eilalfrrhk fsryplydae rgefvgllhi kdlllelaal dhipesfnla
      301 eltrplervs rhmplsqlle qfrkggahfa vveeadgkiv gyltmedvle vlvgdiqdeh
      361 rkvergilay qpgkllvrgd tplfkierll gidldhieae tlagliydtl krvpeeeeql
      421 eveglriiik kmkgpkivla kvlkld
//
LOCUS       WP_010432066             352 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Enterobacter mori].
ACCESSION   WP_010432066
VERSION     WP_010432066.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..352
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39375
     Region          16..247
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mrpdksltpf eirlykhyrv vhgcrialaf vltfvlvrll dvpegtwpli tlvvvmgpis
       61 fwgnvvpral eriggtvlgs alglialkle lisfpvmlaw cgaamflcgw lalgkrpyqa
      121 lligitlavv vgapagdmtt alwrsgdvvl gsllamlftg iwpqraflhw riqmanyvta
      181 fnrvyqagfs pnlverprle khlqkilndv vkmrglitpa skethiqkai feaiqtvsrn
      241 lvcmlelqin ahwasrpshl lmlnaqtlke tqqmtqqtll tiahalydgn pqpilanser
      301 lneivaelkq linerqsdnv aetpihgyvw lsmelarqle llshlicral rk
//
LOCUS       WP_010432121             315 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterobacter mori].
ACCESSION   WP_010432121
VERSION     WP_010432121.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..315
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36818
     Region          153..294
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 maianivhsg ygfrctgtek nlpltlgldg savlerqnvi pdgwlaeald qlfvaaptla
       61 gitlpwatwq depqaqalfr lasgdylare tfwqlplwlk geqpqssggm qfdesrqlyf
      121 plrprrpqge vyrrydpqik rtlsfrvadv tldgerftqw mnnprvnafw emagqqaeqe
      181 sylrrqldst ycypvigcfd dqpfgyfely waaedrigrh yrwqpfdrgl hmlvgeenwr
      241 gaqyirswlr glshylylde prtarivaep rfdnqrlfrh lasagfdtmk efdfphkrsr
      301 limsqrhrff sevgl
//
LOCUS       WP_010432101             191 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein [Vibrio].
ACCESSION   WP_010432101
VERSION     WP_010432101.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..191
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21616
     Region          10..>166
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mveflqsnmw lkqvglglll itvywvikrl gknwietlae nkrvelkrkq fvikcfnill
       61 fllfiavfti vlnlgfgdis lflssifavl gvalfaqwsi lsnltasvli ffvfpyrigd
      121 rvrvaekded isgviiditm fhvilrhssg niitypnnli lqkgvikvlv epelksetvd
      181 tklikaensk s
//
LOCUS       WP_010432199             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor
            [Pseudomonas].
ACCESSION   WP_010432199
VERSION     WP_010432199.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..214
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23521
     Region          32..202
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mikqntfnna sapvtvhvvd ddldtrdllc qlltpagypv qshnsgtafl qaydglagcv
       61 mldlvmpgmr gealldeivr rkfnvvvivm tahatiesai hitragaigf lqkpfdgdql
      121 lktlekislq aqtvfarral vddyrlrles ltsrerevmd lmlaamtsqe iatqlgnskk
      181 tvdihrarvm qkmgastite limgwtllfh gpvi
//
LOCUS       WP_010432205             163 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Enterobacter mori].
ACCESSION   WP_010432205
VERSION     WP_010432205.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..163
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18343
     Region          20..153
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mfslkrfmht sdmpsmfpvf icrlvigvff ftagfnklfv penqllmvdt mhdagipfpv
       61 imavvvafle csmgllltlg lfsrfsalvl mvissvalvt mgiytiprgl nliswlswlf
      121 ylpetlyvvl clfplswggt lcsldgwlvk rwqkvrkivf veg
//
LOCUS       WP_010432280             236 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tRNA-uridine aminocarboxypropyltransferase
            [Pseudomonas].
ACCESSION   WP_010432280
VERSION     WP_010432280.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Funk,H.M., Zhao,R., Thomas,M., Spigelmyer,S.M., Sebree,N.J.,
            Bales,R.O., Burchett,J.B., Mamaril,J.B., Limbach,P.A. and Guy,M.P.
  TITLE     Identification of the enzymes responsible for m2,2G and acp3U
            formation on cytosolic tRNA from insects and plants
  JOURNAL   PLoS One 15 (11), e0242737 (2020)
   PUBMED   33253256
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Meyer,B., Immer,C., Kaiser,S., Sharma,S., Yang,J., Watzinger,P.,
            Weiss,L., Kotter,A., Helm,M., Seitz,H.M., Kotter,P., Kellner,S.,
            Entian,K.D. and Wohnert,J.
  TITLE     Identification of the 3-amino-3-carboxypropyl (acp) transferase
            enzyme responsible for acp3U formation at position 47 in
            Escherichia coli tRNAs
  JOURNAL   Nucleic Acids Res 48 (3), 1435-1450 (2020)
   PUBMED   31863583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..236
                     /product="tRNA-uridine aminocarboxypropyltransferase"
                     /EC_number="2.5.1.25"
                     /GO_function="GO:0016432 - tRNA-uridine
                     aminocarboxypropyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=26775
     Region          22..229
                     /region_name="TapT"
                     /note="tRNA U47 aminocarboxypropyltransferaseTapT/TuaA/
                     YfiP, DTW domain [Translation, ribosomal structure and
                     biogenesis]; COG3148"
                     /db_xref="CDD:442382"
ORIGIN      
        1 mshavsrlrd erlarstrpf iargsraprc pecrvissyc lcewrpsvaa esgicllmyd
       61 teplkptntg wliadvikdt haflwsriev deqllalldd pqwqpyivfp gefvaeervv
      121 nkvacldgkr plfilldatw tearkmfrks pylerfpvls lepeqisryr lrrsrrddhf
      181 ctaevaalcl elagdasasg vldayldvfs ahylgakyqn pidsddaaht hlkafi
//
LOCUS       WP_010432311             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein [Vibrio].
ACCESSION   WP_010432311
VERSION     WP_010432311.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..206
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22447
     Region          5..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mshgiriysf plsghahrve lfvsianikh eivyvdlpsg ehkkepfltl nplgqvpvie
       61 dndivisdsn ailvylarry apdflpsdpm leaevqkflt laageiafgp aaarlitvfd
      121 apfdaqfcqi vaekaltkld tllankdflv ggrptiadia vysyvahape gnvsldkypn
      181 vlrllsnien ldgfkamprt avglya
//
LOCUS       WP_010432334             506 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M20 family peptidase [Vibrio].
ACCESSION   WP_010432334
VERSION     WP_010432334.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11483199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..506
                     /product="M20 family peptidase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56159
     Region          6..506
                     /region_name="PRK08262"
                     /note="M20 family peptidase"
                     /db_xref="CDD:236208"
ORIGIN      
        1 mtkpsklfts iasalaltas vsvwadeqdf ssmqmqgvek vdiqvdiega aqrlsqavqf
       61 qtisnqdrsd fdeqafrdyh qfleesyplv hktlkreevg dprpfsliyt wegkdpslap
      121 aifmahqdvv piaeesrdew keepfsgaik dgyiwgrgsl ddknqlqall eatemklkeg
      181 fqpertilfv fghdeevggp egakhaadii eqryekiafv mdesaplvpg ifpgirenta
      241 ligiaqkgfv sleiaingvg ghssqpgees nivalakave kveaaqfpyk ihdavryqyr
      301 ymgpelpeaq qplykavayg endtvtdlek kfidvmskne vtramlhttt avtmfnagik
      361 dnvlppaata vvnfrpmpgd tpeviiehvk kaigdermti rdisastpat nvadpsgpgy
      421 amlektirqt wgndlivspf fviggsdskh fqardfapdv ytmtaiqles vkefegfhgv
      481 nerilveeyg rsigffyqlm dnlesl
//
LOCUS       WP_010432401             130 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Vibrio].
ACCESSION   WP_010432401
VERSION     WP_010432401.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..130
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14211
     Region          13..>113
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mkvvgntviq pfhkatchcg avelelslpn giekprrcdc sicrrkgaiv gsvaldgikv
       61 lkgaehlkly qfntntakhy fcsncgiyth hqrrsspney gfnigclegv npfdiddvvt
      121 ndgvnhpadr
//
LOCUS       WP_010432491             160 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase [Vibrio
            cyclitrophicus].
ACCESSION   WP_010432491
VERSION     WP_010432491.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..160
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17514
     Region          4..157
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 manrftyyes plgtvtlqgn degllglwfe tyttkpdqlg vrdddfpife lvadqlnryf
       61 sgeaiqftvp isakgtsfqq svwqalttip ygetwsyaql adaignpkav ravglangkn
      121 pvsvivpchr vigkngkltg yaggverkqr llviegreqe
//
LOCUS       WP_010432519             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Vibrio].
ACCESSION   WP_010432519
VERSION     WP_010432519.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..282
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30773
     Region          77..264
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 msdkiyfnts nkfsfkrsli gattnlhyil apshakktar kllltpmrte qknadpkgli
       61 kseikgrdgv lktyslgtgp vwvlthgwsg tasqffplme hiaakgftal aydhpahggs
      121 dgvhghipaf vngleailds vgevaglvgh smgtasalec khvklenkpm lliapvldyl
      181 enlfgsvars gysmklfeav vgeveeqfny piqsvdpygk lalresqtii vhdekdkftk
      241 fdvsqraane mdrvtliatr gqghgrvmkc pqvfesfdnl ig
//
LOCUS       WP_010432537             288 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Vibrio].
ACCESSION   WP_010432537
VERSION     WP_010432537.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..288
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31882
     Region          14..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtsvrvvdhv isahatsdgd gvkiqrlagf nntrfspflm idelksdesk dyvggfpphp
       61 hrgietltym lqghfqhkdh lgnvgelrsg gaqwmaagrg vihsempmme egalhgfqiw
      121 inqpathkmq paqyhdfqsd siaeyqneqi gllrvisggf klhdpadaet iqtqgplqtt
      181 gvplsvvdwr ahsgqkvtlr tdvnhnamty vyrgsikidn kvvnqgqlal ltkaellsld
      241 sledsgvlif sgepinepvv hygpfvmnsm eeieqtiqdy nngvfety
//
LOCUS       WP_010432591             393 aa            linear   BCT 01-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Pseudomonas congelans].
ACCESSION   WP_010432591
VERSION     WP_010432591.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..393
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42233
     Region          15..290
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mqdravtnsa isnvepvtgl ilsgggaraa yqvgvlagia dllppgspnp fpvivgtsag
       61 ainavklasg alhfrvaihq ltefwqsfrs hqvlrsdwsg vihqasrffg rsllgfgrni
      121 pvallnsspl rdllnerldl sgieaaieah hlravavtaf gyesgqavtf yqgrgtiepw
      181 lrhrrigrpt qltvdhllas saipllfapv mldeeyfgdg avrqsapisp alhlganrvl
      241 vvgvsgnprg lkterpapra prgvqpslaq isghmlnstf idnlesdiel lerlntasal
      301 lpedqvrqpg mepvevlvis psrpldeiaa rhrrelppal rtflrgpgat kssgasvlsy
      361 llfesgycse lielgrhdai aqgaelkrfl rle
//
LOCUS       WP_010432638             342 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudomonas congelans].
ACCESSION   WP_010432638
VERSION     WP_010432638.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..342
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37550
     Region          1..337
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 maflqlegls krygsidavv atnlavdkge fvsllgpsgc gktttlqmia gfvevsdgri
       61 vldgrditha kpssrglgvv fqsyalfphm tvadnvafgl rmrkvpaael hprvsrvlel
      121 vrlgqhaery prelsggqrq rvalaralvi eppvllldep lsnldanlre emqfeirriq
      181 nevgittlmv thdqaealsi sdrvvvmqag ritqidepyk lyehprtrfi sgfvgkanml
      241 qgdldssgip qirqesgdgs ltlslrpeki dlvapgcgrl sgrivtryfl gsqwlyriqt
      301 gigevtvvrr ndgqaplekg aavdmdwpte llrvldadev ra
//
LOCUS       WP_010432643             264 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas congelans].
ACCESSION   WP_010432643
VERSION     WP_010432643.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28643
     Region          1..253
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mskngplals fhalvvifmm aplvvvclva ftpentlslp ttqfslrwfk avferadfid
       61 sfynslilaf vsatlatlia vpaalaitrh tfpgrnffna lflspiiiph lvlgvamlrl
      121 falmgvngsf twlifahvlv itpyvlrlvl aaaigidrsa ehaaeslgad rftlfrqitl
      181 pmilpgvagg wllafinsfd evtlsifvts patqtlpvrm yvyatesidp mmaavsalvi
      241 altaatmill drvygldrvl vgkh
//
LOCUS       WP_010432713             447 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Vibrio].
ACCESSION   WP_010432713
VERSION     WP_010432713.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..447
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46502
     Region          15..447
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mseskteiln qdanngilek ffkikahgss vknelvggvt tfatmayiif vnpqimaasg
       61 mdsgavfvat cigaaigcll mglfanwpvg lapgmglnaf fsftvvsemg yswevalgav
      121 fisgilfvgm sfykvrqwii esipvslrys mtagvglflg liglktagiv venpatlvsl
      181 gdftkpeall aaiafliiav lserkifgav ligilsvtlv gmmlglvqyn gffaappsla
      241 ptflkmdimg aldvsmisvi laflfvnmfd tagtlmgvae ranltnpetg kieglskalk
      301 adsissvaga cvgcppvtsy vesaagvaag artglsaivv gvlflaaifl splagmipay
      361 atsgaliyva fvmmssmqhv dwkdftngap aaitalmmpl tfsiangial gfitytvlkl
      421 atgktkdvsi smyflaaifv aklvfig
//
LOCUS       WP_010432725             193 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pseudomonas congelans].
ACCESSION   WP_010432725
VERSION     WP_010432725.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20426
     Region          5..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrvtkaqaqa nrahivetas vqfrehgydg vgvadlmaaa gfthggfykh fgsksdlmae
       61 saacaisqtv akstgidpaq fidyylsreh rdnlgtgcpl aalsgdaarq sdevkttfad
      121 giesllaala paqaspgdee wkqarantid rfahalgall lsrscpndsp ladeilevcr
      181 armraqlesg qtd
//
LOCUS       WP_010432753             293 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Vibrio].
ACCESSION   WP_010432753
VERSION     WP_010432753.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..293
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31633
     Region          2..291
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mfeqvvsilf pvfalasagf avgrwlkpdf kpinrinmdv cipalvfasl ttmpldteql
       61 plitaslvav lvpallmipi ckifklnfka wapphmfrns gnlaiplfty tfgesalapa
      121 vllfvvsacv hisvglalls dgnpikqilk mpiflaaala mtlnlsgiav wnpiyeatsl
      181 lgqaavpiml lslgsqmvnl klsglkvglf ctaqslftgs iaftiiyffi plptlhlqmm
      241 vlftmlppav mnylfaerfn veppkvasmv lfgnflsvit lpillsfals lsp
//
LOCUS       WP_010432873             377 aa            linear   BCT 01-JAN-2025
DEFINITION  fimbrial protein [Pseudomonas congelans].
ACCESSION   WP_010432873
VERSION     WP_010432873.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..377
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=39182
     Region          219..377
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mntasqclay glmalgashf siamagepqq npsnecywrt apgmkdfrrd igalyvarda
       61 kigsvigsvn msaitpdpag levacindgt allefravat vpvfpgvidp ingedvtgki
      121 lqtnipgvgv rtrlgipltp ppggpcnncf ipvdgdptvp ylgihdhrpm isamrilhlr
      181 hevtlvktgp ipsgpqlldg gelwsgsvtp lgkimsfglt gtvhqaqcsv ganavsadpv
      241 qlgewdsadf tgpgftttav pfsislsnce tdtapgtgfv atahiqldgv qgsmpveptn
      301 sgvfsltsds taqgigiqil kadaitpmel ltevplsais pgntvlnfha rfyqtdansa
      361 irpglakgal sftmtyk
//
LOCUS       WP_010432945             262 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterobacter mori].
ACCESSION   WP_010432945
VERSION     WP_010432945.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..262
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28970
     Region          1..262
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mkpliqvqav sqrfstasge flalqnvsfd ihegetvsli ghsgcgkstl lnliagitlp
       61 tegglicdnr eiagpgpera vvfqnhsllp wltcfdnval avdqvfrrtm skaerkewie
      121 hnldrvqmgh alhkrpgeis ggmkqrvgia rplamkpkvl lmdepfgald altrahlqds
      181 vmqiqqalnt tivlithdvd eavllsdrvl mmtngpaatv geilrvdlpr prnrvqladd
      241 sryhhmrqqi lhflyekqpk aa
//
LOCUS       WP_010433016             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010433016
VERSION     WP_010433016.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34010
     Region          3..58
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          119..286
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
ORIGIN      
        1 mdlrqleafa avmsagsvta agkmlgrsqp svtraiqele qelgfalfer sgpkvtpthk
       61 afmmygeves allgvrnihq raqhiaqeen hqiklvaisa laagllpaal srlpehlrpq
      121 qiqlqsmspe nvvqavlskt mdlgavslpl ehrgleihwi geapcvavlp adsalaahev
      181 lsmellrqht litmanpyrf rrridkafqa aggqpprmld tntsliamqm arvglgialv
      241 dpftamgvpv qgvvvrpiac nipfffglis afasplsdva salineiads akillpemim
      301 heasahdall qsiyae
//
LOCUS       WP_010433065             241 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein [Vibrio].
ACCESSION   WP_010433065
VERSION     WP_010433065.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..241
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25471
     Region          7..240
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 meyidqtvli amalifvgsf vqtaigfgla ivaapllflv spdyvpapic lvglfisifn
       61 afkhranisi gglkiallgr ipgslaggal lvmvstsvls lwlgllvvfa vivsllpfrl
      121 eptptkmgia gffsgffgts sgiggppmal llqhqdanql rgnlsaffvf ssiisllvqi
      181 pigfftmhhl iitipllpaa wlgykvalmt tqsipkekir igslllcsis gftaiwqglv
      241 s
//
LOCUS       WP_010433080             366 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: permease [Vibrio].
ACCESSION   WP_010433080
VERSION     WP_010433080.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..366
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=39151
     Region          5..365
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 msnemltmlk daldmfafla veliilflai syivgilqef ltpekiqsil ssrngkgyvv
       61 aallgaitpf cscstipflk gllraragfg pmmvflfgsp llnpviiglf vitfgwqvav
      121 fyflvamtvs vvagyalekl gferyvkpea yessgsassc gtscddsapk kavpvkaess
      181 cgtsacgepa pvmaketscc dskkeepqvt vsgcstdgsa taeivekkep srwmriwfst
      241 wkdfkqvfpy lmmgiaigsf iygfiptdli aqyagegmwy aipvaavigi plyiraeavi
      301 plsaalvqkg malgsvmali igsagaslte villksifkn qmiaaflfvi lsmamgagfl
      361 ysfifg
//
LOCUS       WP_010433152             184 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TMEM165/GDT1 family protein [Vibrio].
ACCESSION   WP_010433152
VERSION     WP_010433152.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..184
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19644
     Region          1..183
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 msvlaisitt valaeigdkt qllslllasr yrkpipiiaa iffatianha laawlgvvva
       61 dylspevlkw vlvvsfiama gwilipdkld ddeqisnrgp fvasfiaffi aeigdktqia
      121 tsilgaqysd almwvilgtt igmllanvpv viigklsadk mpldlirkit allfvglaia
      181 aafy
//
LOCUS       WP_010433289             500 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Vibrio cyclitrophicus].
ACCESSION   WP_010433289
VERSION     WP_010433289.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..500
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=56825
     Region          1..403
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 maiaysyirf sskaqaegds lrrqlqrtke wcrknnvels dknfqdlgis afkektrpsl
       61 ddlfaaiqtd siiegdyiil enldrlsrqg idhttemlrk ilrsgvnvvd ltnglelnkt
      121 slndlvsvir ialaadlayq eskkkservl aakatqrklv regkvinkrl pfwitnsdgy
      181 rlndkaqivr diikqrtsgv gfhriamnln gayeapkakh wsdttireiv ksralygsmv
      241 dkdgevesvf palisftewq aiqaehvssa ggytqhnhla rlvkcecgsa mskkiqkskt
      301 ktktheyntw kcvaatsggc ehkgvirdld vdifkslnhl kinktksdtq lnkiskqiek
      361 ksvrqqeleq alleddapia altkaikktt eelkqlrser dllsvrtdsk llielqdnav
      421 efnielrklv dkivvtpitr nrfqikihqh nghivnclkg rksqrsewtr vfgkteeklr
      481 iateddgmpw vdwaetdepd
//
LOCUS       WP_010433307             317 aa            linear   BCT 01-JAN-2025
DEFINITION  transketolase family protein [Enterobacter mori].
ACCESSION   WP_010433307
VERSION     WP_010433307.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..317
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34331
     Region          14..317
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mikvapagek davemrkvya gfvakqieag seiialeadl mssmamdgva rdypqhvinc
       61 gimeanvigt aaglsltgrk pfvhtftafa srrcfdqlfm sldyqrnnvk viasdagvta
      121 chnggthmsf edmgivrgla hsvvlevtda vmfedvlrql idlegfywvr tirkqapsvy
      181 apgstftigk gnvlregsdi tliangimva ealeaarqle qegvsaavid mftlkpidrm
      241 lvknyaektg rivtcenhsi hnglgsavae vlvetcpvpm rragvkeryg qvgtqdflqk
      301 eygltahdiv saarell
//
LOCUS       WP_010433308              87 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YihD family protein [Vibrio].
ACCESSION   WP_010433308
VERSION     WP_010433308.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..87
                     /product="YihD family protein"
                     /calculated_mol_wt=10188
     Region          1..87
                     /region_name="YihD"
                     /note="Uncharacterized conserved protein YihD, DUF1040
                     family [Function unknown]; COG3084"
                     /db_xref="CDD:442318"
ORIGIN      
        1 mkchrieell elmepewqkd qelnllefii klskeagyeg kleeltddvl iyhlkmrnse
       61 kdemipglkk dqeddfktai lkargil
//
LOCUS       WP_010433338             363 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Vibrio].
ACCESSION   WP_010433338
VERSION     WP_010433338.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..363
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40300
     Region          <18..84
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 mrhfssifsl vcaslsftvm aenseqplti rqdapqvyvv vkgdtlwdis tmyldspwlw
       61 prlwqvnpei enphliypgd klslvwinge pvlslkpvik lspkirvsek kavptvnegl
      121 vlpylqsdrl veqqdiqsaq rvlgtsdgkr flsgedrlfi sgkqqypkwg iyravetyqr
      181 qlpqasmtsl rlvatarlke vdaefsrlqi etqlqevlln dlvlpelgvd qvklsttfyp
      241 apsaagqfan ilgsldgsqy saknqvvvin kgsqdnlrqg smftlsenga vvfgkqgeys
      301 ykesaasdkv qlpstslgsl mvirpyeyfs lalitqsskp vsndilvvsp vdlalkeevk
      361 gtk
//
LOCUS       WP_010433387             504 aa            linear   BCT 01-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Enterobacter mori].
ACCESSION   WP_010433387
VERSION     WP_010433387.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..504
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=52740
     Region          1..488
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mdtwiylsqg favamtpenl vialigcfvg tivgllpglg pingvaillp lafalhlpae
       61 salillatvy igceyggris sillnvpgda aaimtaldgy pmaqqgrggv alsisavssf
      121 fgsliaiggi ilfapalaqw slafgpaeyf almvfaiacl gsmmaqnplk sflsaliglg
      181 latvgvdant gvyrftfdsv hlsdgvqfiv vviglfsvse illmlehtss gqtlvrktgr
      241 mlfnakegaq cvgatlrssv igffvgilpg agatiasait ymtekklsgn sdsfgkgdir
      301 gvaapeaann asacgsfipm ltlgvpgsgt tavmmgaltl ynitpgpamf teqpdivwgl
      361 iaallianvm llvmniplig lftrmltipl wflvpaiaav savgvyavhs ttfdlvlmvl
      421 lgvlgyilrk mhfpmsplil gfvlgemleq nlrralsisn gnmsilwess vtkillamai
      481 mvivappvlr llrrrqrkpe pdvg
//
LOCUS       WP_010433399             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator [Vibrio].
ACCESSION   WP_010433399
VERSION     WP_010433399.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21501
     Region          6..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtthapqdkr qqilsaaekl iaevgfqgls mqklakeagv aagtiyryfd dkdhliddvr
       61 vlvtqrvada vqegvndsdp ikqryrtmwl niwnlagtnl aaiknrvqyd slpitnslnf
      121 relerkmfaq vellfnegke qglfkpldne vlsglslaas vslarkhslg fyqldeaale
      181 aaieaswdai ikh
//
LOCUS       WP_010433609             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterobacter].
ACCESSION   WP_010433609
VERSION     WP_010433609.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..245
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25601
     Region          42..242
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mkvmrdpllw lallfvgllf lmphsaalfs slfpglprpv yqqesfinla lahawlvtis
       61 sviaivlgvg agiavtrpsg refrplveti aaigqtfppv avlaiavpvi gfgqqpaiia
      121 lilygvlpil qgtlagiaav pasvlsvaeg mgmsawqrlr kvelplaapv iiagirtsvi
      181 inigtatias tvgantlgtp iiiglsgfnt ayiiqgallv alaaivvdrl ferlalylsr
      241 hrhgr
//
LOCUS       WP_010433691             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: spermidine synthase [Pseudomonas].
ACCESSION   WP_010433691
VERSION     WP_010433691.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..253
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28085
     Region          31..213
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mteererver ilaevhddfg mirvlevedy rflefgdaie qsctftadps wleydytram
       61 ligalchdap esalflglga gtltqacmkf lpledvevie lrpdvprlam efmgldddpr
      121 lyirigdald lldsaepadl ifvdlytdvg pgvghlawnf lqscqqrlnp ggwliinqwa
      181 tddgkplgaa llrglyhrhy welpvkegnv illvpadldq tldidalrgr aealapdlgy
      241 slasligair pat
//
LOCUS       WP_010433699             286 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterobacter mori].
ACCESSION   WP_010433699
VERSION     WP_010433699.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..286
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31282
     Region          12..278
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtssilaann plldvrdlhv dfinggavth avrgvsfqlg reklaivges gsgkstvgra
       61 llrlhpakaq isasrmqfgd vdlhsvseaq mrgirgkris mimqdpkysl npvvcvgdqi
      121 aeawlthhpg rkaeakakvl emldvvrirq pgrvyhlyph eisggqgqri miammlitdp
      181 elviadepts aldvsvrlqv lgllddlvqs rglglifish dinlvrsfcd rvlvmyagrv
      241 vesiaakdlh nakhpytqgl isalpeinhr rptlpvlqrq asrlte
//
LOCUS       WP_010433842             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Vibrionaceae].
ACCESSION   WP_010433842
VERSION     WP_010433842.1
KEYWORDS    RefSeq.
SOURCE      Vibrionaceae
  ORGANISM  Vibrionaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Vibrionaceae"
                     /db_xref="taxon:641"
     Protein         1..144
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15485
     Region          35..143
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mqelvpfvqe nmilaivwig lvvaiianvi ktsnaaykei taaqtthmin rengvvvdir
       61 tkdefkkghi tdavhilpsd ikannfgsle shkadpiivv cktgqtaqes anllvkagfe
      121 nvsvlksglv awseanlplv kgkk
//
LOCUS       WP_010433878             230 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [Pseudomonas].
ACCESSION   WP_010433878
VERSION     WP_010433878.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..230
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25934
     Region          1..223
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrldrflsnl prfnrqqvrl alasgrvqvd gqatrdphhe vrefscvald geilqagkap
       61 ryfmlhkpqg cvsatsdaqh ptvldlldep dkhelhiagr ldfnttglml itndgqwsrr
      121 ltqpqtkmpk vyyveteqpi deryaakfae glyfafeglt tqpaqltllg prsarlsive
      181 gryhqvkrmf ghfdnkvlrl hrenigalal dpglrpgsyr alnageislf
//
LOCUS       WP_010433910             501 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Enterobacter mori].
ACCESSION   WP_010433910
VERSION     WP_010433910.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..501
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53773
     Region          4..484
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(61,63,67,70,74,107,110..111,120..127,132,135,138,
                     231,235,238,241,243,420,422..423,425..426,429,432..433,
                     435,437..440,449,453,455,469,476..481,483..484)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(147..150,158,173,176,206,223..226,229,247..249,281,
                     385,387,413)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(150,247,278,281)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 metvanfihg ecvtgsgqrv qaifnpatge qirqvvmstv qeteqaiaaa qqafpawarh
       61 aplkrarvmf rfkalleenm erlariisee hgkvfsdavg eltrglevve facgiphlqk
      121 gehsasvgag vdshslmqpl gvcvgitpfn fpamvpmwmf pialatgntf vlkpsekdps
      181 lalalaqllk eaglpdgvfn vvqgdkesvd vlltdprvqa vsfvgstpia eyiyqtasah
      241 gkrcqalgga knhcilmpda dmematnaim gaaygaager cmalsvvlav gdktaddlct
      301 rlekqiaalr vgpgldqtpe nemgplissa hrskvlgyid sgeaqgaklr vdgrgfsvkg
      361 heqgyfvgpt lfdnvtpemt iykeeifgpv lsvvrvadya savdlinrhe ygngsaiftr
      421 dggcarrfce evqagmvgvn vpipvpmafh sfggwkrsif galnvhgndg vrfytrmkti
      481 tarwpemqqe tgaafsmptl g
//
LOCUS       WP_010433959             182 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Vibrio cyclitrophicus].
ACCESSION   WP_010433959
VERSION     WP_010433959.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..182
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19999
     Region          <18..172
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mirlldflaa flgllflwpv lavvtvigml dtgspifiqe rvgrnkkpfk likfrtmsve
       61 tksvashlts ntsitklggf lrktkidelp qlinvvkgem slvgprpnlf nqeelikerd
      121 algvydvlpg vtglaqvqni dmstpkllak tdrkmidtlt vkdyfkyiim tatgsgsgda
      181 vk
//
LOCUS       WP_010434020             548 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Vibrio].
ACCESSION   WP_010434020
VERSION     WP_010434020.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..548
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60714
     Region          14..548
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mldnlsklti karlaigfgt tlflmmlltv lgiqkvnfid etlteitdvn slkqryainy
       61 rgsvhdrait irdiaiarts qeislleqev kqleafyres eaqmnqmrsq gevftadeqr
      121 ilakidkvqq ytlplvdeii rdkksgtvmt dsildsarpa fiqwlaaine fidyqeeqsq
      181 kltseariva gdfqqlmlll taialtmslf vgfiiersfr aslggepwei semikkiseg
      241 nlsqrfikpe eavgiyrsli ilndkvstvi kssrgistqv atsaeqltgv mvdtannaqh
      301 eltqveeisn aiselsstsk evtsnavhae qeakkaidnv fkgnqtlees ielthkinds
      361 vkqtasmivd lktnamdige vtavistisd qtnllalnaa ieaarageyg rgfavvadev
      421 rnlasktqds tksiqdiitk lqaqsekand nmisnveqiq esvtlsenvq qsfshieqsv
      481 qsiseintlv tstsqeqfsl terialntnn afdlvnqnvs gihqtqqaak elsqlaveqk
      541 keleffkv
//
LOCUS       WP_010434023             140 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Enterobacter mori].
ACCESSION   WP_010434023
VERSION     WP_010434023.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..140
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15082
     Region          11..140
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mnslryfdfg ssrsflllia riaivvlfii fgypkltgfs gtvqymtslg apmpmlaaii
       61 avvmevpaai livlgfftrp iavlfvfytl gtavighhyw dmtgdavvpn misfyknvsi
      121 agafillaiv gpgaisldrr
//
LOCUS       WP_010433993             173 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase [Vibrio
            cyclitrophicus].
ACCESSION   WP_010433993
VERSION     WP_010433993.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..173
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19241
     Region          4..152
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 medttykmly napigkmvii sngdaiieid hlnaepelte npdslcleta rqldeyfagq
       61 rtsfdlplep kgtdfqrkaw valtsipyge tisygeqakr mdnpkavrav ggangknpfs
      121 ivvpchrvig angtltgytg gmnrkewlls felkmvnser kminserkrl nnk
//
LOCUS       WP_010434084             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010434084
VERSION     WP_010434084.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35555
     Region          10..69
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(113..114,116..117,120,124,126..132,224..229,
                     235..236,238..239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176111"
ORIGIN      
        1 mrkslmrmtl rqlrifnevc dlrsysraae emsltqpavs lqirqleeli gqplfeyvsk
       61 klylteaaqa lqqasrdifg rlesldmqls dmqgslqgql klavesscky fiphlfaafk
      121 rqhpevslsl mvvnraqvir rlsdnrddlv vmsavpldmg leflpflnnp ivavappdhp
      181 lssretlslk dlepwplltr etgsgtrrac eeffkekrvh ftqtlevsss eaqrecvvag
      241 lglamltrha vcqelatgal velpvaelpl yrswcvaqag dkrlspvaha flafirtera
      301 qisqlverfd grprat
//
LOCUS       WP_010434116             464 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [Pseudomonas].
ACCESSION   WP_010434116
VERSION     WP_010434116.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..464
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=51262
     Region          1..463
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mtdrvlidel qtlvepgkvl tdagsletyg kdwtkqftpa plaivfpktt eqvqaivrwa
       61 nerlvalvps ggrtglsaaa vaangevvvs fdymnrvldl nltdrtavcq pgvitrqlqa
      121 laeenglyyp vdfassgssq iggnigtnag gikvirygmt rnwvaglkvv tgkgdlleln
      181 kdliknatgy dlrqlfigae gtlgfvveat mrldrapknl tamvlgtsdf nsimpvlhaf
      241 hgrldltafe ffsdksfarv margdvpspf dtpcpfyvll efeattedla dqalatfehc
      301 veqgwvldgv msqseqqlrn lwklreyise tishftpykn disvtvskvp eflaeidaiv
      361 aehypdfevl wyghigdgnl hlnilkpesl dkdeffvkca rvnkwvfetv ekyngsisae
      421 hgvgmtkrdy ltysrspvei eymkalkavf dpngimnpgk ifav
//
LOCUS       WP_010434302             180 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase, partial [Enterobacter
            mori].
ACCESSION   WP_010434302
VERSION     WP_010434302.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         <1..180
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          1..77
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 aadvtgvdis ekmlaragel tadpqihyqr sdleslelne nsldlvyssl alhylpalda
       61 lfakvqralk pggslvfsme hpiytcairq gwltddsger fwgvnhyqee gkrvsnwlad
      121 gvikyhrtls ttlnaligag ltisevnewg ptqaqidawp alaeeaerpm lvllaarkaq
//
LOCUS       WP_010434347             407 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein [Vibrio].
ACCESSION   WP_010434347
VERSION     WP_010434347.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..407
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=44934
     Region          2..406
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mptyryvgrs sdgsqvtgql dannedlaae slmskgiipt siklgrsgds vldmdisslf
       61 spnvplevlv lfcrqlyslt kagvpllrsm kgltqncenk qlkaaleevv aeltngrgla
      121 asmqmhpkvf sslfvsmisv gentgrldqa llqlagyyeq evetrkrikt amryptfvic
      181 filiamfiln ikvipqfssm farfgvdlpl ptriligmse ffvnywglml gvifglifaf
      241 kawvktdngl etwdrwrlki pviggvvnra llsrfsrtfa lmlkagvpln qslalsaeal
      301 dnrflelrvq amksaieags tvsstainse iftplviqmi svgeetgrid elllevsdyy
      361 drevdydlkt ltariepill vvvagmvlvl algiflpmwg mldaikg
//
LOCUS       WP_010434368             559 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010434368
VERSION     WP_010434368.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..559
                     /product="MFS transporter"
                     /calculated_mol_wt=59896
     Region          23..316
                     /region_name="ProP"
                     /note="MFS family permease, includes anhydromuropeptide
                     permease AmpG [Carbohydrate transport and metabolism,
                     Amino acid transport and metabolism, Inorganic ion
                     transport and metabolism, General function prediction
                     only]; COG0477"
                     /db_xref="CDD:440245"
ORIGIN      
        1 msdkyaprew aaherptmpg spstplhsta rrwafavvgv ivaltgglgn alvvanlpyl
       61 qgalgatsqd iawlpaayim tnvsmnlllv kfrqqfglra ftelflvlya lvtlahlfvn
      121 didsaiavra ahgmvgaals tlglyymiqa fpqkwrlkal vlgigtaqla tplarlvsed
      181 llqiaqwrgl ylfelgmall slgcvlmlkl ppgdrfkafe kldfltfgll atgfalfcav
      241 lslgriewwl eaqwigiasa asialicagl aiehnrsnpl litrwlgsga ilrlglavil
      301 frvvlseqsv gavgflqaln mgsqqlhtly lvmllgsvsg lavsaltinp ahlikpllis
      361 lammaigawm dshstnltrq snmylsqfll afggtfflgp tlvlgisgvl anprnmvsfs
      421 vlfgitqnig gligsaalgt fqvvrekfhs shvvehltli dplvqarlqs ysasyssvia
      481 dpalrnsqgi ramataatre anvlayndvf mlialiavlt miwisarvlw lkmttqplal
      541 apvapaaspt vsnsgvkss
//
LOCUS       WP_010434405             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Vibrio].
ACCESSION   WP_010434405
VERSION     WP_010434405.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..145
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16014
     Region          1..141
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myrqilvpvd lndkgfsdka velavwhakh snaeihilnv lpgihmsmva syfpkdaanq
       61 mkldvknqlk efadkhidde vvykvhvaeg ktyttildya eklgadlivm pshkrskidk
      121 vvlgsvaskv vqnspinvlv vkpqg
//
LOCUS       WP_010434409             286 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter permease [Enterobacter].
ACCESSION   WP_010434409
VERSION     WP_010434409.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..286
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30035
     Region          13..275
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 miwhtffqpf ieygfmrral vvclalsvst talgvflqlr rmslmgdals hailpgvavg
       61 yllsgmslla msiggfiagi tvalvaglvs rrtplkedas fagfylgsla lgvtlvslrg
      121 snvdllhllf gsilavdnda alfvtgvciv tlitlaifyr glvteafdta wlqvnarglp
      181 gllhglflal lvlnlvagfq vlgtlmavgl mmlpavaarc wvrtlpglll magisgifca
      241 wlglslswaa slpagpsivl tasalffisv lfgtrsrlag slralf
//
LOCUS       WP_010434407             536 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010434407
VERSION     WP_010434407.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..536
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58831
     Region          1..532
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mnndnlieir dlavefvtgd srqrvvenis fdirrgetla lvgesgsgks vtahsilrll
       61 pypiashpsg tiryagedll kveekklrti rgnriamifq epmtslnplh svekqinevl
      121 glhkgltgka atertlelld lvgipeprkr lkalphelsg gqrqrvmiam alanepelli
      181 adepttaldv tvqlkilell kqlqarlgma lllishdlnv vrqianrvcv mqrgciveqa
      241 sceelfrspq hpytrvllsa epsggpstnp agaplleied lkvwfpikkg llkrtvdhvk
      301 avdgirfslp egqtlgivge sgsgkstlgl ailrligsqg tirfkgnale slsqqqirpl
      361 rrqmqvvfqd pfgslsprms vaeivgeglr ihgmgtaaeq qtaiiealre vgldpdtrhr
      421 yphefsggqr qriaiaralv lkpalillde ptsaldrtvq rqvvellrsl qtkynltylf
      481 ishdlavvka lshqlmvvkq gqvveqgaaq difaapqhpy tqqlleaafl apvavd
//
LOCUS       WP_010434412             217 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Enterobacter mori].
ACCESSION   WP_010434412
VERSION     WP_010434412.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..217
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23936
     Region          1..203
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mivmnelvag ydrqpvthpl sggiergsmt aiigangcgk stllktlagf ippvsggfrw
       61 qgkrpvigwl aqrhaleaqf pltvqdvvsm gcwprislft afrretrlri asalervglg
      121 smalstidel sggqfqrmlf arvlvqqapl vmldepftgv deatcnvlmd lmlemymqgq
      181 tllavlhdse rvsrhfpqtl rldadvpqwk tervrva
//
LOCUS       WP_010434443             124 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudomonas].
ACCESSION   WP_010434443
VERSION     WP_010434443.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..124
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14140
     Region          7..103
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mtdspadrrr fkriafdakt dlkqgdkswk vqlvdlslkg llierpdpws gdqtqpfevd
       61 iilsndahvk mdveithdnn rqlgfvcrhi glesishlrr lvelnlgdpe eldrelaali
      121 elqe
//
LOCUS       WP_010434492             219 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Vibrio cyclitrophicus].
ACCESSION   WP_010434492
VERSION     WP_010434492.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25331
     Region          14..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtvrkagrpq qnldvrqlli ehardlfvvq sydkvstrli aeragvniam iryyfgnkag
       61 lfeamlretl rpmqlqmqkl veesshenfl dlmrtyykem vkvpkfprli aqvmnmppse
      121 vqrellekvf ldvakpaqdv ifeklveqgi lkqnmdpklc rvsyislmvf pfiappplla
      181 ihgielneef lnrliehniq lmsegfinve ststlqepr
//
LOCUS       WP_010434527             295 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Enterobacter mori].
ACCESSION   WP_010434527
VERSION     WP_010434527.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13300132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32250
     Region          10..>143
                     /region_name="PRK11242"
                     /note="DNA-binding transcriptional regulator CynR;
                     Provisional"
                     /db_xref="CDD:183051"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,187,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mftlqrtamf iavaeagsft aaaeamgltk avvsfnirql edelgvtlll rstrrltlte
       61 agalfhqrsv allkeaeqlq ddvrashagl agelritttp eygsqvvvpl laefsqqhpe
      121 lrvrhvsssl hadliserfd vairlgtlad sryhaamits failpvaapd wlanhpvetl
      181 eqlakadwii herlpsplrw qvkassgelv sfeitkaprl yadsaqalma faragsgval
      241 lpewlvrnal dagqlasvlp gytfaqqgiy avypdaqhvp akvrkfidfm rarvn
//
LOCUS       WP_010434545             422 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: O-acetylhomoserine
            aminocarboxypropyltransferase/cysteine synthase family protein
            [Vibrio].
ACCESSION   WP_010434545
VERSION     WP_010434545.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..422
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=45702
     Region          1..422
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mkdetlsihf gyetdpttks vatpiyqtva yefddaqhga dlfnlavpgn iytrimnptn
       61 dvlekrmaal eggiaglvvs agsaainyai qtlaqigdni vstpqlyggt ytlfahmlpn
      121 qgievrfakd dkpeslaali dektkavyce signpagnii dlervaelah aqgvpvivdn
      181 tvatpvlckp idfgadivvh sltkyvgghg ttlggvivds gkfpwaehkd rfpvfnqpep
      241 syhgvvytea fgeaafigra rtvplrntga alspmnafml mqgletlslr merhtenalk
      301 vaeylqqhek vswvsyaglp tsefyplaek ymqgkpsail sfglkdgyea gvrfydalqi
      361 fkrlvnigda kslachpast thrqlseaeq kqagvspemi rlsvgiehid diladleqal
      421 sa
//
LOCUS       WP_010434685             353 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA-binding protein [Pseudomonas sp. PvP027].
ACCESSION   WP_010434685
VERSION     WP_010434685.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. PvP027
  ORGANISM  Pseudomonas sp. PvP027
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Pseudomonas sp. PvP027"
                     /db_xref="taxon:2806587"
     Protein         1..353
                     /product="DNA-binding protein"
                     /calculated_mol_wt=39531
     Region          7..119
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <66..>331
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 margginkav vqkarqslla kgmypsidav rvelgntgsk ttisrylkei esfdprpqss
       61 rermgeelsa mvaslldrlm eegdesieqa rsafdlqrva leaqianlqs eltsarrqld
      121 tqqaaieaqt adlqttqssl qaeltrnagi sqrctdleal vgdrdkqiqs leekhvharg
      181 alehyresvk eqrdqdqrrh esqlhesqve qrklqetlvl kqddltrlnr dnerllgesr
      241 qqvktlhahe ariqgltgei qglklaeaky agvneqlqeq iaalrqdaka lneaaaksse
      301 relevrlllt saqaenqqlr rdltiaeerr eidgaaastp prpsnrpskt prk
//
LOCUS       WP_010434688             230 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Pseudomonas sp. PvP027].
ACCESSION   WP_010434688
VERSION     WP_010434688.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. PvP027
  ORGANISM  Pseudomonas sp. PvP027
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pseudomonas sp. PvP027"
                     /db_xref="taxon:2806587"
     Protein         1..230
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=26126
     Region          80..230
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mgmtniekea sellrmlwrd ryhlwgdrei tplqardprk aalaygfeyr efadlgdpkf
       61 irggsgpkia glidrqanri aisqefsptv klftgaheig hlflhqgevm hrdraldgrp
      121 vsgprdreer eadffaacfl mpaklvadrf rrqflcgerl hfndtvayhl dphnieglly
      181 asadslerel alarcqrfnn mnvvslaaqf gvsdsamalr lkelglvrwp
//
LOCUS       WP_010434724             230 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Pseudomonas sp. PvP027].
ACCESSION   WP_010434724
VERSION     WP_010434724.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. PvP027
  ORGANISM  Pseudomonas sp. PvP027
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pseudomonas sp. PvP027"
                     /db_xref="taxon:2806587"
     Protein         1..230
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=26429
     Region          91..230
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mneayiekaa tdllmqiyrd rrylwpdqdt qpmmmrspqi aalvcgydyh vyptlgdtkf
       61 nrhntgtria glidrqanki avatefgdkv qlftgaheig hlvlhedtvm hrdrafdggp
      121 lhsprplaer qadrfaacfl mpqkllrerf efmfcckgql rfsdviafhl dpnhpdrlly
      181 askdsdereq alarctqfnn rnlvslaqqf gvsdsamair ikeldlvrwp
//
LOCUS       WP_010434728             355 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein [Pseudomonas
            sp. PvP027].
ACCESSION   WP_010434728
VERSION     WP_010434728.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. PvP027
  ORGANISM  Pseudomonas sp. PvP027
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Pseudomonas sp. PvP027"
                     /db_xref="taxon:2806587"
     Protein         1..355
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39596
     Region          69..118
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(89,91..93,95,106..107,111..112,115)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mrrtravlel falgmdstla etlqaaewti pklrkqsdwd lmqlgisaei rqslqlcdpp
       61 aipvdtlsev leanramcci crlhnqiiva htivpldagg shsaqniail cqyhhieals
      121 eaqrtrsvgi pptidrlvsa kktwehyyee pdlvsvkqra srpgevnwwy fnllelceiv
      181 kakaqlnqlp sfhsvfkngl cneegipvqa pnapslyqgt gglalyaymf evlfellgtq
      241 slrsiystdr qssvvgtvkk gnlicfqgeh vfeefpsvnt drhlirstsr frrmevsfvf
      301 dldestskla ktmwlcgqke masiilvtqa gyvgttyciv gnvlairsas drvkg
//
LOCUS       WP_010434811             242 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tRNA1(Val) (adenine(37)-N6)-methyltransferase
            [Vibrio].
ACCESSION   WP_010434811
VERSION     WP_010434811.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..242
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26709
     Region          9..238
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mkdktietks fnfkkfsiyg gqsgmpvstd gvllgawinl apkssvldig tgtgllalmt
       61 aqryedasif aididlhaid aatinieqsq wqdrislhhg svltadfsqr fdaiicnppy
      121 fnsgeqaqqs qratarhtgs ldhlqlamrc felttenata sfilptpege gfiklaqqcg
      181 wylakrldvk ttnkktasri lfelskdpac eqdlqceslt ihnnngysea fialtkdfyl
      241 km
//
LOCUS       WP_010434863             287 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pseudomonas congelans].
ACCESSION   WP_010434863
VERSION     WP_010434863.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..287
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31684
     Region          65..283
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 msdiikrlrl ltlrgtftli srilpgitgr ylarrfvtpq asgrakaaei lskatdmqtg
       61 sleldgiria tyvwgdpasq pyvllahgws syalrfigwv pllrsmgyav vgfdqpahgl
      121 sagsishmtq fvavqqhvgr hfgkpaavia hslgassivf aeepqwsper filiapflap
      181 adsvlqqfds vgvahkvfkp fegvlhsltg rrfadydasp rlplldrpal iihdrrdret
      241 pwekgarfae lwpgarlftt eglghnrlid hpsviaeamk flkpdhh
//
LOCUS       WP_010434224              67 aa            linear   BCT 01-JAN-2025
DEFINITION  cold shock domain-containing protein [Enterobacter asburiae].
ACCESSION   WP_010434224
VERSION     WP_010434224.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Horn,G., Hofweber,R., Kremer,W. and Kalbitzer,H.R.
  TITLE     Structure and function of bacterial cold shock proteins
  JOURNAL   Cell Mol Life Sci 64 (12), 1457-1470 (2007)
   PUBMED   17437059
  REMARK    Erratum:[Cell Mol Life Sci. 2007 Jun;64(12):1584]
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   3  (residues 1 to 67)
  AUTHORS   Phadtare,S., Alsina,J. and Inouye,M.
  TITLE     Cold-shock response and cold-shock proteins
  JOURNAL   Curr Opin Microbiol 2 (2), 175-180 (1999)
   PUBMED   10322168
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     Protein         1..67
                     /product="cold shock domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7212
     Region          2..64
                     /region_name="CSD"
                     /note="'Cold-shock' DNA-binding domain; pfam00313"
                     /db_xref="CDD:278729"
     Site            order(6,15,26,55)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:239905"
     Site            order(12..18,25..28)
                     /site_type="active"
                     /note="RNA-binding motif [active]"
                     /db_xref="CDD:239905"
ORIGIN      
        1 mglvkwfned kgfgfispld gskdifvhls alngdnfktl fegqkvefai hrgdkgpaaa
       61 nvtlcdk
//
LOCUS       WP_010434879             322 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudomonas congelans].
ACCESSION   WP_010434879
VERSION     WP_010434879.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35545
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,147,162,164,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 melhnlndia afvssvnags ftaaakqlgl trsavgksiv rlearlqvrl lnrttrslsm
       61 tdegqilyer cvgvlqdldd vedalafrrs tpsgrlrisl pvalgrlhvl qhiecclndw
      121 pslsvditfs drlvdlideg fdlamrigpp kedsrlltrt vayqqmitca spkylaehde
      181 pktpedlseh qclhfvsggr llpwnfrvng ssvpvthggr lqmdsaeslr qsaiaglgia
      241 tlpsyvvndd lrsgklvqll agyaeaaepi rviypskrhl spkirlfidk lveawsprpp
      301 weqqpvkgtt sraknpngmk fs
//
LOCUS       WP_010435080             212 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Pseudomonas congelans].
ACCESSION   WP_010435080
VERSION     WP_010435080.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..212
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23155
     Region          14..209
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mstavtasqa eepiiyvidd dlsvrssled llasvglrsm lfgstrefld tprpdapgcl
       61 ildirmpgms gldfqehmar sgislpvifi tghgdipmsv ramkagavef ltkpfrdqdl
      121 ldaiqqglaq drsrrqsasv gaelqrrhas lnpgeqqvme lvvsgllnkq iaarlnvsei
      181 tvkvrrgsvm rkmeadslad lvkfaerlke lh
//
LOCUS       WP_010435240             467 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cytochrome ubiquinol oxidase subunit I
            [Enterobacter].
ACCESSION   WP_010435240
VERSION     WP_010435240.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..467
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51748
     Region          4..442
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mfeldafhla riqfaftvsf hilfpaitig lasylvvleg mwlrtkndvw rslyhfwlki
       61 favnfgmgvv sglvmayqfg tnwsgfsqfa gsitgpllty evltafflea gflgvmlfgw
      121 nkvgpglhff atcmvalgtl mstfwilasn swmhtpqgfs iqngqviped wlaiifnpsf
      181 pyrlihmsia aflssalfvg asgawhllrg ndtpavrkmf smamwmallv apiqavvgdm
      241 hglntlehqp akiaaieghw enppgeatpl llfgvpdmde ertkygleip algslilths
      301 ldkqvpalkd fpkedrpnsl ivfwsfrvmv gmgllmialg alsvwlryrh rlyhsrpfhw
      361 falcmgpagl lallagwvtt evgrqpwvvy gylrtidavs lhstlqmsis llafivvycs
      421 vfgvgyvylv rlikkgpqpv gtltsntsgt parplsaaes vpeeers
//
LOCUS       WP_010435368             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010435368
VERSION     WP_010435368.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22962
     Region          4..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkvrtearre aiidaaasvf lemgyertsm nevtkrmggs katiysyfps keelfiavvn
       61 rlatahlada vselviqddq qidlrtlftr fgermlmvli nddkalavyr mvvaesghsd
      121 igmmfyesgp tqclqtvtsl malamrrgql rdadphiaal qltslltaet dirlyqqapm
      181 plsieeiram veravdtfml gmekr
//
LOCUS       WP_010435371             140 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF805 domain-containing protein [Vibrio].
ACCESSION   WP_010435371
VERSION     WP_010435371.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..140
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15491
     Region          1..140
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 msmkdlllsf kgrigrktyw iwnvfyyvai tgfasgisvl fpaysyillp ifllllvipd
       61 laitakrwhd rnksnywlll nvplvlgrla spmvatttes vspvhmaatv aalvcglwil
      121 iecgllkgte grndygddpv
//
LOCUS       WP_010435389             497 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Pseudomonas congelans].
ACCESSION   WP_010435389
VERSION     WP_010435389.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..497
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54580
     Region          135..456
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mfsisllalv vsgcavtsqp idrsvseqra ksdlqlmyrd qeplngaltl hqamaravky
       61 nlearlkime ealakrqldl asfdmlprma lsagyagrsn vsasssesve tgtqslepst
      121 sqdrsrrvad ltmvwnvldf gvsyisakqq gdqrlivqer rrkvvntivq dvrsaywrav
      181 aaermltqid slmarvekaq ansqkmseqr vgdpvqalgy qrsliqatrq leeqrkalsl
      241 aktelatlin lplgtdlkla tpddysipel kvdmarlete alasrpelre qdyqtrissa
      301 etrkamlrml pglefsaggh ydsnsflvnd kwadlgvkvt wnlfnvlsap aaidaakage
      361 evaaarrqam siavlaqlyv ananynealr qfktsqqlsn idsqivgqlr nryqaaslge
      421 ldliqgelnt lqadlrrdla yadlrnaygq ifasagldpl pselpstkvq aiavalgare
      481 sqweagnisv aattpkp
//
LOCUS       WP_010435491             728 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Pseudomonas].
ACCESSION   WP_010435491
VERSION     WP_010435491.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..728
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80827
     Region          28..712
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 miaslqritd lpwrrelhsw arsdgvtwvy ifkvllaafl tywlalrlel pqphtamitv
       61 fivmqpqsgq vfaksfyrll gtlagsammv llmalfaqnp lpflgslalw vglcsagaar
      121 yrnfraygfv lagytaamvg lpalahpegs fmsavwrvve itlgilcsta isaavlpqss
      181 saamrnalyl rfggfarfva nglrgdisra efetgnvrfv aeaigleglr svtvfedphm
      241 rrrngrlnrl nsefmavttr fnalhqller lrleqadqvl khidpglenl aelldgfaer
      301 altnddaall vtrlescrah fpeqvrslra elerslpsda erldfhtsfe llyrllsell
      361 dyarthasla ehshereqwk gsfvprthwm talaagarat cvvglmsvyw vltawpsgas
      421 mvlasaatva lsstthnprr mslqmaggtl lgalsgfiet fflfphidgf pllclllapv
      481 fvlgaylgsr pqwtgyglgl liffslgsvp dnltiydpyt findyiamvi gmlicaaaga
      541 iilppnsrwm wqrleqavrn qvvfaisapl krlgssfesq trdlmhqayg laigkplvqr
      601 ellrwmfvvl eighaiielr heqailpvhp ayadyqpwri alrvmgralv rlfilpdavn
      661 lqrclsavdq aikrvqeade pfashfdtsv lrrvksylhf irtslldpqs plaaygvart
      721 asgvahaa
//
LOCUS       WP_010435562             529 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Enterobacter mori].
ACCESSION   WP_010435562
VERSION     WP_010435562.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 529)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..529
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58707
     Region          58..525
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mrklllsavv vslalglagc ddaknketnt psaaksdapk eggsliigit sgdplavnpl
       61 yasdrttlti mqalyaplys fnngniewgl aesltpsadn lsytltlkpn lkwqdgqplt
      121 addvvftfnk lldakqhsff rsmftyggkp vevskvdert vkftlpqvsa aftgtlvqiy
      181 pipqhvfage gdlekstknd apvgsgpfkf keyragqyya ltrfddywng karldsvtyr
      241 fakdsnaanl alqngeinlk mvdpqdvnrl kntgkfdfvv ypegrlaymt fnqnvpvmks
      301 kelrqaiaya inkdelaqta ftsldyakpa tsfltpdtly ktddveqykf dlqkakdllk
      361 asgapdnlkl rlayvntnkt qesmalyiqq alkgigvnve lmpldsnams qrsldmnnta
      421 welnlggyim gsepdgyksl fmsneaynya hyknpqfdal wdkgavetda akradiykqi
      481 qqtvandmty ypiaytnatv avdkrfggtl eaepkpvylf qdlskiyqk
//
LOCUS       WP_010435633             270 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterobacter].
ACCESSION   WP_010435633
VERSION     WP_010435633.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..270
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29826
     Region          10..262
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mahnttkpgl vlenlsagyh kkiivddisl aipqrkmtvl vgangcgkst llstlarllq
       61 plggsvvldg kaiheqptka varqlgilpq spllpegltv felvsrgrfp wqnfmrqwsd
      121 edelaveeal rltgtaefah lpveslsggq rqrcwiamal aqqtpyilld epttyldlry
      181 qveilellht ltrqhgrtvv vvlhdlnfav nygdslvflr qgkvegvlhe gdtctpslik
      241 tvfdvdvhms vnpmtgkpff mpfrkvaeqp
//
LOCUS       WP_010436029             648 aa            linear   BCT 01-JAN-2025
DEFINITION  beta-N-acetylhexosaminidase [Vibrio cyclitrophicus].
ACCESSION   WP_010436029
VERSION     WP_010436029.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..648
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73945
     Region          130..644
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mnyridlavl seqknncrfg ltvhnlsdld vkdwslyfaf drfilpesls qgeltqvgsf
       61 csfkpsspvl kannhyylef siqsapfrfy sdglndafiq shhdgetsvl pvaispifla
      121 spyrernqip evnaaeiali pqpnqielql gsfalsseck ievqsqladk alswlqqell
      181 stfelsisne lstefskdes gdilfrsnpt ldeaeykltv taqqimvesg sqsgfthava
      241 sliqlvqqld aknfsvpcck ivdqprfkyr gmmldcarhf hsveqvkrli nqlahykfnv
      301 fhwhltddeg wrieinslpq lteigawrgp dhalepqyth ltdnyggfyt qqqireviey
      361 aeqrsitvip eidipghcra aikslpdmlv eqadttqyks iqhyndnvln pglpgtyqfl
      421 davieevael fpselihmga devppgvwtn spaaqalmke hkyqdskdlq ghlfryaenk
      481 lkqlgkrmvg weeaqhgdkv sketiiyswl seeaavncar qgfdvvlqpa qftyldmtqd
      541 yapeepgvdw aavipleqay nyealaeisd tdpirkrirg iqcalwceiv tnqkrmdymv
      601 fprisalseg cwthknnrnw ldylsrlkgh lplldrlnvd yrnpwkgq
//
LOCUS       WP_010436113             266 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-dependent oxidoreductase [Pseudomonas].
ACCESSION   WP_010436113
VERSION     WP_010436113.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..266
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=29697
     Region          2..220
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mnilivyahp eprslngslk dfavdhlqnn ghqvqvsdly qmgwkaiida ndapgretss
       61 rfdpalesqr vfaagiqppd ieaeqakllw adavifqfpl wwfsmpaimk gwiervyacg
      121 faygvgehsd hhwgdrygeg tlagkramlv vtmggweshy sergvngaln dilfpiqhgi
      181 lfypgfdvla pfpvyragkv dsaifarict dyghrldtlf tleplpfrrq ndgdyeipal
      241 tlradlaagr qgldihlrde depavl
//
LOCUS       WP_010436157             277 aa            linear   BCT 01-JAN-2025
DEFINITION  ion transporter [Pseudomonas congelans].
ACCESSION   WP_010436157
VERSION     WP_010436157.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..277
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30950
     Region          24..237
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mdsslsrrer lhivifeant pagrtfdkav lvaillsllv tiidsiesih rdyamlfawi
       61 ewgftlmfai eyilrlycsp rplkyafsfy glvdllaivp gvlsiyysda qyllivriir
      121 mlrifrvlkl gtylrqanyl laalrgskqk iivflvtvst lvtvfgtlmy viegpehgft
      181 sipkgiywai vtlttvgfgd ivpktplgqm lsslvmitgy siiavptgif taelanamrg
      241 eqlkhdcpvc sknlhehgaa fcsrcgnqlf kktehka
//
LOCUS       WP_010436207             393 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter permease [Enterobacter].
ACCESSION   WP_010436207
VERSION     WP_010436207.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..393
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43291
     Region          4..393
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mshrrlavkg slsfshpavr awlfqiiavv vvvviaiyli hntvtnlnnr gitsgfafld
       61 rsagfgivqh lvdyqegdty grvfivglln tllvsalciv fasvlgfflg larlsenwll
      121 rklstiyiet frnippllqi ffwyfavlrn lpgprqavda fdllflsnrg lyipspqvae
      181 glyafiiaii ialaisvgvf rynrkhqikt gqlrktwpvg aaliiglpsv ahwlfgaalh
      241 wdiphlrgfn fqggmvlipe laaltlalsi ytsafiaeii rsgiqavpyg qheaarslgl
      301 pntvtlrqvi ipqalrviip pltsqylniv knsslaaaig ypdmvslfag tvlnqtgqai
      361 etiaitmsvy liislmisll mnlynrrial ver
//
LOCUS       WP_010436252             483 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CpaF family protein [Vibrio].
ACCESSION   WP_010436252
VERSION     WP_010436252.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..483
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53907
     Region          85..470
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mffkrknvnp efekkveqvs hdsegvnsve hlssvdvsnq tqksnanvek ekaidearkv
       61 lehelsikhf fhkqlletld lgllssleke rakvdlheai vqlmaedgsh alsaegrkrv
      121 ikqiedevfg lgplepllad qtvsdilvng pksvyverrg klektpytfl ddrhlrniid
      181 rivsqvgrri deaspmvdar lidgsrvnai ipplaldgps vsirrfavdr ltmdnligyd
      241 svspqmakfv eaavkgelni lisggtgsgk tttlnifsgf iprdqriiti edsaelqlqq
      301 phvirletrp anlegkgeis qrelvkntlr mrpdrivvge vrgseavdml aamntghdgs
      361 latihantpr dalsrvenmf smagwnistk nlraqiasai hlvvqmerqe dgkrrmvsiq
      421 eingmegevi tmseifrfqr kgidedgnii gyftatgvvp qyhdqlvkrg lelpfelfte
      481 thn
//
LOCUS       WP_010436369             119 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Vibrio cyclitrophicus].
ACCESSION   WP_010436369
VERSION     WP_010436369.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..119
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=13645
     Region          5..98
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mskkvycvaq fqpkkgklne lfevlkslep ntmredgciq ytvtrhinsp faegesfpia
       61 fneiwadnea feahcqrrei qqffqeqcve etglvenfnv aiysdepeny dgpvlkpcc
//
LOCUS       WP_010436430             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YitT family protein [Vibrio].
ACCESSION   WP_010436430
VERSION     WP_010436430.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..200
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21719
     Region          9..>168
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mekhsrkedw vailtgtflv algvfflqsa nlltggttgl alllsqftpv tfgilyfian
       61 cpfyllawkr fgrhfaissa isgalvsvfa dhlylvisld vhneiycava ggllmglgml
      121 ilfrhrsslg gfnvlclfiq drygisvgkt qmaidacilf asflfvspwv iavsvlgtav
      181 lnivlamnhk ptrysvnyas
//
LOCUS       WP_010436626             598 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Pseudomonas].
ACCESSION   WP_010436626
VERSION     WP_010436626.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..598
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=65781
     Region          <1..426
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mqtlkalyes vekqffntlt kklsslfllv lvsallywva lnirsdimlq lrgtqtdpva
       61 lgviqsqldl lsnaillstl ftlvmvsfmv wyfrhlivrp vmsmtralee vasgegdlsr
      121 dlpllthdei rglastcnlf lakqreiiss iqgltvqiav esarslknis dssdsatdqa
      181 rfarevmdqs nmavgsiedv sqqtqgisst taqnlnmard syaellevtg nisqisssln
      241 efgglvsgln ersssiksiv gliqqissqt nllalnaaie aaragesgrg favvadevrt
      301 laqnvskatd disrnidaml qevsstheqt iqishsaret qlvverasgh fesmigdfes
      361 tndkladiaa hiqqfastnt ginervtriy adsqaidqrm qhsatatrdl ssvaeqvqal
      421 lgrfvlghge ldaaitrasq crdilqvrla elhkqgvnlf dqsyklipgt dpkqyttgyt
      481 erfaqicqde cdkltkgtrg gkvtfivdsk gycpvnnswv sqkptgnrev dlpvcrnkrm
      541 fsdpiglraa gnkqrfllqt ylrdtgeimt eidvpfffeg rhwgnlrmgf daalllgk
//
LOCUS       WP_010436652             151 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NfeD family protein [Vibrio].
ACCESSION   WP_010436652
VERSION     WP_010436652.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..151
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=16694
     Region          26..148
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mvelleqvnh whwlafglal laleligtag yflwigisam lvgallgalp igwqmqwlsf
       61 asfslittwl wwrrqlsndk hsdagrelnq rdkqligrtt rllepvqkgs crinlgdssw
      121 saisthdvaa geevvitavd givltisptk e
//
LOCUS       WP_010436884             334 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterobacter].
ACCESSION   WP_010436884
VERSION     WP_010436884.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..334
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35613
     Region          27..331
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mskmmasedi knvpavpgif qrllcwegfl lavtlavfvv nalaspyfln vwnlsdatfn
       61 ftekaiivlp mamliiarei dlsvastial sstvmgfcaa agvdtpllvc vglgvgllcg
      121 lfngilvtrf nlssivitig tmslyrgity illgdkalns ypesfawfgq gyvwgalsfe
      181 falfivlaav fafvlhrtnf grrtyaignn ptgawysgin vkrhnlilfa lvglmsglas
      241 vlltsrlgst rptiamgwel avvtmavlgg vnilggsgsm vgviiaaflm glvtfglsll
      301 nvpgivmsvi igamlivvis lpiitrrvmq rrrn
//
LOCUS       WP_010436914             484 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TrkH family potassium uptake protein [Pseudomonas].
ACCESSION   WP_010436914
VERSION     WP_010436914.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..484
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52806
     Region          69..483
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mslptlriig fiigiflitl avamivpmat lviydrfedl reflwasait fiaglalvvp
       61 grpdnvqlrp rdmymltvss wivvcifaal pflltqhisy tdsffesmsg itatgstvls
      121 hldsmspgil iwrsmlhwlg gigfigmava ilpllriggm rlfqtessdr sekvmprshm
      181 vakfivlayv gftalgslaf waagmslfda inhamsaist ggfstsdqsl akwpqpavhw
      241 vaivvmilgs lpftlyvatl rgnrkallkd eqvqgligll litwlvmtvw yanttdlpwt
      301 ealrhvalnv tsvvtttgfa lgdyslwgnf slmlffylgf iggcsgstag gvkifrfqva
      361 yillktnlnq lihpravmkq kynghrldde ivrsiltfsf fftiticlia lmlsllgldw
      421 mtaltgaast vsgvgpglge vigpagnfst lpdaakwils ggmllgrlei itvlvlcvpa
      481 fwrh
//
LOCUS       WP_010436707             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Enterobacter].
ACCESSION   WP_010436707
VERSION     WP_010436707.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..321
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36315
     Region          10..307
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          <187..271
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
ORIGIN      
        1 mmnslqlkpr elkiisviaa thsigdaaal lgmaqanvsk ylsdfetrvg lkvferttrq
       61 laltqfgeal lpyvnatldk nsqlinfiad ykhekrgkvt iyaptgivty larhvihkie
      121 eigdirlslk tynldrnefs dgvtfpddcd ilityaqpkd enlvasvltk ysvtafaske
      181 yltkhpikgp edlinhscil idsmlvddan iwrfrvhgse eaqdykvtgn yicdntqtal
      241 elarnnlgiv fapkeslkke lthgmlvpcf phqeewwldl taifrkreyq pwrvqyvldg
      301 vlnclrqqin qavqgrpdlg t
//
LOCUS       WP_010436930             139 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF805 domain-containing protein [Enterobacter].
ACCESSION   WP_010436930
VERSION     WP_010436930.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..139
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15829
     Region          1..135
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mtiqqwlfsf kgrigrrdfw vwmvtwvvam lllffvayna wlstqtaafa lvcllwptaa
       61 vvvkrlhdrg rsgawaflii lawmlvagnw svlpsilpwv vgrmvpsiif vmmvvdlgaf
      121 igtqsenkyg kdtlevkyr
//
LOCUS       WP_010437015             276 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010437015
VERSION     WP_010437015.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..276
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30943
     Region          92..273
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mnrqanakde vkphiylelg klvssvgddm flnnmhqfin tslavsriel sewtvddnqt
       61 vvtdvrllgy agtelnpqmq tvcptrarhh ndhplvrrvl evedgllihl narmknqkgn
      121 dvlgtshqcs misrkanrrc vislhrpqad kdyslqelsf lkylsetllp lserharmhr
      181 qsgrksaggt lphgsvpieh kylqrefner lracdvslsa rekeaclefl aggtvpeiae
      241 klcvksssie tylkrsaakl gisgrhglak wmigae
//
LOCUS       WP_010437022             201 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Pseudomonas congelans].
ACCESSION   WP_010437022
VERSION     WP_010437022.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..201
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21745
     Region          7..192
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mamyyvaiam ltvllvpgpt nslllqsgis rglgiyslkl vaaewaayli qitawglsid
       61 aliehygwvv vaikvlavlf lfyislklwf sihqepdgkp spisipalff atlnnpkglf
      121 fatliapsgt flhldsylsf maifslvvip vgvawtalga ffgrklpsri sgnrinrfvs
      181 vviglfavmt lynvaataif a
//
LOCUS       WP_010437032             284 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010437032
VERSION     WP_010437032.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..284
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30896
     Region          <192..267
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mnmqqlfphl gkvisgigsr qfarllhemi taslpvdath viqglgrsts evagphavga
       61 fggnlhqvln pgidsrrlep vmlsptelad trvdrsirfe spaynaqekt gdlhphaslp
      121 qvhlaypgkg qyvlsvyrsp sakaftsqer arlkdlswvv lpivkqhiat vtptlvstnp
      181 slvakslknk dameglrqrf lgrleasals lssretevcv gllagltvpq laerldlkvs
      241 tvesyfkraa vkmgiagrsa llrwlhaeqr vqhpipvemf qaav
//
LOCUS       WP_010437048             525 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkaline phosphatase [Vibrio].
ACCESSION   WP_010437048
VERSION     WP_010437048.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..525
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57760
     Region          1..362
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mkhfmkpivt avvtstlsfn vlsaeiknvi lmigdgmgpq qvglletyan qapnsiykgn
       61 ktaiyqlaqe gvigsslthp edaivvdsac satmlatgiy sgsevigids qgnhvetvle
      121 kakkagkatg lvsdtrltha tpasfaahqp hrslenqias dmlatgadvm lsgglrhwip
      181 kstndkgety kqlekltqgd vylkskrkdd rnllteaekd gyqlvfnrnm lddakgdkll
      241 glfaysgmdd giaysnkkks gertqpslke mtkkalnils kdedgfflmv eggqidwagh
      301 sndagtmlhe llkfdeaiqt vyewakdred tivivtadhe tgsfgfsyss ndlpkpqkrs
      361 geafadrdya pnfnfgafdi ldglynqkqs yygmisefqk ldkaqqtpek laeivnknse
      421 fpitaeqakn vlaskpnpyr laqhkylsae evpaindfda ffpyndrgnl lareqatgqn
      481 ivwgtgthth tpvnvfawgp aekilpvski mhhselgeyi kqqvn
//
LOCUS       WP_010437051             193 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Ruegeria conchae].
ACCESSION   WP_010437051
VERSION     WP_010437051.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..193
                     /product="YceI family protein"
                     /calculated_mol_wt=20517
     Region          4..191
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mtfksmiaaa altvvvtptf aqtyktdqgh tevrfgwsha gvsnqhgeft kvdgvldlna
       61 ddveastlnv tidtnslasg fgplddhlks adffevetyp eitfisteik rtgdstadvt
      121 gdltihgvtk pvtlkatlth qgehplgsai eyyagdwvaf satgeidhte fgvgpfstgp
      181 itimidtemk adg
//
LOCUS       WP_010437079             141 aa            linear   BCT 01-JAN-2025
DEFINITION  ester cyclase [Ruegeria conchae].
ACCESSION   WP_010437079
VERSION     WP_010437079.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..141
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16003
     Region          7..141
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mkeaervvrq fheswgmrdp drgaeviaed cqfedvarde kqlgklayke dyerwrtafp
       61 dgecivdnvi vsdcgewaiv efhnngthtg vlhsslgdfe ptgkryevry csvmrvvggm
      121 vvegrdyyds atiarhlglv k
//
LOCUS       WP_010437191             221 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter small permease [Ruegeria conchae].
ACCESSION   WP_010437191
VERSION     WP_010437191.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..221
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24797
     Region          1..200
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtnnhslmdr ieevliafil glmtaltfan vvaryvfnsn ilwalemtvf lfawlvllga
       61 syavkkhahl gvdlmvnmvh gnarkrlala aaavcvafsf lmlkgswdyw anfanlpate
      121 grwfplgfeq dyrekgwyet ndipmpgila wmagafnege ayekiprflp yivlpismal
      181 lflrfvqatf silngkadrl vasheveeel aeieaqnaea k
//
LOCUS       WP_010437239             223 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Ruegeria].
ACCESSION   WP_010437239
VERSION     WP_010437239.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria
  ORGANISM  Ruegeria
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Ruegeria"
                     /db_xref="taxon:97050"
     Protein         1..223
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24823
     Region          1..213
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 malerpkslr elalehlrns iidgslkmgq vlserkisee lgvskspvre alaqlrdegl
       61 vsiepqkgar vfslsepevt qicdfrqaie taafelallr npegladdmq rvvkdmeker
      121 rrgnekgyls ldttfhqlif ehagndylta sytryigkia alrthlaklp qhtelsfdeh
      181 skiaiavreg dmakiksllt ahidrtrqay ksaaivlega tas
//
LOCUS       WP_010437205             129 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Pseudomonas].
ACCESSION   WP_010437205
VERSION     WP_010437205.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..129
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=13802
     Region          2..129
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mdipedlths ayfkmlgcel rrldegvaev alpleahlrn rgnvmhggai fslvdiamgl
       61 acssvhgfdq rsvtieckin yvrgvsegev lciakvlhag rrtlvveaev vqgdklvaka
      121 qgtfaviqa
//
LOCUS       WP_010437263             427 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Ruegeria].
ACCESSION   WP_010437263
VERSION     WP_010437263.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria
  ORGANISM  Ruegeria
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Ruegeria"
                     /db_xref="taxon:97050"
     Protein         1..427
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44756
     Region          18..426
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mlattlfltl falllfsvpi giclglatmi vmvfvdgtpp mvllarsvvt gadsfpliav
       61 plfilagdlm qhggmsrrlv gfanalighi rgglayvnvl acvffaaisg sspatvaaig
      121 snmipemekv gytrkfsgal tassgmigvm ippsipfiiy gvtaevsigk lflagvvpgi
      181 lfalmfmlva rvllrkdevv qqstttfsgp gvwqsfrssi wallvpviil ggiysgiftp
      241 teagavavvy aafigifvyg ditlkdlpev lagsaktsgt ililvimata fgrlitlari
      301 ptelattits lsdnpiiill linllllvig mfmetissii imtpillpva talgvdpivf
      361 gviltvnlai gfctpplgvn lfvassiskv sieslsrail pffvgmlill mfityvpais
      421 lalpslw
//
LOCUS       WP_010437305             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Vibrio].
ACCESSION   WP_010437305
VERSION     WP_010437305.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..255
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28549
     Region          2..253
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mfvdshchld kldyqdlhts vedvvnkaka anveqllsvg vtldsfenml dmiapfdnvk
       61 ascgvhpldv esdfclermr eyasnpkvva igetgldyhy qpetaelqql rfkqhvelav
      121 elnkpliiht rnaredtlai lrdggaekcg gvihcftedq sfaeaamelg fyisisgivt
      181 fkqatelkev vknlpldrll ietdspylap ipyrgkqnqp ayvvevaayi aqlkglsmke
      241 vaeqttrnyq klflr
//
LOCUS       WP_010437339             456 aa            linear   BCT 01-JAN-2025
DEFINITION  multicopper oxidase family protein [Ruegeria conchae].
ACCESSION   WP_010437339
VERSION     WP_010437339.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..456
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=49773
     Region          14..456
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mklnrrqfva gtsaliavpt igraatapri iearsglarv apdsypetei wgydggvpgp
       61 eirarqgetv rrtllnslpq ptaihwhglr vpnnmdgvpg ltqeavqtgg efqydlplkd
      121 agtfwyhshn qsteqvargl ygafiveetd ppdtdhditi llddwrlgqd aqivndfgam
      181 hdwthagrmg nyvhahispm tevltnqrlr irmvnvatdr imyvsvggan gklvaydgmp
      241 vrqpedfetl vfgpaqradl ivdvtaesne avqitlherd esfviaeipv sgsgtsanrg
      301 viealppnpv pfledvsdal tvplvmegga mgglrqgtyn gqvmstnelv qegqiwtfng
      361 vaglpenpla avsrgdivri qmqndtvfph amhlhgthfq evlpngslgp lrdtilvdri
      421 etreiafvad npgdwlfhch mlshqaagmk twlsva
//
LOCUS       WP_010437341             157 aa            linear   BCT 01-JAN-2025
DEFINITION  c-type cytochrome [Ruegeria conchae].
ACCESSION   WP_010437341
VERSION     WP_010437341.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 157)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 157)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..157
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16945
     Region          <22..139
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 mnrsaakwls laavviivav igwglsgraq nsasadsarg avlyaencas chganlegqp
       61 dwqtpdpegv lrapphdrtg htwhhgdkll fdytkfggdq tlkqmgvadv ksgmpgfgdt
      121 lsdqdigdil afikeswpdw erklqeqrte aeqtegn
//
LOCUS       WP_010437345              65 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Ruegeria
            conchae].
ACCESSION   WP_010437345
VERSION     WP_010437345.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 65)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..65
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6929
     Region          1..65
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mttlnipems cghcksaiek avatvdssah ldfdmenrrv rvlstnpldh ilaalksegy
       61 eatva
//
LOCUS       WP_010437356             207 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Ruegeria conchae].
ACCESSION   WP_010437356
VERSION     WP_010437356.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..207
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21836
     Region          6..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 msnavrihhf aksghahral vfaklagiah davpvdlaag ahkspeflam npngqvpvle
       61 dgevvvsdsn ailfylarty apdwmptdpv geanvqrwlt laageiafgt caarlitvfg
      121 apldpefaaa taekamqkle hgltgsdwlv garptiadva sysytahape gnvslepypn
      181 irawlarfea lpgfepmpat avglvae
//
LOCUS       WP_010437425             437 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Ruegeria conchae].
ACCESSION   WP_010437425
VERSION     WP_010437425.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..437
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46665
     Region          2..437
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtlsllglga vlilvflrmp iaiamglvgf lgfvelrgfr aaismvgrli idtaqdygls
       61 vvplfilmgl fvnkgglske lyrasyaflg hmrgglamat ivacagfsai cgsslataat
      121 mskvampemr kyrysdslat asiaaggtlg ilippsvilv iyglltetsi gklfiagvip
      181 gllgvllylv avrfsvtrdp dagpagewvs wrerllslrd iwavlllffl vigglygvld
      241 vwpffitfsp teaagmgaag aflialsrra lsfsstmevl ietvqtaatl favligawif
      301 snfvnlaglp ealsnfvlsq glsptlvivl illvyvllgc vfeslsmlll tvpiffpvvt
      361 slgfdpvwfg ivvvvvteis litppvglnv fvlkgvvkdv ptsiifrgvt pfwlvdilrl
      421 liivifpwlv lflpnsm
//
LOCUS       WP_010437378             434 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Ruegeria].
ACCESSION   WP_010437378
VERSION     WP_010437378.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria
  ORGANISM  Ruegeria
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Ruegeria"
                     /db_xref="taxon:97050"
     Protein         1..434
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46077
     Region          6..433
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtpieiglis vvaivfliya gvyipialgv vsfvsiwlmr dnftlalnll kvavgdsame
       61 ysfatiplft fmglivskag lgrdiyevmt mrfrkvkggi gmatvganav faavtgssia
      121 sasvftkvsv pqmmaqaynp rfavgvvags svlgmiipps amliiysfva eqsvgdmfla
      181 gvipgimlai ayvgaiwlmg rftpafvggr vvedtewmsg reiasktlpt lfiitvvlgg
      241 iytgwltave agaagalval viavvrksmt prafwdalle tghitaailf litaasiysr
      301 mlglaglpnq lqdllagnsa sfwsimllyv llmlflgtll dtasiilivv plflpmaeal
      361 dmsliwfgii tvvgaeigll tpplgiscfv ikstinddri slkdvfmgal pfafvmlivl
      421 filiefpils lali
//
LOCUS       WP_010437450             217 aa            linear   BCT 01-JAN-2025
DEFINITION  urease accessory protein UreF [Ruegeria conchae].
ACCESSION   WP_010437450
VERSION     WP_010437450.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..217
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23545
     Region          4..217
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 matptdadil tltqwlspay pvggfayshg leaaidrgtv ansqeteawi sdvlengsgw
       61 ndalfvvaaf naldkdelin vdvtarafca tserlietdl lgqafgnvtk gvweldlgqf
      121 typvsigraa rlqnlplllt tkmflqafas nlvacatrlv plgqtdaqrl irqltplcsq
      181 iaeraqkasl delssttfla diasmkhetq ysrifrt
//
LOCUS       WP_010437481             603 aa            linear   BCT 01-JAN-2025
DEFINITION  BCCT family transporter [Ruegeria conchae].
ACCESSION   WP_010437481
VERSION     WP_010437481.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..603
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=64411
     Region          16..601
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 maleepftdl kirtqrtgfy kgyslpialv sklsvsllvl walvwplsan dtlrswksgv
       61 lsefnafynl svglfvlflf lialipstgr mklgledekp efsnfswfsm mfgaglgvgl
      121 mvyataeplg lwetnaltvs gevtpkseda iegayrytfl htgfhawaiy vvtglslayy
      181 aftrgmplti rtaltpllge ysngiaghvi dilgvvatil gvavtigygv sqlvdgafli
      241 tgakwlveke atkvipstag liaasivvmm mstlsavsgv grgvkylsni nllfslvlla
      301 vfivfgsfaf aaktyatalv dyiknfvpls fqafrpvsev dfasvlpaea apfvgelfag
      361 atdpwgtkat flegltsdta glsdatktav ydagtrgrlf gwqagwttfy wawwiafspf
      421 vglflarisr grtvrefilg aviapslvcf awmallggta idlelngnan gsildastta
      481 tlfatlgemv sgnfltivsi mcvlltmtfl vtsadsgilv mntimsggse dtgllhrilw
      541 gvlltlvigt lliaggggle altnsmiiga lpfsvvlllm cislakamin dlrrlnhetr
      601 tgs
//
LOCUS       WP_010437486             452 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Ruegeria conchae].
ACCESSION   WP_010437486
VERSION     WP_010437486.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..452
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47807
     Region          6..448
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtdgtmvtli slavtflfml gvpvflvigy wvigcsfvlg ltldnmgael lnvfnkgfal
       61 lamplfiltg dlinksgiar rlsdfayacl gwirgglama slgacglfaa isgsnsatta
      121 tigsmlhpem vkggyderfs aataaaggtv giiippsiif ivygflmnlp iselfvagil
      181 pgalmvfgmq facwiicrln gwghliplql nrvlktafga wlgffaiglv lwgiytgkfs
      241 pteaagvtvg fcviaglvsy pinrimgarn dippteksfa emfvvegfti peipsivirs
      301 aqitgilapl iaisvvmqqi lsllgaqqti gdfvtsmggy yavlftsmvi vffsgmvles
      361 lpvtiilapi lapiaasvgi dpihfsvifl vgasigfitp pyglnlyvas gvtgvpyfrl
      421 lrytvpylva llsvwilvsl vpdlalillp ns
//
LOCUS       WP_010437528             431 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Pseudomonas].
ACCESSION   WP_010437528
VERSION     WP_010437528.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..431
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44868
     Region          1..429
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mlerlfqlka hntnvrteil agvttflama yilfvnpsil getgmdkgav fvatclaaai
       61 gstvmglian ypialapgmg lnafftytvv lhmghswqva lgavfisavm ffilsifrir
      121 ewiinsiplp lrsaiaagig lflalialhn agivvsnpat mvgmgdlkqp apilatlgff
      181 livaldhlkv rgavligila vtlvsialgf spfggvvsmp pslaptfmql dimgaldvgl
      241 vsiifaflfv difdnsgtli gvakraglmg kdghmpkmgr aliadstaam agsllgtstt
      301 tsyiesaagv saggrtglta vvvavlflla lffaplagsv pafatapall fvavlmasgm
      361 aeidwdditv aapvvitala mpftysiang iafgfiswta ikllsgrwre lnsalvilsi
      421 lfviklgwfn a
//
LOCUS       WP_010437649             369 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas congelans].
ACCESSION   WP_010437649
VERSION     WP_010437649.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..369
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40150
     Region          21..368
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mtesvqpmks arqpllarry tlelrqqtgw llqaliiala llvglaictv ililagvpad
       61 ellnefvvqt vfdaqnfkav lfqaspmimv glagcmafra rfwnlglegq miwgaigata
      121 islfqvgpea lrlplmmaaa vvcgllwslg pvllklkwqv neiistlmln yiaanfllhl
      181 vygswkdprd nfpyspafqs ferlpdlfag ynaaiplall vtgltlwfvg vsraglylrf
      241 vdanpkvaga vgvpvrkmii gtvllsgala glagfvvtsg qegrltqsfy qgygfsgili
      301 aflarnnpva atvvalliam lfvagrnlqv fyqipfsmvq liqailvicv assdffirhr
      361 lrriqager
//
LOCUS       WP_010437650             329 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Ruegeria conchae].
ACCESSION   WP_010437650
VERSION     WP_010437650.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..329
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37904
     Region          1..328
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mgllvdgvwh dtwydtkstg gafkrsaaqf rnwitangap gpsgrgcfea esgryhlyvs
       61 hacpwahrtl ifrelkglre hisvsvvhpd mldkgwtfet ddhgatgdkl fghdfahqiy
      121 tradpnysgr vtvpilwdkv ektivsness eiirmfnsaf ngitgntddy wpeamrdeie
      181 evnariysdv nngvykcgfa tsqeaydaai gplfdtldwl edrlsrnryl mgdrvteadw
      241 rlfttlirfd pvyhlhfkcn krrlvdypnl waftrelyqw pcvaetvnmn hivrhyhysh
      301 dsinphritp vnpeldysep hgrdqrpaa
//
LOCUS       WP_010437654             232 aa            linear   BCT 01-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Ruegeria conchae].
ACCESSION   WP_010437654
VERSION     WP_010437654.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25162
     Region          24..221
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mpnqlfalpd ipsipvqgeq atypigrifc vgrnyaahaa emghevdrqa pfyftksapn
       61 avltgahvay pagtenyhhe melavaigkp vfqataaqah aaifgygcal dmtrrdlqir
      121 ernkqrpwdl gkdvesgavf apltradhws psddkriyls vngqvkqdat lselvwkide
      181 lichlsgfyh lrpgdliltg tpagvgpvva gdrieggidg lfpvhltlta hd
//
LOCUS       WP_010437709             254 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Ruegeria conchae].
ACCESSION   WP_010437709
VERSION     WP_010437709.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..254
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26496
     Region          16..243
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mdlfslispq emylalivaf vagwvkgmvg fampmvlisg lsmmlppefa laglilptlv
       61 tngvqalrdg vvaaavsvrk frvflavgli cllasaqlin iltpqdyllv lgvpitffal
      121 iqilglrltl kapsvgveav vgavagavgg isgvwgpptv ayltalntpk kdqmrvqgvi
      181 yglgavalvv ahlgsgvlrg etalfsamlv lpalvgmrgg lflqdridqt qfrkltllvl
      241 liaglnllrr gllg
//
LOCUS       WP_010437721              89 aa            linear   BCT 01-JAN-2025
DEFINITION  HPr family phosphocarrier protein [Ruegeria conchae].
ACCESSION   WP_010437721
VERSION     WP_010437721.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..89
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=9151
     Region          1..88
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 mttkslkiin ekglharasa klvevvegfd araevsrdgl sasgdsimgl lmlaasrgtt
       61 idvetsgpda ealaealetl vndkfgegf
//
LOCUS       WP_010437788             457 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Ruegeria conchae].
ACCESSION   WP_010437788
VERSION     WP_010437788.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..457
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49784
     Region          15..431
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mdgnlnaltt vftefyywvt vvfmflihvg fcmyevgasr arnhmhtlmk nimiiplvtv
       61 tffffgwwiy wafpnfpfwg gldteagaan lpwadtmatn lgdritgvfw aafllfswta
      121 asivsgsvie rirssalwvh avmigsvwwi idaawgwhyg gwmvrvlgyh dayasgviha
      181 iaggyalgvi mvlgprlgkf akdgtprdip phnpwlltig ifliytgfwg fyaacnvpai
      241 speaidgqit gvtwtatniy lapttlsait fnflmslsgg lmaayviskg dafwtfsggl
      301 agiitasagn dlyhpvqami iaaigvvivy klhywverrf klddavgava vhgyagfvgl
      361 visgfvlwgv psspyegyat inpvgqitga vimffvlgfl pgwilakiqs aagvlripee
      421 velqgldyae hhayedakaa iiaadkeela argvpae
//
LOCUS       WP_010437795             320 aa            linear   BCT 01-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Ruegeria conchae].
ACCESSION   WP_010437795
VERSION     WP_010437795.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..320
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35762
     Region          12..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(56..57,59,73..75,81,83..84,125,224)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(56,58..59)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(81,84,87,94)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(117,121..124,126)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(122..123,146..148,197..198)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          235..319
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msgaekiqvk vteitplnel vtrfrfervd grqlptfsgg ahtvvemqdg gitrlnpysl
       61 msdpfdqssy tisvrrddqg rggslfmhrq vklgdemtis ypvnlfsldl rarkhlflag
      121 gigitpflaq ikqlellhgh welhyacrnq alasyadqlt drhpnathly yddqsqvidl
      181 enllsgqplg thvyvcgpkg midwvrntaa aegwpedcvh yeeflapqpg kpfevrlass
      241 ekvihvgene slleaiereg vdapylcrgg acgqcetvvl dhdgnfvhrd hwltdeekaa
      301 gkkimpcvsr fegkslvldr
//
LOCUS       WP_010437839             393 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Ruegeria
            conchae].
ACCESSION   WP_010437839
VERSION     WP_010437839.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..393
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=43167
     Region          17..386
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 msdpehrnds aaepspravd dgigvateef rismpigiga vlaalaslat cysgilltyl
       61 vgyealsinp hvqavlmwvf allavsflwr drkrhakelp lvlggiaavi livtlyfgyd
      121 ervealayvl lviaallnqn fildalnhtv rnqtheieal ndrltekvkr qegeidrlar
      181 lkqflapqva elvveensde llkthrryia clfcdirnft aiseaieped vitllqhfhd
      241 evghlvaqhk gtigyragdg lmvffndpvp cdqpvlqavr lakeiseafe girapwqklg
      301 hamglgigis sgyatlglig fhgradytai ggvvntasrl cdfasdgqil lnqralldie
      361 qhveteelge relkgigglv qifrvislfd qak
//
LOCUS       WP_010437942             154 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Vibrio].
ACCESSION   WP_010437942
VERSION     WP_010437942.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..154
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=17142
     Region          3..146
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mfllknieei lasiaisitv lvviinvvlr ygfgfvvpws eelsvicfiw avylgisscy
       61 khklhmgvdv vvamlpekak tpfrlcvslf llalnilmav lsyqylmlsn kvtpvmgmsy
      121 faingvllvc fslmaihtvr fivsdiaslk rsfk
//
LOCUS       WP_010437952             245 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Vibrio cyclitrophicus].
ACCESSION   WP_010437952
VERSION     WP_010437952.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..245
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26998
     Region          19..235
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mrtlttlsll aallpfsvis genvtyqvdg vdyegywsea sdqaplvlli hdwdgltdye
       61 kkrsemlnel gynvfaidlf gkdirptevk dkkqhtgely qdrekmrtll nagameaekl
      121 ggnldnnvmm gycfggaavl eaaragissk ayvtfhggls tpkgqdysqt kapvvvfhgt
      181 adamismedf gnlaaqlett kvshemitys gaphaftvfg snnyqqeadq kswerfthvl
      241 etttr
//
LOCUS       WP_010437959             227 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010437959
VERSION     WP_010437959.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..227
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26093
     Region          24..174
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstkpilhrd dpeaepltgn ikvtrddwln vamdvlisdg veqvkvmnla ermavsrssf
       61 ywyfksrqel ldallarwqa tntaaliaqs elpaetitaa vcnvqrcvvn selfdtaldf
      121 avrdwarrsg kvrrmldqsd arrlaalrtm firfnydete aetrarvlyy mqigydlaql
      181 nepmatrlsm vphylyvftg veprpeevse fsdyakrlwe rtghept
//
LOCUS       WP_010438005             294 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Ruegeria conchae].
ACCESSION   WP_010438005
VERSION     WP_010438005.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..294
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32080
     Region          <58..287
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mgdtdgssra aqgahsqnsn tdsdekggll srifdafspp gdeasqvnga kvtdsqprgm
       61 inlrrmrved vaiptaeiis vpsttpkdel aqifrdsgls ripvyegtld tplgfvhlkd
      121 falthgfngn ssefdltsml rtllfvppsm pigvlltkmq terrhmalvi deyggvdgll
      181 tiedlieqvv geiadehdad edqlwiqekp gcyvvqarvp ledfeaeigr sltshedvde
      241 eeidtlgglv fmlsgrvpar gevvchpegp efevldadpr rikrlrvmlp diaa
//
LOCUS       WP_010438076             304 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010438076
VERSION     WP_010438076.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33601
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 msyldnirtf vrvydlgsms aagrdmrisp avtsarisql edhlgvrlfq rttrnltpte
       61 qgrafypgav avldavdeae aqvthlteap rgslfvaapl gvgrrllaph vpdflseype
      121 idvrlrltdr svdlttegld laffigqped stlrirkiad cqrvlcaapd yvsrcgmpes
      181 gtdlisgkhe clnlrfpgaa efqwmletpd gpkrfavsgr yecddgdvlt dwalsgqgia
      241 mkpvfevseh lkagrlipva tqtppvpvqm aclythrrhq dpkarlfmdf midrvgkvvr
      301 saei
//
LOCUS       WP_010438085             329 aa            linear   BCT 01-JAN-2025
DEFINITION  type I glyceraldehyde-3-phosphate dehydrogenase [Ruegeria conchae].
ACCESSION   WP_010438085
VERSION     WP_010438085.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Sirover,M.A.
  TITLE     Structural analysis of glyceraldehyde-3-phosphate dehydrogenase
            functional diversity
  JOURNAL   Int J Biochem Cell Biol 57, 20-26 (2014)
   PUBMED   25286305
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Nicholls,C., Li,H. and Liu,J.P.
  TITLE     GAPDH: a common enzyme with uncommon functions
  JOURNAL   Clin Exp Pharmacol Physiol 39 (8), 674-679 (2012)
   PUBMED   21895736
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414602
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..329
                     /product="type I glyceraldehyde-3-phosphate dehydrogenase"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0016620 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, NAD or NADP as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /GO_process="GO:0006006 - glucose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=34250
     Region          1..329
                     /region_name="GapA"
                     /note="Glyceraldehyde-3-phosphate
                     dehydrogenase/erythrose-4-phosphate dehydrogenase
                     [Carbohydrate transport and metabolism]; COG0057"
                     /db_xref="CDD:439827"
ORIGIN      
        1 mklaingfgr igrtilrqvl gpsqhsdiel vlindiaple tcaylfkyds tfgtypgsva
       61 aeggalnidg rivpmshsad lakvdlsgvd vmldctgiar tsdvasrglt agagkvlisg
      121 pspaaeitvv lganedhlgn arivsnasct tnglaplvkl ideigglvsg hmttihcytn
      181 sqpmvdaprg dlarsragal smvpttssat hlidvvlpnl agrisgaavr vptasvsavd
      241 lvatlergks adqfdqafrn avaasavlgw tdlplvssdl rsrpeslvla gpetrmigen
      301 qirvfgwydn ewgfsarmld varlmaeag
//
LOCUS       WP_010438112             152 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase [Ruegeria
            conchae].
ACCESSION   WP_010438112
VERSION     WP_010438112.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..152
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16234
     Region          6..149
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mpmiavetqf gclgveeidg aitrlvwngr degpatpvlq eaaaqlrayd egrlqqfdlp
       61 ywikgsefqr rvcdamyaip fgdtrtygel adelgysaqa vgrgcggnpi piiipchrvl
      121 gadgkmvgfs ghggvetkva llrhegaasl li
//
LOCUS       WP_010438118             306 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine recombinase XerC [Ruegeria conchae].
ACCESSION   WP_010438118
VERSION     WP_010438118.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..306
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=33222
     Region          5..306
                     /region_name="xerC"
                     /note="site-specific tyrosine recombinase XerC; Reviewed;
                     PRK00236"
                     /db_xref="CDD:234698"
     Site            order(147,161..162,231,233,252,287)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271179"
     Site            order(161,252,255,278,287)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 mslispacrd alqhwldslg alagrsentl eayrgdvtef lsfmtlhhse rqglaaleri
       61 tvsdmrawma dqrnsdvgar slarklsavk nfyrwlaere gfeptavlst rapkftkklp
      121 rplaedaara mietvelqss sdwvaardva vvtllygcgl risealsltg sdaplpdtlr
      181 isgkggkeri vpvlpaaraa vdrylrlcph pqtpdaplfr gvrsgplnpg iiqavvakar
      241 mqlglpatat phamrhsfat hllsaggdlr aiqellghvs lsttqtytav dtarlmevyn
      301 rthpka
//
LOCUS       WP_010438175             532 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BCCT family transporter [Vibrio].
ACCESSION   WP_010438175
VERSION     WP_010438175.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..532
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57236
     Region          19..506
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mepvkdrysi entdytvgqd nvqkwgfdvh npvfgisaga iiifllallv aepetakaal
       61 dgikwkiign fdgffmwaan ifvifcfali vspygkirig gndakaehsn lswmsmlfaa
      121 gmgiglmfwg vaepvayftg wyqtplgvea yspeaaklal gatiynwglh gwsiyavval
      181 alafftfnkg lplsirsify pilgdrtwgw fghivdivav latlfglats lglgaqqats
      241 ginhvfgtdg gigmqlvvia vvtflatmsv vrginggvkv lsnvnmlval gllifvtiag
      301 glagikaipt almgyienfi plsnphgrdd etwmqgwtvf ywawwmswsp fvgmfiaris
      361 kgrtirefiv avlfipttvi iiwmaifggi aidqvankvg eigvnglqdi tlslfhtyda
      421 lpmssvlsvv siglimvffi tssdsgslvi dsitsggkvd apvpqrvfwa lmggaiaavl
      481 lwvggtesiq alqagtvsma lpfafilllm clslllglrt enklvqqqna ls
//
LOCUS       WP_010438189             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: elongation factor Tu [Pseudomonas].
ACCESSION   WP_010438189
VERSION     WP_010438189.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..397
                     /gene="tuf"
     Protein         1..397
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43298
     Region          1..397
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makekfdrsl phvnvgtigh vdhgkttlta altrvcsevf gsarvefdki dsapeekarg
       61 itintahvey nslirhyahv dcpghadyvk nmitgaaqmd gailvcsaad gpmpqtrehi
      121 llsrqvgvpy ivvflnkadl vddaellelv emevrdllst ydfpgddtpi iigsarmale
      181 gkddnemgtt avkklvetld syipqperav dkpflmpied vfsisgrgtv vtgrvergiv
      241 kvqdpleivg lrdttvttct gvemfrklld egragencgv llrgtkrddv ergqvlvkpg
      301 tvkphtqfea eiyvlskeeg grhtpffkgy rpqfyfrttd vtgscelpeg vemvmpgdnv
      361 kvsvtlikpi amedglrfai reggrtvgag vvakiia
//
LOCUS       WP_010438291             353 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ruegeria conchae].
ACCESSION   WP_010438291
VERSION     WP_010438291.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37985
     Region          10..353
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mslqskaapv rfesvtkmfg kdvvavdnin lhveagklvt llgpsgcgkt ttlrmiagle
       61 matsgkitig drdvtklpat drdvsmvfqs yalfphmsvl envmygltfs gfakdearsr
      121 aldglelvgl kgfdgrlpse lsggqqqrva varalvlepq vllfdeplsn ldaklrrqvr
      181 ediraiqqdl gltvvyvthd qeealavsde ivvmrnaaia qigtprqlyd apndrfvadf
      241 igeanllacq iisvegdmat ieiegyrhtl ssrdmpqgpa tvairpsrlv igaeqgiaat
      301 vakatyvgvr meytltgafg qvfavhddvd aplepgaeir mgfaekgpvl lpe
//
LOCUS       WP_010438304             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator [Vibrio].
ACCESSION   WP_010438304
VERSION     WP_010438304.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21848
     Region          4..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mitkrqkild aalllfsqqg legtstgqia ktagvakatl fhhfenksll idelfrdlkl
       61 elfstlqpht giaeqdryqa fkfmwitgie walenpvamk fftnvhfdpt tqtrevivsq
      121 mfasldeiil kgqedgelms lnidlvrhfi hshflicanw lieqsesppe ktskyindsf
      181 dmcwravggq iq
//
LOCUS       WP_010438372             641 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LamG domain-containing protein [Vibrio].
ACCESSION   WP_010438372
VERSION     WP_010438372.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Hohenester,E.
  TITLE     Structural biology of laminins
  JOURNAL   Essays Biochem 63 (3), 285-295 (2019)
   PUBMED   31092689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Sasaki,T., Fassler,R. and Hohenester,E.
  TITLE     Laminin: the crux of basement membrane assembly
  JOURNAL   J Cell Biol 164 (7), 959-963 (2004)
   PUBMED   15037599
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10597119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..641
                     /product="LamG domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=68081
     Region          481..632
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
ORIGIN      
        1 mqiskvatav alstgllfgc nsdglpiptd sgagsqesvl ttgywqisdg nsssisassn
       61 adlpnvyvfq edgnhkyydd dddlgtytik dasastnnyd eeagtvsfty yetgtstiei
      121 ldgvfsfdda galnisdntt gidysgsdqt atdavqeais eaneanging yvqildtnng
      181 gvkndvgelr lklsdsstga tvdsiasgkv tvdliyqvde dteqeangsg nnayislyas
      241 gtsntnlhge vifnageify rstvtdssgk pqipdepvgt ytlgedlave iswasgyytf
      301 kvndtvydns gngfeafdka avtivslklg dtsntthyel nadnfkvysn dtasdelvfe
      361 dnfnnypngq alsgnpynnn taeatvvvdg gnsepeppvd gdfpvalney tfdnadyttd
      421 sgsadndlts ksgsplittt sgaagtgamh idqdsatggg ygyiyynats ttttgaqaie
      481 dsfsvetvik adrfgydsdv slvdfaetsd ylgfklyles sdnsikfkvy ggldaddkgl
      541 steakssegd vylvednwyh ilatynhlds tanlyidgtl ahsksvdfsv ienttddkfi
      601 llggssssdk nfdgsvdnia vwntvltdvq iqervaqfta e
//
LOCUS       WP_010438492             482 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Vibrio cyclitrophicus].
ACCESSION   WP_010438492
VERSION     WP_010438492.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..482
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52708
     Region          134..452
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mtkpkfrcla iasiligtis spsyaaplsf teawqilqen nnslaaqqan veryqhlqns
       61 tsslnlpsit lganythlds dvtingeqfk nslsgvpnlg evgsilqpil sglggvtsti
      121 teqdifsssi raiwpiftgg ritaaqtaae gkseeaqsql lmekqaryed lskyyfsvil
      181 aedvvktrqa veagltqhrd faikleqqgq iarverlqad asldkavver tkaqndlkia
      241 qlaltqilgq sqsvepseql finknlphmd vfidqtlmty pglkildake kqasslikae
      301 kgkyypevyl ygdyslyedd slasemkpdw lvgigvnvpl idtsgrsdkv aaahsavsqv
      361 qflksqakqd ltvlvqktyl eanqaieevq glnsslslaq enlslrkkaf tqglsnslev
      421 vdaelylasi ktqqsaarfk ylislnklla ltsemnayss yltssvssdf dsrtdtdsqs
      481 kg
//
LOCUS       WP_010438516             260 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein [Vibrio].
ACCESSION   WP_010438516
VERSION     WP_010438516.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..260
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27365
     Region          17..258
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mqldwsllld llilftagvs ggvlnsiagg gsfitfpall fagvppiaan atntfascag
       61 yisgayalrh eiksgtkqlk ivitlcvvgg gigaflllht tealftqsvp wlllfaallf
      121 tfggtlnqwl kkltakhkha nsagalfsal mllivcvygg yfnaglgivt lsylalagyt
      181 ninvmngikl lvsacaslaa ivffivngsi dwpsgiavlf gtlvggyysa kisrripqqy
      241 vrttviiasf litayffyan
//
LOCUS       WP_010438524             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Vibrio].
ACCESSION   WP_010438524
VERSION     WP_010438524.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..239
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27202
     Region          15..235
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mntaikdltl santktrvsd kentksenlt eylveaivng elapgskise pelakrfevs
       61 rgplreaimr veglglieri phvgarvitf saekllelya vrealegmaa rlaarhitqd
      121 eligleglls thskhideve gssyfhqhgd fdfhyriika srnsklisll cdelyhllrm
      181 yryqspraqs rpkealdehk yilqairnrd eelaemlmrr hisgsrllie qqiqskdld
//
LOCUS       WP_010438550             269 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Vibrio cyclitrophicus].
ACCESSION   WP_010438550
VERSION     WP_010438550.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..269
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29329
     Region          4..264
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,195,217..219,221..222)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 myklialdmd gtllnsekvi sqenkdaiak araagvkvvl asgrplegmq nkldelsing
       61 eddfvlfyng smvqnvstke iihseisngk aakeitalae qlggyvhafs kvhglitpen
      121 neftaieari ngleitefdf sqleddheii ktmivaepsk lteiigklpq elktqftivq
      181 sapfflefln pksnkgvgie aiakhlgiks eevicmgdae ndhhmleyag lgiamdname
      241 etkkladhit asnddhgvav aiekfifns
//
LOCUS       WP_010438560             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Vibrio].
ACCESSION   WP_010438560
VERSION     WP_010438560.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..205
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22567
     Region          85..186
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(89..90,123..124,127,131..132,135,176,180)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mkllkavfpl cllvasanil aetndeefey ralpesvqsy dledddndgv inardlcvdt
       61 qigaeidndg cgsyfesteq kelhilfann steinpvflg qirqmaaflk ryesttirlq
      121 gyaskvgnaa hnldlskera snvrralisn giqpsrvtiv gygdtvsnee gtkinhalnr
      181 kvvasvagfk gnikeewhif tkigk
//
LOCUS       WP_010438565             236 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Ruegeria conchae].
ACCESSION   WP_010438565
VERSION     WP_010438565.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..236
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25521
     Region          156..232
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mnpdwaavvd gtwpaagyqt qgpfrlrqgq gggsrvsaan rtgdvtsadi daaesamqam
       61 gqkrifclrp gdealdamla qrgydildpv niysclaqql tdipiprvtv fniweplaim
      121 reiwaqggig periaimyra pgpktglllr hsdqpagtgf vaihegiamv haleilpdhr
      181 rkglgqwamr aaafwaldng aqtlsvictk aneganglyh slgmkivgey hyrqra
//
LOCUS       WP_010438601             290 aa            linear   BCT 01-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Pseudomonas congelans].
ACCESSION   WP_010438601
VERSION     WP_010438601.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..290
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32004
     Region          1..257
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mieqwqidqf heqgflvveg vlaanevaal qqdfdqwvdd srsqnkawgq tqdgrprfdi
       61 esdhrpdhps lrrvasptei spayrhaafq srmaaiaaql iggngtrfhh skinsklpht
      121 atqvkwhqdf lftphsnddl vtallmisdv tpengplnva pgshkqalws hwqnerftga
      181 vedavveqhc qqpvacygps gsvcfmhtrl lhasspnete fprtlfisvy aaedalpfge
      241 nplpsehagl mvaghesglv rstenhirlp qkpkgasffv qqagkdaava
//
LOCUS       WP_010438638             419 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Ruegeria conchae].
ACCESSION   WP_010438638
VERSION     WP_010438638.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..419
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=45200
     Region          1..419
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mlnsataarr saiylldqil aegrllpecl aagtldrlap edraraqrlt ietlrglerv
       61 drlladhlrq tpaltvhnal rlgtvelcqg eaahgvvnsm veivgrsrkh grlkglvnav
      121 lrkiaadgpd awpkmrvprl pewlreplim awgedavkgm ehahfngapl dltpkpsvei
      181 agaemlptgs arlqdagqvs tlpgyeagdw wvqdaaaalp vrvlapkage kildlcaapg
      241 gktlqlsaag advtaldise arlvrvrenl krtglkakvi aqdalehegq ydailldapc
      301 satgtirrhp dlpfakdgse fgglielqar mlahawtllk pggrlvyctc sllpdegevq
      361 ieealdsysd mqvdraalei agveadwite egglrlrpdy wpdkggmdgf yiaclnksa
//
LOCUS       WP_010438655             401 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Ruegeria conchae].
ACCESSION   WP_010438655
VERSION     WP_010438655.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 401)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..401
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42420
     Region          19..285
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mlwdaltlql gynatlvaig atllgisagv tgtflflrkr alvsdaisha tlpgvclafm
       61 alvafggdgr nligllvgsa isawvgllcm nwltrhtrla edaaigavls vffgfgvvll
      121 tviqtmgvgr qaglegfllg stagmlwada lviaiggaat lllvmiirrp mtmvafdpey
      181 aaarglpvhr idlammglvm avtvvglkiv glilivalli ippvtarfwt ersdrvvlla
      241 gisgglsgfl gagisasapn lptgpiivlv sfgsfalsll fapvrgvlaa vlrhlrfqrr
      301 vhirqgllal aqgqkiyepl tirllrragi vradgvatde gkaraakalr dekrwefvra
      361 dqaheataal ydglrdietv ltrdqiaeid rriggpqevm p
//
LOCUS       WP_010438696             292 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Vibrio cyclitrophicus].
ACCESSION   WP_010438696
VERSION     WP_010438696.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..292
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=33406
     Region          50..292
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mpnptkpqmk plirkprssv qkassdqgsa hqefqvptnl vqhlwfrsre sladdglvyd
       61 piaaqackrc qlapecltge ldqqqllyat ltqlcdsqvq qflshnpdaw iinvgagldt
      121 rfyrldngrc hwveldvten llwrqrlfhk neryrlecgs vddltwldel nipeqasvmv
      181 vcehalldcn eqltahfiqs lsryfthaha clvlagdkss salgqklgsg kyahglsspi
      241 dsvlnwlpwa qwvksfsple qqcnrwklwq rllckisqfk krltpqlvlv kw
//
LOCUS       WP_010438722             272 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfotransferase family protein [Ruegeria conchae].
ACCESSION   WP_010438722
VERSION     WP_010438722.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Begolli,G., Markovic,I., Knezevic,J. and Debeljak,Z.
  TITLE     Carbohydrate sulfotransferases: a review of emerging diagnostic and
            prognostic applications
  JOURNAL   Biochem Med (Zagreb) 33 (3), 030503 (2023)
   PUBMED   37545696
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..272
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=31331
     Region          13..248
                     /region_name="Sulfotransfer_2"
                     /note="Sulfotransferase family; pfam03567"
                     /db_xref="CDD:427369"
ORIGIN      
        1 mgfpgtwmte sqsmvyrvvp kcacstigqi myfsdhgrff dgdihdandg mhkwafnasq
       61 dpiarnvqsh gsytftcvrn pytrilssff dkicgiqrng kryrgnlvpt liynygievg
      121 gedgkgefdq iasfrrfllf ardtirwrrp mdpdihwsam sghvstlian ggrydrifwt
      181 ekfndgmqdv ldhldtahrv tlseiprfne seghgpkrah pvedyfddls mhlvyeiykq
      241 dfelfkydfe npankmpige idldeihakl gd
//
LOCUS       WP_010438769             198 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tRNA-uridine aminocarboxypropyltransferase [Vibrio].
ACCESSION   WP_010438769
VERSION     WP_010438769.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Funk,H.M., Zhao,R., Thomas,M., Spigelmyer,S.M., Sebree,N.J.,
            Bales,R.O., Burchett,J.B., Mamaril,J.B., Limbach,P.A. and Guy,M.P.
  TITLE     Identification of the enzymes responsible for m2,2G and acp3U
            formation on cytosolic tRNA from insects and plants
  JOURNAL   PLoS One 15 (11), e0242737 (2020)
   PUBMED   33253256
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Meyer,B., Immer,C., Kaiser,S., Sharma,S., Yang,J., Watzinger,P.,
            Weiss,L., Kotter,A., Helm,M., Seitz,H.M., Kotter,P., Kellner,S.,
            Entian,K.D. and Wohnert,J.
  TITLE     Identification of the 3-amino-3-carboxypropyl (acp) transferase
            enzyme responsible for acp3U formation at position 47 in
            Escherichia coli tRNAs
  JOURNAL   Nucleic Acids Res 48 (3), 1435-1450 (2020)
   PUBMED   31863583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..198
                     /product="tRNA-uridine aminocarboxypropyltransferase"
                     /EC_number="2.5.1.25"
                     /GO_function="GO:0016432 - tRNA-uridine
                     aminocarboxypropyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=22233
     Region          7..186
                     /region_name="TapT"
                     /note="tRNA U47 aminocarboxypropyltransferaseTapT/TuaA/
                     YfiP, DTW domain [Translation, ribosomal structure and
                     biogenesis]; COG3148"
                     /db_xref="CDD:442382"
ORIGIN      
        1 msnqqacggc gfthqcvchl ipsiksqvdl vllthenefs rdtntgkllq qslekceafv
       61 wqrktppadl malledetrq pfllfpsdks iecqqavssv agdrkplfii ldgtwqeakk
      121 ilnksvwlqa ipqahlnits essytlrrnq dsghlctcev gvellkalge eeqarqiddy
      181 fqhylkvfqa dkcghslk
//
LOCUS       WP_010438938             156 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010438938
VERSION     WP_010438938.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..156
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=16855
     Region          39..149
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 maehaiktrr wvllgagtvi agglalreyr lipqdyaghq iavstahqqv rqgdivlidi
       61 rtprewratg igegahpldm rrkdfvpvld qllegdrtvp valicargvr sarlsnqlte
      121 agftnvidvp egmlgsaagp gwvraglpvn dykedt
//
LOCUS       WP_010438948             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [Vibrio].
ACCESSION   WP_010438948
VERSION     WP_010438948.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..429
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=47024
     Region          13..423
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mkilllvgli vlnglfamse ialvaaknsr lkrlaekhrs aqvalelken ptrflstiqi
       61 gitvigllsg ivgeatlsap lavqlelwef dpaqanilst aivvvgityf aivvgelvpk
      121 rfaqsqaeni avlvalpifw lskiatpfvf alsastegil klmgrggeed svteddihal
      181 vkegsesgvi ergeqemirn ilqlddrlvs slmtprrdvd fldidqpveq llkklrlskh
      241 svfplcqdhl nqvvgtvsak allnqagnls iqvimglsks piyvpesmka lrllsyfkgs
      301 gaemvfivde ygdvqglvth ydileaiage lsnnpqdlwt eevedgllvd gliplselkn
      361 rlelseleve kegfqtlngl iswligrlpe vgevveyqqw qfeitsvenn rivsvkatpi
      421 tndfsdasr
//
LOCUS       WP_010439017             156 aa            linear   BCT 01-JAN-2025
DEFINITION  c-type cytochrome [Ruegeria conchae].
ACCESSION   WP_010439017
VERSION     WP_010439017.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..156
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17089
     Region          <28..129
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkhsfdiayf elemlnlsee qmlvcrtlll siftasaala qdidlqnghd lyrtycwqch
       61 gfeatgdgpm aemlairtpd ltrlaaqneg vfpieavarq idgrapllah ggempifgpa
      121 ldsdqkvalt mpdgqpmfag vplanviyyl esiqie
//
LOCUS       WP_010439087             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010439087
VERSION     WP_010439087.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..245
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27346
     Region          18..231
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mrksdreafl gsvlgneqpp ahlartviee klrnaiidgs lpsgtalrqq elatlfgvsr
       61 mpvrealrql eaqsllrvet hkgavvapli tedavdayal rillesealr lsiplldadd
      121 laaakgyieq levetdfgqi grlnrmfhls lyakthnkrl mrlveeglne eerflrfnls
      181 dmglgklsqd dhwqllrlae qkaiepcvea lqyhlnrgvq avtqylnskk atkakstrav
      241 kktpa
//
LOCUS       WP_010439088             202 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Ruegeria
            conchae].
ACCESSION   WP_010439088
VERSION     WP_010439088.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..202
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /note="This protein belongs to a clade of uncharacterized
                     proteins related to peroxidases such as the
                     alkylhydroperoxidase AhpD."
                     /calculated_mol_wt=22282
     Region          40..185
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mswiktipyv eatgrlrkly drvtgpdnnv dnimmahslr phsmeghmam ykavlhhsgn
       61 vipkwflevl gvwvsslnrc gycvehhfag lqrllqdear gnaiwaaiea gepgqaplda
      121 aqvaamyyar llteapadlt eadverlrsa gwddgeilei nqvcsyfsya nrtvlglgcs
      181 tdgdvlglsp nnsenpddwg hr
//
LOCUS       WP_010439135             373 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PhoH family protein [Vibrio].
ACCESSION   WP_010439135
VERSION     WP_010439135.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..373
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=41810
     Region          7..334
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 msnkivtlei nlepadnkrl aslcgpfddn ikhlerrlgv einyrsnfft ivgkphttaa
       61 aldiikhlyv etapvkgnii diepeqvhla iaesgileqh veseidygke vtiktkkgvi
      121 kprtpnqaqy lmnmvthdit fgigpagtgk tylavaaavd alerqevrri lltrpaveag
      181 eklgflpgdl sqkvdpylrp lydalfemlg ferveklier nvievaplay mrgrtlndaf
      241 iildesqntt veqmkmfltr igfnsravit gditqidlpr gaksglrhat evlsevddis
      301 fnffmsedvv rhpvvarivn ayekweakdq kerkefeark reereaklle aqqavttqla
      361 tqnssviaeq gdk
//
LOCUS       WP_010439142             348 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: lactonase family protein [Vibrio].
ACCESSION   WP_010439142
VERSION     WP_010439142.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..348
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=38929
     Region          1..344
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mktlpltigc ytdtpsksqg vyqtqldlet gkllslelir kctnpsfvta tktgiytase
       61 vnqqkqpqli hipnvdsqim snaspisgnh pchiaidphn kfaitsqyss gtfdifslsi
      121 ngsidkrlkt ikmvgsgpnk erqtsphahq clflqnspqf vtvdlgtdri nfycfdeeqe
      181 efldepmqsi kvpagngprh lifnkaedra yvvcelsetl lilekvlgiw nvveeidalp
      241 nmekgeataa iklspdeqfl yvscrhqsri snfkidsetq kltfiesydt egkfprdfhi
      301 tddgkwliaa nqhsnnitsf krdnedgslv ytgyslelda pvcvtqqr
//
LOCUS       WP_010439204             927 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Vibrio cyclitrophicus].
ACCESSION   WP_010439204
VERSION     WP_010439204.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 927)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 927)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 927)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 927)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457611
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..927
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=98918
     Region          76..137
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          172..238
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          263..906
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(556,558,862)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(600..602,664,680..682,711,751..753,773,776,779,798,
                     801)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(863,891,895)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mlgvdenwsi dmnhyttaln glncmgcakk vrtlfgeldn ttindispty idistpfsyv
       61 qlneklatlg ysmgnklhls lsglscgkcv skltqaleht eqisdleisk helslvtlls
      121 epdlielies vgyhaapyie vneplsnsds eddkktapve ptqdkpaasq ytyhlvlegm
      181 tcascvssve kalkknefvd qaqinlaeqt alvftskkrd vienaliesv knagygaefv
      241 ddaatqqkkq qeqqlctqqa flrnsvsall igaplmawgv fggsmtiatf ndqltwglvg
      301 vvclillats grsfftnawq slmhkratmd tlvalgtgaa wfysmlvvli pswfpeasrh
      361 vyfeasamiv glislghyie akakarttks lqalinlqpq kavvivdgke qtiaveviqv
      421 gmqvrvkpge kvpvdgvvvs gesyidesml tgeplpnvks indgvsagti ngdgsliiea
      481 tgigsstmla riiqmvrqaq sskpaiakla dsisavfvpv vvaiaataal vwflvgpqps
      541 asymlvvstt vliiacpcal glatplsitv gvgkaaefgv likdadvlqs askidavvfd
      601 ktgtltqgkp tvqqafygdl leqellayay svevgsehpl akavcqyaes lqvsalphsd
      661 fenqrglgvq aiingknvqv gslkyltqlg ieakigadfv elcrtqswtp ifvvidqkle
      721 gifgisdalk idskqaiaql ksagihtvll tgdndsvaqa igksvgidev isevlpeqka
      781 qhivqlqqqy ksvamvgdgi ndapalaqad igiamgsgsd vaiesaqmtl lnssplsvsn
      841 aielsqatvr nmkqnlfgaf iynslgipia agvlypffgf llspvvagaa mamssitvvs
      901 nanrlrlfkp thsninknhi hevnhds
//
LOCUS       WP_010439238             215 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Ruegeria conchae].
ACCESSION   WP_010439238
VERSION     WP_010439238.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24552
     Region          1..211
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltiwgrkts snvqallwcv geldleyqrh dlghlfggld saafqalnpn rtipvlrdgd
       61 gaplwetgai lrylatrygn etfwpsdpiq raqidkwaew aklniamaft vpifwqvvrt
      121 pakqrddqai rqavidleik ltiadtllad spylagdtft ladiqfghvl yryydieidr
      181 atlphlsryy dtlterpayk rhvmigyeel rppda
//
LOCUS       WP_010439249             276 aa            linear   BCT 01-JAN-2025
DEFINITION  creatininase family protein [Ruegeria conchae].
ACCESSION   WP_010439249
VERSION     WP_010439249.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..276
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=30044
     Region          39..271
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mcqarlrrti wavcivgaal itaslmwiqq tpdptndlfl ehmtwpevha aledgyrtii
       61 iptggteqng phvtlgkhnf vveyasreia eqlgntliap viryvpegdv vpnptghmqw
      121 pgtislpepv fqqvleatir slashgfkei lligdsggnq aaqsraatst slelattgvi
      181 vqhvsdyyek ngqiafledq gfsaeqignh aalrdtselm yvnadevgrs rapvppgwsa
      241 gfdgqpdlat reigkqmvql kvdaalkqiq rrrdan
//
LOCUS       WP_010439313             152 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010439313
VERSION     WP_010439313.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..152
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16871
     Region          2..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mieldeidrr ilralrqdat qsagalgrkf glsqpatwrr ikrledagvi kgrrlrlnae
       61 algfgvtvfl gvklarkgqv sledferavs aipevqtveh vlglydyrlr vvardladfe
      121 rvlrrrvmtl pgageveanv llseerlpgp ig
//
LOCUS       WP_010439344             219 aa            linear   BCT 01-JAN-2025
DEFINITION  DsbA family oxidoreductase [Ruegeria conchae].
ACCESSION   WP_010439344
VERSION     WP_010439344.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..219
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24079
     Region          12..212
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(20,23)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mpspdprptv qidvvsdvvc pwcivgfhql daalkqenvl arlrwhpfel npsmgpegqn
       61 lrehiaekyg ltpeqshqar erltalgael gftfnftdds rivntfaahq lldwaetkgr
      121 qhplklalfd ayftrqqdvs dvdvllgave tagldtvaar aalesgahaq pvrekqrfwt
      181 srgisgvpsm vfegkylltg aqgadtyaqv lqrclaeaa
//
LOCUS       WP_010439362             251 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010439362
VERSION     WP_010439362.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..251
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27647
     Region          15..248
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 msvadflkpe gwlgqtagpr yvqlrhrleq gieegilapn sslppereia eltdlsrvtv
       61 rkaiqelvrk gaieqrqgsg sfvrqpvarv eqslshltsf tedmerrgfe ttstwlergv
      121 flpspdemla lglstndqva rihrlraagg rpmaleraal pldilpnpte vtgslyafle
      181 rsgnrpvrai qkisainlea teaclldvae gtaglriqrt sylesgrvae ltrsiyhgda
      241 ydfvaelrls t
//
LOCUS       WP_010439389              96 aa            linear   BCT 01-JAN-2025
DEFINITION  SCP2 sterol-binding domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010439389
VERSION     WP_010439389.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Burgardt,N.I., Gianotti,A.R., Ferreyra,R.G. and Ermacora,M.R.
  TITLE     A structural appraisal of sterol carrier protein 2
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (5), 565-577 (2017)
   PUBMED   28284963
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Dyer,D.H., Wessely,V., Forest,K.T. and Lan,Q.
  TITLE     Three-dimensional structure/function analysis of SCP-2-like2
            reveals differences among SCP-2 family members
  JOURNAL   J Lipid Res 49 (3), 644-653 (2008)
   PUBMED   18084051
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Bun-ya,M., Muro,Y., Niki,T., Kondo,J. and Kamiryo,T.
  TITLE     New aspects of sterol carrier protein 2 (nonspecific lipid-transfer
            protein) in fusion proteins and in peroxisomes
  JOURNAL   Cell Biochem Biophys 32 Spring, 107-116 (2000)
   PUBMED   11330036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007129
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..96
                     /product="SCP2 sterol-binding domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=9567
     Region          3..95
                     /region_name="SCP2"
                     /note="Putative sterol carrier protein, contains SCP2
                     domain [Lipid transport and metabolism]; COG3255"
                     /db_xref="CDD:442486"
ORIGIN      
        1 msdilekaaa alneklsggd fdasakfaia dlgsiildas garvsddead vtlsadadtf
       61 eqilsgdlnp tgafmsgkls vdgdmgiamk lasvla
//
LOCUS       WP_010439420             231 aa            linear   BCT 01-JAN-2025
DEFINITION  SIMPL domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010439420
VERSION     WP_010439420.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..231
                     /product="SIMPL domain-containing protein"
                     /note="The SIMPL domain is named for its presence in mouse
                     protein SIMPL (signalling molecule that associates with
                     mouse pelle-like kinase). Bacterial member BP26, from
                     Brucella, was shown to assemble into a channel-like
                     structure, while YggE from E. coli has been associated
                     with resistance to oxidative stress.; The SIMPL domain is
                     named for its presence in mouse protein SIMPL (signalling
                     molecule that associates with mouse pelle-like kinase).
                     Bacterial member BP26, from Brucella, was shown to
                     assemble into a channel-like structure, while YggE from E.
                     coli has been associated with resistance to oxidative
                     stress."
                     /calculated_mol_wt=23957
     Region          3..229
                     /region_name="YggE"
                     /note="Uncharacterized conserved protein YggE, contains
                     kinase-interacting SIMPL domain [Function unknown];
                     COG2968"
                     /db_xref="CDD:442208"
ORIGIN      
        1 mktlaflaam taavaalpah aeerritvsg tgtalaapdm atitlgvtnq daqasvamqa
       61 tsdavtqilk rldemglesr dvqtrdlsls pvwsghrnsn deapritgft asnrvsvrvr
      121 dldklgqimd avikdgandf gglsfsvqep kpleaearak avvdatdkaq qlaeasgvtl
      181 gpvisindhg ggvrpmaqmr emamsdaggv pvaggeisvs vniamefeia d
//
LOCUS       WP_010439425             430 aa            linear   BCT 01-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Ruegeria conchae].
ACCESSION   WP_010439425
VERSION     WP_010439425.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..430
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=45713
     Region          1..412
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 msdgptygfd tlqihagarp dpatgarqtp iyqttayvfr dadhaaalfn lqevgfiysr
       61 ltnptvavlq ervatleggv gavccssgha aqimalfplm gpgcnvvast rlyggtvtqf
      121 sqtikrfgws akfvdtddld avkaaident ravfcesian pggyvtdira ladvadaagi
      181 plivdntsat pylcrpiehg atlvvhsttk yltgngtvtg gcivdsgkfd wsandkfpsl
      241 sepetayhgl kfhetfgpla ftfhgiaigl rdlgmtmnpq aahytlmgie tlslrmerhv
      301 enaqkiaawl eaddrvdyvt yaglpsspyh drvkahyprg agalftfavk ggydaciklv
      361 naleifshva nlgdarslii hsastthrql tpeqqeaaga gpgvvrvsig iedaddliad
      421 ldqalskasa
//
LOCUS       WP_010439446             143 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Ruegeria conchae].
ACCESSION   WP_010439446
VERSION     WP_010439446.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20139204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..143
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16185
     Region          23..125
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
     Region          <82..125
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 magdgirras lddvkdcari iwtwakqtgw mpdelpqeel aglireafpn rdvwvagdpp
       61 dcymsvdpve nkvgalyclr tgrgvgkrll dkakegrdhl wltthepnvd aqrfyrregf
      121 ietgreppvp pdtvpvirme wqa
//
LOCUS       WP_010439447             213 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Vibrio].
ACCESSION   WP_010439447
VERSION     WP_010439447.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22824
     Region          1..212
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfdtwiyyl lavliltasp gpssllcmtk gvqsgfklsi ftalgsltai tgiltlsftg
       61 lgviiassel vfniikwtga ayliylgwks lrssqqdydk lsnqkadsqs vkesaakhyv
      121 sgfivgasnp kailfftalf pqfidpsial lpqfavfalt favmelswll vyaylgakss
      181 nwlfakgrak vfnrvtggvf igagallstt sra
//
LOCUS       WP_010439449             485 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: protein adenylyltransferase SelO [Vibrio].
ACCESSION   WP_010439449
VERSION     WP_010439449.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10011099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..485
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55048
     Region          1..485
                     /region_name="PRK00029"
                     /note="YdiU family protein"
                     /db_xref="CDD:234583"
ORIGIN      
        1 msvwdsisfn nrftalprlf ytpiqptpls nvqwlswnhn lanelgfpsf edaseellet
       61 lsgnvepdqf spvamkyagh qfgsynpdlg dgrglllaqv vakcgetfdl hlkgagktpy
      121 srmgdgravi rstvreylcs eamaglnipt tralammtsd tpvyrekqew gallvraaes
      181 hirfghfehl fytnqlaehk lladkviewh fpecldaekp yaamfnlivd rtaemvalwq
      241 angfahgvmn tdnmsiigqt fdygpfafld eydprlicnh sdyqgryafn qqpriglwnl
      301 salahslspl vdkadleaal eqyepqmngy fsqmmrrklg llskqegdsr lfesmfelms
      361 qnkvdyprff rtlsnldtlk pqdvidlvid reaaklwvdn ylqrcelees svvkrcenmr
      421 qvnpkyilrn ylaqlaidka ergdssdida lmvvlanpya ehpdyehlaa lppewgkame
      481 iscss
//
LOCUS       WP_010439453             329 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Ruegeria conchae].
ACCESSION   WP_010439453
VERSION     WP_010439453.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..329
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35421
     Region          23..306
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mkkllsgava afslaasaal aadevtlqlk wvtqaqfagy yvakdkgfye eegldvtilp
       61 ggpdiaptqv iagggadvtv ewmpaalaar ekglplvnia qpfkssgmml tcwkdagiaa
      121 pedlknrtlg vwffgnefpf mswmsqlgis tdgksdsgve vlkqgfnvdp llqrqadcis
      181 tmtyneywqv idagvtpeel vtfkyedqgv atledglyvl eenlsdaafa dkmerfvras
      241 mkgwkyaeen pdeaaeivle ndatgaqtee hqkrmmgeia kltagsngal dpadfnrtve
      301 tllaggsdpv itkqpdgawt hqitdaaln
//
LOCUS       WP_010439489             130 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Pseudomonas congelans].
ACCESSION   WP_010439489
VERSION     WP_010439489.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163535
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..130
                     /product="VOC family protein"
                     /calculated_mol_wt=14568
     Region          2..124
                     /region_name="GLOD5"
                     /note="Human glyoxalase domain-containing protein 5 and
                     similar proteins; cd07253"
                     /db_xref="CDD:319916"
     Site            order(2..9,26..27,42..46,64..75,80..81,84,93,100..103,112,
                     115..116,118,120,124)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319916"
ORIGIN      
        1 midhldhlvl ttadidackd fyvrvlgmtp erfrqgrlaf rfgnqkinvh ergkefepka
       61 hlpvpgsldl cfiatipleq vivhlqeqew pivegpvert gatgpiwsvy vrdpdlnlie
      121 isepavdasi
//
LOCUS       WP_010439490             453 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Vibrio].
ACCESSION   WP_010439490
VERSION     WP_010439490.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..453
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47986
     Region          1..447
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mamlflflmv iafmlvgvpi aislglssvi fllmhsdasl asvaqtlfna faghytllai
       61 pffilassfm stggvakrii rfaiamvgwf rgglamasvv acmmfaalsg sspatvvaig
      121 siviagmikn gyskefaagv icnagtlgil ippsivmvvy aaatdvsvgr mflggvipgl
      181 lagvmlmiai yiaarikkip aqpfvgwgem faaakdaswg llliviilgg iyggiftpte
      241 aaavaavyaf fianfiykdm gpfadkkntk palvkvfqtf fhkdtkdtly dagkltimll
      301 fiianalilk hvlteeripq mitesmlsag lgpitflivv nvllliggqf mepsglliiv
      361 aplvfpiaia lgidpihlgi mmvvnmeigm itppvglnlf vtagvakmsm mnvvkaalpw
      421 vgvmflflii vtyvpwvstw lpttlmgpei itk
//
LOCUS       WP_010439510             320 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-quinone oxidoreductase [Pseudomonas].
ACCESSION   WP_010439510
VERSION     WP_010439510.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..320
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33577
     Region          1..313
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(36..37,117,121,124,142,145..147,166..167,171,186,
                     205..206,227..228,230,252..254,302,307)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkalqgvegh vewveepspa ldvgqvrikv aaaglnradl lqregkyppp pgvtqtlgle
       61 csgviaevgp gtswvvgdrv callaggama eevvvdgrhv lpvpeglslh eaaaipevya
      121 tawlnlfela glkpgekvll hagasgvgsa giqlckafgn pvwvsvgsae rlaycvelga
      181 qggvvrsesl eglndfapfn vildpvgasy aelnvkllal dgrwvligim sgreaqvdla
      241 hvlgkriqlm gstlrsrddt fkadllsdlg qhvwplfteg rlkpqlaksf avkdaeaafe
      301 elatntvsgk ivlvideslv
//
LOCUS       WP_010439523             467 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Ruegeria conchae].
ACCESSION   WP_010439523
VERSION     WP_010439523.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..467
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48930
     Region          6..467
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mdtidiglwv tagllilvvt gmrvafaagl agligliwif wakfgydpgr fgkaltvavk
       61 tagqvphskv ashtlslipt filigylayy agltralfea akrwvawvpg glavstifat
      121 agfaavsgas vatsavfari aipemlsvgy nkrfaagvva aggtlaslip psailviyai
      181 iveqdvgkll lagfipgafs aviygllivg iavifksvgp pvtgftwkqr faalpgalpi
      241 vaviliiicf vynpfgdkaw gtpteggaig afivfcfali hgmrwpefks alletaklta
      301 mifaiiwgvl iyvrflgfad lpgafsdwit slemspmlil icillayavl gmfmdaigml
      361 lltlpvvypa vmalnggeav saadsafgms gpmcaiwfgi lvvkmaefcl itppiglncf
      421 vvagvrpdls vqdvfkgvtp ffiadaltia llvafpgivl ylpslag
//
LOCUS       WP_010439531             199 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tRNA-uridine aminocarboxypropyltransferase [Vibrio].
ACCESSION   WP_010439531
VERSION     WP_010439531.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Funk,H.M., Zhao,R., Thomas,M., Spigelmyer,S.M., Sebree,N.J.,
            Bales,R.O., Burchett,J.B., Mamaril,J.B., Limbach,P.A. and Guy,M.P.
  TITLE     Identification of the enzymes responsible for m2,2G and acp3U
            formation on cytosolic tRNA from insects and plants
  JOURNAL   PLoS One 15 (11), e0242737 (2020)
   PUBMED   33253256
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Meyer,B., Immer,C., Kaiser,S., Sharma,S., Yang,J., Watzinger,P.,
            Weiss,L., Kotter,A., Helm,M., Seitz,H.M., Kotter,P., Kellner,S.,
            Entian,K.D. and Wohnert,J.
  TITLE     Identification of the 3-amino-3-carboxypropyl (acp) transferase
            enzyme responsible for acp3U formation at position 47 in
            Escherichia coli tRNAs
  JOURNAL   Nucleic Acids Res 48 (3), 1435-1450 (2020)
   PUBMED   31863583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..199
                     /product="tRNA-uridine aminocarboxypropyltransferase"
                     /EC_number="2.5.1.25"
                     /GO_function="GO:0016432 - tRNA-uridine
                     aminocarboxypropyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=22723
     Region          1..199
                     /region_name="TapT"
                     /note="tRNA U47 aminocarboxypropyltransferaseTapT/TuaA/
                     YfiP, DTW domain [Translation, ribosomal structure and
                     biogenesis]; COG3148"
                     /db_xref="CDD:442382"
ORIGIN      
        1 msrycpqcsk alkacicqwv tplesnveli ilqhpseehr pmgtarilsl slnnsvtfvg
       61 edfsnneqln illadehyqh vilypsehsv pvksvtysnk klrvilldgt wkkafkmwqv
      121 ssnlhalktv hlpkdlkgny rirkapsens lstveagyhl lrllendrdf splltafdqm
      181 iqfqinqmpp gvfeknyld
//
LOCUS       WP_010439549            1045 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Ruegeria conchae].
ACCESSION   WP_010439549
VERSION     WP_010439549.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..1045
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=110199
     Region          1..1031
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mfsalfisrp klalvislvl tilggigymv lpvaqfpdit ppvvsvtaty tganaetven
       61 tvaapieaqv ngvddmiymt stssdngsys lnvtfevgtd pdiasvnvqn rvaqamaslp
      121 sevtssgvvt qkastnmlll vtltspngty dsvflsnyas inlkdalarv qgvgkadvlt
      181 nleyamriwm dpdkmaalsi tpgdvinair eqnievsags igsppvpegq tfqytiktkg
      241 rltsadefgd ivirtgdaga ivrvkdiart elgaqfysas gyfqsvpatv igiyqapgan
      301 alavservea eldrlsrafp sdveyavpfn ttdfveqsln dvvstliltf ilvitvvfif
      361 lgswratiip avaipvslig tfafllafgm slntislfal vlaigivvdd aivvvenver
      421 iiadegllpa eatrkamgqi tgpviattlv llavfvpvtf mpgisgrlys qfavtistav
      481 vissinaltl spalcglvlk arsgpptgll amfegfigsm rngytaivrk llilpvislg
      541 iiaafaagtg simgvtskgf ipledngylf vdiqlpdaat lertetvsar ldaqiqeipg
      601 vastvlvngf sllngtttng aaifvnltnw eerqepdlsa dailgkvmai anqesaasiv
      661 afnpppiqgl gmsagvemev qqtgggspqd lasavgsyvy aanqrpeiaq ayttfranvp
      721 qlfvdldrek aktlqvsvae ifqtmqaqlg syyvndfnlf grvyrvmiqa egsyrnkved
      781 isdlyvrstk gemvplgtli dvenvlgpvl lkrhnlfrsa tvtavpaagl stgdaitamt
      841 eesatalppg yafewtgtaq qqlasgnlvv vilglailfg ylflvgqyes wtmpvsilms
      901 vtvalfgava avaivgsdin lytqigmiml vglaskngil ivefameqra kglsvkdaav
      961 eaafqrfrav mmtalsfllg vvpllaanga gaasqkaigv avfggmlaat lfgvilvpvl
     1021 yavmqsmrew ikgskndpgp seeta
//
LOCUS       WP_010439575             617 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Ruegeria conchae].
ACCESSION   WP_010439575
VERSION     WP_010439575.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..617
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68371
     Region          4..514
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mlrieninya vegrplfdga satipdghkv glvgrngtgk ttlfrlirge lslesgnisl
       61 pkrariggva qevpssdvsl intvlaadve rsslmaeads atdpdriaei qtrltdidaw
      121 sadaraasil kglgfddedq lkpcsdfsgg wrmrvalaav lfsqpdllll deptnyldle
      181 galwlesyla kyphtviiis hdrgllnrav gsilhledrk ltyyavpydk faerraerla
      241 qaesenakak ariahlqsfv drfrykaska vqaqsrlkmi eriqlvstpq eaalrafsfp
      301 epeelsppii qleggvtgyg etevlrrlnl ridqddrial lgkngqgkst lskllsdrlp
      361 lmagkmtrss klrigyfaqh qvdelhvdet pldhlrrlrp neapgkwrsr lagfglnsdq
      421 aetlvgrlsg gqkarlslll atidaphmli ldeptnhldi esrealveal taysgavilv
      481 shdmhllslv adrlwlvsdg tvkpfdgdle ayralllare kpvkvkpqta kpkrasretv
      541 lalradlrkc edrvkkltdm hdklsaklad pelykddrin dletwnrkfa evveamqkae
      601 alwvaaaerl eqaesaa
//
LOCUS       WP_010439648             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_010439648
VERSION     WP_010439648.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31552
     Region          19..151
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          192..273
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdnkkrskek aeykiteelg gleilnaeye kqnfsrhshe gytlgvieqg aqrfyrtggh
       61 hvapqdaiil vnadevhsgh sateggwayr amyplpeqla kitqelnlpn ygapyfprav
      121 vedpelanql rlvfntides dnrllretlm ygmlvklisr hgksslkpll dgktqrqlvl
      181 vkeflddfpq advsleelsk laalspfhlv rsfqkefglp phayqiqsrl rlsrkllkqg
      241 hsisdtaqec gfhdqshfhr hfkkangytp gqyikmr
//
LOCUS       WP_010439657             204 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010439657
VERSION     WP_010439657.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..204
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21951
     Region          7..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtkrgyhhgn lkqalieaal slieqkgptg ftlseaakta gvtpaavyrh yegredliae
       61 aarqgfemfa dlmqfaydkg qpsalaafea tgraylafar khpghyiamf esgislnrtp
      121 elalaanrak nvlekaagdl sqhippekrp pasmfsahiw amshgvvely arntgasspf
      181 ppedllesgi giylrglglv aqde
//
LOCUS       WP_010439669             407 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpP1/FadL family transporter [Ruegeria conchae].
ACCESSION   WP_010439669
VERSION     WP_010439669.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..407
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43410
     Region          8..404
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mkrslfhaca lcigattvqa ggldrsgqgv nilfeegsav qfrlgytkpd vsgsmedqip
       61 lsptfgetie sgnvsnsfft phlayktslt ekldfalvyd qpfgadidys seyplsqnvl
      121 gfsppfplga nqdvlrakad tdaitallry kldngfsvig glraqrlkas vsvpiagagl
      181 epfpsggyrv etdaeidfgy vvgvawerpd iaarvaltyn skikhdlsqt esndalaftp
      241 fpeiarssad sstevitpqs vnldfqtgva pktllfgsir wvdwpqtvya ppiytgltgi
      301 nlvdyeeatw tyslglgyqf tdefsgavtl gyessqgnsv snlgptdgfw siglggtysl
      361 ekakisggvr ytdigdatan gtgpdnratf tgnsawsvgi qvtyald
//
LOCUS       WP_010439697             338 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nuclear transport factor 2 family protein [Vibrio].
ACCESSION   WP_010439697
VERSION     WP_010439697.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..338
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=38085
     Region          10..147
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
     Region          <259..325
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mskyqeakri vrdyfdamen athenvaevl kahtsedylw rgvypfreqe gaqaaadvfw
       61 apmmksmtrm qrrqdifigg nnevnpdeiw vmsmghfmgl fdaeylgirp tgkimnvrya
      121 efncvvdgki tktglfldll gmmdqagcyp lppstgkhfv ypgprnhdgl lfedaapeeg
      181 vatlalvnkm vddlsalnds gamgcppevl akswskdmiw ygpcgigasy tipryqqqhq
      241 lpfrnnlkdk kfnghvcrfa egnfscffgw pnlsntptgg flgmtggevr anmqvvdvyy
      301 rdgdklsenw vlidlpywlq qqgldvfert stimnptl
//
LOCUS       WP_010439704             161 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Vibrio cyclitrophicus].
ACCESSION   WP_010439704
VERSION     WP_010439704.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..161
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18277
     Region          11..147
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkqkestkev lddtdiaile hiqqdgrmsn sklaekvnls etrcwrrwkr meetgyidgy
       61 aaklnrkklg lhvagftlvt lgnhevente pfeefvavtd wipmchciag gadymvqvla
      121 kdleeyferi ssirrvkgvs aiqsnisvke lknsyklplg e
//
LOCUS       WP_010439719             161 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Ruegeria conchae].
ACCESSION   WP_010439719
VERSION     WP_010439719.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..161
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16638
     Region          1..152
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mtqvsmtvng kavsgdvegr tllssflrdh lsltgthvgc dtaqcgacvv hvngeavksc
       61 nmlaleadga dvgtiegqaa edgslnviqq afqdhhglqc gfctpgmvms aaallkdnpr
      121 ptegeirkyl egnlcrctgy hnivkaimaa sgqdvssiaa e
//
LOCUS       WP_010439714             322 aa            linear   BCT 01-JAN-2025
DEFINITION  XdhC family protein [Ruegeria conchae].
ACCESSION   WP_010439714
VERSION     WP_010439714.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..322
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34253
     Region          9..322
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 merfdsspet alewyragkg aalatvvetw gsaprrvgaq lviagdgrie gsvsggcveg
       61 avivealeai eegearllef gvsdddafav glacggtirv lvepvgkvls epmlaelvaa
      121 rarreplaye vntetghral rrnayterlr mdrsgfeedg qtfvavhnpp lrlivigavh
      181 iaqalvpmar lagydpaivd preafasdvr fpgetiltdw pdeavsklgl dtrtalvllt
      241 hdpklddpal qaalsadvfy igalgskrth akridrmkqs gftdeqisri hgpigldiga
      301 aspseiavai laqmtavlrg ka
//
LOCUS       WP_010439833             158 aa            linear   BCT 01-JAN-2025
DEFINITION  fasciclin domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010439833
VERSION     WP_010439833.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Clout,N.J., Tisi,D. and Hohenester,E.
  TITLE     Novel fold revealed by the structure of a FAS1 domain pair from the
            insect cell adhesion molecule fasciclin I
  JOURNAL   Structure 11 (2), 197-203 (2003)
   PUBMED   12575939
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..158
                     /product="fasciclin domain-containing protein"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=16165
     Region          23..157
                     /region_name="FAS1"
                     /note="Uncaracterized surface protein containing fasciclin
                     (FAS1) repeats [General function prediction only];
                     COG2335"
                     /db_xref="CDD:441906"
ORIGIN      
        1 mfrrtfmgaa aafalalpvk aqaadivdta vaagsfntlv aavqaaglvd tlkgdgpftv
       61 faptdeafaa lpegtvetll lpenkdqlva iltyhvvpak vmsgdiagkr akvltvqgdr
      121 lsvnakngvk vngaevvqad ieasngvihv vdeviipe
//
LOCUS       WP_010439890             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Vibrio].
ACCESSION   WP_010439890
VERSION     WP_010439890.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..429
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=46789
     Region          18..411
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mtkiivvggg agglelatkl grtlgrkkra qitlvdrkas hlwkpllhev atgsldegvd
       61 alsyrahakn hyfdfqmgsl nnidrerkvi alseltddhg ellmpsrele ydilvmalgs
      121 tsndfntpgv rdncifldsp eqahrfrtem nnqflklhak ngqgtvdiai vgagatgvel
      181 saelhnavke lrtygfgdld ssklnvnlve agerilpalp prissaahse ltklgvnvrt
      241 ntmvtqadse glttkdgdki paqimvwaag ikapdfmkdi ggletnrinq lvvkntlqtt
      301 lddnifaigd laqctqadgs fvppraqaah qmascaftni iakmngrdlk dyvykdkgsl
      361 vslsrfstvg slmgnltkgs mmvegriari vyislyrmhq malhglikts lmmlvgrinr
      421 vlrpnlklh
//
LOCUS       WP_010439948             144 aa            linear   BCT 01-JAN-2025
DEFINITION  ester cyclase [Ruegeria conchae].
ACCESSION   WP_010439948
VERSION     WP_010439948.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..144
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16245
     Region          8..127
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mtnsdrlraw ysevweqgnt daidqffapd tmaeglipem qvgaddfrdl vmafrhvlge
       61 ikvdlpkiie ngdwvsgvlh vrtfradnga plevtgqvma rfkgekmvea ynqfdfislf
      121 eqlgqfpqdt lpvcmtgqrl dwvg
//
LOCUS       WP_010440029             226 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Pseudomonas].
ACCESSION   WP_010440029
VERSION     WP_010440029.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..226
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=24893
     Region          16..213
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mrpffktwlt iclfmplaah atnreqqlpa sfsgytaksh sspalatrna pqeatttrtq
       61 ygnnthavqk plsrknakkv aalqasvpak qgnavvkral qavgtpyrwg gntpgkgldc
      121 sglvkyaytd vrevdlprts namaqghgqt vdrkdlkpgd llffniksrn inhvaiylgd
      181 nkfvhaprrg kavtvdtlnk pywnshykia krvlpkqagq mrvvqr
//
LOCUS       WP_010440050             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Vibrio].
ACCESSION   WP_010440050
VERSION     WP_010440050.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28630
     Region          3..255
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mqdvidisww qlllfstllv lpiginywlk lglgkeafig ivrmvvqlfl vglyleylft
       61 lnslwinvlw lftmiivgas siveksklpk nlllapvavs lsvtcvpvvm ficffiikpt
      121 pilnaqylip iagmllgnsl ssnivalqnl fgafetqkse yeaaialgaa ptyaaapfir
      181 naiqkamspi masmattglv tlpgmmtgqi lggaspmiai kyqlmimlai fvmmscslal
      241 slhlalktsl tkegrvlari qptn
//
LOCUS       WP_010440058             503 aa            linear   BCT 01-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Ruegeria conchae].
ACCESSION   WP_010440058
VERSION     WP_010440058.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..503
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=52141
     Region          2..494
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mdfiyyfgdv ftplsfmlll ggtigglilg atpglsptma vallipftfq leaaqglill
       61 gaaytstvag gavsaillki pgapaniatt ldghtmakqg qgaralqlsf lasavggifg
      121 vlllifltpv laqwalafgp shlfwlailg vtvigtldsa svvkgllsgc iglwlatigf
      181 ddimgaqrfi fhpalgggin iiaaliglfa ipqvltmfak grhhtgaevi evqrhsilea
      241 frelfsrtra lsigtltgsi iglipgvggq iaglvaydqt kkfssekdkf gtghsegvia
      301 aesannamvg pslvplltls ipgsptaavl lggllihgif pgsdlfdnhp dvawtfinsm
      361 ligqvlmcif glyvaglaar vaqvpqsvma aivlalsvfg aysvqgsmgd vyvmaclgig
      421 mfflerfgfs aaplvlglil gpiaeanfiq ggmiadatvg kasyfltggl nlllitvvla
      481 siaysvwmel lhrryttkee aqa
//
LOCUS       WP_010440120             538 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Vibrio].
ACCESSION   WP_010440120
VERSION     WP_010440120.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..538
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=57430
     Region          15..537
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mklsvrkkly agfgsilavl vtlvgivwme vigahksade irlddvpgtv tylvlideag
       61 dvyrdalgai tlvdnalndy rtnkneftqa ieqakrlesr gsedhrriqr ieelmgrfth
      121 efesklvpki nneaallsni qqlralyekn lipienlldq asaseradte qslltltdsf
      181 ttieqtimll safamvfggv iafvlsssit nrltrveqva rrvangdltt gdivdesgde
      241 ladlaksinq mqkslvdllg sissvthqvq svtgelssis qdivsgasaq adkanliata
      301 aeelsltise vaqqgtstye earrsetsae dgrnvivemv asieqvsaqm sdmsvqmntl
      361 gshgeqigsv ikviediagq tnllalnaai eaaragefgr gfavvadevr alaerttkat
      421 qevsgiiqsi qsgtqeavty tqdncrlvei gvekssgavs aleaivsgag nvqsmvnsia
      481 taaeeqtavt keiaaditai sdiseqslql atrssentsg lnakvaelev lvgkfkla
//
LOCUS       WP_010440130             333 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Ruegeria conchae].
ACCESSION   WP_010440130
VERSION     WP_010440130.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..333
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35158
     Region          1..329
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,222,
                     244..245,247..248,268..270,320,322,324)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mqtllsvkpg gpetlelttl pdpvpkagei lvrihaggvn fpdtlmirdl yqmkpprpfa
       61 pggeiageit svgkdvvdfl pgdrvlaltg hggfathltl kpataikipd dmpyedaacf
      121 iftygtsyha lkdraqllsg etvlvlgasg gvgsaaiela kamgthviaa vsseekaqfc
      181 kkvgadktli yprdldraaq kalsaeiksl aggegvdvvy davggdyaep alrslawggr
      241 ylvvgfpagi psiplnltll kgcqivgvfw gasvfrdpkv hsqnvgelfk myrsgaicpr
      301 isarfplera aeaitkmdqr ktlgkvvvtm gtk
//
LOCUS       WP_010440132             344 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Ruegeria conchae].
ACCESSION   WP_010440132
VERSION     WP_010440132.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..344
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38066
     Region          28..281
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(33,36..38,41,52,54,86,105..108,206,208,210..211,213,
                     225..226,229,244..245,248)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(33,37,41,52,54,86,105..108,206,210..211,213,
                     225..226)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(36..38,206,208,211,226,229,244..245,248)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mketdstldi navetylnsh ldgfhgplka tkftvgqsnp tyllstpnea yvlrrkppgv
       61 llksahavdr efrvmsalag snvpvpkvhl lceddrvigs afyvmeylqg rtfvdpvmkg
      121 ednttrtgvi demnrvlael hmvdidavgl sdygppgnyf erqiarwtkq yrasetetip
      181 dmnhliaale hqvpeddnqr tlvhgdyrid nlmfetngtg cigvldwels tighpyadla
      241 avimqwqlpp gkegrglagv drenlglptd rafvanycar rgipaienfg fylafnffrm
      301 agilqgvykr aldgnasdpk raqafgayvp ifaqhglsal rsea
//
LOCUS       WP_010440170             173 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma carbonic anhydrase family protein [Ruegeria conchae].
ACCESSION   WP_010440170
VERSION     WP_010440170.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..173
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18398
     Region          1..170
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mtiyalgkht pkihedtwva pdanligkvv leqgssvwfg ctiradheei rvgagsnvqe
       61 ncvmhidagy pltigqncti ghkvmlhgct igdnsligmg aiilngakig kncligagal
      121 vtegkeipdn slvmgspgki vrqiddaaaq kltlsalhyq enmrnfrdsl rpv
//
LOCUS       WP_010440184             336 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Ruegeria
            conchae].
ACCESSION   WP_010440184
VERSION     WP_010440184.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..336
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36137
     Region          13..336
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mdflnalval snfvlvpaia ygsqlalgal gvtliygilr fsnfahgdtm afgamiavlv
       61 twamqaagvs fgplptalla lpfailgciv lvlitdrlvy rfyreqkakp vilvivsmgv
      121 mfimnglvrf iigpddqrfs dgarflikar dfkawtglne glaiktsqai tvvvavvava
      181 alfwflnktr tgksmraysd nedlallsgi npervvmitw iivaalatta gvlygldksf
      241 kpfvyfqlll pifasaivgg lgnplgaiag gfiiafsevt vtyawkkvlt ylapesleps
      301 glvqflstdy kfavsfaill ivllfkptgl fkgkvi
//
LOCUS       WP_010440185             437 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Ruegeria
            conchae].
ACCESSION   WP_010440185
VERSION     WP_010440185.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..437
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=46360
     Region          31..437
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 msepvkntll fvvvgslill tgftqswnaa ililnmglis aimsigvnlq wgfaglfnvg
       61 vmgfvalggl avvlistppt pgawsgggyg vvlslllgaa tvvaavmvaq kmpkgrtrsf
      121 aiigilivgf fvyraifdpn vasieaidpa vagnigglnl pvlfawpagg llaagaawli
      181 gktalglrsd ylaiatlgia eiiiavmkne dwlargvknv ygiprpapvv gyevelqqdp
      241 sfiaraewfg ldpvtastls vklgysllfl ivllillwma qmalkspwgr mmrairdnev
      301 aaeamgkdvt rrhlqifvlg saicgvagam mttldgqltp gtynplrftf lvwvmvivgg
      361 sgnnfgavlg afliwflwvq vepiglwlmn litagmpdgs alkshlidsa ahmrlftmgl
      421 illivlrfsp rglipek
//
LOCUS       WP_010440190              85 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl carrier protein [Ruegeria conchae].
ACCESSION   WP_010440190
VERSION     WP_010440190.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..85
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=8919
     Region          1..82
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 msisdrviai iaeqavleps dvtpdstled lgidslglve sifaieeefd itvpfnanep
       61 tasdfdisnv aaiiagiekl vsekv
//
LOCUS       WP_010440200             185 aa            linear   BCT 01-JAN-2025
DEFINITION  Yip1 family protein [Ruegeria conchae].
ACCESSION   WP_010440200
VERSION     WP_010440200.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Shaik,S., Pandey,H., Thirumalasetti,S.K. and Nakamura,N.
  TITLE     Characteristics and Functions of the Yip1 Domain Family (YIPF),
            Multi-Span Transmembrane Proteins Mainly Localized to the Golgi
            Apparatus
  JOURNAL   Front Cell Dev Biol 7, 130 (2019)
   PUBMED   31417902
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10522553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..185
                     /product="Yip1 family protein"
                     /GO_function="GO:0031267 - small GTPase binding [Evidence
                     IEA]"
                     /GO_process="GO:0016192 - vesicle-mediated transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20066
     Region          13..182
                     /region_name="Yip1"
                     /note="Yip1 domain; pfam04893"
                     /db_xref="CDD:461468"
ORIGIN      
        1 mnsavllnmv vltltnpaea akrllamrfg pdvlwiaffl avilnalvqt lsgfimpfin
       61 pevqqiaepl srtlfvsvaa ilisvvafll vgrvlggegs fndlmtlvvw lqilqiigqa
      121 iiltlvsvlp flflpaslam lvlslyitlh flneahrfqs lgksflvill sglvaipfvl
      181 wlspv
//
LOCUS       WP_010440221             402 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Ruegeria conchae].
ACCESSION   WP_010440221
VERSION     WP_010440221.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..402
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=43199
     Region          <110..387
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mtpaarvqas idilneilag apvekaltgw arrsrfagsk draairdhvf dalrckrsfa
       61 arggaetgrg lmigamrssg qdlaqyfsga ryaptsvtda ekdrgfqtea ealdipdwlw
      121 pefkaslkde anaaaialqg rapvhlrvnr sradpveiiq clsdegivvq phpacdtale
      181 vtagarkisq cnpyleglie lqdaasqavt aaldlqpgmr vldycagggg kalalaarae
      241 gvqvfahdin pgrmadlpar akraraeisl ltsdqvsgqa pfdivlvdap csgsgswrrs
      301 pagkwaltpk rlleltriqa milesvaplt adagtiayat csmlsvenda ivdsflqehs
      361 dwrsgfrktw lvshgadgfy sahltrtwir snnlkefspl iy
//
LOCUS       WP_010440234             285 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Ruegeria conchae].
ACCESSION   WP_010440234
VERSION     WP_010440234.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..285
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=30670
     Region          11..283
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 msrvsilssn qflralwlav rrfndkdgfv msshvamslm malfpfvlft valagalsqg
       61 yvtdelieli fgawpkdvad pivselravl agagsgvitl ggllaiyfas ngvaavrram
      121 tqayhdkdiw pfwktrllcf alviiggaai laiaavevvl pvytrlvsek tavdvdnwls
      181 vdrlrwtftv avpagtvila hlilptrrhr lsqilpgvil tlalwaaggw gfsiyiaqfa
      241 tysatyagla gamaalifly lcsamlilga eyngalidlk naetn
//
LOCUS       WP_010440254             195 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Ruegeria conchae].
ACCESSION   WP_010440254
VERSION     WP_010440254.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..195
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22427
     Region          83..142
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mdgdfrtefv repgalrhhp alvlnadyrp lsyyplslwp wqeaikaawl drvdivaeyd
       61 evvrspstei ripsvvvlkd yvkprkrvaf trfnlflrde fkcqycgsrg eltfdhvvpr
      121 aaggvtswqn vvaacspcnl rkgskslrqa rmslskpprq pdaealrnig rkfppnhlhd
      181 swidflywda eldqq
//
LOCUS       WP_010440338              96 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Ruegeria conchae].
ACCESSION   WP_010440338
VERSION     WP_010440338.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..96
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10886
     Region          8..>74
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mtkaekkvhl rghitvphdr leqvrqalpa hisltraevg cisfevceda nqpgrfevse
       61 vfanraafea hqnrtknsdw yritqgipre yivtse
//
LOCUS       WP_010440354             393 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Ruegeria conchae].
ACCESSION   WP_010440354
VERSION     WP_010440354.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..393
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40774
     Region          1..390
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mngadtawii vatalvlfmt lpglalfygg lvrarnvlsv fmhcfsiacl msilwlvagy
       61 siafgpgesg lwgglgkafl ngvdadslag tlpeilffaf qmtfaiitpa liigayverv
      121 gfgfvltfsa lwmllcyapv vhwiwgggml adggilgeig vrdfaggivv hetaglaali
      181 iavilgprrn rttpphnpgy vmvgaamlwv gwfgfnggsq laadggaama mtvthlsaat
      241 asltwalwer irfgkasmvg lvtgtiagla sitpasgfvg pvqaliigav agilcqeavn
      301 virnklnidd tldvfavhgv ggifgtlmia lfglgtwtaq lgglvivgaf tavvtivlvk
      361 vvalitplrv daetetngld lsvhgerayd mss
//
LOCUS       WP_010440141             566 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Vibrio cyclitrophicus].
ACCESSION   WP_010440141
VERSION     WP_010440141.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 566)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..566
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62954
     Region          1..547
                     /region_name="YnjC"
                     /note="ABC-type uncharacterized transport system YnjBCD,
                     permease component [General function prediction only];
                     COG4135"
                     /db_xref="CDD:443310"
ORIGIN      
        1 mlhalyfvvi avciiptipg vagvvassls fipplglvep slngfeqvfq wegvwhsial
       61 slssafassy iacfltfcii qatwgkpfwk kieltlspml aiphvafaig faflfsptgl
      121 gtralhqlvg eagnsselal lvkdpyafgl iimlaikeip flllmslsil qqidveritk
      181 vsaslgysrs qiwwkvifpq wfiklrfpml avlayslsvv dialilgptn pptfavlvwq
      241 wfndpdlsll praaagaivl fvlasliiat arliewsllk qfkfwqfsgr tginlpgktv
      301 ftilaalsll iiplmiiwsi aqrwrfpdll psryslkfwe yewdgilstv gqslwialas
      361 asvalllalv aheyrirhrw qvpgfiiaip mlipqlsvlf glqvttlyig ssayelwviw
      421 ahvffafpfv ylsldgpwks fndglikasl slgkspfqsw csiklpillp aiafawavgi
      481 svslaqylpt lmlgagrist itteavalts gfdrrvtaiy aiwqallplf ffslaivvsr
      541 lqlryrrltf kgfltnesvs qrprhp
//
LOCUS       WP_010440373             169 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010440373
VERSION     WP_010440373.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..169
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18802
     Region          20..152
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 msvkkqpnar aaqsirspkd dlnqqiirll qqdgrmafse iaqqldvseg tirnrvsglr
       61 dnnmlrivam sdpvateytt damiglnvat gvtprqvaer lernprvvfi lwvagrydli
      121 ielvsddsda lkdfleheih gsndiakadv mpglknfknq fllkqgake
//
LOCUS       WP_010440411              67 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2061 domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010440411
VERSION     WP_010440411.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..67
                     /product="DUF2061 domain-containing protein"
                     /calculated_mol_wt=7026
     Region          1..64
                     /region_name="COG3205"
                     /note="Uncharacterized membrane protein, DUF2061 family
                     [Function unknown]"
                     /db_xref="CDD:442438"
ORIGIN      
        1 metrrrsvvk alvwnamgla mmtlvgliat gsaalggmva lvntaigltm yviyervwag
       61 iswgrng
//
LOCUS       WP_010440434             721 aa            linear   BCT 01-JAN-2025
DEFINITION  LPS-assembly protein LptD [Ruegeria conchae].
ACCESSION   WP_010440434
VERSION     WP_010440434.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..721
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80330
     Region          23..706
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mrpilsllls talilslptv amaqsevpga tndtgatqqn qpallvadei fitpdrklva
       61 egnveafqgd vkltaqsvty dretgeltlv gpiridqggd stlladsaql dsgiqngllm
      121 garmvfeqqv qiasvqatra agrytqfskv aatschvcan gtppiwqira rkvthdqler
      181 qlyfegaqfr ildvpvfyfp tlrlpdptle ratgflvpsi rttsqldtgi qvpyffkigd
      241 hkdltltpyl ssktrtlgfr yrqafkfgri rlrgaytrdd lrpgkdrgyl fadgrfslgn
      301 syrltfdikt tsddsylady glpdfdrlrs eialerikrd tafrtgfihy ktlrdsedqd
      361 eipsrifdln yrkrlfpkal ggevqlaflg hthtrtsded ivgrdvarat fdaewlrnwt
      421 fatglraeaq lgaaidtfni rndssypnnv trstpraaft lrypmlrreq sgatqilepi
      481 aqigwthvsd ndvpndestf qeldqgnlla lsrfpapdrr edgttavvgl nwsrynadgw
      541 ralatigqvf rsdadpdftl tsglqgtksd illagqlnng kgltlaargl lnndfsftka
      601 elraawvkgd talsggyiwl epdpaeannd eiselrvsgr yrvdqnwltr asarydfses
      661 eplrlgfglt yenecvqvnv nvnrrftsts siepstefgf tvaltgysve gngqkfkrrc
      721 s
//
LOCUS       WP_010440454             328 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas congelans].
ACCESSION   WP_010440454
VERSION     WP_010440454.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..328
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33700
     Region          34..321
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mstltlntss tlvkvlprll pavlpllvli illffainap gflswgnlss lvlnnfvlla
       61 ivaigmtwav aaggidlsvg taldfaslgf vvtlngghgl gaaiavalla ggiagafnam
      121 liaglrispf latlgtlfig tsvqqllsdg gqpiyiaqgm lpgisgvlil gvplpllvvg
      181 llaglyglvl argrlgreil algtqpqlay ysglptrria vqvffasala cavagillss
      241 tvnayvpmsg naylinaiga vfigttlsrq grpnipgtll gvlfinvian gllligwnfy
      301 wqqvatgali flvlafsfts rhllrnaa
//
LOCUS       WP_010440478             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hydrogen peroxide-inducible genes activator [Vibrio].
ACCESSION   WP_010440478
VERSION     WP_010440478.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Jo,I., Chung,I.Y., Bae,H.W., Kim,J.S., Song,S., Cho,Y.H. and
            Ha,N.C.
  TITLE     Structural details of the OxyR peroxide-sensing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 112 (20), 6443-6448 (2015)
   PUBMED   25931525
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..301
                     /product="hydrogen peroxide-inducible genes activator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33545
     Region          7..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..297
                     /region_name="PBP2_OxyR"
                     /note="The C-terminal substrate-binding domain of the
                     LysR-type transcriptional regulator OxyR, a member of the
                     type 2 periplasmic binding fold protein superfamily;
                     cd08411"
                     /db_xref="CDD:176103"
     Site            order(110,113..114,117,121,129..133,226,229..230,233,
                     236..237,239..240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176103"
ORIGIN      
        1 mnkwpslkql yylvtlhetr hfsdaadrcf vsqstlskgi qnleeligcp lyekkdkksp
       61 lvftqagelv vkhgrellak gqdlvelgnl cngdamqgql rvgciptiap fllcdlvqev
      121 nqrfpqlnll lredtttnll aalrhgeldv lilalpvdid nmesqvvgqd pfrmvisrnq
      181 adgirvpiky ddlpdesvfl lenehclteh avsackltdk ekinpftats lhtlvqmvan
      241 glgttfipqm aidhgllenq nlvvidppgq qayrdiglvw rpsssrretf hqladvvsel
      301 l
//
LOCUS       WP_010440574             195 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010440574
VERSION     WP_010440574.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..195
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21300
     Region          9..>87
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(10..12,26,43..45)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mskspdafrt isevadwlgv qahvlrfwes kftqvkpvkr aggrryyrpn dmrllggikk
       61 llhedgttik gvqrilreqg vahvashsps lddsppvspp ddtvvpftta ssgqpanqin
      121 mdlgepgqap apikpdisdq pkpqldamda aplmggiasl awnraeyddk llhqiapiak
      181 dlrrwldrve nraag
//
LOCUS       WP_010440644             460 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: multicopper oxidase family protein [Vibrio].
ACCESSION   WP_010440644
VERSION     WP_010440644.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..460
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=51589
     Region          30..459
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mdisrrkfiq sslaisaltv lpacsmkrsa deqgkyvydl taepstaelv kgfntnilgf
       61 ngqipaptir crqgekvtir ftnklseptt ihwhglripi emdgvpflsq ppimpgetfi
      121 yeftppdagt fwyhphmnsv kqlgmglvgl iiveesnpvr fdeehalmlk hwhidkqgqw
      181 kdlmiprlsa rmgtpgewss vngvhepvyq lkqyaatrlr ianvdntity piavegaeaw
      241 viaidgnpvk tpykltqhki gpgmrvdigl iapkagervn vlhmkgrfpf slcefevvds
      301 afaqgrslpl lplnpvpnld lanaeeidfl fewegavspv skdgksmpkf wltnkraweg
      361 mskdnipepl atlelgktyi fdlknvtqyh hpihihghtf tvleldgkki eepfhtdtvl
      421 lgkngrakaa fvadnpgrwm yhchviehmk tglmgyievk
//
LOCUS       WP_010440651             260 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HesA/MoeB/ThiF family protein [Vibrio].
ACCESSION   WP_010440651
VERSION     WP_010440651.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..260
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28643
     Region          3..249
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mlsdfefiry qrqialsevg eqgqrnllns hvlligcggl gnaaslylaa sgvgkivlvd
       61 ddcvdssnlq rqvafresql gslkvealkq qlselngrsq vrtinqrmse sqlelevmla
      121 dlvldctdnf asrqqvnqac fstktplisg saigwkgqfi vfdyqnqkgc yhclfpfrqh
      181 pqttrcsdsg iigpvvgtig nlqalaaiqr ltrgefqvat hqlklfdgqt mnwqnlmvtq
      241 dsecpvcsas vvkhleeeiq
//
LOCUS       WP_010440663             152 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Vibrio].
ACCESSION   WP_010440663
VERSION     WP_010440663.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..152
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17215
     Region          19..151
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mdnntvtnmm aqydalieks qslfvpllll fcrlwvawvf fnsgltkiat wdstlylfel
       61 eyqvpllpwe laaymgtaae lilpvflalg lltrpmaaal fvfnimavvs ypvlweqgfy
      121 dhqlwglmil vvvvwgagpm sldrilrkqf as
//
LOCUS       WP_010440683             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Vibrio].
ACCESSION   WP_010440683
VERSION     WP_010440683.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..220
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23803
     Region          3..215
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnevtilitl asihfialms pgpdfalvvq natrhgrqtg lyialglscg illhsllslt
       61 gisylvhqqp tlfaiiqlag gsyllylgyg alkatwytiq hhdddtdsvh stdliltnkr
      121 eafskgfatn ilnpkalvff islmsslvpa dmslsgkgfa llilfglslf wfsllawmls
      181 tkalqkklhe atvyidglcg avftiigvsi lwqsasslll
//
LOCUS       WP_010440831             293 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Ruegeria conchae].
ACCESSION   WP_010440831
VERSION     WP_010440831.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..293
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31540
     Region          4..293
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mhllltvfei vapvfllagi gfawvrlgfe yrlqfvtrla vtlavpslif valmqtnipg
       61 gdltrftiaa iaahialaav fwafvrltrm eqrtylapli fgntgnlglp lcifafgqag
      121 lgyaviflav talfsftygi ylvagrgafg kvlrepmvwa tllgalflwr gwqtplfltn
      181 tlellgqmai pmmlitlgva iarlttqklq qaiwlsllkl svcfglgwaf aagfglgpva
      241 fgvlvlqmct pvavtsylla erfeadsdav agmvmvstml svaalplila iil
//
LOCUS       WP_010440730             272 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Ruegeria conchae].
ACCESSION   WP_010440730
VERSION     WP_010440730.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..272
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29230
     Region          1..261
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 msrlswfntv sltlgfafly ipmiiliifs fnesklvtvw agfstkwyge lvqneaflda
       61 awvtlrvavf sstlatilgt aaayvlvrgg rffgrtlfsg miyaplvmpe vitglsllll
      121 figigldrgi ltivlahttf smcfvsvvvs srlvtfdrsl eeaaldlgcs pgqafrlvtl
      181 piiapavvsg wllaftlsld dlviasftsg psattlpiki fsavrlgvsp einalstlmi
      241 avvtvgvita slvtkrammr qkqdeqaaar te
//
LOCUS       WP_010440837             149 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Ruegeria conchae].
ACCESSION   WP_010440837
VERSION     WP_010440837.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..149
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16316
     Region          12..145
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mganckqdcl nlsfpatqvq asegiailsa rlekhglpes kaddvrialt eainnvveha
       61 yaeisptdir incslcakel ivqifdsgdp mpglrvpssh papvdtdlen lpeggfgwyl
      121 ihrlssdiqy erkdgvnlly lrfnfdtph
//
LOCUS       WP_010440847             406 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Vibrio cyclitrophicus].
ACCESSION   WP_010440847
VERSION     WP_010440847.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..406
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42922
     Region          11..406
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 msqtvtqvns avesltqssd tlflllgaim vflmhagfaf levgtvrkkn qvnalvkils
       61 dfgvsaiayf figywvayga hffadaetls qgngyelvkf fflmtfaaai paivsggiae
      121 rarfypilia tlftvgfiyp ffegiiwngn fgfqdwlegq fgygfhdfag svvvhgvggw
      181 ialvavyflg mrrgriragk htnfapsnip flalgswilc vgwfgfnvms aqaingisgl
      241 vamnslmamv ggilaalvag kndpgfihng plaglvaica gsdlmhplga lvtggvagal
      301 fvylftymqn ktqiddvlgv wplhgvcgaw ggiaagifgq qafwglggvs fasqvvgtla
      361 giavaligal ivygvlskvt glrlseedef ngadlsihki ssined
//
LOCUS       WP_010440861             326 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010440861
VERSION     WP_010440861.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..326
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36174
     Region          17..323
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpvrtksdqq qdrvqyhfdi lvasgfvlle laslvevlrl anrvcahppf tftyrsrkgg
       61 pvesssgatv stdtvpaqpn anylfvigns dpdqpelslg rvvrdytfrg gqvfllaeaa
      121 sryidensad hmathwenas flrergarfe aklsiateqg svvtcagmea ttdialavig
      181 rhisgaakmt vadimlheni rdfssmqpfs gtrttatgde kldqciklmq anieeplpik
      241 qivdilhvsn rslerkfkai fgttpngfyr emrlakannl llnttmsvre iglvcgfpng
      301 fssvyksffg itpfvlrrqk rrpeyr
//
LOCUS       WP_010440895             343 aa            linear   BCT 01-JAN-2025
DEFINITION  permease [Ruegeria conchae].
ACCESSION   WP_010440895
VERSION     WP_010440895.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..343
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=36145
     Region          37..343
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 maeltqnpkp sarnlvslik tpwalivvil vlvavldpsn waeivtfagk alahtgqyil
       61 favlllsylk atgaevmvar afegretrmi ffaalfggla pfcscevipf iagllalgap
      121 lsavmafwls splidpptll itagalgwpf aigkavaava lglfggfavr almrggafaq
      181 plreynptgc cgcgpkkddk pvwqfwnepe rrtrfraefv hnglfllkwl afayvleall
      241 vsyvpadlia rvvggegvvp ivvaalvgmp aylnsyvapp llaglmeqgm sagaamsfmv
      301 agavssipam aavwslvkpr vfatylglgi sgaiiagiaf qmi
//
LOCUS       WP_010440906             269 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Vibrio cyclitrophicus].
ACCESSION   WP_010440906
VERSION     WP_010440906.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..269
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31126
     Region          95..242
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mqdpsllrlv cfivvfglca iweyrfprkt ltqnkwfrwg nnfalvalns fllatlipia
       61 afqaaviaqd nqwglfntls lpkelvvlic vllldcaiyl qhlvfhrvsw lwklhrvhha
      121 dldidvttgt rfhpiemmls mlikvslvit lgvpviavvi feivlnasam fnhsnarlpl
      181 widkrlrkvi vtpdmhrvhh svivkethsn fgfflsvwdi wfktylaqpm lghdhvhigv
      241 peiqdgkeqr ldfmlrqpfv hyphsrksk
//
LOCUS       WP_010440910             161 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Vibrio cyclitrophicus].
ACCESSION   WP_010440910
VERSION     WP_010440910.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..161
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=17889
     Region          <20..161
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkirkmlavt itlvtltacs stpppfsynk vpskplskse qvtanaylsv yeqwkgvpyh
       61 fggtsfrgvd csafvqiavq natqqalprt tkdqskqgve iayekaisgd lvffktspkv
      121 rhvgvylgnk qflhastskg viisrldnpy waskfwhfrr i
//
LOCUS       WP_010440940             364 aa            linear   BCT 01-JAN-2025
DEFINITION  microcin C ABC transporter permease YejB [Ruegeria conchae].
ACCESSION   WP_010440940
VERSION     WP_010440940.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..364
                     /product="microcin C ABC transporter permease YejB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042884 - microcin transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39471
     Region          1..364
                     /region_name="YejB"
                     /note="ABC-type microcin C transport system, permease
                     component YejB [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4174"
                     /db_xref="CDD:443333"
ORIGIN      
        1 mgayilrrll lviptllgim ivnftlvqfv pggpieqiia qiegqgdvfa gfagggdaga
       61 gaepaggsfd dkyvgarglp pefiaeleke fgfdkppler flgmmgnylt ldfgesyfrs
      121 isvidlvlek mpvsislglw stliaylvsi plgirkaikd gssfdtwtsg aiivayaipg
      181 flfailllvl faggsywqif plrgltsdnw eslsllgkva dyfwhialpi ialtisafat
      241 ltlltknsfl deikkqyvmt arakglserk vlyghvfrna mliviagfpa vfigvffggs
      301 iiietifsld glgrlgfeaa vardypvifg tlfifglmgl vvgiisdlmy vlvdpridfe
      361 kreg
//
LOCUS       WP_010440955             279 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Ruegeria conchae].
ACCESSION   WP_010440955
VERSION     WP_010440955.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..279
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30362
     Region          156..277
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 maykslltvm tetkisqtal aqmvaladgq dahaealclg vdrsqtgyyy aganalilqe
       61 tlsranaead eilkfaqdyl gksgvrwsae ngvaqiadig rhvarrarfs dlvilprpyg
      121 kdrdaeaepi veaamfegha pvllvpdeie pisspktimv gwnesieamr aircalpflk
      181 qaeltrivvi dpprhgpdrs dpggllsqml arhgvkceid vlsktmtrvs dilnrhaadt
      241 eadmivmgay ghsrfreail ggatrnmleq sevpvflah
//
LOCUS       WP_010440963             307 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Vibrio].
ACCESSION   WP_010440963
VERSION     WP_010440963.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34349
     Region          6..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,227,244,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdlatrlell levskagsfa kaadrlnvdr svlskqvkql eehlgvrlin rttrslsfth
       61 vgkqiveqav kvselledte niaacfykep ignlrisstt lfgrrflqka veefltrypr
      121 asielildds rvdlvgegfd ivfrigpmrd ssmiakklad nktvivasea fidkhgmprs
      181 peeltmlpsi iyshagfvad kvqfylesnt geletyalkg nyrvnepeli vesikaslgf
      241 gqigqfmlne glaeqglvql lpereipsfg diyamythrk qsplvlafie ivqeiigtpp
      301 swekhfa
//
LOCUS       WP_010440966             291 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010440966
VERSION     WP_010440966.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30951
     Region          20..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..284
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(111..112,114..115,118,122,124..130,216..221,
                     227..228,230..231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176172"
ORIGIN      
        1 mdwlklppla alrafaafae krnvveagaa lnvshaaisq qlrvlekylg aalldrsgka
       61 ltltadgehl aralqlgfga ieaavgdlar sgldrpvhvs ltssfaaswl mprlpvfres
      121 hpevnlildp saevvdlrpg gvdiairygp ggwsgvhsem llqspvviva apkllggkts
      181 ltpselaqlp wleevgttea tswlaehgvg pergagrtql pgnlvldglr agqgvtvtvr
      241 hfveqdikag rivelyaepd argyhivtan salrpavrtf agwlrrqare t
//
LOCUS       WP_010440994             236 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010440994
VERSION     WP_010440994.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..236
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26665
     Region          8..236
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mssnsrnpna lpiyvqisel lirdiaagrl idgerlpper dmasnlnvsv gtlrkslael
       61 ekkgmleriq gsgnyiretg tqnsvyamfr lelpeggglp radilsvdhl qkpadlpefg
      121 lsdhgsrvrr mrylndtiia veeiwldesa gtidqnllsd slyryyqqql gfwitraedr
      181 vsigslpdwt pegftksagh tvgyierfsw sekaepvefs ktwfdpdrak yvqrlk
//
LOCUS       WP_010441047             159 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Ruegeria conchae].
ACCESSION   WP_010441047
VERSION     WP_010441047.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..159
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17018
     Region          6..157
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 msklhvtttv ngdeveylcd pretlldclr dklnltgake gcgtgdcgac svtvdgrlvc
       61 sclmlgveae gkqietvegi adgyvlhplq kkfieyaalq cgvctpgilv aakslleknp
      121 dpteeearyw lagnlcrctg ydkiiravmd taaelreas
//
LOCUS       WP_010441049             750 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Ruegeria conchae].
ACCESSION   WP_010441049
VERSION     WP_010441049.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..750
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78876
     Region          10..749
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 maldhrksif nfvgtrpdrp dgldkvtgra rfgadayapg mlhgailrsp haharivrid
       61 tskaealkdv kaivtradfa vlpfkpgleg efwnvlenvm agekalydgh aiaavaatsa
      121 laardalkli eveyevlphv tdvdnamaad apviregaad ysvpegmhpn vvryhesghg
      181 dveagfaead lviedsfvte athqgyieph aclaslgmdg kgelwcttqg hwyaqkycat
      241 llgietaqlr vtaseigggf ggkttvfiep valalsrkan rpvklvmnrs evfrstgpts
      301 sasmdikigm kkdgtitaaq gifrlqggaf pgapgdltam cafapydltn vrqvgydvia
      361 nrpkqaayra pgapmgafav esvldelcnq lgldpvdvrl knaaaegska sygptyerig
      421 lvetleaaka hphysaplkp gqgrgiscgf wfnhggetsv slalsedgsa qvmvgtpdig
      481 gsrasmalma aevlgipyen irvtvadtas lgyndvshgs rvtyasglat ikaanhavek
      541 lceraaakwg ipvdavkwed gcavpsgpna gdfdplplad itadmgatgg pisghfeatp
      601 egagvsfgth ivdaevdset gktsivrytv iqdagkaihp tyvegqyqgg aaqgigwaln
      661 eeyiygedgr lqnsifldyr ipvasdlpmi dtvivevpnp ghpfgvrgvg etgivpplaa
      721 ianavsnaag vrmkqlpmsp prilaalkek
//
LOCUS       WP_010441125             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Vibrio].
ACCESSION   WP_010441125
VERSION     WP_010441125.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..259
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28502
     Region          1..253
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 miearglgfs vgdkqllkaf nvsfeqgkiy alvghngsgk stllkllakq qnatsgdiil
       61 kdksiakwsd kdfakqiayl pqhlpatdsl sgqdlvsfgr ypwhgllgrl sskdkqyvqe
      121 amqltdtaky adrlvdtlsg gerqrvwlam llaqrtkyll ldeplsaldi ghqiemltli
      181 krlsstlnig viivihdinm aarfcdhiia lhsgellieg evdevfrepv lqdiygvpmh
      241 itqhaagypv ampgdlepa
//
LOCUS       WP_010441138              44 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF2256 domain-containing protein [Vibrio].
ACCESSION   WP_010441138
VERSION     WP_010441138.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..44
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..44
                     /product="DUF2256 domain-containing protein"
                     /calculated_mol_wt=5397
     Region          1..44
                     /region_name="COG4338"
                     /note="Uncharacterized conserved protein, DUF2256 family
                     [Function unknown]"
                     /db_xref="CDD:443479"
ORIGIN      
        1 mhkkpylptk icpvcqkpfa wrkkwercwe nviycsercr rnks
//
LOCUS       WP_010441159             175 aa            linear   BCT 01-JAN-2025
DEFINITION  winged helix-turn-helix transcriptional regulator [Ruegeria
            conchae].
ACCESSION   WP_010441159
VERSION     WP_010441159.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18098347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..175
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19028
     Region          <14..>74
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
     Region          97..>148
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mdikllvklt srawslnila qlhsgvpgrq apllaatgas rtafaasleh lvslgllern
       61 pghghplrpe frltkagvqa aavaaeimal vpddteltll rrswtvpila ltrqprrfsg
      121 lrsdlqvitd ralssslkql eaqdwvrrdi etsarlpfpt yqavnlgcei nrvvg
//
LOCUS       WP_010441215             444 aa            linear   BCT 01-JAN-2025
DEFINITION  sphingomyelin phosphodiesterase [Vibrio cyclitrophicus].
ACCESSION   WP_010441215
VERSION     WP_010441215.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173353
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..444
                     /product="sphingomyelin phosphodiesterase"
                     /EC_number="3.1.4.12"
                     /GO_function="GO:0004767 - sphingomyelin phosphodiesterase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005543 - phospholipid binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49707
     Region          181..443
                     /region_name="nSMase"
                     /note="Neutral sphingomyelinases (nSMase) catalyze the
                     hydrolysis of sphingomyelin in biological membranes to
                     ceramide and phosphorylcholine; cd09078"
                     /db_xref="CDD:197312"
     Site            order(187,219,254,303,343,345,399,435..436)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197312"
     Site            order(187,219,435)
                     /site_type="metal-binding"
                     /note="metal binding site A [ion binding]"
                     /db_xref="CDD:197312"
     Site            order(219,435..436)
                     /site_type="other"
                     /note="phosphate binding site [ion binding]"
                     /db_xref="CDD:197312"
     Site            order(221,223,251..252)
                     /site_type="metal-binding"
                     /note="metal binding site C [ion binding]"
                     /db_xref="CDD:197312"
     Site            order(343,345,436)
                     /site_type="metal-binding"
                     /note="metal binding site B [ion binding]"
                     /db_xref="CDD:197312"
ORIGIN      
        1 mktqwaclsa ilasasfist saiadtdvyl tnntsqamti qtnhtgtdql qfgdewqqhv
       61 eqigpwetkk lisfnrwtgv ksgktyefdt vvsnavgesv tlnqtmkghw ynstlqhgls
      121 aadvnltlhd drnihrsttd afgvnaelal kadstarydd iyytitppkv deqpepgant
      181 lkvmtyniwa lpaiashigd rydlipqyvk gydvlalqev fangrdeflr elakeypyqt
      241 kmldkdgini ydggvvivsr ypivneaqyv fpdctgtdcf adkgvnyaev ikngqayhvf
      301 gthtasfdtd tardyrqrqf kqmrelaqsl nipaseavvy sgdfnvnklk fpgdyqqmfa
      361 nlqadeptys gytastfdpr innfagepms ggenveyldy vlvsseyaak thndnrvdvp
      421 rstsselwkh ynlsdhfpvs avik
//
LOCUS       WP_010441246             280 aa            linear   BCT 01-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Ruegeria conchae].
ACCESSION   WP_010441246
VERSION     WP_010441246.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..280
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30079
     Region          65..278
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mrllrfgpag aekpgllddn gairdlshwi sdisgdalnd eglnkirald hetlplvdgd
       61 prlgpcvgnv gkficiglny adhaaesgms lpdepvvffk atsaivgpdd nieiprssik
      121 tdwevelgvv igkqakyvse eealeyvagy cvvndlserd fqlhrsgqwv kgksadtfgp
      181 igpwlvtkde ianpqdlpmy levnghrfqd gstntmhfgv ativshlsqf mslqpgdvis
      241 tgtppgvgmg qkpetylkpg dsielgiqgl gvqrqqvisg
//
LOCUS       WP_010441281             246 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Ruegeria conchae].
ACCESSION   WP_010441281
VERSION     WP_010441281.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..246
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26402
     Region          1..218
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mtlisvenls vrygantvlr hvdmvveage ivtivgpngs gktsllraii gatkpavgqv
       61 slkpglkigy vpqklhidpt lpisverfmr ltdrvskvkc ekaletagvp dllkrqmsql
      121 sggqfqrvll aralinqpdv llldeatqgl dqpgsaafyh qieevrretg cailmishel
      181 hvvmsasdrv vclnghvcce gspavvasap eyralfgtgt ggalalyrhd hdhdhdhcet
      241 sqeaae
//
LOCUS       WP_010441290             139 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Vibrio].
ACCESSION   WP_010441290
VERSION     WP_010441290.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..139
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15410
     Region          17..136
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mkvfiphnhr rcqvcsqgff sdspicfeva snnenlakhe alakivptdk aegydgimqg
       61 givtalhdat mlhclfqnni tamtvsltsr fhhpiligqe leiraqwvks krniyflesq
      121 itqggklcss aksqfmssl
//
LOCUS       WP_010441328             391 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Vibrio cyclitrophicus].
ACCESSION   WP_010441328
VERSION     WP_010441328.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..391
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=44097
     Region          1..388
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 msaidlfaga ggfslaahqa gldvlaaiel dasaaqtyqk niierleqkt kllngdilki
       61 dpselrkelg lkkgelqlil ggppcqgfss hrikdagvdd prnklllryy dfveefqpka
      121 flvenvaglf wkkhasylek fkqlaedngy vihfcdtlna kdygtpqnrk rafilgvren
      181 vkrdeltfpp apeffnpnsk evkeqnqkpw ktastvfepl taelieqyie khfrlhtkls
      241 ddeartllqg lesgnpvded dpcnvhmkpt ekmqrrfrst rlngsrmdad pefelkchan
      301 gygghkdvyg rviihtpsnt mttgcnnpsk grfvhpwkhh gftlrhaarf qtfpddyift
      361 gsttdqakqi gnavptilgy kliyaimngm e
//
LOCUS       WP_010441350             341 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Ruegeria conchae].
ACCESSION   WP_010441350
VERSION     WP_010441350.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..341
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=36092
     Region          32..318
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mrplialasl lfvsaclfdk epdvvrlsge tmgttfnita igddldeaal gqavqetlaq
       61 vnakmsnwdp nsevstfsas dstepmpvsd efafvieaan evheksggtf dvtlgpliel
      121 wgfgprkped pvpadaeiat alaqvgqarl lildsaartl aksdagvgin lsaiakgygi
      181 davaaqlrda gienymveig gdlvamgend kgeswrigie kpeagtqaiq livpldnlgm
      241 atsgdyknff eqdgvryshi idpvtgrpit hrttsvtvla ddammadawa tamlalgqek
      301 gmeiaeknkl avffisrdvt sgeeayitvq ssafkdalgt n
//
LOCUS       WP_010441359             447 aa            linear   BCT 01-JAN-2025
DEFINITION  S41 family peptidase [Ruegeria conchae].
ACCESSION   WP_010441359
VERSION     WP_010441359.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..447
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47851
     Region          42..369
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mkkfviagla gtvagliatt qiagpllaqe aenkagvyeq ldlfgdifer iraqyveeve
       61 sdelieaaid gmltsldphs sylspddaeq mrvqtrgefg glgievtqee gfvkvvspmd
      121 dtpadaagie agdfithvdg esilgltldk avdlmrgpvg seivitvvre geqepfdvti
      181 vrdtikltav rartegtsvv lrvttfndqt fpnlkeglee qieeaggien vngvvldlrn
      241 npgglltqai kvsdaflneg eivstrgrnp edgerfnatp gdltggkpiv vlinggsasa
      301 seivagalqd hhraivvgtk sfgkgsvqtv mpirgdgamr lttsryytps grsiqalgvs
      361 pdiiveqprn rpdeededda nartrseadl rgslnndsls edeirqieed rakaeatael
      421 reedyqlaya idilkglsaf nptgpsq
//
LOCUS       WP_010441385             309 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Ruegeria conchae].
ACCESSION   WP_010441385
VERSION     WP_010441385.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..309
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32309
     Region          1..309
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mveiflrtlp ffaiiglgfc agrsrffppe atayltkfvf ffalsamlfr faatlpfaei
       61 fngrlvigyl igtagvyala tavaylrgld iptaaveaqc aaignvgflg lpmlallfse
      121 aaigpvmlvl tvdlvvfssl ivilinggrd grlglatvrl igvgllknpm ilsisagliw
      181 safnvpvpap lndfltilgg aatpgalfai gasladksae riqiagwlsi cklvlhpffv
      241 almviwlipv asfpamvaia aaslpvagnv ymlaahyrva pqrasaaill stlasiltvp
      301 lvigwvstl
//
LOCUS       WP_010441432             245 aa            linear   BCT 01-JAN-2025
DEFINITION  creatininase family protein [Ruegeria conchae].
ACCESSION   WP_010441432
VERSION     WP_010441432.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..245
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=26321
     Region          2..243
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mkldhmtwye vdarinqgaa vllpvgsteq hgpmgrigtd ticaeavala aasrcggiva
       61 pplaytpapf ntgfpgtvsv saevfqmlan eviagllaqg frgvfvvngh ganleplrti
      121 kstlldnqli irswwepdtv ntlrrqlyge wegmhatpse iaitqsllgv lpanlaaepp
      181 rkltaeyvrd hagdrhgppd ehraefpdgr vgshsalanp kdgkrlltma aiaianefrs
      241 feqdr
//
LOCUS       WP_010440427             348 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Ruegeria conchae].
ACCESSION   WP_010440427
VERSION     WP_010440427.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..348
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=38083
     Region          13..339
                     /region_name="AKR_Tas-like"
                     /note="Escherichia coli Tas protein and similar proteins;
                     cd19094"
                     /db_xref="CDD:381320"
     Site            order(19..21,26,48,53,89,131,182..183,208,236..242,245,
                     247,256..258,292,309..313,317,321)
                     /site_type="active"
                     /db_xref="CDD:381320"
     Site            order(48,53,89,131)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381320"
ORIGIN      
        1 mdmkplgrtg imvsdlclgt mtfgtqtsea eahrqmdtal agginfvdaa emypvnpisk
       61 etvgrteeil gnwnaanrsr rgdyvlatkh sgegfvharn gapisketip eaiegslrrl
      121 qtdcidlyqf hwpnrgsymf rqnwdyaplg hnrdeivdem reslialqaq vdkgnirafg
      181 lsnesawgta qwlrasdevg gprvasiqne ysllcrlfdt dlaelclled vgllsfspla
      241 agfltgkyqg gavpegsrma lvpnmggrkt drvfdavaay ldiaqrhgld pihmslawcc
      301 srpfmgstif gattvaqleh ilagkdlkls pevlveisaa hrafpmpy
//
LOCUS       WP_010441438             671 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Vibrio].
ACCESSION   WP_010441438
VERSION     WP_010441438.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..671
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75508
     Region          512..660
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(544,587)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(549,552..553,557,561,583,585..588)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(579,610)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mglvllacsl lpvyvagqli lnqqsqssle qkeiklanst igieqtvfdk vnliasltqw
       61 ysqdrslika ggniffssvv wdkmdsfnsl adsvsatyil drywkpiyds kgslyhfeks
      121 qlledlkqpl ltykqgklfh teftepelvd dasagiafva pilpyrlieg ssytpqgylv
      181 vlmgydrles kvtpflyene svefnhvphs glertsvert naentasetk lvsigndlfs
      241 aplrlsikhn vsdsarllem qqseavfvki lfatlaiaiv calllsrlfs qqlnlltesv
      301 gsyssnklpn hkleehrfte fftlssllgk mwariqhqls eltvrneqli sanyqiaesn
      361 nklenfniql ektveektss layslarees hkhrilkivq fasmrksvey rlipelvnvq
      421 lvsilpnccm qfsfsdkpes skalldskal lgskvlldsk vlvdskgati gyfvskefdr
      481 lseedvlifd lyqkqlagwi elenitrvnm qtgcynrkaf nedfefskrc vvnnrdtlsl
      541 fiidinglkn tndvyghevg dqliqcsvev irkrldsmsn lyrlggdefg iltlsghgqd
      601 lqsagslvqc lyadqegqvi eakagisipv rfsigsscse stdldnlfav adedmykqkr
      661 hyyqsllstd k
//
LOCUS       WP_010441472             438 aa            linear   BCT 01-JAN-2025
DEFINITION  MlaD family protein [Ruegeria conchae].
ACCESSION   WP_010441472
VERSION     WP_010441472.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..438
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46938
     Region          1..240
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 metranyili gaftlagilg afgfflwlak fevtrqyayy dvlfdnvsgl saaggvnyng
       61 lpvgqvisld ldkddpskvr vrleidagip vtketiaqlq slgvtgvayv elsggsptaq
      121 klpqnsvits krssiqslle gapevlekav tllenlnsvv dennrkavsd ilnnlaeasg
      181 kldktltdfq slssdlggaa kdvgeftkrl dtlantaett lstgtdtlks iketsetakt
      241 tletantaia saenviqeei rpfvergsil aerltrlsde gsltlsvise tvlnanttle
      301 svtstmnsak galdsaeraf dsanrvmded ispvaadvsk aanqvaetvs nitekideis
      361 ddvlsasksa sdllgtidgv vqdnrrqvsd flrvglpqfi rfieesqrlv isldrlvdkv
      421 erdparfllg tqasefrq
//
LOCUS       WP_010441487             817 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Vibrio].
ACCESSION   WP_010441487
VERSION     WP_010441487.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 817)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..817
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=90884
     Region          132..369
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          571..786
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mswpvvkall ghyrryplqi ilvwlgltlg vsllvgvtai nqhakqsyah geklfsnplp
       61 yrirpkhnan kipqgfyiql rregfqqcsp fdhhritden ganfmligld pvsmlqlqpg
      121 valkdlttln lmkppypilv sddlaehmew khgdyihlmd gselgpvavd qdniingtrl
      181 iadisllrml krsaglsvia csdmptekfe rlknmlpngl titrsskael esltsafhln
      241 ltamgmlsfv vglfifyqam slsfiqrqpl vgilrqtgvs gwqlakalcl ellilvllsw
      301 icgnifglml anqllpavss slgdlydanv gltlswswrw sgysllmall gaflacawpl
      361 vrllksqpir ltsrlslmrf agteftwqal mgcgfcvaav avyqapqtqe tgfaiialml
      421 vsvalftpfl mwklfnslsy slrwvrarwf fadaassmsy rgvatmafml altanigvet
      481 mvgsfrdttd kwltqrlaad lyiyptnnaa armsnwlsdq pevdsvwwrw ekdvaspvgs
      541 iqvvstgpse gelealtikl gipnywyhlh hskgvlises mslklgirpg dyidlydslg
      601 sgwqvvgvyy dygnpyhqvm mshrnwlygf agrgnvglgv ilkddvnaig lrsrlenvfr
      661 lgserifdnn nihsqamrvf drtfaiadtl gnitlviavf giffatvage vsrqrhislq
      721 rclgvsakel iltgslqlfv fglissliai plglalasli vdivikqsfg wslelqvipw
      781 dylvtfawam aalmlagalp vmrmirntpm kslrdal
//
LOCUS       WP_010441490             411 aa            linear   BCT 01-JAN-2025
DEFINITION  lytic murein transglycosylase [Ruegeria conchae].
ACCESSION   WP_010441490
VERSION     WP_010441490.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR02283.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..411
                     /product="lytic murein transglycosylase"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009253 - peptidoglycan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45017
     Region          1..336
                     /region_name="MltB"
                     /note="Membrane-bound lytic murein transglycosylase B
                     [Cell wall/membrane/envelope biogenesis]; COG2951"
                     /db_xref="CDD:442193"
     Region          354..409
                     /region_name="PG_binding_1"
                     /note="Putative peptidoglycan binding domain; pfam01471"
                     /db_xref="CDD:460223"
ORIGIN      
        1 mrfvftvlfl ivlaapllaq drvfverqfq swlqktvwpq akakgvskqt frqafdgvkl
       61 nwdlpdlvpp gspqktpkvq rqaefgspgr yfnaesvqga tsvgrkmarr haetlarvea
      121 etgvpariil aiwgresgyg qvpirhdafq vlstkgfmst radyftaeli aalqiaeagh
      181 aqgrelkssw agalgqpqfm ptnfltyard gdgdgradiw gsaadtiasi gayleehgwi
      241 adrdwgfevn lpntvscale gpdqgrlird waamgvsrvs gkpfpahela aegylmmpag
      301 qsgpafivtp nfyvlkdynt sdlyalfvgh vgdriqygvg dfhgrwgdvg nlyrsdivtm
      361 qqvlveqghd vggidglpgy ktrrsigrwq aasgraptcf pndrlkaalk p
//
LOCUS       WP_010441559             310 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Ruegeria conchae].
ACCESSION   WP_010441559
VERSION     WP_010441559.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..310
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32178
     Region          1..308
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mltiltsilp ifliialgla lrkggipstd fwnlndklvy wvlmpcllft kislspldks
       61 alglysmtil ggflaalvfa visarlmgya apqatsilqg sarhnsfigl alaanlygpv
      121 gfdiailata ilvpitnivm vvmmvgalkq dtatrlpiai lrelgrnpyv isillaigan
      181 qmigdripvv hevadilgag alpitllavg anlrvramaa salplmlaiv gkmmvfpvaa
      241 lcigilvglp qdvlqiavvy svvptgassy tlskqlggda plmaaivtlq tliaavsipi
      301 slaillplig
//
LOCUS       WP_010441576             192 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Ruegeria
            conchae].
ACCESSION   WP_010441576
VERSION     WP_010441576.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..192
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /note="This protein belongs to a clade of uncharacterized
                     proteins related to peroxidases such as the
                     alkylhydroperoxidase AhpD."
                     /calculated_mol_wt=21238
     Region          41..187
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msawirmisd edadehlknt ldlartphgt vdnvmrvhsl rpntmkghvi lyraclhdda
       61 nsvpmwfqev issyvstlnt cpysyanhwa narhligdda radsieaalt ahrpqdafeg
      121 ahlealsyae kltlspgtme esdvdalkna gwedgeilei nqivgyfnya nrllnglgvt
      181 tkgdvvgyyg ed
//
LOCUS       WP_010441590             177 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter small permease [Ruegeria conchae].
ACCESSION   WP_010441590
VERSION     WP_010441590.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..177
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19603
     Region          4..166
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtamrglrsv ldfiylaagv laalsliail vlivvqmlar wtgevfpgap dyagyamaaa
       61 sflafanaln rgshirvsil lnavpdgfrr ileiwcfaig saimwyfcwy ayrfvywswk
      121 fndisqgqdk talwipqstm ligavilaia ltdhlfhvlf kgdhgitrdl adqshge
//
LOCUS       WP_010441607             478 aa            linear   BCT 01-JAN-2025
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme [Ruegeria
            conchae].
ACCESSION   WP_010441607
VERSION     WP_010441607.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 478)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..478
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=51518
     Region          39..448
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 msladfrssl ksdnlvrnlr egvigdgasi pglfgevslv yadyvasgra laqvedyire
       61 svlpyyansh teasfcgsfm trlraearae isrltnaagc stiftgsgat sglnrlvalf
      121 gindaakavv figpyehhsn llpwreskae vveipeaaeg gpdlalleaa lkdhadadvk
      181 igsfsaasnv tgivtptdev trllkshgal svwdyagagp ylpidmnpad dcqkdavvvs
      241 phkfpggpgg sgvlivrddt vcldipswpg ggtvtfvspw dhryssdiaa reeagtpnvi
      301 gdiraalafi ikdeisqafi sareaemnem alkawsknpq lallgvghph rlpifsfrvs
      361 radgsrfhhq lftrmlsdvy giqvrggcac agpyahrlle igqpeseqlf sdlrdgkell
      421 kpgwvrlnfs ylmddakvqy iidcvneltg rldelevrym sdpatarfai nsdaleva
//
LOCUS       WP_010441619             261 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ruegeria conchae].
ACCESSION   WP_010441619
VERSION     WP_010441619.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..261
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28378
     Region          7..245
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtkqsfliae nleyyalngd illqgvsfal degailaiag pngagkttll nllcgaeala
       61 lgdvrmngqs lkhlsakera rmiavvsqqe fpdgrlslrd yvalgqipir adrsaedhar
      121 elnrildlth lgmladkrma qlsggerqra hiaralaqnp sllfldeptn hldpdakgrm
      181 lslvadlgvt vvmivhdlvm ipefathval mksthltgfg tvaevltper vretfgvdyl
      241 cfhhegrvip aldirrttvs t
//
LOCUS       WP_010441631             136 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Ruegeria conchae].
ACCESSION   WP_010441631
VERSION     WP_010441631.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..136
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14447
     Region          1..132
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mynhilvpva pdhindcsls ldaasrllad ggtvsvlsvl eelpsyigsy fpaeqvqksv
       61 sefeerlgta veasnisthv vtghptnsil dwaekhkadc iivashqpgl sdyligstaa
      121 rvvrhaqcsv vvlrgk
//
LOCUS       WP_010441655             479 aa            linear   BCT 01-JAN-2025
DEFINITION  CpaF family protein [Ruegeria conchae].
ACCESSION   WP_010441655
VERSION     WP_010441655.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..479
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52635
     Region          90..466
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mfsrykkqps aqpvqtpape kaeaatpaaa aastnvvrkp vqkkaaevtv ndkerkrker
       61 lgeiklelhr ellenlnlaa lekaaeaelr aeisaissev lesrnivlnr edrtqlnkel
      121 ydevtglgpl etllqddtvn dilvngpqqi fveragklei sditfkdekh lmriidkivs
      181 avgrrvdesn pyvdarladg srfnamvppi avdgslvsir kfkkdklgid dlvnfgafte
      241 emaaylqaav strlniivsg gtgsgktttl nalssfidda eriltiedta elqlqqthvg
      301 rmesrppnve gkgevsprdc lknalrmrpd riivgetrga evidmlqamn tghdgsmtti
      361 hansardgis rlenmiamag iempikavrs qissavnliv qasrlqdgsr rmtsiteitg
      421 megdvislqe lfkfqrvglt pdnkiighft atgvrsnfse rfrlwgfdlp asiydpttm
//
LOCUS       WP_010441663             288 aa            linear   BCT 01-JAN-2025
DEFINITION  lytic transglycosylase domain-containing protein [Ruegeria
            conchae].
ACCESSION   WP_010441663
VERSION     WP_010441663.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..288
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30105
     Region          45..269
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 myfrdamfca gavaflltga isvsateiep rgvykrikap kpgtrprvti qitpeqhaas
       61 psapstgakl dvpevttpap vppsnppkia gttepvgtye afwsrispel qqasagrlae
      121 avqalsatdv aaprlqtlqd iadargvdil rstvgtnvsp alvlavisve sagktqavss
      181 agaqglmqlm pataerfgve dslkpeqnie ggvkylhwlm eefdndpilv lagynagega
      241 vhkhsgvppy aetrdyvpkv laafqvasal ctsapqfvsd pcvfqaan
//
LOCUS       WP_010441678             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Ruegeria conchae].
ACCESSION   WP_010441678
VERSION     WP_010441678.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10605654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..272
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29863
     Region          53..219
                     /region_name="Lactamase_B_3"
                     /note="Beta-lactamase superfamily domain; pfam13483"
                     /db_xref="CDD:433247"
ORIGIN      
        1 mwrvvavlmm isggavaqer rpshciaiad aapgieylhk aawqdpvpef svrisyvaha
       61 sfliqtqggl navtdftgfi ggaalipdvv tmnhahsthw tahpdpaipy vlpgwgefgq
      121 giehhldlge llvrnvstdi rsayggveer gnsifvfele glcighlghl hhipsdkqfa
      181 algrldvvma avdggttmpl pemiqvlkrl kssiiipmhw fsdfslerfl vdiredfpve
      241 rdgvselivs lrtlpdrptv vvlepqylie qe
//
LOCUS       WP_010441704             387 aa            linear   BCT 01-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Ruegeria conchae].
ACCESSION   WP_010441704
VERSION     WP_010441704.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..387
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39241
     Region          1..387
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mtrafppmqt vstglvvaiv gffssfpivl qglnamgass qeaasglmsa aiamglaaiv
       61 lslfhklpis vawstpgval lavsatpteg fsgaigaflc agaltvlagl wkplgrlaaa
      121 ipitlaqaml agvllplclv pfkatveipw qalpviltwf iagrfnrlia vpaavvaaai
      181 ivslnagdaq lmpdrliaap vwtmptfsva saigigvplf ivtmatqnip gvavmrsfgf
      241 dpvpgrlfss vggasmlsap fgapatclaa itaamcsned shpdpaqryw savmggvfyc
      301 lfgifavait sfaahadpll mgtlagvali gvmanamhaa ldipaereaa iltlvitasg
      361 itvfglgaav wgllaggiay vvtnrvr
//
LOCUS       WP_010441718             321 aa            linear   BCT 01-JAN-2025
DEFINITION  pirin family protein [Ruegeria conchae].
ACCESSION   WP_010441718
VERSION     WP_010441718.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..321
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35801
     Region          25..284
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mswnpthnpe casekdalet liiprardlg gfevrralps vkrqlvgpfi ffdqmgpaef
       61 itdsgidvrp hphiglgtvt ylyqgefehr dslgthqmih pgevnwmvag rgvthsertr
      121 aetrgkrhnl fgiqtwlalp eayedmapdf ehhkqgalph iedkgvsarl ilgaaygets
      181 pvtmlsetfy vdvqldpgas fplpddhedr gvyvtqgsve vagdtfdegr mmvfrpgdkl
      241 svragplgar lmllggatls edryiwwnfv ssskekieta trewntadwa ngafhlppgd
      301 dqefitipde lertrprlar v
//
LOCUS       WP_010441793             551 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Ruegeria
            conchae].
ACCESSION   WP_010441793
VERSION     WP_010441793.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..551
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=60801
     Region          133..531
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 msrlriasgl vlfvfaffhf iniglglfht dllhgmqggr kavnrheigs iviygallmh
       61 mglalvslaq rrtlrmpfsv alqvilglli plqlvshlvq tryaheifgv ndemgyiiil
      121 mwpstaiwfq slllllvwih gciglhmwlr lttwwralvp yligiavfvp gfafagllte
      181 grriwadfad pdlreqyieh ynwpsqdefq alfavkdyaq wvfwaalalt gmvylgrklw
      241 rrrhsvrvry vngpevvsek gmtllemsra ngiphtalcg gkgrcttcrv vveegadqlh
      301 pptevearsl kavsapkgtr lacqmrptdp ltvfrvfrpd gardrahasq gqerqlavlf
      361 ldmrgftart tgqlpydivf llnrffdaiv paitaqggvv dkymgdglla mfetanaass
      421 asaglraaag igralerfnq qleaegsqpv rigmglhlgd lvlgeigaak haprtiigda
      481 vnvasrleae tkalgvellv sdkvldaagl qcdprdlref slrgvsepvp alpvrhaayl
      541 esqttpleqi a
//
LOCUS       WP_010441796             166 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010441796
VERSION     WP_010441796.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..166
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18392
     Region          5..144
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mvatrldeid rkilaelqad grmtnvelak rvgisappcl rrvrtledsg yihgyhadvn
       61 arelgfevqv famvglesqa eselsafedr crewplvrec hmlngevdfi lkcvapdlss
      121 fqqfltgell ttpnvasvkt slvirgakde pgvpfdvled rmnqta
//
LOCUS       WP_010441818             223 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Ruegeria
            conchae].
ACCESSION   WP_010441818
VERSION     WP_010441818.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..223
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=25555
     Region          112..200
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mskntewvet patnqrlrie filfyvavpv liatlfppsw mfpslfaftg lgilllqdtp
       61 gfswaelryg wrnwswtevv afalfmaafc salvlwarpd aafalllyrp emlifiwigy
      121 pllsalpqel lfrslffrry hsilpqeraa yllnaglfsl ahlmywswvv aimtfaggll
      181 ftwayrkrgs ffyavllhai agniifaagl gvyfysgnvq rpf
//
LOCUS       WP_010441852             273 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010441852
VERSION     WP_010441852.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..273
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29778
     Region          19..270
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mesqkrprgr pksmfkessa gtmqsldral gvlttvagle rvalsdlare vdvptatthr
       61 ilvtlqkhgf vsfdeerqew mvgieayrtg asflrrnnvl eigrpilrrl mldsgetanl
      121 avpdgpevvf vgqvetqnpi raffppgart pmyasgtgka ilaalseesl nkvlartdli
      181 aftentnlpq aglhddlaet rrrgwsydhe eryegmscig aaifndraep cagisvsgpt
      241 vrfsldrape lgmlvrnaaq eithlsggrs psq
//
LOCUS       WP_010441956             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ruegeria conchae].
ACCESSION   WP_010441956
VERSION     WP_010441956.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..228
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24199
     Region          1..228
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mndvtlrlsg lsktylpgtp geiqvlrgad lelrageava lvapsgagks tllhiaglld
       61 tpdtgeveia gqgamgkgdr trtairrrdv gfvyqfhhll peftalenii lpqlangtse
      121 kaaqvramql ldrvgvsara ehrpaalsgg eqqrvafcra lankprvlla deptgnldpe
      181 tsdqvfaalm alvrdeglsa liathnldla armdrmlrle ggvlrpae
//
LOCUS       WP_010442030             453 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Ruegeria
            conchae].
ACCESSION   WP_010442030
VERSION     WP_010442030.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..453
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47948
     Region          <197..301
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          298..452
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 mnaksgsggs gtfiwglvag ivvvlvaggl ylsglfdrpq elaepeavet sepnvtakqe
       61 aeepadiqpd eqtteasepa patpvesteq aavieeeqvq ereepetpvl aspvldqifv
      121 esdgngllsg saepgaevnv lldgetihrf tvdasgqfae fvsipfgdda rglvletrsg
      181 estsrsddyl iaalpepvsp vesepsadep vkevaeaqtv vtetndqqaa dqaeteenes
      241 evagtvsppa dqaapatetq setvdvpdqq vailrsgeeg velvqpptvl dtppeqiald
      301 tigysdvgdv eltgraqdgs avrlyldnkl vadlepatdg qwrgevegid pgvytlrvde
      361 vapdgtvvsr letpfkrepv ealraaette agetpsgtpa irsvtvqkgd tlwaisrdrf
      421 gdgvlyvklf eankdsirdp dliypgqift ipe
//
LOCUS       WP_010442080             161 aa            linear   BCT 01-JAN-2025
DEFINITION  lytic transglycosylase domain-containing protein [Ruegeria
            conchae].
ACCESSION   WP_010442080
VERSION     WP_010442080.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..161
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=17567
     Region          <46..134
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mtpllrrsvl tllliaplaa cggpnasggt dtsdpplypn etpelrasin kwadhyelpr
       61 elvhklaire sthrpwavnr pyygllqilp atarsmgyag naqglldadt nlefagkylr
      121 gawllsdgdq qraiflyakg yypeakkrgm lvetglvsat k
//
LOCUS       WP_010442119             291 aa            linear   BCT 01-JAN-2025
DEFINITION  potassium channel family protein [Ruegeria conchae].
ACCESSION   WP_010442119
VERSION     WP_010442119.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..291
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30947
     Region          <140..190
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 madnsdaras wfrdiifpll illgfliicv lrprellafg fevwgyelpp fpiilivata
       61 aglasisahf srhipnwaaw saillgaflt ilafaalnsv vgvyctaaic pgasayvfqd
      121 glpvlvpdgy vgetvmidks frnalyfsvv tfttlgygdm qpspnfrlya gyqavlgyly
      181 lgmivgivid hgvnsrdsgs gsggqtagda ekgrtpkpas pkgtptsnrf aavlqrhfgh
      241 isavracfsa itlylalwga satayglpgf ylpaliqvpi ifggiiwisl g
//
LOCUS       WP_010442136             428 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Ruegeria conchae].
ACCESSION   WP_010442136
VERSION     WP_010442136.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..428
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45242
     Region          20..364
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(22..23,26,58,108..109,111..113,116,136,139..140,143,
                     210,213..214,217..219,222,246,250,300..301,305,309,325,
                     328..329,332..333,336)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mlqvlssawa lllgmgllmv gnglqgtllg vrgeiegfst lemsfvmsay fvgflggsrl
       61 apemirrvgh vrvfaalasf isavmimypm ladpiawslg rvvigfcfsg vyvtaeswln
      121 naannenrgq alslymivqm agvvsaqall lvgdpagyet fviasilvsi sfapillsis
      181 ptpafdttkp mtlrqlmets plgcvgmfll ggifsaqfgm savygaqvgl slveisifva
      241 vfyigavllq fplgwmsdrm drrvliilvs avggvgavig mvlgvtftml lvaaffiggm
      301 tsplysllia ytndyleydd msaasgglvf inglgaiagp iitgwlmgtg vvgpkgfflf
      361 iatlmfamaa yaayrmtqrv ytpvdetgai apiyptsspv alevaqevai eaaqdeqdaq
      421 eptrapel
//
LOCUS       WP_010442148             387 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Ruegeria conchae].
ACCESSION   WP_010442148
VERSION     WP_010442148.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..387
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41818
     Region          1..379
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mrnstrsgvd pfivmdvmea arkaeeagrh vihmevgqpg tgapkgatea lakameqgpl
       61 gytvalglpa lrqriarlyg ewynvdlnpe rvvitpgssg gflltftalf dsgdrvgiga
      121 pgypsyrqil kalglvpvdl ptapenrlqp vpadfagldl qglmvaspan ptgtmldhaa
      181 mqalieaaqg qgasfisdei yhgleyeaka ftaleltdec yvinsfskyf smtgwrvgwm
      241 vvpedqvrvv eriaqnmfic aphasqvaal aamdceeelq anldvyrrnr llmldglpka
      301 gftniappdg afyvyadvsd ltqdsrafaa eildkagvav tpgldfdpvr ghttlrfsya
      361 rstediqdgl drlqrfmaer gaipqta
//
LOCUS       WP_010442161             215 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Ruegeria conchae].
ACCESSION   WP_010442161
VERSION     WP_010442161.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..215
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23259
     Region          8..124
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
     Region          146..202
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msdtttrvli vddhpmvaeg iqsllesfde idvvgtlsng qeavdqatql epdvilmdln
       61 mpglsglnat eiilerlpet rililsmhds peyistalsh gakgyilkdv pteeikqaid
      121 avmrgerylc tgargslepk egdtrealtg reqtillela qgksnkevaq sldisvrtve
      181 thrknikrkl gisstagltr yalehgvlqg tspgl
//
LOCUS       WP_010442203             279 aa            linear   BCT 01-JAN-2025
DEFINITION  2OG-Fe(II) oxygenase [Ruegeria conchae].
ACCESSION   WP_010442203
VERSION     WP_010442203.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Chowdhury,R., Leung,I.K., Tian,Y.M., Abboud,M.I., Ge,W., Domene,C.,
            Cantrelle,F.X., Landrieu,I., Hardy,A.P., Pugh,C.W., Ratcliffe,P.J.,
            Claridge,T.D. and Schofield,C.J.
  TITLE     Structural basis for oxygen degradation domain selectivity of the
            HIF prolyl hydroxylases
  JOURNAL   Nat Commun 7, 12673 (2016)
   PUBMED   27561929
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..279
                     /product="2OG-Fe(II) oxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=32389
     Region          38..225
                     /region_name="EGL9"
                     /note="Proline 4-hydroxylase (includes Rps23 Pro-64
                     3,4-dihydroxylase Tpa1), contains SM-20 domain
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG3751"
                     /db_xref="CDD:442965"
ORIGIN      
        1 maiyqidper lsisvenara aaapfaeeyq sgepynhici dnflpeevlr kvqkdvatle
       61 egedsdtfer aqenlktqyn perlpvysre lfhafnsrpf ilfleemtgi kglipdpyyi
      121 gagihrvkng ghldihadfn lhkqmvverr lnvliylndd wreewggsfe iwsndmttkv
      181 ksfvptfnrm ccfstgtstf hgnpekvnhp dgeprqsial yyytatwdps rkahstifkp
      241 rpgtedqfdr qshrqevlen wlppvvyrri yprlarlgf
//
LOCUS       WP_010442236             255 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010442236
VERSION     WP_010442236.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..255
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28666
     Region          <115..255
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mfdwmeeagr vvekigtpef pcaladglrq vapfdftvvf ghvgteapid lhddfpkskr
       61 rifvqdyqag pyvldpffla atkpitpgly rmrdiapdrf yqgeyyrsyy krtglaeeig
      121 yfidipstgm vvvslmrsvk pfsakeirhl halwplvraa cckhwsdfpt mtrgaaangv
      181 srrvdlafqa fgdgvltpre revveftlkg hsaeavgtil gispgtvrih rrniyaklri
      241 nsqgelfskf iekal
//
LOCUS       WP_010442240             284 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Ruegeria].
ACCESSION   WP_010442240
VERSION     WP_010442240.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria
  ORGANISM  Ruegeria
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 284)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Ruegeria"
                     /db_xref="taxon:97050"
     Protein         1..284
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31174
     Region          4..282
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtnrlksvil lgpglgwlal lmvvpcglif tyaffergiy ggidhvftfe nfvratdply
       61 lgiflrsaki aflttiiail iaypaayait laprrwqtgl lilvilpfws nylirtyawi
      121 vmlnreglin ntlqgaglid eplsllynnf avivglvyny tpfvvlaiys slnrinveti
      181 easedlgapa wttfhrvilp qtvpgiaagg vfvfvlsign fitpdllggg rlqmvgnliy
      241 dqflsardwp fgatlsmfli aimmgllfaq avlanraagq rgqd
//
LOCUS       WP_010442242             353 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ruegeria conchae].
ACCESSION   WP_010442242
VERSION     WP_010442242.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38510
     Region          5..351
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnqgvqlrni tkryglvtai dnvsldirdn effallgpsg cgkttllrtl agfetpqegq
       61 vivagqnvtn irpsrrplnl mfqsyalfph msvekniayg lemeklpkde iatrvaevle
      121 saklsgfagr kpdqlsggqr qrvalaralv krpkvlllde plsaldkklr eemqlelkrl
      181 qhevgitfli vthdqeealv madriavlhd gklaqvgtph elyehpgsrf vadfigvmnf
      241 lngnavdggv dvdgagmlrg vselrgaati avrpervslm qtapqdgrnc lpgtveevay
      301 hgsdlgvhvr vrggrstlsa rvpagqadre siqpgqdvyc vwdakhsril pnc
//
LOCUS       WP_010442245             114 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Ruegeria].
ACCESSION   WP_010442245
VERSION     WP_010442245.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria
  ORGANISM  Ruegeria
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Ruegeria"
                     /db_xref="taxon:97050"
     Protein         1..114
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12824
     Region          15..114
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mttprmqnpl qqtdlvdwgv iptmiegqsr tsgklihkgp dgqsecglwv ctpgkwechv
       61 tkdefchfle grctyvhesg evieitpdta affpqdwkgv ctvhetvkkv ymir
//
LOCUS       WP_010442276             244 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010442276
VERSION     WP_010442276.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..244
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26954
     Region          16..225
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtdilesplt kklqvflals edeldvlkrl hlrrrsftag rdlvhqgqsd qaayilaagw
       61 vcsyklqpdg trqivdfqip gdflglrsvl lrtsdhsfep vtdiqavevl vddlldaftk
      121 tprlaaaflw aasrdeamvv ehlvgvgrrs adarmahfll elgarlklvg mgskegyacp
      181 ltqyhladal glsavhvnrv lrklresgll tfqdgrvtfd nydglvgfsg fdpayldqtd
      241 pllk
//
LOCUS       WP_010442295             250 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010442295
VERSION     WP_010442295.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..250
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27848
     Region          21..234
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mkeehlrtik nspltrklsn fvaltevela vlarlhkrrr tfeagrdlvh qgqseqaayi
       61 lasgwvcsyk tqtdgsrqiv dfqipgdflg lrsvllhtsd hsiepimeiq aievvvddll
      121 eafaqtprla tailwavsrd eamvvehlvn igrrdagerm ahfllelgvr ltqvgmatkm
      181 gytcpltqyh ladtlglsav hvnrvlrqlr ekglltfqsg qvvfddydgl vtlagfdpty
      241 ldqagpllkq
//
LOCUS       WP_010442344             349 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ruegeria conchae].
ACCESSION   WP_010442344
VERSION     WP_010442344.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..349
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37879
     Region          1..348
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mielqdatkr vgnvihikpt nltlqtghfn vllgatgsgk tslikmmagl dpmasgkvcm
       61 dgqdvtklst qkrqislvhq ffvnyphmtv fdniasplrv agmakseivg rveeaadllq
      121 lrpmlhrrph elsggqqqrt alaraiakes ravfldepla nldyklreel reqlpdlfag
      181 rgavvvyats epeealllgg ytalmedgrv tqfgptaniy rnpeniaaar vfsdppvnva
      241 ritvsgaqaq laggggwavt dmadgdymva vrphrvtpfr ssdddveltg rvivtelsgs
      301 dssahfqhgd dawvslasgv hpyqvgedhs fymnpahcry fgqdgkrva
//
LOCUS       WP_010442343             358 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ruegeria conchae].
ACCESSION   WP_010442343
VERSION     WP_010442343.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..358
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39422
     Region          1..346
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maqiklsnlr hsympapkgp edyalkeidv twrdggayal lgpsgcgkst llniisgllt
       61 psegqilfdd rdvtalppdq rniaqvfqfp viydtmtvge nlafplknrg vdpamikrrv
      121 deiaemldvt dmlntrasgl spdnkqkism grglvrddvn avmfdepltv idphlkwklr
      181 sklkelhqrv qatmiyvthd qtealtfade vvvmqegevv qigtpvelfe rpqhtfvghf
      241 igspgmnvlp ceakgdravf eghevilegp thgdggrtdl girpeyvgfg dsgipahvtk
      301 vsdigrhyvv samvgntplk avtehsvpep gsqvylqfkp eqsrvyrdgw iateeral
//
LOCUS       WP_010442432             459 aa            linear   BCT 01-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Ruegeria
            conchae].
ACCESSION   WP_010442432
VERSION     WP_010442432.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..459
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49154
     Region          3..271
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mglfliaflw llsfaplqgm aapyaamvid artgevlhsr nadtrlhpas ltkmmtlyia
       61 feavrngeit ldtqvritkk aaaeppsklg lrtgqriafr yliraaavks andaataigi
      121 alsgseaafa rrmtrtakam gmsrttfkna hgltesghls tardmttlgr hllydypqyy
      181 nlfsrqstha giktvpntnr rllaaykgad giktgytraa gfnlvasakr kderiiatvf
      241 ggksgasrna rvaelldmgf rrapsrapir kparpsyagn aglgavqvaq vgppkkslrp
      301 vlrpteasav qvagavaeta ekngsriqdg iaaaiaaadi apadsatrpv srpedvvlas
      361 veparqpepe pevvtrlsts gghlwgvnvg ryttryeaek vllktalsem ttlegtlrkv
      421 nqsargfdat fqgmtreqad lacrrlqarn vtcfmigps
//
LOCUS       WP_010442452             103 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ETC complex I subunit [Ruegeria].
ACCESSION   WP_010442452
VERSION     WP_010442452.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria
  ORGANISM  Ruegeria
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10521567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Ruegeria"
                     /db_xref="taxon:97050"
     Protein         1..103
                     /product="ETC complex I subunit"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_process="GO:0001932 - regulation of protein
                     phosphorylation [Evidence IEA]"
                     /GO_process="GO:0006120 - mitochondrial electron
                     transport, NADH to ubiquinone [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /GO_process="GO:0032981 - mitochondrial respiratory chain
                     complex I assembly [Evidence IEA]"
                     /GO_process="GO:0042776 - proton motive force-driven
                     mitochondrial ATP synthesis [Evidence IEA]"
                     /GO_process="GO:0072593 - reactive oxygen species
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=11711
     Region          2..96
                     /region_name="NDUS4"
                     /note="NADH dehydrogenase ubiquinone Fe-S protein 4;
                     pfam04800"
                     /db_xref="CDD:461433"
ORIGIN      
        1 mrariyqpsr namtsgmakt rkwvleyapa sarevdplmg wtssndtqtq vrlkfdtkee
       61 aldyakdngi daqvsephkr kpnlrargyg enfatdrrap wth
//
LOCUS       WP_010442479             842 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Ruegeria conchae].
ACCESSION   WP_010442479
VERSION     WP_010442479.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 842)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 842)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 842)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 842)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 842)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 842)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..842
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88363
     Region          1..840
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mslrlagrla rrelrgglrg frvflaclal gvaaiaavgm vrqaiqtglq qegasllggd
       61 aqleftyrfa ndqerawmek tahavsevvd frsmavtgng tntqrgltqv kavddaypll
      121 gsailepelt ltdafagadg lpgavmapsl idrlnlmvge qfelgtqrfv lmaslehepd
      181 gaadgfslgp rtlvrtkdlq ssgllapgtl fstkyrldlp qaaeldalsl eakqafegtg
      241 mrwtdarnga pgisefvgrl saflvlvgls glavggigvs aavraylsqk tetiatlrtl
      301 gadratifqt ymiqiavlsg igiimglvlg gvlplllapl ietqlpipav fslypqplfe
      361 aalygvltaf lftlwplart eevraatlfr dalssarsfp rliyvvatai glaaligaaa
      421 wfsgstrltl wtsaglagal tllalsafai rklaragapw argrpalrwa lsaisdpreg
      481 aasvvlslgl glsvlaavgq idgtlrnais gnlpevapsy ffvdiqkdqm pgfserldtd
      541 pavsrvesap mlrgiitkin gqpareiagd hwvldgdrgv tysaqppqna rvtdgvwwpe
      601 dysgppqvsf aaeeaaemgl klgdeltvni lgrditaelt slrevdfsta gmgfvmsmnp
      661 salagaphsf iatvyaeeqa eaailrdlag qypnitavrv rdaidrvsgl laglaaatsy
      721 gagvslltgf lvligaaaag eparryeaai lktlgadrgr ilrsfalrai llgaaagcva
      781 lltgilggwa vatyifdtdf aiiwssalgi viagvavtlg agmlfalrpl svrparilra
      841 sd
//
LOCUS       WP_010442555             130 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010442555
VERSION     WP_010442555.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10106649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..130
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=13816
     Region          19..119
                     /region_name="Polysulfide_ST"
                     /note="Polysulfide-sulfurtransferase - Rhodanese Homology
                     Domain. This domain is believed to serve as a polysulfide
                     binding and transferase domain in anaerobic gram-negative
                     bacteria, functioning in oxidative phosphorylation with
                     polysulfide-sulfur as a...; cd01447"
                     /db_xref="CDD:238724"
     Site            85..90
                     /site_type="active"
                     /db_xref="CDD:238724"
     Site            85
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238724"
ORIGIN      
        1 maltvkdmmq aanaaverig askaqellgq gallldirda pelertgrav gshhiprgml
       61 efradpdlps hdpelrkdrv iilhcasggr aalagkllkd mgfshvynlg gysdwveggg
      121 etigpmdrgm
//
LOCUS       WP_010442580             334 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Ruegeria conchae].
ACCESSION   WP_010442580
VERSION     WP_010442580.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..334
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=36990
     Region          74..321
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mrpltatrtp vihrtkplag pdadfgaapk seseaepklr lrgtrffgrg rlsdpapsrl
       61 syrfqrwmlt pgirrgvkig lpvlavvglv ggffaaeerr eavsayvisi ktsiqerpef
      121 mvnlmaidga gtalsedire vvpldfplss wdldvemird titgldpvks atvrirpggi
      181 lqvdiverqp vivwrtrdgi elldetgahv dmiaaradha nlpliagkga dkhvpealqi
      241 lttarslger vrglvrvger rwdlvldrnq rimlpterpa ralervlavn evqdllerdv
      301 aavdmrlgqr ptirmnktas edwwntkvdv ssgq
//
LOCUS       WP_010442594             464 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Ruegeria conchae].
ACCESSION   WP_010442594
VERSION     WP_010442594.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..464
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=48312
     Region          17..458
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mtlwtaaeaa eatdgrastd wqvtgvsidt rtlhpgdlfv alkaardghd fvaqalekga
       61 gaalvsripe gvsedaplli vddvqtglea lgqsararta arvvgvtgsv gktstkemla
      121 siletqgkth asvasynnhw gvpltlarmp rdtefaviei gmnhpgeiap larqaqphvg
      181 lvttvaavhl eafdsvagia hekaaifdgl tkggaaivna diehadilrs caqalgakiv
      241 dfgrtaqdya lteveqgtds lqaqgkvgen nisfnvqsag thfamnalaa laacvelgvd
      301 ldqavaglrr wspvkgrgvr evitlpggdq ielfddsyna nptsmeaald vlaasqgnrk
      361 iaflgdmkel gaqehamhaa madvaamaqv dqvhcigplm qalhqalpeg krglwtetsa
      421 emvgqlpeli rngdavlakg slsmalaqiv dglrkmgqgg alep
//
LOCUS       WP_010442635             313 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Ruegeria
            conchae].
ACCESSION   WP_010442635
VERSION     WP_010442635.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..313
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=33398
     Region          25..308
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mtvsrttalh fgtllvlial ffvlpayhvg afsrimvlai yaigfnllfg ytgllslgha
       61 mffaagmygf glsmnfggls vlpafavgvl aagllalgvg llalrtigva fmivtlmfaq
      121 tfylvilyfg eytrgdegfi iqqaqrnlag idlttetary faaftlfaic flamarlvqs
      181 pfgkrlvair eneerarmlg ydvgrlklaa lvvsglfsgv agaayamlfg yvgasfaavh
      241 ysifpllwvl lggagttigp ligvifmfyl idisssftna ymlvagvalv lltlfapqgi
      301 agtirkravs wlp
//
LOCUS       WP_010442723             317 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Ruegeria conchae].
ACCESSION   WP_010442723
VERSION     WP_010442723.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143176
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..317
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34712
     Region          21..304
                     /region_name="retinol-DH_like_SDR_c_like"
                     /note="retinol dehydrogenase (retinol-DH), Light dependent
                     Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and
                     related proteins, classical (c) SDRs; cd05327"
                     /db_xref="CDD:212492"
     Site            order(28,30..33,52..54,80..82,108..110,130,162..164,185,
                     189,218..221,223..224)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:212492"
     Site            order(131,164,185,189)
                     /site_type="active"
                     /db_xref="CDD:212492"
ORIGIN      
        1 madttfgpkg wtperlgdqs gktyiitgan agagfqaari llkknakvvm lnrsaeksea
       61 aiadlrqefd akadvsfvrt elsvldsvre aaeevlktvp ridalinnaa iaqvptrklt
      121 vdgfesqfgt nhyghfllng llfdriaesk grivvvaslg ynmglktikf ddmnwdegyg
      181 antaysqskl aqmmfayelq drlaaagrre vevfvchpgs satslittsg srtmrfiwwl
      241 mtktpmvqta eqgsypevmc ateealteqr alygptgrme avgpvgkgtl nahaydkavt
      301 trlweeseka vgfewkl
//
LOCUS       WP_010442801             606 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ruegeria conchae].
ACCESSION   WP_010442801
VERSION     WP_010442801.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 606)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..606
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66743
     Region          1..559
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mldqpiaqik klrvefqtkd gpvvgvedvs fevnpgetvc ivgesgsgks vsslslmrlv
       61 efgggeiagg qllfdrrdge emnlagadqd lmkqirgnei gmifqepmta lnpvftvglq
      121 lteglrihkd mnkaqaedra lellrqvrip eperrlkqyp helsggmrqr vviamamace
      181 prlliadept taldvtiqae ilalmdrlkr etgtavmfit hdmavvaqma drvvvmfrgn
      241 kveegtvkei fenpqhdytk allaavpklg emqgkaapep mkllgeegqt iapipgtnev
      301 lltvknlttr favkggllrr tisnvhaved vsftlnrgqt lslvgesgcg kssagrsilr
      361 lvepmagevd ldgvdimkld qaglrkarld mqmifqdpfa slnpqmqlvd qvaepmrnyg
      421 vasgselqdr vaqlfdkvql prsfmrrfph emsggqrqri aiaralalnp kliiadeavs
      481 aldvsvqaqv lnlmmelqse lslsylfish dmavvervsh hvgvmylgri velgprarvf
      541 enpqhaytqa lmkavpiadp nkrksekdln fkpipspihp igyepepsey nevepghfvl
      601 ttdsgy
//
LOCUS       WP_010442805             378 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Ruegeria conchae].
ACCESSION   WP_010442805
VERSION     WP_010442805.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..378
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38941
     Region          8..374
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(18..19,22..23,26,58,108..109,111..113,116,135,
                     138..139,142,209,212..213,216..218,221,249,253,302..303,
                     307,311,327,330..331,334..335,338)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 migilaawra vaamfilnga lfgiwasrip avrdrlelsh ealgygllfm aagavcsfpi
       61 tgkltdrfga vaitriiavl ytaslillaf angfwaltaf lfvfgafhgs mdvamnawaa
      121 eveqtydkpv mssfhamwsl gaglgalsgy aavqmglsvv qhfllaggiv vglalalswv
      181 qwtsrrseak kgsvfalpsg alvlvgftal cgalgegava dwsaiflrdv tgaaesiaal
      241 gyaifsvtmv lfrlaggfvi srfgpvatar fggicaalgv ytvvsaseag lalagfalmg
      301 lgyavimpla fsraandprv ppgqaiasva tlgyggllig ppligflael mtlrlafavl
      361 lplavliivl agalkrad
//
LOCUS       WP_010442807             118 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Ruegeria conchae].
ACCESSION   WP_010442807
VERSION     WP_010442807.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..118
                     /product="VOC family protein"
                     /calculated_mol_wt=13465
     Region          4..116
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mqkvngiggv ffrakdpeal sawyeehlgv nhydpvpwkq regytvfapf aqdtdyfgra
       61 dqqwminfrv ddldamiaql etagitveth pdwdsevgnf arihdpegnp ielwqpnq
//
LOCUS       WP_010441765             116 aa            linear   BCT 01-JAN-2025
DEFINITION  H-type lectin domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010441765
VERSION     WP_010441765.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Pietrzyk-Brzezinska,A.J. and Bujacz,A.
  TITLE     H-type lectins - Structural characteristics and their applications
            in diagnostics, analytics and drug delivery
  JOURNAL   Int J Biol Macromol 152, 735-747 (2020)
   PUBMED   32119947
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Andre,S., Kaltner,H., Manning,J.C., Murphy,P.V. and Gabius,H.J.
  TITLE     Lectins: getting familiar with translators of the sugar code
  JOURNAL   Molecules 20 (2), 1788-1823 (2015)
   PUBMED   25621423
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Sanchez,J.F., Lescar,J., Chazalet,V., Audfray,A., Gagnon,J.,
            Alvarez,R., Breton,C., Imberty,A. and Mitchell,E.P.
  TITLE     Biochemical and structural analysis of Helix pomatia agglutinin. A
            hexameric lectin with a novel fold
  JOURNAL   J Biol Chem 281 (29), 20171-20180 (2006)
   PUBMED   16704980
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10559620
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..116
                     /product="H-type lectin domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12929
     Region          41..104
                     /region_name="H_lectin"
                     /note="H-type lectin domain; pfam09458"
                     /db_xref="CDD:462806"
ORIGIN      
        1 mkkflthpig idqgesvlfs dfadggdmwt gqgarerrta irfkeafrsv pfvqigvalw
       61 dvdtssalra evqaeditpe gfnavfrtws dtriarirvs wtaigevahe ddwnis
//
LOCUS       WP_010442828             251 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Ruegeria conchae].
ACCESSION   WP_010442828
VERSION     WP_010442828.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..251
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26970
     Region          6..251
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mfemnlmffa vaipavifag iskggfgsgv afasssilal iltpgqalal mlpilmvidv
       61 atlkpywkrw swpdsrllil gavpgialga wlyrvtdddl lrlliggisv gfviwhvaqt
      121 ggwvrgfanr lppsaglfag lvagftsfvs haggppaavy llsqrltkte fqastvlvfw
      181 vinavkfvpf aylglftwht aladllltpf ailgawlgvr ahfmlserlf fgiayvlltl
      241 tggkliwdal v
//
LOCUS       WP_010442861             151 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Ruegeria conchae].
ACCESSION   WP_010442861
VERSION     WP_010442861.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..151
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16441
     Region          1..138
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mrkflvvldd sreclnamrf aamraahtgg gvtvlsvipp defnhwigva evmreearer
       61 ihahfevfak wmrdkqgvep elairegdpv pqiiehvqsd seigvlvlga gtdkkgpgpl
      121 vtqltrnsgs lpipvtivpg dlskekleai t
//
LOCUS       WP_010442863             150 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010442863
VERSION     WP_010442863.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..150
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16900
     Region          1..139
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mddidskiir alqndgrmtv idladhvgls ptpcarrldr lqrdgiitgy aaqvdpeqlg
       61 fgvtifvsve lekqdrsaid sfekairrcd evmecylmtg srdillrvva kdlnafdafl
      121 enrlmkiqgi rnlrsnfalr tmvkreslpl
//
LOCUS       WP_010442894             281 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Ruegeria conchae].
ACCESSION   WP_010442894
VERSION     WP_010442894.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..281
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30807
     Region          5..261
                     /region_name="SDR_a4"
                     /note="atypical (a) SDRs, subgroup 4; cd05266"
                     /db_xref="CDD:187576"
     Site            order(9,11..13,32..34,67..69,98..100,124,128,148..151)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187576"
ORIGIN      
        1 mtqtlfsfgh gysaratskq ldpaswriig tsrdpkqidt irasgaepiv wpgerpdleg
       61 vthvlistap tadgdpvlae lrdeiaarag qfkwvgylst tavygdhdgg wvdettapep
      121 taergrwrvr aetqwadipd lplhtfrlag iygpgrgpfs klkrgglrri ikpgqvfsri
      181 hvddvaqvli asmakpnpga iynvcdeepv ppqdvigyaa elqglplppa vpfdeadltp
      241 marsfynenk rvrndrikee lgisllypny rvglealmep s
//
LOCUS       WP_010442901              95 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HU family DNA-binding protein [Ruegeria].
ACCESSION   WP_010442901
VERSION     WP_010442901.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria
  ORGANISM  Ruegeria
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Ruegeria"
                     /db_xref="taxon:97050"
     Protein         1..95
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9977
     Region          5..95
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 makpmtktql vaalaeemgt dkksanaale amtglitrev saggavtlpg vgkiycrerp
       61 ermvrnpatg eqfkkeadkv vkmtiakalk dsvng
//
LOCUS       WP_010442921             405 aa            linear   BCT 01-JAN-2025
DEFINITION  phenylacetate--CoA ligase family protein [Ruegeria conchae].
ACCESSION   WP_010442921
VERSION     WP_010442921.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 405)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..405
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43111
     Region          2..392
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mtyfdkletr saderaadha ralpeqinra qaapgykdil sdvqsdavtd mqalaqlpvl
       61 rksdltkaqa grppfggftv kparnfqhvf qspgpiyepg stdhdwwrmg rflnaagvgp
      121 gdivqncfgy hltpagmife sgaqavgasv lpagtgqtel qvtaardvgc tayagtpdyl
      181 kiilekadam gvalqfskav vgggalfpsl rqeyadrgia clqcyatadl gniayespam
      241 egmiidehvi veivtpgtgt pvapgevgev vvttlnpdyp lirfatgdls aimpgaspcg
      301 rtnmrikgwm gradqttkik gmfvrpeqva alvdkhdeiv karviaarqg emdtmtvqie
      361 spcendgaya ksvaevlklk gaievvapgs lpkdglvied qrvye
//
LOCUS       WP_010442951             407 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Ruegeria conchae].
ACCESSION   WP_010442951
VERSION     WP_010442951.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..407
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=43805
     Region          6..404
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mtqhytinrl ghqgdgiadg piyaprtlpg evisgtllgq flsdirvetp sdqrvkapcr
       61 hyktcggcqm qhaaddfvan wkvdvvrnal aaqgldapmr pihtspersr rratiavrrt
      121 kkgtlagfhg rasetiteip dchllhhtli daipvaeala mlggsrkgvl avtltlsevg
      181 ldvavkggkp ldgplelala qatelhglar lswddeviam reppiqrfgn agvtpppgaf
      241 lqatkdgeqa llqavsdatl gakrivdlfa gcgtfslpla qtaevhaveg eaemtkaldq
      301 gwrkaqglkq vtteardlfr rplmpdelkk fdavvldppr agaeaqvael aqaqrpvlay
      361 vscnpvsfar dakilvnagy alewvqvvdq frwsshtela arfslnp
//
LOCUS       WP_010442974             297 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Ruegeria conchae].
ACCESSION   WP_010442974
VERSION     WP_010442974.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..297
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32346
     Region          40..296
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mnarkgkprg lgrglsalma dvapeadgri ssesrrpdlt vpieklqanp dqprrrfaqe
       61 qldelaasvk ekgiiqpliv rsiaggqyei vagerrwraa qmaqlhdipv iirefddtev
      121 leiaiieniq radlnaveea agfkqlmdrf ghtqeklaea lgksrshian llrllslpmd
      181 vqtlviegkl sagharalit aedpselakq vvrnglsvra tealvkkqqg gadksalkpr
      241 nlnagkdadt ralekdlsai lamkvtinhk pgsetgqvvl syenldqldd lcaklsr
//
LOCUS       WP_010442991             365 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Ruegeria conchae].
ACCESSION   WP_010442991
VERSION     WP_010442991.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..365
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39443
     Region          1..334
                     /region_name="COG4782"
                     /note="Esterase/lipase superfamily enzyme [General
                     function prediction only]"
                     /db_xref="CDD:443812"
ORIGIN      
        1 mlryliiian lcllaacvdr siteitpeal kvgtpatvfa attrardmdg sygakraeal
       61 rylemtvsip pshtpgdlnf syanpnpnkq fvvadvtefs gpqdltarlr gvddvvifvh
      121 gynatqteta fraaqlshdi gipgttliys wpsqargtgy aydldsmlfa rdgleqtirl
      181 lksmgvkrvi liahsmgsal smemmrqael repgwsnrnl egvilispdl dvdlfrsqmn
      241 siknppdpfv vmvsrkdkil nlsarlrgta dskrlgniss adalaeypin vidttafnsd
      301 agsshfvaat spallailss vrrvsntfgp drpgidvlvp pserntdgat eiiltetgqa
      361 qvstp
//
LOCUS       WP_010443020             140 aa            linear   BCT 01-JAN-2025
DEFINITION  EVE domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010443020
VERSION     WP_010443020.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Bertonati,C., Punta,M., Fischer,M., Yachdav,G., Forouhar,F.,
            Zhou,W., Kuzin,A.P., Seetharaman,J., Abashidze,M., Ramelot,T.A.,
            Kennedy,M.A., Cort,J.R., Belachew,A., Hunt,J.F., Tong,L.,
            Montelione,G.T. and Rost,B.
  TITLE     Structural genomics reveals EVE as a new ASCH/PUA-related domain
  JOURNAL   Proteins 75 (3), 760-773 (2009)
   PUBMED   19191354
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..140
                     /product="EVE domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=15830
     Region          2..137
                     /region_name="EVE"
                     /note="Predicted RNA-binding protein, contains EVE domain
                     [General function prediction only]; COG2947"
                     /db_xref="CDD:442190"
ORIGIN      
        1 maywlfksep stwswdqqva kgnageewdg vrnyqarnfm rqmqigdrgf fyhsqkdkai
       61 vgivevcaea hsdsttdder wecvdikavr pfatpvtldq ikaderlaem vlvknsrlsv
      121 qpvsdaewqv icglgqtead
//
LOCUS       WP_010443028             503 aa            linear   BCT 01-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Ruegeria conchae].
ACCESSION   WP_010443028
VERSION     WP_010443028.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..503
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=52271
     Region          1..471
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mleglliglq tafslqnllm viagcligtf igmlpglgpm siiaimipva ismgdpsaal
       61 illagvyyga ifggstssil lnapgvagtv assfdgypma rqgkagkalt iaaiasfagg
      121 tigaillmvf apalssvall fhsaeyfalm vvglsaiaaf agsgqvakal imtilglima
      181 tvgegalfnl prftmgimdl qsgfgfitla mamfalpeal flvlkpknlq gddgeikdlr
      241 itkdeakaia pvigrqstqg ffigvlpgag atiasflgya verniapkke qeefgkgsik
      301 glaapeaann aactgsfvpl ltlgipgsgt taillgalia lnvtpgprlm idepqifwav
      361 imsmfignlv llilnlplip yiakvlavpr nylipfilff tlmgayigqn natellilvg
      421 fgvcatalkf adyplaplli gfilggmmed nfarsmqlyd gigfiwerpm tlallviavl
      481 lvllpsyrar rararaagia dgd
//
LOCUS       WP_010443116             233 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010443116
VERSION     WP_010443116.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..233
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25509
     Region          16..223
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msheaqkaia rqslllrslp eqhvetllsh aiwrqydrge tiflqeetaq aihvvlagwv
       61 klfrmtptga eavvsvftrg dsfgeavalr nvpypvsaea vsacdvmhip spilislmke
      121 dpeigisila atfthlhslv aqleqlkaqt gaqrvaefll nlcdtdagec evslpydkml
      181 iagrlgmkpe slsrafsrlk avgvkinrnh avisdiallr dyaesdpaen wgr
//
LOCUS       WP_010443144             262 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome c1 [Ruegeria conchae].
ACCESSION   WP_010443144
VERSION     WP_010443144.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10490041
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..262
                     /product="cytochrome c1"
                     /EC_number="7.1.1.8"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28344
     Region          35..254
                     /region_name="Cytochrom_C1"
                     /note="Cytochrome C1 family; pfam02167"
                     /db_xref="CDD:426633"
ORIGIN      
        1 mfkklaigaa falalapast faagggeqhi edfdfsfegp fgtwdqnqlq rglqiytevc
       61 aachglqyip lrtledlgys eeqvityaad nfevfdpeld dfrpaiptdh fpantgvgap
      121 dlslmakara gfhgpyglgi nqlvkgmgga eyiaslldgy tgeekeeagt vlyenkafpg
      181 gwismappla edqvefadgh patveamsed vaaflmwtae pkmmgrknag fvgvlfltvl
      241 svllylvnkr lwaphkgkir kd
//
LOCUS       WP_010443159              45 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2256 domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010443159
VERSION     WP_010443159.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..45
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..45
                     /product="DUF2256 domain-containing protein"
                     /calculated_mol_wt=5372
     Region          1..45
                     /region_name="COG4338"
                     /note="Uncharacterized conserved protein, DUF2256 family
                     [Function unknown]"
                     /db_xref="CDD:443479"
ORIGIN      
        1 mkmrkkvdlp qkicpvcqrp ftwrkkwesv wdevkycskk crsaa
//
LOCUS       WP_010443225             134 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Ruegeria conchae].
ACCESSION   WP_010443225
VERSION     WP_010443225.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..134
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14186
     Region          4..123
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 msdkieggck cglvrysgir sdlpmfrchc rdcqqltgsg hsemvplvak svsigdalkt
       61 femaggsgls tfsgfcpncg splirrserv sdciyvhaas mddpskyhpa ksiyseaaqa
      121 wdeavitteg agtk
//
LOCUS       WP_010442968             187 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleotide exchange factor GrpE [Ruegeria conchae].
ACCESSION   WP_010442968
VERSION     WP_010442968.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Harrison,C.
  TITLE     GrpE, a nucleotide exchange factor for DnaK
  JOURNAL   Cell Stress Chaperones 8 (3), 218-224 (2003)
   PUBMED   14984054
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087353
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..187
                     /product="nucleotide exchange factor GrpE"
                     /GO_function="GO:0000774 - adenyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0051087 - protein-folding chaperone
                     binding [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=20652
     Region          43..181
                     /region_name="GrpE"
                     /note="nucleotide exchange factor GrpE; cd00446"
                     /db_xref="CDD:271355"
     Region          43..93
                     /region_name="2-helical coiled coil"
                     /note="2-helical coiled coil [structural motif]"
                     /db_xref="CDD:271355"
     Site            order(45,48..49,52..53,55..56,59..61,63,66..67,70..71,
                     74..75,77..78,81..83,85..89,91..92,110..111,113..115,118,
                     124..125)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271355"
     Site            order(61,69,91,94,138,140..141,143..147,163,172,176,178,
                     181)
                     /site_type="other"
                     /note="Hsp70 (ATPase domain) interactions [polypeptide
                     binding]"
                     /db_xref="CDD:271355"
     Region          110..125
                     /region_name="2-helical coiled coil"
                     /note="2-helical coiled coil [structural motif]"
                     /db_xref="CDD:271355"
ORIGIN      
        1 maepknedfl ddimsaeaee laeefaeisd ealeldelra erddykdkfm raladaenar
       61 krgdkarrda eqyggsklar dmlpvydnmk raleaatdeq kelaaglleg veltmralkd
      121 vfqkhgievi tpevgdrfdp nvheamfeap vpgtkagdii qvsaegfmlh drllrpaqvg
      181 vssmpag
//
LOCUS       WP_010443244             427 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Ruegeria conchae].
ACCESSION   WP_010443244
VERSION     WP_010443244.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..427
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44885
     Region          1..425
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mivaivfval ilfgmpigfa iglagvvgli dmggtqflai gpskifngln ifpflampff
       61 ilageimndi gitsrlvkla qvlvgrfrgg lahtnmlasv ffagltgsat adaaafgrtl
      121 vpamvkegyk rdyacavtaa gsiigptipp sglmvvygsl mgvsiaglfa agvlpglvic
      181 ivcmaviaig gkrenlpkal rgasprevwd tfvssltala mpviilggil ggivtpteaa
      241 siavayamfi gifvyrsltf kgfyamlvrt aritgvifvi iafagilgww msferipqli
      301 aetvlglsdn ryaviaiiig lllivgmvmd itailiilap vlvpltqqvg lepihagiif
      361 vlalnislmt ppvgaclfvl ssvtgekler isiklfpfli aeiailfafa fwedaalwlp
      421 rmlgfaq
//
LOCUS       WP_010443374             471 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Ruegeria conchae].
ACCESSION   WP_010443374
VERSION     WP_010443374.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..471
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50697
     Region          16..471
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mfdlktldgs taivnqdtld aldaslrggv yqkgtseyed arttwnsmfe rypgfviral
       61 gasdvqravn fvrdtglvms vrsgghqiag havadetvml dlsqmrsvhv dpvnktarve
      121 pgallgdvdr etqahgltvp vginsttgia gltlgggfgw ttrkfgmtid nllsaevvta
      181 dgaivtaspt shpelfwair ggggnfgvvt sfefqlhelg pdvlsglivh pienapella
      241 efatiadnsp deltvwsvmr kapplpflpv ewqgrevlif aacysgsmee gekamaalra
      301 lgepiadvis phkfvdwqaa fdplltpgar nywkshdfda lssdaisgll eaisslpdpa
      361 cevfiahvgg amarveagst aypqrsahfi mnvhtrwedp skdaeciawa rdlydqmrph
      421 atgsayvnfm pedeadhmag aygdngekls kikgtydpvn lfrvnhnilp a
//
LOCUS       WP_010443391             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Ruegeria conchae].
ACCESSION   WP_010443391
VERSION     WP_010443391.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..206
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20945
     Region          26..198
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mpglenlgtg gpiivllgll sllsltvivv kvirlapvra ggpardaafv qwsggdkksa
       61 qqavaagksp adrvcayamq alidgfkgpa lmaeltrrgn qefavmnswi rvleliamis
      121 pllgllgtvt gmiqsfqele laqgaanasv laggiwqall ttaagllvai paaigaslls
      181 graeagaqsi enavgnlmvl eergah
//
LOCUS       WP_010443415             191 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Ruegeria conchae].
ACCESSION   WP_010443415
VERSION     WP_010443415.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..191
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20511
     Region          86..187
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(92..93,126..127,130,134..135,138,179,183)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mpafssmkti gasafvvvca tqfalaqsne ltadeitdaf nkqktrglvi vpsnsgtett
       61 qdtaettvaa apaeyqpvat edqvniqvrf dfasaalrdd ekpklaslcq amknvdvnvf
      121 qiightdsag saeynqnlsl lrakevkrfl vsdcgisdqr levlgvgeaq plnkdnprad
      181 enrrvefqal g
//
LOCUS       WP_010443426             257 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Ruegeria
            conchae].
ACCESSION   WP_010443426
VERSION     WP_010443426.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..257
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27782
     Region          1..254
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 msqthreiel lealrrlggs arntdlakal dvseetvrrt ikslsktamv arvrggaylv
       61 gtqndpsffr ritqrptekr lianvvstlv sdgmtlfldv gsttafvaee lrrhqnltia
      121 tnsigvaqtl vnvngnrvhi lggemqaner gafghvthrq aqrlvydmai lsadavsprr
      181 gflyhsnaea elaqivaeca dqiliafdhg klsesapfvg paprqishiv tdkapskala
      241 qsldawgika viadgsy
//
LOCUS       WP_010443480             429 aa            linear   BCT 01-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Ruegeria conchae].
ACCESSION   WP_010443480
VERSION     WP_010443480.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..429
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46928
     Region          4..424
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mtrsnaelia drarllgpnv stfydnpvhi vkgegvwlwd adgrkyldcy nnvphvghcn
       61 prvvdaicrq antlnthtry lhdgildyve kltstvddhl dtailtctgs eandialrma
      121 esmtgkrgii atdatyhgnt slvsqlsksn vptvgfglgq ffrfvgapds yrnpdpegmr
      181 faesvaeqia eheksgigfa alvvcpyfln egfpdnpdgw lkptaevvrk aggllicdev
      241 qsgfgrtgth mwahqkmgvv pdvmtlgkpm gnghpiggvv tnseilgtfr kgyryfntfg
      301 gnpvscaaai avleeiedkh llenarkvga harmritrla kkhefigdvr gsglifgaem
      361 vldretkqpa saftdrving mrergvihsk lgrhkntlki rppmpfsien adllfdtlde
      421 vlaktplda
//
LOCUS       WP_010443481             297 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Ruegeria conchae].
ACCESSION   WP_010443481
VERSION     WP_010443481.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..297
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33552
     Region          2..296
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mqdasyhlia arenqvfrvd ingssyalrl hragyrtnee lrselqwmda vsrgglhvpa
       61 piatasgdfl hiadgvqidv lswlngapmg atgqpletkd rtslflgigr emarlhhvsd
      121 rwvlpddfdr cswdrngllg snplwgrfwe nptlsaddre mfealrgkma teltqledtl
      181 dyglihadlv renilvdgdr lqlidfddsg fgfrlfdlat tllknlqepd ypelkealla
      241 gyrserpldd saldlflllr aatyvgwvid klseegselr nqrfidttrk lalrylg
//
LOCUS       WP_010443495             171 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF805 domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010443495
VERSION     WP_010443495.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..171
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18520
     Region          5..169
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mgfgeavktc fskyfqfsgr alrseywwff lfvvlasaal avldtiifgt npetgqgsrv
       61 lssvfqlavl ipmlaagwrr lhdtgrpgwy lllpmalsit tlfvmlggva ffsvleqgte
      121 npdalrgpaa vlgvtgivvv silqlvlsil miwwltrpse eganeygapv s
//
LOCUS       WP_010443500             368 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Ruegeria conchae].
ACCESSION   WP_010443500
VERSION     WP_010443500.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..368
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39789
     Region          5..343
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,229,297,317,319..321)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,177,180,182,229,236,297,317,
                     319..320)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,177,180,182,320)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            182
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 madeklfsgi kagaielknr ivmapltrnr araeddsvhe lqakyyaqra gagliiteas
       61 qispqgkgya wtpgiyseaq idgwkkvtea vhakdgkiai qlwhvgrish yslqqdggap
      121 vapsaigaka ktfdgeqfve tsepralaie eiagivadyr raaenakeag fdgvevhaan
      181 gylidqflrd esnkredeyg gpvenrarfl kevmdvvvdv wgadrvgvrl spfsdannis
      241 dsdpqatfth avkllngygl aylhlvegqt ggprdipegg dlkalyelfd gakmgnnayd
      301 remaveavet gavdlvafgr pfisnpdlvn rlekdaalne ldpttlyggt ekgytdypal
      361 eeeavaae
//
LOCUS       WP_010443550             145 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Ruegeria conchae].
ACCESSION   WP_010443550
VERSION     WP_010443550.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..145
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15537
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mttkivigld gtetgeraia fakdlagrig ecellvvyvi ewspftfqtp eenamrhkrr
       61 eeevelatsr iiapavealk aagfeaqgiv rhgdvaetln titvenggsq ivvgrasadg
      121 fkkrlfgsst qnlvmhadvp vtvvn
//
LOCUS       WP_010443554             304 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010443554
VERSION     WP_010443554.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33930
     Region          14..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(110..111,113..114,117,121,123..129,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176107"
ORIGIN      
        1 mkktrnwhsl peyqalralm qagttaaaar qlglsqsavs rsvgslesrl gkilferdag
       61 rlrptqeavr lnmrldplfe aldridgpge tvqetlrlva ppsyahryiv tliasfirgn
      121 pgffvnlevt tsdmvtlgvl enrfdlavtg ieqsragikl ipfrespavc vmrpehplaq
      181 rsalapadlh eqdlialtyr hgrrgqldrl lhqvraepri vaevstsfaa admareglgl
      241 avinpfpvym yrspdltfvp feapmryrgh fvisdqrpvp riarafmrhl rlntpsdpfs
      301 dknl
//
LOCUS       WP_010443588             281 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Ruegeria conchae].
ACCESSION   WP_010443588
VERSION     WP_010443588.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..281
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31046
     Region          194..275
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mwrpaqetdl pdidaflsqh iqtsmfplan lrdfglrklh prslkawvlg dpfravfait
       61 negmilsqcp ncsddelaea islirghalf giaseatqar wlmqlggwed rpatlnsdep
      121 gfsleldqlr ipdvsgarlv pldevdrait enwrhdylie amdfapdrak tqagedfeay
      181 ctrdshrvll vndrpvamtg fnarlpeivq iggvytppel rgrgyarlav alhlsearda
      241 gvsrsvlfaa sdsaarayma igfqpagyfs lilftnpedt a
//
LOCUS       WP_010443599             152 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010443599
VERSION     WP_010443599.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..152
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16924
     Region          1..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mmidatdrki laalqrkgrm snselseqan lspsachrrv qrleaegyik dyvalldark
       61 mnvpttvfve itlqgqaeev lesfekavar ipdvlechlm agtadyilkv vaentedfar
      121 ihrqylsrlp gvaqmqssfa lrtvfkttal pv
//
LOCUS       WP_010443601             382 aa            linear   BCT 01-JAN-2025
DEFINITION  CAP domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010443601
VERSION     WP_010443601.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..382
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=41910
     Region          2..144
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
     Region          <178..274
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
ORIGIN      
        1 mstastvere mlalinqert srgldplele rnlnessedh stwmldtdrf shtgqggssa
       61 tqrmqaagfd lsgswrtgen iawqsergap gisddvaqlh qnlmnspghr anilnpdfky
      121 igigieegdm qgfdavmvtq nfaatqgevd ldnggttppv nppveevaep eeevttptep
      181 evpdtdvtet eepvdetpva evpetdepae etpdedvtet eeptdetpdt dvtetddqve
      241 etpetdvtet eepetpdtdv tevedpepev pdtdvtevee pepetpevvv dngepgadcf
      301 dvqaflagie afvnalqahf dqfewspvqq adttpemddf dlvfdtdvad dmietvettv
      361 edmnddmcgm fvfemncgfd wg
//
LOCUS       WP_010443647             259 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Ruegeria conchae].
ACCESSION   WP_010443647
VERSION     WP_010443647.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..259
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27684
     Region          10..248
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mslfsdnelt lneflggrvr lwqpktgyra gvdpvllaas vpalkgqsvl elgcgagaai
       61 lcllarvpql qatgvelqpa yaelarrnat qnamdlsvve adlsalprdl kqaqfdhvia
      121 nppyykpgah spstdpgrqi algentplte widvaarrla prgylhmiqk adrlpdilaa
      181 csgrlgsaev lplsarvgrl aelvilrark ggrasfrlqs plimhqgdrh lkdgesytpe
      241 vsavlrdgaa lagfasdrq
//
LOCUS       WP_010443686             197 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Ruegeria conchae].
ACCESSION   WP_010443686
VERSION     WP_010443686.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..197
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=21985
     Region          5..197
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mpakkilvln ghpaesslsr tfaqtyadaa iakghevrmv hlsdlqfdhd fgqgnyedfk
       61 plepvleqvl qdiewsdhlv lttpmwwggl paklkglidr tfipgrtfdt rnttkiglpa
      121 pmlsgrtarv iltsdtpgwf mrliyrqall rqlrdqvlgf vgfkptrfty fasasypnpg
      181 sverwigkva rmgaaal
//
LOCUS       WP_010443824             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Ruegeria].
ACCESSION   WP_010443824
VERSION     WP_010443824.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria
  ORGANISM  Ruegeria
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Ruegeria"
                     /db_xref="taxon:97050"
     Protein         1..282
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31156
     Region          1..279
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mqalnrhihp gwliiaplll mvvalylgpi lnilwlsvtd pepgfgnyak ltegdaliri
       61 vwttvricii ttvfsvifgy siayamvhch qrqktymltl llvsfwisil vrtfawlmll
      121 grkglvnvtl ediglvaepi afmrnelgvl igmvhymipy avlpllvsmq sidqrvmdas
      181 rnlgasgsqt fwrvylpmtm pglvastllv filslgfyvt pavlgggkvl mvaeyisvql
      241 lvtlkwgtaa mlaaimlfgv lamlwimsrf mklstvfgga ar
//
LOCUS       WP_010443931             855 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [Vibrio].
ACCESSION   WP_010443931
VERSION     WP_010443931.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..855
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=95020
     Region          1..855
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mkfikrllfl tliciilgvt tifgfyqyvk pelpdvatlk nvelqtpmqv ysqdgkliaq
       61 fgekrripvt ydeipqdlih aliatedsrf yehpgidpig itraavvval sgsakqgast
      121 itqqlarnff lsnekkimrk ikeifiaihi eqllskqeim elyvnkiflg yrsygfgaaa
      181 qvyfgkslne lslseiatla gmpkapstmn plysldratk rrnvvlmrml dekyitqeqy
      241 dearsepiva ryhsaeiels apyvaelars wavkeygeek aytsglniym tvdsklqdaa
      301 nkasinnila yderhgyrga ekvlwkeges swdteqiekh lkkqptygql ypavvtevdd
      361 ktaqvwvknn deqtiawtgm nwarkyltde rqgavpksak qilesgqqvw vreisttdke
      421 gntthswkls qvpsantafv amnpengavl slvggfnfvh skfnratmsv rqvgssikpf
      481 iysaainkgl tlaslvndap inkwdagsgs awrpknsppt yigptrlrig laqsknvmav
      541 rtlrevglde treyltrfgf didevprset ialgagsltp mkvaqgysvf anggyyvepf
      601 yvdhvedsfg evvfkanpkv icqhncpqmd eqapaedkfv aefgeqdvta dsiapdnale
      661 ndtpqyakqv isaqnaflmr emmysniwgg gswrdgtgwn gtgwraqkld rrdiggktgt
      721 tndskdtwyn gygpgivaia wvgfddhsrt lgrttvnsnl gkgqisgaes gaktaepawi
      781 dfmhvaldgv pqqgksipdd ivrvridrds gllthkvdgs smfeyfekgt epteyvgnsl
      841 edsiysgggs seelf
//
LOCUS       WP_010444610             137 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADH-quinone oxidoreductase subunit A [Pseudomonas].
ACCESSION   WP_010444610
VERSION     WP_010444610.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012780
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..137
                     /product="NADH-quinone oxidoreductase subunit A"
                     /EC_number="1.6.5.9"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=14994
     Region          5..124
                     /region_name="PRK06602"
                     /note="NADH:ubiquinone oxidoreductase subunit A;
                     Validated"
                     /db_xref="CDD:180638"
ORIGIN      
        1 mteatglmah nwgfaifllg vvglcafmlg lssllgskaw grsknepfes gmlptgsarl
       61 rlsakfylva mlfvifdiea lflfawsvsv resgwtgfve alvfiailla glvylyrvga
      121 ldwapqarqk rqaklkq
//
LOCUS       WP_010444624             460 aa            linear   BCT 01-JAN-2025
DEFINITION  multicopper oxidase family protein [Vibrio rotiferianus].
ACCESSION   WP_010444624
VERSION     WP_010444624.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..460
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=51567
     Region          2..27
                     /region_name="TAT_signal"
                     /note="TAT (twin-arginine translocation) pathway signal
                     sequence; pfam10518"
                     /db_xref="CDD:463131"
     Region          38..459
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mdisrrrflq sslaisalti lpacslsrst nkqgqhiydi taepstaelv pgfntdvlaf
       61 ngsipaptir crqgerviir ftnklseptt ihwhglripi emdgvpflsq ppimpgetfv
      121 yeftppdagt fwyhphmnsv kqlgmglvgl iiveeaepvq fneehevvlk hwhldkqgqw
      181 knlmvprlsa rmgtpgewss vngvhepvya lkqnattrlr ianvdntity piaiegaeaw
      241 viaidgnpvk tpymltqhki gpgmrldvgl iapragervy vrqmkgrfpf plcefevves
      301 dlptnqklpl lplnpvpdld lenaeqidyv fewegavtpa dksgkaipkf wlmnkraweg
      361 mskdnipapl stlevgktyi fnlknvtqyh hpihlhghtf tvleldgkkl depfhtdtvl
      421 lgkngsakaa fvadnpgrwm yhchviehmk tglmgyievk
//
LOCUS       WP_010444758             257 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Vibrio].
ACCESSION   WP_010444758
VERSION     WP_010444758.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..257
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27906
     Region          3..254
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgkivaianq kggvgktttc inlaasmaat krkvlvidld pqgnatmasg vdkymvdata
       61 ydllvedtpf dqvvctqttg kydliaangd vtaaeiklme vfarevrlkn alasvrdnyd
      121 fifidcppsl nlltinamaa adsvlvpmqc eyfaleglta lmdtisklaa vvnenlkieg
      181 llrtmydprn rlsnevsdql kkhfgskvyr tviprnvrla eapshgkpam yydkysagak
      241 aylalageml rreevpv
//
LOCUS       WP_010444803             184 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TMEM165/GDT1 family protein [Vibrio].
ACCESSION   WP_010444803
VERSION     WP_010444803.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..184
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19461
     Region          1..183
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 msvlaisitt valaeigdkt qllslllasr yrkpipiiaa iflatianha laawlgvvva
       61 dylspevlkw vlvvsfvama awvlipdkld ddeqisnrgp fiasfiaffv aeigdktqia
      121 tsilgaqyad alswvilgtt igmllanvpv vligklsadk mplglirkvt aflfialaig
      181 aalf
//
LOCUS       WP_010444932             254 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Vibrio rotiferianus].
ACCESSION   WP_010444932
VERSION     WP_010444932.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..254
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28750
     Region          1..253
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 midthahiya sefdndrdev vkraleqgid rillpnidle siepmlktea typevcrsmm
       61 glhpcyvdgn veqtleiirg wfdkhnfiav geigidlywd ktfraeqemt fvtqlnwake
      121 mdlpvvihtr dsieetltll rqeqdgrlrg vfhcfggsve eaqainelgf hlglggvstf
      181 knggmdkvip yldmdwvile tdcpylapvp hrgkrnepay tslvaarvae llevpieevd
      241 rittnnaekl fals
//
LOCUS       WP_010445029             463 aa            linear   BCT 01-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Vibrio rotiferianus].
ACCESSION   WP_010445029
VERSION     WP_010445029.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..463
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48625
     Region          3..440
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mttsnrtsel vyqlndrppl pqtifaalqh llamfvavit psliicqslg vpadqtntii
       61 smslfasgvs sfiqirtfgp igsgllsvqg tsfnflgpii gaglslkagg adistmmaai
      121 fgtilvasfa eillsrvleh arriitplvs givvtliglt liqvglvsmg ggyaamgdgs
      181 fgsldklala gtvlglivil nrsknpylrv asiviamlvg yvmayfmgmv dsstlgetdl
      241 ialpipmqyg lsfdwslfip lvliffital eaigditats evsgepvkgp vymkrikggv
      301 ladglnsaia avfnsfpnst fsqnngiiml tgvasryvgy fisgmlvilg lfpgvasfvq
      361 lipepvlgga tivmfgtiaa agvriisrvd ldrrailima lsfsmglgia qkpeilqfmp
      421 efiksifstg vaaggitaiv lnlllpekle eedelvaqei kes
//
LOCUS       WP_010445056             175 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Vibrio].
ACCESSION   WP_010445056
VERSION     WP_010445056.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..175
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19356
     Region          10..169
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mwwlvgeles irrflgmggd vlvvifilsf mlwavllerw fyfaavapka mkkavsfwee
       61 rsehkswnak mirqeivsrq dienkkglpi vkvlialcpl lgllgtvvgm iqvfdilavt
      121 gtgspramas giskatiptl agmvaslsgl ffstrldhla rvttqkledk lkhia
//
LOCUS       WP_010445105             352 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Vibrio rotiferianus].
ACCESSION   WP_010445105
VERSION     WP_010445105.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..352
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39130
     Region          7..345
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mplfahepks lcflrlsaig dvchavaaiq nvqkhwpntk itwvigkiea qlleglngve
       61 lvvfdkkqgi kgmqsvwqtl kdrkfdalih mqlalrasil ttgirarykv gfnfkrakeg
      121 qwlftnkkip dtqsqhvlds fyafteylgv psqkptwqlp lsredhafat eqlthkatva
      181 icpaaskder nwlperyaqf adfvysqgyq vvlcgssaqr evdlanniiq qtkspiislv
      241 gktslkqlta vlsacelvla pdsgpahiat tqgtkvlgly ghsnpkrtgp ynnidnvvsv
      301 yekfaeeqnk qpveslpwst rvkganvmqa islndvveaf nklikgdidv rn
//
LOCUS       WP_010445057             453 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Vibrio].
ACCESSION   WP_010445057
VERSION     WP_010445057.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..453
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49069
     Region          262..443
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mkgfktlaag llaslfmisg ahaeapknls ellknvkses iveskenkar eaefrnnrdk
       61 qaallqqarn elaaqqalgd elkatfdend kqlteltetl rvrsgtlgem fgvvrqyage
      121 fkglfaasqn avqfperdal lsklaeskel pstqeleafw htilqqvvvs getttapatv
      181 vygegkeavr dvtlvgefna iadgkyvtyv pqtgkfeels rqprknitrl vggfeaadgt
      241 yeplfidpsr gvilsllvqs ptvqeridqg givgyvilam gavgaliala cylrllvigg
      301 kmrkqaksdt vipgnplgev iqayqehkgd nledleakld eiilrnapsi erfissiklf
      361 asvapllgll gtvmgmigtf qaitlfgtgd pklmaggise alvttmlglv vaipllflyt
      421 ivhskgrrlv qtleeqsagf iaryqeklhk aes
//
LOCUS       WP_010445188             261 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Vibrio].
ACCESSION   WP_010445188
VERSION     WP_010445188.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..261
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29356
     Region          7..261
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mfptkenrql frtmvrrevk akyqgtllgf lwnlvtplmm laiystvflt vfkakwhlta
       61 teqadyglml fvgilthtym aevltttsnv irnnsnlvkk vrfpvamlpm isvcsagvny
      121 lfglllafay gafnhyiady tyiiylplvl lvyvctltai aylvsalglf irdvsqmmpv
      181 litvllftst vffsaqsapd elaqvlyfnp ispiadairs ilygqmpnmt hlftlgvvsi
      241 vcgfmtykff grlrpsfsdi l
//
LOCUS       WP_010445255             140 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF805 domain-containing protein [Vibrio].
ACCESSION   WP_010445255
VERSION     WP_010445255.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..140
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15617
     Region          1..140
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 msikellfsf qgrigrktyw vwniiyyili lgfgagiskl fpafsyillp vflmillipd
       61 laittkrwhd rdksiywlal nipliigrva tpmtnpaaqe astpqmlias vslicglwil
      121 vecgflkgta gqnkygpepl
//
LOCUS       WP_010445394             190 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Vibrio rotiferianus].
ACCESSION   WP_010445394
VERSION     WP_010445394.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..190
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22390
     Region          12..187
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhsdlfsdll nhgflenean qliehgqqle lptrhilnhq gefsshiyfv leglchasyl
       61 tdkgkefske fywekdwvig fegliknqps pylletltpc hlfclpievl hqwrtekhpi
      121 yfklleaqlm hkenkerfml lyspkeryql fcqhypdleq ritdsqiaay lgitaislsr
      181 iksrlkkgne
//
LOCUS       WP_010445407             419 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Vibrio rotiferianus].
ACCESSION   WP_010445407
VERSION     WP_010445407.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 419)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..419
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45691
     Region          19..>191
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          144..415
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 msavvklawk slmnrkatai ltimtvaisv vlllgverir tqakdsfant isgtdlivgg
       61 rsgqvnllly svfrignatn nidwksyqef ahhravdwai pislgdshkg frvmgtnhsy
      121 fehykygskq pltfsegkef nglfetvlgs dvakqlgyni gseiiiahgi sdvgfsrhdn
      181 lpfkvvgile ptgtpvdktv hvsleaieai hvgwesgarl gptpkaedlk srdfqpkqit
      241 amlvglksri qtfalqrqin typkeplsai mpgvalhelw gmmsvaeqal mavsgfvvva
      301 gllgmlssll tslqerrrem ailramgarp rhvfsllise aslltfagii tgvaglysil
      361 allqpiiqqs ygihltltal spyewmllgl vqcagivigf ipafrayrqs lsdgmtiri
//
LOCUS       WP_010445679             239 aa            linear   BCT 01-JAN-2025
DEFINITION  SIMPL domain-containing protein [Vibrio rotiferianus].
ACCESSION   WP_010445679
VERSION     WP_010445679.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..239
                     /product="SIMPL domain-containing protein"
                     /note="The SIMPL domain is named for its presence in mouse
                     protein SIMPL (signalling molecule that associates with
                     mouse pelle-like kinase). Bacterial member BP26, from
                     Brucella, was shown to assemble into a channel-like
                     structure, while YggE from E. coli has been associated
                     with resistance to oxidative stress.; The SIMPL domain is
                     named for its presence in mouse protein SIMPL (signalling
                     molecule that associates with mouse pelle-like kinase).
                     Bacterial member BP26, from Brucella, was shown to
                     assemble into a channel-like structure, while YggE from E.
                     coli has been associated with resistance to oxidative
                     stress."
                     /calculated_mol_wt=26864
     Region          5..238
                     /region_name="SIMPL"
                     /note="Outer membrane channel-forming protein BP26/OMP28,
                     SIMPL family [Cell wall/membrane/envelope biogenesis];
                     COG2859"
                     /db_xref="CDD:442106"
ORIGIN      
        1 merisnnasi wlglcliigl gtlgyfiqqt avkyrtyerv vtvkglsere ypadtviwpi
       61 qftvasndvg tmfdeidkqt klvvsyltsk gldkgsisfs spnvfdkkaq qygseqeaef
      121 ryiasqtvtv fshevelvrg aiteigqlgk qgillnqdpy snrieysftk lndikpdmie
      181 eatknareva ekfakdsess lgkikratqg qfsiydrdsn tpyikkvrvv stvqyylsd
//
LOCUS       WP_010445708              93 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HU family DNA-binding protein [Pseudomonas].
ACCESSION   WP_010445708
VERSION     WP_010445708.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..93
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9700
     Region          3..93
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 maitkdqlia diaeatalqk tevrkvleql tdivadqlen ggeitlpgvg klkvterpar
       61 tgrnpstgaa ieiaakkvik lvvakaltda vnk
//
LOCUS       WP_010445940             219 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Vibrio rotiferianus].
ACCESSION   WP_010445940
VERSION     WP_010445940.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..219
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24518
     Region          1..170
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mhfliflgsv rdstpprpar lgmrvsrace klivsqhsqh tveiidplhy dfgdvfkpef
       61 syhrskvpqh lselahkikh adgyvmvspe ynhsmspala nmlnhfgssl fsykpsaivt
      121 ysagqwggar aavsmrtfls elgclpvsam ihipkaqevf deqgvvades eqaqwdsymn
      181 rtlhqliwwa egaslqrdrl dptslaqafq kdpsqrnap
//
LOCUS       WP_010446123             247 aa            linear   BCT 01-JAN-2025
DEFINITION  copper homeostasis protein CutC [Vibrio rotiferianus].
ACCESSION   WP_010446123
VERSION     WP_010446123.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..247
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26229
     Region          2..247
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mntqlevcid nieslhnaia ggatrielcs slalggltps ygfmqqaakq stipvygmir
       61 prqgdffyse eeiemmrwdi eaakqaglng vvlgvltqdg sihmpyatal cefaqalglg
      121 vtfhrafdqc rdaekaleev islgcerilt sglapsapqg idvlralveq aqgriaimag
      181 agvnadnvgq lveqakvtev hlsgkttrps hmtfiaeqsk mgaadvddfs ipvtntdaia
      241 nmvtaln
//
LOCUS       WP_010446216             422 aa            linear   BCT 01-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Vibrio rotiferianus].
ACCESSION   WP_010446216
VERSION     WP_010446216.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..422
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=45817
     Region          1..422
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mkdetlsihf gyetdpttks vatpiyqtva yefdnaqhga dlfnlevpgn iytrimnptn
       61 dvlekrmaal eggiaglvvs agsaainyai ltlaqagdni vstpqlyggt ytlfahmlpn
      121 qgievrfakd dkpeslaeli dentkavyce signpagnii dlervaelah aqgvpvivdn
      181 tvatpvlckp iefgadivvh sltkyvgghg ttlggiiids gkfpwaqhkd rfpvfnqpep
      241 syhgvvytea fgeaafigra rtvplrntgs alspmnafml mqgletlslr merhtenvlk
      301 vaeylsqhdk vswvsyaglp dsefyplaek ymqgkpsail sfglkdgyea gvrfydalki
      361 fkrlvnigda kslachpast thrqlseaeq kqagvspemi rlsvgiehid diladleqal
      421 na
//
LOCUS       WP_010446260             424 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dicarboxylate/amino acid:cation symporter [Vibrio].
ACCESSION   WP_010446260
VERSION     WP_010446260.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..424
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43941
     Region          4..418
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mdkslsskif iglfagllig taiqylfsgv alfdtyllga aegaggmfvs likllvvplv
       61 yvsivcgivd lkditafgrl ggktfalyii ntiiaitaal tvglifqpga danlagtise
      121 tvkltttetp difslvvniv psnpvqafan gdmlqiifma iltglaiqal dsrggpairt
      181 fkmaneimmk lvglvmslap ygvfalmiql gatldantlm svagyvalvv amlvfwifff
      241 ypmavgiatg tspktflrat reqilfslst assnatipvt mrtlteklkv sksvagfgvp
      301 lgatmnmsgv siyialatmf vanafgqpin tadiftlglt illlsigagg vpgggvvmvg
      361 vllhqlglpp eglaiiaavd rindmfctss nvvgdtavnt ivaksegeig keevvdaepa
      421 qasa
//
LOCUS       WP_010446545             272 aa            linear   BCT 01-JAN-2025
DEFINITION  ADP-ribosylglycohydrolase family protein [Vibrio rotiferianus].
ACCESSION   WP_010446545
VERSION     WP_010446545.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..272
                     /product="ADP-ribosylglycohydrolase family protein"
                     /calculated_mol_wt=30462
     Region          33..225
                     /region_name="DraG"
                     /note="ADP-ribosylglycohydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG1397"
                     /db_xref="CDD:441007"
ORIGIN      
        1 miggiigdia gsllegaqlr tynlseakmf chkahptdds iflastaram lddsddfasy
       61 yrhyagifsd ckfgsgmgyw lrtgersehs ygnspaarag vlgyledene vlnlakrsaq
      121 athshqeaid gaqaiawmvw amrkrisaqe iceelyqrwn yyvdqnhshn lvkirkesrg
      181 ldasavntvp laifialyqs hnvetavrac qyvggdtdtl acmagliksq eyapnptwel
      241 mskqilwrka prilqtveef emrfddsksl pf
//
LOCUS       WP_010446785             462 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptide MFS transporter [Vibrio].
ACCESSION   WP_010446785
VERSION     WP_010446785.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..462
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50051
     Region          2..445
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 msnqhqyfgh prglfllfgt elwerfsyya mrailvlylt dttmngglgw stkdaldlyg
       61 iytglvyitp liggyladny lgqrrsilig galmavgqft lampadalgl gslhtfylgl
      121 glliagnglf kpnistmvgd lyqegdnrrd gaftifymgi nigallagvv sgsvtnefgw
      181 kagfvaagig mlvslvmqmt faqswlgdig repaakrdla nknsekkepl tkeevdrikv
      241 ilvmslftiv fwagfeqagg lmniytqqyt drmiggfevp aawfqslnpf fiitlapvla
      301 vlwvklgkre pnspmkfala mfflalgflc mvgavmeqgg dtavktsmlw lvgafffhtl
      361 gelclspigl slvtklaplr laslmmgawf gcnaianyva gyvgshvgel galaifsgia
      421 vtatisgvil llfsntlvrw mhgaenthst aeqieeqqtq va
//
LOCUS       WP_010446954             321 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Vibrio rotiferianus].
ACCESSION   WP_010446954
VERSION     WP_010446954.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..321
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36423
     Region          11..320
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 meqttitlta lafpggpats itgpievltt aaylagvtpp einivtqdnn pvvahggitl
       61 tptvkiesik stdilligsl gepdseltac sekalkwled fadtdipiis istgsfalak
      121 anllskrnat thwryanlfr dmypdtklrv erkvtcdgny yctsctngyn dvmmlvveql
      181 fglsvrdrcq qhifgntdkv qqqslakflp yrqhsdalih qlqdwmhnhh slqfsvfels
      241 erihlserqm krrfklatgq tpiqyiqqir lsaakdklet tkqtveeisr vvgyedvryf
      301 relfkkfvdm tpleyrkryq h
//
LOCUS       WP_010447044             196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator [Vibrio].
ACCESSION   WP_010447044
VERSION     WP_010447044.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22316
     Region          2..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marrndhtre elvnltlstv qeflaensyh dlslrkianm igyvpstlvn vfgnynllll
       61 hvvaqtldel qqqatkatkn skdshqalfq laycyhdfaq qnpyrwqlvf ehnmngaelp
      121 ewhakridgm tgmleallaa iapqrteqev lqasrvlwsg vhgitllsvd dkffssepid
      181 gkelidnlls nylmnw
//
LOCUS       WP_010447134             189 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Vibrio].
ACCESSION   WP_010447134
VERSION     WP_010447134.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..189
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21541
     Region          <115..168
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mteqeyftvh hnltinvevm sedyllpsee sflaeipapf ivasefsqld mladsarlel
       61 qnkdlkhvis lldtqnskln lllsfmlsqq ddpaqrsqtt qfgasqlsyr snllvevgql
      121 vrvklfldhp aaaiycyaqv iecepseqgh lvtlkykllr eadqdllika alyqqqkllr
      181 qrslerdnk
//
LOCUS       WP_010447155             212 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010447155
VERSION     WP_010447155.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24887
     Region          9..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mhkeprkvre frrreqeild talklfleqg edsvtvemia davgigkgti ykhfkskaei
       61 ylrlmldyer dlnellhsad vdkdkealsr ayfefrmrdp qryrlfdrle ekvvkghqvp
      121 emveelhkir asnferltll ikgrisegkl edvppyfhyc aawalvhgav alyhspfwsn
      181 vledqegffq flmdigvrmg nkrkrdtdhs va
//
LOCUS       WP_010447166             423 aa            linear   BCT 01-JAN-2025
DEFINITION  YeaH/YhbH family protein [Vibrio rotiferianus].
ACCESSION   WP_010447166
VERSION     WP_010447166.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11148708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..423
                     /product="YeaH/YhbH family protein"
                     /calculated_mol_wt=48707
     Region          13..421
                     /region_name="DUF444"
                     /note="Protein of unknown function (DUF444); pfam04285"
                     /db_xref="CDD:427839"
ORIGIN      
        1 maqfidrrln gknksavnrq rflkrhreqi kesvadavnr rsitntetge dvsiphkdin
       61 epmfhqgkgg vrdrvhpgnd qfitgdkier pkgggqggga gegnaspdge gqdefvfqis
      121 kdeyldilfe dlelpnlekn qiakitewkt hragyqtagi psniavvrsl qqslarrtam
      181 tagkkrllhe leeelarikn iepaqqleen rlkkeiedlr kkiesvpfid tfdlrfknye
      241 krpvpssqav mfclmdvsgs mdqatkdiak rfyvllylfl trtyenvevv firhhtqake
      301 vdeheffysq etggtivssa lklmneivqd rypvgqwniy aaqasdgdnw addsprcrdl
      361 lvnkllpncq yysyieitrr shqtlwheye klseefpnfa mknirsvedi fpvfrelfkk
      421 eta
//
LOCUS       WP_010447253             546 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Vibrio rotiferianus].
ACCESSION   WP_010447253
VERSION     WP_010447253.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..546
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59752
     Region          1..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mdkydfivvg ggsagcvlas rltedpnvtv clleaggtds spfihtpvgv vammptkinn
       61 wgfetvpqag lngrkgyqpr gktlggsssi nammyarghr ydydlwaslg negwsyqdcl
      121 phfkkaenne vhhdefhgqg gplnvanlrs pseilecylt acesigvprn sdingaeqlg
      181 amptqvtqin gercsaakay ltpnlnrpnl tvitkatthk vlfegkraig veyglkghsf
      241 qircnrevil sagafgspqi lmlsgvgakk eldtygidqv helpgvgenl qdhidlvhty
      301 rcsakrdtfg vslqmatemt kalpqwmknr ngkmssnfae gigflcsded vmvpdlefvf
      361 vvavvddhar kmhlshgfss hvtllrpkst gtvklnsinp ydepridpaf fshpedmeim
      421 ikgwkkqhqm lesdafaeir genfypvdac ddsaieqdir nradtqyhpi gtckmgmetd
      481 plavvdnelk vyglealrvv dasimptlvg gntnaptimi aekvsdkika eyadsqevem
      541 qaaqmg
//
LOCUS       WP_010447402             404 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Vibrio rotiferianus].
ACCESSION   WP_010447402
VERSION     WP_010447402.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..404
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43824
     Region          5..400
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mtsllqqtwq tlmahrmksm laiiaiawgv isvvvlialg egfyrhqtqq lsfmvnnvqi
       61 afpsstskpw hglpsrrqiq ipqdkvdmik qsgfveaass vyakwdasvt ndkgqnltsn
      121 vsgidpsyfs liqrklesgs rnlsptdian htrvavlgdq iakmgeigig qmvkvngipf
      181 lvigiikded agisfgdsrk vfipqttyld lwdakpwmll lkptegmngp afrqaivnfy
      241 akqlhfdptd keainlpdfs egaalitgif rgiqiflgas gamtmavgal gvanimflsv
      301 tertreigvr laigatqksi lsqfilegff lvavgtalgl lvaymvvvll gsitlpewlg
      361 fpvitpdsia wsllvtlvla llasyfparr asrltpvial sara
//
LOCUS       WP_010447488             419 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Vibrio rotiferianus].
ACCESSION   WP_010447488
VERSION     WP_010447488.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..419
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43787
     Region          11..407
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mevlkqksll nnigvqvvia mivgtavgaf mghsatvfap lgaifinlik mlviplvava
       61 lisgaaglgn sqsagkvglv tlgyfgltsa lavalalfmg evfqpgmgid vsgvegmfsa
      121 eyaskgelpt fwatitgmip tnvfqslnea nilqilvfcm ffgiaiskqe karrepiing
      181 vncivdamvw minkvmiiap igvfglmaea vgtfgfgalm vvfklfvvyv aailvfgfvv
      241 ypamvhiftk tsakkfvsam kkpqavalst assmatlpvt mdtcekelgv knstasfvlp
      301 lgatinmsgn aiyyglvaif faqlfnidlg mgayiaiivt stlgavgqag vpgpsflvva
      361 vllaagipie glpllfaldr ifdmirtaln itgdaacavi vdalveeeae qvelqkqea
//
LOCUS       WP_010447637             523 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BCCT family transporter [Vibrio].
ACCESSION   WP_010447637
VERSION     WP_010447637.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..523
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56088
     Region          19..523
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mtkgidkysi dstdytvgqd nvqkwgfdvh npvfgisagf ialfliaalv ldahtaktal
       61 dgikwkiigs fdwlfiisgn ifvifclgli vspmgkirlg gkdavadysf vswlamlfaa
      121 gmgiglmfws vaepvayftg wyetplgvea ntpeaaklal gatmfhwglh pwaiygvval
      181 slafftynkg lplsmrsify pllgdrawgw aghivdilav latlfglats lglgaqqaas
      241 gihhvfgvep glglqivvit vvtllavvsv vrgidggvkv isninmviaf lllilvglig
      301 wavslgsipt tlmayvenli plsnpfgrtd eawfqgwtvf ywawwiswsp fvgmfiarvs
      361 rgrtvrefit avlivptavt lvwmsvfggl aidqvinnvg elgangltdv slamfqmfdv
      421 lpfgnmlsii avvlvlvffi tssdsgslvi dsitaggkvd apvlqrvfwa fmegaiaval
      481 lwiggseavq alqagaista lpftlvllam cvsllmgmrt ekh
//
LOCUS       WP_010447711             374 aa            linear   BCT 01-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Vibrio rotiferianus].
ACCESSION   WP_010447711
VERSION     WP_010447711.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..374
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42474
     Region          <121..365
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mahrsfypfa kplneqmqtl knrmqahlpc vdrvsfakyh pkqgmlksfa esefdtwcla
       61 hheaplrklh nlsiaadnai prlvndlydi nhcpriqtll kegyhssvai pcydqqtftg
      121 fvflnsiqpn afsvealngl kpyfemvqfa vesedhvvna ieilaermqc lmpgyspevy
      181 shtkrigmya kliatelads yqfsdevveq igmftryhal sdiklpadlv cnrrcvnaeq
      241 ealltehieq cvesadniva rignpvhpsv tlfqqitsyq yenldgsgyp ygldrsgipi
      301 aaqiaavanv fdvmtthhpy rqawsipyal lelekrvyqg llsrecvnal rdhqgylkqi
      361 ihkypehyag mglm
//
LOCUS       WP_010447725             740 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Vibrio rotiferianus].
ACCESSION   WP_010447725
VERSION     WP_010447725.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..740
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82109
     Region          25..740
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mnrqfmltpa avaiamvvat pqvlaqeden ivvigqqeds avgpdfsylg aksrtatkmd
       61 lainetprav svvtreqmdd rasisvsdal qytpsiqtny fgednkqdwf iirgfkqans
      121 glyqdgtrly ssgfyswqid pfalervevl rgaasvlygq nppggvinlv skrpqfdags
      181 gqvsleygse drkqisldvn sevneklavr vqglarkngt rvdgveaerf lvapsltykf
      241 tdaseitllt syqkddsdpy lqflpvegtl kpnkngkisd slavgntdwe tfereqvsvg
      301 yefshmfnes tsfvqstrys qmdvklqqmy syvyaadvpg lgplldplne rksilraast
      361 eegssdafni dnrlmhnmqw gsvehnlmvg idyqmvsidg kdfasdplva dgnsilntpi
      421 gmlpdprfdv fnpnysnnvw lldpttlqpl tdadkqrtkv dneqlgiylq dhilvndkwa
      481 vllgaryddt snevhnvttg srtkvdneew tfsvgtayit dtgftpyfsy sqyfdpiiqq
      541 dsagkpakpe sgdqfevgvk yqprtfdgyf nvaayqatke nlarihlnql tqigkvenkg
      601 ieleavanvt psltllgnia yvdseikedv naawvgnsps qvantvssaw ahyrflegtl
      661 dglamglgar ytgesygdnt etlkvpgyfl mdatvsyrig dyklqvaakn ladkeyvatc
      721 dgfcwygdrr nviasltydw
//
LOCUS       WP_010447755              95 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Vibrio rotiferianus].
ACCESSION   WP_010447755
VERSION     WP_010447755.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..95
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10697
     Region          5..89
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 msetifvtae lkmnadkprq qvveaieqfc ldmqsevgcl qanatydske pqrvilwery
       61 enraaieahf amshtqafia aemaelvqaf etqak
//
LOCUS       WP_010447870             240 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein, partial [Vibrio rotiferianus].
ACCESSION   WP_010447870
VERSION     WP_010447870.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 240)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604589
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..>240
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          7..206
                     /region_name="AAA_23"
                     /note="AAA domain; pfam13476"
                     /db_xref="CDD:463890"
ORIGIN      
        1 mafdtftfsn fksfgpkpqt inrkpltlvy gpnsvgkssl lhamllagyq anniqpihks
       61 thfagdvlnl gegnnfihkk andtsctlty ryksdrfleh frgsgypiak slkdsgfniv
      121 dftfekyisf iqniklngyv lpnrivlsma ianpndsnle rhikynkkyf npmfkkcgli
      181 sskeklapli deisnkankk ydienislkt lismfdlely knevdqdfls sqeyvflrda
//
LOCUS       WP_010448051             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Vibrio].
ACCESSION   WP_010448051
VERSION     WP_010448051.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..163
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=18065
     Region          17..159
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mlsavrranf ylnmfgftkv pliwlcrpki laidekhvev riplkrrtkn hlnsmyfgal
       61 avgadvaggf lamskaeeqg erislafkgv kadflkrpeg dvhfvchdgp liddmlrrtl
      121 etgervnqdv kitalcpslh gdepmaefsl tlsikkaaqk qaa
//
LOCUS       WP_010448102             660 aa            linear   BCT 01-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Vibrio rotiferianus].
ACCESSION   WP_010448102
VERSION     WP_010448102.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..660
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=71869
     Region          28..660
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 madkysssas lmsakdssnq ehiisnatvk qalsepfeik amlvssgfdm qdqlgqflti
       61 nryfnesgsn tlnrsyngiv tliqhlgmds nlqnhqyeit lkpwfwllkh thsfrvyqnq
      121 stqeivsdif dnagfkgnfk issmpstkre yclqynesdf dfvsrllaee gvhyyfehts
      181 gshtmilqda qtpfdkasta kfdmketptg slpliedwcp tvafhgasve lssydysqtk
      241 lissgsktss ntianntkla ntryptlgis gdmtdlssnl akrrieyveq dyqsviasak
      301 hdlfelgsyf slsshldkeq lgdfsvvsme veytenaess trlkvipkdt phyprprskq
      361 vvqglqsavv agstagdinq deqgrvriqf qwdtdasgdk tscyvrvaqm lagsgygaqf
      421 vpragqevlv sfidgdpdrp iitgsvynsk nappyaeant tksgiktqls gqsnelyfdd
      481 kkdnellylh aakdltqeve nnqtetikge lsqtitkavs vstednysls vtkalsekak
      541 sisieaddsi elkvgsskit lssssiaiea tnidvkassa lnlegtnvts katsankvsg
      601 tttaleatss nsisglsisi kadttlsaeg slsaefksgl katfdggvmg evkgaivkvn
//
LOCUS       WP_010448146             277 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Vibrio rotiferianus].
ACCESSION   WP_010448146
VERSION     WP_010448146.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..277
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30598
     Region          166..267
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(169..170,203..204,207,211..212,215,257,261)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mlntvqqgfv csllvgivgc sslgypehgn gglaesyqdi sienyqfspv mpdeplgpeh
       61 glrfdwqlsk lhldaliqeg arwcfpaavv qalekqnria releggllld aandlviqrr
      121 rlnqleqqld yvltqtkctp pqdidalrqd ldvvasiyql lnidnqfaid saeinpkymg
      181 hlaeaayllr dhndltlvvt ghadasgdsd ynqklakdra eqvkryltvf gispdrvetk
      241 slgeelplye gqtpgvkltn rrvsieviae tshggtl
//
LOCUS       WP_010448144             105 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Vibrio rotiferianus].
ACCESSION   WP_010448144
VERSION     WP_010448144.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..105
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11799
     Region          5..101
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(20,22..24,30,54,56..58,60..62,65..66,88,92..93,95)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            57
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 melkkietsh tqltleiygd ldakgcreaq sqiddvihsd nhpevevnle nvqfldssgi
       61 gaivylykrl vernrsmrie nvagqpleim cllridhaip vnskl
//
LOCUS       WP_010448164             476 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Vibrio rotiferianus].
ACCESSION   WP_010448164
VERSION     WP_010448164.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..476
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53253
     Region          1..394
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mskaminmsy falaliinks isllmlpvip hflapaqmgk lelltsfnvv ialvvcfaln
       61 ealfrfvgte krtnvqlklr nniytltvsi sfitalalfa ilslvtlpte fmllelivii
      121 lcislegsig igtawlrmkd dkaktlftmm vsttllqvif iitalnasps vlsvllgglv
      181 assiqfawlh linryhfafp skeqiytflr ystpimlagl mafclngaer wfiganasle
      241 tlgvyaiaak falgmcilvq pfgmwwmprr fafleegntn tairithlgv iyiaalttlv
      301 atlayiiiht llpetyhdaf lytlfllpia mlkewyelln lpilykkhtn klllinacsa
      361 slavlllfsl nnigiwgvfi alyiaqmakl vmtlfvgksc ikmrfninll vvmhllsgig
      421 lvlvhsspst fiamlccivm cfiyfliakn ymtkkqrkav ndqvqkwhiq lsrslq
//
LOCUS       WP_010448178             128 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Vibrio rotiferianus].
ACCESSION   WP_010448178
VERSION     WP_010448178.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 128)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 128)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 128)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12153064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..128
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14774
     Region          5..125
                     /region_name="AAA_33"
                     /note="AAA domain; pfam13671"
                     /db_xref="CDD:463952"
ORIGIN      
        1 mtaklilirg lpgsgkstla rklavqqdak hfeadmffet dkgeyqfdaq llgdahqwcf
       61 sqtkkwlkrd rvvivsntfv qrwemqryld lcksegilve ihictgeyqs vhgvplatid
      121 kmrrqwqd
//
LOCUS       WP_010448204             426 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Vibrio rotiferianus].
ACCESSION   WP_010448204
VERSION     WP_010448204.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..426
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48010
     Region          85..404
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mldhhirtfi adklssvgin sdpygveltt vfilasltaa aisylivhhl ivrsvnnvlq
       61 kankplaesl akydvlekls llipimvldv fiplavghyd wlanifdril sisilvifiw
      121 mifalldaln diatfkgitr rmpiksfvql iklftffvgv vvsmsilane spviflsglg
      181 vatgfvmlvf kdtilgfvag iqlsanrmis lndwiqmdsy gangtveeis lttvkvrnfd
      241 ntvsmlpaya lvqnafinwq gmsdsggrri krsvnvdvts irflsdeeie nlksirilrq
      301 yiyeksreis dyneemseep afgnlrqmtn lgmfrayina ylkankdihq ymlimvrqle
      361 ptpegiplqv yaftnntdwa yyegvqadlf dhiysimplf glrpyqmlts ndathltrtn
      421 stssfs
//
LOCUS       WP_010448256             292 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Vibrio rotiferianus].
ACCESSION   WP_010448256
VERSION     WP_010448256.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..292
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=32375
     Region          36..285
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 mkklltvlal sllstsvfas eeiasvdnis qiaslirwsg vffsiiviac twlllkfmss
       61 mvesigsqfv qyrmmlqklq sflqffiylt agsvvfmmsf rindqilali ggtlavsvgf
      121 amkdlaasfi agmtvmvdrp fqvgdrvtfe gnygdiiaig lrsvrmrtlt ddiitipnnk
      181 flsevvvsgn ygaldmqvvi pfyvgmnedi tlardliqea asssryihlp kpvtvlvkqt
      241 itdnylaiql tckayvvdta yeklfetdit lrvmkefkkh sinppkiavh tg
//
LOCUS       WP_010447697             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: 2OG-Fe(II) oxygenase [Vibrio].
ACCESSION   WP_010447697
VERSION     WP_010447697.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Chowdhury,R., Leung,I.K., Tian,Y.M., Abboud,M.I., Ge,W., Domene,C.,
            Cantrelle,F.X., Landrieu,I., Hardy,A.P., Pugh,C.W., Ratcliffe,P.J.,
            Claridge,T.D. and Schofield,C.J.
  TITLE     Structural basis for oxygen degradation domain selectivity of the
            HIF prolyl hydroxylases
  JOURNAL   Nat Commun 7, 12673 (2016)
   PUBMED   27561929
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..200
                     /product="2OG-Fe(II) oxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=23447
     Region          4..189
                     /region_name="EGL9"
                     /note="Proline 4-hydroxylase (includes Rps23 Pro-64
                     3,4-dihydroxylase Tpa1), contains SM-20 domain
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG3751"
                     /db_xref="CDD:442965"
ORIGIN      
        1 mnklidalst hgyyiwddfi sqeevaelrd cipddwkkar igrnddvtri etirsdkiqw
       61 lkrdmgapva sfldkmeeir leanrhfflg lfeyeahfak yekgdfyqkh ldcfkgnenr
      121 rlttvfymne swseedagel vvydlndnei atipprsgrl fvflseqfph evlptnaerf
      181 siagwfring vkdnqldiah
//
LOCUS       WP_010448316             383 aa            linear   BCT 01-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Vibrio rotiferianus].
ACCESSION   WP_010448316
VERSION     WP_010448316.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..383
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43886
     Region          <159..367
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mldypllskt atkekkitai ldelfklaqt sypefsrfsv vlikgkkasn yyvndtiaqp
       61 fgldfedqel rinsslteaa yncqvrivdd lenfdnteri kkliklghks syaspiynrg
      121 siigflfcna tktkffsdeh tqrdfaylsq iisgmfiqld ekqkhfqsal aialkmgher
      181 dpetaehlir mgkyserlar lladknrsit pefihrirly apfhdigkyk ipddvlfsdk
      241 rftaaerevm nqhtifgeri iedvvalsdt smiapdevqf ikniirhhhe yyngtglpda
      301 lcgkdiplea rivtladvfd allskrayka awslsdtanf ikehrllmfd pdcvdmlieh
      361 ldeflairah hrdhegtqna vac
//
LOCUS       WP_010448320             587 aa            linear   BCT 01-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator [Vibrio
            rotiferianus].
ACCESSION   WP_010448320
VERSION     WP_010448320.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..587
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=65134
     Region          11..584
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 melqhitnsn wlstswdrse qaglkqrrrp ddirvtsall edrrhqlhfl idavkqfalp
       61 lfnqlfshsd srliltdaeg viigswgqpk freklteial ssgacwqekl kgtnaigtal
      121 veakpvsvig dqhfiqhhrf iscsaspifd hlgnligvld itseqkkhdf stqvlvqnmv
      181 qqvenqllnq ipkghirvdl aceqgllnsg wqgiiianee gqilahnqva sqllaqtnvv
      241 gqslasildg sasnqslvfk tqplsepktq srsisasndl hygdanvehc wqqanrvidk
      301 disllilget gvgknefvka lhknskrkng plvsvncgal pkdlveself gyvggaftga
      361 nskgyqgkir qahkgilfld eiadlpleaq srllhvlqdk tvlpvgsnqt iqvdtqiiaa
      421 thkdlellvd qgefrqdlyy rlnglivelp rfeersdkqa lienihrrhs eskqsicphl
      481 lslmlsygwp gnlreldslv kvsalmaqge pqlelshvpn hlakklgqsp nivdadtpnt
      541 kdmrstvedk lvktyqanqg nisktsrmlg lsrntiyrkl kslgmln
//
LOCUS       WP_010448606             441 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Vibrio rotiferianus].
ACCESSION   WP_010448606
VERSION     WP_010448606.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..441
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50507
     Region          39..>167
                     /region_name="CIA30"
                     /note="Complex I intermediate-associated protein 30
                     (CIA30); cl21728"
                     /db_xref="CDD:473944"
     Region          276..428
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(313,356)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(318,321..322,326,330,352,354..357)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(348,376)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mkwihklifa lsictitlva lysllgdtrk lvvtpekykf hatndsaegg asqssikwdd
       61 gdlqlncdlk essyawpycg isiytdvkea tkgidlsnyh tvriklryae sgqgtkkirl
      121 ylrnfnevys spqdeytiky ngmqfdssgh tqsieipiqn lqvmtwwlad nkvpiehsgp
      181 efsnitridl atgagaglgh hkiiiekmef egaylaqetl lftllfswma lglafslnel
      241 rkskrafdka qkrhrhlert nntlraqnye faelahrdal tgamnrhavr nwmeqkarqv
      301 rwgtesfsil yldldhfkav ndkyghqmgd dvlrefvmvi assipeeyrl vrwggeefvv
      361 fcpdcsvhqa qeraeklrkn venhlwihge kltcsigvae mqkermteam aradealyqa
      421 khkgrnrvev nfglvslkvv k
//
LOCUS       WP_010448527             399 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Vibrio harveyi group].
ACCESSION   WP_010448527
VERSION     WP_010448527.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi group
  ORGANISM  Vibrio harveyi group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Vibrio harveyi group"
                     /db_xref="taxon:717610"
     Protein         1..399
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45425
     Region          106..372
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mdttqttqdf qylkkgaddy ikrrnlrlla nhrkelrnft raeastylgi daktldkyva
       61 aaeidprrhe dsqwsidise mysvrdllpe nlrkepkfer sesqstqviv iqnqkggvgk
      121 tvsaatiasg latefhqeyr iglidmdgqa tlsmyyapea eqegelsvgd lmmgqfdlde
      181 netleqvyrd aflpttipnl rilpaaqsdr amegwfheqv fshklaspys llsdiinsve
      241 defdiiiidt ppslgyatfn ayfaatsvvf plsitendid atcsyfsyip qvwallenan
      301 hagydfmkil ltnhrdsstt telmnslydy fapylyskef khseairqas sllstvfdms
      361 kseypkskst fqtaqqnsye vtsqilrdiv nvwreqenn
//
LOCUS       WP_010448690             292 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Vibrio rotiferianus].
ACCESSION   WP_010448690
VERSION     WP_010448690.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..292
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31499
     Region          2..291
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mlhqvvsilf pvfalvfvgy lvsrfikpdf rpinrinmdv ftpalvfssl vsmpidmgqv
       61 plllaaiiav ivpgivmvpi tkltglsfka wapphmfrns gnlaiplfty tfgelalpsa
      121 vllfvvsacl hislgvmlls sgnplkqiik mpiflsasla lamnlsgvsi cnplyeatal
      181 lgqaavpvml lslgaqmlnl rldglkvglv ctaqslgtga iafaliywli plpimqlqmm
      241 vlftmlppav mnylfaerln iepmtvasmv lfgnffsilt lplllmftls ls
//
LOCUS       WP_010448971             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Vibrio harveyi
            group].
ACCESSION   WP_010448971
VERSION     WP_010448971.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi group
  ORGANISM  Vibrio harveyi group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Vibrio harveyi group"
                     /db_xref="taxon:717610"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34294
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,222,239,265)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnnlswrgir afiyvaecgs ftsaaeamga skanvsqlvs elesslgvql lyrttrqlrl
       61 teigdgyfrk ckeamlqlda aaewaqqtts eikgrihmns vggpigeeli aplvmsfqsa
      121 ypnveveldf skhrvdlied sydlvlrvge mpdstliarr lttlrthyva spdflerhpk
      181 ilipedlkal plihgsvdhw imknhneqri invgqgikaa tgrtmrhaav sglgvtrltd
      241 vychadlasg rlievlpews ektllslvcp pvkyqlprvk mlmdwiserf eehykqfrfe
      301 gehss
//
LOCUS       WP_010449292             162 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010449292
VERSION     WP_010449292.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..162
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18271
     Region          5..145
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 megqvkldri disilvelqk dgrmtnvsla davglsaspc lqrvkrlesa gyissykahl
       61 nlakitdsvt vfteitlsdh kredfakfes nirlvdevle chlisggydy lvrfmtrsiq
      121 hyqevvesll dknigiskyf syivikspvl kdgvplrkll rh
//
LOCUS       WP_010449448             562 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp70 family protein [Vibrio rotiferianus].
ACCESSION   WP_010449448
VERSION     WP_010449448.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Fernandez-Fernandez,M.R. and Valpuesta,J.M.
  TITLE     Hsp70 chaperone: a master player in protein homeostasis
  JOURNAL   F1000Res 7 (2018)
   PUBMED   30338057
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Mayer,M.P. and Bukau,B.
  TITLE     Hsp70 chaperones: cellular functions and molecular mechanism
  JOURNAL   Cell Mol Life Sci 62 (6), 670-684 (2005)
   PUBMED   15770419
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Bukau,B. and Horwich,A.L.
  TITLE     The Hsp70 and Hsp60 chaperone machines
  JOURNAL   Cell 92 (3), 351-366 (1998)
   PUBMED   9476895
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Rensing,S.A. and Maier,U.G.
  TITLE     Phylogenetic analysis of the stress-70 protein family
  JOURNAL   J Mol Evol 39 (1), 80-86 (1994)
   PUBMED   7545947
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..562
                     /product="Hsp70 family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
                     /calculated_mol_wt=62484
     Region          11..473
                     /region_name="DnaK"
                     /note="Molecular chaperone DnaK (HSP70) [Posttranslational
                     modification, protein turnover, chaperones]; COG0443"
                     /db_xref="CDD:440212"
ORIGIN      
        1 mhsvevshkl aigidlgttn saisvwqddk avfipnslgk fltpsvvain ekdellvgea
       61 aksrlvtnpl csvasfkrfl gtnktfklak keynavelcs lilaslkqda etylsqpisd
      121 vvisvpayfn dsqrkevkaa arlaglnavr lineptaacl syslhkqans rflvfdlggg
      181 tfdvtvvehf dsfievrast gdnflggddf tddvihavla rlqlapeelp lsflsslrah
      241 cetakhryed glivevpepy gqkiqftkqd meevwkssld rilrplgqal sdarlesnqi
      301 delifvggat rlrliqstan rllgrfghse idpdlvvaqg aaiqaacrlr nehvseiilt
      361 dvcpyslgil crrgdregvf spiierntii pvsrvqtfst cnddqtdicv aiyqgerlwa
      421 kdnifidefv vdipkgkagq elidirfsyd ingllevdvt pqstgetvsk vidktpegis
      481 qeqlemshak lsrlkfhpre sipnitllek lhqlyaenta efrtvieeyi fafemalasq
      541 deleirekrt liyqqlgrlg lk
//
LOCUS       WP_010448623             387 aa            linear   BCT 01-JAN-2025
DEFINITION  lipase family protein [Vibrio rotiferianus].
ACCESSION   WP_010448623
VERSION     WP_010448623.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Wong,H. and Schotz,M.C.
  TITLE     The lipase gene family
  JOURNAL   J Lipid Res 43 (7), 993-999 (2002)
   PUBMED   12091482
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Cygler,M. and Schrag,J.D.
  TITLE     Structure as basis for understanding interfacial properties of
            lipases
  JOURNAL   Methods Enzymol 284, 3-27 (1997)
   PUBMED   9379943
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..387
                     /product="lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=42795
     Region          3..221
                     /region_name="Lipase_3"
                     /note="Lipase (class 3). Lipases are esterases that can
                     hydrolyze long-chain acyl-triglycerides into di- and
                     monoglycerides, glycerol, and free fatty acids at a
                     water/lipid interface. A typical feature of lipases is
                     'interfacial activation,' the process of...; cd00519"
                     /db_xref="CDD:238287"
     Site            order(85..86,88..96)
                     /site_type="active"
                     /note="active site flap/lid [active]"
                     /db_xref="CDD:238287"
     Site            141..145
                     /site_type="active"
                     /note="nucleophilic elbow [active]"
                     /db_xref="CDD:238287"
ORIGIN      
        1 mpkltpvlss qlaylpyqli sntdnkylkv sgdikrqfif nkekasfhgk tggifgigrk
       61 segfalvgig kgkykeemvv tvrgtktihn witngniglk gspngaiahs gfvnafysik
      121 pdlkrfilsq phmpkhihcv ghslggalas lvsdwvteef kipvslytfg aprigqesya
      181 rksesrntni frcthgadpv pliplwpfih apfsnkeyrl ddscglyfst hgmgpndvpg
      241 yintakcnsw delkeqsvay lnkpvrlnfd nrhqaaytsr wanllsaalv tllndagprh
      301 akameiqarl sggmtfydkl akelegivsa sdklrdqtig llghmlvfag rsvskitdls
      361 ssfirwvfkv tidklystak qafdsif
//
LOCUS       WP_010449586             359 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Vibrio rotiferianus].
ACCESSION   WP_010449586
VERSION     WP_010449586.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..359
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40751
     Region          209..348
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 msehepvlss eqalddyfsa lldeefesqe spldlleqel sseepepepe pepepepepe
       61 pepepepepe pelkleysqp esyqyhevys peleapnled vqrllsqles tnvvaeldid
      121 dileqntidi asetkhqeve vevaeqvvve eeiqewaiee psvpdsvlet vaiepveeiv
      181 epivdtdlem eveldtqagp epsrewestq rsedfqvlyf dvngvtfavp ldelggihri
      241 aelnhligrp dwylglqtsr enqydvvdta kwvmpdklss deykdsyeyv vmlgesmwgl
      301 asnqllgtet lnvdkvrwre qagkrpwlag mvkekmcali hvhaligmln agldvkslk
//
LOCUS       WP_010449819             334 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Vibrio rotiferianus].
ACCESSION   WP_010449819
VERSION     WP_010449819.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..334
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=36774
     Region          31..320
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mkkwlvafas llvlagceqp adqvhlsgpt mgttynikyi eqdglpspev lqteidrlle
       61 evndqmstyr edselsrfnq hqtsepfevs pqtatvvkea irlngltlga ldvtvgplvn
      121 lwgfgpearp dvvptdeela arkantgihh lsvegnkmsk dmpnlyvdls tiakgwgvdv
      181 vadylqsqgi hnymvevgge mrlkginreg vpwriaiekp tvdersiqei iepgdmaiat
      241 sgdyrnyfes ngvryshiin pqtgkpihhk vvsvtvldks smtadglatg lmvlgedkgm
      301 eianennipv fmivktddgf kelaseaykp fmkk
//
LOCUS       WP_010449967             338 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Vibrio rotiferianus].
ACCESSION   WP_010449967
VERSION     WP_010449967.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13537404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..338
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=37004
     Region          6..>313
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Site            order(50,53..54,57..58,60,86,89..90,93..94,96..97,120,
                     123..124,127..128,131)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          50..77
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          84..114
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          119..146
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          180..208
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          181..>324
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Site            order(181,184..185,188..189,191,215,218..219,222..223,
                     225..226,249,252..253,256..257,260)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          213..243
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          248..273
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          277..307
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdirktvlig avillaacss qqndsdfdgs lysgkpvesl tsdappatee eaiqrgdaal
       61 nnnnidlaly eyirslafpn aqhkdktlyt vgkihlvren yeladrsfra slaenpdhig
      121 slaelgklnt kqgkkevgqs yylrainadq irlggepnlt kdsiskesva glrfdessps
      181 esyvglgvla dvrgnhetaq allrkaveid nrnvnalvsl gysyymiedy frathftsaa
      241 lsvspsnera innlglisla kgqprqalsi fnkhmsepea lnnvgyflil qgkpdeaipy
      301 lqqainknps yyemanknle ralamvregt dtstailq
//
LOCUS       WP_010449971             322 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Vibrio rotiferianus].
ACCESSION   WP_010449971
VERSION     WP_010449971.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..322
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36263
     Region          107..318
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 menqgpiflf llflsvvfis qalilpsagk kvkqkqllkr ikesrknvda esinllrana
       61 lkdlspleqq lvqigifdnl krklelagin vgfskfllas llggvavall flffgqawyl
      121 ciavmfliwv ceylyiqkri dqrlmkfeeq lpealdiikr vlqagqpinq afgevgremp
      181 aplgpeflkt fnllnygydl rlaimqlter tptismlafa savmmqketg gnlieniekl
      241 srilrarfkl trkiktisae srmsawilvl apfamyiiia iskpdyiapl hntptgvkli
      301 gmgmvalfig tlwirkivsm rv
//
LOCUS       WP_010450009             783 aa            linear   BCT 01-JAN-2025
DEFINITION  PilZ domain-containing protein [Vibrio rotiferianus].
ACCESSION   WP_010450009
VERSION     WP_010450009.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..783
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=88598
     Region          145..>224
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
     Region          470..570
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mqqseilsla erlipvygsn dfdfvlgqlt egeapsakil vkmelkrimt pctksidlrg
       61 rvkgecreyi ldgiahwldd vafntyhkni krfggytegv wetlvntrnn frvmgnsnaa
      121 nqatqltdpk spflsepvhl gydlkrqekr lrvqsqveik largqvlhgl sidlsssgak
      181 fkvpsafkya lgeiiqvtfs eisgksqvag iekpleyrvl avddcyends vkylrtlrlt
      241 dtniiarvid ealnsaskra rhdnqdkiir artrgyehia lkhtgnlplf fegsklklam
      301 ltpnnqklwq ywhdernqqs lgalfnpqrv aslikagvkg asnvlysfth ehegkvyfys
      361 mlmpeatreq rqlfwhlgar rkswkafris ifelskkeke dlaafstela nsseslshvg
      421 ilqeisdfna gadylltekp rlpantlnnf rhprkvvgnp kgiyfdarsr rkepryrfkt
      481 plvltasdki qssgftldls krglglildt ptplrsgqev rvnfrelqly dkklplsevp
      541 yrvirvspdg kgvqlviden sktikviafl nsiiehnqdk lipqkellps nallerlhci
      601 llsrivstpi fvskqsssti ktpvmgvnfp lpkhvelfar lghkqhysle plfkgrsstl
      661 iaepikridg aqakhhdayi sveytgkkit giqsklhgef ssikerimfi kkarmagefl
      721 avrissapif damtsllekd lsdltqfgvh qasklekelt alvgyieled iteevlirle
      781 ltq
//
LOCUS       WP_010450493             155 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Vibrio rotiferianus].
ACCESSION   WP_010450493
VERSION     WP_010450493.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..155
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16572
     Region          1..>55
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkarhissgf tlielvmviv ilsvvslyaa srylsagipa aavqdqaiav irqvqvnrmq
       61 snlsdttivd kndfilnvtn ncigskascs sqtesrsdwf mpdgvsfspn lelefnllgn
      121 psgatptiqi tengsgktcs ihinsqgyve krtcs
//
LOCUS       WP_010450658             198 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator [Vibrio].
ACCESSION   WP_010450658
VERSION     WP_010450658.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23099
     Region          4..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mklsekkria lieaaqqefi ehgfsganmd rvceragtsk rtlyrhfesk dvlfiesiqa
       61 vmeiqrarlq fqyspeesie aqlrtyllak ldsmyedfgl plakmvisef mrtpelveny
      121 lhqlqsqdeq lekwfseaid dqkiknlnpa mmsnmlmcll kgnflwpqli anhkvpnleq
      181 rkksiedilt lfldgyrc
//
LOCUS       WP_010450698              96 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Vibrio rotiferianus].
ACCESSION   WP_010450698
VERSION     WP_010450698.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..96
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11060
     Region          2..80
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mihlvaeika fpnhieqvtq lltdllvptr eeegccqyel yldqnieglf mfqeiwasqe
       61 aldkhlqsph iakcfstlee nalleytqir plrfvg
//
LOCUS       WP_010450799             491 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Vibrio rotiferianus].
ACCESSION   WP_010450799
VERSION     WP_010450799.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..491
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53032
     Region          9..479
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mwnklnksmm fcqmmfglsf ygvlvsltrf fledlnynea dtmmivgafs aigplfaiag
       61 gfiadkflga yrslsiafla fasgyallvl gasatnvpls mcgialasyg rglmspsyps
      121 lykrtfksqe dfekgypiny svnnigaflg qylfpmivli igfnggftis avmagaalvm
      181 livfrkglvg vasdldrqsv smknwiffai isaamialvf fmfsnmdigq nivyaiggaa
      241 ilyfvslmlk askaeslkmg tilivtfltt cffvyygqmm tsmnmvaint lkgslfgfip
      301 lepeaamamn plwcmvggpi vagffgmlek rdihlstatk ialafvltai afgiltfavt
      361 tvgedvvimp eiflaihffq aiaevivgsm vvafilsvap khienfsvsl fsvaialsgi
      421 vgaafstsia lekgqeitqe ivqhvygdyf qlltilavvm vaialgasfi irkmleaakq
      481 seaelevveq n
//
LOCUS       WP_010450854             133 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Vibrio rotiferianus].
ACCESSION   WP_010450854
VERSION     WP_010450854.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..133
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14549
     Region          1..129
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mevlkgsclc gkvklevade fkymgnchcs ecrkftgsdy ssaggvaldk liviegaehi
       61 qtyqksante lsfcrhcgss lyskknngiv nvrlgilddi padkpsfhif vgskapwnei
      121 tdelkqfeae pkl
//
LOCUS       WP_010450986             542 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Vibrio rotiferianus].
ACCESSION   WP_010450986
VERSION     WP_010450986.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..542
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=59174
     Region          22..542
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mqfslknlsv rtqvlvpvlf tafalfialw itknnlqaeq evvasnsdsl vfykdtlahi
       61 ddqvyplris avyaiydvsr rdgflnelka gmkeiesdld kiearetfrk eavqvrkgie
      121 ayvdystrav effnrhdrgq vsdseyrnfi sqyrrvgnem vstinalsqr vneiateata
      181 ssnrenirvq nnamitvlsv fvfslvgawf lsgmivtpiq klqevmrkla dgdlsvradv
      241 dgdneisqls kdvnqtasql hdtvdhltri seevasaste laavmtqaea naqqelaeie
      301 qvasavnela stannvsdna tsadatarea dglaqsglai fqesaqaseq msqalndaaq
      361 vvmrlkdqsv qindvievir gvseqtnlla lnaaieaara gesgrgfavv adevrmlaar
      421 tqdstqeiss iieelqaqsg landsmqvsl emlarnnelt qqandalvgi tesvaninds
      481 ntqvataaee qsqvtqdinr nvvnmselvn qnvagisqsa sastelshla ekqkeqlsff
      541 kl
//
LOCUS       WP_010451117             409 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Vibrio rotiferianus].
ACCESSION   WP_010451117
VERSION     WP_010451117.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..409
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=44785
     Region          1..387
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 msnfvvvggg aaglemvtrl assfagksdh tvtlvepssh hlwkprlhei aagtfdneld
       61 svafrlhaac hgyqyvqarm sglnraekai tvsselspeq tlkydylvia vgaisndfki
      121 pgvsdhclfl dsasqaekaw eqmkqmlasg gshrvsivga gatgvelaae wakvskqlnr
      181 yqndtqlsit lieaadrvlp asaecmsakv lkklqkqgvn vrlntkvqra eadrivtene
      241 iipadlqiwa agircpdwla nldglesnri nqlkvlptlr ttldenvfvi gdsaecpqed
      301 gsvvppraqa anqaaahlak qlkrlvkgke lkpfvfkdgg mvvalghdya vgalmndkvv
      361 lrgryvrrly dtifrlhqrv ifgwfrvsal vvlkrvkgll npyykgsws
//
LOCUS       WP_010451236             448 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: magnesium transporter [Vibrio].
ACCESSION   WP_010451236
VERSION     WP_010451236.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Baykov,A.A., Tuominen,H.K. and Lahti,R.
  TITLE     The CBS domain: a protein module with an emerging prominent role in
            regulation
  JOURNAL   ACS Chem Biol 6 (11), 1156-1163 (2011)
   PUBMED   21958115
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Hattori,M., Iwase,N., Furuya,N., Tanaka,Y., Tsukazaki,T.,
            Ishitani,R., Maguire,M.E., Ito,K., Maturana,A. and Nureki,O.
  TITLE     Mg(2+)-dependent gating of bacterial MgtE channel underlies Mg(2+)
            homeostasis
  JOURNAL   EMBO J 28 (22), 3602-3612 (2009)
   PUBMED   19798051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..448
                     /product="magnesium transporter"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015095 - magnesium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015693 - magnesium ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49119
     Region          8..447
                     /region_name="MgtE"
                     /note="Mg/Co/Ni transporter MgtE (contains CBS domain)
                     [Inorganic ion transport and metabolism]; COG2239"
                     /db_xref="CDD:441840"
ORIGIN      
        1 mskfqdlstl ieqivqadea dqvtalndsi ecglepgava lileafpide rvrlwralpl
       61 elhidvltem radvrlsiie alseielklt lakldnlsli ewadslpeef inealeliek
      121 delelydqan eyedeqlgrw aerkiitlpf nitigkarrl merysydtpq qvylinrkkq
      181 frgavnyyei lrsdpdirls tlaietvnvl dskmelpeav ealehsalpa lpvtdsdqtl
      241 igevdwqfal stqreiyear lmagtgmdeg ddlfapvlks sqkrgvwlgi nlltailasv
      301 tiglfehvis qvvalavlmp ivasmggiag sqtltlmvra malnqitpgn rfallknelg
      361 igslngllwa liigglaglw fqspvlggti alaiivniit aalfgvlipi vldklkldpa
      421 lagsvilttv tdvvgffafl gtaslvml
//
LOCUS       WP_010451180             307 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Vibrio].
ACCESSION   WP_010451180
VERSION     WP_010451180.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..307
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33917
     Region          4..307
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mnkiniaivn ypgaskasvy glqelfeman rasieldvec rfhadiidwk egviradeft
       61 vvilppsgae qyylspseal tswlfeqhka gavvtsacag afvlaqagll nnkactthwg
      121 lsglfrdrfp nvtlkpesil inegsiitag gmmswldlgl elvsqlstpa vmrllgkmlv
      181 vdtgareqrf yqqftpnfqh gdsavlsaqh ymadhfshvi snqalseisc ltertlqrrf
      241 qkatglnlnq ylqhlrvqka cdllessnla feviayqvgy qdasafrkvf iktmglapka
      301 frarfsa
//
LOCUS       WP_010451264             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Vibrio].
ACCESSION   WP_010451264
VERSION     WP_010451264.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21602
     Region          1..203
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtltvwlslf tvcllgamsp gpslaivakh slaggrvngf atawahafgi giyafitlig
       61 lavvlqqspl lfktislaga aylaylgfna lrskggvaak lesgeettvi qsaregflis
      121 ilspkialff ialfsqfval gndlsnqmii vatpfvvdgl wytfitlvls nsrvvdrirs
      181 kavlidrlsg ivlmllavrv vvti
//
LOCUS       WP_010451415             430 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Vibrio].
ACCESSION   WP_010451415
VERSION     WP_010451415.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..430
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47913
     Region          1..416
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfssqgfap evvkalaecg yekltpiqqk aipmarkghd ifataqtgtg ktaafslpmi
       61 qqllesgrsa srktaralim aptrelaeqi adnikaytky tdlsvaaifg grkmssqvta
      121 leggvdilva tpgrleehie qgnvsvanie flvfdeadri ldmgfihavr kimmdvdtdp
      181 qimmfsatts sqlnllakdi lrkpkrieve ranttaqtia hvlypvdqer ktellselig
      241 rknwkqvlvf vnyketandv vkelkldgik avvchgdraq sarrraleef ktgkarvmva
      301 tdvaargldi edlphvvnyd mpflaedyvh rigrtgragk qghavsfvnr eeeltvvqve
      361 nliqqhirri elagyepkqr esyieklnsk pafknrqgrr nnpnqsatdq gsaerrlamv
      421 krlkarrssn
//
LOCUS       WP_010451580             215 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Vibrio rotiferianus].
ACCESSION   WP_010451580
VERSION     WP_010451580.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24280
     Region          2..74
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(13,15..16,18..19,22..23,67,70..71)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(13,52..54,65..66)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(52,64..65,67..68,71)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          88..198
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(90,97,156,159..160,163,167)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(90..91,94..95,98,133)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(97,101..102,105..106,164,167)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mklfianqny sswslrawli fsqfklnvev tklklftedf yktlegitpt akvptlvdgd
       61 atvwdslail eyvneqylqg qawpsnsaer akaraiaaem hsgffdlrne lpmnirarrk
      121 vvltdgarkd iaridaiwae qaklhpngwl fgewsiadam yapvalrfqt ygielsegak
      181 ayqqkvlase slqqwleeas qetdiveede agvev
//
LOCUS       WP_010451614             321 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Vibrio rotiferianus].
ACCESSION   WP_010451614
VERSION     WP_010451614.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..321
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33714
     Region          9..321
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 menkplatlv vvehdnqsls vdtlralsaa sqvqqdvasl pvtallvghq cssvldelkc
       61 vqgisqivvi daaeyqhala enqstliaei grdyshilap astfgknlmp rvaavldvgq
      121 lsdviaiesl dtvvrpiyag nalarvrsdd atkvmtirss afdtidlsds pvvenvvtle
      181 tvikaehsef vsqqkaeser pelpaanvvv sggrglgske nfalveqlad klggaigasr
      241 aavdagfvsn dlqvgqtgki vapqlyiavg isgaiqhlag mkdskvivai nsdpeapifq
      301 vadyglvgdl feimpellek v
//
LOCUS       WP_010451644             171 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Vibrio rotiferianus].
ACCESSION   WP_010451644
VERSION     WP_010451644.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 171)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..171
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19110
     Region          33..166
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 msktihtwkq islveeeinl ptgrmithtt iqhpgaavil pitpdgkivl vnqfrpslnk
       61 wllelpagtr egdeeplhca qreleeetgy saekftslgq vtplagfcde iqylfvaeql
      121 nktnryecdd devievvtls reeleqkiiq giitdaktia clskarlcgy i
//
LOCUS       WP_010451697             386 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Vibrio].
ACCESSION   WP_010451697
VERSION     WP_010451697.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..386
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40685
     Region          16..371
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,140,
                     143..144,147,214,217..218,221..223,226,250,254,303..304,
                     308,312,328,331..332,335..336,339)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mentaipats prvtvpvval slyavasgyl msliplmlge ynisadyasw lasvfyggll
       61 vgaifferiv rsvghrkafv gclatfsfti valplvpngi vwlvarfiag mavagvfviv
      121 eswlmsgdes srakrlslym lslyggsalg qfgigilgvs ggvpfvaitt lilmailvll
      181 fidceqpnsh estalsfkqi sklshaaiig civsgltlga iyglmpvela nrkishqdig
      241 tlmalvilgg mlvqpmvtal nkymartvlm affcilgifs igltfvsssa vvlaaalfll
      301 gmatfalypi ainlgcegld erfivsatqv mlfsysvgsv agpvvadkfm gqmhgllgyl
      361 faallatciy mliaatkskh qmaagl
//
LOCUS       WP_010451827             206 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA-J related domain-containing protein [Vibrio rotiferianus].
ACCESSION   WP_010451827
VERSION     WP_010451827.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Hahn,Y., Lee,J., Seong,C., Yoon,J. and Chung,J.H.
  TITLE     Structural analysis of phylogenetically conserved J domain protein
            gene
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 325-333 (1999)
   PUBMED   10542335
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Cheetham,M.E. and Caplan,A.J.
  TITLE     Structure, function and evolution of DnaJ: conservation and
            adaptation of chaperone function
  JOURNAL   Cell Stress Chaperones 3 (1), 28-36 (1998)
   PUBMED   9585179
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10574573
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..206
                     /product="DNA-J related domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=24227
     Region          23..136
                     /region_name="DNAJ_related"
                     /note="DNA-J related protein; pfam12339"
                     /db_xref="CDD:432489"
     Region          157..205
                     /region_name="DnaJ"
                     /note="DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock
                     protein 40) proteins are highly conserved and play crucial
                     roles in protein translation, folding, unfolding,
                     translocation, and degradation. They act primarily by
                     stimulating the ATPase activity of Hsp70s; cd06257"
                     /db_xref="CDD:99751"
     Site            order(182..184,193..194,197..198)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mdeqcnvcqn sqqymenpll wpileilkkq psdwkvhtla qelsehgyip qldsspdkdl
       61 fkrnfllmna lyqlqetlyp dgwlqveamn ivlmsaieas rhsidtndpl reyyldwkny
      121 eanegevrrl lnefwsryqr yiggnsssdl drakalslfe lsadatkaei rkqwrklalr
      181 whpdrdngds erfrvlcdaw nvlrng
//
LOCUS       WP_010451844             261 aa            linear   BCT 01-JAN-2025
DEFINITION  M48 family metallopeptidase [Vibrio rotiferianus].
ACCESSION   WP_010451844
VERSION     WP_010451844.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..261
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28032
     Region          64..245
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(126..127,130,190,194,233)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(126,130,190,233)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mktwikasvl fslvgltacs asptgrnqil mfsdqemssl gansfdqmkk eipiskdkkt
       61 nayvqcvakr itdtippqag fndwevvvfd sdqvnafalp ggkigvytgl lkvaknqdql
      121 atvighevah vladhsnerl sqsqlanagl slanvaigas eykqyqqatm aalglgvqyg
      181 vmlpygrtqe seadivglgy makagfdptq sidlwknmsk aggeqppeff sthpshstri
      241 kdlqatintl paynvkapkc s
//
LOCUS       WP_010451934             244 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Vibrio
            rotiferianus].
ACCESSION   WP_010451934
VERSION     WP_010451934.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..244
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27331
     Region          7..241
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mkeknivvef sgvnkwygey halkdinfsv htgeivvvcg psgsgkstli rcinhlesiq
       61 egelsvfeqp agskmqkpgk vgmvfqhfhl fphltvlenl tlapirtlkl skqeaekram
      121 qylkrvniee qankypiqls ggqqqrvaia rslcmepdll lfdeptsald peminevldv
      181 mvelaqsgmt micvthemgf akkvanrvvf mdegeiiemn spialfetpq hprtqaflnq
      241 ilsy
//
LOCUS       WP_010451955             317 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Vibrio
            rotiferianus].
ACCESSION   WP_010451955
VERSION     WP_010451955.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..317
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35683
     Region          3..316
                     /region_name="COG2374"
                     /note="Predicted extracellular nuclease [General function
                     prediction only]"
                     /db_xref="CDD:441941"
ORIGIN      
        1 msnknhitfa sanlfnfiap pgayydfeni yslddwhdkl awtksqfeql dpdviglqev
       61 fsieetkaff aeigyeyfat vdtphiegdy iysrpvvava srfpiesfea vtfdkealna
      121 fgeidaptfs rkpvracivh piighisvyv thlksqrpad sdtpeqasrp iarwlstqqr
      181 gweaamlrda mqrqyalipm ptvlmgdmnq aitptgvndv ltehygdsvt dlqlndgwel
      241 qmspslesrp athyhfakgn vldyillsqe fdahadvsia evtdyqvlds hlinpsferd
      301 knasdhafva ltveikl
//
LOCUS       WP_010451968             241 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Vibrio rotiferianus].
ACCESSION   WP_010451968
VERSION     WP_010451968.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..241
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27836
     Region          11..149
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mterkqgrrs aeaaeqtkcl ilrvaadmfc elgyervslr nisekagvsh slirhhfgsk
       61 ekiwqavsda mdefmqgyma qlvdempant psnqkiylfm vrmlafalkh phpiqmiada
      121 irhgddallq yflkskdefa aiftelfaey nveypehqid qweskwqmlv fahgaisltp
      181 mmqetwpeda dnrekmllnh welfntiman qfsvnkedmi hpselseivt qmccpieelt
      241 a
//
LOCUS       WP_010451977             188 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Vibrio
            rotiferianus].
ACCESSION   WP_010451977
VERSION     WP_010451977.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..188
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20946
     Region          41..179
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msteftyyda gtapeeskal veqslkgfgm lpnlhavlae apatyeaynt afelfmkntt
       61 fspleqqvvf mtanfennch ycvpghtwmm kagkmpdevi ealregtpip dvklqalhdf
      121 tkelldnrgh igderlqafl dagftkrqal evltglsakl isnftnaiah tepdapfqky
      181 awthpser
//
LOCUS       WP_010451986             304 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Vibrio rotiferianus].
ACCESSION   WP_010451986
VERSION     WP_010451986.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34149
     Region          11..>203
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          139..298
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
ORIGIN      
        1 mtvqfdklat ldfkmlrtll vlmetknvsq saerldlqqs tvsyqlgklr dalgdpllir
       61 sgrgleptsy aqliqpalsa hfnamesllf dshfdekttt gtvrlachrn gsrkfvsgll
      121 selksrlplv rleivdwaeh vpsmlregvi dfavgfeper ssqiqslplv dvgyqivmak
      181 ahpmaeevis eenvfdypha iistneaver wldyladrqk kerliefast smefttmaie
      241 gtqrlmfvad tkdgffdnyn vttqpapfia kqnvkllfhe rasvdplkac mleiikatas
      301 kvfa
//
LOCUS       WP_010452029             191 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Vibrio rotiferianus].
ACCESSION   WP_010452029
VERSION     WP_010452029.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..191
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=21751
     Region          3..191
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mkkvlvinan pktdsfcksl adnyaltaal kyevkqveis emhfeisldn gydsrtslep
       61 dllrfqelvl waehiviitp vwwgtvpakf kgivdrvflp nfafkytegn mfpekllsgr
      121 sselfitldt ppllyklfkg nviykhlkks ildfsgiknr satyfgpvmg sninkrnnwl
      181 dkvaksarki k
//
LOCUS       WP_010452158             240 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Vibrio rotiferianus].
ACCESSION   WP_010452158
VERSION     WP_010452158.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..240
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25419
     Region          11..231
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mdfdstnlla mgliflgsyv qtaigfglai vaapllilwa peyvpapicl valfislmna
       61 mkhrssveig glkmalmgri pgslaggall ffvstealtl wigflvlfav avsvlpfrie
      121 ptpgrmtfag ffsglfgtss aiggppmall lqhqeanqlr gnlsaffvfs siislvvqip
      181 vgfftlhhlv itlpllhaga lgywlaiktt qtlpkekirf galilcfvsg itaviqglal
//
LOCUS       WP_010452288             191 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Vibrio rotiferianus].
ACCESSION   WP_010452288
VERSION     WP_010452288.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21808
     Region          2..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 markanfdrd eklllamdvf wrkgfantsi sdltdelnin rfslyntygd kqqlyyeald
       61 tylkkvslps lndlekddas lpelesflks faelqrkrnc gcfiqnalie hagedddvlr
      121 kghflfdhli diiadaltna qketlvpktl kpeelarfvl nnmqgmrvlg kakryadldt
      181 alscllvlir k
//
LOCUS       WP_010452306             305 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Vibrio rotiferianus].
ACCESSION   WP_010452306
VERSION     WP_010452306.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..305
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33714
     Region          17..302
                     /region_name="hydrolase_YghX"
                     /note="YghX family hydrolase; NF041440"
                     /db_xref="CDD:469331"
ORIGIN      
        1 mvlkhtttkq kashpipqea fdwyddyahg kisrreflnr lgglavlgfs mtalvdaltp
       61 nyalaeqvsf ndpdikatye tfpspnghge grgylvmpqk ktlksptvlv ihenrglnpy
      121 ikdvarrlak dgfiafapda lyplggypgn ddegramqke mdrakieqdf iaaanfikqh
      181 edgngklgav gfcfggyivn mlaavmpdel dagvpfygtp aaqeiqkqvk gplmihfagl
      241 dkrvndtwpa yeqqliatda qyqalmyenv nhgfhndsta ryapeeaala wertlgffkq
      301 hlass
//
LOCUS       WP_010452378             226 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator [Vibrio].
ACCESSION   WP_010452378
VERSION     WP_010452378.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..226
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25715
     Region          32..221
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mrispystgr fksflsdqsk afkdlvyqcq istryfdagq eilqqgakld ylyivpvgrv
       61 smsilaangr rfqlgeancd yhvfgemeff tktacqwnvi adehlqvdvi clnlltealh
      121 khpemmfffa salaedyqds ldiytnrllh pityniaydl lvqkqtntml ggfgkvnqea
      181 erfgtsgrvy rravkdlmdk glirkgeqgl eivdevalka fldaye
//
LOCUS       WP_010452407             226 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Vibrio rotiferianus].
ACCESSION   WP_010452407
VERSION     WP_010452407.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..226
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24720
     Region          26..220
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mfdsildvll alwhqdfsal mapgsagliy fvvgmlifle sgfipaapfp cdsvvvlsgt
       61 laavgildpv filllltvsa afgswaayfq gkwlnrlpkv qgwvnavper rlhqvdvllg
      121 khglialfca rfvpvvrsll plmmgirgkk vnkfhyfswl sallwtlllc gfgmllpllp
      181 enisklvtmg lmaapvitlt iaimsfiivk vrktwskska tpqlpq
//
LOCUS       WP_010452544             277 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Vibrio rotiferianus].
ACCESSION   WP_010452544
VERSION     WP_010452544.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..277
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30113
     Region          10..274
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 msnlisaiql kelmetrsvk lldasitfqi pseapkitdq wiagsirfdy dhdfcaldsd
       61 lphmmpsatl fqqkaralgl nnsdcivvyd nsgtlaspra wwmlsamgat nvlvlngglp
      121 awieagfetv eernepqggg sflaknnasa fisasevlkf steqsanild arskarfyge
      181 vpepreglrs ghiphsinlp fgrllnngaf kpledlrday adldldadkp lvfscgsgvt
      241 acilllaahe igfrnlsiyd gswtewgadt slpikce
//
LOCUS       WP_010452549             333 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Vibrio rotiferianus].
ACCESSION   WP_010452549
VERSION     WP_010452549.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..333
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36178
     Region          23..320
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 msssnqdisi estdllteis vayyqdgatq eeisrkfsis rakvgrmlkq ardegiveit
       61 vkyhpvfsak ieqrlierfg vkralvaldq pneeaqrlqv sglvsnylts tlkngmvvtv
      121 gqgrnvssva hhigvitprd ckfvcgiggi hprggmfnad hicrqfakky ggtsetlyap
      181 ayaenreqkv afmqnatvkq tldlarkadv alvgigdmse nsymvdlgwf tpdevvqsrl
      241 mqgvvgdfag ydffdihgsv antvmsdrvi glgieefrpi aeviaiaaen skplallgal
      301 rtgaidviat svsnaltvln ldeqmhdnst sei
//
LOCUS       WP_010452589             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fumarylacetoacetate hydrolase family protein
            [Vibrio].
ACCESSION   WP_010452589
VERSION     WP_010452589.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..204
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22608
     Region          11..190
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msviqveekk vkvgkvlcvg rnyvehikel dnampeqmvv fnkpatsvst kliafhqepl
       61 hyeaeicfli kdgqysavgl gldltkrglq stlkekglpw erakafdgaa vfsrfrslqg
      121 vniddlnlel lincvhvqkg hvkqmlyppm kildelksyt tledgdvvmt gtpkgvgevh
      181 qgdvflgrlk cgditlleie wlag
//
LOCUS       WP_010452333             309 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Vibrio rotiferianus].
ACCESSION   WP_010452333
VERSION     WP_010452333.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The SHS2 module is a common structural theme in functionally
            diverse protein groups, like Rpb7p, FtsA, GyrI, and MTH1598/TM1083
            superfamilies
  JOURNAL   Proteins 56 (4), 795-807 (2004)
   PUBMED   15281131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12255408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..309
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=35392
     Region          3..148
                     /region_name="SRPBCC_1"
                     /note="Ligand-binding SRPBCC domain of an uncharacterized
                     subfamily of proteins; cd07818"
                     /db_xref="CDD:176860"
     Site            order(6,8,10,19..21,23..24,35,49,51,53,55,57,69,70,79,81,
                     95..96,98,100,108,110,112,114,127..131,133..135,137..139,
                     142)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176860"
     Region          160..304
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mlsyqvnrsi eiektqsdii eylkdfthwp dwspwiimep eceltyseeq gvvgsgyqwn
       61 ghrigtgaiv lestqehrld melhffrpfq shakvtfivm pssngctvew qmqsrvpwfl
      121 vffktmvksm iemdyerglr mlksqletgq ilsqltdlgl rkqneisyig ltgagtlsev
      181 psvmqehvsr lfdmadkenl pvtgelfcfy lsmdmkrgyf efitclpvqt gvvatgdfva
      241 gtiptcetya vehkgdyqfl gnawsyamnl tryngikvkt kplgieryln npndtdkadl
      301 ltevivfkk
//
LOCUS       WP_010452775             346 aa            linear   BCT 01-JAN-2025
DEFINITION  lactonase family protein [Vibrio rotiferianus].
ACCESSION   WP_010452775
VERSION     WP_010452775.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..346
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=38376
     Region          6..336
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mevsnslrfl vgtytdslsk giesisldta tgqlsshltl lntsnpsylh ltknglysfn
       61 eveevegaql ifltkqqthy idingdypch ldsdssesll avanygsgnv svyqldsegk
      121 plnlianlfn egcgtnlqrq tsphthqvkf lrqsselwvv dlgadrvyiy gyadsqfelr
      181 qsielpagag prhlvlnkne diayivcels etlvtlkkqa newciehecd llndsekgea
      241 aaaiklssce qflyvscrhq nrivlfdvks gqperihdid cggafprdft issdgkwfiv
      301 anqhsnnivs fqrdeqsgmf kptgfeieig spvcilesnt kdtqaf
//
LOCUS       WP_010452707             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Vibrio].
ACCESSION   WP_010452707
VERSION     WP_010452707.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..161
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17503
     Region          5..147
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mssgqrditl rflaepgdvn fggkvhggav mkwidlaaya csaawsgkyc itayaggirf
       61 vapihvgnlv evsakviytg rssmhiaidv qasdpkelkn rltthcivim vavdedgkpt
      121 dvpkwipesa edkaleqsai rlmnmrkeig eemeahvkyl k
//
LOCUS       WP_010452742             205 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Vibrio rotiferianus].
ACCESSION   WP_010452742
VERSION     WP_010452742.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..205
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23100
     Region          1..201
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 miklhhlnqs rskriiwlle elgvdyeivp ylrdsvtfla ppelksihpl gkspvledge
       61 eivtesgait eyliekyadg rfapesgska ytqyiqwmhf aessamvpll lkmfvakdga
      121 qtnfladyad aetmkvmgyv dqslegksyf veerltgadf mmsfvvdvln kfgvierfpn
      181 iqrygaqlat hpaftkaeel evkfg
//
LOCUS       WP_010452784             365 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Vibrio rotiferianus].
ACCESSION   WP_010452784
VERSION     WP_010452784.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13386660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..365
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40136
     Region          11..>112
                     /region_name="YhgE"
                     /note="Uncharacterized membrane protein YhgE, phage
                     infection protein (PIP) family [Function unknown];
                     COG1511"
                     /db_xref="CDD:441120"
     Region          168..365
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mksiarmkav mikeirqlsr dritfgmvvm ipliqlllfg faintdirni pvgvvdqsgs
       61 tagrvitesv kvtqvvdvve tfatadqaeq aiqdgivraa lilpsdltqr mvqgrelgqw
      121 ivdgsdtmis sailslqtmp ltdfdfeirp aptktfeval yynpsrrsav nivpgllgvi
      181 ltmtmilfts aaivrererg nlellittpi hsielmvaki ipyifvgliq vfiilglghw
      241 ifgvpingai sqilfgtllf iaasltlglv istiattqlq amqmtvfill psillsgfmf
      301 pyegmpvaaq wisealpath fmriirgvvl rgadlmelwr dtlwllgftv iglfvaslrf
      361 kksld
//
LOCUS       WP_010452817             523 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein [Vibrio
            rotiferianus].
ACCESSION   WP_010452817
VERSION     WP_010452817.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..523
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58346
     Region          8..510
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mpvlqaynis hqfgngetlf qqiscsmtkr rvglvgrngv gksvfasils geqtpisgiv
       61 tlptsfavyr qqpshllgge lsiaqflakd kvlsalkqiq mgdcsehlfe mvgeqwdlpi
      121 qlakqltemg lppqpdfpca qlsggqlarl qlwqlfesev ellildepsn hldrhakqwl
      181 idsmrnfsga illishdrel lremeeiwel sglglqvfgg nydvyaeqkr telqaverql
      241 atvekqkkhl eeqaqrnrek aeqraaqgnk lrkdgsqpki lldgmkdkat araasrnkne
      301 qlrqthlqek eqslrarkeq ikgqklylad sqsrsrkvvs llegvlpfgs aqpitaqvha
      361 ddkvhllgkn gcgkstllkt llgkfslqsg elkintpfyy ldqhfgaiqp eismlenlmq
      421 hcegmkesda rtllagigfr rdrvfrlgsv lsggekmkla mlivshqptq plllldepdn
      481 hldldskiml aqalsayrgg filishdqdf aaesgvsrni els
//
LOCUS       WP_010452821             198 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: superoxide dismutase [Pseudomonas].
ACCESSION   WP_010452821
VERSION     WP_010452821.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..198
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21845
     Region          4..189
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mafelpplpy ahdalqphis ketlefhhdk hhntyvvnln nlvpgtefeg ktleeivkts
       61 sggifnnaaq vwnhtfywnc lapnaggqpt galaeainaa fgsfdkfkee ftktsvgtfg
      121 sgwgwlvkka dgslalasti gagnpltsgd tplltcdvwe hayyidyrnv rpkyveafwn
      181 lvnwkfvaeq fegktfta
//
LOCUS       WP_010452889             188 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Vibrio rotiferianus].
ACCESSION   WP_010452889
VERSION     WP_010452889.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20893
     Region          21..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msvnekkrgr paakqsqlsa esildsaksl mkkdgkvpsi rslatqlnvd pmaiyhyfkn
       61 knallevltt slveeiyqpq vnddwqgelk nlcvsyiell reyngllqtm lsmtshgpaq
      121 vfteryqiiv qplalspqve kdsldllady lhgfafsisc chdaslikte mmdgplnlic
      181 ssllasri
//
LOCUS       WP_010452909             142 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Vibrio rotiferianus].
ACCESSION   WP_010452909
VERSION     WP_010452909.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..142
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16245
     Region          5..132
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mksyvehani svvdarktie flttaipewt irgsgkiddw fgrpiewfhv gdehsyiais
       61 dggngdaghw tthftgmkhl givvpdvdal varlkevgye ldhwgtdhpf rknvyyledh
      121 gmqfefveyl sdkdserndy tq
//
LOCUS       WP_010453024             581 aa            linear   BCT 01-JAN-2025
DEFINITION  amidohydrolase [Vibrio rotiferianus].
ACCESSION   WP_010453024
VERSION     WP_010453024.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..581
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64661
     Region          8..575
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mnyqalcmrl idvkkpvtvf taqkvitmnp eqpeaesvav qngvivgvge tetirsllnv
       61 hrieaqfnnt feesyiyagf aehhmhphil gaylkdshyv gyvdrkaadg svmkgiqsve
      121 qltehlkvli ekdrvrlesd seqwlncwgf dplllagadv trnvldevsk efpiclghas
      181 ghvininsva ielcgyenme edpnlfryes gqvngtvaep elmqfafskg aarmdfseeg
      241 iieagelatk varingctsv tdkgtnfplt pgnvaaegwl kaqaqgrlht rvnmepwfss
      301 idrwvygdkh gwdavhaird eknpylsvgn fkmltdgsiq gftahllpdq nyvtegkpng
      361 hllmskekli eqisigeahg mscsihtngn gatevaiqai eeirktnpnl gfrhslehcq
      421 latenqfyrm kqvgitpnlf tnhlyywgdv hakytvgehg vrrmdacrsa tnhglmhgvh
      481 sddmvtevsp lfsawcavnr rslsgvvyge dqcltvaeam rvitynhawl ahqedvrgsi
      541 evgkwadftv laeeateekr etlkdirivg tviggddifl n
//
LOCUS       WP_010453028             354 aa            linear   BCT 01-JAN-2025
DEFINITION  porin [Vibrio rotiferianus].
ACCESSION   WP_010453028
VERSION     WP_010453028.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..354
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=39008
     Region          10..347
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mktnhylita gafllaspcm aieiakhdsa tlefggwiaa eyshnfddsp ydlgfnsnas
       61 rlffagenqi ndditafgkl eyavafsdmt dtefntrlgy igmrtqygsi eagkvwspfy
      121 diamysdtvf snkdtatgaf fapasevggf gradnsvkyy nkfgfgdgki lvglivgdqs
      181 dqsitdtvtv nttyggslry aqggfqfgva hqvantdglt ngddsisati vgafynsekw
      241 mlggnytfgk nnqkefgaap vasnlvdsdg ieffghyrfs dswkvfvgyn rlttetdtyt
      301 tefsniglvk nfdqklalys eyridhdstk nslfhgdaws igiiyffsey pqyf
//
LOCUS       WP_010453045             407 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Vibrio rotiferianus].
ACCESSION   WP_010453045
VERSION     WP_010453045.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..407
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45543
     Region          7..383
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(15..16,19..20,23,55,110..111,113..115,118,138,
                     141..142,145,220,223..224,227..229,232,255,259,312..313,
                     317,321,337,340..341,344..345,348)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mknktipyla grffdgissg lfmmalpwvm laepdmgtfv alvalsctai sflatpffst
       61 fidrhsrkql lvlnqwlqag maliifiayw lelgshwlla faqmvywvss nfawttnnaf
      121 tqenyqphey akisgqqeii mqsttlgaga lgiillemwg mlefalfaas assiaalfym
      181 vtpyvqqire shsiafmtql keskqifare ptfyafills clsypiltyl gklvpiwfsq
      241 qgisgdwyag fnisfglgsl ltglvvtkil rqfshtniiv vsmsvlafal igmslsaspv
      301 tilmftalfg tfnalnriar inwmhhsvsv hqrgrvdggi smfattvqsl syvliamlsh
      361 ygltqygftl aaatvllavf fmwhlqgkln qqdniyeyrv rdcnevn
//
LOCUS       WP_010453109             129 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Vibrio rotiferianus].
ACCESSION   WP_010453109
VERSION     WP_010453109.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..129
                     /product="VOC family protein"
                     /calculated_mol_wt=14571
     Region          2..128
                     /region_name="VOC_BsYyaH"
                     /note="vicinal oxygen chelate (VOC) family protein similar
                     to Bacillus subtilis YyaH; cd07241"
                     /db_xref="CDD:319905"
ORIGIN      
        1 mkiehiaiwt erleelkafy ekyfnavsnd kyhnptkqfs syflsfesga rlelmsmegv
       61 tacekshsmq vtglahfafa lgseqavdql tktlvddgyq widgprqtgd gyyescildp
      121 dgnrleltv
//
LOCUS       WP_010453116             806 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Vibrio rotiferianus].
ACCESSION   WP_010453116
VERSION     WP_010453116.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..806
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=89260
     Region          1..799
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mkfkpsllac avlsglvglt gcnsdndsss slpgdpivdl avlkyvdpmi gtaasghtfp
       61 gatvpagmvq lspdtfigsn tdhesglnpw hsasgywdss nyetgevvnt dvplygfsht
      121 hlsgtgatdl gdilvlpyad mantqlnsfd kaneeasagy yktklnqgqi evelsatkrv
      181 glhkytfadg adrnvkfdlg htlmnnngks lknkvevvde ytirgrktst gwfqgqdhqg
      241 qdiffyakfn qpiakallge qdkeptremr ngavysgddl taylnfgtge epieirvgis
      301 pvnwqgtqkn leaeapsfdl aqvkedaeya waeklakikv eggtdaektn fytgmyhmmi
      361 apiefydvdg qyvdmlgtvr tlkdgdtpny siystwdtfr avhpmwtiid pdqatlyvkd
      421 lirksndefg llpkweghgs etgtmigyps aailgdavtk glidaeqayt asvksarytp
      481 heypqihddi lsslmagqln yhekeqcvry pnwnsvsysl efsfydwtia emakaagdmd
      541 ayeefkarsy nslkhwdaea gnadgtgffv ptelkegdpc alkyastdfd pyksdafyyt
      601 egnawqwqwa fmqdldklte imggtqglnd klnnlftadp nggeahqdmt gyigqyihgn
      661 epshhviyly nrteesykaq eyldqvydqf ykptpdgiig nedvgqmsaw ylmsalgfyq
      721 isptdptysi grpifdkatv digsgtftvt aenngpdnmy ikevtingkp ldvyntfqhs
      781 efkaggelhf vmtadkseam qanlge
//
LOCUS       WP_010453244             686 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Vibrio rotiferianus].
ACCESSION   WP_010453244
VERSION     WP_010453244.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 686)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 686)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..686
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77270
     Region          326..683
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mqrkrngktw lvvaiaavlm lscysasrev arqwlsvqtq teaqqklldy igevrralkr
       61 fyhlpylvtn npetiafvkg nltyyeplqt qltqldkaan tegwlilsns gevlvsslie
      121 erfslsdrka iveqihnqgg gvslvnktkg ssplyylaap iydgldiagi vvvqinlsll
      181 teqtitsqdi itlqnrqqrf flsssslysa dwfnepsntv qletqrlydn tnisvwtlnq
      241 qryfahtvkl ddlnwyvsyl tpskpiqqai nvigwsvaal lllvvllvii glqrrqkhin
      301 qqriqallee sqrrlkqmin kthvglllid eqgqlfdlnp makrlfclpe svnrhafawe
      361 lfdagnpnst tlkllkdlpk hkelaeistv etiarrsdgs vfpvlfslts fpwhgeqyfl
      421 atiidiskrk kaeqslqqvn qelaqrveer tqalkeaqsq liesskmaal grmssalthe
      481 lnqpltglrt llttnellae rgetemmkan nvlvqklidr masmtsqlkt faynkperlq
      541 eislttalee tlrvyqsqle nvdvrvrvph dlpnimgeeq rllqvlgnlv snaldamdqt
      601 dnpklslivn ptenqvellv sdngcgvsde mlesmfepfq tskkigkglg lglaitannm
      661 rdmggsisvr inhskglsfe lifiaa
//
LOCUS       WP_010453289             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Vibrio].
ACCESSION   WP_010453289
VERSION     WP_010453289.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..206
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22914
     Region          125..204
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mkrlllalpa svliavslfs fmawmvdkgn qrapkpseav rfdmvmvend advqrrqrsv
       61 peqpeppesp epmdvsqaet qvepmsqvtp isalglntal dgiaisapnl kgsmgnqqai
      121 mlyspepryp skavkrkieg yvtmrftida tgrpkdievi dakpkrmfek eairalkksk
      181 yqpkvengva verfgqtrrv efklak
//
LOCUS       WP_010453269             327 aa            linear   BCT 01-JAN-2025
DEFINITION  porin [Vibrio rotiferianus].
ACCESSION   WP_010453269
VERSION     WP_010453269.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..327
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=35074
     Region          38..327
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkmktlavav aalacgsqaf aaevynsdgt smsigghftt digdngdnve vgevsprini
       61 vgkqdlgngl tveakgewqt nlvdggdttf strlgylalh semgkvtvgt qwspyysvas
      121 ltdipikyan dflydggrsg swrsigtgra nkmlsysnnf dfgndmslyf gvgwqgetka
      181 ggsqfddrgq iaaslsfsdf nvglaytggd vdsekltsta iaasygsygk giyvagvygl
      241 nenlygmtds dqisgllayg ldnglnfily yenvdrddnv lnpnrdvlap qveysvtskl
      301 ktfagfrthm gddksddews lgaryyf
//
LOCUS       WP_010453295             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Vibrio rotiferianus].
ACCESSION   WP_010453295
VERSION     WP_010453295.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..455
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48846
     Region          2..>96
                     /region_name="HlpA"
                     /note="Periplasmic chaperone for outer membrane proteins,
                     Skp family [Cell wall/membrane/envelope biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG2825"
                     /db_xref="CDD:442073"
     Region          253..433
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mmkkwlsial issaallpht tfasdtllqk aqqenrkqqs hnvvresgfk ktqqelqamk
       61 nklvaerval qaeadtlgvt fseneaelaq leeklrletg slgelfgvvr qnakeleael
      121 khsvtgvdan syqqnvddiv aakslptlpq leamwrsmee qvkasgelan vsfslldgeg
      181 reqtvdgvrl gsmallndvg yvkwngqrgd avsylrqpen gptassvkag eidavvidps
      241 rgilleqlan sptmadrlna ggvvgkiilg llaigliial argvslmiar qkiakqlknp
      301 aqpednplgr ilavyqkdkh rsvealelrl leavvdeqth lekglsmlkl laalapmlgl
      361 lgtvtgmiet fqvitqfgng dpkvmaggis malvttvlgl vaamplllah nllssqaeni
      421 rnilekqgig lvaeqaerdm pkgqkapntv aenaa
//
LOCUS       WP_010453337             461 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TldD/PmbA family protein [Vibrio].
ACCESSION   WP_010453337
VERSION     WP_010453337.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..461
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49351
     Region          7..459
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mlnsvtakav idhalflgad faelfvehhq tntvqiasge vdkvnsgidf gigirlffgh
       61 kvlygytnst deaelkrvts llaakdkreq iasagslnln rypiqhscrm plgkdanlds
      121 kiafllqvdq aaraesehis qfigsvlqre qqvsifnseg lhvddtrhyi rvagntvaqk
      181 gneqssgmeg pgalagwefs eqldakelgq tiaqqalvkl gadacpsgem pvvigngfgg
      241 vifheacghl lettsvakka svfhdkmgem iahtavnavd dgtmtnewgs ihvddegmkt
      301 qrtqlikdgk ltsfmvdkmg gmktgyeptg sgrrqnykfa ptsrmrntfi eegehslddm
      361 lagiergiya kkmgggsvqp gtgefnfavr eayliengki tkplktatli stgpkvlkei
      421 smvgkdmala pgmcgsvsgs vpttvgqptl kvdnilvggg n
//
LOCUS       WP_010453384             377 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerate kinase [Vibrio rotiferianus].
ACCESSION   WP_010453384
VERSION     WP_010453384.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..377
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38867
     Region          2..374
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mkvviapdsf kesltakqvs eaiktglsrv wqdaefvtvp vadggegtvq slidategeq
       61 vfvtvkgplg ndveafygil gdgetaviem aeasglhlvp sekrdpknts sfgtgqliln
      121 aldrgiqrli iglggsatnd ggtgmlaalg vklldsagqp itlnggglve lasidvsgld
      181 arladcevlv acdvdnplcg ekgasaifgp qkgatpadve lldsalskyg elteqvtgkh
      241 vltkkgagaa ggmgaallgy lparlkpgie ivletvklee hvadadivft gegridhqtv
      301 hgktpmgvak vakeyglpvi alagctgdnf qavyecgida vfvcvprams lpealeeaev
      361 nlanlaenva rlwqlpr
//
LOCUS       WP_010453456             289 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Vibrio].
ACCESSION   WP_010453456
VERSION     WP_010453456.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..289
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32365
     Region          10..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,213..218,
                     224..225,227..228)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176159"
ORIGIN      
        1 manwegvsef vavaetnsft gaanklktsv aqisrrvsal eerlavkllh rttrkvslte
       61 agqlyyqqck hlveglelae lavtqmqaep kgllkvtapv tygemnlapl lhqflekypq
      121 vnldlnltnq kldlieqgvd vairlgrlqd ssliakrlss rqlyvcaspa ylersgepht
      181 lselshhqcl vgtadywhfk eqkrekslrv sgrikcnsgf alvdaakrgl glvqlpdyyv
      241 qealdngelv evltdyrddr egiwalypqn rnlspkvrll idflaenms
//
LOCUS       WP_010453487             177 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Vibrio rotiferianus].
ACCESSION   WP_010453487
VERSION     WP_010453487.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12134272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..177
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19882
     Region          11..147
                     /region_name="Acetyltransf_3"
                     /note="Acetyltransferase (GNAT) domain; pfam13302"
                     /db_xref="CDD:379112"
ORIGIN      
        1 mptqpklfte rlilrpfqhe dservallag ekiiadmtan iphpyelpma ktwidghgpm
       61 fndqrgiaya itlrstgell gavslpried gygtlgywig vpywgkgyaf easqalieft
      121 ksyfqligir vmhlvenqrs ksviqklnvp yvgnktlsmq gadrevcvyq crfdann
//
LOCUS       WP_010453614             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Vibrio harveyi
            group].
ACCESSION   WP_010453614
VERSION     WP_010453614.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi group
  ORGANISM  Vibrio harveyi group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Vibrio harveyi group"
                     /db_xref="taxon:717610"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28782
     Region          4..247
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mkevltikgl slgiktelvr disfslkeke flavvgpngc gkstfirtim gtvnifsgel
       61 sflgkplssy nhkmrsryia fmgqnntvdp qmrvldyisl grfphfhyst rqydnecitr
      121 videlgletl reqkvgqlsg gefqrvnlar vlvqepklll ldeptnhldp kariellkiv
      181 kdkqittiav lhdlnlaeyf adqvmiinrg kmqvcdtven tlnahwikdt fdlntlhflh
      241 pttgkairff eid
//
LOCUS       WP_010453655             128 aa            linear   BCT 01-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Vibrio
            rotiferianus].
ACCESSION   WP_010453655
VERSION     WP_010453655.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..128
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14815
     Region          1..121
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mtkltvfydg tcplcvkemn slkqrdtkqq iktvdiysda fadypqidpe qantilhaln
       61 ekdelllgld vthrawqlvg rgwlyaplrw riikpvadwl ylkfaknryr vsywltgtsr
      121 cnngscsr
//
LOCUS       WP_010453715             188 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Vibrio rotiferianus].
ACCESSION   WP_010453715
VERSION     WP_010453715.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..188
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=19886
     Region          3..185
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mpkvaivyft ntnitgqlaq avaagvesqd invvsyrilg tdiitgryqn sdlfqsiaqc
       61 daiifgspty mgsvaaqfka fadasseywg eqgwsgkvaa gftsggalng dqsttlqyll
      121 tlasqhgmiw vgldsahgfa dkginrlgtq lgvvsraedg qlhevdaata hylghrvahl
      181 vkrlahpe
//
LOCUS       WP_010453757             433 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Vibrio harveyi
            group].
ACCESSION   WP_010453757
VERSION     WP_010453757.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi group
  ORGANISM  Vibrio harveyi group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Vibrio harveyi group"
                     /db_xref="taxon:717610"
     Protein         1..433
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45155
     Region          5..432
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mewqliltlf gsfavllaig vpvsfaigls slatilmslp lepaiavvaq rmaagldnfa
       61 llaipffila gnimnqggia lrlinfakvl ggrlpgslah vnvmanmmfg sisgsavasa
      121 aavggtmspl qkkdgydenf saavnitscp sgllippsnt livfslvsgg tsiaalflag
      181 yipgilmgls imvvagiiak rrgypvaarp slamvwntfl kaapslaliv iimggiiggi
      241 ftateasaia vvytfvlavl iyrevkwrdi pkiilesavt tsivlllvga smgmswaman
      301 adipymiada llaisdnpmm illiinvill ivgifmdmtp avliftpifl pialdmgidp
      361 vhfgimmtfn laigictppv gsalfigcsv anvaidkvik pllpfyvali aalmavtfip
      421 qlslflpnlv lgy
//
LOCUS       WP_010453794             179 aa            linear   BCT 01-JAN-2025
DEFINITION  CAP domain-containing protein [Vibrio rotiferianus].
ACCESSION   WP_010453794
VERSION     WP_010453794.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..179
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=18817
     Region          33..178
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
ORIGIN      
        1 mptkilvpal alllsacggd gessasansg sqspdtppts ttfaeqmlaa vnnarsktqq
       61 cgsktmppvg altwsydles aayghssdma nsdfmshtgs dgstlssrvn atsyawsrlg
      121 envaagqssi davmnswlss eghclnimna dfdqmgssmv enqsasyryy wtqvfakqr
//
LOCUS       WP_010453819             399 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Vibrio rotiferianus].
ACCESSION   WP_010453819
VERSION     WP_010453819.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..399
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43504
     Region          3..312
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mtkliysvll chfisafaal gmplflpvvl ptlgtqidtd wagvlfilpt fctavaarfw
       61 gqfadkygrr rsllraqlgl aagfaicgla nnltmfvfgl ivqgtfggtm aasnsylssq
      121 iedaktlgks lnktqlsarl aliiapiglg wglsetnpln aylwlsimpl lalaitltlp
      181 adqtikpvae rnqafeetqr nknqslrtly wvfgaqfsfa fsmvvtfpyf spyvqqygtt
      241 nqawigllya lphgvyllla gkahlwseci nghqpqrtlw lgfgllslst amhlvhyeav
      301 ligarltfgl gmvccyqglh qalakqldrq lcgkvfsrfd amskwggvaa glcasfissl
      361 gwlevpflls alvsiatlia liihskfghq hvthsilsd
//
LOCUS       WP_010453865             205 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Vibrio rotiferianus].
ACCESSION   WP_010453865
VERSION     WP_010453865.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..205
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22573
     Region          <13..187
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 mkmlllslsv vfvsacssnd gsgdqydyip tpvaeqsadh mdddrdgvin hrdlcpgtpe
       61 gseldndgcg eyakssqkmq irvlfandsd vinpifskqi rdlsaflkey pstsielqgy
      121 tsitgtdeyn ldlskrraen vrqelikngi spnrlrivgf getklasfgt devshalnrr
      181 vtatvvgykg evkkewtift alpkn
//
LOCUS       WP_010453878             575 aa            linear   BCT 01-JAN-2025
DEFINITION  type VI secretion system Vgr family protein, partial [Vibrio
            rotiferianus].
ACCESSION   WP_010453878
VERSION     WP_010453878.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         <1..575
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
     Region          1..530
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 vyslvlvpal erlslrqnsr ifqlktvqdi isqilgemgv adfsfalkra lsqrefcvqy
       61 retdlefvhr laaeegityy ieqadgkhtv vffddsalis kygapvlhng laggqsgepf
      121 vsqfkiehqs epshltfkdy sfkkpsygfl qeqqgadlsf qqssyehydf pgrykddgsg
      181 iafsqlrley lrresnlghg ksnhhalqag vkfdlsenle asanrdwivv avthqgtqpq
      241 aleedggyga ttysnqftvi panktwrakp qpkpqvdgpm iakvvgpage eiycdehgrv
      301 kvhfpwdres eqnehsscwv rvsqgwagaq ygfmavprig hevivsflhg dpdqpiitgr
      361 tyhatntppy plpanktrtv irtethqgdg fneirfedqa gqeeifihaq kdqnnvvnnd
      421 ettkvghdrs edvgndenin igqnrtetvg ndetitignn rtetvggnev vtvkgntaet
      481 taiakaetvg aakalsigag yqvsvgaskn vsvgltyteq vgvlrqlivg eryevvcges
      541 kfimnsdgti lftakkisis gqdkveidak tvevn
//
LOCUS       WP_010453886             282 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Vibrio rotiferianus].
ACCESSION   WP_010453886
VERSION     WP_010453886.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..282
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=31663
     Region          17..211
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(94..95,97..98,102,105,114,116,117,121..122,125..127,
                     129..130,134,137,146,148,150,154..155,158..160,162..163,
                     166,169,178)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          116..146
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          148..178
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msnkepkpet ffsgellpia qaiksndidr akelsknldn idetgfenft llafsvadsn
       61 aaaihmlmel gadpahqigr hkdrgtigsf smwnqsteal rallesgmdp dqretdrtli
      121 ykvpelrdnd slkllvefga dvnvtdrlgq tpilhfvlas fdeaiyllen gadpfvmdka
      181 gvtlaysvqn rienmssele ayqklltiqq kmielgvtfp altpfgerfr ndivyckepr
      241 gyrpraeckv egvnrflkpq seeskladek ilrerygina kl
//
LOCUS       WP_010455060             226 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SOS response-associated peptidase [Pseudomonas].
ACCESSION   WP_010455060
VERSION     WP_010455060.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..226
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=25386
     Region          1..225
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgrlsqyrg ihdfvavlsi pdalinhvgd eplarynaap ttqlallhle pdglhadsvr
       61 wgwrphwakd raapinarve kvahgpffra iwphraivpi dnwfewvdag dttrqpwlir
      121 rrdrapiyca aigqfphggs eprgddgfvi itadsaggml dihdrrpvvl svqlahewld
      181 patpkeraeq mvlmqgevse vfewyrvdka vgnvrnqsam lidklt
//
LOCUS       WP_010455142             215 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pentapeptide repeat-containing protein [Pseudomonas].
ACCESSION   WP_010455142
VERSION     WP_010455142.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..215
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=23180
     Region          40..203
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mkylplllwl aalpvfadng ddspliingc tiadhsqcpg anlkganlsn qdlrnmnlsg
       61 adlrdadlrh arldlanlek aqlqganltr aslqqsnlrl adftgstlma iqgwgmfaqg
      121 aqfqdanlsg aylqfarlsg armhntnlra adlemtwlsk adlkganlsd anlqeaklse
      181 snleqanlsg srqhyanfqd anmegcsgcp ttwnk
//
LOCUS       WP_010455225             335 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aldo/keto reductase [Pseudomonas].
ACCESSION   WP_010455225
VERSION     WP_010455225.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..335
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36278
     Region          9..321
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(14..16,46,51,77,140..141,181..182,205,234..240,276,
                     293..296,301,304..305)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(46,51,77,140)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mslkdklpga lgfgtaplgn mfraipedea qatvhaawda gvryfdtapf ygsglseirl
       61 gaalaqynrd dyvlsskvgr vildevedas ardlgeksgv fehgrpnkiv ndysadatmr
      121 siedslkrlq tdrldivwvh diaqdfygdq wleyfnqart gafkvltrlr eegvikgwgl
      181 gvnkvepcel tldlteaqpd gfllagrytl ldhdralqrl mdaalaqnve ivvggpyssg
      241 ilaggthfey qkaspaivdk veqikriaaa hgvdikaaal qfslanpava avipgssrpd
      301 riaedvaals avipaafwqa mrdaklvser aplpl
//
LOCUS       WP_010455258             437 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010455258
VERSION     WP_010455258.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..437
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46773
     Region          24..429
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,254,257..258,261..263,266,294,298,356..357,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnnpsaetlr laaasaterp tsvrwrifli mllltainyi draslsvalp lissefqipp
       61 aleglmlsaf fwsyalmqip ggmlldrfqt rrviviatva wgafqalaag ahnwitllit
      121 rmglgiaesp impagaklng awltpnergr gavlvdggap lgsafgaiii agligwfdsw
      181 riafviagig tmlagvlawk yirnhpsehp gvnaaelahi tegnrkvsqp gtvtsislke
      241 llkdrsvlam fagyccilsv fyglltwmps ylhqthglni ssmggatfli fmcgfvgelv
      301 ggylgdkwkt sgaspnlvmr smfsgsalva alcmlavayt neagkaigll cvamffirwc
      361 gmywcipsil ggtsktgvla gtmnfcgnma gvivpiligl ivqftgsyfl vliffvvmam
      421 llaifsslid yrergla
//
LOCUS       WP_010455268             309 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010455268
VERSION     WP_010455268.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33950
     Region          21..73
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          103..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(117..118,120..121,124,128,130..136,231..236,
                     242..243,245..246)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mvpslgsias rlrlkqlrll ialddrgslh kaaehisisq sgatkalhev esllgmplfe
       61 rqpkglvane mgrcmiryar liysdvehlr eemlsimqgq ggrlsvgvim gavplltral
      121 selrlkqpel svelventsa tllglldqgr ldlaicrtsv gqrsdaydci elseeplavv
      181 askdhplara eslqlsqlsd yrwvvypkdm pmrqalerel neagleipry pletsstfat
      241 illvqqdptl lavipvevaq fceqhdllvk lpvsmralie pygvisraga dlspaatlli
      301 nelkqdltt
//
LOCUS       WP_010455289             315 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010455289
VERSION     WP_010455289.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34404
     Region          4..312
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtsvafvvfe gfqsmalaam pvfeyanfsa gealyevsvi seegrslras gglsvgtqaf
       61 dervfdtviv vggdsileqa pegvlaylrd svktarrtas icsgafvlaq aglldgrrat
      121 thwayardlq arfpsikved driyvvdgsi wtsagmtagi dlalamvekd hgadlarsva
      181 qklvmyqrra ggqsqhsall elepksdriq tvlgyarehl tsalsveqla evarlsprqf
      241 srtfraetgq spakaienlr leaarqmler grltldqiaa eagftdrrrm reaflrafgq
      301 ppqvirrnar lqmta
//
LOCUS       WP_010455299             535 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [Pseudomonas].
ACCESSION   WP_010455299
VERSION     WP_010455299.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..535
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58747
     Region          1..535
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mtydyiiaga gaagcilanr lsasgkhsvl lleaggkdss lwfkipvgfa kmyynptfnw
       61 myysqpqkql nnreiyaprg kvqggsgsin amiyvrgqah dfddwaangn egwsfkdvlp
      121 yfrklenhpl gdteyhggsg pisitpmkgq thpicdvflk gcdelgyphs ddfngprfeg
      181 sgiydvntrn gqrcsssfah lhpalsrpnl tvehyalvdr vlfdnaratg isisqhgvvr
      241 tftankevil cagavdtpki lqlsgvadqa llarhnipli khlpavgqnl qdhlcasyyy
      301 kaniptlndq lsslfgqfkl glkylftrkg alamsvnqag gffrgneqqa npnlqlyfnp
      361 lsyqipknnk aslkpepysg fllcfnpcrp tsrghieias knprdaalid pnylstqkdi
      421 deviqgsrlm rkimqapalk gitveevlpg paiesdeqml qyfrensgsi yhlcgscamg
      481 tdeqrsvvdk rlkvhgldnl rivdasifpn vtsgnthaav lmvaekgadl ilqda
//
LOCUS       WP_010455313             454 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010455313
VERSION     WP_010455313.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48408
     Region          21..399
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,256,259..260,263..265,268,293,297,348..349,
                     353,357,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 msvqptkidd lpigrfhlki agltfgahft dgyilgligi aftllspqmq ldafwqglig
       61 asaliglflg slffgwisdk vgrqkiflvs fvlitlaslm qfyaetamgl flcrvligig
      121 lggdfsvgha mlaefapkkh rgvllgsfsv iwtfgyvaat fvgtamlslg ddawrwmlas
      181 saipaalili arigtpespr wlvnqgriae araivkkhlg dnieldetrs tetrsgyavl
      241 fsreyrkrta fnclffvciv mpyfaiytfl psilqkmgla egfgtelmln mllilgalig
      301 iwctikfsrr gflinsfiil avalfglavl pssaaflmvl vfglftlvls avsnlvgvfp
      361 aesfptevra sgiglatavs rlgsavstfl lpvsvagigl sptmgilaai lalgallswa
      421 wapetksltl sqackaqspv eggatvavka vapv
//
LOCUS       WP_010455367             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cysteine hydrolase family protein [Pseudomonas].
ACCESSION   WP_010455367
VERSION     WP_010455367.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..240
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25980
     Region          33..217
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 msndsnriap qyadpaepal pdpgmkldls raalvvidpq idflspegvs wgvfgksive
       61 hdtvkhigql faaakgagit vavsphyyyp cdhdwhfggp lekvmhsicm fdrkgpltld
      121 gfensgadfm peykpyildg ktiiasphkv ygpetndlal qlrkhgvsqi ilagmaanlc
      181 veshlrelle lgfevavvrd atagpttpeg dgylaaliny ryianalwst aqtveflngk
//
LOCUS       WP_010455379             307 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas mandelii].
ACCESSION   WP_010455379
VERSION     WP_010455379.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..307
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34331
     Region          24..170
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <175..290
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mnpaieelrr lvmraenkwt dtglprvamv qaeacasqvy qpmlhlvlqg aktlsigdqv
       61 yqylpmtyfl vpvdvpatge ihpggpglpy laisltldps viatllttdi kttapppasr
      121 faavpaqaem idawlrmmrl mdrpneaavl apmlereilf ralqgplgpm lreiarpdgr
      181 laqirratqw irehytepfr veplatmtdm svaafyrhfk sitgmtpiqy qkrlrllrar
      241 wlllfdprda asiaftvgye sasqfsreya rlfgmppard aarfrapvvp getdmttldl
      301 qpelnpa
//
LOCUS       WP_010455478             422 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpP1/FadL family transporter [Pseudomonas mandelii].
ACCESSION   WP_010455478
VERSION     WP_010455478.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..422
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45536
     Region          8..422
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mqlktavlpa ctlfalccqq aqaggimlye igtdnvglan agaaaraqgp stiasnpagm
       61 sylpgtqitg glqvlygdls fdrdsntngt gsgsgnafdp ipggsffish qfddhwsvgf
      121 gnygdfglaa nydndwsgry faqnvslagl sfvpsvayrf ddqwsvgvgv kamygmlqaq
      181 taidrspfgf tdrsdgqfky kdndwgfgan vgviyapqpg triglaytsk vdldfedrld
      241 vkgdgrller vnntntqldm tvpqtatlsl fqqldprwal lasvnwqdws efgdiavqvd
      301 ttavgsqstt vdahfkdtwq lalgaqyqat pqllwnfgva ydssavsdgn rtftvpmdes
      361 wrvaagatya lnkvtdinvs wamvwlgdmp vdqtkstsgt rtsgqfdnaw iqavtgnmtw
      421 rf
//
LOCUS       WP_010455519             348 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Pseudomonas].
ACCESSION   WP_010455519
VERSION     WP_010455519.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..348
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=37310
     Region          156..>281
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
ORIGIN      
        1 mdearlndfm gklvndmgga amlanvilge elglyramad sqpitpeala dktgcnprll
       61 rewlsahaas gymeheggqf rlpeeqalal aiedspvyia ggigvvasff hdkdklvnam
      121 rgngalawgd hhpcmfsgte rffrpgykah liaewlpale gvvaklqaga kvadigcghg
      181 astvimaqaf pdsrfvgfdy hapsvtvatq raeeggvsgr arffqgtaks fpgddydlic
      241 yfdclhdmgd pvgaakhayd alkpdgtvll vepfandsld dnvtpvgrlf yaastfictp
      301 nslsqevglg lgaqagearl rkvfteagfk tfrratetpf nlileark
//
LOCUS       WP_010455524             393 aa            linear   BCT 01-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Pseudomonas mandelii].
ACCESSION   WP_010455524
VERSION     WP_010455524.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40358
     Region          1..393
                     /region_name="PRK05656"
                     /note="acetyl-CoA C-acetyltransferase"
                     /db_xref="CDD:168156"
ORIGIN      
        1 mqdvvivaat rtaigsfqgs lanvsavdlg aavirqllaq tgldvaevde vimgqvltag
       61 agqnparqsa ikaglpftvp amtlnkvcgs glkalhlatq aircgdaevi iaggqenmsl
      121 snyvmpgart glrmghaqiv dtmisdglwd afndyhmgit aenladkynl treqqdafaa
      181 asqqkataai eagrfvdeit pilipqrkgd plsfatdeqp ragttaealg klkpafkkdg
      241 svtagnassl ndgaaavilm sadkakalgl pvlakiaaya nagvdpaimg igpvsatrrc
      301 lgkagwsidq ldlveaneaf aaqslavakd lewdlnkvnv nggaialghp igasgcrvlv
      361 tllhemikrd akkglatlci gggqgvalai era
//
LOCUS       WP_010455555             284 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010455555
VERSION     WP_010455555.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..284
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31950
     Region          1..276
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mpslrdlitd paldltpaer kviralldqy prnglgpmsr laehagvsdp tivrlvkklg
       61 fsgyadfqda llsdmdhrlr spsallqlrs hvqkddawsh yladthralv dthaltqped
      121 vrilvqwlld trhqvhcfgg rfssflanyl lnhlrllrpg cfalednaql pdrlfdvqrq
      181 dvvlvfdyrr yqsqalrvan aaksryarvv lftdiyaspl remadliisa pvesvsafdt
      241 mvpalaqiea liacltlrsp eladrlegid alrtdfathl ledk
//
LOCUS       WP_010455659             497 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Pseudomonas mandelii].
ACCESSION   WP_010455659
VERSION     WP_010455659.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 497)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..497
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55212
     Region          173..483
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mqilkqqkvp apdapaaegq srsgqfnllr wfslgsflii avvamglgyv strfvvdesi
       61 erdsmltaqf iqaigdaeir hagitlkrtm gemldpredn aypdvnpgar aaariefldh
      121 vehlpdtlla vvyaldrtvv wstnpqmigm rvegdeelde sfemkepvst syhqideerp
      181 eqmllrepky lfienyipmf nadkskviam veiykepadl veriqrgfka iwlatllggl
      241 liylglfwiv rrasvllqsq qkqlitnetf valgemssav ahslrnplan irssaelaqe
      301 iasqsaqkni gdiinqvdrm srwvrellvs lrpinddset vdlvlaiddt lsafdalirr
      361 snvevrftpq tcppvvsqrv lltqilnslf analeampkg gmltiaieqp rpglvrmtls
      421 dtgkgmskqq qesvfkpfft tkqgglgvgl alvkrimerf egsveltsqe qegtrvclnf
      481 kvatggeyga qhtagrg
//
LOCUS       WP_010455720             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: lytic transglycosylase domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010455720
VERSION     WP_010455720.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..202
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21691
     Region          <68..194
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mktlttgllg cllltsvvqa dvfvsvdakg syvlsnvhrp grtyervihe pqsslvgldq
       61 qpqmiarqpy aelvsaaata nelpaallha vireesryns datspkgagg lmqlmpdtar
      121 emgvknvydp kaniqggaky lkrlltlfdn ditlavaayn agpqavlsrg gvvppfaetq
      181 ryvpsvlrqy rrlqglamda pl
//
LOCUS       WP_010455748             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Pseudomonas].
ACCESSION   WP_010455748
VERSION     WP_010455748.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..240
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26368
     Region          10..237
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mltlrkasdr gaanhgwlks fhtfsfanyr npkeqgfsdl lvinddrvaa gkgfgqhphr
       61 dmeifsyvle galehkdtlg tgsvirpgdv qlmsagsgva hseynhsatr pvhflqiwiv
      121 pdvsgakpry qqehfstqkk rgrlqliisp dgakgslkvr qdarvyaali dgkesatlel
      181 aanryayvhv argsvelngv qlqegdgvrv rdeqvlalsn gvdaevlvfd lrpqelpemp
//
LOCUS       WP_010455734             138 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Pseudomonas mandelii].
ACCESSION   WP_010455734
VERSION     WP_010455734.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..138
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15008
     Region          6..136
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mntsrwdera qdfgllflrv tggvfllwvh glpkllnisa qlqviedpfh lganvtlmla
       61 ifaevlcpll iiagvlvrla clpilavlli allvvhaqws ldegqfgwll livftsllia
      121 gpgrlalnvr fagalrya
//
LOCUS       WP_010456001             313 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010456001
VERSION     WP_010456001.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34766
     Region          17..74
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          106..306
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(120..121,123..124,127,131,133..139,235..240,
                     246..247,249..250)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mttpiisrsl lnrlrykhlh mlvtlsssqn lhrasqslnm sqpaatrmlh eiedmfgcdl
       61 ferlprgmrp talgselirf aesalsgldr caedliarqq ggygylsigt imgaapdlvm
      121 dsiaeikaln pqlririmgd tsdqviqlle qgridlaiar rnaatdsehy efeqlgnerl
      181 lvvvhaghpl vqretlelse lvsgwpwilq petsparigl dqalqrlalp tpadiiecss
      241 vysmqqliql tdaimvlset alrdylkmgl vvalpveldv qlapfglllr kgehisrelg
      301 lfidllrrka avf
//
LOCUS       WP_010456004             431 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010456004
VERSION     WP_010456004.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..431
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46266
     Region          13..415
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(27..28,31..32,35,67,117..118,120..122,125,145,
                     148..149,152,248,251..252,255..257,260,289,293,343..344,
                     348,352,368,371..372,375..376,379)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mktlpaplla kiswrllpfl llmyimafld ranvgfakqa fqadtnisda afafgagvff
       61 vgyallevps nlilhrvgar lwmcrimvtw glvsaamvfa htetsfyvlr fllgvaeagf
      121 fpgvilylty wfpsaargka mgffyfgapl afifgsplsg llleldgfag vhgwqwlfav
      181 eglmatavgv waywyldnrp adakwltvee rqqvqgildq edshkqnhgr sllnvlcqps
      241 vlylcliyll iqasvygvvf ylptqvggll gtkvglmvgl vtaipwicai vaaylipgys
      301 drtgerrrta cltllmsaag iacsvtfasp flgivalcfa asgfiavqpv fwtfpssyla
      361 gsaaaagial insfgalggf iapvlknwae gafhspaagl yvlagttvia allvlgirsp
      421 vhkpsntpat v
//
LOCUS       WP_010456298              99 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudomonas].
ACCESSION   WP_010456298
VERSION     WP_010456298.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..99
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10903
     Region          10..98
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 msqtdrdyse krdfirmrvd advslihegd evpavcidls ssgmqveapr lfkvgdrlsv
       61 ridsdhaalk gleadtevvw vkeqdggsqk lgltilkmk
//
LOCUS       WP_010456551             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010456551
VERSION     WP_010456551.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..240
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27257
     Region          8..230
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mldqldppvv tqdesetlse nvfrriqaai vkgeiapgsk isepelarty gisrgplrea
       61 ihrlegqrll vrvphvgarv vslshaelle lyeiresleg macrlaaerm tveeidelrr
      121 vletherdea fqagvgyyqq egdfdfhyri iqgsgnrtlt qmlcgelyql vrmyriqfst
      181 tpnrphqafa ehhrildaia drdgelaell mrrhigaskr niarhyqdga nqtaterges
//
LOCUS       WP_010456568             307 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010456568
VERSION     WP_010456568.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33362
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 metfssiecf vrsaevgsfa eaarrlsltp aavgksvakl earlgvrlfq rstrsltlte
       61 aghlflgevs sslhtiqnav anlasaegrp agtlkvsmgt vfgrlyvvpl lgeflrrfpa
      121 inpdwhfdnr qvdliaqgfd aaigggfelp qgvvarkltp ahrvlvasae ylaarpvive
      181 pdqlkdhdgi lirspqtgrv rswqltsrtq qhnplalkar mtmsdseaac ataaqglgia
      241 lvsmpfavgy leagtlqrvl pdwyvddgni siyyaehkll pgktrafvdf iieqfaergw
      301 vqrfsav
//
LOCUS       WP_010456724             266 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010456724
VERSION     WP_010456724.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..266
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29403
     Region          13..264
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 msraelgpag vyhrvvvyvl failllplag tliysiassw satilpsgft fkwyiqlwsd
       61 prflhafgqs llvcvgalil svvlilpllf vvhyhfpkld almnilillp favppvvssv
      121 gllqlygsgp famvgtpwil igcyftialp fmyraitnnl qainlrdlmd aaqllgastw
      181 qaaflvvlpn lrkglmvall lsfsflfgef vfanilvgtr yetlqvylnn mrnssghfts
      241 alvisyfffv lvltwaanil nkdkse
//
LOCUS       WP_010456802             208 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Pseudomonas].
ACCESSION   WP_010456802
VERSION     WP_010456802.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..208
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22538
     Region          <21..195
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlkrfaplvp lalvtllfgc aahspvtqqe qqqqvknsvt aqsssvlfqe elatdkelan
       61 fadgksyqlp vladsilerg msligtryrf ggtseagfdc sgfigylfre eagmnlprst
      121 reminvdapl varsalkpgd llffatngrr grvshagiyl gdnqfihsss rksggvrvds
      181 lgdsywsktf ieakralama ptvvtark
//
LOCUS       WP_010456832             158 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Pseudomonas mandelii].
ACCESSION   WP_010456832
VERSION     WP_010456832.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..158
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16822
     Region          4..142
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 maenpvfera trflsalrhc qvlglrvhsa snegltvilp yspqivgnpq tgvihggalt
       61 slmdtscgms tlcvlpefev cptldlridy mhaaephkdv ygfaqcyrvt tdvifargfa
      121 yqddpeqpia hvvgtfmrmg kavkgakglg gaiaggak
//
LOCUS       WP_010456861             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycine betaine ABC transporter substrate-binding
            protein [Pseudomonas].
ACCESSION   WP_010456861
VERSION     WP_010456861.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..283
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30761
     Region          28..283
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(37,39,85,113,142,146..147,193)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mkmrrllgag aalvlaigst manaesktls igyvdgwsds vatthvaaev ikqklgydvk
       61 lqavatgimw qgvatgklda mlsawlpvth geywtknkdq vvdygpnfkd akiglivpey
      121 vkaktiddlk tddtfkkriv gidagsgvml kteqaikdyd ltgyqlkass gagmiaeltr
      181 aekknesiav tgwvphwmfa kwklrflddp kgvygaaetv nnigskelat kapevakflk
      241 nfqwaskdei gevmlaiqdg akpdaaakdw vakhpervad wik
//
LOCUS       WP_010456955             101 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: STAS domain-containing protein [Pseudomonas].
ACCESSION   WP_010456955
VERSION     WP_010456955.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..101
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11202
     Region          6..100
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(21,23..25,31,53,55..57,59..61,64..65,87,91..92,94)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            56
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 msvvtdvspd gkkltisieg rfdfgrhqef resyeklekk pesvvvdlrk atyldssalg
       61 mllllrdhag gdssdirvvn snsdvrkila isnfdklfdi t
//
LOCUS       WP_010457032             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: 2OG-Fe(II) oxygenase [Pseudomonas].
ACCESSION   WP_010457032
VERSION     WP_010457032.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..256
                     /product="2OG-Fe(II) oxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=28420
     Region          133..243
                     /region_name="2OG-FeII_Oxy_3"
                     /note="2OG-Fe(II) oxygenase superfamily; pfam13640"
                     /db_xref="CDD:463943"
ORIGIN      
        1 mmldverlde tcikklanee vlairvkgll pqplaiqigd kilapgfegy inapsigrig
       61 mafyeaenqp lliedyfeha srniaelrkr capysspvdt lrcmldeswp agahlenlyg
      121 rkmyvglsrv vkpgvcflah hdifakdapd syqarsleaq facnvylnmp seggalqmwd
      181 hdispdqfde mrgdsygidp allgtpalei rpepgdfimf nsrcmhsvtp gvadprlsls
      241 ffvgyrgnas pltfws
//
LOCUS       WP_010457247             326 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010457247
VERSION     WP_010457247.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..326
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36266
     Region          4..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtahrigfli wpstkaltla laeealrvaq rvhpdvvyel sflqaeppte gawqlpgepw
       61 agklenfqkl flladepptt lapalssslk qlvragcvig glsagvypla qlglldgyra
      121 avhwrwqddf aerfpkviat shlfdwdrdr ltacgglsvl dlllavlard hgaelagavs
      181 eelvverire ggerqriplq nrlgsshpkl tqavllmean ieeplttdei aqhvcvsrrq
      241 lerifkqyln rvpsqyylel rlnkarqmlm qtsksiiqig lscgfssgph fssayrnffg
      301 atpredrnqr rssspfelss vpserg
//
LOCUS       WP_010457301             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudomonas mandelii].
ACCESSION   WP_010457301
VERSION     WP_010457301.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33178
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mnklellrtf vrvsemssft lageslglpr stvsdhvqal etllgtrllq rttrrvqatq
       61 dglvlyersk dllshmddie glfrqdpasl vgriridmpn flarqvvmpq lpefmarhph
      121 leleisttdr rvdllregfd cvlrvgsqpd qsvvarrvcd famvncaspa ylarygipet
      181 ledlaqhrmv hyvgvlgsrs dgflyevegk prqlpmagnv tvnstdayel acvggfgliq
      241 apvkgmqshl nsgdlvavlp qfsapsmevs llyarqrhlp lrvrafmdwl anviqstt
//
LOCUS       WP_010457358             314 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Pseudomonas].
ACCESSION   WP_010457358
VERSION     WP_010457358.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..314
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34674
     Region          25..289
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mihdtfwlta sdrsrlfvnq wlpdpplkav illahgmaeh sgryarlaek lcaqgygvya
       61 pdlrghgkta engtlghfad ddgwckvvgd laslnqhigq qhpgvpivll ghsmgsyiaq
      121 ayllhhsasl hgavlsgsnf qpialyraar qiarveklrq gpkgrsalie wlsfgsfnkk
      181 fkpvrtrfdw lsrdpaevdr yandplcgfr ctnqlwidll gglqqiskas nlaqidpglp
      241 llviggecdp vsegkrlkdl adalraagsq nlqltiypqa rhelfnesnr devindvlnw
      301 iaqalshrrp prse
//
LOCUS       WP_010457364             662 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Pseudomonas].
ACCESSION   WP_010457364
VERSION     WP_010457364.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..662
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71765
     Region          16..654
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mpitlqalfa pdrralqfai ktliggglal wlalrwgleq pawalmtafi vaqplsgmvv
       61 qkglarllgt lvgtimsvvf mglfaqtpwl fllalalwlg lctasstllr sawsysfvla
      121 gytvaiialp aithpltvfd qavarcteic lgilcataas allwpmrver qladqaraaw
      181 nsgmnaarat lagdaqarkg lleilgriva vdaqrehawf egglgrqrar aisglsqkll
      241 mllriarsvr rqwkqlepqe aeqlspwmte vqvalsgddt atlqalrprl ldashdphis
      301 saqsyclarf tllldtamaa taamkaveeg retvdpprtl aphrdlslal vfgarsalaf
      361 lvvscfwlat awpaasgalv ltcvvcslfa srengaqigm sfmrgiflai paaffvgqil
      421 lpqwsgfall cmgmgvplff galgmakpqi gatatsfclh fivlvsplna mkfdvatffn
      481 saqamvvgvg aavlafhlli lrnpawhgrr llaatlddlv rltrrnlrga eswfggrmad
      541 rllqlarhyp elpeparsrw ddgllgldig dellhlrlsl avaqvpvsap qrryleqlek
      601 vleqgpagnc adalerpsad flktlyalpp sdavklaqga vlqlqsswra wcrqqeqshg
      661 la
//
LOCUS       WP_010457386             386 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010457386
VERSION     WP_010457386.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..386
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42006
     Region          1..365
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matlelrnvn ktygpglpdt lknielsikd geflilvgps gcgkstlmnc iagletitgg
       61 aimigdqdvs gmspkdrdia mvfqsyalyp tmsvreniaf glkirkmpaa dieaevarvs
      121 kllqiehlln rkpgqlsggq qqrvamgral arrpkiylfd eplsnldakl rvemrtemkl
      181 mhqrlktttv yvthdqieam tlgdkvavmk dgiiqqfgtp kdiynnpanl fvasfigspp
      241 mnfiplrlqr kdgrlvalld sgqarcelpm gmqdagledr evilglrpeq ivlagsepng
      301 lptiraevqv teptgpdtlv fvnlndtkvc crlapdvapn vgetltlqfd pskvllfdak
      361 tgerlgvagq pkaeshganv aqfkgr
//
LOCUS       WP_010457493             156 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Dps family protein [Pseudomonas].
ACCESSION   WP_010457493
VERSION     WP_010457493.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..156
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=17552
     Region          2..154
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 maidigisee drksivdgls rllsdtyvly lkthnfhwnv tgpmfrtlhl mfeeqynela
       61 lavdsiaeri ralgfpapga ysiyerlssi keeagvpsae dmikqlvdgq eavtrtargi
      121 fpllekvsde ptadlltqrm qvhektawml rslldq
//
LOCUS       WP_010457515             210 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Pseudomonas].
ACCESSION   WP_010457515
VERSION     WP_010457515.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..210
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22822
     Region          4..76
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(15,17..18,20..21,24..25,69,72..73)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(15,54..56,67..68)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(54,66..67,69..70,73)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          90..203
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(92,99,161,164..165,168,172)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(92..93,96..97,100,136)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(99,103..104,107..108,169,172)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mslhliigdk llsswslrga laldltgapy teeliklgqp dtrerllkhs ptgkvpllks
       61 vhgtiadsla iaeylaeqfp daglwpkdta araqarsaca qmhagffamr gnmpfdlsrd
      121 aplsptppev qadiermlal waecravate tgpflfggat ladaffapia vrlrtyqvkl
      181 pavdeayvet vyqwpsfkaw qkagleeigq
//
LOCUS       WP_010457542             241 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RDD family protein [Pseudomonas].
ACCESSION   WP_010457542
VERSION     WP_010457542.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..241
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=26138
     Region          22..164
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mlettalprn atlpppldtr yqvetpegid lplrpaglmv ralafsidlg lrglilgvlf
       61 ivlaflgklg aglgsillfg vswwymvlfe vlnqgrspgk qwmglrvvhd dgtpigwsas
      121 llrnllrfvd llpfgyflga isclqhpsfk rlgdlaagtl viyreqpltr pqlpdvqprr
      181 pafaltlpeq ravlgfaerq gelsearshe lasilaqplq vpapravael naiargllgp
      241 a
//
LOCUS       WP_010457563             439 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010457563
VERSION     WP_010457563.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48045
     Region          28..431
                     /region_name="MFS_KgtP"
                     /note="Alpha-ketoglutarate permease of the Major
                     Facilitator Superfamily of transporters; cd17367"
                     /db_xref="CDD:340925"
     Site            order(38..39,42..43,46,84,142..143,145..147,150,170,
                     173..174,177,256,259..260,263..265,268,296,300,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340925"
ORIGIN      
        1 mdnsnalplg saavpakert tasriksifs gsvgnmvewy dwyvyaafsl yfakaffpkg
       61 dttaqllnta aifavgflmr piggwlmgly adkagrkkal masvylmcfg sllialspgy
      121 etigigapil lifarllqgl svggeygtsa tylsematkd rrgfyssfqy vtlisgqlia
      181 lavlivlqqv ltteelyawg wripfaigal cavvalylrr gmeetesftk kekakesamr
      241 tlmrhpkelm tvvgltmggt lafytyttym qkylvntvgm sisdsttisa atlflfmclq
      301 piigglsdkv grrpiliafg vlgtlftvpi lttlhtiqsw wgafflimaa liivsgytsi
      361 navvkaelfp teiralgvgl pyaltvsifg gtaeyialwf ksigmetgyy wyvtaciavs
      421 llvyitmkdt rkhsrietd
//
LOCUS       WP_010457573             351 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010457573
VERSION     WP_010457573.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..351
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37455
     Region          1..351
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msglilenve khygsacavk dvnlhlpegk lvcflgpsgc gkttllrmia gletlsggei
       61 rldgedight pahqrnfgmv fqslalfphm tvgeniaypl klrgvskadq qarvvellel
      121 iqlsemidrp vaklsggqrq rvaiaraian hpkillldep lsaldaklre smqveirqlq
      181 qrlnittimv thdqreamtm adivvvlgeh rvqqvgspie iyrhpanefv adfigsgnif
      241 patalgngkv glpggaalev picssivvge kvkmlirped lqlshpqata gnrllgtvtf
      301 vrdigatiet tvecsgvsft alstpcqgfg lsignpvsvt lpaeacrvlg a
//
LOCUS       WP_010457592             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010457592
VERSION     WP_010457592.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33187
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..287
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,222,239,266)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlqamrvf vsvvdlgsqs aaadhldlsr pvvsrylael edwvgarlmh rttrklslta
       61 agseilprcr qmldlstdmq aavsepdeap rgllrisvst sfgqaqlada maayvkrypg
      121 vsidmqmldr tvnlvderid lairtsndld pnliarrltv crsvicaspa ylsehptpqr
      181 vedlsqhncl thsyfgkslw hfeengepvs vpvegnisan eastllratm agagvamlps
      241 yqagvhihsg elirllphae prqmnvyavy asrkhmpaal rsmldflvlr fpeepawdig
      301 l
//
LOCUS       WP_010457692             369 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010457692
VERSION     WP_010457692.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40202
     Region          16..347
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mspplllnlr nlacgyqdqr vvqnlnlhln agdigcllgs sgcgktttlr aiagfepvqe
       61 geitlageti sragftlape krrigmvfqd yalfphlsva eniafgirkh pqkdrvteel
      121 lelvnlknlg krfphelsgg qqqrvalara lapepqllll depfsnldge lrrklshevr
      181 dilkargtsa ilvthdqeea favsdhvgvf kegrleqwdt pynlyheplt pfvasfigqg
      241 yfirgqlssp esvqtelgel rgnraytwpv ggavdvllrp ddivyapdsg lkarivgksf
      301 qgastlyrlq lptgaqlesi fpshadhqvg aevgirvaae hlvlfqasgs taaqipvves
      361 gvrrystas
//
LOCUS       WP_010457727             212 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Pseudomonas].
ACCESSION   WP_010457727
VERSION     WP_010457727.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22952
     Region          17..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 miplqdllif aaaallmvlt pgpnmiylis rsicqgrkag vtsllgvvag ffvhlfaaaa
       61 gltavflavp mayevlkwag alyllwlawq avkpgarspf eaqqlppdss rklitmgflt
      121 salnpkiavf ylsvfpqfit pehgsvftqs ivlgltqisv sfcvnlliai faagiaswfv
      181 nnptwlalqr yfmgfvlsal avrlmleqrr ta
//
LOCUS       WP_010457715             464 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aspartate aminotransferase family protein
            [Pseudomonas].
ACCESSION   WP_010457715
VERSION     WP_010457715.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..464
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=52142
     Region          9..458
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 msdiriatpe dqvlldkeak ycsygdtvhy idpprifsrc egsyvwdted qayldlqmwy
       61 savnfgyanp rlnnalkqqi dtlpqiasqy lhkgkielse miavdakkkf gldgrvhfnv
      121 ggsqsiedsl kvvrnatngk slmfafeggy hgrtlgassi tssyryrrry ghfgeranfi
      181 pfpyhfrgpk gmtkeeygsh cvqqfarlfe teyngvwdpk vgqseyaafy vepiqgtggy
      241 vippmnfyse lkhvldqhgi lmvvdeiqmg fwrtgklwsi ehfdvkpdvi vfgkaltngl
      301 nplggiware elinpkifpp gsthstfasn plgtavglem fkmtsevdyg krvmnkgkyf
      361 leglkdlqkr ypiigdvdgl glalrceicg pdgftpdkat ldfmveegmk gdieidgkrl
      421 glildvggyy knvitlapsl eisypeidlg ialldrlldr amkr
//
LOCUS       WP_010457734             327 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YncE family protein [Acidovorax].
ACCESSION   WP_010457734
VERSION     WP_010457734.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..327
                     /product="YncE family protein"
                     /calculated_mol_wt=35914
     Region          11..218
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <156..303
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mkifsiarac avlgglwisi ggalaaappl fvlnsleanv svidpvtwte tariptgkep
       61 hhlyltpdek siivanalgd tltfldprta evqrtvrgiv dpyhlrftpd mkwfitaanr
      121 lnhvdfyrwd gkelnlvqrv atsrtpshlw idsrsttvys tmqdsdelva idiatqtikw
      181 rtktgampad vygsaddkrl fvgltgsdsv evfdvsgrep lsikkiktgn gahafraagd
      241 grhlyvsnrv ansiskidmt tqqvvetypv pggpdcmevs adgrfiyvss rwarklsvvd
      301 teakkvvrqv tvgksphgvw tlqhapr
//
LOCUS       WP_010457753             473 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Pseudomonas].
ACCESSION   WP_010457753
VERSION     WP_010457753.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..473
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50906
     Region          9..458
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mpvgnhlphg etaqggplkr elgerhirlm algacigvgl flgsakaiem agpaimlsyi
       61 igglailvim ralgemavhn pvagsfsrya qdylgplagf ltgwnywflw lvtcvaeita
      121 vavymgvwfp dvprwiwala alismgsinl iavkafgefe fwfalikivt iiamviggig
      181 viafgfgndg valgisnlwa hggfmpngvq gvlmslqmvm faylgvemig ltageaknpq
      241 ktipnaigsv fwrillfyvg alfvilsiyp wneigtqgsp fvmtferlgi ktaagiinfv
      301 vitaalsscn ggifstgrml yslaqngqap agfattssng vprralllsi fvlllgvlln
      361 ymvpekvfvw vtaiatfgai wtwvmillaq lkfrkglsas eraglkykmw lypvssylal
      421 aflvlvvglm ayfpetrval yvgpaflvll tvlfyvfklq ptnvsqgavr saa
//
LOCUS       WP_010457775             350 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acidovorax radicis].
ACCESSION   WP_010457775
VERSION     WP_010457775.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..350
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37755
     Region          1..341
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maylqlrgie kffgehraik ginltiqqge fivfvgpsgc gkstllrlia gleaidggsl
       61 mldgrditdq psskrdlamv fqsyalyphm svyenmsfal klakvdkqvi ddkvqnaari
      121 lnltsylqrt pkelsggqrq rvaigraivr apkvflfdep lsnldaalrg qtrveiaklh
      181 rdlgattiyv thdqveamtl adrvvvlrdg vieqvgtple lydkpanqfv aqfigtpqmn
      241 vvpvdklpqp vqqqaptard gaavgaiglr penitvrhtg atpvggqvdl iealgaetli
      301 yvstpggaqf vsrqndrtgl ragdavsldi dashahwfdt agrvvaghaa
//
LOCUS       WP_010457776             244 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Acidovorax radicis].
ACCESSION   WP_010457776
VERSION     WP_010457776.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..244
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25722
     Region          6..241
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msatqtlqgq vaavtgaasg igfasakama dagarvvlid rdeaalakac aaidpsalpl
       61 vldlldaqqc asllqrtlal agrldifhan aglyvggdlv dadpdaidrm lnlnvnvvmk
      121 nvhnvlphmi ergrgdiivt sslaahfptp wepvyasskw avncfvqtvr rqvfkhgirv
      181 gsispgpvit slladwpaek laeakasgsl ieasevadvv lfmltrprgm tirdvvmmpt
      241 nfdl
//
LOCUS       WP_010457946             471 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010457946
VERSION     WP_010457946.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..471
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48950
     Region          26..460
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(33..34,37..38,41,73,123..124,126..128,131,152,
                     155..156,159,282,285..286,289..291,294,322,326,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mphspsaqap siskqdtnri lalavilsaq lmlqmdfliv mvalpqiqad lgfspaalsw
       61 vpnafalalg gllllggrlg dvygrvrafk aglavfvlas llgglanspl mlitarilqg
      121 igaaiaapsv lalvmniarn eaernrglal fitvssvgas aglilggalt eyfswrwsll
      181 invpvgifil vmigsvvket vgqraqfdig galtatagsi alvfgfinaa ehgwahfgtl
      241 psfvtavall tafwiiegra kqpllnlnll rnrtrivala vmaiivgmhf smlflvvqyf
      301 qkvlgfgpla aglaylpvtc tvfavthfmp glierfgasr lqlsgcilva csfagfafid
      361 idgsyagsvl gpmlvhslgi alvftpgtvl tmegvaaeqs giasgllqmd qqiggalgia
      421 vvtsvfafts lpgdfvsglp mafgvaalls amaavltyvv mlrapslirp i
//
LOCUS       WP_010457950             110 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thioredoxin family protein [Acidovorax].
ACCESSION   WP_010457950
VERSION     WP_010457950.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..110
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11939
     Region          22..103
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(33,36)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mpyaarhlaq ppsrddvdrl pgatvvefgt pwcghcqraq plieqalkdr advahikved
       61 gpgqrlgrtf gvklwptlvf lkdgkevarl vrpqtlqdvl dalpangapi
//
LOCUS       WP_010457991             838 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Acidovorax radicis].
ACCESSION   WP_010457991
VERSION     WP_010457991.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 838)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..838
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=89176
     Region          6..832
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mpttdsttgl dpavaaqrlr eegpnelgis qrrtlrdmaw dvvtepmfll llgagaiyla
       61 mgdahealil lgfvviimai tvlqerrtdn alnalrdlss pralalrggt lvrlagrdvv
      121 redllmiaeg dripadgtll qahelaanes mltgesepva kqpadkvfag tlvvsgqgll
      181 rvtavgrhte lgrigqsldt ialqasplrd emtrltrklv viglslcall valfwalrgd
      241 alqavlagit lamgilpqel pvimivflal aarrlaaqqv ltrrlnaiet lgqttvlcvd
      301 ktgtltqnrm avaalciagq eldvqnlpaa adgsalpdaf helleyavla seiephdpme
      361 qafhrmaadh lvdtehlhpa wslareyels pqllamshlw rdgtsahdtv atkgapeava
      421 dlchlpdaer aavsaqaarl adrglrvlgv akarhhtqdt wpdaqhdfdf ewlglvalad
      481 plrpevplai aqcrqagirv vmitgdhprt araiaaqagi andrvitgde lahmppqvla
      541 eqvrqvsvfa rikphqklal vealkaqgev vamtgdgvnd apalkaahig iamgqrgtdv
      601 areaaalvll hddfaaivla ihrgrqtfsn lrqamvytla vhvpiiglal lpvlfglplv
      661 laplhiafle lvidpacsiv feaeegaadl mqqppreane pllssrhill sllqgsvvta
      721 avvglyawll gqaahaatas taafvvlvaa naalilpsrs sqtswrslwa gltpvslwvl
      781 ggtlaglaav ttvpwlaapf kfaplsvlqw laalgaglat vavlqgckrw frvaatph
//
LOCUS       WP_010457986             122 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PH domain-containing protein [Pseudomonas].
ACCESSION   WP_010457986
VERSION     WP_010457986.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10547098
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..122
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13641
     Region          4..120
                     /region_name="bPH_1"
                     /note="Bacterial PH domain; pfam08000"
                     /db_xref="CDD:462337"
ORIGIN      
        1 midfnnkgff klkqndeyaa rvsdllidge hvidayksmr dgvvftnkri iavnvqgltg
       61 skkdftslpy knivaysvet sgtfdldsel evyfsslgkv kfeftgrtsm veisklisqh
      121 ll
//
LOCUS       WP_010458028             136 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Acidovorax radicis].
ACCESSION   WP_010458028
VERSION     WP_010458028.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..136
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14191
     Region          26..>80
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(33,36)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mqspaplpep tpqspaaatp gvwwavclca awcgtcgvyr plfdelalah pdvrfewvdi
       61 eddaeiagdl dvetfptlli adgeralflg pllpqapvlg rllaslqaas pqaggaggtg
      121 geaqevferv raarsr
//
LOCUS       WP_010458031             301 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudomonas mandelii].
ACCESSION   WP_010458031
VERSION     WP_010458031.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33662
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,223..228,
                     234..235,237..238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdlfqamtvy vkvveagsmt aaaqqcemst tmvgnhlral eqrlgvrlln rttrrqrlte
       61 fgsayyqrcl evlglvedse rlaeqsqdtp sgtlritapl tfgteklapa lsdftlrypq
      121 vkldvvltng rpdllengld vafrlgaiep snliarplid ytltmcasks ylarrgtpek
      181 pedlqqhdcl sfaypvgddw qsvekqwrls gpegevmvav rgpmlinssa glhqaartgm
      241 givmlpdalv eqdllsgnlv almqdyrlps rpmhlvyaqd ryrlpklrrf vdfamqmwak
      301 h
//
LOCUS       WP_010458108             270 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010458108
VERSION     WP_010458108.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..270
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28915
     Region          2..240
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mptivpaasr tmallevfar errelsnsdl arlmdlpess csdllhtlhe lgylmrtart
       61 rrfyptarll tvakgiaagd slyavaseac ellrdktget gmcgrveagv vkvlafaegt
      121 hplryvenvg nkialhvsal gkaelalgtp eeaarqlrlk plkqiapgsi tdlavleaqi
      181 aqareqgwmw venegfdgla aiavagylgd eplalsiagp terlrrtkda clqalqevra
      241 lvfhpqnpsp plratasgrr gagtkdttpa
//
LOCUS       WP_010458110             136 aa            linear   BCT 01-JAN-2025
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Acidovorax radicis].
ACCESSION   WP_010458110
VERSION     WP_010458110.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..136
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14026
     Region          19..128
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mkplqptlye laddghslnf ffaqcsacgg lsfpanapgc mhcgeplska pritrpggge
       61 llefvtlhvp llpgmaapsi agdiriapgi veegvmavad esalkhgmav ravaevkpee
      121 gvyacrfvpa negaar
//
LOCUS       WP_010458112             269 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Acidovorax radicis].
ACCESSION   WP_010458112
VERSION     WP_010458112.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..269
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29475
     Region          12..263
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mttpdiqdlg tllyqvrdrv avitlnrpdr mntlggtmkp dlaraffela rnddqvravl
       61 itgsgdkafc agadikerat dvvrgteyfv rqkathelfr nieefekpvi aaingvalgg
      121 gleialccdl risasharfg lpeiklgvip aaggtqrlpr lvgearakel iltadlvdae
      181 talryglvsr vvpqaelmta alelsqriaq hpplavrfak rainrgmqtd ldsgleyery
      241 aaamivdsed rvegmrafve krepqfkgr
//
LOCUS       WP_010458128             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
            ligase [Pseudomonas].
ACCESSION   WP_010458128
VERSION     WP_010458128.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..455
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=47094
     Region          5..451
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mlkalklsel tgalnarlia adatfdgvsi dsraikpgql fialagprfd ghdylndvas
       61 kgavaalver evadsalpql lvkdtrqalg qlgamnraaf tnpvaaitgs sgkttvkeml
      121 asilrtrgpv latrgnlnnd lgvpltllel apehtsavie lgasrlgeia ytvgmtkphv
      181 avlnnagtah vgefggpeki veakgeiieg leadgvavln lddkafgiwk araagrkvlt
      241 falnnpsadf yasdldrdar gcpafnlhsp egvervqlnl lgthnvtnam aaaaaahalg
      301 vslfgiatgl gavqpvkgrt vaqlasngmr viddtynanp tsmcaavdil agfsgrtvlv
      361 lgdigelgdw aeqghrdvge yargkvsaly avgplmahav nafgpqafhf stqaelikal
      421 gaeqdtntti likgsrsaam enivaalcgs slekh
//
LOCUS       WP_010458174             159 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Pseudomonas mandelii].
ACCESSION   WP_010458174
VERSION     WP_010458174.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..159
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17992
     Region          3..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mhkldrydlk ilrilaedgr itkssladai nlsvtpawer vrklealgli kgyraqidwn
       61 avfksqqvlv eitlarhtaq dmrrfeqrmc eaaevafcya tgggvdymam iqapdidhyq
      121 rfidqllldd lgieryftyi vtktiktgga lpaelaqep
//
LOCUS       WP_010458181             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Acidovorax].
ACCESSION   WP_010458181
VERSION     WP_010458181.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..239
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=25432
     Region          6..216
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mesqfgianv wiqgdfvtra vailllamsl aswivilika ldiikfkkht raaqdfwhse
       61 dfaagltklg adptnpfrhl alegreatah hrntkahlhd sldvsdwvtr clrncideft
      121 srlqsglail asvgstapfi glfgtvwgiy hallaigtsg qstidkvagp igealimtal
      181 glavaipavl gynalvrgnk silgglnsfa hdlhayfvtg arvnapgeqg kvlpmkkgg
//
LOCUS       WP_010458216             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Acidovorax].
ACCESSION   WP_010458216
VERSION     WP_010458216.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21159
     Region          2..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkpkddekqr aiaqatfelv aqtglsgltl adiaraagia tstlyvyyps kdelisqlyq
       61 daktvtaari megiapgmpy rarvrrawgn llrhrldqya evvfqeqyyn spwftdgnre
      121 fstrlmagff almeegqqqe ilkavpipll taslvgsvre tgnlirtkvl pdeeavhqma
      181 fglcwdalka
//
LOCUS       WP_010458201             194 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TMEM165/GDT1 family protein [Pseudomonas].
ACCESSION   WP_010458201
VERSION     WP_010458201.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..194
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20415
     Region          1..187
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 mldsllvpta ivalaeigdk tqllalilaa rfrkpwpiia givaatlanh aaagavgawf
       61 gsffsnavlh wilaasfaat alwtlvpdkm dddeastark fgpflttlia fflaemgdkt
      121 qvatvmlaaq ypdlwlviig ttagmlianv pvvlagnfaa dklpltlirr laasaffvla
      181 ivavykamqs sgwv
//
LOCUS       WP_010458203             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M48 family metallopeptidase [Pseudomonas].
ACCESSION   WP_010458203
VERSION     WP_010458203.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..272
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28905
     Region          78..262
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(144..145,148,202,206,245)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(144,148,202,245)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mnktlvvcal saglllagcq svnttsggav gverkqymfs mlstdevnqm yaqsyqktvg
       61 eastkgvldk tsndakrvql iadrliaqap vfrpdsaqwk wevnliksde lnancgpggk
      121 iffytglidk lqltddeiaa imgheiahal rehgreamsk aygvemakqg agallglgqd
      181 slaladtvak ygmtlpnsrg neneadligl elaaragynp naaitlwnkm skasegappe
      241 flsthpasss riaslqaaip kvmplyekap ks
//
LOCUS       WP_010458239             229 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Acidovorax radicis].
ACCESSION   WP_010458239
VERSION     WP_010458239.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..229
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25265
     Region          7..214
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mhyavaifdl dnclldarav gplfepafea irqanrhtlt pavleqalhq cwftafdlva
       61 eryrftpamr aagwqqfsqm qvraplqgyp digllsripl rrylvtsgfr rlqdskidal
      121 girpwfeqvl idaiddpqdk vgalhgkrpl feqilaregc tpqqalvigd nplselaagr
      181 algattvqtv rpgvqpwela dhqveglegv lkllspagqr qanalpara
//
LOCUS       WP_010458273             227 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acidovorax radicis].
ACCESSION   WP_010458273
VERSION     WP_010458273.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..227
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23806
     Region          1..200
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mirtrglayt yatggaaplr fpdvdlrqgg tlllrgrsgs gkstwlslma glrgasggdl
       61 fvagtqlgtq rgaeidawra rnigflpqkl ylssalsvad nlalvyfasg lprddaairr
      121 alaqvgvael aarkphqlsg gqaqrvalar avllapqlll adeptasldd eaaadaltll
      181 qqsaaacdas lviathdhrv vqaladvqtl dlnemgvqrl tdkreql
//
LOCUS       WP_010458291            1030 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Acidovorax radicis].
ACCESSION   WP_010458291
VERSION     WP_010458291.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..1030
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=111596
     Region          7..1016
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msasrfnlsa lavrersitl flialitlag lvaflqlgra edpaftvkvm tivtawpgas
       61 aqemqdqvae kiekrlqelr wydrsetytr pglafttltl ldstppslvq eqfyqarkkv
      121 gdeagnlplg vigpmvndey advtfalyal kakgeaqrll vrdaetlrqr llhvpgvkkv
      181 nitgeqseri yvefsherlg tlgispqdvf aalhsqnalt pagsvdtkgp qvfirldgpf
      241 delqkirdtp vsaqgrtlkl sdiatvqrgy edpatfmirn ggepalllgv vmregwngld
      301 lgkaldgevs ainadlplgm gltkvtdqav nisasvdefm vkffaallvv mlvsfvsmgw
      361 raglvvaaav pltlaivfvv maatgknfdr itlgslilal gllvddaiia iemmvvkmee
      421 gysrvaasay awshtaapml sgtlvtavgf mpngfaasta geytsnmfwi vgialiaswv
      481 vavvftpylg vkllpnfkkv egghaaiydt qrynrlrqvl grviarkwlv asavvglfvv
      541 ailgmgivkk qffpisdrpe vlvevqmpyg tsitqtsdat akveawlakq aeasivtayv
      601 gqgaprfyla mspelpdpsf akivvstgsq eerdalkhrl rqavadglap earvrvtqlv
      661 fgpyspfpva yrvigpdtdk lreiaaevqq vmttspmmrt vntdwgtrtp tlhftlnqdr
      721 lqalgltssa vaqqlqffln gvpvtavred irtvpvvars vgdvrldpar iadftlsgan
      781 gqriplsqvg kvdvrmeepv lrrrdrmpti tvhgdiadgv qppdvstsit aqlrpvmdkl
      841 pggyrieeag sieesgkatq amlplfpiml aatlliiifq vrsisamvmv fltsplglig
      901 vvptllvfgq pfginalvgl ialsgilmrn tliligqidh nqqeglepfq avveatvqra
      961 rpviltalaa ilafiplths vfwgalaytl iggtlagtvl tlvflpamys iwfrirpddn
     1021 kplvaretpv
//
LOCUS       WP_010458335             215 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: adenylate/guanylate cyclase domain-containing protein
            [Acidovorax].
ACCESSION   WP_010458335
VERSION     WP_010458335.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Sinha,S.C. and Sprang,S.R.
  TITLE     Structures, mechanism, regulation and evolution of class III
            nucleotidyl cyclases
  JOURNAL   Rev Physiol Biochem Pharmacol 157, 105-140 (2006)
   PUBMED   17236651
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..215
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016849 - phosphorus-oxygen lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0032555 - purine ribonucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=22886
     Region          42..188
                     /region_name="CHD"
                     /note="cyclase homology domain; cd07302"
                     /db_xref="CDD:143636"
     Site            order(47,49..54,89,91..93,96,147..149,153..154,157..158)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(49,93)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(54,66,69..70,73,77,89..90,141,142,148..151,154)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
ORIGIN      
        1 mtavphtphd kaslrrllsq rnqepgntaa idaaieqafv rnvailvldm cgfsritarh
       61 gvihflamvh qmeqaarpai sgnggevikq eadnlfavfa taeqaleaal dtlraleamn
      121 avlpserall vsagigygpt lviasedlfg pemncacklg ediagagdil lthaahaslp
      181 anryacseea heisglvlqs yrfgqclfdr pwrsa
//
LOCUS       WP_010458292             685 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Pseudomonas].
ACCESSION   WP_010458292
VERSION     WP_010458292.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..685
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=72872
     Region          157..684
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mqaflspgig llgrfgfark fqllfllfil plagslvmig qdyraklnli sgeragvrql
       61 laldaldnll aaqrdraarw ratetnrqpt patlaamagf davqpavaqa tsdlgdalkt
      121 egaegetltr yqalqtalng ldskslssvg wwpdgydrft nalsalqalr eqiamdnrlt
      181 lapwletyll tqistqhapd liervgrlas vgqasvvsgq ftlqsrlqlr dlrsrigdar
      241 eqlaktasll earlpsalqs wagqyhdslk hldaelkvld dgvfggsikl kpeefersld
      301 slltdlaslr qqslvsldqr ldyyhgsais qfilvatifg clllaalylf iclqasirrs
      361 asgitllaea lrdgnlslqv pvqgrdelaa istalnvavv qlrnsllgvd hetlqvsnav
      421 rtlnhhssga lgeveaqqlq isqiaaaatq laatsqgvaq sceqasgsaq htqriaadss
      481 rdsqrttasi qqlnqrlndt aaalgrvseq gqqiqlvvdt irgvaeqtnl lalnaaieaa
      541 rageqgrgfa vvadevrsls qrtqsstaqi agtvdslrst vneavslmea acsqaqsdaq
      601 svtglgerlg eiahavqgvt dtlaqiatav eeqastadev sgniqqvdqa avrllegara
      661 vnlaadtlsq gskalsantg rfqls
//
LOCUS       WP_010458367             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Acidovorax].
ACCESSION   WP_010458367
VERSION     WP_010458367.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26299
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlttqrkqli lhrlqqdgqi varalseelg isedtvrrdl relaaegrlq rvhggalpas
       61 aavgslqvra qlatdekrel gragaalvqp gqvviidggt tslqvvqhlp ldlratvvth
      121 spsvavalad hlqvevlmlg grlfrhsmvn vgasvteaam rlradlylmg vtgvhadagl
      181 ttgdfeeaav krtlharaae tvvlasidkl gaaspfgiaa lkelatlvvp aatpgkvvas
      241 lraagakvvs arp
//
LOCUS       WP_010458371             185 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010458371
VERSION     WP_010458371.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..185
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=20593
     Region          8..176
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnalhttlle lgtvrqvdar qlllrageva rrlylieqgc arlylvdtqg retstqfffe
       61 gdvvssmesf ltgrpsalhl vtmepcrvrv vegaalkara ktdpslqadi qaltqqrlih
      121 yanlytsaia dsptqryqal qathqhqler iplhilaayl gvsavhlsri rrklkenppe
      181 adprg
//
LOCUS       WP_010458404             689 aa            linear   BCT 01-JAN-2025
DEFINITION  M3 family metallopeptidase [Acidovorax radicis].
ACCESSION   WP_010458404
VERSION     WP_010458404.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..689
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=76872
     Region          1..686
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 msnalldfsd lphfdritpq dvvpavdvll eranaaleav tapdfparwd aiakvldvat
       61 erlgtawgsi shlnsvadtp elraaynaal prvtefwtrl gaderlyaky kaidpatlta
      121 eqrqahlnav rnfvlsgael tgaakerfaq iqerqaelsq kfsenaldat dayayyatae
      181 elegipddvq qaalaaaqad gkegykltlk mpcylpvmqf atrselrekl yrayvtrasd
      241 qaegdarkfd ntaliseila lrreeaqllg yanfgevsvv pkmaqspaqv itflrdlarr
      301 arpyaekdia dlrafaaehl gladpqawdw pyiseklkea ryafseqevk kyftapkvla
      361 glfkiietlf evsirrdtaa vwhpavefyr ierahpegth kgtqlvgqfy ldqpartgkr
      421 ggawmddvrt rwlrpdtgvl qtpvahlvcn fasgvdgkpp llthddvitl fhefghglhh
      481 mltqvnerdv sgiggvewda velpsqfmen fcwewdvlkh mtahvdtgep lpralfdkmi
      541 aaknyqsgmq tlrqiefslf dmllhtehdp aqdimplldq vrrevavlqp pafsrtahtf
      601 shifaggyaa gyysykwaev lsadayaafe etsgsdglps ietgrryrqa ileaggsrpa
      661 mesfkafrgr epsldallrh qgmaeesta
//
LOCUS       WP_010458463             519 aa            linear   BCT 01-JAN-2025
DEFINITION  amidase [Acidovorax radicis].
ACCESSION   WP_010458463
VERSION     WP_010458463.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..519
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55107
     Region          6..476
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mttapstlve lttnelrhri atreispvel ldacieriea vnpyvnaita tcydrartea
       61 kaaeqavqrg eplgllhglp lgvkdleata glltsygsei yrsnipaedn vlvarlraag
      121 aivagktnip emgagansrn tvwgatgnpf npnlnaggss ggsaaalacd mlpvctgsdt
      181 ggslripasi cgvvgfrpsp gvvpssrkll gwtpisvvgp mgrtveeacl qlaatagmsa
      241 gdplsypldp msfllpdtvd lsrlrvayte dfgacavdng iravfrqkvq amkhlfarcd
      301 aididlgdvh rcfdvlraea fvastreaye rdpaslgpnt ranyemgaam tlldsawaqa
      361 eqtrilarfq klyedydvil apttpvspfa wtqlfashin gepqanyyrw laltyvttlt
      421 thpalslpcg lddagvpfgl qivgrfradr htlgvghame qafkgiagla rprpdlaklm
      481 qthaepalts ivtgapdprd arslprddra asavqvsav
//
LOCUS       WP_010458497             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010458497
VERSION     WP_010458497.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..222
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24714
     Region          4..220
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mqiqpleqgn lsarayyair egliagnfrp gerlvmqdla dklgtsvtpv reaclrlvse
       61 rglelrsgrf amvpeltmsr ylevrtiria leglaaelat rnvtpqdltr leelhasfqq
      121 adqandgpqa mhfnrefhft vyrlaamdml taqieglwvs mgpilnlfyt kghntyigad
      181 ehlvliealr ekkpakarka iaedimrggv siigfitese gk
//
LOCUS       WP_010458486             421 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010458486
VERSION     WP_010458486.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 421)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..421
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46612
     Region          <197..419
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 msvssidapa cvdtlavahy qssrrkrwvs mllllpllay tcvffalpig mmfyravsnp
       61 ellqafptai rtmvdepakd stalptdrvf daleqdfina psnavigeaa rrlnyensgy
      121 rflvmntart yrtplanpes qsarerlaai derwispqvw edfrraspay tpyyllaald
      181 lkqtdqgvap veesqrvyld ltfktlkial ivsllclllg fpfaalmvka spalqvllfl
      241 avmlpfwtsl larttawivv lqdkgivntl llrfglidhp lpmifnlsgv yivmvhillp
      301 fsvlplynvm knipphfmra saslgahpir gfmqvylplt ltgigsgtll tfivaagyyv
      361 tptlvgsare qmlgyfiafy tnttvnwgma salglvlisc vmviyllaar lvgirqiagl
      421 r
//
LOCUS       WP_010458530             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Acidovorax].
ACCESSION   WP_010458530
VERSION     WP_010458530.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..163
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=16508
     Region          93..>162
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mnnlmisqrp ahriatilav salalglsac gkkeeptagq rldsavakte qaaaearaka
       61 esamqnaetk veqgaanaes svkeaankgm vflsdaeita qisaslakdp dlsavkinvd
      121 tangrvtlkg papstvarer aegiakavng vssvnnqlvv sas
//
LOCUS       WP_010458542             137 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Acidovorax].
ACCESSION   WP_010458542
VERSION     WP_010458542.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..137
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14102
     Region          25..133
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mftslqnpla lasrlllaal flpagisklt gfagtvgyit svglpmptva aavaaavevl
       61 gslalifgfg trfaalalaf ftlvasfffh afwnlpadkq mmqqllffkn vgvtggllal
      121 aafgaggwsl darqsgr
//
LOCUS       WP_010458570             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Acidovorax].
ACCESSION   WP_010458570
VERSION     WP_010458570.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..224
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24739
     Region          8..224
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtlrrpsplq dpapkrraad vaydaietmi stlqlqpgsp vveaeiaest glgrtpvrea
       61 llrmvsigli vqqprrgllv shidladhld viqtrrvler llasnaarra tapqrqaivr
      121 caenmvqaaa rghldgymla dheldlvthq asqnhsavkc vqplivqcrr fwyayqhege
      181 vsegarahmq laqgiasgde aqamagaeql meylerfarr iidr
//
LOCUS       WP_010458567             421 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Acidovorax radicis].
ACCESSION   WP_010458567
VERSION     WP_010458567.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..421
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44231
     Region          1..419
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mittlfflaa llvgvpigvc lclsgavyil sigspvlfqs fpmqmfggvd sygliaiplf
       61 iligeimnsg gitrrlvdls mafigsvkgg layvnilanm lvssiigsat aqvaimsqvm
      121 vpemvkqgyd ktfaagltvy ggmlgpiipp svmfvvfsvl aqvavgdmli agilpgvllt
      181 lmffivialm gfiydyprse krtlaqrart ivqasptlli pivivgsils glanpteaaa
      241 vgalasalvg ryvtkefrfs ampaillrsa iysaivlflv aaaavfswll iygkvpqlva
      301 awvqtvahdp vtflllvnvi llvigtvidg ipglimtvpi llpiatdvyh idprhfgvvv
      361 vvnlvlglmt ppvglsffva savtgakpgk mfivtlpffi iscvalvvls lfpslslgll
      421 k
//
LOCUS       WP_010458593             322 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Acidovorax radicis].
ACCESSION   WP_010458593
VERSION     WP_010458593.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..322
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=34595
     Region          50..311
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mftapstttf aqtactwlra salgsamlvc savfaatpip agplvstewl aqnldnqqvr
       61 ivevsvnpgl yerghvpgav nfswhqdlnd rvrrdivgke afeallskag vsqdttvvly
      121 gdtnnwfaaw gawvfdiygv knvklldggr kkweaenqpl nnrvpdvaat sykvtkvntd
      181 lrarlsdala aaegksnakl vdirsadeys gkifapagvp elsiraghip gaanvpwgqa
      241 vkedgtfksa edlkklyasa gldgskpiit ycrigerssh twfalskilg ysvknydgsw
      301 teygnsvgvp isnpagtiwa ak
//
LOCUS       WP_010458623             261 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Pseudomonas].
ACCESSION   WP_010458623
VERSION     WP_010458623.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..261
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27301
     Region          6..261
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mdfvnfglvv aglvvgfivg mtgvgggslm tpillwfgin patavgtdll yaaitkssgv
       61 lvhrknnnid waitgwltlg svpavaltlw flsslqtspd amnavikqal gfvlfatala
      121 iffkkrlldf ahkragghyn psgsrlnvlt vitglvlgtm valtsigaga lgtvalfily
      181 pllptrrlvg teiahavplt lvaglghasm gnmdwqvlgy llvgslpgiy lgshltgris
      241 devlrpclat mlvligykla f
//
LOCUS       WP_010458641             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Acidovorax].
ACCESSION   WP_010458641
VERSION     WP_010458641.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..145
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14841
     Region          1..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mfkhilvpvd gsntsmlavs kaaalaktfg savtavyvvd pypftgvgad faygqaqyin
       61 aataeanaal eatrkamaea gvnvttlvge ghavhdgilr alestgadli vmgshgrrgl
      121 eklvlgsvtq rvlgvvhipv lvvrd
//
LOCUS       WP_010458760             339 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010458760
VERSION     WP_010458760.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..339
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37143
     Region          1..332
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mafvqleglg krygeidavv atnlsvekge fvsllgpsgc gktttlqmia gfvevssgri
       61 lldgrditha kpasrglgvv fqsyalfphm tvkdnvafgl rmrkvpgael qqrvdrvlkl
      121 vrlnqhaery prelsggqrq rvalaralvi eppvllldep lsnldanlre emqfeirriq
      181 revgittlmv thdqsealsi sdrvvvmqag ritqidapyt lyehprtefi sgfvgkanll
      241 pgerdgagvv qvqrggeltl slrpekidlr ehgqgrlqgq ivsrfflgsq wlygvstnlg
      301 elsvvrrndg sapltegtav gldwdatllr vlsvdevpa
//
LOCUS       WP_010458777             651 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acetyl/propionyl/methylcrotonyl-CoA carboxylase
            subunit alpha [Pseudomonas].
ACCESSION   WP_010458777
VERSION     WP_010458777.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..651
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70339
     Region          6..458
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          583..648
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(605,614..616,623)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            615
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 msapvitsll vanrgeiacr vmrtakalgl ttvavhsatd rdarhsread irvdlggska
       61 adsylqidkl iaaakasgaq aihpgygfls enagfaraie dagliflgpp asaidamgsk
      121 saakalmeta gvplvpgyhg eaqdfdtfrd acerigypvl lkataggggk gmkvvedvsq
      181 laealasaqr eakssfgdsr mlvekyllkp rhveiqvfad qhgnclylne rdcsiqrrhq
      241 kvveeapapg lspelrramg eaavrsaqai gyvgagtvef lldsrgefff memntrlqve
      301 hpvteaitgl dlvawqirva rgealpmtqe qvplighaie vrlyaedpsh dflpatgrla
      361 lyresaegpg rrvdsgveeg deispfydpm lgkliawged reqarlrlls mldefaiggl
      421 ktninflrri iahpafaaae ldtgfipryq eqllpepadl sdefwqaaaq afaqsqpgsp
      481 raddlsspwa vgngfraglp reitlhlsce gqdraltlgn vdahtaqlkg eqlltehngv
      541 rrqhrvirrg evvylqwege lrrieaydpi saveashshq ggltapmngs ivrvlveagq
      601 tveagaqlvv leamkmehsi raphagvika lycqegemvs egsalvelee a
//
LOCUS       WP_010458856             280 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HDOD domain-containing protein [Acidovorax].
ACCESSION   WP_010458856
VERSION     WP_010458856.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..280
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=30389
     Region          7..253
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mkqlttdail rsvhelpalp avvleliqsf gdshisaeql avkishdqai aaktlrlans
       61 sfyglprqvt siaeatailg lrtlrsvata aglvggfsks rcqgfdfdaf wrhsigtalt
      121 cralaqrtrl dedaaftlgl vhdigrlvlv ssyeeeyaha iayraehdcl mhaaerhhfg
      181 vdhaevggvi aehwhfapei vtaiachhrp pstrnrglad lvhvadniah gldlshkedd
      241 mvpllsldaw grlalgdkdy aevfdavaeq hevvchalla
//
LOCUS       WP_010458816             215 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Acidovorax].
ACCESSION   WP_010458816
VERSION     WP_010458816.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..215
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22558
     Region          1..207
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mlsiiqaagw piwpliacsi lgmalvferf valktarvap pklldeaitv sskavptpdv
       61 vnqlaqnsal gevlasglrt lnsnpqcset dlraamegag ravahrleky laalatiasa
      121 apllgllgtv igmieifgsq sgsggvgqam gggnpaqlah gisvalynta fglivaipal
      181 ifwryfrarv daylltlela seqfvrhilr lrkak
//
LOCUS       WP_010458871             510 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA carboxylase subunit beta [Acidovorax].
ACCESSION   WP_010458871
VERSION     WP_010458871.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..510
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56068
     Region          1..508
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mqdildqlek kralarlggg qkridaqhak gkltarerie lllddgtfee wdmfvehrct
       61 dfgmednkip gdgvvtgygm ingrlvfvfs qdftvfggal sethaekick vmdqamkvga
      121 pviglndsgg ariqegvasl ggyadvfqkn vlasgvipqi smimgpsagg avyspamtdf
      181 ifmvkdssym fvtgpevvkt vtheevtaee lggavthttk sgvadmafen dvealmmlrr
      241 lynylplnnr ekapvrpsnd padrmdrsld tlvpenpnkp ydmkelilkt vddgdffelq
      301 peyaknilig farmegqtvg ivanqplvla gcldikssik aarfvrfcda fnipvvtfvd
      361 vpgfmpgtsq eyggiikhga kllyayaect vpkitvitrk ayggaydvms skhlrgdvnl
      421 awpnaeiavm gakgaveiif redkndpvkl aareaeykqr fanpfvagar gfiddvilph
      481 etrkricrsl vmlrdkklen pwrkhgnipl
//
LOCUS       WP_010458932             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fumarylacetoacetate hydrolase family protein
            [Acidovorax].
ACCESSION   WP_010458932
VERSION     WP_010458932.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..231
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24494
     Region          22..231
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msyvfspapv asvpvvgsgd rfpvhriycv grnyeehake mgftgreppf ffmkpadaiv
       61 vvnagetgql pypsltanlh heielvvaig kggkniaaad afthiygyav gldmtrrdlq
      121 ndmkkqgrpw cigkgfdasa pigpitpaaq agdvakaaiw lqvngadkqr stvaqliwni
      181 aetiehlsaa welqpgdliy tgtpegvgav vrgdvleggv eglgtlrlsv v
//
LOCUS       WP_010458934             183 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Acidovorax radicis].
ACCESSION   WP_010458934
VERSION     WP_010458934.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 183)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10632273
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..183
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20568
     Region          8..40
                     /region_name="Nudix_N_2"
                     /note="Nudix N-terminal; pfam14803"
                     /db_xref="CDD:464323"
     Region          44..167
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04511"
                     /db_xref="CDD:467545"
ORIGIN      
        1 mtfrspikhc racgtavvyr lpddgdtkqr avcpvcntvh yenplnvvgt vpalpdgril
       61 lckrnieprw gkwtlpagfm eldettaqga aretdeeaga qiemgplfsl lnvrrvgqvh
      121 lfyratllsd qfnpgyetie arlftedevp wdelafrtvk etlecyfadr kagtmgmhfi
      181 die
//
LOCUS       WP_010459000             299 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010459000
VERSION     WP_010459000.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33130
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mprhnlndll afvtvaregs ftraaallgv tqsalsqtvs glekrlkirl ltrttrsvsp
       61 tsagerlmqa ighrfdeiea eldaltelrd kpagtvritc gdfvlktill prltpllley
      121 pdikvefdin ygfrdivadr fdagirfgdt vdkdmiaapi gpevrmaava spsyfarnsm
      181 pkkpqdlvnh tcidiryptl ggvdawefek rgrkinvrvv gqvivntsah vpaaavnglg
      241 iaylpeeefa phieegrlvr vledwcplfp gyhlyypsrr lptpafslvl nalrgeafy
//
LOCUS       WP_010457494             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Pseudomonas].
ACCESSION   WP_010457494
VERSION     WP_010457494.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Lindquist,J.A. and Mertens,P.R.
  TITLE     Cold shock proteins: from cellular mechanisms to pathophysiology
            and disease
  JOURNAL   Cell Commun Signal 16 (1), 63 (2018)
   PUBMED   30257675
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20378504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..200
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21644
     Region          1..112
                     /region_name="CSP_NTE_dom"
                     /note="cold shock protein N-terminal extension domain;
                     NF041604"
                     /db_xref="CDD:469488"
     Region          133..196
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mlkivhllmg aaalllsfip slqpeaapyl qqpaalylaf fgllnltlap vipywnkgpr
       61 hqlqnlvsal lvlavvlqtl tllapmpvia gqpavlfslv aaliavllhl aisfyksspa
      121 aaspsydmsn rdtgtvkwfn tskgfgfisr dsgddifvhf rairgeghrv lvegqrvefs
      181 vmnrdkglqa edviaalprr
//
LOCUS       WP_010459069             478 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acidovorax radicis].
ACCESSION   WP_010459069
VERSION     WP_010459069.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..478
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50517
     Region          8..466
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mttplqsntl laveglgiqv ggrrllrdin fslrpgealt lvgesgagks llaqaimgnl
       61 ppalqatgqi tldgtstraq daaarralwg rklallpqep slalnplarv apqlaevyrl
      121 lhqqppsaas aqaeqvlsaa glggagshyp wqlsggmaqr avaaitlvgg apvlmvdept
      181 kgldahwrgr mvelfqcvlq aggclltith dmqvaqalgg qvivlrhgqa aeqgdihtva
      241 aapqhaftrq llqadpahwr pfaeptlges vvqargiska ygaqklfapl dlelhsgeri
      301 avqgpsgtgk stlgnvllgl vapdtgrver sarlrphafq klyqdpvssf aphislaqsl
      361 rdaarlhrcd wkavqqrlaq lrvpedllar kpeqvsggel qrialarvlv aqpallfade
      421 ptsrldpitq heslkvllda vqetgaalvl vthdehiaga istrtlhfaa aaphplgp
//
LOCUS       WP_010459100             552 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: arylsulfatase [Pseudomonas].
ACCESSION   WP_010459100
VERSION     WP_010459100.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..552
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60610
     Region          33..482
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16142"
                     /db_xref="CDD:293761"
     Site            order(40..41,82,135,137,260,313..314)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293761"
     Site            order(40..41,82,135,137,260,314)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293761"
ORIGIN      
        1 meqlsdrfkl sivfaallsl nglahaaqte ktnilfivsd dtgygdlgpy gggvgrgmpt
       61 psidelaaeg vtfysfyaqp sctpgraamq tgripnrsgm ttvafqgqgg glpaaewtla
      121 svlktggydt yftgkwhlge adyalpnaqg ydvmkyvgly hlnaytyadp twfpdmdpet
      181 ramfqrvtkg alsgkagekp ieefkvngqy vdtpvvdgkp gvvgipffdn yvekaalefl
      241 dtaaksdkpf finvnfmkvh qpnmpapefv hksmskskya dsvveldthi grildklkal
      301 gldkntlvvy ttdngawqdv ypdagytpfr gtkgtvregg nrvpaiavwp dkikpdtknh
      361 ellggldlma tfasvagvkl pekdregqpi ifdsydmtpv ltgsgpsprk ewfyftenel
      421 spgaarvgny kavfnlrgdd gaqtgglavd tnlgwkgaek yvatvpqvfd lwqdpqeryd
      481 lfmnnftert wtmvpitgai mklmktyvdy pprklqsmgy dgpielsqyq kfqtvrdtlk
      541 keginlpmpa gn
//
LOCUS       WP_010459109             378 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Pseudomonas mandelii].
ACCESSION   WP_010459109
VERSION     WP_010459109.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..378
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41362
     Region          4..357
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(24,26,57,99,233,310,331,333..335)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(24,26,57,99,101,108,180,183,185,233,240,310,331,
                     333..334)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(26,101,180,183,185,334)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            185
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 midlfesqlv ggtlrlknri vmapmtrtrt segdvpnelm atyygqrasa glivaeatdv
       61 apssngyamt pgiytpaqrq gwslvtdqvh rnggtiflql whvgrmahps lmpngeapwg
      121 vtderaesqv fahgpdgkld hipagqprrl tseevmalvd tftqecihar eagfdgveih
      181 gangylveqf mnsvlntrtd sygggslenr trfllevvea avrewgpgrv gvrlspfgkf
      241 ngipadplte etllyvaerl grlgvaylhl vyelmpeenm elaefksnhl dhallakvra
      301 afpgaiiwcg gftdrnsaqa aldtglvdli afgrpfianp dlaerlkhgw plaeadrsay
      361 ytrrgevgyt dfpayslg
//
LOCUS       WP_010459151             308 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Pseudomonas mandelii].
ACCESSION   WP_010459151
VERSION     WP_010459151.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..308
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33504
     Region          1..241
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mqpirlglvg ygkiaqdqhv painanpafq lvsvatqgqp cagvenfrsl gelldkgpqv
       61 daiafctppq grfalvqqal sagkhvlvek ppcatlgeam alvsqvqeqg vsglfawhsr
      121 yapgieaara wlatrtlhsl qidwkedvrk whpgqawiwq pgglgvfdpg inalsiathl
      181 lalplfvesa elrvpnncqs piaasikmsd arhldvraef dfdhghdelw sieirctegt
      241 lrldnggall sidgvrqavs eegeyaavyr hfqqligdkt sdldlqplrl vadsffvgsr
      301 vsvepfyd
//
LOCUS       WP_010459165             421 aa            linear   BCT 01-JAN-2025
DEFINITION  YeaH/YhbH family protein [Acidovorax radicis].
ACCESSION   WP_010459165
VERSION     WP_010459165.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11148708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..421
                     /product="YeaH/YhbH family protein"
                     /calculated_mol_wt=47597
     Region          14..417
                     /region_name="DUF444"
                     /note="Protein of unknown function (DUF444); pfam04285"
                     /db_xref="CDD:427839"
ORIGIN      
        1 malqiidrrl agknksvgnr erfvrrfkeq iadsvrravs qrgirdieqa esitiprkdi
       61 gepvfhhgqg girdvvhpgn adhvrgdrie rpkggsgrgs qasdsgeged dftftltkee
      121 fmqiffedla lprllrthig enpqwksrra gysqdgipnn lavlrtmrga lgrrialgka
      181 shrelialql qldallaqdd gtseavaelq rridglaari gripyldpid lrfrarvqvp
      241 vpnsqavmfc vmdvsgsmde grkelakrff illylfltrh yekidivfir hhtqaaevse
      301 dqffhstesg gtvvssalvl ldqiiraryp qgdwnvyvaq asdgdnfpnd sgncrnllvd
      361 rilplvryfa yvqvteveqn lwdeysqllp lfshfamrkv sepgdiypvf rdlfkkegvq
      421 v
//
LOCUS       WP_010459192             164 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Pseudomonas].
ACCESSION   WP_010459192
VERSION     WP_010459192.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..164
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17716
     Region          <41..153
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mssfdtslqd taapdgvcyg cgssnphglh iksfwhadgv hvmaehvpdp mycgwpelvy
       61 ggliamlvdc hsnwtamayh yreenrevas lprincvtgn lgikfikptp mgvpltlrar
      121 vegdvgrktr vicevyagdv ltavgdsvfv rvdtdqlaaa ahsr
//
LOCUS       WP_010459220             144 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Pseudomonas mandelii].
ACCESSION   WP_010459220
VERSION     WP_010459220.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..144
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15569
     Region          7..129
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 msiersykgs cfcgaveftv sgepaamgyc hcescrhwsa gpvnaftlwk pdavqvtrga
       61 dnigtynktp rsyrkwcktc gghlftdhpe mglidvyaav ipdlayspgv hvhyqetvlr
      121 ikdglpklkd vpgesggsgi svee
//
LOCUS       WP_010459228             359 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Acidovorax].
ACCESSION   WP_010459228
VERSION     WP_010459228.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..359
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38180
     Region          <116..350
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mcsavtdqhp ttlppralnl givaasyvlm aavlllvmwr gllpgllcvc lgflltralt
       61 gwfaqglgri qrqptpsats lrvaqvtaag lvmllplall aaglthsrgy lvsapqqyqe
      121 lltymartvl elrlklpadv ashlpegvad iqriianylg akagalamag rawlagvlfa
      181 yvglligala avrppvlarg plaqqlklri tlfgeafrqi vaaqfwiaaf ntlltalfll
      241 fvlplwglql pytpvlitft fvaglvpivg nlvcnvviti vglsvsplaa aaclgflili
      301 hkaeyvinak vvgrrtqmgv wellsvmfva eavfgpaglv aaplfyaylk kelvasrlv
//
LOCUS       WP_010459238             292 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Pseudomonas].
ACCESSION   WP_010459238
VERSION     WP_010459238.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..292
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31892
     Region          <6..291
                     /region_name="bifunc_ST_SDO"
                     /note="bifunctional sulfur transferase/dioxygenase Blh;
                     NF040641"
                     /db_xref="CDD:468609"
ORIGIN      
        1 msvklhvegf fdsatntvsy lvldeathhc alidsvldyd pksghtstts adkliarvke
       61 lnakvdwile thvhadhlta apylkeklgg kigigsqist vqevfgtlfn tgrdmardgs
      121 qfdhlfvnde pfaigtlqch alhtpghtpa cmtyvisdgi etaafvgdtl fmpdygtarc
      181 dfpggnartl fqsinkvlsl pantllymch dyqpggrevq fvstvadqra hnvhvrngis
      241 eeefvamrtk rdaslemptl ilpsvqvnmr aghlpepean gtrylkipln va
//
LOCUS       WP_010459243             334 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Acidovorax radicis].
ACCESSION   WP_010459243
VERSION     WP_010459243.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..334
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36258
     Region          1..334
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkpvvwgvls takigvqhvi pamlssplve lraiasrtlp paqeaarslg iaqaygsyee
       61 lladpaieav ynplpnhlhv pltlqaaaag khvlcekpva lsaaeaetlr tasarvhiee
      121 afmvrhhpqw rrarelvrag rigelravqv ffsyfnddpd nirnqpgigg galydigcya
      181 vlagrylfes eprravslvd rdpqlgtdrl tsalldfgag rqlnftvstq svrfqrvqvv
      241 gtlgrielfi pfnaargeqm hlaldeggll dgssvtvetl paadqyrlqv eafcrrvrdg
      301 aspqaggled avaqarvida lwlsertgrw eaia
//
LOCUS       WP_010459284             484 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TrkH family potassium uptake protein [Pseudomonas].
ACCESSION   WP_010459284
VERSION     WP_010459284.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..484
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52283
     Region          69..481
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mslaairlig filglflitl avsmaipmit lvvyersddl saflwsslit ficglllivr
       61 grpdtgqlrp rdmyllttgs wvvvctfaal pmvfisdisy tdaffetmsg itttgstvlt
      121 gldssspgll iwrsmlhwlg gigfigmava ilpllrvggm rlfqtessdw sekvtprshm
      181 aakyilllyl gltgigtlal wlagmtpfea vnhamslist ggfstsdssl ghwtqpaihw
      241 vavaimilgs lpftlyvatl rgnrrallkd hqvrgfigfl fvtslcvgtw lyfhsdygww
      301 dafrivavnv tsvvtttgva vgdytlwgsf avllffyltf vggcsgstag glkifrfqva
      361 aallvsslkq lihpraviqk kynghpidee ivrslltfsf fftitiaaia lglaligldw
      421 ttalsgaata vcnvgpglgt iigpagnfst lpdaakwllt igmllgrlei ltvlvlvtpv
      481 fwky
//
LOCUS       WP_010459277             300 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010459277
VERSION     WP_010459277.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32081
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 medlkrmavf aavmqhgsms gaaralgmst savsqqvrkl esdggvtllh rstrklalte
       61 agqryharca amcaaadqar aelaasrdap sgelrlsatv gfarhiapal gellaahpal
      121 rlrllvddst idlinaridl avrygrlads twaarrlggm qwflcaspgw vaahgmpqhp
      181 dallshswlg farengglli dlrsptgdpr alrveprias nnqlsiqqmc eaglglalvg
      241 smdshdalqa grlvrllpdw sfgtldiwav tpqrdaqpak vrqaiaalhr ylgqvpgvte
//
LOCUS       WP_010459282             185 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Acidovorax].
ACCESSION   WP_010459282
VERSION     WP_010459282.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..185
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20185
     Region          1..138
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mlnafidrcc rwinlliala lavmvllvfg nvvlryvfns gisvseelsr wlfvwitflg
       61 aivavkehgh lgtdilltrl ppigkricla asyglmlfct wllfsgalaq arinwdveap
      121 vtgasvaify asgvvfavas gllllmhlwr llsgqvpddq lvqvteseev aaiphlhldr
      181 tsgpk
//
LOCUS       WP_010459381             211 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pseudomonas mandelii].
ACCESSION   WP_010459381
VERSION     WP_010459381.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23746
     Region          14..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 metadllers ypgrraelkr difrkalalf neqgleatti emiraecdts vgaiyhhfgn
       61 keglvaalff talddqallr dsylaeaqtt eegvhalvhs yvdwvdsqpd warfqyharf
      121 avtkgpfkee latrnkirnq tlgqwlaepg rrdelrafpa ellpsliigq adsycrawls
      181 grvvaspkay rallaeaawr sicdnsraet q
//
LOCUS       WP_010459455             296 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010459455
VERSION     WP_010459455.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..296
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32803
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..279
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,162,221,238,265)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     215..219,226..227,230)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 miriddlglf irsaalgsft aaaleadllp gqvaaaikrl ereldvrlfa rttrslrlta
       61 egeqylptah svletlkqge enlrgenatl rgvlqvtaps dlgrnillpw ltlfrrqhpe
      121 ltlrfflsdq manlfrdpvd vairygpned anyvalplap wnqrvlvasp eyvqrcgspq
      181 tpddlskhac llylqngrvy dkwnlggqtv qvsgplfsdd advvrrwsle gegiankswl
      241 dvsadvaaer llvllpdypg easplslvcp hrkqispavs qlytwlssqf salers
//
LOCUS       WP_010459456             312 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010459456
VERSION     WP_010459456.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..312
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34496
     Region          17..76
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          106..305
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(121..122,124..125,128,132,134..140,234..239,
                     245..246,248..249)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 meqttdttsq llnrlrmrqv alllaidehr tlhaasqrmg mtqpaatkml heledalgqr
       61 lfdrvgrglq lnaagqavmg tfrgmrgtme alnrelqalr lggagklcig simaaspeql
      121 tdtlirlked ypllsieisv dtsdrlvdqm regaldlvig rmlgpvrdnl lfrpigeepl
      181 sivvatdhpl vgrkrvlfed mlqfpwilqp hgspmrevld qefrdhhagf hsglietssi
      241 ltttnlifkt qmiavipess asryqahgll kilpytishr laaygsivrs drpvgkaaar
      301 flellhapsq eg
//
LOCUS       WP_010459497             410 aa            linear   BCT 01-JAN-2025
DEFINITION  Yip1 family protein [Acidovorax radicis].
ACCESSION   WP_010459497
VERSION     WP_010459497.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Shaik,S., Pandey,H., Thirumalasetti,S.K. and Nakamura,N.
  TITLE     Characteristics and Functions of the Yip1 Domain Family (YIPF),
            Multi-Span Transmembrane Proteins Mainly Localized to the Golgi
            Apparatus
  JOURNAL   Front Cell Dev Biol 7, 130 (2019)
   PUBMED   31417902
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10522553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..410
                     /product="Yip1 family protein"
                     /GO_function="GO:0031267 - small GTPase binding [Evidence
                     IEA]"
                     /GO_process="GO:0016192 - vesicle-mediated transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42269
     Region          8..179
                     /region_name="Yip1"
                     /note="Yip1 domain; pfam04893"
                     /db_xref="CDD:461468"
ORIGIN      
        1 mnlieraksi llqpketwat idtestdvat lftryamvla aipavcgfig msligfggfg
       61 vtirtpfvag lvnmvvsyvl slvgvfvlgl iidalaptfg gqkspiqalk vavyastaam
      121 lggvfsllpa lamlgllaal ysiyllytgl pvlmknipek svvytvvvii aaivmgviig
      181 avsalflprg gamfggadap sitmntpggk vsidtaglea agkkmeeaar kmeeaqksqd
      241 paaiaaaagn aakaaagafg ggqaiaaqsl kgalpeklag lprtgfdvqd gaalglptsq
      301 asaqygndtr qvrleivdig glgqvavmam gmaqgekedk tsaektwqeg grtlhqryek
      361 dgshaefkti lknglvvsie gdnmgakelq gfmsqvdlna leglqrkgks
//
LOCUS       WP_010459500             138 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RidA family protein [Pseudomonas].
ACCESSION   WP_010459500
VERSION     WP_010459500.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..138
                     /product="RidA family protein"
                     /calculated_mol_wt=15317
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mstpthtrir mfntketypn qsldndlcqa vragntvyvr gqvgtdfegr lvglgdpraq
       61 aeqamrnvkq lleeagsdlt hivktttyli dpryrepvyq evgkwlkgvf pistglvvsa
      121 lgqpqwlmei dviavipe
//
LOCUS       WP_010459616             363 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Pseudomonas mandelii].
ACCESSION   WP_010459616
VERSION     WP_010459616.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..363
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38691
     Region          4..338
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,55,97,231,292,312,314..316)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,55,97,99,106,178,181,183,231,238,292,312,
                     314..315)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,99,178,181,183,315)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            183
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msslfdsydl adqvlpnriv mppmtrarve gtvpsedmat yyaqragagl iisesaqvsp
       61 qgrgylytpg ihsaaqiegw krvtdavhqa ggrmflqlwh vgrvshssll dgrspvapva
      121 mpasqtlvha ydsdgkpgqv pvsapvalda egirqviadf rlasanalsa gfdgveihag
      181 ngylfeqfin ggfntredrf ggapianrlr llletvdavs aqigsakvgv rvspfahlad
      241 lhpfdgeeat wlalagalsq rqiaylhash lgtpdfqkdf raaydgtlmv sggftletaq
      301 qaieeglsdl vvfgrpfian pdlvnrlrhg wplaeagrea yygggahgyi dypaysspva
      361 esa
//
LOCUS       WP_010459622             500 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Pseudomonas mandelii].
ACCESSION   WP_010459622
VERSION     WP_010459622.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..500
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53433
     Region          7..484
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(64,66,70,73,77,110,113..114,123..130,135,138,141,
                     234,238,241,244,246,420,422..423,425..426,429,432..433,
                     435,437..440,449,453,455,469,476..481,483..484)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(150..153,161,176,179,209,226..229,232,250..252,284,
                     385,387,413)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(153,250,281,284)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 msdapvighy ldghvqdsgs erfsnvfnpa tgevqarvgl assktvdaav asavkafpaw
       61 seqsslrrsr vmfkfkelld rhhdelaeii srehgkvfsd akgevtrgie iveyacgaps
      121 llktefsdni gggidnwnlr qplgvcagvt pfnfpvmvpl wmiplalvtg ncfilkpser
      181 dpsasllmar llteaglpdg vfnvvqgdkt avdallqhpd ieaisfvgst piaeyihqqa
      241 tsrgkrvqal ggaknhmivm pdadldqaad aligaaygsa gercmaisia vavgdvadql
      301 iakllpridq lkvgngmqgd sdmgplvtae hkakvegfid qgvaqgaqli vdgrgfkvpg
      361 aengffvgat lfdhvttems iyqqeifgpv lgivrvpdfa savalinahe fgngvscfts
      421 dggiarafar tikvgmvgin vpipvpmawh sfggwkrslf gdhhaygeeg irfysryksv
      481 mqrwpdsiak gpefsmptak
//
LOCUS       WP_010459662             210 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010459662
VERSION     WP_010459662.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..210
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23167
     Region          13..176
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mspttarrrl treesraqtr erlidtaqql fvsngyggas irdiadkagy sqgafysnfs
       61 skedvllell rrhmeaeamq lstvmgkdsq qpdqmlaeld awastlnqda dwcmlsielq
      121 lhanrsptfa aeyqkvwdkh rseiggvigr lfeklgrapp aapdelaaaf malshglalq
      181 rttdrlhpsg rmimvflrgl iasansespg
//
LOCUS       WP_010459666             130 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Acidovorax radicis].
ACCESSION   WP_010459666
VERSION     WP_010459666.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..130
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13918
     Region          1..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mhkgsclcgt vryevrgklg aaiychcslc rkatatafat napvaaidfv vikgesalka
       61 fdsspgvhri fcsncgspii srrdampdvv rlrlgtldtp lptpptahyf vaskaewdei
      121 hdglpqfaer
//
LOCUS       WP_010459786             200 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Acidovorax radicis].
ACCESSION   WP_010459786
VERSION     WP_010459786.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..200
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=21173
     Region          4..185
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mktiaiiyhs ahghtahiar qvlegaqgvp girvdllqae dlartpddll rydglilgsp
       61 tylggvsgpf ktfmdatgrl wktqqlknkl aagftvsslp agdkqstlls mfvfgmqhgm
      121 vwvgnpilpe qhagvpydea anrlgswsgl maqaghgaap dafvpgdtkt armfgrhfae
      181 tlqrlggvam aeqpgeqvaa
//
LOCUS       WP_010459770             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Pseudomonas].
ACCESSION   WP_010459770
VERSION     WP_010459770.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..197
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=21722
     Region          47..192
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(82,125)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(87,90..91,95,99,121,123..126)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(117,145)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mlipgkpvkr gactdplrsp lqerellrdl arkaeqelmg vqmasmdelt llpnrhgfta
       61 laqqgmdacq qlglpatllf fdldnfkrin ylygraegdh alktfadvlr iafresdvig
      121 rlgndefval ltgasvvels aikarleeil aernatanrs faihfsigqv efdarlnpta
      181 edvltladka mhdtdhc
//
LOCUS       WP_010459845             469 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Acidovorax radicis].
ACCESSION   WP_010459845
VERSION     WP_010459845.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..469
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=48446
     Region          130..469
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mtapaapplp pnsspaplaa epapeatpat sspgagtphp pappslapta qpappppatp
       61 ettatatgat taqapaqata aptphpdaaa tastpasafl pgplmlhmpv dvrnlslall
      121 alfasvallh wasavfipim lslllttalr pvvevlrrcy vprwlgagvl liaivfglas
      181 aawslsdgaa qlvdslpvaa kkvrdsikar sgasspldtm qkaatqieqa anensaaasp
      241 prrgvqrvvv erppfnirdy lwsgtmglms algqltvvvf ltffalasgn lfrskllria
      301 gtslerrkvt ihvleditnq iqrylmvqvf tsvlvgvatg laywalglen aavwgvvagv
      361 lnlapyigsa lvtgasalva flqfgtldma laiggasmvi htlvgnlltp wltsrtssms
      421 pvavfvsvla wgwlwglwgl llgipvmmav kavcdrvedl kavgellgd
//
LOCUS       WP_010459868             192 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Acidovorax radicis].
ACCESSION   WP_010459868
VERSION     WP_010459868.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..192
                     /product="YceI family protein"
                     /calculated_mol_wt=20855
     Region          29..192
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mrkplfslla vaaatamtag aaqaanyaid pthtfvtfei ghfgattnra rfdkkqgtve
       61 fdraakngkv ditidttsvn sgtppfdkhl qsadlfdaak hptikfvsdk fsfngdkvse
      121 vtgqltllgk tapvtlkatq fncydspmlk revcggdfet tidrtqwgmn ygvewgfpkn
      181 vrlvvqieav kq
//
LOCUS       WP_010459924             318 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Acidovorax radicis].
ACCESSION   WP_010459924
VERSION     WP_010459924.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..318
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33745
     Region          25..251
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(38,42,48,71..72,89..94,216..217)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(41,43,95..96,98..103,155..157,159,161..162,170..171,
                     174,176..177,180,185..191,199,203..206)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 mssnlhpmln vaikaaraag aiinraaldv esvrisqkqi ndfvtevdha sekiiietll
       61 taypghgila eesgteygak dsefvwiidp ldgttnfihg fpvycvsial avkgkveqav
      121 iydpsrndlf tstkgrgayl nerrirvskr tqlkdclvst gfpfrpgdnf ksylnmmsdv
      181 mqrtaglrrp gaaaldlayv aagftdgffe tglsiwdvaa gsllvteagg lvgnftgead
      241 fleqreclag npriygqlvp ilgkyskfas agdkaavrqa aaadapasae aeaaadvesd
      301 ttgaapqadt pksedapf
//
LOCUS       WP_010459939             252 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Pseudomonas mandelii].
ACCESSION   WP_010459939
VERSION     WP_010459939.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..252
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27778
     Region          39..229
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mkpisliess lpgqvwnsar qldnipvint etlvptgara vviaphpgde vvmcggllql
       61 lsslghplql isitdgsash pgsqqwsekr lsvfrgqesv ealrrlglpm hslkwirggf
      121 tdnalakhet qltqfiaryl rpgdvvfttw redgtcdhda vgrasanaas mvgatinelp
      181 vwawhwptrd qglfpwhrar kvrldtwtva rkshathaya sqldgepaig iapllprvil
      241 ermrlpyevv fv
//
LOCUS       WP_010459999             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Pseudomonas].
ACCESSION   WP_010459999
VERSION     WP_010459999.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..161
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=18079
     Region          2..145
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 marlwrygll lsrqrhvaed lvqatcvral eragqfvpgt rmdrwllsil hsiwlnevrs
       61 rrvrqgqglv dadsqlsvdg esiaqthvla aqvirrvdal peaqretvyl ayveglsyre
      121 vaevlqvpig tvmsrlaaar vklaeypplh tvpnpftger r
//
LOCUS       WP_010460037             277 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acidovorax radicis].
ACCESSION   WP_010460037
VERSION     WP_010460037.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..277
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29846
     Region          11..274
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mnptaasthp smttkfieih gveqtfktak glfpalrdin ltiakgefva lighsgcgks
       61 tllnliaglt tptngallca nkeikgpgpe ravvfqnhsl lpwltcfdni ylavervfgg
      121 ketkaqlkar tdtalalvgl tpagqkrpge isggmkqrvg iaralsmepq vllmdepfga
      181 ldaltraklq delleivart qstvvmvthd vdeavllsdk ivmmtngpaa tigevlavnl
      241 arprrrvela edpqyvhyrk avidflytrq ghvekaa
//
LOCUS       WP_010460050             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_010460050
VERSION     WP_010460050.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..254
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28038
     Region          4..252
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mrsivkavsl nkyydqfhal kdvnieveqg evlciigpsg sgkstllrcv nqlekidkgg
       61 lwvdgelvgy rvvgnklhel nesqiarqrl stgmvfqrfn lfphmtvlqn iiegpcqvlk
      121 rspkeaheea vellarvgla dkrnsypiel sggqqqrvai aralamrpkl mlfdeptsal
      181 dpelvgevls vmrdlaqtgm tmivvthelg farevanrmv fmdggqivea gspeeilisp
      241 qnprtqsfis avrt
//
LOCUS       WP_010460103             310 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit alpha/FixB
            family protein [Acidovorax].
ACCESSION   WP_010460103
VERSION     WP_010460103.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..310
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=30850
     Region          2..310
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 msvlviaehd nasikgatln tvtaavacgg dvhvlvaghn agaaaaaagq iagvakviha
       61 dapglehgla envaaqvlai assyshilfp atasgkniap rvaakldvaq isditkviaa
      121 dtferpiyag naiatvqsad svkiitvrtt gfdaaaatgg saavetaaat adagkstfvg
      181 seiaksdrpe ltaakiivsg gralgskekf deimtpladk lgaalgasra avdagyapnd
      241 wqvgqtgkiv apqlyiaagi sgaiqhlagm kdskvivain kdpeapifsv adygleadlf
      301 tavpelvkal
//
LOCUS       WP_010460142             304 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010460142
VERSION     WP_010460142.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31972
     Region          17..74
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          104..284
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(119..120,122..123,126,130,132..138,230..235,
                     241..242,244..245)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mvtaarrttd yrvdpfdlhl fsavvehgti tsaaeavnls laaasarlka leaatgarll
       61 drskagavpt dagrafarha srvlaelesl hvemasfgng lrgtvrllcn taamsealpr
      121 alghflvsnp eldvdvqels sdaaldalrr gtadlgilad yvdtsglvvq pwkddrlval
      181 lprrgpwgsq rslafgellq hplvglsrds glsrflasqa srsgrvprhr vrlggfdaia
      241 hmvaagvgaa vvpesaasrf sdpkktriaa lsdtwarrkl licmtpqgae ltgvsalaea
      301 lass
//
LOCUS       WP_010460162             147 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010460162
VERSION     WP_010460162.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..147
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16586
     Region          1..128
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mddldrrlin rlqlglplvr hpwrvlaael qssstelldr lhtlladgvl trfgpmfdie
       61 rlggaftlaa lavpeerfdd vaeqlnglpe vahnyrreha wnmwfvlgca teegiaetlq
      121 rietltglpl lnlpkeetyh vglyfpv
//
LOCUS       WP_010460193             227 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010460193
VERSION     WP_010460193.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..227
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26109
     Region          17..226
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mvlhrvhhqi lrshhlfepl neeqldelms tshllsidkg eplfrqgepa dsfyfviaga
       61 vkiyrltpdg qekvfevigd rqtfaeamml mdtpnyvasa eaicptqlyr lsnstymrll
      121 qsnsrltfal lgklcvrlhq rvneietlsl knathrvvry lltqlvrqqt vgsqfelpma
      181 kqliaghlsi qpetfsriir rlideniitq dgrqiaildr lrleqfe
//
LOCUS       WP_010460224             142 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ExbD/TolR family protein [Acidovorax].
ACCESSION   WP_010460224
VERSION     WP_010460224.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10021508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..142
                     /product="ExbD/TolR family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=14989
     Region          14..136
                     /region_name="tolR"
                     /note="TolR protein; TIGR02801"
                     /db_xref="CDD:274306"
ORIGIN      
        1 mpamasrgrg rrtineinmv pfidvmlvll iifmvtapml tpgvvdvpsv gkgknmpkvv
       61 aqvivnkdgs lqfktpeatr slnqreigda asrwqkaqga dsasavvisa dkgvqyenvv
      121 kamdalqkag vqrvglsvkq gg
//
LOCUS       WP_010460246             539 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Pseudomonas].
ACCESSION   WP_010460246
VERSION     WP_010460246.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..539
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58205
     Region          1..539
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 maklttaqri vigfaiapla lmgmafyalh dlatlkeqav vivkqdwpki dpimviatgv
       61 rdnarntrdl lidkdnqqvq qsidatkkri tqaldtlepl fylpegktay aalkknreay
      121 vaaftqvqvl irqgafddam aqlkqkvvpa erevygsldq lmalqgkifa dreqsaqaly
      181 sdarrnmlgl flfcvalvia aavivtrsvt rplggepdda arflsqiaqg dltiqvpvns
      241 saggsvmmnm hqmqqslnam vrhiamsvdq vassseelsa vssqtssnlq lqgleieqaa
      301 tavnqmtaav devarnavst seasrqseqt aqrgreqvqe tvvsigalad gvtdtsqrie
      361 qlagrvqdis kvldvirsia eqtnllalna aieaaragda grgfavvade vralahrtqe
      421 stqeieqmig nirldtghav tamqsssnlv ratlevaqrs gdaldeitrs isqinernmm
      481 iasateeqal varevdrnlm girnlseqvl lgaqhthtag hdlaqmagal hqtvarfkv
//
LOCUS       WP_010459882            1633 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD-glutamate dehydrogenase [Pseudomonas].
ACCESSION   WP_010459882
VERSION     WP_010459882.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 1633)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1633
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..1633
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=183522
     Region          5..1612
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mafftaaska dfqhqlqaal aqhiseqalp qvalfaeqff giisldeltq rrlsdlagct
       61 lsawrllerf dhaqpqvrvy npdyerhgwq sthtavevlh hdlpflvdsv rtelnrrgys
      121 ihtlqttvls vrrgskgell eilpkgtqge gilqeslmyl eidrcanaae lnvltkeleq
      181 vlgevrvavt dfepmkdkvq eilsgldnsq yavdpeekae iksflewlvg nhftflgyee
      241 fvvrdevdgg hivydqdsfl gltkllrtgl tyddlriedy avnylreptl lsfakaahps
      301 rvhrpaypdy vsireidadg kvikecrfmg lytssvyges vrvipyirrk veeierrsgf
      361 qpkahlgkel aqvvevlprd dlfqtpvdel fstvmsivqi qernkirvfl rkdpygrfcy
      421 clayvprdiy stevrqkiqq vlmdrlkasd cefwtffses vlarvqlilr vdpknrldid
      481 pvllekevvq acrswqddya slvvesfgea hgtnvladfp kgfpagyrer faahsavvdm
      541 qhllsltekn plvmsfyqpl gqvsgqrelh cklyhadtpl alsdvlpile nlglrvlgef
      601 pyrlrhnsgr efwihdfaft aaegleldiq qlndtlqdaf vhivrgdaen dafnrlvlta
      661 glpwrdvall rayarymkqi rlgfdlgyia stlnnhtdia reltrlfktr fylarkltsd
      721 dledkqqrle haiitaldev qvlnedrilr ryldlikatl rtnfyqtdan gknksyfsfk
      781 fnphqipelp kpvpkfeifv ysprvegvhl rfgnvarggl rwsdreedfr tevlglvkaq
      841 qvknsvivpv gakggflprr lplggsrdei aaegiacyri fisgllditd nlkdgalvpp
      901 anvvrhdddd pylvvaadkg tatfsdiang iaidygfwlg dafasggsag ydhkkmgita
      961 kgawvgvqrh frerginvqe dsitvvgvgd magdvfgngl lmsdklqlva afnhlhifid
     1021 pnpepansfa erqrlfdlpr sawsdydtsi msegggifsr saksiaispq mkerfdiqad
     1081 kltptellna llkapvdllw nggigtyvka steshadvgd kandalrvng nelrckvvge
     1141 ggnlgmtqlg rvefglnggg sntdfidnag gvdcsdhevn ikillnevvq agdmtdkqrn
     1201 qllasmtdev gnlvlgnnyk qtqalslaar ralpriaeyk rlmndlegrg kldraieflp
     1261 aeeainerva aghgltrael svlisyskid lkeallnsqv pdddyltrdm etafppslvs
     1321 kfsqamrrhr lkreivstqi andlvnhmgi tfvqrlkest gmspanvaga yvivrdifhl
     1381 phwfrqiesl dyqvsadvql elmdelmrlg rratrwflra rrneqnaard vahfgphlke
     1441 lglkldells geirdtwqar yqayveagvp ellarmvagt shlytllpii easdvtgqnp
     1501 advakayfav gsalditwyl qqisalpven nwqalareaf rddvdwqqra itisvlqqgd
     1561 gtqdvetrla lwmeehegmi erwramlvei raasgtdyam yavanrelld lalsgqavvp
     1621 apvtaaaele paa
//
LOCUS       WP_010460283             315 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Pseudomonas].
ACCESSION   WP_010460283
VERSION     WP_010460283.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Grant Pearce,F., Hudson,A.O., Loomes,K. and Dobson,R.C.J.
  TITLE     Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and
            Evolution
  JOURNAL   Subcell Biochem 83, 271-289 (2017)
   PUBMED   28271480
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Laber,B., Gomis-Ruth,F.X., Romao,M.J. and Huber,R.
  TITLE     Escherichia coli dihydrodipicolinate synthase. Identification of
            the active site and crystallization
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 691-695 (1992)
   PUBMED   1463470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..315
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0009436 - glyoxylate catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33975
     Region          9..272
                     /region_name="DHDPS-like"
                     /note="Dihydrodipicolinate synthase family; cd00408"
                     /db_xref="CDD:188630"
     Site            order(12,44,47..49,136,164)
                     /site_type="inhibition"
                     /note="inhibitor site"
                     /db_xref="CDD:188630"
     Site            order(44,47..49,136,164,209)
                     /site_type="active"
                     /db_xref="CDD:188630"
     Site            order(48,53..54,82..83,107..108,116,120)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188630"
     Site            164
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188630"
ORIGIN      
        1 msaniftgcm palmtpctae rkpdfdalva kgrelidigm savvycgsmg dwpllteaer
       61 qegvarlvaa gvptivgtga vnsreaisha ahaakvgaqg lmviprvlsr gaspaaqkah
      121 faaileaapn lpsviynspy ygfatraelf felrrehpnl igfkefggaa dlryaaenit
      181 skdddvtlmv gvdtqvvhgf vncnatgait gignalprev lqlvalskqa akgdatarrl
      241 akelesalqv lssfdegcdl vlyykhlmvl ngdkeytlhf netdalsdaq rryaetqytl
      301 frqwyknwsa eqnva
//
LOCUS       WP_010460308             211 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor
            [Pseudomonas].
ACCESSION   WP_010460308
VERSION     WP_010460308.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..211
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22839
     Region          8..203
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 magvtehvvy vvdddqgmld stvwllesvg lkalpftsgv eflsacdatl dacvlldvrm
       61 pgmgglnvqe emrarelnlp iifvsghadv pivvrafkag ahdfiekpyn eqllldsvqq
      121 alsncaanrs gnqghdalqa rlltltprer dvllplvqgy ttreiaeqlg vsaktvdlyr
      181 srvmkrmqas nlpdlvgmai aaglvdplkl r
//
LOCUS       WP_010460291             196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-dependent oxidoreductase [Acidovorax].
ACCESSION   WP_010460291
VERSION     WP_010460291.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..196
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=21107
     Region          6..196
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mtpkcivliq ghpdasaphl chalaqayaq gaiaaghevr eievaaidfa llrsqhewel
       61 gllpavlkpa qadigwaqhi vlffplwlgd mpallkgfle qvarpgfafn tegsnpfgrk
      121 gltgrsarvv vtmgmpalvy rwyfrahsvk slernilgfv giapvhetlv gsveqlgddg
      181 vakwkarmra lgakaa
//
LOCUS       WP_010460322             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Acidovorax].
ACCESSION   WP_010460322
VERSION     WP_010460322.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..145
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15553
     Region          1..134
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 meldkkdrqi lmalqhdarq slsalgkqig lsqpamserv kkledagvia gyaarinlaa
       61 vglglqavvr vrtthehipr yvqlfqslpe vldavrvtge dcfvvrcafg qpadlervvd
      121 alaafgsvst slvlshpvnk avpld
//
LOCUS       WP_010460325             195 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Acidovorax radicis].
ACCESSION   WP_010460325
VERSION     WP_010460325.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..195
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21090
     Region          11..185
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mppqgnhthp gktqfygass ldgflatpdh dlgwllqfge iegssypafi rdvgalamgs
       61 htyewmlrha idagqpwpya qptwvfssrt qraipgadvr fvqgdvrpvh qamvqaaagr
      121 nvwivgggel vgrfydagll delivqiapv tlgagkpllp rriaqpalrm qsvatlgglf
      181 aelryevppa pqrnp
//
LOCUS       WP_010460326             212 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010460326
VERSION     WP_010460326.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23011
     Region          22..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrttnsrstr dfsptsgpap gtepaadvrs rildtasrlf yergvravgv dlvvleaava
       61 ktslyryfpt kddlivafle redvefwdqw dsvaaqfadd pageleahmr wigerlarsn
      121 yrgcpqinva aefaeqdhpa rhvarrhmqa lrgrlhevav rlkaphpeql aaqlavvvng
      181 afvsagllsa eeatgvlvaa vqalqagars pg
//
LOCUS       WP_010460377             759 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Pseudomonas mandelii].
ACCESSION   WP_010460377
VERSION     WP_010460377.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..759
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=84681
     Region          175..757
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msysiavral ceftakvgdl dlrftpspta legivghrtv asrrsegyqs evaleglyrt
       61 lkvkgradgy dpaqncleev ktyrgdlskq panhrqlhwa qakvygwlmc qklelaqinl
      121 alvyfdivse ketclveafs agelqsffeh hcglfllwae qemahrearn haaqklafph
      181 adfrpgqrhl aesvfkavst grclmaqapt gigktvgtlf pmlkalapqq ldkvffltak
      241 tpgrklalda aqvilesada pplrvlemia rdkacehpdk achgescpla qgfydrlpaa
      301 rqaaselsll nqdalrrvas ahevcpyyls qemarwadvv vadynyyfdf sallfglsqa
      361 nnwkvavlvd eahnlvergr qmysatldqs tlsgvrktap dalkkplqrv nrewnalhnl
      421 qlapyqaydk apekllqals scsasigdyl ndhpqgldsa lqsfyfdmlq fcrvaelfde
      481 qflfdiskrd lerkqnlsql clrnvvpagf irprltaars tvlfsatlsp rhyyadllgt
      541 ppdtvwidve spfhadqlkv hivsqistrf vhrqaslepi veliarqfsq rpgnylaffs
      601 sfdylqqvaq llaerhpqis lwsqsrgmae gqrqafldqf tvhsqgvgfa vlggafgegi
      661 dlpgarliga fiatlglaql npvneqmkhr maaifgagyd ytylypgvqk vvqaagrvir
      721 tqqdqgvvml iddrfgdskv khllprwwsv eqahlasga
//
LOCUS       WP_010460387             155 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010460387
VERSION     WP_010460387.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..155
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16816
     Region          1..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkldtldlri laelqadgsl snvelarrvh lspspclarv kaleaagvis ryvalanaaa
       61 lglglnvfis islktqskea ladferriae hdevmecylm sgdsdylirv aladigaler
      121 fileqlapip gvekirssfa lkqvryktal plpra
//
LOCUS       WP_010460434            1060 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudomonas mandelii].
ACCESSION   WP_010460434
VERSION     WP_010460434.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12011349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..1060
                     /product="efflux RND transporter permease subunit"
                     /calculated_mol_wt=114906
     Region          3..1039
                     /region_name="ACR_tran"
                     /note="AcrB/AcrD/AcrF family; pfam00873"
                     /db_xref="CDD:395701"
ORIGIN      
        1 mnfsqffisr pifaavlsll iliagaislf qlpiseypev vpptvvvran fpganpkvig
       61 etvaapleqa itgvenmlym ssqstadgki tltitfalgt dldnaqvqvq nrvtrtepkl
      121 peevtrigit vdkaspdltm vvhltspdkr ydmlylsnya llnikdelar lggvgdvqlf
      181 gmgdyslrvw ldpnktasrn ltatdvvtai reqnrqvaag algappapna tafqlsvntq
      241 grlvseeefe niiirsgdng eitrlkdiar velgssqyal rsllnnqpav aipifqrpgs
      301 naieisnevr dkmaelkknf pegmdfsivy dptifvrgsi eavvhtlfea lilvvlvvil
      361 flqtwrasii plvavpvsli gtfavmhlfg fslnalslfg lvlaigivvd daivvvenve
      421 rhielgetpv eatkkamrev tgpiiatalv lcavfipaaf isgltgqfyk qfaltiaist
      481 visafnsltl spalaavllk shhapkdrft kvldkllggw lfrpfnrffe rashgyvgtv
      541 arvirssgia lllyaglmvl tffgfahtpt gfvpgqdkqy lvafaqlpda ssldrtedvi
      601 krmsdlalkq pgvesavafp glsingftns pnagivfvtl kpfderkdps msagaiagal
      661 ngqfagiqea ymaifppppv qglgtiggfr lqiedrgnlg ydelyketmn iitkshnvpe
      721 laalftsytv nvpqvdaaid rekakthgva vsdifdtlqi ylgslyandf nrfgrtyqvn
      781 vqaeqqfrle pdqigqlkvr nnkgemipla tfikvsdtsg pdrvmhyngf itaeingaaa
      841 pgyssgqaqa aiekllkeel pngmtyewtd ltyqqilsgn talfvfplcv llaflvlaaq
      901 yeswslplav ilivpmtlls aiigviasgg dnniftqigl ivlvglackn ailivefakd
      961 kqqdeglspl aavleacrlr lrpilmtsfa fimgvvplvf ssgagaemrh amgvavfsgm
     1021 lgvtffglll tpvfyvlirn fvergekrka akvlkleaqq
//
LOCUS       WP_010460453             119 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator [Pseudomonas].
ACCESSION   WP_010460453
VERSION     WP_010460453.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..119
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=13160
     Region          1..119
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 msstpstilv vedddivrml ivdvleeldy kvleadgskk aleflndedq hidlmmtdvg
       61 lpdmdgrela kqarmlrhel pilfasgyae sielpagmqv igkpfsidkl rdkvkgmla
//
LOCUS       WP_010460460             301 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas mandelii].
ACCESSION   WP_010460460
VERSION     WP_010460460.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401161
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34622
     Region          22..103
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
     Region          <100..288
                     /region_name="PRK13503"
                     /note="HTH-type transcriptional activator RhaS"
                     /db_xref="CDD:184094"
     Region          205..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtrtarvtdl syelmddhng lsiiyrqhgf pcplvrwhfh keyelhliva ssgkvfigdy
       61 ignfypetlf ltgpnlphnw isqvaedevv pkrdmlvnft delfesghqv faelktlapl
      121 leraqygief rckrtirqam tlmqriadtk gvtrlghffi llellaasdd fqllsgattp
      181 qladehnidr tnravdyifa hyardlplee vaehlgmkpt yfsrvfkqat grcfiefvnr
      241 lriskscell adgdkpvtdv cfesgfnnis nfnrrfqqlk gmtpshyrrl avqrlteqnl
      301 a
//
LOCUS       WP_010460558            1060 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit [Acidovorax].
ACCESSION   WP_010460558
VERSION     WP_010460558.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..1060
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115998
     Region          11..1051
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mtqvqpkegf nlskwaldhp altrylmvvl mllgfaayfq lgqdedppft framvvrtyw
       61 pgataqqvae qvtdkiertl qevpyadkir syskpgesqi ifqikdsskg sevanvwysv
      121 rkkvgdmryt lpqgiqgpff nddfgdvygv iyalesegfs yaelkqfadd arqqllrvpd
      181 vakvelfgvq deklfieisq krlsqlgldm nqvlaqlgqq navesagaiq tpqdqvqvrv
      241 egqfnaiedl rampirgpsg aqlrlgdiae vkrgyvdpat vkvrhqgqev ialgvsmakg
      301 gdiialgkal haatdrigst lpagvklvnv qdqpkavats vnefvkvlie avvivlavsf
      361 ialgfhkrpg knplwkrwyi dprpglvvgi tiplvlavtf lamwywgigl hkislgslii
      421 algllvddai iavemmvlkl eegydkvraa tfayeitamp mltgtlitaa gflpiglaks
      481 ttgeytfaif avtvialvls wivsvyfvpy lgtlllkvpp hvvaaqankg itddphevfd
      541 spfyrvfrrl vnwcvlhrwl tigatvltfa lgivgmgqvq qqffpdssrp eimvdiwfpe
      601 gtsfagneev tkrveqrlls epgvntvstw vgsgvprfyl pldqvfpqsn vsqfivvpkd
      661 lkvreslrvk lpallaeefp evrgrvkllp ngppvpypvq frvvgpdplv lreradevka
      721 qlrqnpnmrg vndnwnesvk vlrlevdqak aralgvtsqs iaqasktils gtqvgqfreg
      781 dklidillrq pldernaitd ianaylptas gksipltqia kpvftwepgv mwrenrdyai
      841 tvqgdvtegl qgatvtaall palkdieakw raagqtgyri dvagaveess kgsasiaagi
      901 pimlfitftl lmlqlhsfsr amlvfltgpl glagvaaali llnrpfgfva llgvialmgm
      961 iqrnsvilid qieqdrargv pawdaivesa vrrlrpivlt aaaavlamip lsrsvfwgpm
     1021 avaimgglvv atvltllalp amyaawfrvk rpapevlggv
//
LOCUS       WP_010460646             147 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Acidovorax].
ACCESSION   WP_010460646
VERSION     WP_010460646.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..147
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15444
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykriliatd gsplsdkave hglslaaltg asavalkvvp ryprsyfegg mpvdtndvkr
       61 iesqwgdaaq amvdgvkaqg gaqgvtvkav iaksdlvaea iisaakkhkc dlivmashgr
      121 kglkrlllgs etqhvlthsh ipvlvlr
//
LOCUS       WP_010460659             333 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Pseudomonas].
ACCESSION   WP_010460659
VERSION     WP_010460659.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..333
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36957
     Region          16..55
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          75..319
                     /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"
ORIGIN      
        1 mtdnslsqae ydaitdaaah wcmrlhavdc taeeriafeh wrdvhplhaf eyeamleiwe
       61 vagdlprpea vtsvarfkqa apwrtvgiaa avcalalpla aysgwnmgwl pnsyqhfeas
      121 dtvrqvtlsd gsqvelnlgs elifsnykdq rrvtlekgea ffsvshdlah pfvvraadgr
      181 irvtgtkfnv wmyedqvrvn liegsvlvss nddlpgdglr lgpamqaryk hgdftpqinq
      241 typndnslaw rsgklviddl alndalplin rylskpvmva dhstgtirlg giynikelnn
      301 lvaslpkvlp vyltrnkegn pvlnsipqqt pks
//
LOCUS       WP_010460689             300 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Acidovorax radicis].
ACCESSION   WP_010460689
VERSION     WP_010460689.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..300
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32422
     Region          50..295
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mkptpvrril wviaillllg llmaglaraq pvhikddrgr evslprppqr ivsllpslte
       61 svceleqchr lvgvdrysnw peavigklpk vgggidpsie aivalkpdlv lmsvssrasd
      121 rlealgltvv qlepkthadv rrvlgtvsdl lgvpraqgsd rlwrvidagv laaaqslppk
      181 aknarvyfev srgpyaagea sfigesltrl gvrnvvpasl gpfprlnpef vvranpdiim
      241 ignrsmqamv pypgwatmra irdnrlcvfg pgdsdvvvrp gprmaeaari marclvdkap
//
LOCUS       WP_010460744             211 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Acidovorax].
ACCESSION   WP_010460744
VERSION     WP_010460744.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22314
     Region          14..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 masritpsps avpaeastdr rqdilnaala caaeggvdav sidgvrarcg asvgsiyhhf
       61 gnrdgivaal ffdifhdqsr svqaqldaaq gveagvqalv tgyldwvvaq perarflfqa
      121 rgavaagqrt pdlaeaarrr nqalvawfep hrqsgalrdl pcelmpslvm gpvqsycraw
      181 lsersglggg lpspttyrae ladaawravt a
//
LOCUS       WP_010460730             297 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Acidovorax radicis].
ACCESSION   WP_010460730
VERSION     WP_010460730.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..297
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31943
     Region          8..292
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 manriresrp asfwllaivf slfvlfmygp mfvifilsfq gpeggltfpm rgvslhwfyk
       61 laeglgvvdi gaalwrslgl gvavmlctvv lsvlaglafr krlaggntlf fivvaslimp
      121 siivslgigl efrlidngik aalewlgmes tlegygtslg lftsalgahl twtlpfglli
      181 mfavfnrfnp ayeeaardlg atpwqgfshv vlpliapsvv gigmfgftls wdeiartsqa
      241 igdvntlple lqgltstvtt psiyalgtlt tvvsfivmgi tlalvwalgr rrkgrsg
//
LOCUS       WP_010460764             210 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Pseudomonas].
ACCESSION   WP_010460764
VERSION     WP_010460764.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..210
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23068
     Region          1..195
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mnalrriweh feegfivfll aamtlvtfvy vvlnnlytlf yslaeswesa seslfaigdg
       61 vmgmaqamtw stsltkalfg wliffglsyg vrtaghigvd alvklaskpv qrfigiiacl
      121 fcltyaglls iasfgwiqtl mvaqigaedl gqygimqwhi glivpvgfal vfirfaeilv
      181 rilqnrqtgl gladeaadal klteheddks
//
LOCUS       WP_010460775             153 aa            linear   BCT 01-JAN-2025
DEFINITION  group III truncated hemoglobin [Acidovorax radicis].
ACCESSION   WP_010460775
VERSION     WP_010460775.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..153
                     /product="group III truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16658
     Region          20..129
                     /region_name="TrHb3_P"
                     /note="Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 3 (P); cd08916"
                     /db_xref="CDD:381257"
     Site            order(30,43,46..47,54,57..58,61..62,72,74..76,79..80,83,
                     86,90..91,94,118,121..122,125)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381257"
ORIGIN      
        1 mnlqttspeg lgahappsve sitrlvhgfy gdvrqdpllg pvfekalhgq wdthlqrlvd
       61 fwstvalgtr sfkgdvfgkh malegvtpah faawvglwqq htsrlfapev ardlqvaahg
      121 iarnlfrgyf gtdpafvppl sednghgpqp rdg
//
LOCUS       WP_010460776             126 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor
            [Pseudomonas].
ACCESSION   WP_010460776
VERSION     WP_010460776.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..126
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13998
     Region          6..>120
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 msnipiisiv ddddtlrmsl dslvrsmgyv trtyacaeec ladyaldsts cmisdirmpg
       61 mnglqmleql lardmrfpvi fitacigetp evkarelgav gyfkkpfdse qlmrrvqhvl
      121 sgrpae
//
LOCUS       WP_010460820             629 aa            linear   BCT 01-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Pseudomonas mandelii].
ACCESSION   WP_010460820
VERSION     WP_010460820.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..629
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=69682
     Region          8..624
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mkpalinaha qqvlqavqgt hathgpiadl aitrswrrcl dqyqldpasr rapnvvehpr
       61 lqdhrapleh iiavahwqms nlhqqlgrdg hvvlltdarg vaidsvfnds eraelqrsgl
      121 wlgsvwsedc egtngvgtcl verqhvtirr dqhfrgkhag ltcsaspifd asgellavln
      181 lssvreeqgl qqhfkamalt nltahliesc yflghdpqry llrfhpesgy vgllgeglls
      241 fdesacicsv nhaalellgl sreqvvgqsl tmlletpldq vmsqassqps vcwpmrlldg
      301 rqlygqlrep lrrvpsgtpa ipkiddgqvc ledprlqrgf aralrvlerd vpvflqgetg
      361 tgkeafsaal hrassrvsqp fiaincaaip etlieselfg yhggsftgar kdgmigkleq
      421 ahggilflde iadmplalqt rllrvleerq vvplggatar pldirlisas hqdlntcvve
      481 grfredlfyr iagfsvqlpp lrersdkgrl ldlllreetk darirleagv rerllthpwp
      541 gnvrqlrtcl rtlialsmeg rvtledlael lpavpavlae nplgvserqt lltlieaehw
      601 hiahvaarlg isrntlyrkl rqhgisrpg
//
LOCUS       WP_010460876             310 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Pseudomonas mandelii].
ACCESSION   WP_010460876
VERSION     WP_010460876.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..310
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33659
     Region          13..307
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(38..39,42,97,111,113,145,179,267,270,306)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(237,242,257,267..269,272,294,298)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mntintlgpn tprialigec mielqqradg tlqqsfggdt lntavylsre lgtrgivdyv
       61 talgddsfsd amcqtwadeh iglgmvqrlp grlpglyciq tdaagerrfl ywrneaavrd
      121 cfttpaaapi laalpdydvl yfsgitlavl gvqgrvklle tliearqrda rivfdnnyrp
      181 rlwasveear aayrsvlpyv dlalltvdde qalfhfsdge avfaayeqig tpevvlkrga
      241 eaclircdge lfevpaqkve rvvdttaagd sfsaaylasr lkggsaveaa eaghrlasrv
      301 iqvpgalipr
//
LOCUS       WP_010460883             129 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RidA family protein [Pseudomonas].
ACCESSION   WP_010460883
VERSION     WP_010460883.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..129
                     /product="RidA family protein"
                     /calculated_mol_wt=13905
     Region          1..127
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msitrygtgs taaggqprpf araveadgwl hvsgqvpavd geiitggive qthqamknli
       61 aileeagygl edvvragvwl edprdftsfn kvfseyfkse haparacvqa nmmvdckvei
      121 dciaykkka
//
LOCUS       WP_010460940             104 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SCP2 sterol-binding domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010460940
VERSION     WP_010460940.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Burgardt,N.I., Gianotti,A.R., Ferreyra,R.G. and Ermacora,M.R.
  TITLE     A structural appraisal of sterol carrier protein 2
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (5), 565-577 (2017)
   PUBMED   28284963
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Dyer,D.H., Wessely,V., Forest,K.T. and Lan,Q.
  TITLE     Three-dimensional structure/function analysis of SCP-2-like2
            reveals differences among SCP-2 family members
  JOURNAL   J Lipid Res 49 (3), 644-653 (2008)
   PUBMED   18084051
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Bun-ya,M., Muro,Y., Niki,T., Kondo,J. and Kamiryo,T.
  TITLE     New aspects of sterol carrier protein 2 (nonspecific lipid-transfer
            protein) in fusion proteins and in peroxisomes
  JOURNAL   Cell Biochem Biophys 32 Spring, 107-116 (2000)
   PUBMED   11330036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007129
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..104
                     /product="SCP2 sterol-binding domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=10847
     Region          5..104
                     /region_name="SCP2"
                     /note="Putative sterol carrier protein, contains SCP2
                     domain [Lipid transport and metabolism]; COG3255"
                     /db_xref="CDD:442486"
ORIGIN      
        1 mtsvadavqa mkakfnpaaa agldlvfgfr iddtqnfslv vkdgacelqe genpdaqvtl
       61 vmdgetlqgi vdgstdgmqa fmggklraeg dmmlamklse lfps
//
LOCUS       WP_010460994             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF799 domain-containing protein [Pseudomonas].
ACCESSION   WP_010460994
VERSION     WP_010460994.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..219
                     /product="DUF799 domain-containing protein"
                     /calculated_mol_wt=22646
     Region          2..219
                     /region_name="COG4380"
                     /note="Uncharacterized conserved protein, DUF799 domain
                     [Function unknown]"
                     /db_xref="CDD:443506"
ORIGIN      
        1 miarslklma gllalavlgg cvspktvdys aykqarpkti lvlpplnnsp dvkasysmls
       61 qvtyplaeag yyvlpitlvd etfrqngltt padihqapan klqeifgada alyitvtdyg
      121 trymiisset vvtataklvd lksgttlwtg sarasseegg nngggglvgm litaavkqvi
      181 nsatdaghpi agvasarlls agqpagllyg prspkygtd
//
LOCUS       WP_010460941             488 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Acidovorax radicis].
ACCESSION   WP_010460941
VERSION     WP_010460941.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..488
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52700
     Region          86..466
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mntlqcpvap gsrplhrplr lsllgaavvl agcasvspdg lrsdvaalta grtagieaal
       61 pathtgareq aqqsvdgwla qpltqdaavr iallnnpglq arlaalgvad aervqaitlp
      121 nphlalgrft nghereiert lafslldlit lpwrtarqae rlqiatlqaa qdvvslaadt
      181 rrawvravaa eqvaathdrm veaaeagael arrmvqvgnw srlqqareqa vlqeatrqra
      241 rarlaaater eqlnrrmgvw glqtqyqlan qlpplpttal padgieatal rerldvqaar
      301 rqldtlatrq gwsragamfg diglaysrnt tterdsghre itrgwelelp lplfdwggaa
      361 rtrahseveq saaqlqdtav rarsevraaw ltyrtaldla rqqqaevvpl rqlisdettl
      421 ryngmlasvw dmlaearnst qavanaieaq rdfwlaetdl qlaltgtspg alqgltsgaa
      481 asstpqgh
//
LOCUS       WP_010460995             286 aa            linear   BCT 01-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Acidovorax radicis].
ACCESSION   WP_010460995
VERSION     WP_010460995.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..286
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31020
     Region          66..283
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mklmsysiag retwgvvvdd gvaelaartg hatladfias pdfarrdalv aglgadakla
       61 dvvylpvipr pekivcavrn ymdhhqevla agmhrelseq ppiflrvwrs qtphqgpivr
      121 phvsesldwe gelaviigke grdisevdaw ahiagyscyn dasvrewqfh akqiasgknf
      181 estgafgpwm vtadeiapgr elkletrlng avvqsshtgh mifsiprlia yastiftlvp
      241 gdviitgtpa gvgwskkppq fmkpgdvvev eieaigllrn pvvaqa
//
LOCUS       WP_010459637             134 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TraR/DksA family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010459637
VERSION     WP_010459637.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 134)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 134)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 134)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..134
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15456
     Region          15..130
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mtkdkllamp addymnaeqh affyellqnm kvetherieq nriaiesldt padpadaasv
       61 eeertwlvna idrdqrmlpq leqalerike dsfgwcddsg eaiglkrlli spttkyciea
      121 qerheqidkh qrqa
//
LOCUS       WP_010461012             306 aa            linear   BCT 01-JAN-2025
DEFINITION  SPFH domain-containing protein [Acidovorax radicis].
ACCESSION   WP_010461012
VERSION     WP_010461012.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..306
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33250
     Region          3..294
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 meiavvilii avifvarsvk vvpqqnawvk erlgkyagtl tpglnflvpf vdkvaykhsl
       61 keipldvpsq vcitrdntql qvdgilyfqv tdpmrasygs snyivavtql aqtslrsvig
      121 kleldktfee rdiinaqvvq aideaalnwg vkvlryeikd ltppkeilha mqaqitaere
      181 kraliaaseg rrqeqiniat gereafiars egekqavink aqgeaesika vaeanaqaie
      241 rvaaairqpg geqavqlkva ekaveaysqv aadstttliv psnmtevsal igsamkmvqt
      301 tgtprn
//
LOCUS       WP_010461019             186 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fasciclin domain-containing protein [Acidovorax].
ACCESSION   WP_010461019
VERSION     WP_010461019.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Clout,N.J., Tisi,D. and Hohenester,E.
  TITLE     Novel fold revealed by the structure of a FAS1 domain pair from the
            insect cell adhesion molecule fasciclin I
  JOURNAL   Structure 11 (2), 197-203 (2003)
   PUBMED   12575939
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..186
                     /product="fasciclin domain-containing protein"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=18728
     Region          31..185
                     /region_name="FAS1"
                     /note="Uncaracterized surface protein containing fasciclin
                     (FAS1) repeats [General function prediction only];
                     COG2335"
                     /db_xref="CDD:441906"
ORIGIN      
        1 mthrfntrma tialaaamaa aavpamaqvm vggapmlask diidnavnsk dhttlvaavk
       61 aaglvetlkg tgpftvfapt naafaalpag tvdtllkpen kptltkvlty hvvagkydaa
      121 alskmiadgk gmasfktvag gtltakasgs simvsdekgg masvtiadvy qsngvihvvd
      181 kvllpn
//
LOCUS       WP_010461103             394 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Acidovorax radicis].
ACCESSION   WP_010461103
VERSION     WP_010461103.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..394
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41688
     Region          5..280
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msserklrya mvggghgafi gavhrkamal dgqfelvaga lsssperara sgaelgladd
       61 rnhgswqdll adelrrspde ridlvsivtp nhvhhpvala fvqagfhvvc dkplvhtsaq
      121 adelvaavkk agtvfgvtyn ytgypmvrea rhlvhsgalg tlrkvtveyn qgwlataveq
      181 ggsnkqadwr ldparsgavg tmgdigshae nlaatvtgqr pealcadltt fgagrqlddd
      241 aqlllryagg argvivasqv aaglendvrl qvsgtlgtlv wrqedpnhlv hspvdgprri
      301 ltrgspwlse salragripa ghpeafieaf anvylgvaad iraraagrta saleadyprv
      361 edgaegvrfi ekvvesagse rkwtalanga gpki
//
LOCUS       WP_010461148             210 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Acidovorax radicis].
ACCESSION   WP_010461148
VERSION     WP_010461148.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21633
     Region          1..193
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtiatllvfa lvalvaiatp gptvllalan gsrygmrrsl pgmlgavasd lvlvgavalg
       61 lgallaasef wfsvvkwlga aylawlglrl lrsqggldia aaggaasgpl atprsifars
      121 flvavtnpkg ylfcsallpq fidsgapqwp qyaaiaavfa sldfavmlay aligaravkl
      181 lrrravlwld rccggallal agslaiykrt
//
LOCUS       WP_010461196             288 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TlpA disulfide reductase family protein
            [Pseudomonas].
ACCESSION   WP_010461196
VERSION     WP_010461196.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..288
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31170
     Region          27..>119
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
     Region          133..263
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mltftlgtfa ialnhlllis alalatfvgw rvakrggenp esalfslfll gmlaarvgfv
       61 gvywahyrnd pwqiidlrdg gflawpgviv llltalyrgw rrpglrrplg fgvasglafw
      121 llatfslsiy eqgtrlpeia lrnaagetvq ladykggplv inlwatwcpp crrempvlen
      181 aqqqrpdltf lfvnqaesmq svstfletqg lsltnvlfdg sgrlgqavgs malpttlfys
      241 pdgrllgshl gelsdaslar alenfdtpsp avpatssrkl pcpasatc
//
LOCUS       WP_010461210             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010461210
VERSION     WP_010461210.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22813
     Region          29..75
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          94..204
                     /region_name="TetR_C_24"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17932"
                     /db_xref="CDD:465574"
ORIGIN      
        1 mdeqkalgvm relvdsgqlt dpdsargkll qvaahlfrnk gyerttvrdl agavgiqsgs
       61 ifhhfkskde ilravmeeti ryntalmhaa laeagnvrer vlalircelq simggsgeam
      121 avlvyewrsl sedgqaqvla lrdiyealwl qvlgeakdag firgdvfitr rfltgalswt
      181 ttwfraggsm sldqladeal ilvleek
//
LOCUS       WP_010461260             402 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ammonium transporter [Pseudomonas].
ACCESSION   WP_010461260
VERSION     WP_010461260.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..402
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42201
     Region          7..398
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 menlqsavds lvhssntlfi ligavmvlam hagfaflevg tvrqknqvna lskilsdfai
       61 stlayffigy wisygvtfmq paavinadhg yglvkfffll tfaaaipaii sggiaerarf
      121 vpqlcatali vafiypffeg miwngnfglq awlleqfgas fhdfagsvvv hamggwlala
      181 avlllgprqg ryregrlvaf apssipflal gswilivgwf gfnvmsaqtl qgvsglvavn
      241 slmamvggtv aalivgrndp gflhngplag lvaicagsdl mhpvgalvtg viagtlfvwc
      301 ftaaqvkwri ddvlgvwplh glcgvwggla cgifgqsalg glggvslisq ligtslgviv
      361 allggfvvyg gikalhglrl sqeeeyygad lsvhkigavs qd
//
LOCUS       WP_010461319             277 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acidovorax radicis].
ACCESSION   WP_010461319
VERSION     WP_010461319.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..277
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30372
     Region          1..255
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mahagtlair glnkqyevkg ealpvlqdih ltiepgefvs ivgssgcgks tllrlvigle
       61 gdyqgeillg gqrivgtsln rgivfqehrl fpwltveknv algllnsslt egqqratvre
      121 hielvglqgf etayphqlsg gmsqrvaiar alvnrpdill ldepfgalda mtrahlqqel
      181 hriwqqegit milvthdvee avylgnkvvv meprpgrirr ivpvdlphpr ertsfaftta
      241 kdgvlkefsa hpaadlaepp lkrgeqiapa sqwqfav
//
LOCUS       WP_010461382             350 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Acidovorax].
ACCESSION   WP_010461382
VERSION     WP_010461382.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..350
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36065
     Region          18..311
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msderntpsp faalmrhrla wpiitlllll avntafnasf lhiewrdghl ygslidilnr
       61 aaplvlvslg mtmviatrgi disvgavvai aaavaawmig gsvsgtesrf plpvailgal
      121 gvallcglwn gvlvarvgmq piiatlilmv agrgiaqlit dgqiitiyyt pyffigggyl
      181 aglpfslfiv aavfavlyla vtrtalglfv qavginptaa rvagvqagrl tvaayvfcgv
      241 cagiagllis snvksadgnn agqlleldai lavtlggtal tggrfslvgs vigaliiqtl
      301 tyaiyslgvp pevnlvvkav vvfivmllqs pefraqigai arrpgagavs
//
LOCUS       WP_010461397             178 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Pseudomonas
            mandelii].
ACCESSION   WP_010461397
VERSION     WP_010461397.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..178
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /note="This protein belongs to a clade of uncharacterized
                     proteins related to peroxidases such as the
                     alkylhydroperoxidase AhpD."
                     /calculated_mol_wt=19522
     Region          40..173
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msrveipsre ntppethetl daiakrfgff pnlyrltais pktlaalvgi qtplmkaldl
       61 ktrerialvv sevngcpycv aahtfvalnl akdspeeitl arkgqstdsk irviiqfaak
      121 vaemrghvse deiacvreag ysdaeiievi glviqfsltn yinnvfdtdi dfptdtlv
//
LOCUS       WP_010461393             178 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Pseudomonas
            mandelii].
ACCESSION   WP_010461393
VERSION     WP_010461393.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..178
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18996
     Region          40..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 marittptrd qapasthatl daigsqvgfi pnmfrmlass pdtfagiigf qaamskslnv
       61 ktrdaialav tqvndchycm kahtyiatnl vkssaeeial nrqgrsedpk raaaatfakn
      121 lverrgkvtd qelaavragg ytdpeiidit alavqflltn fmnnmadsdi dfpsvtaa
//
LOCUS       WP_010461468             357 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Acidovorax radicis].
ACCESSION   WP_010461468
VERSION     WP_010461468.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..357
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38144
     Region          3..333
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,225,287,307,309..311)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,173,176,178,225,232,287,307,
                     309..310)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,173,176,178,310)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mnplftpiri grlvapnrvl mapmtrsras ddgvvgditv tyyaqrasag liitegvfps
       61 algkgyvntp gvetqaqvva wknvteavha rggrifmqlm hcgrvshpsl lhgqtpvaps
      121 aiqpegqawt pagqvdfvtp ralgleeiag viddyrqatr raldagfdgv elhaasgylp
      181 eqflssgsnq rtdlyggsve nrarfvlevl damtaeagad rvgikispem nynsitdaap
      241 qetytylvgq lrdrglaylh valfgnpavd yhavlrplfs gtylmgsglt kgsaekllqd
      301 kqadaavfga pflanpdlpe rfrvgaalna pdrntffapp takgyidypa lvpaead
//
LOCUS       WP_010461491             571 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudomonas mandelii].
ACCESSION   WP_010461491
VERSION     WP_010461491.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..571
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=62166
     Region          47..568
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 msiqrlftii faaiiisamt lslvvmamin nqqnlsdsee nryksyllad elrqssddls
       61 rmartfavtg enryaqlyqq ilsirngeeh rptnynypym dflatgqqve tgfdpampll
      121 elmrqqgisq tefaklkeae rasnelarie seaietasga kgkvpdlnas thlvyspryd
      181 aekarimasv keffislnqr tqqevndlrf tnsvymsvvc amvlllivia gigiiairrk
      241 vsgallrlsn daqrvaegdl stnldtqngg efgvlshafg kmviklrdvv tnvvnsssql
      301 gvsaeqltnt trttlenmrq qelhtsevat aitemaatvq evahhsaqta eaaqkadtsa
      361 tngravveqm vntiqqlydd igkaaeviqi latdtssigg ildvirsiad qtnllalnaa
      421 ieaarageqg rgfavvadev rnlakrtqds tqeiqdmimr lqegakqavc vmdqsriqae
      481 agsrqadnag haleditkan rvisdmavqi asaaeeqavv ahdisqrieq irelashnat
      541 gsdqvssase gvarlaqgln aqvshfnlvr t
//
LOCUS       WP_010461499             383 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Acidovorax radicis].
ACCESSION   WP_010461499
VERSION     WP_010461499.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..383
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=38476
     Region          <297..380
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          297..323
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(298..299,302..304,306..307,311,314,323,325,327,
                     331..332,335..337,339..340,344,347,356,358,360,364..365,
                     368..370,372..373,377)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          325..356
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msapdddlvr ryreasaqed arpgaqvrea vrahaqmlaa aaamapspta aapsrtaanq
       61 srwkisalat vavvglagll mlqfergtpe eqetaygrrr aeapapaalp aptpapstap
      121 aaetssaaaa apsaaaalpa rardtaippa mstaqkpaap gharplakta papspapatt
      181 apeaesssgr saagavsgfp asppitaeka mtprpapppa psaapaprae mrersavqdg
      241 aasrevvpqp qampsaaapa aapaarspqg gnaasgklaa ttpsadvgss vlllqhlwea
      301 artgdplqve nlvrqgspid ardsggrtal mlaathgqtt tvqkllalga nrtlvdregl
      361 naaqqarqrg htriadlida eqr
//
LOCUS       WP_010461534             180 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Pseudomonas].
ACCESSION   WP_010461534
VERSION     WP_010461534.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..180
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19401
     Region          40..176
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mprsaaltpd qvpvdskstl dafttnlgft pnmlatfaqs piafnawatw raslnraldl
       61 ktreiislav sevngcdycl avhsytanma klpadeiila rkghatdlkr daavqfarkv
      121 ievrghvsdt dlktvrnagy tdatiaeiva lvavysltnf fnnvfdpekd ypavppagsi
//
LOCUS       WP_010461669             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Acidovorax].
ACCESSION   WP_010461669
VERSION     WP_010461669.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..207
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22770
     Region          11..205
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mlpstyfslp aetevlaage vlrrrnevlt svlhlesgrv lrgvlddgyl rhqlgavegp
       61 fwldaasalm gmplpvdmva dtrvqvrrlp ieefrrslae mpagarglll dmaqgyrqqs
      121 elavsrlaqd aesrcaqwll khaepdhsgt mqvtlhqrkr liaaqlgiap etfsrvlrhl
      181 relglihgtg nvlnlpqpra lqsmagc
//
LOCUS       WP_010461682             127 aa            linear   BCT 01-JAN-2025
DEFINITION  RidA family protein [Acidovorax radicis].
ACCESSION   WP_010461682
VERSION     WP_010461682.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..127
                     /product="RidA family protein"
                     /calculated_mol_wt=13004
     Region          15..127
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mneaeiaagl pstphyqyaq rvgsqlflag qvpqasdgsi vapgnpcaqa sqclanlnkv
       61 lavhgfaapd irrlvvyvvg eqadlsaawd avtehfggqv ppatllgvar lgypgqvvei
      121 datvvkg
//
LOCUS       WP_010461722             234 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010461722
VERSION     WP_010461722.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..234
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25273
     Region          7..203
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mslsqtqiaq qvvesilaqk lapgerlgeq eladlfgvsr tlvrealmql qargfvevrs
       61 rrgwyvveps vedardafsa rriiesgila dagkplqtvt rrlrahiade qqaiegadaa
      121 traflladfh vclaeamghr slsdilrdlt arttlaasly qsqhaasqsc aehaaiveal
      181 eagdtvlare rmlahighve galnsgqplv rdrlreslap ltgqrakaas thrg
//
LOCUS       WP_010461725             343 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [Acidovorax].
ACCESSION   WP_010461725
VERSION     WP_010461725.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..343
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36144
     Region          22..289
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mkkrsflqsa allaaastfs laqaqtltpi kfqldwrfeg paalflqpva kgyfkaagld
       61 vtvdagngsg gavqrvasgt ydigfadlaa vmefhannpd aqnkpvavmm vynntpasvm
      121 alkksgitkp adlagkklga pvfdagrraf pifqkangig avqwtamdpp lretmlvrgd
      181 vdaitgftft sllnlearga kaadvvvlpy adfgvklygn viiaspklik enpaavkafl
      241 saftkgakdv ianpaaaieh vkardgivnv pletrrlqla idtvinspda raegfgqakp
      301 grlslmasqv sdafntktrv naddvwnasf lpsaaelnil pkk
//
LOCUS       WP_010461750             155 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Acidovorax radicis].
ACCESSION   WP_010461750
VERSION     WP_010461750.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167397
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..155
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17620
     Region          6..144
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cd07812"
                     /db_xref="CDD:176854"
     Site            order(7,9,18..20,22..23,38,45,47,49,51,67,69,71,78,80,
                     95..96,98,100,107,109,111,113,128..132,134..135,138..140,
                     143)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176854"
ORIGIN      
        1 mhllaektvy lhrparevfa yvsnmekfge wfpgvisies lntlphgqlg keyletvfvp
       61 lrgrqkitlq vrevrghqff ategrfppll prmeitlnet aanaceltwr ifsrnsnpvv
      121 rylllplarr vmdkratlgv aalkgwmega gtarr
//
LOCUS       WP_010461762             697 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LTA synthase family protein [Pseudomonas].
ACCESSION   WP_010461762
VERSION     WP_010461762.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..697
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=77332
     Region          34..615
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 manpdalsqq rassrllqpt vkshlaytll camvmmvmfs llrvallvyn remiqdspas
       61 tfieafangl rfdlrlvvyl ciplilalfs aramaargff rfwltiaast alflglmemd
      121 fyrefhqrln glvfqyvked pktvmsmlwy gfpvvrylla wafgtliltl afkgadratr
      181 prgpfsggsi garqiapwyt rgvvfvvcll vcvvaargtl rqgpplrwgd vyttdsnfan
      241 qlglngtlsl iaaaksrmse erdniwkatl dqpvaqqtvr dmlltpsdkl vdgetaavrr
      301 nyspaadktl piknvvvilm esfaghsvga lgrpgnvtpy fdklskegll fdrffsngth
      361 thqgmfatma cfpnlpgfey lmqtpegshk lsglpqllsa rdyddvyvyn gdfawdnqsg
      421 ffsnqgmtnf igrndfvnpv fsdptwgvsd qdmfnrglee lkardgkdkk pfyallqtls
      481 nhtpyalptp lpvervtdrg slnehltamr ysdwalgqff eqarkepyfk etlfvvvgdh
      541 gfgneqqite mdlgrfnvpm lligpgvqek fgqvdhtvgt qidivptimg riggdvihqc
      601 wgrdllnlpe gdkgfgvikp sgsdqtvall tadrvlvlpk emppklyqye lganskgeli
      661 pasadeaalk qklesfiqta tkslidntag vvdgkpd
//
LOCUS       WP_010461775             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit beta/FixA
            family protein [Pseudomonas].
ACCESSION   WP_010461775
VERSION     WP_010461775.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26197
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkvlvavkrv vdynvkvrvk adnsgvdlan vkmsmnpfce iaveeavrlk ekgvateivv
       61 vsigpttaqe qlrtalalga drailvesae dltslavakl lkavvdkeqp qlvilgkqai
      121 dsdnnqtgqm laalsgygqg tfaskvevsg dtvavtreid ggaqtvslkl paivttdlrl
      181 nepryaslpn imkakkkple vltpdalgvs tastnktvkv eapaarsagi kvksvaelve
      241 klkneakvi
//
LOCUS       WP_010461784             337 aa            linear   BCT 01-JAN-2025
DEFINITION  porin [Acidovorax radicis].
ACCESSION   WP_010461784
VERSION     WP_010461784.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..337
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=35823
     Region          26..337
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mrrsfpfala acglsvsaav paaaqdlqvy gqvrltvnnv ktgnagsvte erdnasrlgf
       61 rgkedlgdgl aalfglemgl eadsgaattp afrnsyaalr gglgtvalgr ldsanptgsp
      121 lysqvtrits faandagata igtsilnarn rtsnaigyqs ptwggvnlra ryylrgdakt
      181 peqengaksl dlglnyadgp wsagigygkd trpggllane fsskwqagmr ydfgaiepyv
      241 llgrdtyara sattradvdy wlvgtrfsad qhaivvnvmq rdvqaslrgl rkrqqvayty
      301 alskrtelqa fidrdgidss rsnvsvraig agvrhdf
//
LOCUS       WP_010461844             261 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Pseudomonas mandelii].
ACCESSION   WP_010461844
VERSION     WP_010461844.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..261
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28559
     Region          2..256
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mlvdshchld rldlaahdgs ldaaldaarq rgvghflcig vsvenatdvk alaerygdvd
       61 csvgvhpldv qpgaapaldw llrelnhprv vaigetgldy hyepeaaelq qasfrlhlqa
      121 aqqtgkpvii htrgaradtl sllreaalpq agvlhcfted wdmakaaldm gyyislsgiv
      181 tfrnadalrd vaskvpadrl lvetdspyla pipyrgkpnl pqyvrevaef lamlrgeaye
      241 rfaeqttenf krlfplahvk g
//
LOCUS       WP_010461876             327 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: XdhC family protein [Pseudomonas].
ACCESSION   WP_010461876
VERSION     WP_010461876.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..327
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=35601
     Region          6..321
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 mdsadlnvlr svlewrragr rvvlysvvqt wgtaprapga mlalredgvv igsvsggcve
       61 ddliarlhdg rippdgppvq litygvtree aarfglpcgg tlrlteervg dpgwvaelle
      121 rceaheivar sldiatgevi lqaanksdvl sfdghtlrai ygprwrllli gagqlsryva
      181 emarlldfev licdprsefv ygweeqhgrf vsgmpdeavl tietdertai valthdprld
      241 dmalltalds rafyvgalgs rvnslkrren laqlglssqa ierlhgpigl higshspaei
      301 alsllaeiva ikngvelkqk kplqevv
//
LOCUS       WP_010461893             211 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Pseudomonas].
ACCESSION   WP_010461893
VERSION     WP_010461893.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..211
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22752
     Region          1..197
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mwelvksggw mmlpiilssi aamaivaerl wtlrasrvtp ehllgqvwvw ikdkqlnkek
       61 lkelranspl geilaaglan skhgreimke cieeaaarvv heleryinal gtiaamapll
      121 gllgtvlgmi difsafmgtg mgtnaavlag giskalitta aglmvgipav ffhrflqrri
      181 delvvgmeqe aiklvevvqg drdvdlaegk a
//
LOCUS       WP_010461919             471 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Pseudomonas].
ACCESSION   WP_010461919
VERSION     WP_010461919.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..471
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50821
     Region          2..461
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 msgqnshsge lkrglknrhi qlialggaig tglflgsagv lksagpsmil gyaicgfiaf
       61 mimrqlgemi veepvagsfs hfahkywggf agflsgwncw ilyilvgmse ltavgkyihy
      121 waphiptwvs aagffvlinl inlanvkvfg eaefwfaiik vvaivgmial gsyllvsghg
      181 gpqasvtnlw ahggffpngv sglvmamaii mfsfggleml gftaaeadkp ktvipkainq
      241 viyrilifyi galvillslt pwdsllatln asgdsysgsp fvqvfsmlgs dtaahilnfv
      301 vltaalsvyn sgtycnsrml lgmaeqgdap kalakidkrg vpvrsilasa avtliavlln
      361 ylipqnalel lmslvvatlv inwamisfsh fkfrqhmdks kqtplfkalw ypygnyvcla
      421 fvvfilgvml lipgiqisvy aipvwvafmw vcygiknkrs aqhalqaana k
//
LOCUS       WP_010461934             314 aa            linear   BCT 01-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Acidovorax radicis].
ACCESSION   WP_010461934
VERSION     WP_010461934.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..314
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34224
     Region          62..267
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mnfefpitel pavmrgprve rrrvlvggsa cwgtiveega qqgqlrlddg rvldptsvqh
       61 lppvspskvi avhisyssrs fetrnqpkpt etptyftkpp tsvnghgcei hkpadsqyln
      121 yegeyavvig ktcrnvlpde awdyiegfcp aldmglqnyr dtdqgsmlrv kgadtllpig
      181 pgivrgvnlf eqtlrtyrng lvvqeahigd etiwgphyvv adiarhitlv pgdvilmgtp
      241 chsrsvdpgd lveceitglg rlagtvvaia aprasalgvg hqptdspevr rvacgfderv
      301 pehlkanyrq aakk
//
LOCUS       WP_010461954             484 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TrkH family potassium uptake protein [Pseudomonas].
ACCESSION   WP_010461954
VERSION     WP_010461954.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..484
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=53070
     Region          69..483
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 malptlriig fiigiflitl aiamvvpmat lvifertsdl psflwasmit fvaglalvip
       61 grpehihlrp rdmylltvss wlvvcvfaal pflltqhisy tdsffesmsg itatgstvln
      121 hlddmspgil mwrsllhwig gigfigmava ilpllriggm rlfqtessdr sekvmprshm
      181 varlivaayv gitilgslaf wwagmspfda inhamsaist ggfstsdqsl akwtqpavhw
      241 vaivimilgs lpftlyvatl rgnrralikd qqvqgllgml lvtwlvlgtw ywwttqlhwl
      301 ealrhvalnv tsivtttgfa lgdyslwgnf slmlffylgf vggcsgstag gikifrfqva
      361 yillkanlnq lihpravikq kynghrldee ivrsiltfsf ffaiticvia lllsllgvdw
      421 mtaltgaast vsgvgpglge tigpagnfat lpdaakwils fgmllgrlei itvfvlcipa
      481 fwrh
//
LOCUS       WP_010462002             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tRNA-uridine aminocarboxypropyltransferase
            [Pseudomonas].
ACCESSION   WP_010462002
VERSION     WP_010462002.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Funk,H.M., Zhao,R., Thomas,M., Spigelmyer,S.M., Sebree,N.J.,
            Bales,R.O., Burchett,J.B., Mamaril,J.B., Limbach,P.A. and Guy,M.P.
  TITLE     Identification of the enzymes responsible for m2,2G and acp3U
            formation on cytosolic tRNA from insects and plants
  JOURNAL   PLoS One 15 (11), e0242737 (2020)
   PUBMED   33253256
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Meyer,B., Immer,C., Kaiser,S., Sharma,S., Yang,J., Watzinger,P.,
            Weiss,L., Kotter,A., Helm,M., Seitz,H.M., Kotter,P., Kellner,S.,
            Entian,K.D. and Wohnert,J.
  TITLE     Identification of the 3-amino-3-carboxypropyl (acp) transferase
            enzyme responsible for acp3U formation at position 47 in
            Escherichia coli tRNAs
  JOURNAL   Nucleic Acids Res 48 (3), 1435-1450 (2020)
   PUBMED   31863583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..197
                     /product="tRNA-uridine aminocarboxypropyltransferase"
                     /EC_number="2.5.1.25"
                     /GO_function="GO:0016432 - tRNA-uridine
                     aminocarboxypropyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=21557
     Region          1..197
                     /region_name="TapT"
                     /note="tRNA U47 aminocarboxypropyltransferaseTapT/TuaA/
                     YfiP, DTW domain [Translation, ribosomal structure and
                     biogenesis]; COG3148"
                     /db_xref="CDD:442382"
ORIGIN      
        1 msriqcprcl rpqthclcpl ipsldsrtrv lllqhpsevn halntarlaa lglknaeliv
       61 gevfedlpvl lnppgyqarl lfpaddaqpl qayttneepl llvvpdgtwr karkmlhlnp
      121 llaalprvtl vdggvsryrl rkapgpgals tveaivqalq tleapssfep llkpfealie
      181 gqiaamgeet yqrnhgr
//
LOCUS       WP_010462093             509 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tripartite tricarboxylate transporter permease
            [Pseudomonadota].
ACCESSION   WP_010462093
VERSION     WP_010462093.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadota (proteobacteria)
  ORGANISM  Pseudomonadota
            Bacteria; Pseudomonadati.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     Protein         1..509
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=53735
     Region          1..491
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 msefdsllqg mnliltpghi glmvigvllg ilvgvlpglg apngvalllp ltftmspvsa
       61 iillscmywg alfggsitsi lfnipgepss vattfdgypm aregraaeal taafssalig
      121 alagvllltf lstkiaafam sfsspeffav yllafctfig msknpplktv vammigfama
      181 avgmdtvsgn lrltfdqpal mtgisfevav iglfgigeil ctveeglvfr geharitpmv
      241 ilrtwaklpr ywwtilrstl vgcwmgitpg gptaasfmsy slarrfsknr enfgkgeleg
      301 viapetadha agtsallpml tlgipgsata avmlgglmiw glhpgptlfv eqhdfvwgli
      361 asmylgnvvs livvlatvpl fasilripfs iiapiiimvc aigaysvhns fvdvvlmlgf
      421 galgylfkkl gypiaplvla avlgdkaeda frqsmlfsdg hvgifwsnpl vgclttaall
      481 mlfwpliska lgtltglrkp qvakpksvl
//
LOCUS       WP_010462067             203 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Pseudomonas].
ACCESSION   WP_010462067
VERSION     WP_010462067.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..203
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22971
     Region          3..200
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 maaddaqllq rllageqqaf kelvstyqsp mravayaivg nrhadevvqd awlsvvrnls
       61 kfearsslkt wlltitanaa kgrykqnrre vllddlpsph gtidddrfss adghwlvapf
      121 awhqdtpeal lterelrecl ehtllslsel qrsvlllrer qgleledicn lldislsnvr
      181 vllhrarlkv fatvehfeet gec
//
LOCUS       WP_010462100             341 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acidovorax radicis].
ACCESSION   WP_010462100
VERSION     WP_010462100.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..341
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36246
     Region          4..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mpavsfqais ktfatpkgpf qalnqvnldi eegeffgllg pngagkttli silaglaras
       61 sgrvlvqgsd vqadfaearr klgvvpqelv fdpffnvres lriqsgyfgv knndawidel
      121 lenlgltdka nanmrqlsgg mkrrvlvaqa lvhkppiivl deptagvdve lrqtlwhfva
      181 rlnkeghtvl ltthyleeae alcgriamlk sgrivalnrt sellqaasgs ilqfktdaal
      241 ppalagvarv tgrivqlpah daaeieshla alrvagvdvh dmeirrpdle dvflqvmsgt
      301 svsnipmsev tsaaapgrpk hgaaplggse dtavssggaq r
//
LOCUS       WP_010462130             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: spermidine synthase [Pseudomonas].
ACCESSION   WP_010462130
VERSION     WP_010462130.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..228
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24226
     Region          67..191
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mkrfvlldta pipenggalc lfeygedfvi kiqggdggql mntrmhgsed alaeipcrkv
       61 agrpnsrvli gglgmgftla salkhlgkta evvvaelvpg vvewnrgplg ekagnplldp
      121 rtvirledva kvlqaepqgf daimldvdng pegltqrans wlysagglsa cakalrpkgv
      181 lavwsasadk qfsdklkkag fkaeevqvfa hgnkgtrhti wiaeklkg
//
LOCUS       WP_010462169             128 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GtrA family protein [Pseudomonas].
ACCESSION   WP_010462169
VERSION     WP_010462169.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..128
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13751
     Region          7..128
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mtsaeksali qrglrfavtg lfvtalhalv avlfihyvlp lpplangaaf avatvvsyli
       61 nttwsfsarl hgktllrfmm vsaagfllam lvawaaqmag lhyllgigav altlpaftfv
      121 lhnfwtyr
//
LOCUS       WP_010462173             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Pseudomonas].
ACCESSION   WP_010462173
VERSION     WP_010462173.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..322
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36396
     Region          17..199
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(20,22,107)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(54,106..107)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            105..107
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mthqhgtqlt ghvqlslvip vfneaatidl fiaritdvfk detliglemv fvndgstdtt
       61 ldlllerqqt dsrlrivdls rnfgkeaalt aglqtatgqv vvpidvdlqd ppevilemia
      121 lwregyevvl ghrvsrktds wakqtsanwf yrlhnkiaeq hlpenvgdfr lmdrcvvdal
      181 qtlpesrrfm kglfawvgfr tthvnyerle rvagaskfng wrlwnfaleg itsfsteplr
      241 iwtylglfvs lisfsfaifi ilrtlisgvd lpgyaslmva vtflgglqli gigvlgeylg
      301 rtyieskrrp vylvrrvydp kd
//
LOCUS       WP_010462207             234 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Acidovorax radicis].
ACCESSION   WP_010462207
VERSION     WP_010462207.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423250
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..234
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25890
     Region          27..219
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
     Region          54..147
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 msapefdaha dsyrqtldra laigggdsly yaerkfaslr ayqkereraa ptavldfgcg
       61 tgtnlpflrd lfsdaalqgv dvsprsleva serqvlgcrl aiydgvtlpf edaifdmvvv
      121 snvlhhieps hrastlkeia rclkpgglla vfehnpfnpv trrvvrdcpf dagvtlvrpr
      181 eiksilreqg yqiaslwnii ffpaalkkln avepqmrwlp lgaqyalfae wpgs
//
LOCUS       WP_010462236              99 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF805 domain-containing protein [Acidovorax].
ACCESSION   WP_010462236
VERSION     WP_010462236.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..99
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=10853
     Region          6..98
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mdfvsaiksc ltqyagfsgr avrsefwwff lfqvvvmvaa sflgdvisgi vsialvlpaf
       61 avgarrlhdi grsgwwqllt ltgigvlvli ywwvqpseg
//
LOCUS       WP_010462239             349 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Pseudomonas mandelii].
ACCESSION   WP_010462239
VERSION     WP_010462239.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..349
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=38635
     Region          31..338
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mvlqveeacg aldvgegfga gtgtggpslk rtvkegidrw levqralkas stvvnyvska
       61 mhvekkfgkr rivdisksdi elfqaqllkq glapktvndi ftivrgvwad afgdgilksn
      121 pldrisnvgs dvdlehadpf srteieligk adpdrradar miefncwagl slseliglav
      181 edidleaglv hvrralvvge fkvpkersrv rvvelidpal almreivvaa keaptveiii
      241 iqrdnitskk mkvrflfrss tsgllwsgkt lsnwftahlr kaavrhrgan qcrhtfasqm
      301 lssyvpvewv arqlghsdtt mvrkhygrwi pkdtksmagm vskmlgfrt
//
LOCUS       WP_010462279             273 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HDOD domain-containing protein [Pseudomonas].
ACCESSION   WP_010462279
VERSION     WP_010462279.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..273
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=30517
     Region          14..239
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mseladkvqq dlveaidndd lvlptlpeva lqirkaaedp evsvstlskv igrdtalsar
       61 likvvnspll ratqevtdlh taitrlgvny ssnlaiglvm eqifharsev vaqkmrdvwr
      121 ksleiagvsy alcrsytqlk pdqaalgglv hqigvlpilt yaedhyells davslnhvid
      181 rihpligdkl lrvwefpeml vqlpglyldf krqservdyv dlvqvaslyc hkdtdhplar
      241 idafsvpafk klgidpenea mcrdleesrs mfy
//
LOCUS       WP_010462294             370 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Pseudomonas].
ACCESSION   WP_010462294
VERSION     WP_010462294.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..370
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41063
     Region          16..354
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mnlhfeeltg tdgarigias ldaekslnal slpminalrd qmdawakdpq ivcvllrgng
       61 akafcaggev rslveacrah pgevpplaah ffaaeyrldf nlhtypkpli cwghgyvlgg
      121 gmgllqgasi rivtpssrla mpeisiglyp dvgaswflsr lpgklglflg ltgahmngrd
      181 aidlgladrf lldeqqeeli egllqlnwqe qtpmqlnsll kalqqeavaq mpaaqwlprr
      241 qqidelldis dvrcawkais alrdhsdlll sraaktmteg spltahlvwe qiararhmsl
      301 aqvfqmeyti slnccrhpef segvrarlid kdqkphwhwp dinnvpdavv eahfhkvweg
      361 rhpladlsey
//
LOCUS       WP_010462347             487 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Acidovorax radicis].
ACCESSION   WP_010462347
VERSION     WP_010462347.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..487
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=49873
     Region          7..458
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mtatpgvmmt lqqafallas ripsarlvgd gatplvrvht dtrtlqagdl fvalkgerfd
       61 anaflsdars ggaaaaiahg gleaaglpgi evpdslaalg alaagwraql glpligvtgs
      121 ngkttvtqmi asilrawkge aafatqgnfn ndigvplmll rlrashaaav iemgmnhpge
      181 iallaamaqp tvalvnnaqr ehlefmhtve avarengsvf aslpadgvav fpvgdaytgl
      241 wrslgagrrt vtfgdggdva caqaawgqga wavtlatpqg evathlhiag rhnvtnalaa
      301 aactlaagap laaiaqglnd fvpvkgrsra fsvhsagrei tvvddtynan pdsmraaidv
      361 laelpgpqll vlgdmgevgd qgpqfhaeag aharaagipl lfalgtqsvh aatayggarh
      421 fndmsallta vrdalstvgs vlvkgsrfmk meqvveaisa tataaaqpqe qqqkqnrale
      481 ghhgath
//
LOCUS       WP_010462366             587 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: STAS domain-containing protein [Acidovorax].
ACCESSION   WP_010462366
VERSION     WP_010462366.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..587
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=63295
     Region          <49..>71
                     /region_name="XPF_nuclease-like"
                     /note="nuclease domain of XPF/MUS81 family proteins;
                     cl41760"
                     /db_xref="CDD:425391"
     Region          501..577
                     /region_name="STAS_2"
                     /note="STAS domain; pfam13466"
                     /db_xref="CDD:433231"
ORIGIN      
        1 mskeettpgg llskvvrfvk nptvnwteld siqddresqy skqmlkemie rkrrndfvrr
       61 refdqlrklr qrevlqgqrv edaagrpsff qssmaspddr avtlkkidei eaqmsqqwwk
      121 skqgaeaptq pgampaaasg aatsdsehar ayaptapgsl paplenkpgv qplfaddsma
      181 igrfggtdaq mlpgegpgea sfspaaataa tpapasepee fvhepdleea airfangdha
      241 gaesglldvl aqhqqdapdd qleiwmtlfd lyratgqhdr fdtlaidfaa qysrsaplwf
      301 smleqlgmap ppaaaapgap aaapvgavrr dfswnapptl avssvaalqa slarsaspwt
      361 lswarlgaid eaavpllaeq ftrwaerdgq lvfsgvekln alldaktqsg drstspewws
      421 lrmaalrlmg kpdefelval dycvtyevsp pswvsprcgy sdnegassgs aplaadsdfm
      481 asdlgdasap apletgpvaq lsghidgdat plleafqafl rpgvpltiac dklirvdfaa
      541 agsvlnwaae qqghghviqf hnlqrlvaif fnvigineha wvvprkn
//
LOCUS       WP_010462474             295 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Pseudomonas mandelii].
ACCESSION   WP_010462474
VERSION     WP_010462474.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..295
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31424
     Region          6..294
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mstpaihgii gytitpftan gegvdldalg rsidrlidgg vhaiaplgst gegaylsdae
       61 wdqvsefsik hvakrvptiv svsdlttaka vrrarfaeah gadvvmvlpt sywklseaei
      121 lahyraigds igvpimlynn patsgtdmsv dlilrivnav envtmvkest gdiqrmhklq
      181 llgegrvpfy ngcnplalea faagakgwct aapnlipqln ldlydavlan dlgkgrelfy
      241 rqlplldfil kgglpatika glratglevg dprlpvfplg eagisqlqdl lkalr
//
LOCUS       WP_010462391             294 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010462391
VERSION     WP_010462391.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32271
     Region          1..292
                     /region_name="trans_reg_YafC"
                     /note="DNA-binding transcriptional regulator YafC;
                     NF040888"
                     /db_xref="CDD:468824"
ORIGIN      
        1 mkttleelqa fvavvdggsi taaadqlgqt vsgisralar lekkldttll rrttrrtelt
       61 eegqafllrt railasieea eesmaarrqq pagrlrvnaa tpfmlhavvp lvpafrkayp
      121 qitlqldtde ayidllerrt dvairigplq dstlharplc tsrlrvlasp dylaragkpk
      181 smvdlashtl lgfnqpesln hwplrgvhgd awpivpslta ssgetlrqla lahvglvcls
      241 dfmtagdrea grlvqvlard tvdvrqpina vyyrntqlaa riacfldflq ermg
//
LOCUS       WP_010462475             142 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Acidovorax].
ACCESSION   WP_010462475
VERSION     WP_010462475.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..142
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15329
     Region          13..138
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 msavfspppa alptdkelvl kvipmpadtn gngdifggwv maqvdlagsv lparyiqgrm
       61 atvavnefif kqpvrvgdil sffssitrvg ntsvtvevev yaerftdqgr yvkvtearlt
      121 yvaiddhgrp rpvpkhtpnp ss
//
LOCUS       WP_010462483             358 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Acidovorax
            radicis].
ACCESSION   WP_010462483
VERSION     WP_010462483.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..358
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38829
     Region          40..333
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mrflfktsye qdlrlakhgg hvfwysllaa glvaapwvap eywlaqltfv liyaivglgl
       61 mllagftglf slghaaflgv gaytqavltg mgwpfalsla caaglsaavg vvvglpalrv
      121 kgiylgmatl sfgfiveevf arwesvtggn sgkhlvppei wgfkfestes fyflclviav
      181 vstlailnll rsptgrafva irdseisaqs mgihlarykt lsfsisaala gvggalyahk
      241 lqfispdqfn ilqsidlllm ivigglgsvh gaflgaifli tmpqmislsk dwlpaaigqa
      301 pglqavvygv vliafvlfep mglygrwlkv rtwlqmfpfy rrglfkrqks fqksdrlk
//
LOCUS       WP_010462554             345 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Acidovorax radicis].
ACCESSION   WP_010462554
VERSION     WP_010462554.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10606006
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..345
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=38791
     Region          12..131
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
     Region          202..>309
                     /region_name="PRK05771"
                     /note="V-type ATP synthase subunit I; Validated"
                     /db_xref="CDD:235600"
     Region          257..>330
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mtnierydya fdpdgeewaa rllrrvpsgg gsvlelgpgp gamtrvllar ghrvtvvend
       61 pealevlktl dveiisgnld gadwldavkg rqfdtvmacd vlehlrkped vlqrlsefva
      121 pmgcllisvp niayagvlas mrsgifdysd kgqldrthvr fftkrsiekv lldcgwaprv
      181 weanrvpvec sefagywsal sgdqrqalla gwqdfdvyqw mvvvtpsvat ptwelkearg
      241 madslrgelq altvlhqrer asllehqkaf aeakdiiskl qqditklqee inelrtdvgs
      301 lrsekaaves elaktrielq artveltdra wrsrwrrlmg shysh
//
LOCUS       WP_010462593             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010462593
VERSION     WP_010462593.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34078
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 msemddlaaf avlieagsft laaqqlgcsk gqlskrisll etrfsvvllq rttrrlslta
       61 agaallpqaq alvvqvekar qalarlkddm agpvrmtvpv slgetffdgl llefsrqype
      121 vqieldlnns fhdlsrdgfd lairsevand qrlvarplla whemtcaspa yleqygepqt
      181 pqaladhrcl lnshysgree wlyhqqhell rvrvsgpfas nhysllkkaa lagagiarlp
      241 syllqtelad grlrwllrdy qtrsmpmylv hpyqgglpkr tqvladylid wfkrsgeala
      301 rlqq
//
LOCUS       WP_010462721             166 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CinA family protein [Pseudomonas].
ACCESSION   WP_010462721
VERSION     WP_010462721.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..166
                     /product="CinA family protein"
                     /calculated_mol_wt=17465
     Region          4..157
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mkeitqlaae lgrrlqvlna hvaaaesctg ggiseaitri pgssawfeag yvtysnrqkt
       61 eqlnvppelf etvgavsrev veamvrgaqe ksqahfavav sgvagpdggs pnkpvgtvwl
      121 awgvgeqvfs evqhfagnrd evrrqtvkaa legllrhaag eisnqg
//
LOCUS       WP_010462777             209 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor [Acidovorax].
ACCESSION   WP_010462777
VERSION     WP_010462777.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..209
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22667
     Region          11..205
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mtdsapslsp lihlvdddaa vrdglgllis tvglrvqtwa dpqsfmagfd rasigaivld
       61 vrmpgisglt vleqllaqgv dqpmilltgh gtvemcrraf kagaaeflek pvddevliea
      121 lqnavrqhvr srerhqadqq arerfaqlsa rerevlgliv egltnkeigr alelsprtve
      181 thranlfgkl gaeslaqlir ryaalvdas
//
LOCUS       WP_010462596             572 aa            linear   BCT 01-JAN-2025
DEFINITION  GspE/PulE family protein [Acidovorax radicis].
ACCESSION   WP_010462596
VERSION     WP_010462596.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..572
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=62374
     Region          18..570
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mklsaevgev esvdlaaprl gemlladqkl srndlerale vqrsmggrlg rllislglvs
       61 eidvysalsr qaglplvrqd afpkekpdts rlntsfllan nllplgnaed aestpdfasv
      121 dpksaalrda lrlvfgaapr vffgleseis nqlnawyvqe sepdgevvad qfeasefieh
      181 lrdmaseapi iqrvshilsq avaaqasdih ietyeeksvv rirvdgelyp ideidnkdap
      241 avvsrikils qldiaerrmp qdgrtklrvh gkemdsrvst iptmfgesvv mrlleknfdl
      301 lsleslhftp ptlktmrqll svphgiflvt gptgsgkstt lyasmqeleg enlkiltved
      361 pveyrlqwln qvqvqpqigl tfakvlrsfl rqdpdvimig emrdgetaei avqaaltghl
      421 vmstlhtnsa lgaivrlinm gvepylitas vigvlaqrlv rklceeckap llpdqaqaaa
      481 aslgvameeg qtiyrsvgcp acrgtgyrgr lavhellvmt edvkkvvler gsslgsgdga
      541 yaggnllqdg atkvfkgltt aeevlrvarq nd
//
LOCUS       WP_010462871             448 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Fic family protein [Pseudomonas].
ACCESSION   WP_010462871
VERSION     WP_010462871.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..448
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=51097
     Region          127..440
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mkkpplftgr sdpvfdllaq sphkerltdy lallkplddq grylpfhelr yrwapgmdss
       61 lcwalvkkar taqyssllpl gepvqwgnfv ltplaqkais avdrqattaa leymtsrige
      121 hahfsyllnd liedeaisss qlegaatttr vakdmlkrkr lprtpdermv vgnykmmnfa
      181 werrydplsv qlimamhrvg vegiddaqys pgefranddv vvqdgegntv htpppavglv
      241 srlrtlsewi nqshddpert dylhpmikgi alhfalgyeh pfrdgngrva ralfywfmfk
      301 ndfsafryia isillrnapv kygrsylnte addldltyfi dfqcsvilra vsgfteayrk
      361 slayterfdr wltesgffdr ltekqravyq vaksgmakef tavnvkenld csyntasatl
      421 nglvelnvfe krkmgrewvf flraasvt
//
LOCUS       WP_010462873            1021 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Pseudomonas].
ACCESSION   WP_010462873
VERSION     WP_010462873.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..1021
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112702
     Region          4..1018
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mgfnlsewal rnrqivlflm lllavvgals ytklgqsedp pftfkamvir tnwpgataqe
       61 vsrqvterie kklmetgeye rivsfsrpge sqvtfiards lhsvqipdlw yqvrkkvsdi
      121 rhtlppgiqg pffndefgtt fgniyaltge gfdyavlkdy adriqiqlqr vkdvgkvdll
      181 glqdekiwie lsnvklatlg lplaavqqal eeqnavstag ffettserlq lrvsgnfqtv
      241 deiknfpirv gdrtfrisdv advrrgfndp paprmrfmae naiglavamk dggdilvlgk
      301 aleiefdriq knlpagmqlr kvsdqpaavk tgvgefvqvl vealaivllv sffslgvrtg
      361 mvvalaiplv lamtfacmyy lgiglhkisl galvlalgll vddaiiavem maikmeqgfd
      421 rikaasyawt stafpmltgt litaagflpi ataqsgtgey trsifqvvti allaswivav
      481 vfvpylgekl lpdlakihaa khgtgqpdpy gtpfyqrvrr lvewcvrwrk tvivltvvlf
      541 igsivlfrfv pqqffpasgr lelmvdlkla egaslsntad evkrleallk dhagidnyva
      601 yvgtgsprfy lpldqqlpaa sfaqfvvlak tieeretlrt wlietlneqf palrsrvtrl
      661 engppvgypv qfrvtgehie evralarkva akvrenphva nvhldweeps kvvylnvdqd
      721 raralgvsta nlskflqssl tgssvsqyre dnelieillr gtlhertels llpslavptd
      781 ngrsvalsqv atleygfeeg iiwhrnrlpn vtiradiygk eqpatlvqqi lptldpirae
      841 lpdgylldvg gtvedsargq nsvkagvplf ivvvltllml qlrsfsrtvm vfltaplgli
      901 gvtlflmvfr qpfgfvamlg tialsgmimr nsvilvdqie qdiaaglkpw qaiieatvrr
      961 frpivltala avlamiplsr svffgpmava imgglivata ltllflpaly aawfrikkes
     1021 v
//
LOCUS       WP_010462907             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Pseudomonas].
ACCESSION   WP_010462907
VERSION     WP_010462907.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..304
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33668
     Region          31..261
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mrilgilcll ltlsgcssll fypepgqlft pekakldyre vtlitadglr lnawwlpakn
       61 gvevkgtvlh lhgnggnlpm hlggswwlpe egyqvllidy rgyglsegep slpaiyqdid
      121 aafkwldqap evkgkplill gqslggsmav hylvqhperq kqlkafvldg vpasyrsigr
      181 falsnswltw alqvplswlv pdgdsainsm aqlndvpkli yhsiddpivp lsngirlyqa
      241 appprvlqlt rgghvqtfad pvwrkvmlry lddpqhfngl rrlgeipnyp appnsedeps
      301 espq
//
LOCUS       WP_010462908             224 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Acidovorax radicis].
ACCESSION   WP_010462908
VERSION     WP_010462908.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..224
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=25138
     Region          25..210
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mtveptsppr dlpdlpeglf adeagcprct wcqatpfyrh yhdqewgfpv addrrlfeki
       61 clegfqsgls wltilnkreg fraafanfda eqvaafgptd verlvqdaai vrhrgkiest
      121 innarrvlel rrefgslahy awryepaaad rperltreva rtlstspasi amskdlkkrg
      181 wsfvgpttvy afmqamglvn dhlegchsra palkaraefv aprg
//
LOCUS       WP_010462927             315 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Acidovorax radicis].
ACCESSION   WP_010462927
VERSION     WP_010462927.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..315
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33652
     Region          6..313
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mpaisnyrgi ipaiscpftp dhridepalr klaswlaghe gvvaimtngh tgevfsltpa
       61 eraevtriva delkglarpv pvissivceg ladaaehara aveagavald vmpphhwlrf
      121 gftpghalqy feaihkaaps adlichvypa wtrasyssql ladlarlpyl qafkvgqrdm
      181 nkyardiqai readaskail tchdeyllas mvqgvdgalv gfatfipqli idlwnavkag
      241 dlkkamavqa vitplkdavy gggeptgeah armkggmyla gvlddatvrp pteapnakev
      301 ealraavkqa gllkr
//
LOCUS       WP_010462965             242 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Acidovorax].
ACCESSION   WP_010462965
VERSION     WP_010462965.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..242
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26419
     Region          10..234
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mldirkaqhr gnanhgwlhs rhtfsfghyh danqqgfsdl lvinddrvap gkgfgthphr
       61 dmeifsyvle galehkdsmg tgsvirpgdv qmmsagtgvr hsefnhsgee pvhflqiwiv
      121 pgargaapry qqvhfseadk rgrlrqiisp egadgslavh qdarvyaglf dgseeaadld
      181 vgpgrnvyvh vargslevng erlsegdgar irdagalrfa hgegaevlvf dlrpnelptm
      241 ph
//
LOCUS       WP_010462945             335 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010462945
VERSION     WP_010462945.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..335
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36215
     Region          176..333
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <278..333
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 msvpgpqpga gphpdavral srsllalgql arhtqpqdml hqalqtlqal vpfdsawwge
       61 msagdvhtsp rnwlhgsmgl sqsfaqewne lsavdefarq smsrlgvvir erdvtgdiae
      121 haevlafser hglyhcmalt aelphsgllf fvsvyrpqar teftdeetvl fgefvvhllq
      181 hwhhrlqalq sdspsrpwds falaepsgdl lfaglrisla lgeahpgwag trlptavvqg
      241 larapctvav gkacrlrmep cgslvaisia srhpksplap relsaamlya qgrshkdiaa
      301 tlgltpatar tylrtayaal gvsnklelva alrta
//
LOCUS       WP_010463000             268 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Acidovorax radicis].
ACCESSION   WP_010463000
VERSION     WP_010463000.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..268
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=28642
     Region          109..254
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 madtpamatp qpmgqapvar ingvalnsta ewlddealrq ractellrqa aqqggflaqd
       61 dvpgvegais tkasnaieql lerelpipdp seeacrryhd ahpaahahge raqlrhvlfa
      121 vtpgvdvkql rlraeamlid lrcaddggak faeaaaqwsn cpsgqqggdl gwltradcap
      181 efarevfgsa eigvlarlvh srfglhvvev vardpgqqps feevrqaial tlrqqawvna
      241 lrqylqllag aavvegvald aadsplvq
//
LOCUS       WP_010463018             437 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010463018
VERSION     WP_010463018.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..437
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46440
     Region          20..424
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(32..33,36..37,40,79,137..138,140..142,145,165,
                     168..169,172,255,258..259,262..264,267,295,299,351..352,
                     356,360,376,379..380,383..384,387)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mttsttysda ptqptnsatr vatasfigta iefydfyvya taaalvigpv ffpqtsgtaq
       61 mlsafltfgi aflarplgsa lfghfgdrig rkstlvasll lmgvcttlig vlpgydsiga
      121 wapillcvlr fgqglglgge wggaallate napkgkrawf gmfpqlgpsi gflaanglfl
      181 tlamtlndeq frswgwripf llsaalvmvg lyvrlklhet pvfanamarq ervkiplvel
      241 fsqywvpmll gagsmvvcya lfyistvfsl sygvstlgys retflgllcf avlfmaaatp
      301 lsawasdryg rkpvliiggv lailsgflme plltqgstwg valflcielf lmgvtfapmg
      361 allpelfpth vrytgasaay nlggivgasa apffaqklva mgglsyvggy vsgaavlsli
      421 avlclketrh ndlnrvt
//
LOCUS       WP_010463051             304 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Acidovorax radicis].
ACCESSION   WP_010463051
VERSION     WP_010463051.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..304
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31656
     Region          14..303
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mpstnprnyd atpsrkvafl glgvmgypma ghlalaghev tvynrtatks iawcaeyasa
       61 kapkhaatph eaaagadivf ccvgndddlr svtlgadgaf agmkpgavfv dhttasaeva
      121 relhaaakal glqfvdapvs ggqagaqngl ltvmcggdaa afeaaqpvam afsraftllg
      181 esgagqlakm vnqiciaglv qalseavafg qnagldmkqv ldvigkgaaq swqmdnrgks
      241 mvddkfdfgf avdwmrkdlg lvldeakrng srvpvtalvd qfyadvqkmg gnrwdtsslv
      301 krlk
//
LOCUS       WP_010463053             222 aa            linear   BCT 01-JAN-2025
DEFINITION  BON domain-containing protein [Acidovorax radicis].
ACCESSION   WP_010463053
VERSION     WP_010463053.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..222
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=23529
     Region          46..196
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mkqttmnrte rtvctvlaaa alaaglsaca plivggavvg gvmavdrrtt gtqiedegie
       61 lraanriret lgdrahvnvt synrqtlltg evpsaqdrqt veqivsqven arsvvndlav
      121 lpasslsqrs ndtfitgkvr aslvdaqdis ansfkvvter nivylmgrvs qreanratei
      181 argvsgvskv vrvfeivsee elrriapqpa pvttdnsasp gg
//
LOCUS       WP_010463114             316 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Acidovorax radicis].
ACCESSION   WP_010463114
VERSION     WP_010463114.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..316
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=35512
     Region          97..196
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mnnifldart irdidkvvdr vhlelgykdg aidlrdvrea lrldlkyyrl ddpglldevv
       61 hkltvgakqv iarpgllvea vrtfnlsalf lpdrkrifvd qsvpelkkrw yetheiahsl
      121 ipwhadytlg dnrstlsqgc herieaeany gggrllfpne afthcrlsgp msvgrvreia
      181 khfgntitst lwrcveqsde lmfaaigehp rrprdgkpvv eyfirsktfe tqfpgvtdmd
      241 vwnwmsgycv gkttgplgtt eipvqdrngq shifliesfg ngynaltmar wlrkapaivs
      301 vggltaplli aplagq
//
LOCUS       WP_010463140             393 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010463140
VERSION     WP_010463140.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..393
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42558
     Region          204..390
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 msgeerdpqp vgipgfetlm aeslealgep gmverllhrv geslgshkvv lfcplpgsdd
       61 plaayqwgmp ddflaryanl iqgsdawsea lerqqaqala rggslsqqlv gtqalrrgaf
      121 yadylkplgi damvnsivea spevgmhvla myndlgqsef tpeqfarlra vtpwvrslmr
      181 aqrrlqrarr hssalertld qlplglmhan qrgevrylne harawlgved ecrillrnat
      241 gwqarqplql aqihpgltpl ltaslstrsp vsarlqtqqd papgtlvala aplrngpgpa
      301 aeplaqfilv peapphagat vsvcsalygl tpaeaallpl llqgmtprem adnrhvkmpt
      361 vrsqlaslya ktgtrgqael aqrvlrvaal vta
//
LOCUS       WP_010463178             105 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Acidovorax].
ACCESSION   WP_010463178
VERSION     WP_010463178.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..105
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=10900
     Region          24..>105
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mkyaralafa avagitiita tgcsvareqq tvgsyvddag ittavkakma edknvsatsi
       61 svetlngtvq lsgfaksqae knqaeaiarn tknvrevrns ivvrp
//
LOCUS       WP_010463166             249 aa            linear   BCT 01-JAN-2025
DEFINITION  HesA/MoeB/ThiF family protein [Acidovorax radicis].
ACCESSION   WP_010463166
VERSION     WP_010463166.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..249
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26124
     Region          2..246
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mtddqllrys rhilldemgi egqeqvlash avivgagglg spaalylasa gvghitlvdd
       61 dvvdltnlqr qiahttarvg rpkvesaasa meainpgvrv talqaradat vldalvqdas
      121 vvldcsdnya trqainaacv rhrkplvaga virfdaqitv vdprhaaspc yacifppeae
      181 feevrcstmg vfaplvgvvg amqaaealkl lagigtslag rllmldgrtm ewstmnvara
      241 ahctvcvvr
//
LOCUS       WP_010463147             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010463147
VERSION     WP_010463147.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35026
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqnmraf syvaeagsft aaavqldttt anvsravsnl eahlqtrlln rttrrialte
       61 agkryllrce qilayveeae aeasdaharp agqlkvhtmt gigqhfvida iaryrkthpd
      121 vtfdltmanr vpdlldegyd vsivlaselp dsgfvsqrlg itysivcasp ayvkangcah
      181 kpsdllnhac lrlvspvipl ekwtfdgpeg qemvtinssp flvnsadamk taiisgmgvg
      241 vlpvyaaieg lrngtlvrvm pnyrsqelnl yaiypsrqyl dakiktwvey lrgslpeila
      301 ahqaelvaye lsgslggvrv an
//
LOCUS       WP_010463256             418 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: patatin-like phospholipase family protein
            [Acidovorax].
ACCESSION   WP_010463256
VERSION     WP_010463256.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..418
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44675
     Region          11..299
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mppsapsdtp ashrpptgll ltgggaraay qvgvleaiad irhacgeggg pnpfpiitgt
       61 sagainaaal acgadnfdra vrriarvwrq fhasqvygad slsvmrsgar wltlvsmgwa
      121 larwrrmrpr slldnsplek llvkmvplvr lpglirkghl talavtassy ssgehvtffe
      181 aatpvkpwvr sqrkaasdri thehllassa ipfifpakai evddhieyfg dgsmrqsapi
      241 apaihlgaer ilvigagrmh epkgdaaanp tatyptlaqi aghalsnifl dalavdverv
      301 qrinqtlsli peekrlhsal rpiellviap sqrldavaar hvgdlpgpvr amlgalgvts
      361 nmadvrgaal asyllfesgy tkelmalgra dtlamraevc rffgwtdtga evqmrehs
//
LOCUS       WP_010463309             198 aa            linear   BCT 01-JAN-2025
DEFINITION  LemA family protein [Acidovorax radicis].
ACCESSION   WP_010463309
VERSION     WP_010463309.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..198
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21061
     Region          1..198
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 msatawivlg lvavlavwav tvynrlvqlr nrianafgqi dvqlkrrhdl vpnlvevakg
       61 ylsheaatle avikargqaq gaaaavraep gsanamgala aaegvlgssl grlmvvaeay
      121 pelkadatmq slseeltste nrlgfarqay ndqalefnda aaqfpdlvva rllgfptvpm
      181 lestrsdeer tapqvrfs
//
LOCUS       WP_010463334              91 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HPr family phosphocarrier protein [Pseudomonas].
ACCESSION   WP_010463334
VERSION     WP_010463334.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..91
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=9502
     Region          1..90
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 mpareieiin klglharasa kfvgvagqfp gctirvgrtp esavdgksim ammmlaagkg
       61 tkihlstege qeqeamdalv alinnffdeg g
//
LOCUS       WP_010463338             203 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Pseudomonas mandelii].
ACCESSION   WP_010463338
VERSION     WP_010463338.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..203
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22455
     Region          4..197
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 maftlpalpy aydalephid aqtmeihytk hhqtyinnln aavegsefae wsveklvasv
       61 rqlpeklraa vinqggghan hslfwevmap hgggkpegal akaideqlgg ldsfkdaftk
      121 aaltrfgsgw awlsvtpqkt livessgnqd splmngntpi lgldvwehay ylqyqnrrpe
      181 yinafynvin wpevatryqa alv
//
LOCUS       WP_010463364             341 aa            linear   BCT 01-JAN-2025
DEFINITION  formylglycine-generating enzyme family protein [Acidovorax
            radicis].
ACCESSION   WP_010463364
VERSION     WP_010463364.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..341
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=37707
     Region          21..327
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 malaavlaca cahagpekta apaswtnslg mvfqqvpags ftmggveppd vlaraypale
       61 prrftdlade gpahtvhirq afylgrhevt vgqfqrfiea sgyqpesead gtggygynaq
      121 ydpattrrgd afegrdprys wrnpgfaqgp dhpvvnitwn daqalarwls rteghhyrlp
      181 teaeweyacr agtrtryphg ddpqgllkna ntfdqeaapl wprwqqhala gsdghaftap
      241 vgsyapnafg lhdmlgnawe wvsdwhgdty yahsprsdpk gpadgtvrvr rggswhtwsf
      301 yarcgyrnwn spetrytlvg mrlvreiapt prppsrgaak r
//
LOCUS       WP_010463400             316 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Acidovorax radicis].
ACCESSION   WP_010463400
VERSION     WP_010463400.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..316
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33072
     Region          141..>307
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mprpalysss rhtrrsppep veqapvptaq satgtdvtlp npsnqpstqa ananlsrrhl
       61 rtlwalitll atlllyslwl hqrpashrit qedidaavlr tletttppsa aaraveaisp
      121 sivrvvgysr skngkeever gigtgvvivd kgviltnlhv vagadriait fhdglettas
      181 itgaqpendl avlqahkvpd dlfaaplrst qdlrpgdhvv avgfpfgigp sasagvisgl
      241 kreftspegk rqlsnliqfd aaanpgnsgg plvtldgevv givtailnpt sartfigigf
      301 avpienaasa vgmppf
//
LOCUS       WP_010463418             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010463418
VERSION     WP_010463418.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..322
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34740
     Region          3..316
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mslleiknln vrfgdknavp vvdglditvd kgevlaivge sgsgksvtmm almgliehpg
       61 ivtadalnfd gknmlklsnr qrrqivgkdl amvfqdpmta lnpsytvgfq ieevlrlhlk
      121 msgkqarara iellekveip gaasrmdayp hqlsggmsqr vaiamaiage pklliadept
      181 taldvtiqaq imdlllalqk eqnmglvlit hdlavvaeta qrvcvmyagq avevgqvpql
      241 fdipahpyse allkaipehs lgatrlatlp givpgrydrp qgcllsprcp yvqdscraqr
      301 paldpksnsl arcfyplnqe va
//
LOCUS       WP_010463449             185 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease [Acidovorax].
ACCESSION   WP_010463449
VERSION     WP_010463449.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..185
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20655
     Region          75..133
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mkvlklsaqg lpqswisleq avihyaagev rwesggqiar frgghnaitg eqsviavnsi
       61 igtkgvpsin pfdlkpgltn sklfardrnv caycgghfhe edltrehivp farngqdhwm
      121 nvvtacrpcn hrkgprtpeh ahmpllyapy vpslwedfil rnrriladqm eflmahvpks
      181 srlla
//
LOCUS       WP_010463434             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010463434
VERSION     WP_010463434.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 238)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 238)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..238
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24842
     Region          28..204
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mairygkgli ggavvvalla llvhwigint iehyrddllf ylqahlilvl vsmlaalvvg
       61 ipagiflsrp smvgraerfm qifnigntvp plavlaialg ilgigsgpai falflasllp
      121 ivrntyeglk nvqgslkeaa vgigmtptqv lwrvelpnav piiiggvrva lainvgtapl
      181 afliganslg slifpgialn nqpqlllgaa ctallallld glvtlasrlw lerglrps
//
LOCUS       WP_010463462             978 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF4132 domain-containing protein [Acidovorax radicis].
ACCESSION   WP_010463462
VERSION     WP_010463462.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15768542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..978
                     /product="DUF4132 domain-containing protein"
                     /calculated_mol_wt=108448
     Region          <477..566
                     /region_name="DUF5724"
                     /note="Family of unknown function (DUF5724); pfam18991"
                     /db_xref="CDD:436893"
     Region          602..782
                     /region_name="DUF4132"
                     /note="Domain of unknown function (DUF4132); pfam13569"
                     /db_xref="CDD:433317"
ORIGIN      
        1 msehweasat qrargqrfea wllgyvqeak dagrlddder airngdadsp fcsalqqtfg
       61 neaeqhltdf fmfpvlhesi pnmraradrv wgfardvndl lteavkkwgr dytcqlalqr
      121 lrhqlshpad atecaaprwm daeraliraq yaepvrshqi adlkaaltrs shpflepapd
      181 tlaqlicdmk ssratldelm dlmerscdtw vdeqfrpppq vedcectgrm rtaeffglte
      241 qadelaqaya rqgplsaewv krlfdlewpr sarvvgacls qeddvlkdfq pealdwvygh
      301 cvkplteait slgqlaqelg vdyesgerrs lsgirfvmag arllaqmpsp ppilglvqtd
      361 aersaaralk licnvqplga aesadlvvel rqfapevllq llrhcraqad evlealgwgs
      421 aaplyrfmre reradaneyf dvpllkehlq ragksgelll awhkkykhlk vtvyrieavq
      481 gvqdkklagm lgklsqehir vwgmtplrdt adlrerfdff kgagkqaskl fgsersanvr
      541 daaaaalvql ahnagfadvt emewsldats qsaqdwswqq ddyavelslv rfqpqlqvrk
      601 agkalkslpp alkkdaglap llaqldllkd qskryriale nlmvsgrala pdqlrelsnl
      661 pmarqlltal ylqtpdgglg llddslaqlr lldadgalad aarpvelplt iahvhsilat
      721 grliacqrha vqsslvqpfk qafrecyvlt paereardvs rrfegrrvkt svlgailsar
      781 gwrvdgsdfd fvarkrlapd iavelslpdv yqfltqeeat vlgeisftrq aepmaleeap
      841 plgfseamrd ldlvitagaa dsdehsaevq harvalvgal lpslglknvs leghhaiiqg
      901 krasyrlhlg tavihvipag ylcivpadka sqkavalpfv dddqrtsevl skllllsadd
      961 kikdpsilaq iegrvaqa
//
LOCUS       WP_010463501             336 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: inorganic phosphate transporter [Acidovorax].
ACCESSION   WP_010463501
VERSION     WP_010463501.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..336
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34991
     Region          19..336
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 metvqtalwv vvllvalail fdfmngfhda ansiatvvst gvlkpaqavl faaffnfvai
       61 fvfhlsvaat vgkgivqpgi vdthvvfgal vgaitwnvit wyygipssss haliggivga
      121 viakagagal vsagilktva fifvspllgf algslmmvgv awifrrarps kvdkwfrrlq
      181 lvsagayslg hggndaqkti giiwllliat gyssasdasp ptwtivscyv aiglgtmfgg
      241 wrivktmgqk itklkpvggf caetggaltl flattlgipv stthtitgai vgvgstqras
      301 avrwgvagni vwawiltipa safvaavayw islqmf
//
LOCUS       WP_010463556             936 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Pseudomonas mandelii].
ACCESSION   WP_010463556
VERSION     WP_010463556.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..936
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=101990
     Region          3..519
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          463..932
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mtlpaaflrd aqqlipqerr fddplstlaf gtdasfyrli pklvirvese devvallkla
       61 qrdqvpvtfr aagtslsgqa isdsvlivlg dnwngreirg qgtqirlqpg vigaqanawl
      121 apfgrkigpd pasinackig givannasgm ccgtaqntyh tlagirlvla dgsrldtedp
      181 asvaafhqsh aallerlatl gretranael aarirhkyrl knttglslna lvdfdepvdi
      241 lshllvgseg tlgfisavty dtvidhpnka salivfpdve tccnavtvlk sqpvsavell
      301 drrslrsvqd kpgmpafvqq lsnnacalli esraasstll qeqlaqimas ltsfpvekqv
      361 dftedpvena rlwairkdtf pavgavrktg ttviiedvtf pveqlaigvn rlielfdkhh
      421 ydeailfgha legnlhfvft qgfnnpeeva ryqafmddva qlvavefggs lkaehgtgrn
      481 mapfvelewg sdayqlmwql krlldpngil npdvvlsedp qihlkhlkpl paadeivdkc
      541 iecgfcepvc pskgltlspr qriviwrdiq akkragvdta eleaayeyqg idtcaatglc
      601 aqrcpvgint gelvkklrgr kathtktanw legnfatalq garftlhvan garmllgapr
      661 laklsatltk lskgqvpqwt nampqpekai rfspvvsdqr prvvylaacv srvmgpaagd
      721 keqmslydkt rgllekagyq vvfpdnqdsl ccgqpfaskg yaeqaehkrq eligallhas
      781 rggldpiycd tspctlrlvq dlgevrldly dpvrfirthl mdrldftpqe apiavhvtcs
      841 tqhlgesqal idlarkcskn vvipegihcc gfagdkgftt pelnahslrs lkdavqfcae
      901 gistsrtcei glsqhggidy hglvylvdrv trvrpa
//
LOCUS       WP_010463599             277 aa            linear   BCT 01-JAN-2025
DEFINITION  ZIP family metal transporter [Acidovorax radicis].
ACCESSION   WP_010463599
VERSION     WP_010463599.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..277
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29109
     Region          <54..271
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mtlvaiilat laagigsvwl aallmrlglg gradsvgpqh llslaagall atafmhllpe
       61 afesqagahd lfatllvgvv ffflldkael whhghehshp eparqdhdhg hahsheghgh
      121 ahhhhaprag gwavltgdsv hcfgdgilia safmadirlg viaavsvlah evphhmgdlv
      181 vlrqtspnrr malvkvslag avtalggvvg yflvgqlqdl lpyflavass sfvyvaladl
      241 ipqlqkrlta retiaqiawl vagmvivtlv sgaahgh
//
LOCUS       WP_010463613             488 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Acidovorax radicis].
ACCESSION   WP_010463613
VERSION     WP_010463613.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..488
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54869
     Region          130..302
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mfyaiplenr ptwrnppwmt vvlilvnmlv fwgpqrseek aqdraaafyv asplpavevp
       61 rfvawleetg dkhlkdaral qkagdhrmll rwmeqedgfq qrlksprfvp pedpqyadwk
      121 aartqyearl papftrqwaq sfekdaelrp vtwltatflh gstghlignm vflflfgfsv
      181 elalgrgwyl afyllggvgg sllagwayad mgsyglgasg avsalmgmya vlyrlrrvrf
      241 fyqlffyfny vtapallllp awianellqh wlsgkgvaym ahlgglltga slmalamllc
      301 kkpmevpvtq daapddgfdt hvanaqrlak gmkfeqalaq wraaaklrpq dqtvlsawfk
      361 taslwpeged fhraarrifr lhahdeqtlq fqhacyrtyf ekakpgarlq pddmarlsrr
      421 faraqqwgda eklfnalhkt apthpelget lgmlvsalch agrraeavaw gpllqqlapg
      481 svalrglg
//
LOCUS       WP_010463653             319 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Pseudomonas].
ACCESSION   WP_010463653
VERSION     WP_010463653.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..319
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=34442
     Region          58..294
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mrlqlfnaai ivasmaatdp slageastas asqpdktpst haakqeiklt rltpeywrvt
       61 fhnppyniyg petmpqlnev vtaietdpkv vvvvfdsdvp dfflthydfv ppltdttslp
      121 ngptglpplp dmlvrlskap vvsivsirgr atgvgselal asdmrfasre kailsqweig
      181 aalvpgggpm arlprlmgrg ralevlltgn dingelaery gyvnralpda eldafvdtma
      241 rriarfdkqs iadikrlvda aslppneaia aewdgfigsv krpaaqqrit qlmelglqkk
      301 advekrlahy tgtlgeask
//
LOCUS       WP_010463652             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Acidovorax].
ACCESSION   WP_010463652
VERSION     WP_010463652.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28367
     Region          3..253
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqkngplala fnalvitfml apllvvciva ftphntltlp ttefslrwfk avfehsdfvq
       61 sfwnslwlal asatlatvla vpagiaitry efagrgflng lflspliiph lvlgvallrl
      121 fallggtgsf gwlvfahali vtpytlrlvv aalvgfdrsa ehaalslgas qatvftritl
      181 pmilpgvtgg wmlafinsfd evtmsifvts pstvtlpvrm ymyatesidp lmaavsalmv
      241 altacamvll drvygldrvl vgrk
//
LOCUS       WP_010463632             191 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Acidovorax].
ACCESSION   WP_010463632
VERSION     WP_010463632.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..191
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21503
     Region          12..191
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mstpqpdrel mdlldriaaq ddsalkrlye rtssplfgla lrivrnrdva edvlqeafls
       61 iwrgasnyra slsppmawmg livrsralda lrkrtsdrad lmnelddela qtlegdspnp
      121 mdaadaseqs falhhclgkl dhkqrevvsl aylrdqshge laeqlklplg tvktwirrgl
      181 eqlrtcmary a
//
LOCUS       WP_010463663             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Acidovorax].
ACCESSION   WP_010463663
VERSION     WP_010463663.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21832
     Region          14..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpkalteaev qdfrlrllsv aerafadhgv dgvsvrqlaq elgcsamtpy ryfrdkneil
       61 aavtaaaldr fseslelafa tetgawersa avrqaylgfa fenprayklm fdlphpdvag
      121 fpdlaraalr aeqimaapie llvkggflag esrllgrifw saihgavslq lagkldsdpa
      181 fehvlenmlr flvagasadh p
//
LOCUS       WP_010463654             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Acidovorax].
ACCESSION   WP_010463654
VERSION     WP_010463654.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..290
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31436
     Region          5..288
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mnlattllhk kaapwwlsgp alllftvlll vplaltavls fnafdpatgv kageftlehy
       61 ahvftdsyyh tifwrtfwia glvtlicvai gapeayilsr mgnpwrsill lvvlapllvs
      121 vvvrafgwsm llgpeglvng alqwlgigpv kmlyteiavv ialvhvmlpf mvipvwtslq
      181 kldpgvenaa lslqatpftt lrrivlpqvl pgilsgsliv fglaassfai pgllggrrlk
      241 mvatvvydey lhelnwplga aialtllvan lvvmlsynrl vegrykkalg
//
LOCUS       WP_010463687             211 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Acidovorax].
ACCESSION   WP_010463687
VERSION     WP_010463687.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..211
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22127
     Region          10..209
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 matatdvpst nlqalihaaa ggdhaafaqv yqrthvhlfg vavrmlgqgq aaedvlqeay
       61 vsiwknagsy rsevggqpiq pmtwliaivr nkaldalrar arrpesawhd taelagsdgd
      121 gsdasgaasa ltpapsalhl leqatqalri egcmnalegs yrqslalayy qglshsevaa
      181 qmgaplgsvk awirrglerl knclatqgvg a
//
LOCUS       WP_010463738             508 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [Pseudomonas].
ACCESSION   WP_010463738
VERSION     WP_010463738.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..508
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53998
     Region          15..491
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(72,74,78,81,85,118,121..122,131..138,143,146,149,
                     242,246,249,252,254,427,429..430,432..433,436,439..440,
                     442,444..447,456,460,462,476,483..488,490..491)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(158..161,169,184,187,217,234..237,240,258..260,292,
                     392,394,420)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(161,258,289,292)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnasltpnet tvqtvkllid gewvesqtte whdivnpatq qvlakvpfat aqevdaaisa
       61 ahrafqtwkl tpigarmrim lklqalireh skriavvlsn eqgktiadae gdifrglevv
      121 ehacsigtlq mgefaenvag gvdtytlrqp igvcagitpf nfpamiplwm fpmaiacgnt
      181 fvlkpseqdp mstmllvela ieagvpagvl nvvhggkdvv dalcthkdik avsfvgstav
      241 gthvydlagk hgkrvqsmmg aknhavvlpd anrvqalnal vgagfgaagq rcmatsvvvl
      301 vgaakqwlpd lkalaqkltv nagsepgtdv gpviskkakq rildliesgi kegakleldg
      361 rdvtvpgfek gnfvgptlfs gvtpemqiyt qeifgpvlvv levdtldeai alvnanpfgn
      421 gtglftqsga aarkfqteid vgqvginipi pvpvpffsft gsrgsklgdl gpygkqvvqf
      481 ytqtktvtsr wfdddsvndg vnttinlr
//
LOCUS       WP_010463720             191 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Pseudomonas mandelii].
ACCESSION   WP_010463720
VERSION     WP_010463720.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..191
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=21570
     Region          4..186
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mskrmlvilg hpstdsfcga lsetyvqaak daghdvrllr ldaldfdpvl hhgyntiqpl
       61 epdllqaqad itwaehltfv ypiwwggipa lmkgfldrif lpgfafkyre gkafpdkllk
      121 grtahllvtm dtppwyykwi yhmpglhqmr kttlefcgik plktltfgpi lgskstqrda
      181 wleqarvtag s
//
LOCUS       WP_010463734             189 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Pseudomonas].
ACCESSION   WP_010463734
VERSION     WP_010463734.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..189
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20428
     Region          6..70
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mnnplelenv ivstreilaq llvmsvddid enssivedls adsldivdls fqlgrqygct
       61 lpktsvldha vavcgdagef lasgriteng kalleqslsa yspdqlqsgm qpaqvfaatt
      121 vrnwaqqcrn lfnylpqncp dcgaqkavln erqqvvcdac sarlvpadgd evsrqlveqf
      181 vathvketv
//
LOCUS       WP_010463770             232 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Acidovorax radicis].
ACCESSION   WP_010463770
VERSION     WP_010463770.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..232
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25092
     Region          62..156
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mtdnepqavk aryarrdaav dearyslyan aaalqaqqer lralariwqa hgwsslayrp
       61 mlevgcgsag nlhdlvrlga tpacltglel lperaaaara slpagvpive gdaalapvqp
      121 asqdavlaft lfsslldedy rrhlahviwq wvapgggvlv ydfvvnnpan sdvqgiplre
      181 lsilfpeaqi hsrrvtlapp larrlpapai apasallwfl rthritwavk ph
//
LOCUS       WP_010463813             405 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Pseudomonas mandelii].
ACCESSION   WP_010463813
VERSION     WP_010463813.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43120
     Region          10..389
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(18..19,22..23,26,58,111..112,114..116,119,139,
                     142..143,146,221,224..225,228..230,233,258,262,317..318,
                     322,326,341,344..345,348..349,352)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mnpstrnaql iiaarlvsdf gvflnmvala tyvyllsnsa msvgiflasr vgggvfasli
       61 gtsfyrrwag rmpliafdll ragllglllv lpvaqqalll pliafglgfg nsmfaiglns
      121 qlphliegeh llktnawits assaamvggs lvagllvaaf gfetvfalnv vtyllaalfi
      181 lplrfsrpas dpeqaqprse whalrqglrs tpvvaamlav tmadtlgsaa hnvgfpiisr
      241 lltpesastt lglmlavwac gkligarias rlkgadnahl errfffgvll mscgfilmfq
      301 qqtlyglllf slpaglgdgf sevglmsrlq repdslrlpi fslltllqmt gfgvgmliaa
      361 pfyswwtpga vvllfhgvpl ttllvvkvla ikgervtrss ptpgs
//
LOCUS       WP_010463833             294 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [Pseudomonas].
ACCESSION   WP_010463833
VERSION     WP_010463833.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..294
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32437
     Region          80..292
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mlkpallilv climlgvsir lllkglrqtg tervlnrlaq gqpqlvvekt swaglerafl
       61 raglgrpneq lgrwmllwaf gtligfaagg wiglvvcllv pplafrlfis wryqrrlkrm
      121 ieqlptlldh tvrslksgrt ladavlgaih aadnplkeam grvqrnvqlg vslpdaasdf
      181 aelyekdelr lfalglkvnh ryggnasell enlikmirer eqaarqlsam tgetrvtawv
      241 lgslplglat yflaanpayl lamwhdssgq mmlasafglq avgslalwrm lrsv
//
LOCUS       WP_010463960             888 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Acidovorax radicis].
ACCESSION   WP_010463960
VERSION     WP_010463960.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 888)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 888)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468444
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..888
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91927
     Region          <191..410
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          <233..811
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mqamlallrt fswqdlrhhp wrsaaavaav mlgvalafav hvinasalde fsqavravng
       61 qpdlelramq gslpealygq lathpqvara spllelsava ralrqgsgta tvptppptpl
      121 rvlgvdalll pamapalmpr pwagadrlal fapatvflnt aalqalglpt tpptsaepsp
      181 qlllqaglqq wpvrvagtva aggaplavmd igaaqdlfgr agqlsridlq lqpgtdrsaw
      241 eqavraqpgw paqvvfaqpg daaqrisnls rayrvnltvl alvalftgaf lvfsvlalsv
      301 aqrapqfall avlgatprqr lalvlaesav lglvgsaagi algtalaaaa lrllggdlgg
      361 gyfagvqpvl qwsapaalay galgvlaalv ggwwparaaq tlppaqtlkg lgtvssqadq
      421 gwigiiliai gailtsappv fdiplaayla iglllvggia vlpwamawll hrlqplaarh
      481 alallalera rrmrgtaaia vggvvaslsl avaltvmvss frgsvtqwld avlpsplyvr
      541 salgapgsea allpagfaes vaqlpglarv qalrasplql datrpalmvi srplgtapar
      601 hlplvgealp vpagrtgvyv seavvdlygl rpgmewpals daftplaldr qaqpaifyia
      661 gvwrdyarqs gavamdravw lrltgdarts dlalwpaeei nitalqdair alaaaqagrv
      721 ppardgtsaa dealvefvsv gairerslri fdrsfavtyw lqavaigigl fgvaasfsaq
      781 ilarrkefgl lahlgltrrq ilavvagega awtgvgaaag lllglavsvv lvhvvnpqsf
      841 hwtmdlslpt grllglcvav vasgtvtawl agraaagrda vmavkedw
//
LOCUS       WP_010463846             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peroxiredoxin [Acidovorax].
ACCESSION   WP_010463846
VERSION     WP_010463846.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..161
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17802
     Region          7..149
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(42,45,120)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 maivvnkplp efeanatggl kvsntshlgq ilvlyfypkd ntpgctteam qfrdkykdfv
       61 kagaavfgvs rdnmkshddf keklelpfel iadteekmch mfgvvknkim ygkkvkgier
      121 stfligpdgl lvqewrglkv pghvdevlka vksikalkka a
//
LOCUS       WP_010463976             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Acidovorax].
ACCESSION   WP_010463976
VERSION     WP_010463976.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..277
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30079
     Region          31..275
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mkrtpllvsl tlaiavtagc atldakqrew ifqpsdrswg gaqstadmqd vwidfqsdas
       61 gkaerlhglw laheradapv llylhgarwn vagssgrirr mqelgfsvla idyrgfgqss
      121 aalpseatag edaraawdwl gqqqpgkpry ifghslggai aidlarqvpd eqgtmvegtf
      181 tsipevvstf kwgwlpvsgl itqrfesvrk vaeigspllv vhgsqdsliq palgrklfea
      241 aqepkqfilv eggshhntns vgqglyream aslfklk
//
LOCUS       WP_010463980             351 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphotransferase enzyme family protein
            [Acidovorax].
ACCESSION   WP_010463980
VERSION     WP_010463980.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..351
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37959
     Region          20..336
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mfalnaqsia qttptgeaia qavvsfwalg pvkhcvlmrr gfnqvyelhf dngrhaiarl
       61 saerprgepn iayetalllh lqargipvaa plaagdgtfs lvlslpegpr almlfdflpg
      121 dppgeslvdi eatgrglaql htaaqdyagp asryvldlpe lldaslerml qaptvdgpla
      181 refsalardl herfatlhgl thvrchgdch gsnnfmsdgp hgtgeghrva affdfddtgp
      241 gllayelsvy lwvllprsle tptsaatqer wrrylagytg vravpevdla aiapclavrq
      301 fwvmgeyagr ipvwgtqamp thwlrkqvpl mrawmdmpla dgniggapaa a
//
LOCUS       WP_010464030             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Acidovorax].
ACCESSION   WP_010464030
VERSION     WP_010464030.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33865
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdqiqamrif vrvveagtft raadslslpk atvtkhvqal eerlrvklln rttrrvtvtp
       61 dgaayydrtv rlltdlddie asmtnaranp rgrlridvgt avaqllliph ladfharypd
      121 iqldlgvsdr ivdligdnvd cvirggelsd qslvarrign lefitvaspd ylarkgtpah
      181 pleieekhts llyfsphsgr hyplefrkdt esidisgpyq lsvneanayv tslvaglgig
      241 qitsfqaerh lksgalvqll pqwtqpvlpv yvvyppnrhl sakvrafvdw aaelfrseah
      301 lqrsg
//
LOCUS       WP_010464038             226 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Acidovorax radicis].
ACCESSION   WP_010464038
VERSION     WP_010464038.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..226
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24002
     Region          144..226
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mttinpfdrp vwasltfapd laeggglakr yrrdvnlfas ardddgasla avadlvtege
       61 svfvlqaqpi pvpkgmqalr raqgvqmlag raiaaetgae vvvalgdada aemlalarlt
      121 epgpflarth tmgrfvgirs dgvlvamage rmrfeggtev sgvcvhpdfr grgfarrlss
      181 vvahaiqqrg dqpflhawat neaaialyes lgfeirtemq vavlgr
//
LOCUS       WP_010464070             394 aa            linear   BCT 01-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Acidovorax radicis].
ACCESSION   WP_010464070
VERSION     WP_010464070.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 394)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..394
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40989
     Region          4..392
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mptpdivlcs pvrtpigsyg gslketpasa lgaavireai hrsglaaeav dtvvmghviq
       61 agtrmnparq aaiggglpvq vpaltvnrvc gsgaqaiata aleiaagyas aavaggmenm
      121 dqapylvpga rwgqrmgdap mldsmlrdgl hdafsgqhsg whtedlvary gitredqdrw
      181 aarsqqrfsa aqaagkfaee ivaielssrk gpvsfsrdea hrpdttvesl aklkpafrkd
      241 gtitagnapg lnsgaaamiv aergfaekhg lqpwarlvsh gvaavepgmf gigpvpavkl
      301 aleragwkht diqrieinea faaitlaclr eldlpedivn veggaiahgh aigatgavlt
      361 trllhsmrrd glrrgivtlc igggqgiala leml
//
LOCUS       WP_010464158             334 aa            linear   BCT 01-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Acidovorax radicis].
ACCESSION   WP_010464158
VERSION     WP_010464158.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..334
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=36076
     Region          40..119
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(40,52..53,55..56,58..59,62..63,65,72..79,81)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          108..325
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mqgsagtvdd llneesegla eesgselrsa qigagqhaar ldraladlvp efsrsylqql
       61 laqglvslng kpvtkvatrv kvgdqvvlem rptlqsqafr pepmeievvh edahllvvnk
      121 paglvvhpap gnwsgtllng llardekalt vpragivhrl dkdtsglmvv ardrstmdal
      181 valiaerkvq rqylalahga wsgpksrtvd apvgrdprnr lrmavvdlvl hagklartdv
      241 rwlagsdegc wvqctlhtgr thqirvhmas lkhplvgdsl yggapvgamq rqalhayrla
      301 fvhpvtgeal efhapvpedm rqalslwglg ynap
//
LOCUS       WP_010464192             644 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Pseudomonas].
ACCESSION   WP_010464192
VERSION     WP_010464192.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..644
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=67670
     Region          209..643
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 msavlsllqs rllrpvfvtl giallvqvlv avaltrstvt aleadlgvrl gvdsqklsge
       61 leqagrevts sldnlststr qrltaglstr lkdeqvqlra tlekdlkdsa ndmaqllasv
      121 apramwdsdv ptlsefarra qrnpnvlfvv yddatgqhlt rylnrenpin kallekgqge
      181 raldkvldaa kndpsvyyle asinpngvei gkvlmgvsta svetdlaald krfaaliasg
      241 dqlvgdslkg aaadsatamr arltsaqata semkanttst vqeaastlrw rigmflalvg
      301 cgvllllavv lgrrvvnrlk mliaamddla agegdltkrv qinskdeigd maaavnrfvd
      361 klqpivreag dvaqrtgvei gamtlrnaga daaagmqrde vaeslralsq madeaqsesn
      421 amqaalqqvv dirsatdent rtsakvgsli ealagqvdtg akvierlaqq seqievvltv
      481 ihgiaeqtnl lalnaaieaa ragetgrgfa vvadevrala sktqsstgdi qahivalqqg
      541 areavaaigq agrqanegll vlrdsarlqq svqasveqvh aaiglatqaa ahqaqgaqav
      601 rgrvetihaq aekaaqavve ttasgkvldg laaqlkaslg qfra
//
LOCUS       WP_010464214             488 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TrkH family potassium uptake protein [Acidovorax].
ACCESSION   WP_010464214
VERSION     WP_010464214.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..488
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52722
     Region          67..488
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mtdmfpvlrv lgilvmifsl smglplavsl wtrdgvwhvy plamgatlla gawlwwrlrl
       61 frqelqprhg vmlvslvwml lplsaalplm laghhtghpl sfthayfeav sgltttgstv
      121 lagldampvs vnvwrtflqw mggmgilila vavlpllgvg gsqlfkaeaa gplkdtkltp
      181 rmtgtakglw gvyalfsvlc glafwaagme pldalmhmfa tvslgglssh dlsfgyfqsp
      241 lleaicivfm lvascnfaly fvafrkgqwg gfwrdpelra tlfsligggl lvalllwvkg
      301 vyapldalrh gmfnlvsmat ttgfatvdyl awpvfapvfm lllsgvatsa gstgggikmv
      361 rmlilvkqar remnrlvhpr avqpvrlgda vvdnrvifsv lafmlvyggt vfglsmvmll
      421 tdldpvtafs vvlasvncag pglgsvgpas nyavltdfqi wvctlgmllg rleilsfmal
      481 ltpafwrr
//
LOCUS       WP_010464368             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PDR/VanB family oxidoreductase [Acidovorax].
ACCESSION   WP_010464368
VERSION     WP_010464368.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34331
     Region          12..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(53..54,56,70..72,78,80..81,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(53,55..56)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(78,81,84,91)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          238..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mtaqetlqvr vvrkqaeadg iasfelarvd gaalppfsag shidvhlpgg ltrqyslcna
       61 sheshryria vlrdpasrgg svamhdsvhe gdvitistpr nhfalhpaqh tvllaggigv
      121 tpllcmadrl artgadyalh yctrsaerta fageiaaspm aprvhfhfda gtpeqkldla
      181 avlaapgpdk rlyvcgpagf idhvvntaka mgwaqdhihl eyfgapaqdt sgdqgfevri
      241 astgkvyaia pdvsvvealr gegidiltsc eqgvcgtclt rvlegevdhr dmyltdeeka
      301 aneqfmpccs rarskllvld l
//
LOCUS       WP_010464357             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Pseudomonas].
ACCESSION   WP_010464357
VERSION     WP_010464357.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..256
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28358
     Region          1..249
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mrrvvfnqkg gvgkssiacn laavsasegy rtllvdldaq anstqyltgl tgddipmgia
       61 dffkqtlssg pfskknkvdi yetpfenlhv itataeladl qpkleakhki nklrklleel
      121 gedydriyld tppalnfyav saliaadrvl ipfdcdsfsr qalygllaei eelkddhneg
      181 levegivvnq fqaraslpqq ildeliaegl pvlpvyltss vrmreshqan tplihldprh
      241 kltqqfvelh nllena
//
LOCUS       WP_010464405             118 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Acidovorax].
ACCESSION   WP_010464405
VERSION     WP_010464405.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..118
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12670
     Region          4..112
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 msatryqgsc hcgkvafeve gtidsglacn csmcgrrgsl lwfvprdalr lttpeadvat
       61 ytfhkhviqh rfcpacgihp fgegvdpkgn rvaavnlrcl dgvdldavpv hhydgkav
//
LOCUS       WP_010464422             324 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010464422
VERSION     WP_010464422.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..324
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35082
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..275
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,147,161,163,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,190,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mainelraia tfakaaelgs lrqaasaqgi tpqaaslalg qleshlgvrl fhrttrslsl
       61 teegrqflea aqpglstlqr avhgarrgre eiagplriva prsvmlevvw pvldafcrry
      121 plvepdvqld drignwvedr vdvgfrsgyp peggviarrl malqlvacat pdylarhgtp
      181 triedlaqhr csgfrhpttg kpmpwefqvg ddivahaipp afcvndiele aravlgghai
      241 gqlvgvtaap lvrsgqlvpv ltefvpqhlg lyvyygsraa qpararafid lavemladnp
      301 afglsaqelr gtaprprrrk psva
//
LOCUS       WP_010464401             479 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Acidovorax].
ACCESSION   WP_010464401
VERSION     WP_010464401.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..479
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48739
     Region          17..464
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(24..25,28..29,32,64,114..115,117..119,122,143,
                     146..147,150,275,278..279,282..284,287,315,319,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlsiegrar wpalillclg elmivldtti vnvalpsika dlgftetslv wvvnaymltf
       61 ggclllggrl gdlyghrrlf lagitlftva slacglantq gllvaaravq gvggavvsav
      121 alslimnlft epgeraramg vygfvcaggg sigvllggvl tsalswhwif lvnipvgvai
      181 yaaclallpg gkgqahgqrl dvagavtita slmlavyaiv ngneagwtsl qslgllgasa
      241 alllvflyve shvaaplvpl allrlrnlai snvvgvlwaa gmfawfflsa lymqlvlgyd
      301 amqvglaflp snlimaacsl glsawvvmry girstlgwgl vlatvglalf alapvdgqfv
      361 lhvlpgmvll gvgagialnp lllaamgdvk pedsglasgv vntafmmgga lglavlasla
      421 dartgalrea gasvqmalng gyqlafwvaa ggslvaallg glvlrpaqps gagapvavh
//
LOCUS       WP_010464448             261 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA-uridine aminocarboxypropyltransferase [Acidovorax radicis].
ACCESSION   WP_010464448
VERSION     WP_010464448.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Funk,H.M., Zhao,R., Thomas,M., Spigelmyer,S.M., Sebree,N.J.,
            Bales,R.O., Burchett,J.B., Mamaril,J.B., Limbach,P.A. and Guy,M.P.
  TITLE     Identification of the enzymes responsible for m2,2G and acp3U
            formation on cytosolic tRNA from insects and plants
  JOURNAL   PLoS One 15 (11), e0242737 (2020)
   PUBMED   33253256
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Meyer,B., Immer,C., Kaiser,S., Sharma,S., Yang,J., Watzinger,P.,
            Weiss,L., Kotter,A., Helm,M., Seitz,H.M., Kotter,P., Kellner,S.,
            Entian,K.D. and Wohnert,J.
  TITLE     Identification of the 3-amino-3-carboxypropyl (acp) transferase
            enzyme responsible for acp3U formation at position 47 in
            Escherichia coli tRNAs
  JOURNAL   Nucleic Acids Res 48 (3), 1435-1450 (2020)
   PUBMED   31863583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..261
                     /product="tRNA-uridine aminocarboxypropyltransferase"
                     /EC_number="2.5.1.25"
                     /GO_function="GO:0016432 - tRNA-uridine
                     aminocarboxypropyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=28346
     Region          38..251
                     /region_name="TapT"
                     /note="tRNA U47 aminocarboxypropyltransferaseTapT/TuaA/
                     YfiP, DTW domain [Translation, ribosomal structure and
                     biogenesis]; COG3148"
                     /db_xref="CDD:442382"
ORIGIN      
        1 mtqpvdpsat gvatpatpha vsrlrterla rsakpflarg gpkgercagc rlvpshcica
       61 lrpvlptrag mcllmadiep lkpsntgwli advvadthaf gwartevhpg llalladpqw
      121 qpyvvfpgef vapervvtqi glgapsdgkr plfvlldatw pearkmfrks pyldrfpvls
      181 lqpeqlsryh lrrstrtdhf ctsevgalcl alagelqaaq tleayldvft hhylqakhql
      241 ppdwageahq alrnasigga g
//
LOCUS       WP_010464469             460 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Acidovorax radicis].
ACCESSION   WP_010464469
VERSION     WP_010464469.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..460
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47222
     Region          41..437
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(42,77,124..125,127..129,132,155,158..159,162,272,
                     275..276,279..281,284,314,318,367..368,372,376,392,
                     395..396,399..400,403)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mpntpassts aaasaslids pqaawrlltt lglvvlgnss myvvsvvlpa vqaefgvgra
       61 daslpytlmm vclglgglwt grmadrhglm pvlcvgavav cggfvwagls gsiwifglah
      121 glmgligssa tfaplmadta lwwnkrrgia vaicasgnyi agalwppivq hgieaigwrq
      181 tyvlmglvcg agmlllalrm rqrapmvlmd vaaaaaatav passaslpsa vgaaagaass
      241 tataapaplv psavdrsrpf glrpvhaqll lcvagvaccv amampqvhiv ayctdlgfga
      301 argaemlslm lacgivsrlv sgvicdrigg vrtlllgsal qgvglalflp fdglvplyvi
      361 samfglfqgg ivpayaiiir eyfapqeaga rvgavimatl igmalggwms gwifdvtgsy
      421 qaafingmgw nllnlsimgw lywrvrrqga vvgrvqpsag
//
LOCUS       WP_010464541             244 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TerC family protein [Acidovorax].
ACCESSION   WP_010464541
VERSION     WP_010464541.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..244
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25713
     Region          27..190
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 meflaspefw lalgqiiiid illggdnavv ialacrklpp aqrtkgiiwg tagaivlrvi
       61 liafamtlla lpflkfvgal llvwigvkll apdedghgdv qgsdkllaai ktiivadlvm
      121 svdnviaiag aaqnagehsf llvvlgllis ipiivwgsql viklmerfpm iitlggmllg
      181 wiaggmlvtd pafsnpdkwq wmlklpqtdv vkygasvaga llvllagkfi varraaaapa
      241 eqqg
//
LOCUS       WP_010464567             151 aa            linear   BCT 01-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Acidovorax radicis].
ACCESSION   WP_010464567
VERSION     WP_010464567.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..151
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=16975
     Region          17..119
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mhppraplta edavtrvvaf fehlspadva tigefyapqa rfkdpfnevq gvpaiqaifa
       61 hmfealeqpr fvvtgrvvqg tqcfltwdfl fafkgfdkgv tqtvrgashl vldeqglvtl
      121 hrdywdaaee lyeklpvvga lmrwlkkran r
//
LOCUS       WP_010464576             439 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S41 family peptidase [Pseudomonas].
ACCESSION   WP_010464576
VERSION     WP_010464576.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..439
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46315
     Region          51..392
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mlhlsrltsl altialviga plafaaqpap avapagtaat tkaplpleel rtfaevmdri
       61 kaayvepvdd ktllenaikg mlsnldphsa ylgpedfael qestsgefgg lgievgaedg
      121 fikvvspidd tpaskagiqa gdfivkingq ptrgqsmtea vdkmrgkigq kitltlvrdg
      181 gtpfdvtltr aiiqvksvka qllesgygyi ritqfqvktg eevskalakl rkdngkklng
      241 iildlrnnpg gvlqsavevv dhfitkgliv ytkgrianse lrfsatgkde seavpmvtli
      301 nggsasasei vagalqdqkr avvmgttsfg kgsvqtvlpl nndralkitt alyytpngrs
      361 iqaqgivpdi evrrakitne qdseyfkead lqghlgngng gadkpsgsss kakampqddd
      421 yqlaqalsll kglsitsgr
//
LOCUS       WP_010464638             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010464638
VERSION     WP_010464638.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..231
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24909
     Region          3..228
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mtidlygfgp alaagalmtv klalsalclg lvlgllgala ktspykplqw lggtystlvr
       61 gipellwvll iyfgtvnlmr algeffgnpd lelnafaagv ialglcfgay atevfrgail
      121 aipkghreag valglskfri ftrlimpqmw rialpglgnl fmilmkdtal vsvigleeim
      181 rhaqigvtvs kqpftfymva afmylgltil amtgmyfmek raargfarst q
//
LOCUS       WP_010464629             274 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AzlC family ABC transporter permease [Acidovorax].
ACCESSION   WP_010464629
VERSION     WP_010464629.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 274)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..274
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29282
     Region          16..>175
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 msrraaigst lrhpsfrvaa idmagtavgi gawglvtgvv mvksglpvgi aifmslvvya
       61 gsaqlavipl mavgaplwvv wltascvnlr fvifssmwrs yfvhlplrqr lavgyfsgdv
      121 iyvafmkrfp eprpqpeqvp yfwgaattnw lawqvpsiag illanavpls wglgfagvla
      181 llgvllsllf dratwlatgv aataaiaafa lplklnilva iaaavaagll meavdrrrhk
      241 pelvllpads vlppeereqv eagdvvplre erhp
//
LOCUS       WP_010464664             323 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Acidovorax].
ACCESSION   WP_010464664
VERSION     WP_010464664.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..323
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34589
     Region          70..314
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mslrrtltft tlaaltlata saqaqttahn ggrlraliaq kqaaaapaal sagvqriadv
       61 pygtdpaqrm dvyvptsptt gtnslvasav rapvifmvhg ggwrhgdkam grvvqekvnr
      121 wvpkgfilis inyrmlpdap vavqerdvqa almaaqqrag twggdpsrfi lmghsagahl
      181 vallnarapq alregawpwl gtvsldsamt nvparmraph lplyddafgt dpaywvamsp
      241 fhqwtvgapp mqmvcsaqra ddpcqqsdam arhvrnqggr aevlpqdldh geinaqlgle
      301 sdytraveaf mgsldaevar rlq
//
LOCUS       WP_010464724             137 aa            linear   BCT 01-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Acidovorax radicis].
ACCESSION   WP_010464724
VERSION     WP_010464724.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..137
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=14574
     Region          26..119
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mntvetlehp ttiptaataa pdlaaryiaa wnatdgaqrd ylvrstfssd vqyrdpmieg
       61 qghdglaali agaqqrfagh rftllgtpeg hhdvvrfswa laaegaepva rgtdvaeida
      121 hgrmrrvtgf ldyvaga
//
LOCUS       WP_010464791             296 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudomonas mandelii].
ACCESSION   WP_010464791
VERSION     WP_010464791.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..296
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33047
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..291
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(100,104,143,157,159,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(101..102,106..107,109..110,113,117,119..125,186,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdqvkamkvf vriyerssft laaedlslpr atlthtlnqf eawlgtrlle rstrrvrptl
       61 dgeayyqrcv hllaeleeae lafrgcapkg rlrvdlhgtl arhfvipalp qfmerypdie
      121 lsiseadrfv dliaegvdcv lragtlsdsa ligkrianlr qitcaspayl rkhgepqsle
      181 dlkhhravny vsrttaklfp fefmvdgelk evaiegavsv fgaeiyaasa iaglgliqcp
      241 hyrmeaqisq glvqevlidt pppsmpvsvl ypqnrhmspr vrvfvdwlge lftgav
//
LOCUS       WP_010464816             373 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Pseudomonas
            mandelii].
ACCESSION   WP_010464816
VERSION     WP_010464816.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##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="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40787
     Region          30..370
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtaaiqrrle ipephkaeqt elhpdlnrah vrfiglgkty tgqqgpvaal hgidlaiqrg
       61 evfgiigrsg agksslirti nrleqpssgr vlidqvdige fdedrlvalr rrigmifqhf
      121 nlmsaktvwq nvelplkvag vpkekreqkv rellelvglq gkhkaypaql sggqkqrvgi
      181 aralvhdpei llcdeatsal dpettqsilg llreinqrlg ltivlithem avirdicdrv
      241 vvlehgkvve qgpvwkvfgd pqhevsktll aplqhalpee lqsalrpqpq ssdaavvlrl
      301 rftgsatdep dlaalfsalg grvrllqggv eriqghalgq lllavtgssl gaeqlrqrag
      361 hwaqqvevlg yvv
//
LOCUS       WP_010464845             394 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Acidovorax radicis].
ACCESSION   WP_010464845
VERSION     WP_010464845.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..394
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41298
     Region          3..349
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mnknlwllal cqglfltnnv vfiainglvg lqlapfgwma tlpvmgyvvg galstplvar
       61 tqmrwgrkvs fqiglavava saalcawaaf sasfwllcta tlvagyysan gglyrfaaae
      121 lakpdyreka vslvlaggll gavagpnlas atrtlfpvpf agayialigv allsmlcmta
      181 irfeaqpvvl naagqreqgr plsvlmrqpa fivaivgaal gygvmnllma atplamqvcg
      241 fdfdasalvl ewhvigmfap gfvtghlikr fgvlpimgtg vllnlacvav almgvelhhf
      301 gialfflgvg wnflftgstt lamtayrpee kdraqaainf cvyatlalsa fssgvlvttq
      361 gwtllnagsl vpivvtglal awlgvqrkrv stga
//
LOCUS       WP_010464869             188 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TMEM165/GDT1 family protein [Acidovorax].
ACCESSION   WP_010464869
VERSION     WP_010464869.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..188
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20001
     Region          1..188
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 meaffistai valaemgdkt qllalvlaar frkpwpivfg ilvatlvnhg lagavgawvt
       61 tflgpqvlrw ilgasfiama vwmlipdkld egeadgsprw gvfgttvvaf flaemgdktq
      121 iatvmlaaky naylwvvagt tlgmmlanap vvwlgeritr kvpiravhlv saaiflvlgl
      181 laifssag
//
LOCUS       WP_010464851             290 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Acidovorax radicis].
ACCESSION   WP_010464851
VERSION     WP_010464851.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..290
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30706
     Region          32..267
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mtseetlpst lttftasdge nlavqdwplp egepqrgtvl lvhglgehvg rydavarrln
       61 awgfaargyd qyghgessgp rggltsdlrl lddladmvda trarlpagqp lvllghsmgg
      121 lvasrfvamn lrpvdalvls spaldaglga vqklllatlp riapnlrvgn gldaqylshd
      181 pavvaaylad plchdrisar larfianggp atvaraahws vptllmwagg dklvnpagsr
      241 afaaaapkal vhahcfeplf helfnespel adpvfdllqq wlvqrcpvas
//
LOCUS       WP_010464936             236 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Pseudomonas mandelii].
ACCESSION   WP_010464936
VERSION     WP_010464936.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..236
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26461
     Region          16..229
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtqkpnplss ikvngpipah larsvieetl rsaildgrip cgtalrqqdl adlfgvsrmp
       61 vrealrqlea qallnviahk gavvaplvqg davetyalri llesealrls ipllekedve
      121 raakhiddle mehdyseigr lnrlfhmaly ckapnqrllr lvedglneee rflrfnleam
      181 glgklsqedh ralllavedr nvelavelle hhlnrgvevi trylnspeal nkktpr
//
LOCUS       WP_010464963             159 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Acidovorax radicis].
ACCESSION   WP_010464963
VERSION     WP_010464963.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..159
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17143
     Region          6..154
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 maphiatvtw qrgnddfldk ryhrahtwhf dggatvaass sphvvplpys daaavdpeea
       61 yvaalsschm lwfmdlasra gfrlnsytda avgtmakneq gqlvvtqvql spvtrfdaah
      121 apsaaqldyl hhrahascfl ansvktridc apvlevega
//
LOCUS       WP_010464997             175 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Acidovorax radicis].
ACCESSION   WP_010464997
VERSION     WP_010464997.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..175
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18955
     Region          9..141
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mphptlafpl eggcacrhvr yrmetaplfv hcchcrwcqr esgasfalna mieadrvtpt
       61 vgavelidtp sesgfgqkva rcphcqvavw shyagagplv afvrvgtlda pdhlppdvhi
      121 ftaskqpwvv lppgtpavae yydrealwpa aslarrqtll priaayrtam gldpa
//
LOCUS       WP_010465016             169 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Acidovorax].
ACCESSION   WP_010465016
VERSION     WP_010465016.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..169
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=17738
     Region          <42..169
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mrvfhslala actaallalt gcgtsrppsp sfpsssapsr ttppltadqa hdiaihalgl
       61 vgtpyryggn tpdsgfdcsg ligyvyrnqv gtppprtvaq lnswgypidg gelragdlvv
      121 fgtgrqpnha giyvgegrfv hapstggtvr ldqlqsrhws rqnaafrrp
//
LOCUS       WP_010465034             265 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Acidovorax radicis].
ACCESSION   WP_010465034
VERSION     WP_010465034.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..265
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27410
     Region          12..254
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mkntaaapta plllerngai atlrfnrpda lnaidvpman avlaavqtva adpgvravvl
       61 cgngrgfmag gdlatlradp vqgaidiltp lnaallllaq mnapviaqvh gvaagaglsl
      121 llmadyviaa egtrlnlayi nlgascdvga swalprlvgv rkaleialmg eaftagdalr
      181 mglinrivpa veletatttl aqhlaagptv aygamkrlmr esmdrplseq laaekdafvh
      241 cagtedfrag veafhqrqsp qfvgr
//
LOCUS       WP_010465023             666 aa            linear   BCT 01-JAN-2025
DEFINITION  acyltransferase family protein [Pseudomonas mandelii].
ACCESSION   WP_010465023
VERSION     WP_010465023.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..666
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=73543
     Region          1..352
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          396..646
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 mstlayrrdi dglraiavia vvlfhfgvpg ftggfvgvdi ffvisgylit siiwnqrqvg
       61 rfsfvdfwar rarrilpalf amiiavlavg wfllapkdye elgrsvryqv mfvsnilfmr
      121 qdgyfdvasd lkpllhtwsl aveeqfyivf pllltllssr lkawrlalfa vllvsfglsv
      181 wavahhpeka ffllpmrawe llagamlava prsqwrltta gaqvvslagf glillaivgy
      241 dkstpfpgva allptlgvva liwanghrqt lvggllasrv lvgvglisys wylwhwpvfv
      301 fasyasveep gpfdiaglil ltlvlgylsw kfvetpfrer rllagrrqml laagvgvlvl
      361 glagqtlrwt hglpsrlsdq alqyakakew rpelmrclad dktpddklfc hygapalssr
      421 llvwgdshat alipvfdega qkhgvsvila sstgclpveg lehdqrcarf nrrveqelkp
      481 qsvgdvvlva rwslylygda kgdlghalkd ahgryerana eqqlaeglqa tirqlrnggl
      541 rvwlikeapl qpfsppyrls rlamlhrptd dvglavaehf krqafisqlf aqiaaanpgv
      601 tvvdpapllc dhaglcraql dghslytddn hlsevgarfi apvleplfkr lqarttlgng
      661 nanaak
//
LOCUS       WP_010465037             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_010465037
VERSION     WP_010465037.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..245
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26701
     Region          3..241
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mpllrisalh kyygdhhvlk gidlsveegq vvaiigrsgs gkstllrtln glesindgvi
       61 evdgeyldaa radlrtlrqk vgmvfqqfnl fphltvgenv mlapqvvqkv pkakavelar
      121 emlervglge kfdafpdrls ggqqqrvaia ralamspkvl lcdeitsald pelvnevlsv
      181 vrqlakegmt limvthemrf arevgdklvf mhqgkvhevg dpkilfanpq taelanfigt
      241 veaag
//
LOCUS       WP_010465045             210 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Pseudomonas mandelii].
ACCESSION   WP_010465045
VERSION     WP_010465045.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..210
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23521
     Region          2..162
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mlqqflqefg yfalflgtff egetilvlag flafrgymdi kivtivafcg syagdqlwyf
       61 lgrkhgrkll arkprwqlmg dralehirkh pdiwvlsfrf vyglrtvmpv aiglsgyppg
      121 rylllngiga aiwatalaaa ayhfgavleg mlgsvkkyel wvlgallvlg lglwlrrrfk
      181 narlakkiya deqaelaela kaaetktpte
//
LOCUS       WP_010465047             411 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sterol desaturase family protein [Pseudomonas].
ACCESSION   WP_010465047
VERSION     WP_010465047.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..411
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46947
     Region          79..235
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mdfilyavpf ffvliavell adrwrglsny rladainsis tgvlstttgl ltkgvglvty
       61 afalkhlalf elsadsvwvw vfafvlydfc yywlhrmghe rnilwaahsv hhqsedynls
      121 talrqtstgf llswifylpm avlgvpllvf isvaalnlly qfwvhtkhip klgwfewffv
      181 tpsnhrahha qnalymdrny ggvfiiwdrl fgsfqeeddn epvifgvttp laswnplwan
      241 vqfyaqlwdd arraestwdk lriwfmrtgw rpadvaakyp mnkpdlsqfr kfevpldgrq
      301 qvyvalqfcv yialgsylmn leprlptaal vlgwgavafg lftlgmalen rpqalklell
      361 rlasnvplvw lapvvglwpa savgwiglfs ysllsgigly ccrdrftrla s
//
LOCUS       WP_010465102             270 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Acidovorax radicis].
ACCESSION   WP_010465102
VERSION     WP_010465102.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..270
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28738
     Region          2..254
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 makifcvanq kggvgktttt vnlaaglaki gqrvlmvdld pqgnatmgsg vdkrsldltv
       61 ydvllesasv keaavlsekc gywvlganre lagaevelva ldhrekrlka alaeadgdyd
      121 fvlidcppsl smltlnglcs ahgvivpmqc eyfalegltd lvntikqvha nlnadlqiig
      181 llrvmfdpri tlqqqvsdql kghfgekvfn sviprnvrla eapsyglpgv vfdpaakgsq
      241 afvefaqemv ervqtmpaaa ssmakmassa
//
LOCUS       WP_010465131             212 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Acidovorax].
ACCESSION   WP_010465131
VERSION     WP_010465131.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..212
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23100
     Region          20..174
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mnttpprrdd ihsyeprlgh glphdpfnai vgprpigwis tqsaagatnl apysffnafn
       61 yvppivgfas igykdtvrnv eatgefvwnl atrdlaevmn qscaavppev sefeltglst
      121 rpstrvrppr vaespvtfec rstqilrlqg vdgekvdtwl vlgevvavhi drallkdgvy
      181 dtanaghilr gggpadyftv gpeqlfkmvr pr
//
LOCUS       WP_010465189             227 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010465189
VERSION     WP_010465189.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..227
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24512
     Region          16..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnhrvspkag vrrthaersa atrqhliata idviqnrsle emsihelaks agmtsgavqh
       61 hftskavlmm nvlseliess vlsgalwpds alasreratr fvqavwglvy aqprfivawn
      121 iylgcrnqpe vlghiaelrq svqarmrdgf ftafpelatd anrdgllglv lsslrglgml
      181 qlfapaqqst pdaaqqaqla cladliatrc eaaassaasa kaqarrr
//
LOCUS       WP_010465192             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Acidovorax].
ACCESSION   WP_010465192
VERSION     WP_010465192.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..268
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28666
     Region          1..203
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mttateisnr iieavmaqkl apgsrlgeqq lamlfdcsrt ivrealtrls trgivtvsar
       61 rgwyviepse deareafear rvielgllhq lktvdkgavr qlkahlqrek aalagsdvgv
      121 rsfllgdfhv claeclgnsl ladtlrdfta rttliamlyq sshdaaqsca dhvriveale
      181 agdiahaeal msehigsvqs alrlqastdp laglrdalap vrkstaaadt taqprqrkpr
      241 aasksstpka sdqdaapada stylgall
//
LOCUS       WP_010465199             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Acidovorax].
ACCESSION   WP_010465199
VERSION     WP_010465199.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..264
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28317
     Region          23..262
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 matavdttpa pahdgivvga ppivditalr ksygtnevlk gidlkvqkge viaiigksgs
       61 gkstllrcvn glevfqegal svngkklmhd sptamrelrq qvgmifqsfn lfphlsvgrn
      121 imlaptlvks rdaataaaqa rklldrvgla ekfdampdql sggqqqrvai aralamepqv
      181 llcdeitsal dpelvgevlr vveslalegm tlmmvthema farkvsdrvi fmhqgrvhet
      241 gtpaelfgnp qtaelqqfls slhd
//
LOCUS       WP_010465228             285 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Pseudomonas mandelii].
ACCESSION   WP_010465228
VERSION     WP_010465228.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..285
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30796
     Region          6..265
                     /region_name="SDR_a4"
                     /note="atypical (a) SDRs, subgroup 4; cd05266"
                     /db_xref="CDD:187576"
     Site            order(10,12..14,33..35,70..72,109..111,135,139,158..161)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187576"
ORIGIN      
        1 msapsvliag cgdvggrlat qlmasgwevh glrrdvsrlp egvigvsgdl fnkdcpetwp
       61 igavdylvyc aaatnhdeag yraayveglk hvlewlddyg qvpnrllfvs sssvygqqeg
      121 ewvdetsptl asgysgrlml eaekvalqsg ipasivrltg iygpgrewll tqvrrgyrva
      181 vdpplygnri haddaaglma flleadrrgv alddiyigvd dapaplaevv gwlreylgvt
      241 ewaddasvrr tgskqcsnar akalgwapky ptyregyaai legrc
//
LOCUS       WP_010465274             219 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010465274
VERSION     WP_010465274.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23636
     Region          14..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mspassaprr sprqersqft vdaifeavar ivatqgedal ttnriaelag vsvgslyqyf
       61 pskeaillam ldqhcdqvml eldallaqar tegwtpeqqv rgyvrhylqa fgggaregra
      121 larlswkldy rasvlisvrg aserlalhlq rvaqeqqmpa psaaqlfvlt rafmgavraa
      181 sleqspllds pefeqalvel ciatlapgtg lrggatmap
//
LOCUS       WP_010465291             207 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010465291
VERSION     WP_010465291.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22728
     Region          15..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 medmqtpqpk vsfkeqmhqa redailqstc qllgekafda mtmddvanav giakaslykh
       61 fcskeelcsa amvqilgrvq ayladlpaem ppleklhalv rwslerllsn empllpsrns
      121 tlravlmank dylnglvtvs dqigewitqa qaqgvisptl pplvvlytly aracdpvvsf
      181 lkeggqysda eivdlvvrtc fdglaar
//
LOCUS       WP_010465330             178 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF3299 domain-containing protein [Pseudomonas mandelii].
ACCESSION   WP_010465330
VERSION     WP_010465330.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..178
                     /product="DUF3299 domain-containing protein"
                     /calculated_mol_wt=19399
     Region          16..156
                     /region_name="COG3495"
                     /note="Uncharacterized conserved protein, DUF3299 family
                     [Function unknown]"
                     /db_xref="CDD:442718"
ORIGIN      
        1 mrrflltfll lstglahage lpetdwlelm pksdqkalea mpeidhnspe gdgtftekgg
       61 mkqskglpav mystktvpsm ndkniriggy pvplesdakg hstlfflvpy pgacihvppp
      121 ppnqlvlvry pkglklddiy tplwvtgtlk vekvnndlad aayaldaakv rvvqesdl
//
LOCUS       WP_010465297             382 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Pseudomonas].
ACCESSION   WP_010465297
VERSION     WP_010465297.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..382
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40094
     Region          4..366
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mnapvvivgt glagynlare frkldsetpl llitaddgrs yskpmlstgf gknkdadgls
       61 maepgamaeq lraevrthtr isgidpghkr lwigeeaviy rdlilawgae tvrvpiegda
      121 advvfpindl edyarfraaa agkhrvlllg vgligcefan dlilggyevq lvapceqvmp
      181 tllhpaaaaa vqagleslga rfhlgpvlnr lqhvadgvea hlsdgqviac dvvvsaiglr
      241 pridlaaaag vqvnrgvmvd rhlktshani yalgdcaevd glnllyvmpl mscaralaqt
      301 lagnptavsy gpmpitvktp vcplvvsppp rgaegvwtve gqgadikalc rdasgkllgy
      361 altgaavmek lalnkelpal la
//
LOCUS       WP_010465350             454 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Acidovorax].
ACCESSION   WP_010465350
VERSION     WP_010465350.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48918
     Region          2..449
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mtgpatrltl gtklsyatgn vglqmliaam nfmlmifytd valvapavag aallvgkvwd
       61 tvndplfgwv tdrtrsrhgr hrvyliygal plgvaaaavw mvppglspwa aflwialtyt
      121 vfdtlmtlvq lpyqamaanm trdydertsl tayasmgall gffagsvfmp mlvraapdar
      181 tgyalagscf glvagvamav vawrvrepag dpvrpadads pamwesvret lrttlhnrpf
      241 lmlmsaatlv rlgltlvqas layfviyqlq gdkgdlprfm gtllgvvgls lfvwkrvvdr
      301 weknlayilg lvfcaaglva lywvgpgdqr lvtailvvvg igmgshwivp famvpdtidh
      361 ghmqtgerkt gmyyglyglm dklartlatv lvagmldltg yvpnvaqsat alqgitlmtg
      421 ilpavclvla ipllvaypit rsrhaeilrh sgtp
//
LOCUS       WP_010465381             160 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Pseudomonas].
ACCESSION   WP_010465381
VERSION     WP_010465381.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..160
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17956
     Region          5..136
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mepgnaqlsm tvlmtpdman fsgnvhggtl lkyldevaya casryagryv vtlsvdqvif
       61 repihvgelv tflasvnytg ntsmevgikv vtenirersv rhtnscfftm vavdddrkpa
      121 avpplqpqns edkrrfmqaq qrrqirqele kryqeikgda
//
LOCUS       WP_010465411             251 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010465411
VERSION     WP_010465411.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..251
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28331
     Region          14..239
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mnsptelqpl ldrnsesplw aqfrdalrlq ilqgelaiga klpseaelge qfgisrivvr
       61 ealadlvrnn liykikgrga fvaarerded fvstvlgfsd emerkgrsvr tqvlvqqlrd
      121 ptpqeisalg ltddtqvval krlrsvdgel rllvetvvpa dlapglhrmr lddrslydvl
      181 rrqygvrlvr aerwidavlp daetctllql ehpepllrie siaygangrr leyynalhrc
      241 kssrlhvqtt t
//
LOCUS       WP_010465437             265 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas mandelii].
ACCESSION   WP_010465437
VERSION     WP_010465437.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 265)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..265
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30247
     Region          7..265
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mllslyrtlr syrgfifgsv qrefqaryrn slfgalwpvl nplsmiivyt vifshimrar
       61 lpgvddsmay svylcaglla wglfaeitlr sqnmflenan llkkisfpri clpvivlfna
      121 ginfaiimal flgfllitgr wpgmalfali plmalqmmfc aglgvilgvl nvffrdvgql
      181 fgiclqfwfw ltpivypmsi lpdwvqrllq lnpltnlivs yqnmflygqw pvwssllpif
      241 vtglvfclig lrlfrqrvge mvdel
//
LOCUS       WP_010465452             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010465452
VERSION     WP_010465452.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32851
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like_2"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08471"
                     /db_xref="CDD:176160"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176160"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176160"
ORIGIN      
        1 mdrfqemqvf aavaqdqgfs aaarrlgmsa asvtravaal etrigtqllt rttrsvhlse
       61 agqryledcr riltevqeae dsaagshaqp rgqltitapv lfgelfvtpv mvdylaqfpe
      121 vsinallldr vvsvveegid vavrigdlpd snqhairvge vrrvicgspa liaahgrpsh
      181 pqdlvqapii atsatgqlrn wpflengdpl tvrtearlvv tanqaaitaa clglgftrvl
      241 syqvarkvaa gelqivlaef elaplpihvi yqggrkapar vrsfvdftvn alrehpalkn
      301 ealll
//
LOCUS       WP_010465475             290 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Pseudomonas mandelii].
ACCESSION   WP_010465475
VERSION     WP_010465475.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..290
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32009
     Region          32..290
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mavkkrglgr gldallsgpt vssleeqavq adqrelqhlp ldliqrgkyq prrdmdpqal
       61 eelaqsikaq gvmqpivvrp igsgrfeiia gerrwrasqq agqetipamv rdvpdetaia
      121 malieniqre dlnpieeava lqrlqqefql tqqqvaeavg ksrvtvanll rlialpevik
      181 tmlshgdlem gharallglp enqqvegarh vvargltvrq tealvrqwls gkqepaepvk
      241 qdpditrleq rlaerlgsav qirhgkkgkg qlvigynsld elqgvlahir
//
LOCUS       WP_010465521             341 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010465521
VERSION     WP_010465521.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..341
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37222
     Region          <21..77
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 mrksllalll lasaglahgq vqlkegfpqq ytvvtgdtlw disgkflrep wkwpelwqan
       61 pqienpnliy pgdslslvyv ngqprltlnr gasrgtikls prvrsspvad aipsiplqsi
      121 nsfllsnriv dkvedfdkap yivagdaerv lsgtgdrifa rghfdpnqpv ygifrqgkvy
      181 tdpdskeflg inaddiggge ivategdvat lalqrttqev rlgdrlfsge ersinstfmp
      241 sapkteingl iidvprgvtq igaldvvtln kgqrdglaeg nvlvvmktge tvrdritgqp
      301 lkipderagl lmvfrtydkl syglvlnasr slavmdkvrn p
//
LOCUS       WP_010465546             133 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Pseudomonas].
ACCESSION   WP_010465546
VERSION     WP_010465546.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..133
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14737
     Region          5..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 msefhtggch cghlryqfsg plhdiahchc sicrrvsggi vttwitvpvs afkwlkgtpa
       61 qyessttcvr yfcpncgaql alithlspes idvtiatldh peqapaerhi wtrshlpwlh
      121 ldehlpgeae enl
//
LOCUS       WP_010465569             312 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MlaD family protein [Pseudomonas].
ACCESSION   WP_010465569
VERSION     WP_010465569.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..312
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=33272
     Region          1..303
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 metrahhvli glftvivvag allfglwlak ssvdtefkdy evvfneavsg lskgsavqys
       61 gikvgdvvtl rldpkdprrv larirlggdt pikedtrail altgitgtsi iqlsggtpqs
      121 ptlkgkdghl pvivaspspi arllndsgdl magvntlmhn anlmfstenv erisktlehl
      181 eqttgtiadq rgdirqamqq lasvgkqaga mleqtstlmr nangllndqg kqmfgsaeqa
      241 mksleqssat inkllttnqd slnsglqgln glapavrelr dtltslrais qrleanpsgy
      301 llgndknkef tp
//
LOCUS       WP_010465580             302 aa            linear   BCT 01-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Acidovorax radicis].
ACCESSION   WP_010465580
VERSION     WP_010465580.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..302
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32222
     Region          <41..147
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 misistlhsf wlrllarlal llafgafaas agaqttitff hndilgspai atdadgavvw
       61 kenylpyghr lqapaagann klwfagkpyd qtnwitymga ryyipligrf tgidpqgivp
      121 enphsfnrya yannnpyryv dpdgrsatla lkvlvtaavl vgaanhltpe qrarmeqaga
      181 llqqrtsell drasglvfne gggaasippd pasgsepdrg gltkagraqq khgdrvgsaf
      241 dpvkgtpedk ntqgqrtldg ivnspervdg pnrhggvdvr espggrgarf gpdgkftgfl
      301 ep
//
LOCUS       WP_010465584             284 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Acidovorax radicis].
ACCESSION   WP_010465584
VERSION     WP_010465584.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..284
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=30828
     Region          <113..>260
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mgihqrqflf gktlttswps aiqiqhwtqv lgtlrarlln psgdtipngl aptptakpgp
       61 dfnlrecvaa leemhqaler etaqrqeler tyqgthlali qaeadlacvr sgerrarhqa
      121 lhdeltalpn rrhllqqlgh alaqrrpghp gptviyidld hfkavndthg hgvgdevlri
      181 aaarlsaavr hgdlvvrlgg defacllqgi adtgplrqlc sklldavsrp mkvaslqlrv
      241 cpsigvaicp qhgtaaedll acadaamyaa krdrrgfafy geag
//
LOCUS       WP_010465599             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Acidovorax].
ACCESSION   WP_010465599
VERSION     WP_010465599.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..143
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15381
     Region          1..126
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mksfgveipf vshlgftlhr meggeselhy eakpehlnsf dvthggasmt lldvtmataa
       61 rsdtpdmgvv tiemktsfmq pargplvakg rlihrtatma ftegtvvdaq gkvcchatgt
      121 fkyvrrlpld srsanglkvi std
//
LOCUS       WP_010465586             233 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010465586
VERSION     WP_010465586.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..233
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25866
     Region          9..214
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhrpenallh rlppaarqql ldhcepfelv lsaelsvrgk pleyahfpie gflslvidvd
       61 shpplevgmv gaeamlgsel ilglaatpwr alvqgagssw rigahelraq iteipaletl
      121 lqacllarlh qqtlaaacqr yhliaprlar wllmsqdrsq sehfhvtqef malmlgvrrv
      181 gvteaashfq ddglityhrg eltvldrpal eaeacscyaa dkqiyhrlmk akh
//
LOCUS       WP_010465613             291 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endonuclease/exonuclease/phosphatase family protein
            [Pseudomonas].
ACCESSION   WP_010465613
VERSION     WP_010465613.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..291
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32264
     Region          28..272
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mrrwgtervv glhdprvneh hlestglpad srlrllsfni qvgisteryr hyltrgwqhl
       61 lphtgradnl qkignllgdf dlvalqeadg gslrsgyvnq vehlaqlgaf pywyqqlnrn
      121 lgrlgqhsng vlsrlrpwai edhplpgpkg rgailvrfge gpealvvvmm hlalgarars
      181 mqlayireli ggykhqvlmg dmnthasdll qnsplrdlgl lapqleatfp swrpqrcldh
      241 illsptltle kvevlaqpis dhlpvaveir lpgsltadaf palspapsri p
//
LOCUS       WP_010465619             317 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Acidovorax].
ACCESSION   WP_010465619
VERSION     WP_010465619.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..317
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34107
     Region          4..316
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mnpeffvisl lngvsyglll fmlssgltli fsmmgvlnfa htsfymlgay faftisgvvg
       61 fwpalvlapl vvfvlgaafe ryclrrvhkf ghvpellvtf glsylilelv qlvwgrstvp
      121 yglpeqlqgp lfslygtqfp ksrsfvmlva lvmlvsvwll ltrtriglvi qaalkypemv
      181 ealghnvprv fmlvfgggaa laglagvigg ntyitepama asvgsiifvv vvvggmgsla
      241 gaflasllig lvqtfavald yslihvfkav gvavtdqtfg ypllkltisq vapilpylfl
      301 vlilifrpkg llgtred
//
LOCUS       WP_010465655             246 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SURF1 family protein [Pseudomonas].
ACCESSION   WP_010465655
VERSION     WP_010465655.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..246
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=27525
     Region          3..234
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mkrfrpgivp tlvvalllpm lvslgfwqls rgaeksallh syaerrtaep mastellhte
       61 dpafrrvqih gqfdaahsll ldnrqrdgkv gvellqpfqd qatglwllvn rgwlpwpdrr
      121 tppqfttptq alsldawvyv spgatfqlha dpstttwpql itavepaklw taldrdgfay
      181 elraeagpas yqadwpvvam gpekhiayav qwfamsialf glylylgwhn akekhhgsgh
      241 estqhv
//
LOCUS       WP_010465654             332 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Acidovorax].
ACCESSION   WP_010465654
VERSION     WP_010465654.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..332
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36164
     Region          34..322
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mstpraniev lprsvqfsla lglaalllfp vvgsdfyvqm vtrmmimaif amsldllqgv
       61 tglvslghaa yfgvagyala fltpadtpvs lwwslplavv gaglvaliig ffvvrthgiy
      121 fimvtmafaq mvfylffdnk vlggsdglyi nfrpdasifg wlpfdlegrk tfyyftlalv
      181 vivyvllrrl lwsplgrals girinehrmr amgfgtrgyk ltaftvagal aglagylwga
      241 qtgyvnpelm gfhmsahaim miilggmgnf agaivgafaf eyllhvfkdi tkhwqllmgs
      301 fivlvvvaap rgllgmlgqr raakaqedph hg
//
LOCUS       WP_010465762             178 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Acidovorax].
ACCESSION   WP_010465762
VERSION     WP_010465762.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..178
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19575
     Region          1..166
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mlrrwldriy laagavgaaf ialicvlmva qsimrelglr tgaindivaw fcaaaaflam
       61 ahafkhgdfv rvtlllekls prrcrqlevv slaigsvavg ylmwaacsyt yeswefndis
      121 qgllpmplwi pqlsfalgsi llwvavvdef iivlrggvpt fvraveerha kgdfssdi
//
LOCUS       WP_010465777             252 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Gammaproteobacteria].
ACCESSION   WP_010465777
VERSION     WP_010465777.1
KEYWORDS    RefSeq.
SOURCE      Gammaproteobacteria (g-proteobacteria)
  ORGANISM  Gammaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Gammaproteobacteria"
                     /db_xref="taxon:1236"
     Protein         1..252
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=27548
     Region          <42..204
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          42..68
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(70,72,76..77,80..82,84..85,89,92,101,104,106,
                     110..111,114..116,118..119,123,126,135,137,139,143..144,
                     147..149,151..152,156,159)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          70..101
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          104..135
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          137..168
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          171..202
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mnikhrvfii vmlsvvssca agqkvggmtp qqafsdplva elvvaatqnd fqkvdekvqa
       61 gadvntigad gvtpliwqvy lrnvrgaekl lklganpnyr deklhasply lavgasrvdl
      121 ldvllrykgd pnligpngds llhqaviefc eacvrllven yhanvnvqcd ngdtpakvav
      181 amgrfdlvay flqkglnnnl qdlalsvqir qvpaesdamk hkvqvidmlk argvqypdpr
      241 yrprqpppgw ep
//
LOCUS       WP_010465818             353 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aldo/keto reductase [Acidovorax].
ACCESSION   WP_010465818
VERSION     WP_010465818.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..353
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=38690
     Region          13..344
                     /region_name="AKR_Tas-like"
                     /note="Escherichia coli Tas protein and similar proteins;
                     cd19094"
                     /db_xref="CDD:381320"
     Site            order(19..21,26,48,53,88,132,179..180,205,233..239,242,
                     244,258..260,296,313..317,321,325)
                     /site_type="active"
                     /db_xref="CDD:381320"
     Site            order(48,53,88,132)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381320"
ORIGIN      
        1 mnkvplgqsd llvtpiclgt mtfgeqvnea dshailsrsl ergvnfidta emysvpakae
       61 tfgatetiig nwfaknpgar qklvvatkva gpsrgmpwvr enkgmsakdi vascegslrr
      121 lqtdvidlyq ihwperhvpa fgnlyydpsk etsttpiheq lealaglvka gkvryiglsn
      181 etpygvhefv rlaeqhglpr vatvqnpycl inrtwengld etchrldvsl laysplgfgl
      241 ltgkydesgi tgpsapqgar istyesvrkq rwgrpealta srrynalara ngmtptqmal
      301 afcytkwqva stiigvtsva qldedlaawg ttlspevlqa idairwelrd pal
//
LOCUS       WP_010465869             273 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas mandelii].
ACCESSION   WP_010465869
VERSION     WP_010465869.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..273
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=29868
     Region          18..254
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtrtwgkaqs raelipithn ypgfpqgvsg aellarlrnq aeryniyvrr atvqallkrg
       61 ddfiadiddd rvvastvlla tgvidkppei rdlreatlgg yvrwcpicdg ydvidqdial
      121 lasakegfrh alflrtytrq ltlivqpggr eldnderlki aqtgirlied piaqirkikg
      181 hrvairlang gelsfdtryp mlgcnartel akslgvtfds ngellvdtgq rtsvlglyaa
      241 gdavnalnqm svgvahaata ataihnalkd nyr
//
LOCUS       WP_010465952             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Acidovorax].
ACCESSION   WP_010465952
VERSION     WP_010465952.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..144
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16408
     Region          14..>91
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(15..17,31,48..50)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mgtplpsipa kryftigeva elcgvkphvl ryweqeftql rpmkrrgnrr yyqhhevlmi
       61 rrirdllydq gftisgarnr lqelahpard dvgpdapldg ldsempsmlv dsardlsiea
      121 tgftldsnav rkelfeiral lsln
//
LOCUS       WP_010465971             318 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Acidovorax radicis].
ACCESSION   WP_010465971
VERSION     WP_010465971.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..318
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34989
     Region          7..188
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(10,12,96)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(43,95..96)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            94..96
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mhpeisvvip vyceeagirh tlrevekflt lsastweivv vddgskdntw neittisqtl
       61 pqlrglrlsr nfgkeaavsa gleaaggkav iimdgdmqhp psllptmiet wrtgefdive
      121 avkssrgdes alsaaraklf ylilrafsgh dlngasdykl ldqrvieayr tmkernvffr
      181 gmiswmgfrs tqipfevepr iagdsgwsvf glirlaaiav tsfstfplhl itifgvlffa
      241 fsvvlgmhtv ymklsgaain gfttvillll iigsslmigl giigeylari ydevkqrpry
      301 ivsqklplsp sskspgsh
//
LOCUS       WP_010466066             186 aa            linear   BCT 01-JAN-2025
DEFINITION  dTDP-4-dehydrorhamnose 3,5-epimerase family protein [Acidovorax
            radicis].
ACCESSION   WP_010466066
VERSION     WP_010466066.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..186
                     /product="dTDP-4-dehydrorhamnose 3,5-epimerase family
                     protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /calculated_mol_wt=20159
     Region          6..175
                     /region_name="RfbC"
                     /note="dTDP-4-dehydrorhamnose 3,5-epimerase or related
                     enzyme [Cell wall/membrane/envelope biogenesis]; COG1898"
                     /db_xref="CDD:441502"
ORIGIN      
        1 msrlavaplp laglfrvqrq plvdergffs rmfcaeelag agwtapiaqi nqsytalkgt
       61 vrgmhyqkpp haemklvscl rgevwdvavd lrqgsptflq whaehlsadn gnallippgf
      121 ahgfqalsdh aellychsaa yapaaeaglh pleprlaiaw plpvgqmspr dagqpgmtee
      181 fegvrl
//
LOCUS       WP_010466096             307 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudomonas mandelii].
ACCESSION   WP_010466096
VERSION     WP_010466096.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..307
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33397
     Region          4..219
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnvidiegvs qrygqttvlh dlnlslgege vlglfghnga gkttsmklvl glleasdgqv
       61 rvfgrqpsdp hvrrllgylp envtfypqms gletlrhfar lkgasnaqvd qlleevglaa
      121 aarrrvktys kgmrqrlgla qallgeprll lldeptvgld piatqdlyrl ldrlrgqgts
      181 iiicshvlpg veahinraai ltqgrllalg slrklredag lptlirangl kragslqtsw
      241 nidghvtqrw gveglevaal ngsklrllrq llneddpsdv eiappsledl yryymgqvgv
      301 hakgeta
//
LOCUS       WP_010466149             440 aa            linear   BCT 01-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Pseudomonas mandelii].
ACCESSION   WP_010466149
VERSION     WP_010466149.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..440
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47892
     Region          18..436
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 msmingftse dadrlsdkek rlverrarll gpayrlfyeh plhtvrgegv wlydeqgrry
       61 ldaynnvasv ghchprvvea isrqaaqlnt htrylqegml dyaeqllgtf pdhlervmft
      121 ctgseandla lriakqftgg sgviitrfay hgvtgdiael spslgpsmvl pphvrtirap
      181 dayrlgedqv astfagdvra aiddlrkhgi rpaailvdgi fasdgvfadp agciaegial
      241 aqaegllyia devqsgfart glnlwgfqrh nvrpdlvtlg kpmgnghpia glvgraqvvd
      301 hfgqnmryfn tfggnpvsca agqavldvir deqlqqrsht lgeylltglr elaerypiig
      361 dvrgagmflg velvtdratk apaatqtrqv vnamreqgvl isaagplenv lkirpllafe
      421 qehahlllea vgmaleglqp
//
LOCUS       WP_010466152             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alanyl-tRNA editing protein [Acidovorax].
ACCESSION   WP_010466152
VERSION     WP_010466152.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..253
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26787
     Region          1..253
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mtqdlfrqda ylrecsahit avtdtgivld qtvfyplggg qagdsgvlvl adgteiaitd
       61 trkgkdaegn ptsdivhipa pgqedrvaql alqgpgtavt aridwerrhr mmrlhttshl
      121 lchvvpqlvn gcsitpdyar ldfamtdpld kealtaaiat lvaaahpltv asisdeelda
      181 npalvksmsv qpprgtgrir tiriggdnda plidlqpcgg thvantselg aivvtkiekk
      241 sattrrvvlg faq
//
LOCUS       WP_010466159             233 aa            linear   BCT 01-JAN-2025
DEFINITION  cysteine hydrolase family protein [Pseudomonas mandelii].
ACCESSION   WP_010466159
VERSION     WP_010466159.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..233
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25564
     Region          26..210
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mshlyadpae palpgtgfkl dlskaalvvi dpqndflspt gaswavfgds ivenntvenl
       61 eklfkafkaq klpvavsphy yyphdhdwhf ggplekvmhs icmfdrkgpn tlenfessga
      121 dfleaykpyi ldgetiiasp hkvygpetnd lalqlrkkgv sqiilagmaa nlcveshlre
      181 lleqgfeivv vrdatagprl pdgdgylsai inyrflahgl wtteetiakl qpa
//
LOCUS       WP_010466174             270 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010466174
VERSION     WP_010466174.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..270
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27887
     Region          20..265
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 masttldlph addedtprtp rgiqsvevgg qllkvlartg rrmalkdlar aadmtaakah
       61 pylvsfgklg lieqdavsgh yglgplamql glislqqvdp vrlaiaelpa laqrigytvs
      121 asvwgdsgpt iirveegpta vyvamrhgtt asvrhtatgk vfaafgprer aaaalaaegf
      181 agaldepafa aeleavrqyq isavtdqllp gisalatpvf dgfgqlvlci avigpsatlq
      241 tgpaspaaqh lrdtarnlsq rlgaaqggnp
//
LOCUS       WP_010466190             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Acidovorax].
ACCESSION   WP_010466190
VERSION     WP_010466190.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32690
     Region          8..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..297
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(111..112,114..115,118,122,123..129,223..228,
                     234..235,237..238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 msqsfnyrhl fyfwvvakeg giaraaerld mavqtisaqv relekalgvs llrtegrnlv
       61 ltdagvaalh eadhifalge llpvrvreaa tgqtlrlnlg isdgiaklav hrlltpvlde
      121 phlrllcheg efqpllgela lhkldavlad raappnralr ttsqllgtsa iawyapplwa
      181 daaatdfphs lavvpvllpt dhaamrarid hwlererirp riagefedsa llstfaatgm
      241 gvmpapvslg ehlaqthglv qvgttpdvqe qfhliysark vmhplltrll evgksgmlln
//
LOCUS       WP_010466162             201 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Acidovorax radicis].
ACCESSION   WP_010466162
VERSION     WP_010466162.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..201
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21244
     Region          26..200
                     /region_name="PRX_like1"
                     /note="Peroxiredoxin (PRX)-like 1 family; hypothetical
                     proteins that show sequence similarity to PRXs. Members of
                     this group contain a conserved cysteine that aligns to the
                     first cysteine in the CXXC motif of TRX. This does not
                     correspond to the peroxidatic...; cd02969"
                     /db_xref="CDD:239267"
     Site            61
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239267"
ORIGIN      
        1 mkllrrtlia taalvalgaq aaatvgqpap dftlkdatgk tvrlsdfkgk hvvlewtnpg
       61 cpfvrkhyds gnmpatqkda tgqnvvwlav nstekassdy lepakltawl terkavptav
      121 lmdeegtvgk sygarttphl yivnpqgvlv yaggidsips arpadiekat nyvkvglsea
      181 lagkpisaat tqpygcsiky k
//
LOCUS       WP_010466221             317 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Acidovorax].
ACCESSION   WP_010466221
VERSION     WP_010466221.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..317
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32452
     Region          1..317
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mlsvllitfp ffalvlcgyl aarrgvlpqp aipglnafvl yfalpcmlyr fgastpiaql
       61 ldpavagvyv lcalvmvgat valtrsarig wndaafgalv aafpntgfmg vpllvallga
      121 qsagpaivti vvdmvvtssl cialsrldga gthgvgvalr safrgmatnp mpwsialgal
      181 asalhfqlpg pvdktiamla daaspvalft igavlarsqm nqheqvpard yvpvalakll
      241 vhpllvwgvg maamalgvpl tpfaltvlvl laalpsasnv sllaekfgan ngrvariilv
      301 stalaflsfs aavallt
//
LOCUS       WP_010466218             503 aa            linear   BCT 01-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Acidovorax radicis].
ACCESSION   WP_010466218
VERSION     WP_010466218.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..503
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53978
     Region          28..501
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mthphpprra vlaalgasll palghgadap hawrssytpy ngplkaplas gplpvrgrwp
       61 aalqgtlyri gparrelggv amnhwfdgdg mlqafrfegg qastqtppri shrgallatp
      121 kltaeeaagr llysgfattl pgspplsgpd avnpaninll alparkelfa lweagsalav
      181 dpvtlqaqgf kawspqtqga pfsahprvap dgsvwnfgym pgsgkllvyd iaptgqlrrq
      241 hvltteqadm vhdfaiterh lvfllmplqf nghpgagspl shyqwndkap lvvllvdkvd
      301 fkvqrfelpa tglfhlanaw eeggtvqvrf vaqpdilnal hhlnvdgars tpaaaatrwa
      361 hitltpstgq arletpglah vefprihpar nglptrfttl marspgmdaq vqgfdtvltl
      421 qgdktpqrhr ygagwiaeeh vyipasptaa egrgwvlgta yhwpserttl svfdaqavna
      481 gplasvtlpy glplglhgqf vrt
//
LOCUS       WP_010466223             696 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Acidovorax radicis].
ACCESSION   WP_010466223
VERSION     WP_010466223.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..696
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77374
     Region          3..658
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 msaglnlaql qavhytdgac lvlagagsgk trvitqkiah miekgmdpkr iaaitftnka
       61 aaemrerakg ligrrakdvl vctfhalgvr mvredgvvlg lkpqfsilda ddvtgilkea
      121 sggttdmata rqwqwviskw knmgltseqa laqaaddner iiatlmarye erlaayqsvd
      181 fddligmplr llrdfpevra kwqallshvl vdeyqdtnat qyellkllvg erghftavgd
      241 ddqsiygwrg atldnlkklp idfpqlkvik leqnyrstsa ilraannvig pnpklfpktl
      301 fselgegepv rvvdadseeh eaeravariq slraasnppp dwkgfailyr anhqakpfek
      361 alrkanipyk vsggtsffdr aeikdlcawf rlwinndddp aflraittpk rgighttlas
      421 lgafatqhkq smfgalfngm lpaavpkram dglhefgryi nyleysarrt hgaeeartfl
      481 newlkeigye qhlydnedse kvaaarwsnv mefcdwmaqr aggqiddtag avvaketksl
      541 levsqtiall stiserekeq dmvtlstlha skglewphvv lvgvtegmlp fkldddegrq
      601 qkvsddtlqr lqeerrlmyv gitraqrtla vswtkrrkkg remvaaqpsr fiaemgldkt
      661 taredprekl kalraefaak aqattaanaa aaatpe
//
LOCUS       WP_010466236             290 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2145 domain-containing protein [Acidovorax radicis].
ACCESSION   WP_010466236
VERSION     WP_010466236.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..290
                     /product="DUF2145 domain-containing protein"
                     /calculated_mol_wt=31776
     Region          39..278
                     /region_name="COG4727"
                     /note="Uncharacterized conserved protein, DUF2145 domain
                     [Function unknown]"
                     /db_xref="CDD:443762"
ORIGIN      
        1 mnvqqmtvtt pararvrssf npamlglalv agaallavpa ahagrsceaa kpvpakvier
       61 gmqlaqqasa aldaeharsg aqvvvlarag qdlskyglry shlgwayktp egpwwvahkl
      121 necgtavghl yrqglgeffl ddlwryeavy avptpevqqr liavlqdkgr ttalqhppys
      181 mvsyawgrky qqsnqwalet lamamepttv rtrdqaqawl qfkgyeptal klgpltrmgg
      241 rvgsaniafd dhpnekrfsd rietvtvdsm lawlqraqlv aapvvlvvkn
//
LOCUS       WP_010466280             134 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010466280
VERSION     WP_010466280.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..134
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14372
     Region          14..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mriqrlsdea iadqlgnair errlrkdikq ddlaeavgvs tptiqklekg kgtiqvliav
       61 lrelnclell mnllaaprvs plavaktgkt trvravgasq vksrtiatkv nggvttgkle
      121 gqtpnllipr rsrg
//
LOCUS       WP_010466251              64 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Acidovorax].
ACCESSION   WP_010466251
VERSION     WP_010466251.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..64
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=6912
     Region          1..64
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mhnhvkalrq drgmtqqala dalgvsrqtv hsieagkydp slplafkiat vlgrtieqvf
       61 vpdd
//
LOCUS       WP_010466315             215 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SOS response-associated peptidase [Pseudomonas].
ACCESSION   WP_010466315
VERSION     WP_010466315.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..215
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=23866
     Region          1..212
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcshfhapep rqlaiafgtq pegdyvtdlw pgytgafvrr hphadaqdda vprydvsagt
       61 fgllpfwaks atlarstyna rsetaaekps frnawkkgqr ciipaqcife pdwrtgkais
      121 triaradgel mgiaglwewr rpedplkgeg lsftmltvna sghqlmenfh kpgdekrmva
      181 ilspaqfdew ldapvsstms flrqypadrl vatig
//
LOCUS       WP_010466373             318 aa            linear   BCT 01-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase [Acidovorax radicis].
ACCESSION   WP_010466373
VERSION     WP_010466373.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..318
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32631
     Region          5..308
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mptlitltln paldlatttg hvapthklrc gpvqrfaggg ginvarvlhr lgadvlawal
       61 aggaagaqvr qlladegvpt vlqpiagdtr dnfsvvettt gqefrfvlpg ptlqaaewqa
      121 cldaltaqqp pprwliasgs lppgtpenfy dqlaralstr gvrvaidtsg pplaaalqag
      181 valvkpslre lrevvrqple haadwcaaaq slvhsgaagi valsvgeqga vlatregvwq
      241 apalnvpatt gttgagdcfl aalvwaldrg dapaealrwg laagaaallh pgttlaqadd
      301 vqrlvhrvpa pvafatqp
//
LOCUS       WP_010466515             311 aa            linear   BCT 01-JAN-2025
DEFINITION  DsbA family protein [Pseudomonas mandelii].
ACCESSION   WP_010466515
VERSION     WP_010466515.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..311
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33535
     Region          84..243
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mtlrlktfip tvltavalsq avsyaalnvw geqyltskme taasmrekae ieeyskaqfa
       61 kfsaaadevp ndarvygelk arftlaefsd mecpfckklh pnlkeivdrs ngavnwqwrh
      121 lplsfhnpaa tddakaaecf aeqkgnrgfw vfldqifeks agngggvkdm sdivkwlggd
      181 kvkfaqcmss dnykdriaeh mrmgekigat gtpatviidn ltgekefvsg aqpisafisi
      241 mkkmmvgeka eaqaqaqkeq gqpidggdvv sqkilgygsr adaaptvdak lpaaptapgs
      301 qpsngaspvs k
//
LOCUS       WP_010466606             148 aa            linear   BCT 01-JAN-2025
DEFINITION  YeeE/YedE family protein [Acidovorax radicis].
ACCESSION   WP_010466606
VERSION     WP_010466606.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20802814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..148
                     /product="YeeE/YedE family protein"
                     /calculated_mol_wt=15224
     Region          3..142
                     /region_name="DUF6691"
                     /note="Family of unknown function (DUF6691); pfam20398"
                     /db_xref="CDD:466547"
ORIGIN      
        1 mklqrisefg iglvfglgli isgmtdpgkv lgfldlagqw dpslafvmgg ailvgvvafa
       61 varkrstsvf ggpmqlptar hidrrlvlgs llfgagwgia gfcpgpavvs lgtgepkaav
      121 fvlamlagmg afewlemrka arstphaa
//
LOCUS       WP_010466656             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Acidovorax].
ACCESSION   WP_010466656
VERSION     WP_010466656.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24533
     Region          24..182
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnpprkalaa gsstapkplk rprqararft vqaiydafvr iwqrdgwdkl ttrnvaletg
       61 isvgtlydyf pnktallsgy vrhcieslla aidreavqpt dlpwtarvhh lvrlvcgvda
      121 pelppfhpdm laleaqmaep rhhrrvheel vtawgrvfaa csdlpcppgq ellqvlhlsa
      181 wggrryvlll qldavqmrqw aegveqlcca airqapsppd
//
LOCUS       WP_010466675             319 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Acidovorax radicis].
ACCESSION   WP_010466675
VERSION     WP_010466675.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..319
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32706
     Region          11..319
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtspafklpp latlgpfial ilacaffatq serflsaqnf alilqqvmvv aviaigqtlv
       61 iltagidlsc gmvmalggiv mtkmaadygl sapvaiacgm avtmlfglin gllvtkiklp
      121 pfivtlgtln iafaatqlys gaqtitdipa gmtalgntfq lgqtaivwga vlmlalylvt
      181 wfalretapg rhvyavgnsp eatrltgiat dkvllgvyvl aglfygiasv lsvartgagd
      241 pnagqtenld aisavvlggt slfggrgvil gtlvgalivg vfrngltlmg vssvyqilvt
      301 gilvilavat dqlsrkgvr
//
LOCUS       WP_010466801             284 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Pseudomonas mandelii].
ACCESSION   WP_010466801
VERSION     WP_010466801.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..284
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30239
     Region          17..281
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mpiaqlispq aldlkkdapg lvildcrfal edpdygqrsy aeghiagssf adlerdlsgt
       61 vvkgvtgrhp lpepeelier lqawginads evvlyddgpg ayaarawwll awlgkrdgvf
      121 ildgglkawh aaglplslda cdtprgtftg tpddalilsa eqlqkrlgqp mltlldaral
      181 prfkgevepi dpvaghipga qcaaftenlg sdgrflpadq lkqrfaaklg draptdlvay
      241 cgsgvtachn lfalclagyp lgslyagsws ewindpahgi aige
//
LOCUS       WP_010466824             159 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Acidovorax radicis].
ACCESSION   WP_010466824
VERSION     WP_010466824.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..159
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17000
     Region          3..158
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mpsknticlw fngsaldaat fyaatfpdsa vgrvmhapgd ypagqqgdvl tveftvlgip
       61 clglnggpaf vhseafsfqv atddqaetdr lwsaivdngg qesacgwckd qwglswqitp
      121 rvltqavtdp draaakrafd ammemrkidi aaieaawrg
//
LOCUS       WP_010466858             299 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Pseudomonas].
ACCESSION   WP_010466858
VERSION     WP_010466858.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..299
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32848
     Region          213..290
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mtlpsdlppe lahrgvrpad rlgftlflaa lihlalllgv gftmvepkqi sktleitlat
       61 fksekkpaka dflaqenqeg sgtldkkaip kttevapfqd tkvqkvtppp aakppvpeaa
      121 pkaavttvap kpkkapakne eikpitkpav aaptfdteql ssdiasleae laneqqlyak
      181 rprihrlsaa stmkdkgawy kdewrkkver ignlnypdea rrkqiygnlr lmvsinrdgs
      241 lyevlvless gqplldqaaq rivrlaapfs pftgdlsdid rleiirtwkf argdrlssn
//
LOCUS       WP_010466921             134 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Pseudomonas].
ACCESSION   WP_010466921
VERSION     WP_010466921.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..134
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14937
     Region          3..134
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mnfhtrkwvk pedlnpngtl fggsllrwld eeaaiyaivq lgnqrvvtky iseinfvsas
       61 rqgdiielgi tatefgrtsi tlkcevrnki trksiltvdk ivfvnlgedg lpaphgqtei
      121 kyvkdqfkdd vase
//
LOCUS       WP_010467076             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ammonium transporter [Acidovorax].
ACCESSION   WP_010467076
VERSION     WP_010467076.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..455
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46940
     Region          49..452
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mravnhrffv vvslclglca salaqtalda agavaavpsp pltrpglvaq ttisaadtaw
       61 mmtstalvll mtlpgialfy agmvrkknvl ntmasvvaia alvsllwfga gyslaftpgs
      121 pwlggwerig fagldfqlag gklavshvap hipesvyamf qltfaiitaa llvgafverm
      181 rfsamlifis lwtllvyapv ahwvwepggw laqmgaldfa ggsvvhvnag vaglvcawfl
      241 grrtgygrep fepynlgltm agagllwvgw fgfnagsava adgraglama vthlaaaaga
      301 lswmlgewvv rgrpsllglc sglvaglvai tpaagfvtlr savaiglvag lacywgatgl
      361 krllraddsl dvfgvhgigg ivgslltgvl asrtvggvsg slltqaigvg avmayslvat
      421 avllwitnfa vglrvdeqse qtgldiaqhr erlgs
//
LOCUS       WP_010467087             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MlaD family protein [Acidovorax].
ACCESSION   WP_010467087
VERSION     WP_010467087.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..321
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=33349
     Region          1..308
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 menkshalaa gifvlvvaam laglaiwltr dsanyeqyel stkdgvsglq pqaavrykgv
       61 avgkvtrigf dpqvtgnvli riavneqapi spttfavlgy qgvtglahvl lddadkpype
      121 lppgpsglpr lpikpspfgk laeqapaila qvdeatrrin qllgdtnqqk ltealgniaq
      181 aagsvntltq rldatvaqrl dpalaalppl asdarktlqs lqqagasvsv laadvskttq
      241 rlgaeggpid qitigtqsla raadqfsttt lprlnraadd tsraarqlsr taggvtdnpq
      301 lfiygsgrip pgpgeqgfaa p
//
LOCUS       WP_010467112             230 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dienelactone hydrolase family protein [Acidovorax].
ACCESSION   WP_010467112
VERSION     WP_010467112.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..230
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24575
     Region          1..225
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mgqfvdlkss dgftfpawva qpdgaprgav vvlqeifgvn shiravadrf aargylavap
       61 stfhrvqqdv dmgysgddmk agmalkaave alpapgvmpd iqaaidhaaa qsgrkvgivg
      121 fcwgglltwr aacqlqglsa avpyygggmt tpeeaarhpq vpvlahfgqr dhyipldgvq
      181 afarahpdve vhiyeadhgf ncdqrgsyde psamtardrt laffdkhlia
//
LOCUS       WP_010467125             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Pseudomonas].
ACCESSION   WP_010467125
VERSION     WP_010467125.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 429)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..429
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47814
     Region          148..414
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mprssavris hflpslllll aglaaayikd lnvfftslfn vlptlvlllg gaycavyrrq
       61 relflmvtvy iayflldtqt dyyrdngkvr edaavvfhlc clllpllfgv faawqerthl
      121 fqdmvarfav llavgsvalg leqsypqall mwlseirwpa lhgawmsliq lsypvfiasf
      181 lllswqywrn prplhaaqlv glvglfwalp ktfilpftln imcsqvmlmi aaavaheayq
      241 mafrdeltgl pgrralnerm qrlgrnyvla msdvdhfkkf ndthghdvgd qvlrlvaskl
      301 skiggggray ryggeefalv fagktleecm phleviresi atyniqlrnq dsrpqddqqg
      361 rqkragsgat svsvtvsigv aerqeqrtpe kvlksadeal ysakgagrnc vvafgqtrrg
      421 avrmdaaag
//
LOCUS       WP_010467131             217 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Acidovorax radicis].
ACCESSION   WP_010467131
VERSION     WP_010467131.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..217
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22490
     Region          7..215
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 mnaqterltl sgpagaieav rdaatladga aaprgvaiia hphplfggtm dnkvvqtlar
       61 afvqcgwtav rfnfrgvggt egvhddgqge lqdllavveq vapaaagqri alagfsfgaf
      121 vtshalatlw pqgrvdhavl vgtaasrftv apvppdahlr tlvvhgehdd tvplaavmdw
      181 arpqilpvtv ipagghffhg qlpllknlvv rhlqsgg
//
LOCUS       WP_010467159             423 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YeaH/YhbH family protein [Pseudomonas].
ACCESSION   WP_010467159
VERSION     WP_010467159.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11148708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..423
                     /product="YeaH/YhbH family protein"
                     /calculated_mol_wt=48533
     Region          13..420
                     /region_name="DUF444"
                     /note="Protein of unknown function (DUF444); pfam04285"
                     /db_xref="CDD:427839"
ORIGIN      
        1 msyvidrrln gknkstvnrq rflrryrdhi kkaveeavsr rsitdmehge qisipgrdid
       61 epvlhhgrgg kqtvvhpgnk eftsgehiar ppgggggrgp gkagnsgegm defvfqitqe
      121 eflefmfedl elpnlvkrnl tgtdtfktvr agisnegnps riniirtlrs aharrialsg
      181 ssraklreak eellrlkrde pdnfgdiqei eaeieklsar ihrvpfldtf dlkynllikq
      241 pnpsskavmf clmdvsgsmt qatkdiakrf fillylflkr nydkidvvfi rhhtsarevd
      301 eeeffysret ggtivssalk lmqeimaery psnewniyaa qasdgdnwnd dspicrdili
      361 nqimpfvqyy tyveitpreh qalwfeyeri aeafsdtfaq qqlvsagdiy pvfrelfqrr
      421 lvt
//
LOCUS       WP_010466795             531 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Pseudomonas mandelii].
ACCESSION   WP_010466795
VERSION     WP_010466795.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Khan,M.W. and Murali,A.
  TITLE     Normal mode analysis and comparative study of intrinsic dynamics of
            alcohol oxidase enzymes from GMC protein family
  JOURNAL   J Biomol Struct Dyn 42 (19), 10075-10090 (2024)
   PUBMED   37676256
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17335521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..531
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57381
     Region          49..531
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
     Region          78..297
                     /region_name="GMC_oxred_N"
                     /note="GMC oxidoreductase; pfam00732"
                     /db_xref="CDD:366272"
ORIGIN      
        1 mpvpdpfreg margwktyng sqltqdltld advaiigsga gggttaeils aagykvllie
       61 egplktssdf kmledqayts lyqegigrms kdgaitilqg ravggttlin wtssfrtpdp
      121 tlehwarehn vkghspaema pwfekmeqrl gvapwmvppn anndvirkgc eqlgytwhvi
      181 prnvrgcwnl gycgmgcptn akqsmmvtti patlekggel lylaraetls ikdgkvtglq
      241 cvamddhcva ptgrtitvka rhyvlagggi nspalllrse apdphqrlgk rtflhlvnms
      301 aglfdevinp fygapqsiys dhfqwqdgtt gkmsyklevp plhpalastl lggfgkenag
      361 hmenlphtha mlallrdgfh pdspggsvel rgdntpvldy qvspyawdgl rrafhsmaei
      421 qfagganavm pmhadaryvk tlaeartlid glslelyrtr lgsahvmggc amgedpknav
      481 tdslgrhhqi snlsihdgsl fptsiganpq lsvygltaql atslaerlkn p
//
LOCUS       WP_010467184             274 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010467184
VERSION     WP_010467184.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 274)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..274
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29423
     Region          10..270
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mlspymspie rvwfyslril cglillflil pvlviiplsf nsgsflvypl qgfslhwyqd
       61 ffasaewmra lrnsiivapa atvlamifgt laaigltrgd fpgkalvmal vispmvvpvv
      121 iigvasylff aplglgnsff slivvhavlg vpfviitvsa tlqgfnhnlv raaaslgasp
      181 ltafrrvtlp liapgvisga lfafatsfde vvvtlflagp eqatlprqmf sgirenlspt
      241 iaaaatllia fsvillltle wlrgrseklr taqv
//
LOCUS       WP_010467305             265 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Pseudomonas
            mandelii].
ACCESSION   WP_010467305
VERSION     WP_010467305.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..265
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29911
     Region          18..265
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 msisepvgst deqqpvitav rrftvltvnt hkgftalnrr filpelreav rsvsadvvfl
       61 qevhgthedh pqrydnwptm pqyefladtl wpqfaygrna vypagdhgna llskfqiirh
      121 dnldvsisgh enrgilhcvl rlpgdgqevh aicvhlglre shrteqlkll arrledlpvd
      181 apvivagdfn dwrqradall kpcglrevfa ehhgkparsf parlpalrld riyvrnlkas
      241 rpqvlaarpw shlsdhapls veiel
//
LOCUS       WP_010467314             421 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas mandelii].
ACCESSION   WP_010467314
VERSION     WP_010467314.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 421)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..421
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45760
     Region          18..233
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          138..417
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mylfrlamas lanrrftail tafaialsvc lllavervrt eakasfasti sgtdlivgar
       61 sgsvnlllys vfrignatnn irwdsfehfa nnpkvkwaip mslgdshrgy rvmgtteayf
      121 ehyqyghqqh leladgrafa sdpfevvlga evadalhykl ggklvlahgv avislvkhdd
      181 kpftvvgilk rtgtpvdrtl hislggmeai hvdwhngvpa qgkgrisadq arnmdltpqa
      241 itafmlglns kistfavqre inefrgepml ailpgvalqe lwslmstaek alfvvslfvv
      301 ltgligmlta iltslnerrr emailrsvga rpwhiatllv leafalalag vmaglgllyv
      361 gialaqgyvq anyglylpla wpseyewtll ggiliaallm gsvpawrayr qsladglsir
      421 l
//
LOCUS       WP_010467347             637 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sigma-54-dependent Fis family transcriptional
            regulator [Pseudomonas].
ACCESSION   WP_010467347
VERSION     WP_010467347.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..637
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=70167
     Region          1..634
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mhdnhlsrha qqvltvtqgk shlhgpgsdp siarswlrcl edyhldpalt maptvlehgr
       61 vlesrerlqq vlhiagsemt slhqqlsgag havlltdarg vilncvtapa erkiferagl
      121 wlgadwseac egtngigtcl verqsltihq dehfrgrhtg ltcsaspvfd phgellavld
      181 vssarhevsr qsqfhtmalv nlsakmiesc yflryfdnqw llrfhlqaes vglfseglla
      241 fdgegrisav nqsalnllgh irggllgkpv eaffdcsldd llgrasvnas aswplrtrdg
      301 rslfavlrgq prsipvpvvp gptiaerprl sgiclgdaal qedfrkslrv ferdvpllin
      361 getgsgkeaf akavhqasqr adkafvalnc aaipeslies elfgyrggsf tgarkegmrg
      421 klqqadggtl fldeigdmpl alqtrllrvl edrqvvpigg epesvnvrii sathrhller
      481 vqdgsfredl yyrlngleia lpalrersdk sqlldfllae eagaetvlid eparqallgf
      541 awpgnvrqlr nvlrtlaalc ddgrigledl pvmirqvrpv pvvaveetse hplddaerla
      601 llnaleqtrw hmthtaeqlg vsrntlyrkl rkhgiar
//
LOCUS       WP_010467459             431 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Pseudomonas].
ACCESSION   WP_010467459
VERSION     WP_010467459.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..431
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44639
     Region          1..429
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mlerlfqlka hntnvrteil agvttflama yilfvnpsil getgmdkgav fvatclaaai
       61 gstvmglian ypialapgmg lnafftytvv lhmghtwqva lgavfisavl ffllsifrir
      121 ewiinsiplp lrsaiaagig lflalialhn agivvsnpat mvglgdlkqp apilatlgfa
      181 livalealav rgavligilv vtiasialgf tpfggvmsmp pslaptflql dikgaldigl
      241 vsvifaflfv dlfdnsgtli gvakraglmg kdghmpkmgr aliadstaam agsllgtstt
      301 tsyiesaagv saggrtglta vvvailflla lffsplaasv pafatapall fvavlmtsgl
      361 aeidwdditv aapvvvttla mpftysiang iafgfiswta ikllsgrgre lnpalvilsi
      421 lfviklgwfn a
//
LOCUS       WP_010467469             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010467469
VERSION     WP_010467469.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43895
     Region          15..393
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(25..26,29..30,33,65,120..121,123..125,128,148,
                     151..152,155,227,230..231,234..236,239,263,267,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mpsqaplllr hhrpfiafwl arvftasgfq mltvaigwnl yqltgnvldl glvglvefap
       61 rvlfmlhtgh vadrydrrkv aaicqslqal ialslaigsa tdhvtremif ilafllgaar
      121 sfempttqal lpsivpsalf pravaaaqsa qqsativapa lggllyafgs vwvygptvil
      181 yliacllmln lparqtplnk gkatldslla girfirsrpd ilgaisldlf avllggatal
      241 lpvfakdill tgpwglgllr sapavgallm slylarfave rkvgrvmfta vgvfgvatia
      301 fglstsfwfs lavlvvlgaa dmismviras fvqletpdem rgrvsavngl figasnqlge
      361 fesgltahwf gtvpavvmgg igtlvvtgaw iklfptlanr drmhvpieea ka
//
LOCUS       WP_010467471             479 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cytochrome ubiquinol oxidase subunit I [Pseudomonas].
ACCESSION   WP_010467471
VERSION     WP_010467471.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..479
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53388
     Region          4..447
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mfglealdla riqfaftisf hilfpaitig lasylavleg lwlktnndty rdlyhfwski
       61 favnfgmgvv sglvmayqfg tnwsrfsdfa gsvtgpllty evltafflea gflgvmlfgw
      121 nkvgrnlhff atvmvaigtl istfwilasn swmqtpqgfe iingqviptd wfavifnpsf
      181 pyrlmhmata afvataffvg ssaawhllrg kdnpairtml smamwmaliv apiqavigdf
      241 hglntlkhqp akiaaieghw enhgdeptpl ilfgwpdmke ertkyaveip ylgslilths
      301 ldkqvpalkd fppedrpnst ivfwsfrimv glgmlmiftg lwslwlrksd klytsrpfly
      361 lalwmgpsgl iailagwftt eigrqpwvvy glmrtadass nhsflqmsit lvlfvvvyfa
      421 lfgaglgymm rlvrkgpkid egketpeggp gkkrtparpl saaddsaddd hgpsltkei
//
LOCUS       WP_010467509             310 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010467509
VERSION     WP_010467509.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..310
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33213
     Region          35..308
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mtaetsissh shhdhescah shgvidpsla sserglwavq wstagllvtv llqmgavyls
       61 gsvalladll hnvgdiical plgiafwmgr wspnrrfqyg ygrvedlagv miiliiaasa
      121 vatgyesiqr fihpqsldhl gavaiaagig figneavalf rirvgneigs aalvadgyha
      181 rvdglvslav visavglwlg ytwadplvgl gitfalihiv wesgqtvltr lldgvepett
      241 ealqqalagy dyknlkarwm ghqlyaqvcl avepemsmgd gdaianqlrs hlhqeipyls
      301 disiemqpks
//
LOCUS       WP_010467573             311 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010467573
VERSION     WP_010467573.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 311)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..311
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34207
     Region          61..181
                     /region_name="AAA_22"
                     /note="AAA domain; pfam13401"
                     /db_xref="CDD:379165"
     Site            67..74
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(68..75,145)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            order(127,142..146)
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
ORIGIN      
        1 mpikrhkrrl angeervyly avskdgsqrr slssipassv slplyrraek nrivaalqan
       61 ssllvvgeag igksvlgeav aeelqelgfm vaiehpltak qayldiaqql gvetvtiegk
      121 sltsnqlsta isewlkdnta fvicddahry tvqfrtwlaq lhdqgqslll latfppardi
      181 flrlprielk plpdkpirqi mrstaqslgi dmmpsqlskl qqrcggnpml aqrvvreeyl
      241 gldatnpdht qwidgtpfli aglmilvitr figlglnsts lyliggiltv avgvirllvy
      301 amprksgklg r
//
LOCUS       WP_010467688             223 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010467688
VERSION     WP_010467688.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..223
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=24850
     Region          44..208
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(114,121,138..140,181,187,191)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mlkwliqqsq svrspwqrwg mvvtglafgl fvaiatllpq ietldtqill aihhlhtptl
       61 drlmvlvtyl geplilfpft lamggillwq krrqealgfv iaiggslgln iwlkelfarh
      121 rpalwdqilq vpfysfpsgh amvslvfyav vvyglirqfr sfrllmvtmg tsliatigfs
      181 rlyigvhwpt dvvagyaagl vwlavclisq slllarstet asd
//
LOCUS       WP_010467697             122 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010467697
VERSION     WP_010467697.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..122
                     /product="VOC family protein"
                     /calculated_mol_wt=12613
     Region          1..114
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 maaefkhvml mvkdipatvk fyseglglav kmqspgwael daggttialh aagetaggds
       61 pilsfhvedv haaianlesl gaqlegrvre pafgkvaamr tpdgnllsll qpsevpatsh
      121 sh
//
LOCUS       WP_010467766             418 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Streptomyces somaliensis].
ACCESSION   WP_010467766
VERSION     WP_010467766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..418
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=44146
     Region          8..259
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,32..33,62,67..70,82)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,65,81..84,88,90,127,129,
                     131..132,134,148..149,152,169..172)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,65,81..84,88,129,131..132,
                     134,148..149)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,88,90,127,129,131,152,169..172)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(148..156,165..172)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgevfagrye lidpigrgav gavwrawdqr rrryvaakvl qqsdahtllr fvreqalrid
       61 hphvlapasw aadddkvlft mdlvgggsla hligdygplp aryvctlldq llsglaavha
      121 egvvhrdikp anilleatgt rrphlrlsdf gismrkgepr ltetdyvvgt pgyfapeqlt
      181 gaepdftadl favglvalyl lqgrrpdsra lvahflahgt pgapegvpep lwqvlagllq
      241 pdpevrfrta ngarkalssa vemlpgpage espievfdql gplppgygpe gpvpvpapss
      301 vpgraapare pspsetgsfh lapppprihp pqppaapqpy gpypsapqpy gpypsaphpa
      361 paaypgppph saappavaaa vpppaprrrp gppravavpv vllalvcyav giwaltra
//
LOCUS       WP_010467823             262 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010467823
VERSION     WP_010467823.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..262
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28737
     Region          1..247
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 maeplielkg iskafgkhvv ldgadltiyp gdalailgps gtgkstilri iagllapdkg
       61 evyingkrrc gsldnfdnpi rmsmvfqqaa lfdsltveen vgfflyqnsa lprqrirdlv
      121 neklevvglp gighlfpael sggmrkrvsf araildnpdd dlddpkilly deptagldpi
      181 astmiedlil elqrssgcet yaivthqnst irrngkrlvl lyqgqvqwqg iwdeietsdn
      241 pylqqfmsgs vqgpmdlvgd yl
//
LOCUS       WP_010467889             292 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Streptomyces].
ACCESSION   WP_010467889
VERSION     WP_010467889.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..292
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30895
     Region          42..209
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mstetrihdi gyrayegprl grayarrsly vqslrgaygl grsarskvlp vllfgvmcvp
       61 alivvaiait mksrslsvdy tsypifmqlv ialyvasqap qsvsrdlrfr svplyfsrpi
      121 ervdyvlaky gamasalfvl taspllvlya gsllakmdfa dqtedfaqgm vsvalmsllf
      181 ggvglvlaal tprrgfgvaa viavlsvsyg avttvqaiaw gtgnpdavvw lglfspttlv
      241 dgvqtaflga stsfpggegp gaavgavyll vvlalvagsy avlmrryrkv gl
//
LOCUS       WP_010468040             306 aa            linear   BCT 01-JAN-2025
DEFINITION  FHA domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010468040
VERSION     WP_010468040.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..306
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33912
     Region          9..102
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 miatsfeipq lliqmgsnce pfefqsglew tvgrhpsnpi qlgdrcasrq haklvrlqdh
       61 hycyvdlnsr ngsklrgrsi kypvllqngd rikigdtyli fqdipthrtt gngtpdkaqv
      121 lllqadalqg kiwqtvlhsq tidsywesad idlkaylprr vasgslpqll vldtqilgdq
      181 tyevcawcaq tfpqlkiivn nsqerqilms erqkaaqagc lnwfpafrep klidniagiv
      241 vqangvmnil ggtlrqdtlf tvlksfekll gevatlqppp kpvapsqpsp atadqngdlt
      301 qvsrkg
//
LOCUS       WP_010468045              67 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Streptomyces].
ACCESSION   WP_010468045
VERSION     WP_010468045.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..67
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7060
     Region          1..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 matgvvkwfn aekgfgfiqq dgggadvfah ysniatsgfr elqegqkvtf dvtqgqkgpq
       61 aenilpa
//
LOCUS       WP_010468076             751 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010468076
VERSION     WP_010468076.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..751
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=80015
     Region          66..407
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          85..113
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(88..89,92..94,96..97,101,104,113,117,119,123..124,
                     127..129,131..132,136,139,148,150,153,157..158,161..163,
                     165..166,170,173)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          117..148
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          150..176
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          186..213
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          215..294
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <278..551
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          297..346
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          353..380
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          421..453
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(422..423,426..428,430..431,435,438,453,455,457,
                     461..462,465..467,469..470,474,477,486,492,494,498..499,
                     502..504,506..507,511,514,523)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          455..486
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          492..523
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          506..748
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          525..555
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(625,627,631..632,635..637,639..640,644,647,656,658,
                     660,664..665,668..670,672..673,677,680,689,691,693,
                     697..698,701..703,705..706,710,713,722)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          625..656
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          658..689
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          691..722
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          724..748
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mdlsqaignl fdqeegakse dsklsdllsr iaqllpdtss snpdgdqdae vlyrqltdaa
       61 rsgqndlfle lvkaektqpp sneptllmaa vlahqhevvk almaagadvn akvkkffefn
      121 aldlavgeen iaitqtllea gadpnwints pglapitkai qknntelvrl llkhnasvvf
      181 etkakplvea aqndnpeiin llieagcsin dknynsqsal qiaclncnve tiktllaaga
      241 qlsasgdelf sifyakgyar qlsgllgekp dptpkiplal qalidagadl nvvsntgtta
      301 lataiqhgyl eavklllakg adpnlscqsi dswmlqnpel qdhyrerfdk tmplnlaaaf
      361 grfemvqtll dagadpgcid ekgrtalkia ikeghqdivt llkktgapdt pevmehpsdt
      421 llgaakkghl ellssalaag adpnasqvsa grqrrektal mfaaerghld vvkrlleaga
      481 evdlsdrpgk kfgktplmya aqsdqadilk yfleagavid aqdkrgqtal fyaveakaaa
      541 avevlltyga dphkqswdgt pfeqasysns qitklittad hqrssemsae arvemlssaa
      601 fdgnadlvrd lihqgvdina tdkdsgwtal msgaaqghit vvqlllaaga evnrdlpsgk
      661 talseaaywg rteivkllis aganlnsads dgwtpvmktl vwnatevlqv lldagadasv
      721 rnedgkmvla iaiadgktei anilrqagvt e
//
LOCUS       WP_010468122             169 aa            linear   BCT 01-JAN-2025
DEFINITION  leucine-rich repeat domain-containing protein [Streptomyces
            somaliensis].
ACCESSION   WP_010468122
VERSION     WP_010468122.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..169
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=19163
     Region          3..24
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <4..>162
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          25..47
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          48..70
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          71..93
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          94..116
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          117..139
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 mehtldfwra gltevpdpvw rrtdlrvlil agnaltslpp evgrlrrltt ldlghnrltt
       61 lpdslghlch lrelrlrgna ithlppsaae lrelrhldlr enaltevprp larlpllrri
      121 dlrgnrlggl pdwlarlpsl erldlrwngi dpslplvael errgcfvlv
//
LOCUS       WP_010468139             180 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Streptomyces].
ACCESSION   WP_010468139
VERSION     WP_010468139.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..180
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19678
     Region          28..137
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 msahaapdgl lvptghgrtl tapahqvtfk vtgeharaas sfevvvppgf dvgahvhahs
       61 eelfyllege levlafeprv rtrddwrhwe spggrrtvra epgtvivvpp gcphafanrt
      121 deparmffqa spppdheryf eelleildgg gppdhaaiaa lrarydieql tpmrygapvr
//
LOCUS       WP_010468152             198 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase family protein
            [Streptomyces].
ACCESSION   WP_010468152
VERSION     WP_010468152.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..198
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21188
     Region          1..192
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrivisefvs ldgvvqapgg peedtdggfa hggwthpffd pevvggafde alekadallm
       61 grrtwramag awpdragdpf adrmnslrky vvtetlgddd ltwentsrip ggeavarire
      121 lraapggdll vmgsptlvrt lldedlvdel rlvvmpvilg ggksifprng rmrtlepvse
      181 ttgptgarvc vyrpvaga
//
LOCUS       WP_010468224             278 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Streptomyces].
ACCESSION   WP_010468224
VERSION     WP_010468224.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..278
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30446
     Region          7..256
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mertppegta eilfvgnatv lirygeltll tdpnflhrgq rahlgyglvs rrltepavdv
       61 adlphadlda vvlshlhgdh fdrvarrgld rglpfvttph acrllrglyg frratglrtw
      121 qsrtlrhgds svrvtslpgr hapgpfrlll ppvmgsllef gdrsgetrlv lylsgdtlfh
      181 aglreiaerc pdihlavlhl ggttlpgglv vtmdagqgad lldllrprra lpvhyddytv
      241 frspledfld earrrghgar llrcapgerv tvgpeaaa
//
LOCUS       WP_010468233             330 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Streptomyces].
ACCESSION   WP_010468233
VERSION     WP_010468233.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..330
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35557
     Region          15..329
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 makgsshavr peglhrvvvv vdedsnpfel gcaievfglr rpeigrdlyd falcspeprt
       61 pmrdgfftlt gvadleaadt adtlivpnrp dveaphhpav ldavrrahar garliglcsg
      121 aftlaeagvl dgrratahwq wadsfrarfp svrlepdvlf vddgdvltaa gsaaaldlgl
      181 hvvrrdhgae vagsvsrrlv faahrdggqr qfverpvpdl pdeslapvla waqerldapl
      241 tvsglaaraa vspatlhrrf raqlgttpla wltgerlsla crliergesr fevvarrsgl
      301 gtaanlrtvm rratgitpsa yrrrfgpaad
//
LOCUS       WP_010468253             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YihY/virulence factor BrkB family protein
            [Streptomyces].
ACCESSION   WP_010468253
VERSION     WP_010468253.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..321
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33852
     Region          33..312
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mgtvvhvpqt rdmvgeelsg deaftalrhy ggrdllvdsf arfryadgfs sarslgyqmv
       61 lgivpftial vgvattmhte glgraieltl arivpgtsad lvrqaladtr rsagadvaga
      121 vamwlglgfa vlnlasamaq vergcnriyg ierdrpflak ygrgvllavc aglplgggfl
      181 avvagrdige svvrslhwpp vlldwwlplh vpvgvllaal asavifrwap rrdqpgytwl
      241 vfgsgvhlll wvaatwllal yvgrsgsfga vygpltafva lllwanvtgv alflgvafaa
      301 qleaaragit epvhpdpgpg a
//
LOCUS       WP_010468265             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Streptomyces].
ACCESSION   WP_010468265
VERSION     WP_010468265.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18795604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..220
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23608
     Region          10..194
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
     Region          54..144
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mtehdalsat rdaydaiapt yaelfrdslr dspldrailg afaevvradg ndrvadlgcg
       61 pghvtahldg lglaafgvda spamvdlarr ahpdlrfevg smaaldiadg tlggvlsrws
      121 vihtpprelp avlaefhrvl apgghlligf sasddpsrpv qvfdhavapa yrwapdrlaa
      181 mlreaglaev armvreprpt drrqfrevql larripaeta
//
LOCUS       WP_010468281             259 aa            linear   BCT 01-JAN-2025
DEFINITION  ADP-ribosylglycohydrolase family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010468281
VERSION     WP_010468281.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..259
                     /product="ADP-ribosylglycohydrolase family protein"
                     /calculated_mol_wt=28627
     Region          1..232
                     /region_name="DraG"
                     /note="ADP-ribosylglycohydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG1397"
                     /db_xref="CDD:441007"
ORIGIN      
        1 mlgaiagdii gsvfephwrr ikrkefdlfs kkskftddtv ltiavadail hqkeyvhtik
       61 dyyrrypkag ygktfrewga sdsmepyhsw gngsamrvsa vgfafddlet vlqeaeqsaa
      121 vthnhpegik gaqatavaiy lgrqgrskae iktyiettfg ynlssrleei rpqyqfdssc
      181 qgsvpqaita flestdfeda irnavslggd sdtqaciagg iaqgfyggvp eriaqetwtr
      241 ldadlqqvve afnaiyqiq
//
LOCUS       WP_010468307             315 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010468307
VERSION     WP_010468307.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..315
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=34975
     Region          1..82
                     /region_name="Methyltr_RsmF_N"
                     /note="N-terminal domain of 16S rRNA methyltransferase
                     RsmF; pfam17125"
                     /db_xref="CDD:465356"
     Region          <51..290
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 msklltkfsl klwsdpqqqq afiqaltepq pyspciawik ertdkaffqr vdalpwqlpf
       61 vdrlavgerp gkhdlhhqga yycldfssvf aatpltvirk kpnvvldlca apggksllaw
      121 rllqphllvs nevigkrvgm lisnlkrcqv kpvqvlsadp svlaeaipas advvlvdapc
      181 tgqsllakge sapgcfhpas iqhnvkrqrr ilanasrlvv pggylaymtc afseaenerv
      241 crwftrrfln fepqtvdall tfqshltdmp cyriwpqsgl gagaftmlfr ntqgaesmvq
      301 plgawldena rwsse
//
LOCUS       WP_010468383             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Streptomyces].
ACCESSION   WP_010468383
VERSION     WP_010468383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..272
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29080
     Region          2..110
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(3..5,19,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            40
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(51,54,58..59,68,82,86,92,96,99..100)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          121..266
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mftigdfarh grvsvrmlrh ydavgllrpa rvdprsgyrf yeagqlarln rvialkdlgf
       61 tldqvrsivd eevgadelrg mlrlrraele tavaeatvrl grvaarlrai esegrmptqd
      121 vvvkslpavr laelsgtaag fepaeigpvv sslyeelcar laaagvtdlg pgltyyedap
      181 sgdgailaha gvivppgtav pgvdlvdlpp varaatvihr gpmdqvlptv qtltawtaah
      241 ghrssghtre lylecpqdpa gwvtelqepl ad
//
LOCUS       WP_010466286             123 aa            linear   BCT 01-JAN-2025
DEFINITION  TraR/DksA family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010466286
VERSION     WP_010466286.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 123)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..123
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13211
     Region          1..121
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mdktqaapfr qlllaqqsgl raqlaaqrgg vigraeaaad hfgqpedpra qlaterelef
       61 alderetthl aaveaalari edgtygectd cgthitaarl hatpeaarcv hcqekaeqhr
      121 raa
//
LOCUS       WP_010468397             290 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010468397
VERSION     WP_010468397.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..290
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31346
     Region          3..283
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mpwariisgl iaivlalgmi llggwyftlg fcilvylaqd eyfdlvrakg nrpagkttmi
       61 vsqlllitat ingmladavl pvagtficfy llfqpklati sdisssilgl fyggylpsfw
      121 irlrslgtpe asnlplwgyw peqwsninll pvgltitlla fgciwaadig aytfgrlfgk
      181 trlsdispkk tvegavfgvl gsltvaiiga ytfiwpfwlf lgaalgllig vasllgdlte
      241 smmkrdagvk dsgqlipghg gildradsyv ftaplvyyfv tlllplieai
//
LOCUS       WP_010468399             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Uma2 family endonuclease [Streptomyces].
ACCESSION   WP_010468399
VERSION     WP_010468399.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..193
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21522
     Region          10..157
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mpalpdwmrp praegwfaed ldhlpeaprh telidgalvf vvppqrswhg rlvtaltttl
       61 maqapsgvev eremtirlda rnrpepdlll thlpydpdrt wyapedvslv vevvspesah
      121 rdrtvklrky aeagiphywc iededgapvv hvyeldeptg ayapagifrg alqrpvpfei
      181 gigldkltpp rsg
//
LOCUS       WP_010468400             108 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010468400
VERSION     WP_010468400.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..108
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11667
     Region          2..95
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(13,15..17,23,46,48..50,52..54,57..58,80,84..85,87)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            49
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mrpnvttiqp nnildgvtga vfrqevaaav eagadivlvd cqdisfmdss glgalvlalk
       61 fmraaerqlv lcslnqqvkt lfqlteiaqv fqiydnrqhf eqsgllgs
//
LOCUS       WP_010468415            1407 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010468415
VERSION     WP_010468415.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 1407)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1407)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1407
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..1407
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=158450
     Region          724..1387
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mfesstassk kqaqlaadyl alspldqqlv qvlsvayepv nrsailtcln rqaaadsdyk
       61 twdskllkqh leglldqgiv lqergqgpqc hpllaeiatr dvlemgkfet lapiiqgavp
      121 vyepwgsgpr sfrseaqflr earigfysqd lkflteqlsd yqkvfkrqdp lslddvitii
      181 cnnpfdadwi qtlptdfyel altsilsnsi ldlssseeaf evlqedfanq ktrcsdylkv
      241 vlaeqlllrs yveevssvle sideknqdnt apywgwlafl qgdtdqsidl ftsaltelrk
      301 tkrkrsyyft sisglffila llqegsserl iqaqgyvqhm vrksgywlrt tyswldsliq
      361 iqqgnlstkk tllqaslnpy eghhsldilf galcqywvda ekakkwlprv lsplcrqatq
      421 sgyhwfamet aeliaklete eadnpyqaqa qllrqgsgik plvdiirsqe pwelclnala
      481 hlqqeapvvq aelrlawfit lygqtwllqp keqkmtakgg wskgrpialk rlygkpgefn
      541 yltdqdlrvc sqletyssyg sygyynktey rfseeaivel ishplvfwed apttrvevvk
      601 gepelliqkq kgdklaltfs palkasqtlv vtketptrlk iidikpehrq ianilgeknr
      661 ltvperakeq vlaaigavss lvtvhsdigg gvasatevpa qalphvhllp ageglkvavl
      721 srpfaeggpy yppgsggetv iaeiegqrlq tirnlvkerq lakaaiaacp tlakltpqdh
      781 ewlvedpeac lelllelqdl kesvvlewpe geklsvrhra dlgqlqlqik rqrdwfaatg
      841 elklsddlvl dmqallalle qtpsrfipig egqfialtqe frkrlddlra yseqqgkglr
      901 fhplttmtle dmvedvgklk vdkhwkahvq klkdvqalqp qlpttlqael rdyqqegfew
      961 larlshwgvg acladdmglg ktlqalavml trapegpalv iaptsvglnw iseaqrfapt
     1021 lrplqfgtsq rqelldqlqp fdllvcsygl lqqeevaqml aqvnwqmivl deaqaiknmt
     1081 tkrsqaamnl qaefkllttg tpienhlgel wnlfrfinpg llgsmerfnq qfaapieksq
     1141 dpqarqrlkk liqpfllrrt ksqvleelps rteitlqvel seeemalyea lrrkaianla
     1201 dsdaqagakh lqvlaeimkl rrtccnaqlv mpesppasak lqlfgevlee llanhhkalv
     1261 fsqfvdhlki lqdyldkkqi ayqyldgstp akvrqqrvka fqsgegevfl islkaggtgl
     1321 nltaadyvih mdpwwnpave dqasdrahri gqrrpvtiyr lvakntieek ivdlhrhkrd
     1381 ladsllegte isgkistdel lrliqng
//
LOCUS       WP_010468565             422 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces somaliensis].
ACCESSION   WP_010468565
VERSION     WP_010468565.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..422
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43681
     Region          22..419
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 madadgtfvi vggglagaka aetlraegfp grvvlvgdet eppyerppls kgylsgeedr
       61 dgvlvhepaw yarsgielll grpatavdrd rrevrlgdgt avpydrllla tgaeprrldv
      121 pgtdldgvhr lrrlhhadrl raalaglgrd nghlvvagag rlglevaaaa rgygaevtvv
      181 epaatplhrl igpelgqvlt elhaehgvrf rfgvrltgiv gqdgevlaar tddgeehpah
      241 avllavgavp rtalaeaagl alagpahggg iavdaslrts dprvhaagdv aavhhpllgv
      301 rlrsghrdga lhggpaaara mlgrdvsydr lpsfssrqyg lalehsgwap pgsydrvvlr
      361 gdvggrrfla fwlkdrrvla gmsvgagdga grvrdlvrag aagaavdpea ladpsaplpp
      421 ap
//
LOCUS       WP_010468472             257 aa            linear   BCT 01-JAN-2025
DEFINITION  ZIP family metal transporter [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010468472
VERSION     WP_010468472.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..257
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26233
     Region          1..255
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mnlivvgsia sliaglatgi galpvlfvkt ltdrlqgifl gfgggvmlaa tafslivpga
       61 dlamgqgnte tqaalimvlg illgggflwl ahnnfphehf fkgqegpstp nlariwlfvv
      121 aitlhnfpeg mavgvgfsgg slssgialai giglqnmpeg lvvavalrsl nysslyalgv
      181 acltglvepi ggvvgasiis laqpllpwam afaagamlfv isdeiipets rkgiqqegtl
      241 gimlgfvvmm yldvalg
//
LOCUS       WP_010468525             213 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010468525
VERSION     WP_010468525.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..213
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23000
     Region          4..192
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mdwisldtlq tlahqygywv vcfgimlenl giplpgeaiv lvggflageg dlnyfgvlgs
       61 aiagstiggt cgywvghfgg wsllsragrl vnmseerlle ikdgfstnaa rtvligrfva
      121 llrifaspla giaempfprf affntlgacl walvmvtlay fageiiplsr lvssvsqfgl
      181 fvllaiaawl lwprlhnlir rtalqeases dtp
//
LOCUS       WP_010468474             490 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010468474
VERSION     WP_010468474.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..490
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53310
     Region          24..>156
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mnrqrflvlv taiiliaisw lgvfkarsgl vvrsltandi pmifiapkns dpvpgvliah
       61 gfagskqlml gygytfaqag ygsllwdfsg hganpaplnm etlqpdleva yqalteqpev
      121 dperlailgh smgssavmta sieqrdrfda tiaisptrae vtadkpanlq lqvgsgegqf
      181 vesarkllqt aggknqnlae grgrklivvp kvehitilfs dishqsalqw lnqtfnqfkt
      241 ssymdrrigw yglhligglm alaaivpwfa apavqqaflk pwqnwgglla aplaatagvs
      301 lisrgvelen lgglkvggal giwfclggli wigvqglwpi kkrrygqfsp artvgtgmlv
      361 fillwfafga maqvvwvqww liparlqlwp llslaclpwf lasgiaqqei giskrllwwl
      421 gqtvvliagl vwtislipql gfiflllpif piffgilsfv aayvknawsy gigsalffgw
      481 slaaafplva
//
LOCUS       WP_010468522             431 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [Streptomyces].
ACCESSION   WP_010468522
VERSION     WP_010468522.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..431
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=45866
     Region          22..419
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mtgglvagav alvvvawlaa caeaglarvs gfraaeavrs grrgaarlaq vasdptryln
       61 vallvrvace maagalvtya cleefagtws alavaigvmv lvsyvavgvs prtigrqhpl
      121 ntataaayvl lplarimgpv pqlliligna ltpgkgfrkg pfaseaelra mvdlaeresl
      181 iedeerrmvh svfelgdtlv revmvprtdl vsieryktvr qaltlalrsg fsripvtges
      241 eddvvgivyl kdlvrkthin reaeadlvst amrpaafvpd tknagdllre mqrernhcav
      301 vvdeyggtag ivtiedilee ivgeitdeyd relppveelg dgryrvtarl digdlgelfg
      361 ldayddedve tvggllakal grvpiagasa vvglpdgral rltaespagr rnrivtvlae
      421 pvppepedea a
//
LOCUS       WP_010468613             278 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010468613
VERSION     WP_010468613.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..278
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31443
     Region          195..278
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mklilfedav afcdrtqpyl lrypaehnll lgiqsalvrv peafttspdl flvesageiq
       61 avgmrtppyn lvlskvqnls aveiivdyfq qaetalagin sfireaqafs qawqshtgqs
      121 stlkmhlrih qltqvhrpms vqgylrkatr rdrkqllews eafsletfga letdierild
      181 lqikrqdlyv wcdrkqvsmv vgrvsqpggg rigpvytppd crrrgyatac vaavsqmlld
      241 rgaqrcclft ditnptsnhi yqtigyeavc dwydyrfa
//
LOCUS       WP_010468664              78 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Streptomyces].
ACCESSION   WP_010468664
VERSION     WP_010468664.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..78
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=8366
     Region          1..77
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 msatydrlve ivtklhdapg drigpdatfa qldvdsltmv eiamgierdl gvhiddselr
       61 edltlgatae lvdsklar
//
LOCUS       WP_010468750             239 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010468750
VERSION     WP_010468750.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..239
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25884
     Region          <104..222
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 matietlqqi idkqavisle tfregktill eniqsklkdi gaytfildgl ygprteialn
       61 kfcnavfldn mqtqligptf aqklldappp sfsagpgqdn ffirpveqgv vtsefgyrih
      121 pltglnrlha gidiggnnrk pifaasggtv siagfvsgyg nfieiqhnni fssayahmen
      181 ffvnvgdtvn qgdligrvgq tggvtgphlh feilqngsfi nprdkvafpa rgiefslln
//
LOCUS       WP_010468778             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010468778
VERSION     WP_010468778.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..146
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15963
     Region          1..135
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 meeldrrive llvkdgrmsy tdlgratgls tsavhqrvrr leqrgvirgy aavvdpqavg
       61 lpltafisvk pfdpsapddi adrladipei eachsvagde nyilkvrvat pleledlltr
      121 irsqsgvstr ttvvlstpye arpprv
//
LOCUS       WP_010468830             478 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RsmB/NOP family class I SAM-dependent RNA
            methyltransferase [Streptomyces].
ACCESSION   WP_010468830
VERSION     WP_010468830.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..478
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=51302
     Region          28..478
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mseqdrrrpp rphrrprkdp arllafealr avderdayan lvlppllkka rerdgfdard
       61 aalatelvyg tlrrqgtyda vvaacvdrpl revdppvldv ltlgahqllg tripthaavs
      121 atvelarvvl gdgrarfvna vlrriaehdl dgwlekvapp ydedpedhla vvhahprwvv
      181 salwdalggg ragiedllra dnerpevtlv arpgratpae lldvlgegag epgrwspyav
      241 rlaeggepga idavregrag vqdegsqlva laladapldg pdarwldgca gpggkaallg
      301 alaarrgaal laaekqphra rlvrralagn pgpyevvtad gtrppwrpgs fdrvlvdvpc
      361 sglgalrrrp earwrrrped legfaplqrs llaealkavr vggvvgyatc sphlaetrav
      421 vddvlkghgg aqdtaaewid arplmpgvpa lgdgpdvqlw phlhgtdamy lallrrta
//
LOCUS       WP_010468849             173 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease [Streptomyces].
ACCESSION   WP_010468849
VERSION     WP_010468849.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..173
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19356
     Region          66..122
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mrdtlvlnas feplstvslh ravvlvlqdk avveqahpel rlraaqvelp vprvirlcry
       61 vrvpfrrhap wsrrgvlvrd qyrcaycgrr attvdhvvpr sqggadswln tvascaednh
      121 rkadrtpeea dmpllrrpfv pspadamlla lragerselp ewlavqrpea aaa
//
LOCUS       WP_010468916             266 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Streptomyces].
ACCESSION   WP_010468916
VERSION     WP_010468916.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..266
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28040
     Region          16..244
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtsldpdlvv ldkdavrlav edavatvtla dpakrnaqsp amwralaeag ralpgsvrvv
       61 vlraegrsfs agldrqaftp egfdgepsfl dlargsdkel daaiagyqea ftwwrrndiv
      121 svaavqghai gagfqlalac dlrvvtqdvq famretglgl vpdlagtqpl vaavgyaral
      181 eicatgrfvh adeaerigla nlvvpadeld atvrdlaaal laaprdavve tkallrgaag
      241 rtydeqraae raaqarrlrd laglsd
//
LOCUS       WP_010468946             564 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010468946
VERSION     WP_010468946.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..564
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=61122
     Region          228..550
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mvirlylaag lgialiglgi qpslgqtpea tapesklnrd ssllsvptqa sdveinldqp
       61 ltlqqayela lrnnltlqvt elqlqqnqsf lsqakaanwp tlsvqsaltr tdsanfllnq
      121 tpiqvdaaaq lqaqqrtlls lqtqqfqsqq elsidiqqlq lrlqqdqnqs qqqifdqqiq
      181 qlqlrantsa tsfaitnvtp lqpiaavpis qgnqggisnr iqgtisatyn iytsgfrsgq
      241 ieaakaqvki selelkrqle qlrldvandy ynlqqssali tvskdavrna easlevarvr
      301 eqagigtkfd vlqaevqlad tiqnatqaen lqkiaqrqla qrlniketvn lsaadqvnia
      361 ggwllnleds ivlalqnrve laqllsqrrl aqqqrrvala ankpqlqafa saevvdeldd
      421 dvsgafgysv glqvsinffd ggaaksnaaq qeeniaiaet qfadtkndlr feveqayadl
      481 qsnlrninta qssvqlaees lalarlrssa gigtqldvts aensltqakg nlisailnyn
      541 ralialqrat sfaqpvsgvt plgg
//
LOCUS       WP_010468950             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Streptomyces].
ACCESSION   WP_010468950
VERSION     WP_010468950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..192
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20882
     Region          28..170
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mttgteprpa vyehavdgfg tvrlvpvdpd rdaallhswv gedrarfwgm rdmsvedvrd
       61 vyahldsltt hhaylahrdg vpvalfqtyd peadrisecy ealpgdigvh llvapaatpe
      121 pgftahlmea lvayclsghr rivaepdaan akavallars gfelgpevvl pevvlpevrl
      181 aqkrarlafl gr
//
LOCUS       WP_010468976             400 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar ABC transporter permease [Streptomyces].
ACCESSION   WP_010468976
VERSION     WP_010468976.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..400
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40889
     Region          36..392
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mnalrralgs gveaagrrlg tgepgvlpvv vgvlviwsvf qglngnflap rnlsnlgvdi
       61 vgpgmiavgv vfvlligeid lsvgsvsgla aalfavlsvr hgvaewlava aavlcgaaig
      121 alhgllvarv gvpafavtla gllgwnglml yvlgaagtvn ldeesllgrl tghyfhevaa
      181 ayglaaagsv lyflvshrdr rrrraagmph rpltriavrt gavalvafla ahvlnrfqgl
      241 plallafllv vggldlvlrr trygrkvyal gggggeparr agidvvrvrv svfalsgtma
      301 avgglflasr itsvsqtsgs slllmnviaa aviggtslfg grgttwsall gmlviqsias
      361 gmsllgieaa vqftvtggvl laavvvdtva rrirrehgra
//
LOCUS       WP_010468986             226 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Streptomyces].
ACCESSION   WP_010468986
VERSION     WP_010468986.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..226
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23637
     Region          5..196
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mhvqewletv pavsiyilvg vvigleslgi plpgeivlvs sallasqhgd idpyvlgaca
       61 sagaivgdsi gyaigrrggr pllawlggkf pkhfseania laersfqkwg vwavffgrfv
      121 allrifagpl agvlrmpywk fllanvfggi lwaggttavi ysvgvvaeaw lkrfswlglv
      181 lavavgltsm lvlrhragka aekseaeraa tapagahqap apaaad
//
LOCUS       WP_010469019             153 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Acaryochloris
            sp. CCMEE 5410].
ACCESSION   WP_010469019
VERSION     WP_010469019.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..153
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16735
     Region          11..144
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtqrfdisqs dpnayqamvg letylrkcgl qpqllhlikt rasqingcaf cidmhtkear
       61 adgeseqrly glsawaetpf ftpaeraala ltevvtrise qavpdavyae acqhfsetev
      121 tqllmaivti nswnrlaias qvlpgsytvp vaa
//
LOCUS       WP_010469087             534 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Streptomyces].
ACCESSION   WP_010469087
VERSION     WP_010469087.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..534
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56612
     Region          150..>363
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
     Region          430..529
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mpttrparrt tarrttarrr tavlaaaall aaaagcggdg grdggedagg eamrklaaqk
       61 lswkpcapsa teggevppsp lpdgtrweca fmdapldhad pggetielal iragardrsr
      121 rigsllfdfg gpgvsgvtal psftpeyetl rrrydlvgfd prgvglssgv kclepralda
      181 ffardatpdd aaeerayqna lkeyaqacee rsgevlphvg tenaardmdl mrrvlgddrl
      241 hyfgfsygte lggvyahlfp rrvgravfda vvdpgataee galgqakgfq lafrnfaadc
      301 vrrgdacalp ggtpqeierf vtgllerlde rpvrgigdra ltqthaangi aqalysreyw
      361 kyleqgldea dggdgallla lsdslngrde ngdydnlqaa naaincvdtr qrftaeqvra
      421 rlprfreasp vfgellawgm lgcsqwpvpg rsdrpdvsap gappilvvgt tgdpatpyeg
      481 aaamasalge gvgvrvtyrg eghgaynggd acvrrvvdgy lldgkvpepg tvcp
//
LOCUS       WP_010469114             171 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Streptomyces].
ACCESSION   WP_010469114
VERSION     WP_010469114.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 171)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..171
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18657
     Region          43..153
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mslhddavlv lkgyedqedl rraylehlaa hedamwrtca aghltasalv vdpergrvll
       61 tlhrklrmwl qmgghcepgd rrvaaaalre ateesgvpgl allpggpvrl drhptpcawh
      121 ldvqyaavap pdavaaisee sldlrwfayd evarvadgsv arlveatrar l
//
LOCUS       WP_010469190             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Acaryochloris].
ACCESSION   WP_010469190
VERSION     WP_010469190.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris
  ORGANISM  Acaryochloris
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10508417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Acaryochloris"
                     /db_xref="taxon:155977"
     Protein         1..269
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29410
     Region          19..260
                     /region_name="UPF0014"
                     /note="Uncharacterized protein family (UPF0014);
                     pfam03649"
                     /db_xref="CDD:427424"
ORIGIN      
        1 mlqnlsipqs llalivlqpi dlawalglma iaiglsvwqq ldltwslfla mgrtilqlmi
       61 mgyvlwfifd wkhpgavlal vagmltvasi esrnrigkdi phlipwlwgs ifistvltls
      121 yttlfilqpe nwfdpqylip lagivmgnam ngaaiagerl vkslkanrne iethlclgas
      181 pqqaiaqyrr dairaglipt inammvvglv klpgiitgql lsgvnpqeaa syqilimfml
      241 afatlvttll vakgvyrqff nasaqltlp
//
LOCUS       WP_010469197             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase family protein
            [Streptomyces].
ACCESSION   WP_010469197
VERSION     WP_010469197.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..181
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19367
     Region          3..177
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mnkvyaslgl sldgflagpr agpdnpfgdg garlrewlvt pedparagay vmgrrtfdeg
       61 eriwsdpppf gapvfvlttt ardaqvregt vftyvtdgvh aaldrarava gsrdvrisgg
      121 ahtvrqylne glvdelvlhl vpvlvgsgvr lfdgvdpalr lakapavdva elthlryriv
      181 h
//
LOCUS       WP_010469198             209 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010469198
VERSION     WP_010469198.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 209)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..209
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22494
     Region          1..205
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 msyifqnpdl vlelllehlq mtgialggav iiavpiawii yrwtwlqgpi mailgviyti
       61 pslalmilli pllglssmta ivamtlyaqv ilvrsilvgl qsipqpilea aqgmgmsawq
      121 cwwqvqvplm rpvflagvrl attvmialgt iaakfgaggl gvllfegiaq agrydkiwag
      181 tivvgllavi sngllwlweq qlqpksppv
//
LOCUS       WP_010469260             361 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Streptomyces].
ACCESSION   WP_010469260
VERSION     WP_010469260.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..361
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36085
     Region          140..359
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mfvawrdlkf akgrfalmgt vivlitllvg llsgltaglg rqntsaitsl padaiafgsp
       61 ggeepsyans tvderqwqrw artpgveaae plgitttras agsrsagvsa fgvrpgsala
      121 pesgridgra avlstaaaad lgvaegdgft lagqevtvaa vsgdaffsht pvvwtsldlw
      181 rkavpptgkg gaptatvial dtasgvdvga adraagtrtv srddslsaig sytsengslq
      241 lmrgflfais alvigafftv wtiqrsgdva vlkalgasta tllkdalgqa vvllvggtli
      301 gtgaaaglga lvagsdvpfl ltpatvllpa avmialgvlg aalsirrits vdpltalgsa
      361 r
//
LOCUS       WP_010469276             143 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010469276
VERSION     WP_010469276.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..143
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=15210
     Region          <33..139
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mkrsllvafa fltpllwacp vqaadpeqvq qllatntcpg cdltnadlrq thligadlrn
       61 adltgaqlqe anlegadltg arlkqadltd afltnaslnl thlesvnltr arlynvearg
      121 aviadlnltd vkmwgtpisv gge
//
LOCUS       WP_010469445             366 aa            linear   BCT 01-JAN-2025
DEFINITION  saccharopine dehydrogenase family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010469445
VERSION     WP_010469445.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..366
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39574
     Region          33..359
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mrtedgilia ggygvvghqi tslirqrhsd lpliiagrtl dkaesvahql gnassisldv
       61 eqpnpleglk praiiavvnd phdyllrdav kngipyvdit rwserfkdai awlsveklka
      121 pvllssgwmg glaaviaval aqsqhqvnsi disvlfstkd ksgpnsveym drlatpfevm
      181 idgehrhvfp ytdprtttfp ggyttkvyrf dtpdlltlps tigaktvsar iafddassmn
      241 llrfltrsgi wklisgdcft plrrsllynp gsgasheivi tvsgvdrdgh piaanamisd
      301 pkgqthltal galtqlerll gldgtpppap givypdtapq tdsvlqvlsd fgvsissqdf
      361 nrpyrk
//
LOCUS       WP_010469447             220 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010469447
VERSION     WP_010469447.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..220
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=23509
     Region          6..219
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 msellnvlvv gatggtgrat verlaaeghr vtafsrsadr laneidgitt vngdvtdpha
       61 veqavagqdv vivtlgiten plrvrflgpa rtpinvrsqg tkhvisamkk hgarrlivqs
      121 sygvgetqgf lgftdqllfs lllkpqiadt eiqeqyvras gldwvlaqpv hlkddeatkp
      181 flstqgetrl mqvarqtvak flalaaheea yvgqsvtisg
//
LOCUS       WP_010469459             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Streptomyces].
ACCESSION   WP_010469459
VERSION     WP_010469459.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..255
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26652
     Region          1..233
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mevtwwghat ctvedsgvrv ltdplfarrl ahlrrrrgal pppeaaladl vlvshlhadh
       61 lhlpslarla pgtrlvvprg avravpglrr leglritevg agdevavgpv avravpaahd
      121 grrlpvgphr spalgyvvrg aartyfagdt glfdgmaaav gevdvallpv ggwgpflghg
      181 hldagraara laalapraav pvhygtywpv gldavrphef hapgdefarl aarlapgvav
      241 hrlghgesvr pgaar
//
LOCUS       WP_010469484             584 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010469484
VERSION     WP_010469484.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..584
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64125
     Region          <448..576
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 msnlptnanr daaypeepgq anelnelrsl ligpdlkgrf enaqlrsedv srvlpeaiql
       61 tlktsdetvs eavmptveha ikssvntdqn ilsealfpim gpairkaiaa aiqnltdsln
      121 qslehslspq slswrfeawr tgksfaevll lrtlvyqveq vflihkssgl vlqhlaaata
      181 aaqdadlvsa mftaiqdfvr dsfsvsdeal gslqvgelti wvnegpqaii acvirgnppg
      241 klrqmmenal erihlvqerq lhefqgdssa fepsqpylee clqsqyqtkk krssplkwig
      301 gaagililgl gvwgflsnye rnqvqsfvdq lnresgivvl qtkkqngkyv isglkdplas
      361 kptdlisktd ldpnkvafsw epylsfdtef iesrvisllq ppetvelkvd angaiqasgt
      421 apqswiteak qlalrlpnvt qfntqqivpv eagaladika kleahtifft qnaqlvpqqd
      481 vklktvaedi kklaktakti nqtvavlveg htdtsgseli nlyvretrak aiisllskqg
      541 idknlfqvvs veppavekld sakisksnrk vtfkvifvqp sdad
//
LOCUS       WP_010469493             138 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010469493
VERSION     WP_010469493.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 138)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..138
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /calculated_mol_wt=15780
     Region          11..132
                     /region_name="NUDIX_DIPP2_like_Nudt4"
                     /note="diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase
                     type 2 and similar proteins; cd04666"
                     /db_xref="CDD:467551"
ORIGIN      
        1 mtpvegryqh saalpyliqp dglkvilits rkrsrwiipk geiepdltaw dsaakeawee
       61 agiegliate plgtyahqkw gstctvqvfp lvvtqlhrew qedhererrv vsvakayklv
      121 emkslrkmlg kfekwlnl
//
LOCUS       WP_010469558             348 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010469558
VERSION     WP_010469558.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..348
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36046
     Region          1..341
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mndlqvsglv kaygpgapvl dgldltvrgg alaavlgpsg cgkttllrvv agflkadagt
       61 vtvagrllgg pgvhlpperr rigivpqega lfphlsvarn iafglrdldr parrtrvgem
      121 ldlvglpgyg drmphelsgg qqqrvalara laprphlvll depfsaldsg lrgavraevr
      181 avlresgatg llvthdqqea lstadvvavl rggrvaqcaa peelyrrpvd pwlasfvgda
      241 vlvpgtadgd tattalgrvp laaapagrre glvllrpeql rivepggada egvvtdvrff
      301 ghdalvtvav dgldgpvdvr apaplrvepg rrvgvrltge atlhphgd
//
LOCUS       WP_010469512             395 aa            linear   BCT 01-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010469512
VERSION     WP_010469512.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..395
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42641
     Region          21..153
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          35..65
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(86..87,118,121..122,125,145..146,149,152..153,156,
                     176..177,180,183..184,213..214,217,220..221)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          99..125
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          113..256
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          128..157
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          158..184
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          195..222
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          249..395
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mivselvsvl seletgdfqs rwetakqipd fgepaieflv dllhnksddp elqwfvarvl
       61 gefnhadavi alaqlmqnae eddvaeiaaq mlaqigpqsv dalaalless psrlrvvsal
      121 aqmqdpiivp illkvvadtd vsvrvmavet lsrfhdvrvi sallqglsdl ngkvrqvaia
      181 gisyraplfq mhdhdpvali vpclndfdvq vcqtaalalg rlgtkeavea lsitagaetv
      241 plplkltivq algqigndqs vqmlqklwph prsslqvvdd edqtlaaviv kalalnrqvd
      301 rstealiycl hhqpvsdpal qktlasalgq sgqpqaipel iqllgipdmg vrlhaiaalk
      361 qispelaytq lqaladndtv dqnvrdgvai alqew
//
LOCUS       WP_010469618             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphatase PAP2 family protein [Streptomyces].
ACCESSION   WP_010469618
VERSION     WP_010469618.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..233
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=23761
     Region          26..188
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(105,112,129..131,173,179,183)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mplvravavg cgtaalvlll lvttawapll afdravaegl hplavrrpal tegmrvlsdw
       61 vwdpltlrll lgavavalwr agergpaall avmgllaaav qhgakalvgr erprwpdpvd
      121 saefaafpsg hamtaavvcg llwwaaarta rralagpvaa vgtvsavgvg vtrvylgvhw
      181 psdvlggwll gaclaaaavl ayerwaaarg rvpsrgagga drsrsaagta tgp
//
LOCUS       WP_010469650             213 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010469650
VERSION     WP_010469650.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22629
     Region          6..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgheqpdtrt riqeaaaalf rrngypgtgl kriateanap fgsiyhffpg gkqqlaeetv
       61 rtagaaygrm vlallesvad pvesvehafg aaaddlaatg yadacpiatv alevantdev
      121 lrvataevfa ewveagagwf grwvpdreaa rslaqsmimi legafvlsra ardpeplrva
      181 grtmaallra alertgvert gvertgvert ged
//
LOCUS       WP_010469702             139 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010469702
VERSION     WP_010469702.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..139
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15679
     Region          3..138
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mkqsadtivq vlkekglrvt pqryavyanl lsrtdhptve hllqdlnqdf pissqatvys
       61 slqalrdvgl vrevlleegv srydanvdph hhfrcrqcge iedipwncfq eislsnlrpg
      121 lkaqtyevtv sglcdrcqp
//
LOCUS       WP_010469712             158 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010469712
VERSION     WP_010469712.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..158
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18517
     Region          4..142
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          77..150
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mhlsidfrpi cdddlnnlkq iyastraeel qvlswsqeek eiflqrqfqa qhqyyqaqfr
       61 eaeylmileg nqpigrlyvd rrpdeiriid iailpayrgq gigssllqqi laegqcshks
      121 vrihveqnnr alklyqrlgf qkksengvyf lmewmpns
//
LOCUS       WP_010469765             266 aa            linear   BCT 01-JAN-2025
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Streptomyces somaliensis].
ACCESSION   WP_010469765
VERSION     WP_010469765.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..266
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28142
     Region          18..244
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mttpprhpap tpsfvpslev rglayaypdg hqalfgvdlt vergervall gpngagkttl
       61 vlhlngilta gagtvavagl pvgpanlaei rrrvgivfqd pddqlfmptv redvafgpaa
      121 aglrgpalda vvtralervg maayadrpph hlsfgqrrrv avatvlamep eilvldepss
      181 nldpasrrel adilrsldvt vlmvthdlpy alelcprsvv lsegviaada ptgelladge
      241 lmrrhrlelp fgfdpaavpt rgpgrh
//
LOCUS       WP_010469785             289 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Streptomyces].
ACCESSION   WP_010469785
VERSION     WP_010469785.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..289
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30690
     Region          20..287
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 msakdapppl peplpvavad shthldmqsg tveealtkag lvgvetvvqv gcdlagsrwa
       61 aetaaryanv haavalhpne aprivlgdpe gssrqgprea ggdaalddal aeidrlaald
      121 qvravgetgl dffrtgpegk eaqersfrah veiakrhgka lvihdreahe dvlrvlaeeg
      181 apertvfhcy sgdadmaric aergyymsfa gnvtfknaqp lrdalavapl dlvlvetdap
      241 fltpapyrgr pnapylipvt vramaavrgi geeematala entarafay
//
LOCUS       WP_010469827             330 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hydrogen peroxide-inducible genes activator
            [Streptomyces].
ACCESSION   WP_010469827
VERSION     WP_010469827.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Jo,I., Chung,I.Y., Bae,H.W., Kim,J.S., Song,S., Cho,Y.H. and
            Ha,N.C.
  TITLE     Structural details of the OxyR peroxide-sensing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 112 (20), 6443-6448 (2015)
   PUBMED   25931525
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..330
                     /product="hydrogen peroxide-inducible genes activator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34719
     Region          16..75
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          104..284
                     /region_name="PBP2_OxyR"
                     /note="The C-terminal substrate-binding domain of the
                     LysR-type transcriptional regulator OxyR, a member of the
                     type 2 periplasmic binding fold protein superfamily;
                     cd08411"
                     /db_xref="CDD:176103"
     Site            order(116,119..120,123,127,135..139,234,237..238,241,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176103"
ORIGIN      
        1 mfspahfahk gkqpslaqlr afaavaeylh frdaaaaigm sqpalsgavs aleealgvql
       61 lerttrrvll spagerlavr tkavldavae lmeeaeavra pftgvlrlgv iptvapyllp
      121 tvlrlvrdry pdldlqvhee qtyslleglt agrldvllla vplgvpgvte lplfdedfvl
      181 vmpgghrlgg rsdiprealr elplllldeg hclrdqaldv creagradga avtttaagls
      241 tlvqlvaggl gvtllprtav rveaerapal atgcfadpap srrialamra gaaraaefee
      301 laealrgala slpvrvlpag sgqtrqtgra
//
LOCUS       WP_010469828             495 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010469828
VERSION     WP_010469828.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..495
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=53992
     Region          4..>337
                     /region_name="K-ycf53"
                     /note="Signaling protein combining a Ser/Thr protein
                     kinase domain and the GUN4/Ycf53 porphyrin-binding domain
                     [Signal transduction mechanisms]; COG5752"
                     /db_xref="CDD:444462"
     Region          <387..477
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 meiyctrpnc qrpnnyfadl ddpqtlktvq qkfclscgmp liligrylps rllakggfga
       61 aylacdrytp glrecvvkqf qptglgpnqm qmaqslfqre aevleklgrh pqipdlfaff
      121 elpvsgrgsq paedffylvq efingktlee eledktqfqe keilellqel lpvlqfvhen
      181 gsihrdikps nimrhthtnm tqtgngllyl ldfgavkqva nvaaptpska tsiytpfyap
      241 peqthgnqvf pssdlyalav tcivlltgka pndlfdtshn qwkwrpyvqv sdrlalildr
      301 iletspqkrf qsaaeilaal gqphsslgqp lnysqpvpqs ppapaapast papsppspaa
      361 ptpqavspaa papvrvktpp sfsivrllgg aaftgfeggl lavaltsflg ttlvsggfwl
      421 glvavlvycq lqqwiervdl viiagltlli iffvpalqgg npiqsilllg vvsglvlmtl
      481 slvfrliygv lsqfl
//
LOCUS       WP_010469795             604 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Streptomyces].
ACCESSION   WP_010469795
VERSION     WP_010469795.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..604
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66276
     Region          8..507
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          542..602
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 maanlvnvea vskvygtral ldgvslgvse gdrigvvgrn gdgkttlirv lakleeadgg
       61 rvthsgglrl gvltqhdsld paatvrhevi gdladhewag sakirdvltg lfggldlpgf
      121 pqgldtvigp lsggerrria laklliaeqd livldeptnh ldvegiawla qhlrtrrsal
      181 vcvthdrwfl dqvctrmwdv qrgtvheyeg gysdyvfara ereriaatee tkrqnlvrke
      241 lawlrrgapa rtskpryrie aaneliadvp pprdtselmr fasarlgrtv fdledvtvqa
      301 gpkvllkhlt wqlgpgdrig lvgvngagkt sllralaeaa atqgerqpaa grvtvgrtvr
      361 laylsqdvae lppalrvlea vqqvrdrvdl gkgremtagq lcerfgftke kqwtpvgdls
      421 ggerrrlqll rllmdepnvl fldeptndld ietltqledl ldgwpgsmvv ishdrffler
      481 ttdrtfallg datlrmlprg ideylerrqr mveaasaapa appaaapaaa akasaadara
      541 akkelqrier qldkvstrea alhtriaena tdfelvakld aelrelaaer edletrwlel
      601 aeda
//
LOCUS       WP_010469860             312 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [Streptomyces].
ACCESSION   WP_010469860
VERSION     WP_010469860.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..312
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32965
     Region          104..309
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mdnlplltlg vtllagllav lgvhayaagr aqqkalvarm tqtgpapaag rgrrfpgldr
       61 rlrrtgpgrr lerklavtgl avtpaeyavy alagllalya avtavfapff galavlaglw
      121 gadafldwhr rrrteafinq lpeltrvlan atqaglalrt aismaadeld dpageelrrv
      181 adqlavghsl ddalgaladr lpsrelvvlv ttlvlsnrag gqvvgslrnl tgtlderket
      241 rrevatllsq ikvtalalpl lglgfllmin gmnpgaldem tgsfagqags vlafalyaag
      301 fmmirrlsrv rv
//
LOCUS       WP_010469923             128 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF423 domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010469923
VERSION     WP_010469923.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..128
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13035
     Region          1..126
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 makifllaga afgglsvaag afashalkaq lseksqqife tgtkyqmyha lalilvslll
       61 sraeggegll tlagyafiag ivlfsgslyg lslseikwfg pitplggvaf lvgwgciaia
      121 alksspis
//
LOCUS       WP_010470101             691 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: iron ABC transporter permease [Streptomyces].
ACCESSION   WP_010470101
VERSION     WP_010470101.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 691)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 691)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 691)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 691)
  AUTHORS   Koster,W.
  TITLE     Cytoplasmic membrane iron permease systems in the bacterial cell
            envelope
  JOURNAL   Front Biosci 10, 462-477 (2005)
   PUBMED   15574383
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11484808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..691
                     /product="iron ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=67762
     Region          48..690
                     /region_name="PRK10577"
                     /note="Fe(3+)-hydroxamate ABC transporter permease FhuB"
                     /db_xref="CDD:236720"
     Site            order(440,444..446,568..569,571..573,575..576,578..583,
                     585..587,628,635)
                     /site_type="active"
                     /note="ABC-ATPase subunit interface [active]"
                     /db_xref="CDD:119348"
     Site            order(445,447,452,507,509..510,513..514,517..518,521,
                     524..525,527,538..539,542,618,670,673..674,677,680..681)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:119348"
     Site            order(527,552,610,614,658,667)
                     /site_type="active"
                     /note="putative PBP binding regions [active]"
                     /db_xref="CDD:119348"
ORIGIN      
        1 mtgtavrppg aragrarrap rlpagpaavv aggvaalllv aaahlgygrs gvglgdllrl
       61 avgggdaear avllggrlpr tlaglaagaa lavagcllqs svrnplaspd tlgvtagayl
      121 avavgaitgf ppgglprggv afaggllaaa lvhavaggar grpahlvlag vsvtlalssv
      181 tavlvvlfqe etgavffwgh gslavadtgr slaalpllga glagglllar tldvlgtgdd
      241 targlgvpvg rvrlaavlla vlltacavav tgpigfvgla aphlvrfagv rrhavllpaa
      301 alwgavllla adllarvtsp tgnevaagvv talfgaplfl wlarrlppep aapgtvmpar
      361 ggrrppyppl laggaavvaa llagglllgd vavppgelpg llagggdell rgvvleyrlp
      421 rllvaalaga llavaggvvq tvarnpladl tvmgvsggag fgaalvlval psvpyaalpv
      481 aallggaaaf altyglslrk gsvaperlvl vgvgtfaltt aatnylvvga rfqvaqaltw
      541 lsgstyarda adlsvlagaa avgvpllvls frrldllalg edtprtlglp lertrlavla
      601 lavalaacav avvgtvafvg lvaphaarml tgsrahrllp vaallgaalm iaadtagral
      661 vapaeipsgl laaligtpyf vwhlrrghra g
//
LOCUS       WP_010470134             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010470134
VERSION     WP_010470134.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17310
     Region          1..136
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 midhldgrli allareprig vleasrrlgv argtvqarld rlqangvirg fgpevdpaav
       61 gypvtafatl eikqgqgadv rehlagvpev lelhtttghg dmlcrlvars nadlqrvidr
      121 vvgfdgivra staivmenpv plriiplveq aaadtapppp rrg
//
LOCUS       WP_010470179             396 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S41 family peptidase [Streptomyces].
ACCESSION   WP_010470179
VERSION     WP_010470179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..396
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40594
     Region          94..383
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mslpgpgfsl rprrigrgav lpvlfatvla taavtdslpr dgsapsraar ggpptapqsr
       61 agavreqvvr aavraaedgk pvakaaeeaa srsgdrwsav ydkdeyedlr raldgaytgv
      121 glwarrtadg rvevarvqrg gpaeraglrp gdrlrtvdgr svhgraaaev vallrgdgar
      181 aragsavvlg vqrgartwtl tlrrarlaae avtvrrlgda vlirvsaftr gsgelvrrav
      241 drapdgagvl ldlrgngggl vaeavaaasa fldgglvaty dlhgeeraly aepggdtgrp
      301 vvalidggtm saaelltgal kdrgravtvg trtfgkgsvq mpsslpdgsv aeltvghyrt
      361 pagarvdgrg iapdvpaptr aeerartvls glgaga
//
LOCUS       WP_010470247             160 aa            linear   BCT 01-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010470247
VERSION     WP_010470247.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..160
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=18502
     Region          20..141
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 mdsvkfqgis frvtnpplrp lsiqalsave dhlgflfped yrqfvttlgp gitnlsiqif
       61 spqrivdifl sevrerlsdc wfwdnspnvl tqaqavecvp ffdsnlgddi lfhpsdpnrw
      121 filgheeeev vvvqsfqelf dfylkiyddl qppyefdsye
//
LOCUS       WP_010470383             749 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: transglycosylase domain-containing protein
            [Streptomyces].
ACCESSION   WP_010470383
VERSION     WP_010470383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..749
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=79736
     Region          1..680
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mpknrsgggl tatqqaakfl gvsvlsgvvl aglampaaga lglaakgtvq gfdeipasmk
       61 rpplsqrtri ldaeggliat vyyrdrtvvp lkdispymqk aivaiedsrf yehgavdlkg
      121 vlramnrnaq eggvaqgast ltqqyvknvf veaagddrdk faqatqqtlg rkiqelkyai
      181 qvekelgkkt ilenylnitf fgqqaygiea asqryfskra kdltlgeaam laglvqspsr
      241 ydpvndveea tnrrnvvlqr matvgdisqa eadrakaepi glkvtqpkng citardgagf
      301 fcdyvrevfl sdrvfgetre erakiwnrgg ltirttldpq aqkaaqnslk dhvyqgdkva
      361 aaitmvqpgt grilamgqsk pygfgknetq inysvnrgmg gsnfgfptgs tfkpfvaaaa
      421 ieqgkpasqv ypspykmpyp dtvqscsgtp wrnvendtve nenesevgpy alreameksv
      481 ntyfvqmlge igmcpvvrmt dklgvvmgdd kklpekpsal tlgsqgmspl tmatayaafa
      541 nrgtyctpta iesistsegr slkvprstce ramtertadt inkllrgvvd sgtgqeaglq
      601 sranagktgt tdsrrnawfv gytpnlsgav wvgsptqqvk mesitiggry hdkvfggkvp
      661 gpiwkdamtg aleghpapaf ndvpipeapk pqppaptpdp gggdkpggnq pfpgfsfpsd
      721 llggtqtggg gngngghggn gngnggrdr
//
LOCUS       WP_010470405             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SURF1 family protein [Streptomyces].
ACCESSION   WP_010470405
VERSION     WP_010470405.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..255
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=26962
     Region          3..244
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 myrflttprw wginvfvlla ipfclfmgvw qlgrfedrvd shreaeqrpa sraagaaapl
       61 aellpvdket sgrratasgr ygkqflvpgr eldgkagsyv ltllhtpegk vlpvvrgwlp
      121 kgaaapappp gevtvtgalq asehagsgga haagglpegq vgiisaaslv nlvpdevyda
      181 wvtlgespag ltpvpaaaaa gtgldlkafq nlgytgewfa fagfvvfmwf rlfrreaeae
      241 rdralgldpe tpgtl
//
LOCUS       WP_010470464             460 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: replication-associated recombination protein A
            [Streptomyces].
ACCESSION   WP_010470464
VERSION     WP_010470464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..460
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=49026
     Region          10..451
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mepdlftaaa edrqekepsh splavrmrpr tldevvgqrh llkpgsplrr lvgeggggpa
       61 gtssvilwgp pgtgkttlah vvsratdrrf velsaitagv kevravidga rraaggfgke
      121 tvlfldeihr fskaqqdsll pavenrwvtl vaattenphf svispllsrs llltlepltd
      181 ddlrdllrra ltgerglage vtlpedaeah llrvaggdar raltaleaaa gaalakgepe
      241 itlatleetv draavrydrd gdqhydvasa liksirgsdv daalhylarm ieagedprfi
      301 arrlmisase digladptal ptavaaaqav amigfpeaal tlshatiala lapksnaatl
      361 aiqaaradvr aglagpvpph lrdghykgaa glghaqgyvy phdvpggiaa qqyapdavre
      421 rryyrptrhg aearyadvve kvrerlrgdg aeprrpprer
//
LOCUS       WP_010470469             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptidylprolyl isomerase [Streptomyces].
ACCESSION   WP_010470469
VERSION     WP_010470469.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..262
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=27354
     Region          92..262
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mvnndqrrrq larekferqq rrreesrrka krrntivaaa lavvlaagga vyasvqltgr
       61 gtdrvdaadg pgatpapgas spspepsmav dteaaytmtl ktnvgdmvis mnaartprtv
      121 nsfkhladgk yfdgtkchrl ttqgifvlqc gdpqgdgtgg pgynipdedl aslgkagpdg
      181 kvtfkagtva mantgspdsg gsqfflvyrd trlppqytpf gtldaaglka vrdvaaagve
      241 ggtgdgapkk pvtvekatvs kr
//
LOCUS       WP_010469760             350 aa            linear   BCT 01-JAN-2025
DEFINITION  energy-coupling factor ABC transporter permease [Streptomyces
            somaliensis].
ACCESSION   WP_010469760
VERSION     WP_010469760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Rempel,S., Stanek,W.K. and Slotboom,D.J.
  TITLE     ECF-Type ATP-Binding Cassette Transporters
  JOURNAL   Annu Rev Biochem 88, 551-576 (2019)
   PUBMED   30485755
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18403195
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..350
                     /product="energy-coupling factor ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34617
     Region          1..205
                     /region_name="CbiM"
                     /note="ABC-type Co2+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG0310"
                     /db_xref="CDD:440079"
     Region          244..330
                     /region_name="PDGLE"
                     /note="PDGLE domain; pfam13190"
                     /db_xref="CDD:463803"
ORIGIN      
        1 mhvpdgfina pvsaaaglva agavaaglrg arrelgeera aplaglvaaf vfavqmlnfp
       61 vaagtsghll ggalaailvg pwtgvlciav vllmqgvlfa dggltalgvn vtvmggvtvl
      121 vayalfralv rvlprtrrsi taatfaaavv svpasaaaft llyavggttd vplgevlaam
      181 lgvhaligvg ealittatvg avlavrpdlv ygarglsapl klrvggelvd aapaprpapa
      241 agtrrvwaag lavsvllagl vsfyasaspd glervaadhg idrqarehaa adspladygv
      301 kdlddarlsg glagtigvca tlalgtgvfl aarrrrtgaa tpaarpteta
//
LOCUS       WP_010470601             287 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: spermidine synthase [Streptomyces].
ACCESSION   WP_010470601
VERSION     WP_010470601.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..287
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30147
     Region          36..231
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 marsrqrggr aaettaeavd gglaelvpdr erprawtllv dgapqshvdl ddpahldfay
       61 qrrlghavdl aappgrplrv vhlgggaftl aryvaatrpr stqqvvevda plvrfvrrml
      121 pldpaarirv rdgdaragla rlpdgwadlv iadvfsgart pahltstefl tevrrvlgpg
      181 gqyaanladg pplahlrgqi ataaalfpel alaadpavlr grrfgnavll asaaplpvae
      241 ftrrvagdph pgrvehgral adftggaapv tdasakaspk pppaafr
//
LOCUS       WP_010470627             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HAD-IIA family hydrolase [Streptomyces].
ACCESSION   WP_010470627
VERSION     WP_010470627.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..259
                     /product="HAD-IIA family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27750
     Region          8..254
                     /region_name="HAD_Pase_UmpH-like"
                     /note="UmpH/NagD family phosphatase, similar to
                     Escherichia coli UmpH UMP phosphatase/NagD nucleotide
                     phosphatase and Mycobacterium tuberculosis Rv1692 glycerol
                     3-phosphate phosphatase; cd07530"
                     /db_xref="CDD:319832"
     Site            order(13..17,45..48,151,184,208..210,213..214)
                     /site_type="active"
                     /db_xref="CDD:319832"
ORIGIN      
        1 maerkpiesw ltdmdgvlvh egvpipgada fvrrlrdrer pflvltnnsi ytardlrarl
       61 armgldvpve niwtsalata rflddqrpgg tayvigeagl ttalhdigyv ltdhdpdyvv
      121 lgetrtygfe tltkairlih ggarfictnp detgpsaegp lpaagsvaal itkatgrdpy
      181 fagkpnplmm rtglnaigah setsamigdr mdtdvlagle agmetflvlt gltapadvdr
      241 ypfrpssvvg siadlvdrv
//
LOCUS       WP_010470652             257 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010470652
VERSION     WP_010470652.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27171
     Region          2..251
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mrveidavtv eisgarlved aslragsgqv vgligpngsg kstllrcvyr alrptagavr
       61 ldgddllams tresarrlaa lpqdtaaefd ftvaevvamg rlshqravar etdedrrvca
      121 aaleqvgagh lagrgfltls ggerqrvlia ralaqqprvl vldeptnhld iaqqlevldl
      181 vrasgltvlt alhdlnlaai hcdavhvvdg grivasgaph dvltpallad vfgvrahrvp
      241 hpetgavrll fdrlptr
//
LOCUS       WP_010470670             157 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010470670
VERSION     WP_010470670.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..157
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16872
     Region          2..128
                     /region_name="ComGD"
                     /note="competence type IV pilus minor pilin ComGD;
                     NF040982"
                     /db_xref="CDD:468912"
     Region          2..63
                     /region_name="FimT"
                     /note="Type IV pilus assembly protein FimT [Cell motility,
                     Extracellular structures]; COG4970"
                     /db_xref="CDD:443996"
ORIGIN      
        1 mgftltetiv lvviigifat lstpsflgwl nqkkvddala kiegaiketq reaikrsqdc
       61 tinipkginq titgsclstg nreidevtid hsasadpwti sfdfkgrnrt pstdpgtlwl
      121 tipnssvqpk cmtisvgigl mragdyndtt spkcqap
//
LOCUS       WP_010470674             591 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fatty acyl-AMP ligase [Streptomyces].
ACCESSION   WP_010470674
VERSION     WP_010470674.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10148874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..591
                     /product="fatty acyl-AMP ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63630
     Region          18..572
                     /region_name="FAAL"
                     /note="Fatty acyl-AMP ligase (FAAL); cd05931"
                     /db_xref="CDD:341254"
     Site            order(172,175..180,182..183)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341254"
     Site            order(199,219..221,295,298..301,327..331,336,379,447,458,
                     461)
                     /site_type="active"
                     /db_xref="CDD:341254"
ORIGIN      
        1 mepfdhasgp slvhildqra lrtpdrlafr flpdgtsdhl vdwtyadlaa raeavaarlr
       61 ergvdggrvv laldpgldyv aalfgimrag ctavpcfppf grravarfls ivadcapsav
      121 itdarftgqv ddfhralpas sdrprwlfpd eefflarpdg gvpprvvepa llqytsgstg
      181 dpkgivlehe hllsncrvle khmgyeedrv gcswlppyhd mglmgtimla vhggwplvtm
      241 splhfvqdpy rwlkaisdhr vtitvgpnfa fdlcattvgd eelaaldlst lrqvfcgsep
      301 vsratldrfr drfgpacgfd pssvipcygl aeatlfvsgk plgvpgvpav rldrealerg
      361 evrrtgardt gaavdvvscg tvahghhvlv vdpdsrrpvp pgrvgelwva gpnvaagyhd
      421 rpdltaaafr arpegaadgp eylrtgdlgf lldgelfvtg rlkdlivisg rnlhpqdiee
      481 svtrvdpamr raaafsvraa drdeeevvvv aeyrgtpref aaresglrer vteavtadhg
      541 vrpaavhfgp pgtvltttsg kvrraatraa ylsgglkafa pvaeeagavl s
//
LOCUS       WP_010470695             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Streptomyces].
ACCESSION   WP_010470695
VERSION     WP_010470695.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..269
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28118
     Region          16..259
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpssrasstd aarsagtggv qslerafdll ermadaggev glselsagsg lplptihrlv
       61 rtlvacgyvr qqadrryalg prlirlgesa srllgtwarp hlarlveetg etanlalldg
      121 devvyvaqvp sghsvrmvte vgrrmlphst gvgkallahv ppeevralla rtgmpaater
      181 tittpegfla alervrasgy avddgeqetg vrclavpvpd apapaaisvs gpagrmteaa
      241 eerfapvlqe varalaaalk npsgprsrr
//
LOCUS       WP_010470697             612 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Streptomyces somaliensis].
ACCESSION   WP_010470697
VERSION     WP_010470697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..612
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=61826
     Region          25..276
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(25,48..49,78,83,88..91,103)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(32..33,35..38,40,52,54,86,102..105,109,111,148,150,
                     152..153,155,164..165,168,185..188)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(32..33,35..38,40,52,54,86,102..105,109,150,152..153,
                     155,164..165)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(36,109,111,148,150,152,168,185..188)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(164..172,181..188)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msggqhhggt vfqpleeddp rsvagyrlaa rlgaggmgkv ylsytpggrp vaikvirpdf
       61 aqdaefrrrf arevqaaqrv qglytapvid adtdarepwl atayvpgpsl adavrkhgpm
      121 pvdtvlllva giaealqvih gagivhrdlk pgnvllasdg prvidfgiar aadatsltgs
      181 gvtvgtpsfm apeqaaggev tpatdvfalg qvaayaalgg pafgegashg vlyrivheep
      241 sldglpdrlr elvtrclakd pagrpsvaev ltmchqasdq talrrpegwl pgavaaditt
      301 rtaapapaaa ttppppvapp agtaapapah patahaappt pppgfgpppa adpghaptpp
      361 phptpashpy ahpaagptpy gpgapttpap aaapkrgprt aliaaaavva favaggatay
      421 allnekdggt gqargtasgt sttppadada idqgegdlag eiagleadve vggsappetg
      481 tpatppqpvd fkgidltegy elsladdpvk pkedggdvry gisgistpgs grlvllrngq
      541 agsldtclde trfatsvdds qmskgsrmcl qngagdvall tvvgfspesd psdyvtldvk
      601 vwrgamdvep ts
//
LOCUS       WP_010470760             427 aa            linear   BCT 01-JAN-2025
DEFINITION  S41 family peptidase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010470760
VERSION     WP_010470760.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..427
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47003
     Region          46..424
                     /region_name="Peptidase_S41_TRI"
                     /note="Tricorn protease; serine protease family S41;
                     cd07562"
                     /db_xref="CDD:143478"
     Site            order(47..48,50..51,54..58,63,71,73..74,77,85..86,89,
                     92..93,95..97,101..105,107..108,228..232,234,237,251,258,
                     260..261,265..266,269..270,285,288..289,294..296,298,
                     305..310,313,315..317,331,335..336,339,343,356..359,
                     363..369,371,380..385,391..393,402..405)
                     /site_type="active"
                     /note="Domain interface [active]"
                     /db_xref="CDD:143478"
     Site            order(101..102,335,391)
                     /site_type="active"
                     /note="Active site tetrad [active]"
                     /db_xref="CDD:143478"
     Site            order(102,288..289,335..336,361,363..365,380)
                     /site_type="active"
                     /note="Peptide binding site [active]"
                     /db_xref="CDD:143478"
     Region          142..222
                     /region_name="cpPDZ_Deg_HtrA-like"
                     /note="permuted PDZ domain of Deg/high-temperature
                     requirement factor A (HtrA) family of housekeeping serine
                     proteases and related domains; cl49614"
                     /db_xref="CDD:483954"
     Site            order(144..147,148..150,159,162,188..189,192)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467621"
ORIGIN      
        1 mktviqklkr hksyllsfli tlgmglvlwl sqgtmssvss aqpslldavw stvnenfydp
       61 kfnsldwaal ksqyqpqvak assraekaev inemldqlqt shthlftvde payyqvlgif
      121 yprikelrtq lkstfpegkv qyegigivtq aiqgktfikt ifegspaaka glkvgdqiln
      181 vagqpfqaiq sfkgkadqpi kvriqrtadp ndqqtitvtp krfdctqmfv eaiansvqvi
      241 etdgqrigyi hvwslagdsh qqeledeviy grlknadalv ldlrdgwggd pmtalhlfts
      301 rgpsltsirr ngatstyqgq wnkpvvmlvn egsrsakeil aygfqqydig pvvgsstaga
      361 vvagrpylmp dqsllyvavs dvyidktarl egvgvtpdvv vpfpipyaqg qdpqkeraia
      421 marqaiq
//
LOCUS       WP_010470823             154 aa            linear   BCT 01-JAN-2025
DEFINITION  divergent PAP2 family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010470823
VERSION     WP_010470823.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..154
                     /product="divergent PAP2 family protein"
                     /calculated_mol_wt=16256
     Region          5..147
                     /region_name="YuiD"
                     /note="Acid phosphatase family membrane protein YuiD
                     [General function prediction only]; COG1963"
                     /db_xref="CDD:441566"
ORIGIN      
        1 mqdfgnilhn qvllvslaas liaqglkiii dliqngkinf rvlvetggmp sshsasvttl
       61 atcvgqvqgw dstefaiatv faiivmydaa gvrqaagkqa kvlnqivdem fqehpefned
      121 rlkellghtp vqvivgsilg vaiaillgpa glll
//
LOCUS       WP_010470803             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Streptomyces].
ACCESSION   WP_010470803
VERSION     WP_010470803.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..143
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16035
     Region          62..141
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mivrredgye idtapdrldi glvhhwlstd afwalgrsre tveqsvrasl nfgvyhpdgp
       61 qvayarvvtd latfawlcdv yvapahrgag igtwlagavr dhlapyrlkr vilstldahe
      121 vyervgfvpf pephklmmlk peq
//
LOCUS       WP_010470871             108 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010470871
VERSION     WP_010470871.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..108
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11887
     Region          13..92
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(13..15,21,44,46..48,50..52,55..56,78,82..83,85)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            47
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 msykiiqpls ltdgiglnqv rneidtvlne gvktilldlq dvtfinssai galvamhkav
       61 hgrsgklsic smrkqvslvl klsrmdqifd iftdkeefqq kneapiis
//
LOCUS       WP_010470877             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Streptomyces].
ACCESSION   WP_010470877
VERSION     WP_010470877.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..145
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15725
     Region          19..132
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mrtaalllse pppggaryrl tapnlpttpg iardwvvlvl rtanlprlve parlctsevv
       61 tnahrygrtp sitvevalad rrttvlvhdd rpgelprpat sdrytgeehg rglllvdsla
      121 edwgvrvldg rtkavcftlv dhegs
//
LOCUS       WP_010470910             242 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF4097 family beta strand repeat-containing protein
            [Streptomyces].
ACCESSION   WP_010470910
VERSION     WP_010470910.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..242
                     /product="DUF4097 family beta strand repeat-containing
                     protein"
                     /calculated_mol_wt=24697
     Region          43..>240
                     /region_name="YvlB"
                     /note="Uncharacterized conserved protein YvlB, contains
                     DUF4097 and DUF4098 domains [Function unknown]; COG3595"
                     /db_xref="CDD:442814"
ORIGIN      
        1 mrqllrglgv faasgiavga lascgivqgt theddavlsg eitsvridng sggvtvngvt
       61 dgshrlhrti efrgerptga thriengvli lggcghrcsv gytvavpagi pvggevssga
      121 vrlarvgsve vttssgrvem ngvtgtvrvr tsngridgtg ikadriqaqt sngrinlapd
      181 tpadvrartt ngdvtltvpe aayrvtvasn ngdrtvdvps dpagkhkldv rtsngditvr
      241 ng
//
LOCUS       WP_010470916             450 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010470916
VERSION     WP_010470916.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..450
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49439
     Region          4..365
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(14..15,18..19,22,54,109..110,112..114,117,137,
                     140..141,144,224,227..228,231..233,236,258,262,315..316,
                     320,324,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mqtflliwlg qvvsllgtkl tefalgvwvy qqnqsisqla lvilftylpn tlispiagsl
       61 vdrwdrrwam ilsdaaagig tliigalvlt nqleiwhiyl avgvnsifna fqvpaytaai
      121 sqltpasqys rmngmvqisr giarvispai agfligivgi ggiliidfst flialstlli
      181 arfpkivrtr ptkppqirrl lqemqfawry itkrpglsrl llfmstnffs vgilevvfwp
      241 lildfgsree lgyvlsiggs glllgsivmt awggpkrrvy gllyfiplqa gimlmaalqt
      301 sillaamglf vylfaqpiiv scnqaiwqsk vpqhyqgrvf alqqmieksl aifayivvgp
      361 lvenfleplm aggpfaetvg pyiggigegr gialmvlmmg ignlvatama frsrrlrrld
      421 veiptvktld rptsksdird aysfeevtsp
//
LOCUS       WP_010470925             551 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid adenylation domain-containing protein
            [Streptomyces].
ACCESSION   WP_010470925
VERSION     WP_010470925.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10147744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..551
                     /product="amino acid adenylation domain-containing
                     protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0043038 - amino acid activation [Evidence
                     IEA]"
                     /calculated_mol_wt=59625
     Region          43..518
                     /region_name="A_NRPS"
                     /note="The adenylation domain of nonribosomal peptide
                     synthetases (NRPS); cd05930"
                     /db_xref="CDD:341253"
     Site            order(175,178..183,185..186)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341253"
     Site            order(178..179,295..296,317..322,346,409,421,424,512)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341253"
ORIGIN      
        1 mtkssvptas ptslppwsid padqagpapa lgdlvraaag nwpdrpalhd grggltfael
       61 eqqarafaaw laeqgvgpgd rvailaekca vmpvlaigiw kcgavyvpld aaqpvtrlrs
      121 llgrlrprav ialddrepav ddvhwagrtr ldailagpap drptvahrpe dtayiiftsg
      181 stgepkgvei tvanlvayfg nhnevlrftp dsrvfslspf hfdvsiedtl lplslgafvy
      241 qfrgvhagav mrtvimreri thliavstll tmiteggrqv trenfpalem vmtgaevcdp
      301 gvinvwkngl pevrvinvyg pteativcva heiervdper tasypigrpl rgvvarived
      361 dgteihehdr igelwiggeq vmrgyfdqpe etarrvvevd gvryyrtgdm csydedgdiv
      421 frgrnddevk lagrrihlge irqtalscpg vervavalvp rhghdvialv vmapdravvg
      481 dvekrladll paymrptlva wspeltvsst gktdekalmr rlaeaagetg athfaftaag
      541 dvepvdgdgh a
//
LOCUS       WP_010471013             133 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010471013
VERSION     WP_010471013.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..133
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14098
     Region          1..132
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mfktilfpid qsrasqdaae kvaeivkfcn sklvilsvqs dagntpenst panqaidqll
       61 qnakiafsdw giaaeitkqv grpafcicdy adeinadliv mgcrgvglte egasesvsnr
      121 vinlapcpvm vip
//
LOCUS       WP_010471057             372 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LOG family protein [Streptomyces].
ACCESSION   WP_010471057
VERSION     WP_010471057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..372
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39017
     Region          161..368
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mahlhphhgh ddeiqtldaf drvaaggslv grrvqnldlt drtaalvsad ataavflgcr
       61 mapdaaakvr adgalvfppv pdvpfdpyrg vlytpgelft glesggyaat pdartyawfr
      121 rtardgdvfa smlravhdda isdalderla gvpvvgvmgg hamergtgay agaarlgrsl
      181 sragltvatg ggpgameaan lgayaapypd gmldealtml ggepsyapsv gdwaraafgv
      241 rarwpeggds igiptwfygh eppnafaghi akyfanatre dgllarctag vvylpgaagt
      301 vqevfdnatp nyygsrgept pmvlvdrahw tdrlpvwpll ralaegrpma arvalvdtve
      361 eataellrla gh
//
LOCUS       WP_010471064             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycerophosphodiester phosphodiesterase
            [Streptomyces].
ACCESSION   WP_010471064
VERSION     WP_010471064.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..243
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25643
     Region          15..239
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 madavtrpap agpvravtav ghrgdpyrvr entvaslrsa largadavev dvrltrdgvp
       61 vllhddtlrr lwrvdrplaa lslaevrelt gpqgvptlre alaataphrv mldlpgatea
      121 svravvgtvr ecgardrvyy csgasamllv raadpaaeia ltwttlapar pvlldavspr
      181 wlnyrfglvg ralvdrvhgd gllvsawtad trrtmrglva agvdsittnr vdalasvlag
      241 gra
//
LOCUS       WP_010471099              93 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010471099
VERSION     WP_010471099.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..93
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=9776
     Region          <2..75
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mitaivlikt svdripeiae aiaaldsvse vfsvtgtydl iamvrvpahd dladvipgri
       61 skipgvvatd thvafrtysq hdleaafaig ldt
//
LOCUS       WP_010471127             324 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carbohydrate kinase family protein [Streptomyces].
ACCESSION   WP_010471127
VERSION     WP_010471127.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..324
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35082
     Region          2..294
                     /region_name="ribokinase_group_A"
                     /note="Ribokinase-like subgroup A. Found in bacteria and
                     archaea, this subgroup is part of the ribokinase/pfkB
                     superfamily. Its oligomerization state is unknown at this
                     time; cd01942"
                     /db_xref="CDD:238917"
     Site            order(52,254,257)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238917"
     Site            order(195,223,252,255..256,259,281,284)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238917"
ORIGIN      
        1 mriavtgsia tdhlmtfpgr fadqfvadrl htvslsflvd tldvrrggvg anicfgmgql
       61 garpvlvgaa gpdfdeyraw lerhgvdtds vrisevlhta rfvcttdadh nqigsfytga
      121 msearlielk avadrvggld lvlvgaddpe amlrhteecr trgipfaadf sqqiarmdge
      181 eirtlldgaa ylfsneyekg liesktgwsd eeilgrvghr vttlgargvr ieragepave
      241 vacpreeakv dptgvgdafr agflsglswg vgleraaqvg cmlatlviet lgtqeytlrr
      301 ahfmerftea ygeeaaaevr arlg
//
LOCUS       WP_010471144             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Acaryochloris].
ACCESSION   WP_010471144
VERSION     WP_010471144.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris
  ORGANISM  Acaryochloris
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Acaryochloris"
                     /db_xref="taxon:155977"
     Protein         1..181
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=20223
     Region          1..156
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mikkilvamd hsinaiqafe vameiaesch arlmllhvls iegegyqahp vfpgtylypa
       61 fsdiplnrfq qewnkykeke lhrlailseq aksvgittei tqkfgnprqe icdfakewna
      121 dlilmgsrgh sglkelvlgs isnyvvhhal csvmvvrtpn qlavqpstns saeqlrfmis
      181 t
//
LOCUS       WP_010470672             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA desaturase [Streptomyces].
ACCESSION   WP_010470672
VERSION     WP_010470672.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Los,D.A. and Murata,N.
  TITLE     Structure and expression of fatty acid desaturases
  JOURNAL   Biochim Biophys Acta 1394 (1), 3-15 (1998)
   PUBMED   9767077
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..321
                     /product="acyl-CoA desaturase"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0006636 - unsaturated fatty acid
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=34867
     Region          29..309
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 msaadtgadr agyrasaada papvdaaarr lawitvgvpt lgtaaalafa weygftwvdg
       61 lllvtmyalt slgveggfhr ffshrsfsag pavtafwgia gsmaaqgpvv fwvaihrqhh
      121 aftdrdgdph spralgpgla arlrglwhgh vgwlftvrrq ewgkrapdlv rdrlvmrlnq
      181 yyfvwvlagl alptllgwll tggtargalg gllwggftri flldhvtwav nsvghtlgnr
      241 pyrtrdnsrn vaplaalsvg gswhnnhhar pglahnrhgl wqidptgavi ramdrlglvs
      301 daryperlrt dteehtareg s
//
LOCUS       WP_010471194             333 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010471194
VERSION     WP_010471194.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..333
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35556
     Region          3..329
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mplltvdelt vtfggrgrtp stavdgvsft vdqgqvvglv gesgcgksvt slalmgllps
       61 kgvtvggrav fdgddllrms pkklrdmrgs klamifqdpl sslnpvipig lqvteilerh
      121 rglkgeaark eaahlldrvg ipdphrrlke yphqlsggmr qraliamava caprlliade
      181 pttaldvtiq aqilellkel vdqegtallm ithdlgvvag lcdqvnvlya gkavetagrr
      241 elfahpthpy ahgllgsipr ldaprgeplt pirgsindki awadgcafap rcdfytmecl
      301 tgtpqltepr teghrvrcvn pvlpdapaee vpa
//
LOCUS       WP_010471218             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010471218
VERSION     WP_010471218.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21882
     Region          5..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdtrstrrqa trtklyeaav tliaeqgfsa ttvdeiaera gvakgtvyyn fksktelfee
       61 llrhgvgllt aslraacdet aarggtrvea ldamiraglv fidrnpavtq lyvaelwrtn
      121 rawqatlrgv rqeavavvet vlrdavasge ldedvdvplt aaalvgmvlv aaldwqafqr
      181 erslddvhga lsrllrghag gr
//
LOCUS       WP_010471223             161 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010471223
VERSION     WP_010471223.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..161
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=17574
     Region          24..142
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 messslihsq nivtpsgeht qrnrrplvlv ieddqdnlll lyhlvtslgc dvllaregqa
       61 glamvkdtlp dlilldivmp hlsgfdilrr lkqlpqarsv avvavtglat seekqkllea
      121 gccdyvckpy lidvleslic kyasiqsppq ftkptrlpas a
//
LOCUS       WP_010471284             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: siderophore-interacting protein [Streptomyces].
ACCESSION   WP_010471284
VERSION     WP_010471284.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..279
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=30826
     Region          2..259
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 madepsrrtp kvheaqvvrt eriaphlvrv vlggrgldsf atggltdhyv kilfppegvt
       61 ypepfdleri rqelprdrwp aqrtytvraw dpvereltid fvvhgdegla gpwaararag
      121 etvrflgpgg gyapdpeadw hllagdesal paiaaaleal pddavahali evdgpddelk
      181 iaapagarvr wlprrgrpvg ealveavrel dfpegtvhaf vhgeagavre lrrhlrgdrg
      241 iplerlsisg ywrlgksdea wravkrewna qvereeqss
//
LOCUS       WP_010471287             248 aa            linear   BCT 01-JAN-2025
DEFINITION  creatininase family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010471287
VERSION     WP_010471287.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..248
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=27026
     Region          12..238
                     /region_name="Creatininase"
                     /note="Creatinine amidohydrolase; pfam02633"
                     /db_xref="CDD:426892"
ORIGIN      
        1 mqlhlctwle vetylqrsqg iimpigsteq hgptgligtd aicaeviakg vgeatealvg
       61 ptinvgmalh htefpgsmsl rpstlllvir dylvslarag frqfffingh ggnvatlkaa
      121 fsetyatiad lnlpeadqtr crlnnwymns qvyqlakely gnregshatp sevavtqfvy
      181 peaikdapls aevasghpiy gatnfrqhyp dgrmgsdpsl atpehgqrly eaavesiakd
      241 yhkfldtq
//
LOCUS       WP_010471356             202 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010471356
VERSION     WP_010471356.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..202
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22100
     Region          18..187
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mhfdafvtyp dwalhvrilg gfisvlwvle iadtlilkgw lnrfgilprr wiglrgivla
       61 pllhgnlrhl smntvplvvl gwlilvrstq vfvvvtaavw ligglgiwlf agsksnhiga
      121 sglvfgylgf llmngyveqs gvaiatatlv gllygstlws ilplqrgvsw qghlfgvltg
      181 glcayylpqi qdwlqttlpk lv
//
LOCUS       WP_010471370             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010471370
VERSION     WP_010471370.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..219
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23418
     Region          14..215
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 myqrhvtmig kslwsqlrdl aprrvrpars vllrqgdpgt hvilldsgst lvtltggnge
       61 rtllavrgag ellgelavld aqprtasvia aetccvhiip asdflafvde hallapllrh
      121 aiarvreaea vrlematspv avrlasalgr llqaasgegc dyvvrltqie lsqmigasrn
      181 avgtalkpwr eqgwlvneag ggliirdmls irshadaqr
//
LOCUS       WP_010471417             124 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Streptomyces].
ACCESSION   WP_010471417
VERSION     WP_010471417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..124
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12551
     Region          5..120
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mtlklsvdag aptapyeqlr aqiseqarsg rlpvghrlpt vrglaeelgl aantvakayr
       61 aleadgvvet rgragtfvaa agdaagrraa aaaaayarea hrlgltaaea rsavaealra
      121 ayge
//
LOCUS       WP_010471481             506 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces somaliensis].
ACCESSION   WP_010471481
VERSION     WP_010471481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..506
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=54334
     Region          15..409
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mrvlvvgggy vglytalhlq kklragmrsg evevvvvapd pymtyqpflp eaaagnispr
       61 hvvvplrrvl ghcrivigev tsldhagrta tvttlateee gtgpleltyd elvlapgsvs
      121 rtlpipglae haigfktvee aiglrnhvie qmdiasstrd pavrdaaltf vfvgggyagv
      181 ealaeledma rytaryyhni rpedlkwvlv easdrilpev geemgrytvr elrarnidvr
      241 letrlescad riavlsdgsr lptrtvvwta gvrpapvlaa tglpldargr lvctphltve
      301 gvdhawaagd aaavpdvtap epgrqcapna qhavrqarvl adnlvaslyg rplrryahry
      361 agsvaslglh kgvahvygrk lkgypawfmh rtyhlsrvpt fnrkarvmae wtlaglfkre
      421 ivslgslehp raeferaagp ppppsdtavt adsspgahdt eepcgteepr gteeprggpg
      481 tgntdgrkgp hdtdgngpgr tgpatg
//
LOCUS       WP_010471563             561 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010471563
VERSION     WP_010471563.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 561)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 561)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418077
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..561
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61982
     Region          <66..>170
                     /region_name="An_peroxidase_like"
                     /note="Animal heme peroxidases and related proteins;
                     cl14561"
                     /db_xref="CDD:353811"
     Region          120..528
                     /region_name="HerA"
                     /note="Archaeal DNA helicase HerA or a related bacterial
                     ATPase, contains HAS-barrel and ATPase domains
                     [Replication, recombination and repair]; COG0433"
                     /db_xref="CDD:440202"
ORIGIN      
        1 mvreqhkqat nvigtvkgpg esgnqyvfit adtqhikige fvsyrlthid nipveilgki
       61 sactlvdhlp drifadteid psaiasligf kysspeiyev avdvigyfhp nlgfmnprqp
      121 pepgakvyra ddqtlrriln krqvgdvgsa tigslllrdl davpisldvk alvsthmail
      181 agtgsgksyt agvlieellr pynraavlif dphgeygtle amrghpafss edgyapqvqi
      241 ltpeqitiri sslnyadikm llpemserqq ailnkafnnl qarkrknarw dindliyevn
      301 eadvvqdkng neqpgssaqa lewkleklan spyfhafehl tpqdlfepgq vtvlqmneis
      361 qeeqqvicaa ilrqanqarm ntlkekitae denylpypvf illeeahrfa pahepsrcka
      421 virtilsegr kfglgvglit qrpgkldsdv lsqcmsqfim rivnpvdqds lkygveaagr
      481 dllkelpalt kgqviisgmc vntpvlcqvr lrltahgget ldapslwqah fqshrlrera
      541 aasaplagrr qaatvrgvsi d
//
LOCUS       WP_010471500             561 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease J [Streptomyces].
ACCESSION   WP_010471500
VERSION     WP_010471500.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..561
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=60848
     Region          14..561
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mshphpelga ppklapgslr vtplgglgei grnmtvfeyd grllivdcgv lfpeeeqpgi
       61 dlilpdfttl kdrlgdieai vlthghedhi gavpyllrlk pdipligskl tlalieaklq
      121 ehrirpytle vaegqrealg afdcefiavn hsipdalava irtpaglvvh tgdfkmdqlp
      181 ldnrltdlha farlseegid lllsdstnae vpgftaherd istvmrsvfa gaqrriivas
      241 fashvhriqq vldaayeygr rvafvgrsmv rnmgiardlg ylrvppglvv dvktlddlpd
      301 hevvlvctgs qgepmaalsr manrdhqiri vqgdtvilas slipgnenav yrvingltrw
      361 ganvvhkgna kvhvsghasa gellyfynic kpknlmpvhg ewrhlranae lgaltgvpkd
      421 riviaedgvv vdlvdgkaki vgkvqagyvy vdglsvgdvt egalkdrril geegivsvfv
      481 vvdsttgkiv ggpyiqargs giedgafdav lpkvedalnk saqdgvveph qlqqlirrti
      541 gkwvsdtyrr rpmilpvvve v
//
LOCUS       WP_010471583             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thioesterase II family protein [Streptomyces].
ACCESSION   WP_010471583
VERSION     WP_010471583.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..256
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=26918
     Region          3..235
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtpdpvpllc lpyagagasl fhawqpqvpp girlaplqlp greertdeep frdaasavra
       61 llpeavaaaa ghrrvavlgh smgavlafel vraleertei pvahlyvsgs pgpchgraes
      121 tadlddeafl aaverlagyr haafdvpelr elllpllrad valhetyrpl adapveaplt
      181 clrgdldslv taedaaqwsr attgpftyre psgghmylld spgellrlva adlhpgapaa
      241 agvlpagdgp agrevp
//
LOCUS       WP_010471633             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Streptomyces].
ACCESSION   WP_010471633
VERSION     WP_010471633.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..255
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27873
     Region          6..254
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mtanamvkae gvhksygaah ilkgidleva pgevfcligp sgsgkstflr cinhleqina
       61 grlyvdgelv gyrqkgdkly elkddevalk rrdigmvfqr fnlfphmtal envmeapiqv
      121 rreskavare ravklldrvg lgdraghyps qlsggqqqrv aiaralamep klmlfdepts
      181 aldpelvgdv ldvmrdlaes gmtmvvvthe mgfarevgds lvfmdggvvv esgnprdvlt
      241 npqhdrtkaf lskvl
//
LOCUS       WP_010471615            1065 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type I restriction endonuclease subunit R
            [Streptomyces].
ACCESSION   WP_010471615
VERSION     WP_010471615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1065)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1065)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1065)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1065)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..1065
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=117648
     Region          2..1020
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mspihtesaf gdaivaamve rgwreasrqn yradlgldtg elfafiretq pdewgelltv
       61 yggdpneaqr gfaarldqai ttnglldvlr ngvkdrgvll rvayfkpnlv ahdsvldgyr
      121 anrltvvrel eyatkqadwg nrldlvlfln gipvataelk npltrqgveq akeqyrterd
      181 pteliftrrv vanfavdpdl vfvatqlkgk ntrflpfntg sngpgqpgga gnpaptvygt
      241 yatsylweqv wqpdnwldll qrfvhlhksk tpgggttktm ifprfhqwda vkkltahaat
      301 hgaghdylvm asagsgksnt igwlahrlsd lhtptdprel dpeavakglk pgvpvfdkvi
      361 vitdrrnlda qlretvgsfe qtaglvvkid ekhgakgeql akalsrdtgk ivtvtlhsfp
      421 alldylqrnp teiqgsrfai ivdeahssqs gdaatavrsa lrdlgldsds ddagatmvka
      481 egatleeqlk kraeqrsraa nlsyfaftat pkaktlelfg tlqdvdgkaa yrpfhtysmr
      541 qaieegfild plrnyvtynt ywklvnqnpd erevdpskan pllaryalth dstvaqhaqv
      601 ivehfathsr grlggrakam vvtasrqsav qmaraiksyi kdrdydtkyp dlgvlvafsg
      661 sltidgeett epkengglse salpkafayt raddkavrag gpgqreykil vvaekyqtgf
      721 dqpllttmyv nktltgisav qtlsrlnrta erktqadlav ldfvndaedi qesfrpyfee
      781 antlpsdpnl lytaqsrvmq aavlsgqemd efaaayfaak ekaagsqskw eklhaelyrl
      841 lspavarfta llesededdq etaegfradl ndyvrkygfl aqivpyqdae lerlhlygry
      901 llnrlprrad ggvdigevdl shlrvektge ydvslapegp atmqgfgdgs ggakeaeksl
      961 lseliekfne rfgtdfteqd virpfeeata dpkvkaaalv ndeenfglvf dtvfadkmad
     1021 hidtiagmgr qyfgpdkgfk ssldrsarka awrmlrreag lddgi
//
LOCUS       WP_010471651             203 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010471651
VERSION     WP_010471651.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22309
     Region          1..191
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 magnperrra lldaaievla hegargltfr avdararvpa gtasnyfssr ddlltqagsr
       61 ihvrmtpppa rveaamrpep drelvaglmk wlvrrmaeer tgylamlelr leatrrpalr
      121 aeleravrae ldrntrfhld aglpgdagtv lalhlamtgl llehltlpgv lppaeldrtv
      181 ealvervvpe agprrdadrg rdr
//
LOCUS       WP_010471658             283 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010471658
VERSION     WP_010471658.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18100327
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..283
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31702
     Region          19..282
                     /region_name="PLN02244"
                     /note="tocopherol O-methyltransferase"
                     /db_xref="CDD:215135"
     Region          61..188
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mahsaltlpy fdlilkqldq gdaifeqafg rhvhwgywan pdqatytakd ygaaaeqmsv
       61 eiysaaqvqd hqtildvgcg vggtlaslne rftnvnllgl nlderqlaya rqmvtarpen
      121 tiefhqgnac slpfadqsvd avlavecifh fqdrkqflqe alrvlkpggw laisdfapfe
      181 megwpaffwq snsvfpsfyg afditytlqk yrvlseqvgf gamqsrdvtq ntlptygffq
      241 rlplaieisp dllpaiaqtl llegtsrlgl lrymilswqk pll
//
LOCUS       WP_010471680             629 aa            linear   BCT 01-JAN-2025
DEFINITION  vanadium-dependent haloperoxidase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010471680
VERSION     WP_010471680.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..629
                     /product="vanadium-dependent haloperoxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140905 - haloperoxidase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69168
     Region          301..601
                     /region_name="PAP2_haloperoxidase"
                     /note="PAP2, haloperoxidase_like subfamily.
                     Haloperoxidases catalyze the oxidation of halides such as
                     bromide or chloride by hydrogen peroxide, which results in
                     subsequent halogenation of organic substrates, or
                     halide-assisted disproportionation of hydrogen...;
                     cd03398"
                     /db_xref="CDD:239492"
     Site            order(398,406,487..489,574,580,584)
                     /site_type="active"
                     /db_xref="CDD:239492"
ORIGIN      
        1 mtdrrqdsya vrveaaelar srnhpdhkan gdeeryagak yfmsftkglp hnrktglled
       61 sqdfvefrra iddgfidaft spvrhgakfa lneesgkvee icepedfrqw eaptagvvfe
      121 legpdaqavt mppappllda sgkpnpelvl emaevyelai lrdqpfnnfe kdkangdies
      181 sinrlnklsy vknqtgrprk vnlktrelda qtvfrgsspg vevgpyisqf lligntding
      241 gggkvaegki tygvlqidqr vpvakpsvdy mtemgeyvri qrgllpktnp eiyikaggtd
      301 aiapdrpgrr fistprdlat yvhydalyea ylnaciillg mktpfdpgfd hlsgvgeaan
      361 spttkrnagg falyggphil nlvtevatra lkavrfqkfn nhirlrpeal aarielvrrl
      421 gsppvsppvd ekerlsekek aavpqllkkh ianfstelkp tldalegnyf lpmafpegsp
      481 mhpaygagha tvagacvtil kaffdtsavl avsgdtvafk rqesddspiv frapdlssps
      541 dapsgnlved reikyfltle gelnklaani sigrdmagvh yftdyydslr mgeeiaigil
      601 eeqaltystd pfvlsvptfd gdvrrigrr
//
LOCUS       WP_010471682             401 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkaline phosphatase family protein [Streptomyces].
ACCESSION   WP_010471682
VERSION     WP_010471682.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..401
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42717
     Region          57..397
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 maqptttasa wpdepvplpl dtapvpeygs gsladllptl aaglgvpgfe priaeltpad
       61 rvcvflidgl gweqvrahpa eapfltslld ssrggtgrpl tagfpattat slasvgtglp
      121 pgghgltgya vrdpdtgelm nqlrwrpwtp phvwqpyptv frladaagvh taqvsspafq
      181 dtpltkvals ggtfhgrlsg edrmdlaarq lagadralvy tyysevdgag hrfgvdsddw
      241 rgelmradrl vrrlaeqlpa rsalyvtadh gmvdipfdee sridvdedwe lragvallgg
      301 egrarhvyav pgagndvlac wrevlgdrfw vagreeaiea gwfgprvder vlgrigdvva
      361 aahddvalta slaephesam tgmhgsmtaa eqlvpllevr t
//
LOCUS       WP_010471685             317 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010471685
VERSION     WP_010471685.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..317
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=35221
     Region          30..195
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mansehfqil ekgteawnqw rqdnptvspd lqaanlsgkd cceinlsgan ltqanlsrtf
       61 irwanlsqaq lvgaqltgtd lsgtnlehvn lsqanlqgat mrwvdlsfan ltqanlqgat
      121 lsgsnlchst laetdfrrae frwadlrgad lleadltwad lrgadlrtaa lestiaiaad
      181 ftqaiftgac lqnwdisiet klddieclhi ylqadqqdrh psegdftpda frklvqpkla
      241 tldlifmdgi dwlaflqafq slctkfnqde ieirdiekkh ggtysirlkv dnhsdlenie
      301 sfikqaydeq lltagkv
//
LOCUS       WP_010471690             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Streptomyces].
ACCESSION   WP_010471690
VERSION     WP_010471690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..256
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26587
     Region          74..251
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 maftrstgkh rapsrmsrrs aqaagaaala tsgvigtlas pafaadaeha sledtglnqa
       61 itryeladev edqavaqela aevaerqaea eaaaerqaei rvqaareaqe radreaerkr
      121 ldsfqlpvag syvstaygag galwssgshs gvdfhapygv svvsvgrgtv veagwggayg
      181 nnvvirmhdg tytqyahlas vsvavgqeve pgqqiglsgs tgnstgphlh feartsgeyg
      241 sdidpvsylr argvnv
//
LOCUS       WP_010471755             213 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010471755
VERSION     WP_010471755.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23858
     Region          7..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mspkivdrea krqailaaai avfaekgyha tkmadiahka emgkgtlyey frtkeelpks
       61 ifglmleafd qeiaqleqah tdpveaimag iqlcfqdlde fayvtplvfe ilgnkdldrs
      121 iglsedfkqw lesinqffia qiqagqaqgq issklsapif armlvsildg mathycmfhf
      181 qpdffsaqvn vledmvrsyi knlrtdtstk vst
//
LOCUS       WP_010471769             339 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Streptomyces somaliensis].
ACCESSION   WP_010471769
VERSION     WP_010471769.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..339
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=35631
     Region          22..288
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22,46..47,76,81,86..89,101)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,84,100..103,107,109,146,148,
                     150..151,153,169..170,173,191..194)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,84,100..103,107,148,150..151,
                     153,169..170)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(33,107,109,146,148,150,173,191..194)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(169..176,178,187..194)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 masgadlpsg rpsglvgqrv ahyridaeig rggmavvyra tdlrldrtva lkllapelar
       61 ndtfrrrfty esrvaaaidh pnivpvfeag etggllyiam ryvpgqdlra lldrtgplpv
      121 aaavriavqi asaldaahah dlvhrdvkpg nvlvaegtds erpehvyltd fgltkkslsl
      181 tgftsvgqfv gtldyvapeq isgrpvdgrc dvyslgcvvy emltgappfr rdddmallwa
      241 hqydpppppg dvrpglppgl dgalakalak apehrfgsct afaaelrraa agagtgtgag
      301 erdagrgagp pppppgpppp ppapprwalp afrggpppr
//
LOCUS       WP_010471788             113 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010471788
VERSION     WP_010471788.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..113
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12357
     Region          6..104
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 mkitqmqtlp neivrhnaai skkvmlrage ipqltqfsqa rfpagqmaka hshpdmyevf
       61 fveagtgtmq iegithaltp gicitvephe vhevvntgqe dlvltyfglq adv
//
LOCUS       WP_010471802             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Streptomyces].
ACCESSION   WP_010471802
VERSION     WP_010471802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..192
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21524
     Region          1..88
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          100..176
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mslphailta llekpssgle ltrrfdrsig yfwsathqqi yrelgkleqa gliralpapa
       61 tpargqrkey evlpagrael adwtrraedp kpvrsalllr lraaavvgae gmadevrrhl
      121 glhraqldey ldmerrqfpp erdteadrlr hlvlrggiel erfwvawlte aleglegpkv
      181 rqdpgapgnr ga
//
LOCUS       WP_010471815             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Streptomyces].
ACCESSION   WP_010471815
VERSION     WP_010471815.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..143
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15533
     Region          5..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mlmvgkilrf devrgygfiv preggedvfm handlvddky lyqagrevef ylemgdkgpk
       61 aseirlvdrp aarraaapap asggpedqgd ldddgldvlt aaefrtelte alveadgtlt
      121 aaqlkrvras llelardhgw veg
//
LOCUS       WP_010471856             414 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleotide sugar dehydrogenase [Streptomyces].
ACCESSION   WP_010471856
VERSION     WP_010471856.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..414
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=44283
     Region          4..405
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mpadlavigl ghlglplaqa atavgfdtvg ydadprpvae laagrppvdg sltpseirrm
       61 lsagfrptth paelgrvrta vicapttpgd dsrtldltav tdaaralaar lrphttvlle
      121 spvppgtted vlrpileegs glcagrdfhl ayspsrldpg drarghahtp kviggltpac
      181 tesaaafygr ltdkvvrarg treaetvkll etnfrhvnia lvnemavlch elgvdlwdvi
      241 rcaetkpfgf qafrpgpgvg ghgvpldtvg phhplrlvet asrinermpr yvirrcatll
      301 nehgksvrga rilllgvtyk pdladregsp apeiagrlmd mgaavryhdp yvpvwrvrdl
      361 pvpradslye aaadadltil lqhhrtydlq glsvkaqlll dtrgaapvga ahrl
//
LOCUS       WP_010471925             241 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010471925
VERSION     WP_010471925.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..241
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26765
     Region          36..141
                     /region_name="Methyltransf_24"
                     /note="Methyltransferase domain; pfam13578"
                     /db_xref="CDD:433324"
ORIGIN      
        1 mntpnipdyv kgwltdteaq flysqakacp pgtviveigs wkgkssicls qgsaeggnvh
       61 iyaidphqdd syqefehnvs sagvrelvtp ivktsadace gwtqpigllf idgnhehdmv
      121 eqdfllwsrf vveggiiafh dstsspfnql mgylgpkrvv dkylfqskdf khigftgttt
      181 yatksssqtv tdtlarwsmr lkkafpdtlm llhqyvllkl ptgvldgirr lmgyrnlnlg
      241 r
//
LOCUS       WP_010471929             215 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010471929
VERSION     WP_010471929.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10606006
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..215
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24606
     Region          64..197
                     /region_name="Methyltransf_23"
                     /note="Methyltransferase domain; pfam13489"
                     /db_xref="CDD:404385"
ORIGIN      
        1 mpnsdrccpl cqslqtsafh qdsrtyfrcq vcllvfvlph qflsaqaeka iydshensae
       61 dlgyrrflnr lflplsqcll pqscgldfgs gpgptlsvmf eeaghamely dlfyapdirv
      121 lqrqydfisa sevvehlhhp rrelerlwsc lkpngvlgim tkrvidqaaf arwhyksdlt
      181 hvcffsietf ewlanhwqaa ltvsgndvvl lskiy
//
LOCUS       WP_010471733             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: prohibitin family protein [Acaryochloris].
ACCESSION   WP_010471733
VERSION     WP_010471733.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris
  ORGANISM  Acaryochloris
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Yoshinaka,T., Kosako,H., Yoshizumi,T., Furukawa,R., Hirano,Y.,
            Kuge,O., Tamada,T. and Koshiba,T.
  TITLE     Structural Basis of Mitochondrial Scaffolds by Prohibitin
            Complexes: Insight into a Role of the Coiled-Coil Region
  JOURNAL   iScience 19, 1065-1078 (2019)
   PUBMED   31522117
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Acaryochloris"
                     /db_xref="taxon:155977"
     Protein         1..277
                     /product="prohibitin family protein"
                     /GO_component="GO:0005743 - mitochondrial inner membrane
                     [Evidence IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0035632 - mitochondrial prohibitin
                     complex [Evidence IEA]"
                     /calculated_mol_wt=30176
     Region          26..219
                     /region_name="SPFH_prohibitin"
                     /note="Prohibitin family; SPFH (stomatin, prohibitin,
                     flotillin, and HflK/C) superfamily; cd03401"
                     /db_xref="CDD:259799"
ORIGIN      
        1 mkdwnpanlg iiiallvllg lssvviinpg qagvlsilgk ardgallegi hvkapfisrv
       61 dvydltvqkf evpaqsstkd lqdltarfai nfrldatevv evrrkqgslq nivskiiapq
      121 tqesfkiaas rrtveeaitq revlksdfdd alskrlekyg iivldtsvvd ldfspefaqa
      181 veekqiaeqr aqravyvare aeqealaevn rakgkaeaqr llaetlkdqg gklvlekeai
      241 eawrqggsqm prvlisgsgk dggqmpflln lngdskg
//
LOCUS       WP_010471969             443 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010471969
VERSION     WP_010471969.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..443
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=48611
     Region          1..>330
                     /region_name="K-ycf53"
                     /note="Signaling protein combining a Ser/Thr protein
                     kinase domain and the GUN4/Ycf53 porphyrin-binding domain
                     [Signal transduction mechanisms]; COG5752"
                     /db_xref="CDD:444462"
ORIGIN      
        1 mslcinpsca dpqssddhlf cascgselll egryrvislr gqggfgktye vsdlesspki
       61 lkiltdnypk hvelfqrean llsqlnhpgi pkvepnsyft fyprnwkepl hclvmekivg
      121 ldlqdylrqr ghpideklav qwlkqvlkil qvvhqqqvlh rdikpsniml kangniclvd
      181 fgtarsvtnv tntqqggtrv vssfytpreq ihgqavpqsd ffalgrtfvy lvtgkelsqf
      241 ydgstdkfew rstainispr fanlldwlma pvasqrpana evvlqqlvvl essgqsipas
      301 vlnstmgmep tqavnsvqpn ssgssipasg qstsqpagpa sfaqptsqpi eppptpsstg
      361 pvssapesat vpivpssqpv irpefgqkcq nilaefigpi saivyqrtlt qypgvteqel
      421 vkllsqqipv aeqatefrqr lrs
//
LOCUS       WP_010471946             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Streptomyces].
ACCESSION   WP_010471946
VERSION     WP_010471946.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..283
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29632
     Region          6..278
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlnriktlaa ltgttalavg ltacgtasdp aasgsgddas kplvvaaspt phadilayvk
       61 dnlaekaglt levkeftdyv lpntatqdgq vdanyfqhkp ylddfnkknk ttivpvvdvh
      121 leplglysqk ltslkdlkag qtvavpndtt negralklla dnglitlkag vgadaglsdv
      181 adskglefke leaatipral sdvdaaving nyaieaeltp aedalvlekp egnpyanfla
      241 vkdgneddpr vrklaellas pevrtyient ykgsvipasg ttk
//
LOCUS       WP_010472019             341 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010472019
VERSION     WP_010472019.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..341
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=37230
     Region          20..316
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 maplsktnvv vigggpggta taircaqhgl qvtliegaee srphtsetlh peiepllkkl
       61 gvrdqvlaan fprcpgrwia lqgerqfygf genkhgpklg fqvkrsqfdt llleqakamg
      121 vkvlqpcrai eplvsrgqvq glittaggie atyvvdatgs hqwlarklkl nttpyspslq
      181 veygyrighc pkqdysplia papggwvsva kvqplryqwt rlkwfqpsdt pwsppnlael
      241 lpsdtthvmd mtwrlinpaa gpgyflvgda aaildpissq gvlkaiasgm maahlinqqf
      301 qqaklplsia dryatwsrtn fhqdlmalqr lytpilskvt a
//
LOCUS       WP_010472027             442 aa            linear   BCT 01-JAN-2025
DEFINITION  AAA-like domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010472027
VERSION     WP_010472027.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 442)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10628838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..442
                     /product="AAA-like domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=50260
     Region          111..438
                     /region_name="AAA_35"
                     /note="AAA-like domain; pfam14516"
                     /db_xref="CDD:373105"
ORIGIN      
        1 mendadfswp vardfanqli fmatakhlsd levqvllgsw hhqtyeqmae qlhygaayln
       61 rdignplwkr lgqalnekvs ktnfkealrr aweqqvhapp vvtsspapii egpispespf
      121 yleragveql gcqtllkpga llrikapqlm gktsllyhlm afaqqqtypt vyidmgsidk
      181 svlaslekll kwlcamtsrq lhlpnrlsel wdseifgsnd nctayfedhi fpevqgpfvl
      241 gldnvdrlfp fqdiiedffg mlrswhekgr isqqwqqlrl ilvhsteayi pldyhqspfn
      301 tgvpiglsef tahqiqhlaq lhqvaltese lsklmamigg hpylvrvals alstreltfn
      361 qlvqtavsde giysahllhh wvtlqqtpdl mqafqgvlma taslnpvqay klhsmglikr
      421 ennqviprnd lyesyfqriy sh
//
LOCUS       WP_010472108             188 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Streptomyces].
ACCESSION   WP_010472108
VERSION     WP_010472108.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..188
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20249
     Region          21..165
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mstagtrass gigaltfrpl dpaadaalvh rwvthpkasy wlmqdhtpee vereyaaiaa
       61 hphhdaflgl hdgepaflme rydpaevelv glydplpgdv gmhflvaptd apvhgftrav
      121 itavmaelfr dpavrrvvve pdvrntavha lneavgfvpv dkitkpekea llsvctreaf
      181 eaaagaar
//
LOCUS       WP_010472135             475 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: N,N-dimethylformamidase beta subunit family
            domain-containing protein [Streptomyces].
ACCESSION   WP_010472135
VERSION     WP_010472135.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20801894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..475
                     /product="N,N-dimethylformamidase beta subunit family
                     domain-containing protein"
                     /calculated_mol_wt=52471
     Region          69..452
                     /region_name="DUF6605"
                     /note="Domain of unknown function (DUF6605); pfam20254"
                     /db_xref="CDD:466405"
ORIGIN      
        1 mrrtprtgdn pvvrenglsg srewemraag irpandrdgq iqgyasatsv gpgesvdfhv
       61 svrgsdhftv avhrlghygg agarrlvtsp rlrgtarpip aekpgsrlld cawpvswtle
      121 iprtwvsgmf lavftsedgh rsytpfvvrd larpadilmv apfttyqayn mwprdgrtgr
      181 nlyrgykseg ktggsperay evsfdrpyan tglptlyemd tgftrwaeqs gydityasgv
      241 dlhegridpa rysaivfpgh deywskemrd haeaalaagt hiaflgannl yfntrleasr
      301 rgrdcrvvac ykeepdpnpg eggptirwrk ldddhrraeq aflgvqyngm lkdpvplvvs
      361 aadhwlwkgt glkegdgipd lvsieadghd edmpapddae qvllshspyq dsmgrglrhq
      421 ntslcthahg tllfaagtfg wplalydpeh adervrkata nlfarmlgpr gssav
//
LOCUS       WP_010472180             152 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peroxiredoxin [Streptomyces].
ACCESSION   WP_010472180
VERSION     WP_010472180.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..152
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16974
     Region          3..151
                     /region_name="PRX_AhpE_like"
                     /note="Peroxiredoxin (PRX) family, AhpE-like subfamily;
                     composed of proteins similar to Mycobacterium tuberculosis
                     AhpE. AhpE is described as a 1-cys PRX because of the
                     absence of a resolving cysteine. The structure and
                     sequence of AhpE, however, show greater...; cd03018"
                     /db_xref="CDD:239316"
     Site            order(25..26,28)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239316"
     Site            order(43,46,117)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239316"
ORIGIN      
        1 maievgtkap dfelkdnhgr tvrlgdfrge knvvllfypf aftgvctgel calrdqlprf
       61 vnedtqllav sndsihtlrv faeqegleyp llsdfwphge vsraygvlde ekgcavrgtf
      121 iidkegvvrw tvvndlpdar dldeyvrald al
//
LOCUS       WP_010472225             278 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010472225
VERSION     WP_010472225.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12010215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..278
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=29861
     Region          36..74
                     /region_name="Pentapeptide"
                     /note="Pentapeptide repeats (8 copies); pfam00805"
                     /db_xref="CDD:459943"
     Region          56..252
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mskyksamag ehlallyrgp eiwnqwrqdn shnspnlagc nlgqmdlqaf dlshtdlsda
       61 nlrkanlagv nlsnsllcga nltdaqltgi kgvainlhha qaqgadlrda nliggdlgea
      121 vlldaelsra nlvgcslkha dirraeleaa qlhradlsfa eleaanliqa dlsqanlsya
      181 tltgaylyga dlsranlraa hcsqayfvra nftninaeav dlawsnlskv nfsganlrra
      241 nlrgarlhra qfhqtcldga vwdlasleqa rgfpslsc
//
LOCUS       WP_010472241             442 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010472241
VERSION     WP_010472241.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..442
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49068
     Region          11..206
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          58..84
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(59..60,63..65,67..68,72,75,84,86,89,93..94,97..99,
                     101..102,106,109,118,120,124..125,128..130,132..133,137,
                     140)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          86..118
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          120..148
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <248..>440
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          276..306
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(312,316..317,320..322,327..328,332,335,344,347,
                     351..352,377..379,381..382,386,389,398,400,402,406..407,
                     410..412,414..415,419,422,431)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          312..344
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          346..398
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          400..431
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mskteaswqt lalninfnld gqigeqlyha ihddqahhfh slltknkidv atygpsflma
       61 sisagslhti qlllhlelsi nwkddlqdey pltqacrlgr ldivkfliqa ganinlsgyd
      121 splwaaiqsn nlhiaellik sgadinleid dfynllgiaa dkgylegvkl ltesaihqsl
      181 npellnmela lrhaamsgea eifdylvnlc thhiesfehs aiddlqdtlr igisrksrre
      241 dpcisdclka veenditrlq eliasgidin lytekgytll htaidkgsig ivhvlidagi
      301 dyelrdeycf qetpllmasr gnfpnhpaiv eallnagadv kathkgmtpl miaintyfrq
      361 iidvprglvf psweerrsna ikvirlllqf gsevnyqdpq grtplmlaap tddsvlmqll
      421 ifagadpnqq daagktyvdy vp
//
LOCUS       WP_010472279             418 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: serine/threonine-protein kinase [Streptomyces].
ACCESSION   WP_010472279
VERSION     WP_010472279.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..418
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=43990
     Region          17..258
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(23..24,26..29,31,43,45,77,93..96,100,102,139,141,
                     143..144,146,155..156,159,176..179)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(23..24,26..29,31,43,45,77,93..96,100,141,143..144,
                     146,155..156)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(27,100,102,139,141,143,159,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(40..41,69,74,79..82,94)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(155..163,172..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mammrlrred prvvgsfrlh rrlgaggmgv vylgsdrrgq rvalkvirpd laedqefrsr
       61 farevsaarr irggctarlv aadleaerpw fatqyvpgps lhdkvaeggp lpaadvaaig
      121 aalseglvav heagvvhrdl kpsnillspk gpriidfgia watgastlth vgtavgspgf
      181 lapeqvrgaa vtpatdvfal gatlayaatg dspfghgsse vmlyrvvhee phldgvpdal
      241 aplvraclak epeerpstlq lslrlkeiaa reaqglgmaa vpaeartals rsgraerper
      301 adrgtgggra ahpvpgater ytertmrgra qrtpaprgrg pqptppgtgg srarqhpsqp
      361 gtrpgprtgp rrtgtgpgts pgrlrpanpr llrqrlfvfv vvtlvvllgi agaqalqg
//
LOCUS       WP_010472311             278 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010472311
VERSION     WP_010472311.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..278
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31212
     Region          5..115
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          148..271
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mdfqirpaqq tdlprirawa vqeswnpgry dlevywrqns llvgwlgdqp vgcisaaayd
       61 adfgflgcyl vdhrhrghgy grflwekais slparcigle gavalqdtyl rhgfvksclh
      121 vrhqlksgng npvasslqai hsipfeqvld ydtrhfvgmr sqflqhwlgs pemqgwgvvq
      181 adhllgygli rpadmgyrig plfadradva qqllaallqi ppsdqpvymd vpksneqanq
      241 lmknvqaipl fsncrmykge fpelpldeiy gvttlemg
//
LOCUS       WP_010472343             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HAD family hydrolase [Streptomyces].
ACCESSION   WP_010472343
VERSION     WP_010472343.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..239
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26259
     Region          3..226
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mairavlwdi ddtifdyaaa dragmrrhlr eeglsggfdg vedalrcwre atvlhwarfa
       61 agettweeqr rdrvrtflga pladgeadaw ferylahyea awelfpdtvp vldllatgyr
      121 havlsnssll nqdrklrllg vrdrfeavlc aadigvskpe aaafhiacdt lglapdevay
      181 vgdqpdidar gaaeagllgi wldraglggr peltritdlh qlpgllrgdt rfgapdtfg
//
LOCUS       WP_010472409             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pentapeptide repeat-containing protein
            [Acaryochloris].
ACCESSION   WP_010472409
VERSION     WP_010472409.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris
  ORGANISM  Acaryochloris
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Acaryochloris"
                     /db_xref="taxon:155977"
     Protein         1..218
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=23723
     Region          26..200
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 manaehldli kqgievwnnw rgqnllvrpd leganlsgci leaanlgqan ltyanlegad
       61 lrqanlqras lqganlrmad lihanlesan lecanlegad lyktnlsqsk chkanlskai
      121 irraslvgan lkatensltd yfqanmmrvn fymananqan leganliean lglanflean
      181 lrkanlcran lyranlcran pyeallkgtt mpdgtihd
//
LOCUS       WP_010472417             413 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Streptomyces].
ACCESSION   WP_010472417
VERSION     WP_010472417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..413
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42529
     Region          8..405
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mraddralvi vgaslaglra aevlraegfa galtivgdep hlpydrppls kqvlasadrp
       61 aapelplpka lgarwhlgra aagldperrt vvladgtllp ydgllvatgs aarswpadrp
      121 appagvltlr twddtlalrd rlvpgqrlvv vgagflggei adsarargld vtlvevsaqp
      181 leraigttag afiaalhrea gidlrtnttv tdfqagadgr ltgvrlsdgs llpadvavla
      241 lgavpatgwl agsglalegg vhcddrlral rpdgsvvpgv faagdvarvp qplaggapla
      301 lghwtnaveq gtaaahalls pdapepftgi psfwsdlhgv rirsvglpaa adearvvehd
      361 pvarrlevay hragqlvgam tigrtsrlaa yraelqerma cqeaapdslt aav
//
LOCUS       WP_010472503             142 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PH domain-containing protein [Streptomyces].
ACCESSION   WP_010472503
VERSION     WP_010472503.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..142
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=15867
     Region          61..>114
                     /region_name="bPH_6"
                     /note="Bacterial PH domain; pfam10756"
                     /db_xref="CDD:431475"
ORIGIN      
        1 mtksrttfrn gvypfaglfv iavvglayld mtagarsggd ltfytllcag avalasrsfi
       61 wtavvaderg vqvrnplrtq rfawreirgf raedrlviel adsrevrcwa vqraniarml
      121 krrshadava edltnlrery la
//
LOCUS       WP_010472528             333 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010472528
VERSION     WP_010472528.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..333
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34723
     Region          6..139
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          190..321
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 madgaitfdr ldrrivgalq vdgraeasrv agalgvsart varrlarmrd agavsvvrla
       61 ppeevvgata lrvrvvrgra eavaeafaar pdvlsvdlvt ggeeisvlll gddadqgrll
      121 yrqvpataai tsvsahsvlr vfadarqwra dvltpeetaa llpsgaeeae gggggaefvr
      181 steaedgvpd avdrrllavl drnarlgfae lghlagvpet tvrrrmrrla aggqvrtlvr
      241 vrpgllgltv danlwmrvpp arlheageal aahplthava attgacnlva avycrdlral
      301 ydfttgvlgp lgvesvettv iaravkpvga grg
//
LOCUS       WP_010472543              85 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein, partial
            [Streptomyces somaliensis].
ACCESSION   WP_010472543
VERSION     WP_010472543.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Leiros,H.K., Tedesco,C. and McSweeney,S.M.
  TITLE     High-resolution structure of the antibiotic resistance protein NimA
            from Deinococcus radiodurans
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 64 (Pt 6), 442-447
            (2008)
   PUBMED   18540048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         <1..85
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          <4..75
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 pgraagreva fevdhideaf srgwsvllvg parvvtdpge aralaeraft tpwagaerdl
       61 wvvvaparvt grrirvhrlr pesga
//
LOCUS       WP_010472607             501 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptide MFS transporter [Streptomyces].
ACCESSION   WP_010472607
VERSION     WP_010472607.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..501
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53340
     Region          11..501
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mapsltkdpa nepaagktff ghprgmatlf mtelwerfsw ygmrailvly lvhgvldgpl
       61 qdrealaasi ygvynavvym aampggwiad rlwgarkavl vggviialgh ytlavpgdva
      121 fflglgliav gtgllkpnis amvgglyegq pgarrdagft lfymainigg miaplvvgyl
      181 genvdwhlgf avagvgmtla viqyvlggky lgdvgsepat patpeercsv lrkaglwtav
      241 avaalladil lgtfdiehiv nvlaiagivv pilyflaifr npalrsedrp kikafvwffa
      301 tavlfwviyd qsgslltffa dnktdrvigg wefpaswyqs vnpaliivla plfaalwvrl
      361 aqrnrepgtp mkfalamlli ggsfaimgla gaaaassdtg kvtvfwllsv ylvqtigemc
      421 lspvglslst klapkvfvgq imglwflata tgnalngwvt qlnavlgdaa yytmwaviaa
      481 aagvtfmias krigklmgdv k
//
LOCUS       WP_010472780             302 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010472780
VERSION     WP_010472780.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33536
     Region          1..>161
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          91..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdisvlklfv dvvrqgsfag aardrnidps svsraiagle keldlrllqr ttrqlsltea
       61 gktyferiep lieelqqase iaadvvgqpk gqlrvtvsas fglkcivpfl pqfeqlypdl
      121 tvnllfsdav edlllnridv airlgllrds tliaqqlmqt ryrvcaspdy lkqsppiatp
      181 ediadhnclr fplagfqsqw lfkdaqgtlt evpihgntvi sngialqqca ianmglallp
      241 nwlinedlrt gtlvdvlpay evtgtdfsta awfvypsrcy vplklkvfie ffkqnvprlv
      301 mp
//
LOCUS       WP_010472830             144 aa            linear   BCT 01-JAN-2025
DEFINITION  HIT family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010472830
VERSION     WP_010472830.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..144
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15770
     Region          3..143
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 midtcpfcai aqgdapvstv yedeavmafi plhpvypgac lvipkahidh ftdipdplaa
       61 kvivvaqqvg rkimtvykpl rigmlvhgft vahahlhlip qygpldimhk hyaycedgnv
      121 kfgdkdiptp srqeldqmas tlkl
//
LOCUS       WP_010472835             421 aa            linear   BCT 01-JAN-2025
DEFINITION  S-layer homology domain-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010472835
VERSION     WP_010472835.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Gerbino,E., Carasi,P., Mobili,P., Serradell,M.A. and
            Gomez-Zavaglia,A.
  TITLE     Role of S-layer proteins in bacteria
  JOURNAL   World J Microbiol Biotechnol 31 (12), 1877-1887 (2015)
   PUBMED   26410425
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Mesnage,S., Fontaine,T., Mignot,T., Delepierre,M., Mock,M. and
            Fouet,A.
  TITLE     Bacterial SLH domain proteins are non-covalently anchored to the
            cell surface via a conserved mechanism involving wall
            polysaccharide pyruvylation
  JOURNAL   EMBO J 19 (17), 4473-4484 (2000)
   PUBMED   10970841
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Engelhardt,H. and Peters,J.
  TITLE     Structural research on surface layers: a focus on stability,
            surface layer homology domains, and surface layer-cell wall
            interactions
  JOURNAL   J Struct Biol 124 (2-3), 276-302 (1998)
   PUBMED   10049812
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Lupas,A.
  TITLE     A circular permutation event in the evolution of the SLH domain?
  JOURNAL   Mol Microbiol 20 (4), 897-898 (1996)
   PUBMED   8793886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..421
                     /product="S-layer homology domain-containing protein"
                     /GO_component="GO:0030115 - S-layer [Evidence IEA]"
                     /calculated_mol_wt=44465
     Region          37..78
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
     Region          97..138
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
     Region          161..203
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
ORIGIN      
        1 mlrvsprfsr ialawgvsls tiapifsalp asaqanfsdv slgywarpfi eklaeenvik
       61 gfpdgtfkpd qpvtraqfaa ivrqafdres trqyrgfadv ptnhwaqpai dkaystrfms
      121 gypgnlfqpn qripkvqalv slasglelep daptdevlat frdaadipgy adkgvtaate
      181 aglvvnypna nflnpnqqat raeiaafvyq alvdqgdldp ipdkaranny ivkldgtasp
      241 ekpstpintg niiasgskip vrypgpnkvn livapgetvd tklevaediv naagtvlipk
      301 gsliegtlvp vnvgttpgtq fvaktlkvga rnydiransd pqvavsrqsv kpndirgais
      361 ttagrtilns vlgsgfnlgs lltgallsgv vtspsapkds vivvdpaale ltiqssldlt
      421 t
//
LOCUS       WP_010472846             231 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF433 domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010472846
VERSION     WP_010472846.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Sala,A., Bordes,P. and Genevaux,P.
  TITLE     Multiple toxin-antitoxin systems in Mycobacterium tuberculosis
  JOURNAL   Toxins (Basel) 6 (3), 1002-1020 (2014)
   PUBMED   24662523
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..231
                     /product="DUF433 domain-containing protein"
                     /calculated_mol_wt=26174
     Region          173..224
                     /region_name="COG2442"
                     /note="Predicted antitoxin component of a toxin-antitoxin
                     system, DUF433 family [Defense mechanisms]"
                     /db_xref="CDD:441983"
ORIGIN      
        1 mrnwnadiyn iptysvvdaa rylriplvtl rswiqgrsys tkqgkkdfnp liqrpkpnlp
       61 qlsfanliea hvlrvireih gvrldtvraa ldylsnnleq ehpliqktfk tdgislfvds
      121 mdqlvdvgrs gqlamretiv hlltriewde ngiasrlfpf iqpegdesmd lyidprisfg
      181 rpviagrgvp tiaisdlyea geniddlane yecttkqita airfeslfra a
//
LOCUS       WP_010472921             389 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein, partial
            [Streptomyces somaliensis].
ACCESSION   WP_010472921
VERSION     WP_010472921.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..>389
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
     Region          6..389
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 msevlefklp dlgeglteae ivrwlvsvgd vvaidqpvve vetakamvev pcpyggvvta
       61 rfgeegeelp vgaplltvav gateapaasa apgkpgaalq adtvggcaep adegsgnvlv
      121 gygtstasar rrrvrpaapi aasaprtapa papepapvpa pavpaegpvp visplvrkla
      181 rergvdlrql rgsgpdglil radveraqdr aqdraqaaap arpapagaer vplrgvrgav
      241 adklsrsrre ipdatcwvda datelmaara amnaaggpki sllallaric taalarypel
      301 nsrvdldare ivrlpevhlg faaqtdrglv vpvvrdahtr saedltaefa rltevaragt
      361 lspadltggt ftlnnygvfg vdgstpiin
//
LOCUS       WP_010472978             403 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphoglycerate kinase [Streptomyces].
ACCESSION   WP_010472978
VERSION     WP_010472978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..403
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41770
     Region          6..403
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mqtihtller gvdgkrvfvr adlnvpldgt titddgrira vlptvralae agakvvvash
       61 lgrpkgapdp afslrpaaar laellgtpva fagdtvgsea hdtvaglgag qvavlenlrf
      121 nagetskdda eraefaarla aladvyvgdg fgavhrrhas vfdlpkllpa yaghliatev
      181 gvlrkltddv arpyavvlgg skvsdklgvi dhllekadri ligggmaytf lkarghevga
      241 sllqedqipa vreyleraek rgvefvlpvd vlvsadfpdl aakapthpat vaadaipagq
      301 kgldigpetc elyasklada atvfwngpmg vfehpdyaqg travaqalad spaftvvggg
      361 dsaaavrtlg fdenafghis tgggasleyl egktlpglaa led
//
LOCUS       WP_010473001             232 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010473001
VERSION     WP_010473001.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..232
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25794
     Region          52..229
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtqllpvkki ifltlglisi sqatgqnpap aiaqnaslip sgstqkqadl llyggprtrs
       61 plvqwyleel avsyqyisld irgqeqrqpe flainpmgkv pamvdgtfkl wesgaillyl
      121 tdkygkepqs ieerallnqw vifanatlgp glfredrrer emprllapln diveqqpfil
      181 gselsaadva vgsylyyakl glsldfsdyp avetylnrls krpafiktmg qr
//
LOCUS       WP_010473004             157 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010473004
VERSION     WP_010473004.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..157
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16867
     Region          27..152
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtstassnrw ltllfqstsd ttvwfqvalt ilrvvvsffm ihngvdklgd vegfatnvva
       61 ngmglpfpvf ltycsayaei igsillilgl lsrpaalslv ftmvmaiyfh ikvdglqigs
      121 fetatlyacs flfflvnggg qysldalisn qlggske
//
LOCUS       WP_010473063             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Streptomyces].
ACCESSION   WP_010473063
VERSION     WP_010473063.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..248
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=23565
     Region          29..231
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; cl46157"
                     /db_xref="CDD:480497"
ORIGIN      
        1 mstlilalaa gavvglalga lggggsvlav paliyllgft paaattasli ivtatsltal
       61 yvharagnvr wkagalfaaa gllpaaaaga aaarlpqpvl tgafavvaal aavrmlrpar
      121 adagraaahp akaagvgagl galtgllgvg ggflavpala tvlafemqaa vgtsllvisa
      181 nsvaslatrg atatgvdwav vapfagaail gawdgkrlaa kasgtllrrv faaallvvaa
      241 lmladall
//
LOCUS       WP_010472123             294 aa            linear   BCT 01-JAN-2025
DEFINITION  SH3 domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010472123
VERSION     WP_010472123.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..294
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=32422
     Region          99..>183
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 mkrnqrlsfv lllclfglgl siqacqqtsa dtnspstetp adrqqsgagq sgpfsqeldk
       61 igkpesssss pdegeirevt yiaekitpvp aqlvskdpns rinvrsqpst rskakhfgyk
      121 gdavtllqka kgegeaiwyy lrfnqsqaeg wirkdfislt ssklnpkqqy lpfnlktdpw
      181 issfnqsyka akqtnepwlf naptvalkll gypntdgckp tnvstiehsp skvtvivsng
      241 peqvlpcagd svlasetrvd lvkqkriwai ewvggryrch qgrgqqefap arcn
//
LOCUS       WP_010473072             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Streptomyces].
ACCESSION   WP_010473072
VERSION     WP_010473072.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..316
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33268
     Region          4..314
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mgaiealekl apvvlafgcg vllakrkvvp agsskafady aflfavpcfl fgniyrsdla
       61 alfdwravsg yavaavlaaa avgvlarvfg vrdprgvalr imaavqvnta yfavpvfiml
      121 fgdaapifpv llfqvcvlsl vvisimelgr pdrtggpgrr ltaavaaslt tpvviacnag
      181 ivlnllpvel pgvvldsfaf vgdsaspval falglhlggt gvrirgttae eirliafkcv
      241 afplltfavc rhvldvrgdw lhhlvliaam papqnlfvfa qrydvdvdms aalvvkssvv
      301 allllplwmq wvahsg
//
LOCUS       WP_010473084             546 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: serine/threonine-protein kinase [Streptomyces].
ACCESSION   WP_010473084
VERSION     WP_010473084.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..546
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=58145
     Region          66..322
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(66,90..91,124,129,134..137,149)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(73..74,76..79,81,94,96,132,148..151,155,157,193,195,
                     197..198,200,210..211,214,231..234)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(73..74,76..79,81,94,96,132,148..151,155,195,
                     197..198,200,210..211)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(77,155,157,193,195,197,214,231..234)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(210..218,227..234)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mtnrggqqep tsyplrpplp aqrrgeptea agaadgppap ppgppraepa aapgpdsgag
       61 rlvggryrll erlgsggmgt vwrardevvd rdvavkeprl petlseaerh tahrrmqrea
      121 raaaridhps vvcihdvvte dgspwivmel vrgrsladll degtlppaea ariglavlga
      181 lnaaheagvl hrdvkpgnvm vgrhgrvvlt dfgiaqvege qkltetgafi gspeyiaper
      241 vlgrragpes dlwslgvtly qavegvspfr rqttpstlqa illaelppar haeelhetir
      301 gllrkepesr ltarqalgml rsaaageerp aadaertaps atgpgapgag srrrryllaa
      361 aagaavlalv aglllrsgge elpegwkryd eyrmqlsvaa pekwtitted dlessggpyt
      421 atrysapsgd rsilvdelkg vtetavatae rwkreyeegt ppeggepava dvravthqgr
      481 daalftgsyn antegaprrl qktlvvvssr qerltltval pagkgaekta edllgkarla
      541 feirdl
//
LOCUS       WP_010473098             128 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: STAS domain-containing protein [Streptomyces].
ACCESSION   WP_010473098
VERSION     WP_010473098.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..128
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13710
     Region          11..107
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(27,29..31,37,62,64..66,68..70,73..74,96,100..101,
                     103)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            65
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mttspddslr ltvtdggrel clalagdldy dtaedlthav reylaehpap dvlsvdcarl
       61 afcdstglaa llmvrrltag tgtalhlrdr palldrlleq tgtfdhlvgt gragerdtea
      121 qtrpprqp
//
LOCUS       WP_010473138             127 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Streptomyces].
ACCESSION   WP_010473138
VERSION     WP_010473138.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..127
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13755
     Region          8..116
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mvsmvqnmai dcadayglar fwsgvtgrpl hpesrpgdpe vqvplaeglv lyfnqvpeak
       61 taknrihlcl rpetsreqev erllglgatl fadhrnpdgs gwvvladpeg nefcvlrses
      121 draaaap
//
LOCUS       WP_010473158             109 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010473158
VERSION     WP_010473158.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..109
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12192
     Region          6..103
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mselnlrltp nqevilaalr lhrrygleil aaiensggkq igfnslypnl kklehkglvq
       61 sewgdespee hsrarrkyyr itdvgirald lkqellagva awipetega
//
LOCUS       WP_010473172             332 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010473172
VERSION     WP_010473172.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..332
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=35165
     Region          22..217
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     Region          156..322
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mkakallqqy annvfdfsgq tlagldlaga dliginlsaa dlrntnlsla ylnrvdlqts
       61 nltqsnlsga tltqanlsqa nltdaalhga nlqravlfka dltladltda nlmeadlrev
      121 tlrstnltga clrsanlree nrncadlrga ildgvdlqga nlrgadlskv slqganlrna
      181 nlraanlaga dlqganleqa llieanlqqa nlshatlada klervnlqma qlvnsdlsdc
      241 tlveselsqa nlqgatlyrs rlnranlsra nltaanlqea fliqaflart dltdahlqga
      301 nltrsdwssa iltrtvltga tlpdgtvcms qt
//
LOCUS       WP_010473223             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphotransferase family protein [Streptomyces].
ACCESSION   WP_010473223
VERSION     WP_010473223.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..304
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33819
     Region          70..267
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mrteaertat lerevrralg dggirvlpwr egvdyfadla rrrdggivgv vrsprhevlp
       61 tsyegtvdfa dvlakevnvl gllreagvpa psvlawrrrg gsqgvswmlc ehvdhrptde
      121 lnedqqhelg ritraihsir pgttvgrpqe swrsyvlerv adrlraaery cprlpvetll
      181 srcaagvpng pgqadvllhl dlrppnlcvr ggritavidv anaitgdpwl elarirfcgl
      241 fteafrtgyg igdadvgrre rlldlyeldi aalmvvvaae etndeellks srdrlehlca
      301 riir
//
LOCUS       WP_010473224             230 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010473224
VERSION     WP_010473224.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..230
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=25341
     Region          13..223
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mvplrdnnpt ritpfvtyvl ialnvvvflh elrlgpelda ffrlwavvpr eltasfqgep
       61 ttlphpawit lftsqflhgg ilhiagnmlf lwvfgnnied klghvkylvf ylscgalaal
      121 sqwffsvnse ipslgasgai agvmgayiir fpkaevltli plgffwwtvn lpavfflgfw
      181 faqqafnsva slnapmnmgg vaywahaggf vfgallgplm glfdddqsrr
//
LOCUS       WP_010473243             403 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010473243
VERSION     WP_010473243.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181070
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..403
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47243
     Region          54..392
                     /region_name="CE4_Ecf1_like_5s"
                     /note="Putative catalytic NodB homology domain of a
                     hypothetical protein Ecf1 from Escherichia coli and
                     similar proteins; cd10969"
                     /db_xref="CDD:213026"
     Site            order(97..98,180,184,329..331)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213026"
ORIGIN      
        1 mnirstslkl kniyrknipe vkayfqgsyp sfifdstsev ideipvftfh avapevfeqr
       61 lkylkenhyq tlkaaeflei ilankpiprr svlltfddgw gslwtfaypl lkkygmyatc
      121 flipgliqss srnyhnledv wsgqvdhdll iqrerssepy ctweeisimy qsgvfdfqsh
      181 tlyhsqvhts skiidflnps fdyaignhnv pivksngher wdrqlefgtp iyeysprmgg
      241 kkryvddenl rlhcttfvrn sggkdfflqk nwrkslykvv kdfknqhdnq ghyettedle
      301 keifndllss kqliqeklpn nevdqlcypy yvgsplavkl skeagykcsy wgfidgkptn
      361 rvgddphqiv rlnddfifll pghkckkfhq lfvdkfrtrf ikh
//
LOCUS       WP_010473264             202 aa            linear   BCT 01-JAN-2025
DEFINITION  peroxiredoxin [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010473264
VERSION     WP_010473264.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..202
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22453
     Region          12..184
                     /region_name="PRX_Typ2cys"
                     /note="Peroxiredoxin (PRX) family, Typical 2-Cys PRX
                     subfamily; PRXs are thiol-specific antioxidant (TSA)
                     proteins, which confer a protective role in cells through
                     its peroxidase activity by reducing hydrogen peroxide,
                     peroxynitrite, and organic hydroperoxides; cd03015"
                     /db_xref="CDD:239313"
     Site            order(12,53..54,57,120,130,143..145,147..149,153..154,161,
                     177..180)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239313"
     Site            order(51,85..86,111,113,125)
                     /site_type="other"
                     /note="decamer (pentamer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:239313"
     Site            order(52,55,131)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239313"
     Site            order(55,177)
                     /site_type="active"
                     /note="peroxidatic and resolving cysteines [active]"
                     /db_xref="CDD:239313"
ORIGIN      
        1 msqhevhecl rvgqaapdft atavydqefs evklsnyrgk yvviffypld ftfvcpteit
       61 afsdrynafk dlntevlgis vdsefshlaw tqtdrksggv gdlnyplvsd ikkeistayn
      121 vldpdagval rglfiidkeg vvqhatinnl afgrnvdetl rtlqaiqhvq shpdevcpag
      181 wqpgdktmnp dpvkskvyfe sv
//
LOCUS       WP_010473299             172 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010473299
VERSION     WP_010473299.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..172
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18787
     Region          <49..>154
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          54..79
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(55..56,59..60,62,86,89..90,93..94,96..97,120,
                     123..124,127..128,131)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          84..114
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          119..147
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlrqrlpksl lasivvssla lisiqstiar pnsypskthp taiifskenq sqkylldgiq
       61 kalsgdypga ieaydlalqf apanaeayyn rgvayfsigh sdnalqdfer aisitpsmae
      121 aygnrgtirl qmgeyksals dfqtaadlfe qeddhisaea mrslihqnta qp
//
LOCUS       WP_010473385             458 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Streptomyces].
ACCESSION   WP_010473385
VERSION     WP_010473385.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..458
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=49841
     Region          6..413
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mstterpril vvgggyvgly aarrilkkmr ygeatvtvvd prsymtyqpf lpeaaagsis
       61 prhvvvplrr vlpkaevltg rvttidqerk vatvaplvge ayelpfdylv ialgavsrtf
      121 pipglaeqgi gmkgieeaig lrnhvleqld kadsttdeev rrkaltfvfi gggfagaeti
      181 gevedmvrda akyyrnvsre dmrfilvdaa dkilpevgpk lglygkehle grgvevylst
      241 smescvdghv vlknglevds ntivwtagvk pnpalarfgl plgprghvdc qptlqvtgtd
      301 yiwaagdnaq vpdlvgrkag nenawcppna qhalrqakvl gdnvlsgmrg fpqkeyshan
      361 kgavaglglh kgvamivmgk akiklkgrla wymhrgyhgm amptwnrkir vfadwtlamf
      421 lkrevvslga iespreefye aakptpapaa qqekakas
//
LOCUS       WP_010473506             283 aa            linear   BCT 01-JAN-2025
DEFINITION  lysophospholipid acyltransferase family protein [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010473506
VERSION     WP_010473506.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Valentine,W.J., Shimizu,T. and Shindou,H.
  TITLE     Lysophospholipid acyltransferases orchestrate the compositional
            diversity of phospholipids
  JOURNAL   Biochimie 215, 24-33 (2023)
   PUBMED   37611890
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10168420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..283
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006644 - phospholipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=32052
     Region          37..274
                     /region_name="LPLAT_MGAT-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: MGAT-like; cd07987"
                     /db_xref="CDD:153249"
     Site            order(59,62,67,84..87,133..135)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153249"
ORIGIN      
        1 mkstvsskpr qgwslddrdp aaiaaliprw kwfydcyfrv qtsgwqhvpt akalfvgshn
       61 gglaapdlhm lmydwfcrfg aerpiyglmh kgmwqvspsv aefatlggai rayptvaraa
      121 fqmgasvavf pggaqdvfrp hrlrdrihfc drkgfiklal qeevsiipfi swgahdtlwv
      181 ladcyefikq lhhlgmpwll dtdptifpiy lglpwglsig plpnfplpiq ihtqicppih
      241 ferygrkaak dkvyvqacyd rvvrnmqdal dqlilkasea req
//
LOCUS       WP_010473557             447 aa            linear   BCT 01-JAN-2025
DEFINITION  GTPase family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010473557
VERSION     WP_010473557.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466459
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..447
                     /product="GTPase family protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=48653
     Region          43..373
                     /region_name="YeeP"
                     /note="Predicted GTPase [General function prediction
                     only]; COG3596"
                     /db_xref="CDD:442815"
ORIGIN      
        1 mvensqppdp scppqsiskk fwqpgpakkf lktarhllqp irqgsqslkr yfqideqeva
       61 ailervkatl ptteviligk pqsgkssiir sltgattdii gqgfrphtah tqqyayptee
      121 lpllyftdtm glgeaqpdts dpmmelsqll tpdssltvdt psakvmiltv klndfatdfl
      181 qnviaqlreq hpqvpcllav tcahelypph venhpayppn eaevsrafaa iqkqfegicd
      241 rsvlidftle edaftplfyg ldtfvdqlae llpeaesrll hqilddagig teigslyret
      301 srrylttfaa maatlaavpl pfatmpalta lqvtlvsllg rlygqslsls qaggvisaia
      361 ggfiaqvvgr elikfvpgfg svvaatwaaa ytwalgegac vyfgdllggk tpdpqqiqqt
      421 mqqsfqeaki rfkgevwsad sqsppte
//
LOCUS       WP_010473595             360 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010473595
VERSION     WP_010473595.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 360)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..360
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39786
     Region          <10..349
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mpclytnlee kvdertqels qaledlqlaq egliqsekma algqliagva heintplgai
       61 rssieyianf ldqhlttlpq ffrelpieqa eqfqslllra ltpsptlsgr errhtrkaia
      121 kqlteqgils aeslasllld lgicddlhdl lpllseprse pllkmvrqft rvrestrdia
      181 tasdrsakiv falktyaryd hsgdkieani tdgidavltl yhnqikhgvt vhrsfaeipp
      241 iacyfdelnq vwtnllhnal qamdhqgtld idvsqqadqv cvkitdsgpg vplelkekif
      301 epffttkppg egsglgldiv rkiidkhqgt lsldsvpgrt tfsvtlpmsv mptpqptpal
//
LOCUS       WP_010473638             148 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010473638
VERSION     WP_010473638.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..148
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15986
     Region          7..136
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtgfspdatd wrilqalqad grasfaelar avsmsasavt ervrrleeag vitgytavvd
       61 qealglpvla fvrlryphgn ykpfhdllda tpevleahhv tgddcfvlkv aarsmrhlee
      121 vsgrigalgs vttsvvyssp lprrpvtr
//
LOCUS       WP_010473705             286 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010473705
VERSION     WP_010473705.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..286
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30115
     Region          1..283
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 msdtpgarlq alfdghrltp tqrriahwmv rraadvpfls svelaelagv sqpsvtrfav
       61 algfdgypal rrhlrevapa epartgtggd pagdtaaney qqavhaeien lrhlaellad
      121 papaeragrl laasrplpvl glraaaaqar gfayfaakvh pdvrvldegg smltdrvdaa
      181 vragatallc falprhprev ldaleyakaa gltvvtvads afapvarhsd lllpaavgta
      241 lafdtacgpm llgrvlleam cdvlpdaqar leefdaraaa rglfve
//
LOCUS       WP_010473748             326 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Streptomyces].
ACCESSION   WP_010473748
VERSION     WP_010473748.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..326
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35097
     Region          130..326
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msttasrspq pqpqpqpqpq pqpqppvkak arekagarvr agarpaapae etgfvapsae
       61 eladllvadp drrpprpsal sasltfgrra llkikhvpeq lfdvtafpim mvlmytylfg
      121 galagsvsay vqfllpgilt msvvmitmyt gvavntdidk gvfdrfrtlp vwrpapmvgy
      181 llgdvvryli asavmlavgl aigyrpagga agvlagvall mvfafafswi wtmfglllrs
      241 eksvmgvsmm vifpltflsn vfvdprtmpg wlqafvnnnp vthlatsvre lmaggrpaad
      301 lawtlgwsav fvavfgavtm rlynrr
//
LOCUS       WP_010473813             171 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: STAS domain-containing protein [Streptomyces].
ACCESSION   WP_010473813
VERSION     WP_010473813.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..171
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17437
     Region          7..105
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(23,25..27,33,56,58..60,62..64,67..68,90,94..95,97)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            59
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 msddpevltt taaglrivrv sgefdfdsae nlaralapap gdapagtvld lsqvtfadss
       61 flhvllraag ehraagtpll lvrpsppvar llevtdttgs ftfvdsvtaa asaaraapgg
      121 ehgevrpvsg pprradgagr reddesegge hggprhrdep capphhrggg a
//
LOCUS       WP_010473834             235 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endonuclease V [Streptomyces].
ACCESSION   WP_010473834
VERSION     WP_010473834.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..235
                     /product="endonuclease V"
                     /EC_number="3.1.21.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003727 - single-stranded RNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=24411
     Region          5..220
                     /region_name="Nfi"
                     /note="Deoxyinosine 3'-endonuclease (endonuclease V)
                     [Replication, recombination and repair]; COG1515"
                     /db_xref="CDD:441124"
ORIGIN      
        1 mtiletpagw padenealav qdelrarvvl depgppvgtg lvagvdvayd derdlvaaaa
       61 vvldartldv vdeatavgrv afpyvpglla frelpavlaa ldalaagpgl vvcdgygqah
      121 prrfglashl gvltglpvlg vaknpfafth eqpgprrgdt aplldgaeev gralrtrdgv
      181 kpvfvsaghr vgldaacaht laltpryrlp ettrradalc rralreaaar qgsgv
//
LOCUS       WP_010473866             297 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010473866
VERSION     WP_010473866.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..297
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=34128
     Region          18..290
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mselvlatva teflsrpgya tstlksyelt llplleqqgh lpiellsrgv ledylnsleh
       61 lsytthrrhq silqsllnfa vergylrsnp iahlrqrrpd aqqgesltde lvrylspqql
      121 erlyqlvrpd vrlhalvall hrsgarisei lsldlevidl kgrkyqvlgk gnkkrwcfys
      181 qdaeqileky ihhyrhsgng alftarqpmt rtisrlsytt vykawkkmtr depllkgvri
      241 hdlrhtfate rvglmgieel rallghqhiq ttlryqkvts araeevamqa lkkltsg
//
LOCUS       WP_010473871             211 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: superoxide dismutase [Streptomyces].
ACCESSION   WP_010473871
VERSION     WP_010473871.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..211
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23285
     Region          5..198
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 matytlpelp ydyaalapvi speiielhhd khhaayvkga ndtleqleea rdkdqwaaln
       61 glqknlafhl sghilhsiyw hnmagdggge plekdgtgel adaiaesfgs farfkaqlsk
      121 aaattqgsgw gvlayepvsg rliveqvydh qgnvgqgsvp ilvfdaweha fylqyknqkv
      181 dfieamwkvv nwqdvakrya eakdrvplia p
//
LOCUS       WP_010473877             201 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010473877
VERSION     WP_010473877.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..201
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22442
     Region          4..195
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 miaitelspe llqcviardl tagqilfqqg dpakyvfwve sgrlklvsft eqqminfytv
       61 gagesfaeta lntetysctv maeqpsrvla ipkhdfleal qqssnlckry vchltqrfea
      121 vkqllelrsi rsardrllhy ltqqcqpgqs tiplttslkv latnlglspe vlsrtfsqle
      181 seqilsrkkg svtllaewls s
//
LOCUS       WP_010473914             158 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010473914
VERSION     WP_010473914.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..158
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17112
     Region          <42..>145
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          42..67
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(43..44,47..48,50,74,77..78,81..82,84..85,108,
                     111..112,115..116,119)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          72..102
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          107..133
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrrklvgayf tsgiaafcls laccsprplf aqepsnpltn phfaaatsll eqkdfqgamr
       61 elnrailldp slataysfrg vlhldaknyq eatadfaqvt rlqpksadah lnlaksqlml
      121 kdyqsalqsa tkatqldpqn qaaallvkmi phlskpaq
//
LOCUS       WP_010474015             482 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Streptomyces].
ACCESSION   WP_010474015
VERSION     WP_010474015.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..482
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49234
     Region          20..479
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mpstatappa asgpqpagsr naldrffkis ergstvgrev rggfatffam ayiivlnpii
       61 lgsaedvygh qldggelvta tvlsaafgtl lmgvvgnvpi alaaglgvnt vvalqlaprm
      121 awadamgmvv lagiivmllv atglrervmn avpaglrkgi aigiglfill iglvdsgfvs
      181 ripdaahttv plqlgadghl ggwpvlvfav gtlltlaliv rrvpgailvs ivamtvaami
      241 vnavaevpsw glttptwpgn plstpdfgll gqvslfggfe kvglltgslf vftvllscff
      301 damgtilgvg dearltdekg dfpginkvlf vdglavaagg atsssattcy vestagvgeg
      361 artglasvvt gglftvalfl tplatmvpsq aatpaliavg flilagsvrd idwgdftiav
      421 paflamvmmp ftysitngig igfiafsvlr laagrgrevp vpmyvvsavf vfyyampalg
      481 lt
//
LOCUS       WP_010474143             774 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010474143
VERSION     WP_010474143.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18107293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..774
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=87589
     Region          <341..754
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          565..>751
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          604..639
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          645..673
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(646,649..650,653..654,656,686,689..690,693..694,
                     696..697,726,729..730,733..734,737)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          678..714
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          725..751
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdadqalrqv eqlviaqtge rlselqqtil rqvwlgykyf diadaygcte ghakdvgsdl
       61 wkllsqilge kitkknlrqv ltvhrhgsvp skqayrldfv grhqaihhln hlnqqgatai
      121 aiqgegglgk ttlaqqylqs qnfaivlell makepdnits vqrvveewlt rdlheepgle
      181 fgisldrlkr hlhqrpigvl vdnlepaldq qglligehrq yvelfrvltd prnlgltlvt
      241 srdriceasl nlhhyrlsgl dveawqqyfq lqeltidptl laqihraygg nakamtllcg
      301 sirsdfggda aafwqdqqqd llvaadlahl innqidrlqn ldpqayqlfc rlgcyryqtl
      361 atlskagvla llwevpeakq raslmslqnr slvecrqgry wlhpvtraaa itrlqpspdw
      421 qqahryaaqy wsdsvqtltt tedalqalea fyhykaiqdy phaaavllqv rqnqwqqyls
      481 lgsslyrmgl hqslvgelps lmthlpcdrs ycelqnilad yywstgqirq gialqkdsls
      541 lstqalaspn ldprhhrhfq iqvldshlsl glyyidlwel ehsahcfqqv ikiatqtdqd
      601 rwvpkasicl alvlthlgkt eqaqqlatqa wgerlpkteq aarlaffmql lgqtytalgd
      661 lfsahalfeq altvaeashy phiqartltg ravihrlqgk fnlavvdhdq aiallkplna
      721 tcdlaeayfq wgltyqamhq icdrnqafhq atqlftamda pcqvqrvlac tttp
//
LOCUS       WP_010474200             746 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: transglycosylase domain-containing protein
            [Streptomyces].
ACCESSION   WP_010474200
VERSION     WP_010474200.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..746
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=78866
     Region          19..661
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mgrakarrsr geqggggirr lftwrkllgt lfvfcllllg gfyavyllvp vptanaeakl
       61 qsnvykysdg svlarsgkvn rsivgldkip dpvekafvaa enktfyedsg vdfkgtargi
      121 vntltgkgkq ggstitqqyv knyyldqsqt vtrklrelvi slkvdqrqsk dqilagylnt
      181 syygrgaygi qaaaqayygv dadkltveqg aylaavlqap sqydwtsatp sarklvterw
      241 nyvldnmvee swldpaeraa mtfpapqkpk papgmegqtg ylveaanqel vdqgvkeedl
      301 raggwtitlt vdkkrqrelv eavdkqlesr ldregdevda tvqagatsvd pktghvvaly
      361 ggvgatehwm snatrrdhqp astfkpivfa salenesttq dgrrigantr ydgtsgrpvk
      421 ggdtpfapqn lddysygevt vqeamnksin svfaqmivdv gpakakktal algmkdsdgf
      481 veqpamtlgt mgastwdmag vyatldnhgk kvtptivksa ehehravrpa dpigpqavsr
      541 qtadtvtsvl tgvvangsgl aayspayqaa gktgtsennk sawfagytpe lvtvvalfge
      601 daekgtqvsl tgtansgras gggfpariwa dytldalggg sdarfdlevl esydpgpkpt
      661 aqpsrstppp ssrpspsddp aepsrtpsss assttpapqs psadpptptp ptpspsppsp
      721 sasesgggps tepgpdgggr daaagq
//
LOCUS       WP_010474226             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010474226
VERSION     WP_010474226.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..321
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34098
     Region          19..235
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtsddhhtar ahpgcghaie aeevrrrydg gfeavsgvtf avphgevfal lgtngagkts
       61 tvelleglap vsggrvrvlg hdpyreraav rprigvmlqe ggfpsdltva etvrmwagct
      121 sgarptgeal davglagrar vrvkqlsgge rrrldlalal lgrpevlfld epttgldaeg
      181 rrdtwalvrd lrdagttvll tthyleeaea ladrlsimhg grivasgtpa evtasrpari
      241 rfelpagtpa allplslraa qpdgrrveir thdlqsalae llrwadergv rlealdarsa
      301 sleeafleia rsgaaaepvg v
//
LOCUS       WP_010474227             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Streptomyces].
ACCESSION   WP_010474227
VERSION     WP_010474227.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..269
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27512
     Region          76..269
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 maaataphrp gsrpgtttaa grlgalarae aallarnrta lfvtllmpll migalragld
       61 raglektgmt lveasvsggl gmilvivvyl nlvpayvgrr eelvlkrlrt geasdaeilt
      121 gtalpsvala vaqcvimvva avaflgvrap qrpellvagv lagvvllgal aaftaaltgt
      181 vesaqlttmp lflvsalgsg lfvplealpe rveavcallp asgvvalvra gwlggaeage
      241 lvragaaalv wtaaavfavr wrfrweprr
//
LOCUS       WP_010474276             279 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010474276
VERSION     WP_010474276.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..279
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32359
     Region          90..247
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mleqwiidqg anlqvgvffs fyslfllaev ympqrrtspk rrsrwpanll lsviniavls
       61 llpislfgla twaesqrigl lnqltlpiav fiisnlllrg fisffthwlm hkipwlwrlh
      121 rvhhldteld vtstlrfhpl efvatllpgm llvitfglsp wlllvyevld avvtafshan
      181 itiprfidrg lraiivtpnl hrihhsswqp etdsnfsavf piwdiifgtf rprsrepqat
      241 melgledird rrvhqffwll rspflrqdvs dplmpklhs
//
LOCUS       WP_010474322             250 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Streptomyces].
ACCESSION   WP_010474322
VERSION     WP_010474322.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..250
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26370
     Region          53..229
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mpdaaltlvg rsvrlsrrnp dalitamvlp vmlmlvfvyf fggaidtgtr tsyvtyvvpg
       61 vlllcagfga sttavrvsed mragivdrfr sldvgatpil aghvgasvlr nvlstalvvg
      121 vafligfrpe agfagwaaal glllafvlav swlsaaagll artpeaasgf tflmmflpyp
      181 ssafvpidtm pgwlhgfaeh qpvtpviesl rgllldrpvd dapwialaww agllvlalal
      241 sgtlfrartr
//
LOCUS       WP_010474341             299 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Streptomyces].
ACCESSION   WP_010474341
VERSION     WP_010474341.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..299
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30649
     Region          48..>194
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
     Region          <143..277
                     /region_name="COG4099"
                     /note="Predicted peptidase [General function prediction
                     only]"
                     /db_xref="CDD:443275"
ORIGIN      
        1 mpdpaapdaa ardaaardaa eeasalshpa vapdatapyg ahpdqvvdfy aprdrsgrvp
       61 lvvvlhggaw rapydrwhvs pfadrlarrg favanveyrr gaalpapsga epvagrwpet
      121 fddvaaalda lpalaaehlp qadprrtvvt ghsagghlal waaarhvlpa gspwrrpepp
      181 elrgvvalap iahfgravel gvcggavtql lggeegfeer aasadpavlp ptgiatvvvq
      241 gredtvvplp vaeayaeaaa raggavgltv ldgvghfpli dpaadacgvv aekitrlar
//
LOCUS       WP_010472278             219 aa            linear   BCT 01-JAN-2025
DEFINITION  alternative oxidase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010472278
VERSION     WP_010472278.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Affourtit,C., Albury,M.S., Crichton,P.G. and Moore,A.L.
  TITLE     Exploring the molecular nature of alternative oxidase regulation
            and catalysis
  JOURNAL   FEBS Lett 510 (3), 121-126 (2002)
   PUBMED   11801238
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Berthold,D.A., Andersson,M.E. and Nordlund,P.
  TITLE     New insight into the structure and function of the alternative
            oxidase
  JOURNAL   Biochim Biophys Acta 1460 (2-3), 241-254 (2000)
   PUBMED   11106766
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Siedow,J.N. and Umbach,A.L.
  TITLE     The mitochondrial cyanide-resistant oxidase: structural
            conservation amid regulatory diversity
  JOURNAL   Biochim Biophys Acta 1459 (2-3), 432-439 (2000)
   PUBMED   11004460
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Sluse,F.E. and Jarmuszkiewicz,W.
  TITLE     Alternative oxidase in the branched mitochondrial respiratory
            network: an overview on structure, function, regulation, and role
  JOURNAL   Braz J Med Biol Res 31 (6), 733-747 (1998)
   PUBMED   9698817
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   7  (residues 1 to 219)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..219
                     /product="alternative oxidase"
                     /EC_number="1.10.3.11"
                     /GO_function="GO:0009916 - alternative oxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25736
     Region          17..202
                     /region_name="AOX"
                     /note="Alternative oxidase, ferritin-like diiron-binding
                     domain; cd01053"
                     /db_xref="CDD:153112"
     Site            order(29,68,71,120,189,192)
                     /site_type="other"
                     /note="diiron binding motif [ion binding]"
                     /db_xref="CDD:153112"
ORIGIN      
        1 mirllvgvlv fvlktvyrdr piprfyvlet varipyfsyl svlhfyetlg fwrradwlkv
       61 hfaeswnelh hllimealgg dkkwidrfla rhvallyywi vvalyvvspr sayhfmelve
      121 qeafqtynsf lhdhaeelks qpapqiavsy yrdgdlymfd efqsarvpee rrpavdnlyd
      181 vfvnirddem ehvktmvacq sleaqanlsp hsptliaes
//
LOCUS       WP_010474351              57 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CsbD family protein [Streptomyces].
ACCESSION   WP_010474351
VERSION     WP_010474351.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..57
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..57
                     /product="CsbD family protein"
                     /calculated_mol_wt=5843
     Region          6..57
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 msakgkasak aqqargavke nvgravgdee maaeggaera radlreaaek vkdafkr
//
LOCUS       WP_010474393             390 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: 8-amino-7-oxononanoate synthase [Streptomyces].
ACCESSION   WP_010474393
VERSION     WP_010474393.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..390
                     /product="8-amino-7-oxononanoate synthase"
                     /EC_number="2.3.1.47"
                     /GO_function="GO:0008710 - 8-amino-7-oxononanoate synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_process="GO:0009102 - biotin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39167
     Region          13..383
                     /region_name="PRK05958"
                     /note="8-amino-7-oxononanoate synthase; Reviewed"
                     /db_xref="CDD:235655"
     Site            order(110..111,114,177,206,209,238,241)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:99747"
     Site            241
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99747"
ORIGIN      
        1 mpedvpgdta pgapfdwida earrraaagl vrtlrprpad tdlldlagnd ylgltrhpev
       61 agaaadaarr wgagstgsrl vtgstalhae lerelaafcg feaalvfssg yaanlavlta
      121 lgprgslivs dagnhasivd gcrlsraeta vvphadpgav retlgahpgr ralvvsdsvf
      181 svdgdaaplg alagacrehg aalvvddahg lgvlgeggrg alaaaglaga pdvvatatls
      241 kslgsqggvv lgparvvehl vnaartfifd tglapaaaga alaalrllrr epdlagrara
      301 vaaalhtelt aagltaarpd aavvsvraps pesalrwaad craqgvavgc frppsvpdgv
      361 srlrltarad ldgerigrav svilrtappr
//
LOCUS       WP_010474467             398 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Streptomyces].
ACCESSION   WP_010474467
VERSION     WP_010474467.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..398
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42887
     Region          10..381
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mddcfagrph hqlrqqvref aeaevrprip ameaarsvqr elsrliarqg wlgatigtdl
       61 ggmgvghlgk tviieelsrv saamgamvqa sqlgvakilh fgsdeqrktw lpaiaagacl
      121 ptiavtepes gghvlgmaat avrdgeeyvl ngrkvfvgns hvgdlhgvvv rtgpgpkglt
      181 aflveadrpg lrvgdekpam glhgfgfgel sfedcrvpaa nrlgeegdgl avaysssvly
      241 granlaavsl glhravleet trfceerhry geplhalpsv rlrlgrlqsr lmtarltayh
      301 avhlldqglp cdaelmnakl vnaewaldsa reameihaaa glftdrpier ylrdahhlfa
      361 pagtsdvqll rlaevalgta rgqwserlad vvrrepar
//
LOCUS       WP_010474576             396 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Streptomyces somaliensis].
ACCESSION   WP_010474576
VERSION     WP_010474576.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..396
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41080
     Region          145..390
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtpprppred vllasaglag glllwslglf nqgarhaivd apwavlppll vtaslglvrr
       61 trpraallvg tvavvadqft rgsiatvlmf tdlvyaaavy gpaafarrlp rttglvtvav
      121 siaslawyre pwalllgvla glvsfvpatt gaivrnhrqa adaarlraeq tallaemdrr
      181 eavvaerarm arelhdmvag hlsaiaihst aalsldepat srealgvire nsveglaemr
      241 rlisllrdsg adrdpapapt lvglsalvrq aaahgtasgl vftltapppd gdlpapvela
      301 ayrivqeslt nalkhagage vavvvertgh altvvvtspp grpaagprap gsgaglvgmr
      361 ervallggef eagpvdgawr vravlpvaed drepaa
//
LOCUS       WP_010474594             180 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Streptomyces somaliensis].
ACCESSION   WP_010474594
VERSION     WP_010474594.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..180
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18530
     Region          19..173
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mkhatphagt pagtftqlls strrgarlar llavrelhsw gapddltdra elvvaelaan
       61 avlhgrvpgr gfrlalafdp sapclrvevt dargesypri ppaapeaapl ppravhpdpl
      121 rpgplppgaf ppsalppdal rsggrglalv aaladrwdcv phppsgktvr avltspaaga
//
LOCUS       WP_010474603              76 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF433 domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010474603
VERSION     WP_010474603.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Sala,A., Bordes,P. and Genevaux,P.
  TITLE     Multiple toxin-antitoxin systems in Mycobacterium tuberculosis
  JOURNAL   Toxins (Basel) 6 (3), 1002-1020 (2014)
   PUBMED   24662523
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..76
                     /product="DUF433 domain-containing protein"
                     /calculated_mol_wt=8351
     Region          3..65
                     /region_name="COG2442"
                     /note="Predicted antitoxin component of a toxin-antitoxin
                     system, DUF433 family [Defense mechanisms]"
                     /db_xref="CDD:441983"
ORIGIN      
        1 msyrdiitie pdkrggkpci rrmritvynv lgwlaagmsv aeiiddfpel teadiracle
       61 faadrdhrlv asvsaa
//
LOCUS       WP_010474660             194 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010474660
VERSION     WP_010474660.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21106
     Region          2..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 martkefdpd aalqsalelf wrrgyeatsm adlvehlgig raslyatfgs krelylramd
       61 ryaetrdpll laelsqpgpa lpavravvrr faaeatspeg rskgcfvtnt aaelaphdpe
      121 aarrvdigwe rfetslhsal vraraqgelp egrdpralar mllvllqgvr vvgkasgdpa
      181 rvrdaaeqal alld
//
LOCUS       WP_010474671             242 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010474671
VERSION     WP_010474671.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Hahn,Y., Lee,J., Seong,C., Yoon,J. and Chung,J.H.
  TITLE     Structural analysis of phylogenetically conserved J domain protein
            gene
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 325-333 (1999)
   PUBMED   10542335
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Cheetham,M.E. and Caplan,A.J.
  TITLE     Structure, function and evolution of DnaJ: conservation and
            adaptation of chaperone function
  JOURNAL   Cell Stress Chaperones 3 (1), 28-36 (1998)
   PUBMED   9585179
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20412282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..242
                     /product="J domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=27371
     Region          5..57
                     /region_name="DnaJ"
                     /note="DnaJ domain; pfam00226"
                     /db_xref="CDD:395170"
     Site            order(33..35,44,47..48,51..52)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
     Region          <147..>241
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          151..178
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(152,155..156,158..159,161,185,188..189,192..193,
                     195..196,226,230..231,234)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          183..220
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdiadcyrll qltsranied lkasyrrlar qwhpdtnpgd qlahekfiqv teayktlqki
       61 vppapnnstv pasvpsrata kprsapsvkv stqpakpssp pppqqpqhqt rpqasisrpr
      121 vtvpkqptpq pkpssaprks plspadiklk vdsykqlqel iqrqrfprav aliealaqrl
      181 pqdvevrqwq aiiyqswgrq lirerklnqa raylkkalnt dphnkalwae ieldfkkiem
      241 af
//
LOCUS       WP_010474760             260 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010474760
VERSION     WP_010474760.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..260
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28700
     Region          10..243
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mnsttqsfgi tvdnlsvtyn narlalynat cnvepgtitg lvgpngcgks tlfksimgfl
       61 rptqgqirvq glpvqkaqkr qlmayvpqad evdwnfpvsv fdvvmmgryg ymnllripsa
      121 kdrrlvmssl ervgmvdfrh rqigelsggq kkraflaral aqeskvmlld epftgvdvkt
      181 ekriidlmlq lrqenhtili sthdlasvst fcdrtillnq tilasgttae tfteenlalt
      241 fgglpirsln pmplqsevea
//
LOCUS       WP_010474799             438 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010474799
VERSION     WP_010474799.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..438
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=49136
     Region          12..>256
                     /region_name="K-ycf53"
                     /note="Signaling protein combining a Ser/Thr protein
                     kinase domain and the GUN4/Ycf53 porphyrin-binding domain
                     [Signal transduction mechanisms]; COG5752"
                     /db_xref="CDD:444462"
ORIGIN      
        1 mkeaiqqtik dytiirslaq ggfgvtflae dsnqkrlvik qlrpiaqndl essltyfike
       61 cdrlkavghh driptfieyf eeggqhhivq qyipgqnlle eargrdryse tevidllldc
      121 letldfihsk nlihrdikpa nlirrqidsk iclvdfgaak avsetilakt shtligsvsy
      181 sapeqmigha tyasdlyalg atclflltgq eptdlysiae dqwcwqetyq tspefaevln
      241 klihratskr yttakearnd vadvcdrirk reknearahq iqtlrrhqlv rttrkvalrv
      301 aavaalgvgi wqvtpvitsn ieklptiitt edqppiiien depkpevnpf efegdsksie
      361 elvkskmiaa gypamivepi pfmlgavkfv vlasgifslg ftyisfsrge rldtsrlvts
      421 gllmifvlig phlliall
//
LOCUS       WP_010474845             588 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010474845
VERSION     WP_010474845.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..588
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65408
     Region          121..499
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mkhftaqave npksppkvdv dsylwsppal giyaclgllv atnfkgqkrk gvlargqlat
       61 dthkaaarke amklikrrrh nevalyiqtp eglryrkkgk ktvisipedp qtlyfpnmea
      121 gtaaigatgs gksyslinrl ikaafdqhfp viyfdlkytd kesptsqlig iakkrgykvn
      181 vfapslpesc ivnpvdllan eldaeiarqf alvlhrnftp akssegnpff pqaaqkliqg
      241 lmmlakmsqy pdlmmcrsil ktpnladlie qadipemvkv vfdtmisskd spetfasivs
      301 tvsntlgnlm tpnvlpaicg ktnmpldleg rqllifgvng qcvdvvlpii atvlhlvvnr
      361 nvtrprqtpl ilgldeipsi flpalddwln qrrsaglcti lgfqsmemle klytkpgasr
      421 ilggcttqai fqlnesesak lfaelpgsed alfrqrsrss grksrsttna eqrqttklve
      481 pneiatfprg kalifsrgns dgknvrvplv enivipqrdi devnasvkqw pkirqelier
      541 safsmptnqd frnrdqevye llkarltpeq eaalekqrlk daeefrnl
//
LOCUS       WP_010474905             275 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pentapeptide repeat-containing protein
            [Streptomyces].
ACCESSION   WP_010474905
VERSION     WP_010474905.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..275
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=29218
     Region          <187..267
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 msvlpphter adlradcagc fglccvalpf arsadfaadk pagtpcgnlg ddfrcgvhar
       61 lrdsgypgct vfdcfgagqk vsrvtfggrd wrtdpdsart mfavfpvvrq lhellryaae
      121 aldlpaarpv hrelrrrhde idaltrgdar tlleldvpal raevnalllr aselarsgvp
      181 grrrdhrgad lagarlrgak lrgaslrgar liaadlsgad lrgadltgad lrdadlsgad
      241 ltgalfltqp qltsargdga tllpaalrrp ghwaa
//
LOCUS       WP_010474938             151 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010474938
VERSION     WP_010474938.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..151
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=16824
     Region          7..>142
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtraprinal paphrerlma lsrevafepg hrlfderrpa drfwiirtga vtldsrvpgs
       61 prpaviemlg hgelvglswm fppyewelga eamslvrase fdaavvrelc aaetafgyal
      121 tqwvgqvlsh rlqstrvrll dmyaphgsgv f
//
LOCUS       WP_010474991             260 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Streptomyces].
ACCESSION   WP_010474991
VERSION     WP_010474991.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10061613
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..260
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26606
     Region          <12..116
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          67..116
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          <169..258
                     /region_name="SLT"
                     /note="SLT domain protein [Mobilome: prophages,
                     transposons]; COG3953"
                     /db_xref="CDD:443153"
ORIGIN      
        1 mpargkhrrp rnsrlsrgia vastggaala lpltgaaaas aapaaapaai adkpaaapaa
       61 akaakavtyt vtagdtlsgi aeehsvrggw kklyqdnrka vgddpslirp glrltvgaka
      121 paakgkpaak rsaparadrs earpavapla akaytddldg wiresldvma rngipgtyeg
      181 ihrnimress gnpsainnwd snaaagtpsk gllqvidptf rayhvpgtsm dpfdpvanit
      241 aacnyaadry gsidnvhgay
//
LOCUS       WP_010475018             344 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010475018
VERSION     WP_010475018.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..344
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37985
     Region          1..340
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mtrvlalipg dvgrqllffp tletlhrhys qveidvivep rakqafrlcr tvdnvltfqf
       61 enrngaadwg nligqmrdrr ydasltisre wtagllcwlv gipqrvgyen lalpawvrfa
      121 rkrfptlggt vadlsgkclt aavppnarpy daqryhdlll glgidtpcpd isiqiplddq
      181 nwakaeqerl giagqpyiil hggtgaensd depsqfypir swesviegyl erqpdtplvv
      241 vqtaenkewv aslvavcpql qivmpqhvgq laafidaghl micadraplh lgvavktrlv
      301 alfgaleptr hlptaphfag lksltskvad ippiqvlekv wgvs
//
LOCUS       WP_010474997             327 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010474997
VERSION     WP_010474997.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..327
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35768
     Region          49..292
                     /region_name="AKR_unchar"
                     /note="uncharacterized aldo-keto reductase (AKR)
                     superfamily protein; cd19100"
                     /db_xref="CDD:381326"
     Site            order(65..67,97,102,125,156..157,192..193,213,245..251,
                     262,279..282,287,290..291)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381326"
     Site            order(97,102,125,156)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381326"
ORIGIN      
        1 mspktqrrtf llsslaatgg llgslllhkd rrsvsvppss apknssipkk vlgktgielp
       61 ilglggagqt plsqpgaeke avdmiqqawd lgiryfdtaa sygpsedylg kvlpqyrsqi
      121 flasktakrd rdgawreler slkrlntdyl dlwqlhhvsf aeeietlfsa ngaikameea
      181 ksqgiikftg itghhepqii ieglnrypfd ttlipinaad vhhprpfiss vlpvahqqqv
      241 gviamkvpay gkllrpgvls gmseamgysl sqpgvhtcii aaetvdqlta niqtaqafqe
      301 fdvatlanie krtqatwedh sffrkwa
//
LOCUS       WP_010475083             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Streptomyces].
ACCESSION   WP_010475083
VERSION     WP_010475083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..249
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26412
     Region          5..239
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mepqlehrvt dgvatvvisn pakrnamtaa mwralpella elaadrevra lvltgagdtf
       61 cagadistlh epddrqqala vraeealaaf prptlaavrg ycvgggcqla aacdlrfaea
      121 garfgvtpar lgivypssst rrlvslvgps takyllfsae lidderalrt glvdevlpag
      181 gldgrveaft rvllsrsplt qaaakefaag ltgrdahwar eaaasgdrae gvaaflerrr
      241 prftyrsrp
//
LOCUS       WP_010475115             175 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010475115
VERSION     WP_010475115.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..175
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18597
     Region          6..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtakpmpfde ldrkivatlm anarasfsei gaaiglsata vkrrvdrlrk advitgfrat
       61 vrpsalgwrt eayievycdn aapprrlaev arkypeiaaa mtvtgaadal lhvratdveh
      121 feevlerirs epfirktisy mvlshllpds peagasesap galpggapgg agnvl
//
LOCUS       WP_010475126             440 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Streptomyces somaliensis].
ACCESSION   WP_010475126
VERSION     WP_010475126.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..440
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45299
     Region          154..440
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtttgahqda agttsrgfgw werrrgaald iglgvvsale caaegadfag tahlpaagga
       61 lfglaagsvl alrrrrpiav vlvsiavtpa qmgylmavvg lytlaasdvp rritavlasv
      121 spvavflvtf vrlrqdvaas dfdpgswyvp lasvlmsvgl tappvllgly igarrrlmes
      181 lreradsleq elslladqae qraqlartqe rtriaremhd vvahrvslmv vhaaalqava
      241 lkdprkaaan aalvgemgrq altelremlg vlrtepvppa aapppaapgg gaasaereaa
      301 gaggsaedgs gpglggveel veqsraagta vellvqgear aypphveqta yrvvqealtn
      361 vhkhaagarv vvrlahrgee vamqvengpg daaaasarlp sggngllgmr ervtalggvf
      421 vsgptdeggf rvsavlpavr
//
LOCUS       WP_010475157             326 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010475157
VERSION     WP_010475157.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..326
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37492
     Region          1..324
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mgllvngfwk dqwydtaktg ghfvrkdaqf rnwvtldggp gptgssgfka esgryhlyvs
       61 yacpwahrtl ifrllkglea hisvsvvhwf mgdhgwtfne gegvvadpif dakfayeiyt
      121 hadpnytgrv tvpilwdkqt qtivnnesse iirmlnsafd qvgaksgdyy pvnlrteids
      181 lnhriyhtvn ngvykcgfat tqdayeeale plfttldwld erlanqrylt gnqiteadwr
      241 lfttmvrfdp vyvghfkcni rrlvdyphlw pyvrdlyqtp rvaetvnfmh ikrhyyqshg
      301 tinptqivpn gpeidfmtph hrgksg
//
LOCUS       WP_010474469             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Streptomyces].
ACCESSION   WP_010474469
VERSION     WP_010474469.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..190
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=20554
     Region          <34..>186
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
ORIGIN      
        1 mtydptghll ltpvdreapa rvlrlrqlgl geypdpafda faarlaevtg apysmvnfid
       61 enrqffaglh tptgtrsglr pgadpaasgt vgrymardhg ycphvvvrrk alvledvcdy
      121 prfagnpvvd eigirsylga plidrtgttl gticvvdtep rpwgraglet ikslaaelve
      181 qihqredggl
//
LOCUS       WP_010475221             425 aa            linear   BCT 01-JAN-2025
DEFINITION  S-layer homology domain-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010475221
VERSION     WP_010475221.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Gerbino,E., Carasi,P., Mobili,P., Serradell,M.A. and
            Gomez-Zavaglia,A.
  TITLE     Role of S-layer proteins in bacteria
  JOURNAL   World J Microbiol Biotechnol 31 (12), 1877-1887 (2015)
   PUBMED   26410425
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Mesnage,S., Fontaine,T., Mignot,T., Delepierre,M., Mock,M. and
            Fouet,A.
  TITLE     Bacterial SLH domain proteins are non-covalently anchored to the
            cell surface via a conserved mechanism involving wall
            polysaccharide pyruvylation
  JOURNAL   EMBO J 19 (17), 4473-4484 (2000)
   PUBMED   10970841
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Engelhardt,H. and Peters,J.
  TITLE     Structural research on surface layers: a focus on stability,
            surface layer homology domains, and surface layer-cell wall
            interactions
  JOURNAL   J Struct Biol 124 (2-3), 276-302 (1998)
   PUBMED   10049812
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Lupas,A.
  TITLE     A circular permutation event in the evolution of the SLH domain?
  JOURNAL   Mol Microbiol 20 (4), 897-898 (1996)
   PUBMED   8793886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..425
                     /product="S-layer homology domain-containing protein"
                     /GO_component="GO:0030115 - S-layer [Evidence IEA]"
                     /calculated_mol_wt=46277
     Region          273..317
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
ORIGIN      
        1 mespkigfgv glafalflpi agcsgdavqq afsadpqasq wsnlstlpkg fpadlsypna
       61 nlqgvqqsqt nlpsspnsqr ppqqtrwatp dnsqkvqqyy sqllqkrswq lsgrklsqqq
      121 lillakrdql qvrvtipatg tlvpvrtgnn sgrripmtvf fidysqekal skvesptqsl
      181 pkpgdldfig pvanqtpess ntdasqssae vpatlqayvs dvqrlevidl gnpnqpiqrg
      241 tfarwlvktn nrlyqdrptq qirlaatnqt pifkdvpssn pnfpyiqgla eagfipspls
      301 gdadqatfqp nqpltrevll swkvpidfrk ilpsattakv qevwgfkdtk qistptlsai
      361 ftdhnngela nirrllgsal llqpkksvtr aeaaatlwfi gvagegysak dvlraeqqae
      421 aagps
//
LOCUS       WP_010475347             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010475347
VERSION     WP_010475347.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..322
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35027
     Region          27..252
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msattrslae lerqaahrrd rpayghdali acdrlvrifs rraggdavev qalqgldllv
       61 hegeltalvg asgsgkstlm nilagldtpt agtarvagrd llamdakarl ryrrevvgfv
      121 wqqtarnllp ymtaaqnvvl pmrlaglprr rragrarell sllgvadcrd rrpqqmsggq
      181 qqrvaiaval anapavllad eptgeldsat gqqvfaafrr aneelgttvv ivthdqavag
      241 evrrtvaird grtstevlrr tevdaagres lvareyamld ragrlqlpse ytaaldmrdr
      301 vlleleedhi qvrpdgdrgr dt
//
LOCUS       WP_010475362             107 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: STAS domain-containing protein [Acaryochloris].
ACCESSION   WP_010475362
VERSION     WP_010475362.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris
  ORGANISM  Acaryochloris
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Acaryochloris"
                     /db_xref="taxon:155977"
     Protein         1..107
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11704
     Region          5..93
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(11,13..15,21,44,46..48,50..52,55..56,78,82..83,85)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            47
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mshkvvqpte lldgisanql rreitdvmae gvktilvdlq dvtfmnssai galvatlkav
       61 ragggemflc slndqvriif eltkmdqifk icadrqefeq kfavtan
//
LOCUS       WP_010475407             241 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010475407
VERSION     WP_010475407.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..241
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25487
     Region          11..223
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mslfgqdlsf lealsaqdrr allaegaprv yepgtvmire rdtsayvlal lsgwavvsvg
       61 tergtrlila lrgagevvgd laavdrgprs atvtalgrvr avavsgdrfr rflaarphat
      121 slimqqlsar lrsadverrs lasetvlqrl aarlaelaer agrpgprgtv leiplpqqdl
      181 aaaigatrea vakalrvlre rgvvrtaprr vvvtdmaell rlaqgrgpgp agpaeksppg
      241 v
//
LOCUS       WP_010475419             124 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator
            [Acaryochloris].
ACCESSION   WP_010475419
VERSION     WP_010475419.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris
  ORGANISM  Acaryochloris
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Acaryochloris"
                     /db_xref="taxon:155977"
     Protein         1..124
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14143
     Region          18..111
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mnvqdihqyf knpppvyitk evavcyiltv lleegdsygt allkhiranh ppyrisdtvl
       61 yaalnflide emlsgywqne sgrgrprrmy qvaegreeda knlsqlwlkf lgkdpaltes
      121 lvlt
//
LOCUS       WP_010475434             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010475434
VERSION     WP_010475434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..267
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28829
     Region          18..267
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 maddiegars ggariptvia ddvhvvyrvn gggtagrgsa taalnrilrr dkgegrgvrr
       61 vhavrgvsfv ayrgeaigli gtngsgkstl lraiagllpt ergrvytdgq psllgvnaal
      121 mgdltgernv ilgglamgms reeikeryqd ivdfsginek gdfitlpmrt yssgmgarlr
      181 faiaaaknhd vlmidealat gdrkfqirse erirelrkea gtvflvshsn ksirdtcdrv
      241 lwlekgellm dgptdevlra yeketgr
//
LOCUS       WP_010475462             324 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Streptomyces].
ACCESSION   WP_010475462
VERSION     WP_010475462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..324
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34807
     Region          36..304
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mpavtvqnpl tlprvaapag aaarpvlavt tapsgfegeg fpvrrafagi dyryldpfim
       61 mdqmgeveyq pgepkgtpwh phrgfetvty lidgtfvhqd snggggtitd gdtqwmtaga
      121 gllhieappe slvvsgglfh glqlwvnlpa rdkmkdpryq dirggsvrll tspdggallr
      181 viagaldghe gpgithtpit mvhatlrpgs evtlpwrpdf nalayvlagr gavgterrpv
      241 rtgqttvfgd grsvtvrade kqdgntpdle ivllggrpir epmahygpfv mntreellqa
      301 fedfqagrlg rvpavhgaer krpf
//
LOCUS       WP_010475471             352 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010475471
VERSION     WP_010475471.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..352
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38335
     Region          23..348
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mttiektgdt pvpsgaadgt rpllevrdlh vefhtrdgva kavngvnysv ssgetlavlg
       61 esgsgksvta qaimgildmp pgripkgeil fhgqdmlkms aeerrrirgr kiamifqdal
      121 sslnpvlsvg yqlgemfrvh lglskkdaka kavelmdrvk ipaakarvnd yphqfsggmr
      181 qrimiamala lepdliiade pttaldvtvq aqvmellael qrefnmglil ithdlgvvad
      241 vadkiavmya grivetapvh elykrpahpy trglldsipr ldqkgqelya ikglppnltr
      301 iptgcafnpr cpkaqdvcrt dlpplhrvte qdgtelvgrg sachfwketi hg
//
LOCUS       WP_010475481             331 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010475481
VERSION     WP_010475481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..331
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36410
     Region          2..320
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mllevsdlhv efrtregtar avdgvtfsvd agetlavlge sgsgksvtaq avmgildtpp
       61 gritagrilf qgrdlltlre eerrrvrgar mamifqdals alnpvltvgd qlaemytvhr
      121 gmskrdarar avelmdrvri paarervgqy phqfsggmrq rvmiamamal epaliiadep
      181 ttaldvtvqa qvmdllaelr remgmglvli thdlgvvadv adriavmyag rivetapvhd
      241 lykapahpyt qglldsiprl dhkgrelyai rglppsltai ppgcpfhprc prvrdvcrtd
      301 dpplyevsad rrsachfwre tlhkepvdaa r
//
LOCUS       WP_010475525             408 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Streptomyces].
ACCESSION   WP_010475525
VERSION     WP_010475525.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..408
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44065
     Region          6..406
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 maeftlelnd dqkevrdwlh gfardvirpa aaewdereet pwpviqeaak vgiysldfya
       61 rqffdptglg ipvameelfw gdagialsiv gtglaavgvl angteeqigt wipqmygtpe
      121 dvkvaafcss epdagsdvaa mrtravydga kdewvldgtk twatnggiad vhvvvavvdp
      181 elgsrghasf vvppgtpgls qgqkfrkhgi rashtaevvl qgvrvpgscl lggkeklder
      241 lararerark ggervknaam atfeasrpav gamavgtara ayevaldyat trhqfgrpii
      301 dnqgvafqla dmrtridaar llvwraswma atgkpftsae gsmsklyase takdvtarav
      361 qilggngytr eypvermhrd sgiytifegt seiqrlviar alsgvpir
//
LOCUS       WP_010475576             172 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010475576
VERSION     WP_010475576.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..172
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=18912
     Region          <41..144
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mnprikpwlr tisvvfavvw lvgscfvlns qptwaddgaq nftfadlrye dfenknfega
       61 slagaillka nltnanlkgt iltmatfqrs nltnadltet fadrvlfnea dltnaiftda
      121 mltsskfyda titgadfsya fldrdqvtmm ceyadgvnpv tgvstresle cp
//
LOCUS       WP_010475738             239 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010475738
VERSION     WP_010475738.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..239
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=25715
     Region          13..229
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mvplrdenpt qitpyvtygl ivlnvlifgy elslspgqls lfmqrwavvp ieltasfggf
       61 savdagewgt litsqflhgg flhvagnmly lwifgnnvee qlgrgrfllf ylacgalavl
      121 tqwffnplsv vpslgasgai agvmgayifr fpqvriltlv plgiylttfr ipailylgfw
      181 flqqafygva sldapvtvgm eaggiaywah aggfvfgail gpllglfska dsavlsaed
//
LOCUS       WP_010475750             406 aa            linear   BCT 01-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010475750
VERSION     WP_010475750.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..406
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=45144
     Region          20..111
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mtdvllyvln pmplpahlli qamyeainer nvakaleyvd pdccyqdlnf ptpfqgkaav
       61 eelftesckg mpadllfvvd ditegdalav gilwhvelgg iplpngrgvs fcrlsektgk
      121 lifardlvep vikpgkgafl ilrliaplvr lllkpaesge tslqssaspp dssqpwisrl
      181 lwllagayiy ilflsppgql mpgepvwaiq aetwqevlne slnfffilpl anmlgihyle
      241 aplvhpvdqa ffnfaiawif iflpllladv rsqklpkvpi wsmalfltna fmipymamra
      301 ampipaevps pskglltrvf gwtgllvsgm alfwfgfvgp efgtvaerln yfgtqvttnr
      361 vsaafcvdfv fftffqivll gavesnpqkr wlrfvpfwgl vawlii
//
LOCUS       WP_010475844             278 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010475844
VERSION     WP_010475844.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..278
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29014
     Region          50..265
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mdplslglfa vlgiaagtla gllgigggml ivpglfylfd liqlpqeslm hmaagssmci
       61 mictaasstw ahhrqehiqw sifrtiiagi avgvvsgnll anrmptqile lifgifllvv
      121 stkiffekks eeaeeqtvga pgimptsavg mvigfksgvl gigggalsvp fllycglpmk
      181 kasgtsasft lpiaivgtls flllsgnqta ipwstgyvyw pavllvapft mlgapigakf
      241 agivapeklr tifaglllvi smrmlsgtgl iawdfplv
//
LOCUS       WP_010475868             238 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010475868
VERSION     WP_010475868.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..238
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=25684
     Region          11..234
                     /region_name="ASKHA_NBD_ROK_PPGK"
                     /note="nucleotide-binding domain (NBD) of polyphosphate
                     glucokinase (PPGK) and similar proteins; cd24058"
                     /db_xref="CDD:466908"
ORIGIN      
        1 mgtpadesll vlsvdiggsg ikamvldesg qpiterqrie tpaypnppav ldvivelakg
       61 qgdfnrvsvg fpgvvqngvi ktavnlnkew idydlaknle arldapvrva ndadiqgyga
      121 isgqgvelvv tlgtgfgsal fvnghlvpnl eiahhpfikg ktyeqqlgrq amkkkgkkaw
      181 nrhlaqaiqn lehlfnydrl ymgggetkrv kielpdnvei vsnragilgg ialwrdrg
//
LOCUS       WP_010475878             476 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
            ligase [Streptomyces].
ACCESSION   WP_010475878
VERSION     WP_010475878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..476
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=49475
     Region          2..469
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mialslaeia ditggqahdi pdpdvrvtgs vvydsrqvep gglfaafage nvdghdyaeg
       61 avaagavavl atrpvgvpav vvpdvtaalg alartvverl gttvvaltgs agktstkdll
      121 aqllqrkgpt vwpagnlnne iglpvtalra teetrhlvle mgargvghir yltgltppri
      181 glvlnvgsah igefggreri alakgelvea lppaeeggva vlnaddplvk amasrtrarv
      241 vlfgespeas vraenvrlte dgrpafrlht ptgcsdvtmr lygehhvsna laaaavahel
      301 dmpvheiava lseagslsrw rmevterpdg vtivndayna npesmraalr alaamgeaar
      361 akggrtwavl glmaelgdea laehdavgrl avrlnvgklv avggreaswl qlgaynegsw
      421 geesvhvsda qaaidllrse lrpgdvvlvk asrsvglerv aqallentae gevagr
//
LOCUS       WP_010475906             184 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010475906
VERSION     WP_010475906.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..184
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=20212
     Region          1..156
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mfrkilvald hsetaldvfd qaldlaattq anlmllhvls mddqdapdap tsfpsmyyyp
       61 glsatsikvy qqqweqyaht aqdileaqse earlagvsvr ttqkqgapge ticevakewq
      121 adlillgsrg raglsewllg svsnyvmhha pcsvlicret etpppnsipd hlnrqlmsnl
      181 ggwq
//
LOCUS       WP_010475957             416 aa            linear   BCT 01-JAN-2025
DEFINITION  filamentous hemagglutinin N-terminal domain-containing protein
            [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010475957
VERSION     WP_010475957.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10530825
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..416
                     /product="filamentous hemagglutinin N-terminal
                     domain-containing protein"
                     /calculated_mol_wt=45255
     Region          23..>195
                     /region_name="TPS"
                     /note="TPS secretion domain; pfam05860"
                     /db_xref="CDD:461762"
ORIGIN      
        1 mikpifwtya vagwslflcp afsqvtpdqt lgnensiieq qiqrklikgg avrgstlfhs
       61 lkelsiqkgq qvyfanpsdi siilarvtgg nqsningtlg vlgnadlflm npsgitfgpd
      121 atmnlngsfi attgssfife ngqifsatnp qiapslrisv pvgiqfdgts gqievngnsk
      181 lisnpkssrt falvgdgint nntsiiqnkg niffisistg iaqisqqqdr ykllshnfdg
      241 lsdikiqnsv lfvqdevlfi dqasdnssln gvffqskslf issfilftsf gegvdipeiv
      301 kkpqkiqksc rpgqaignss fvhigrggvp lgpnhlqtpp aiwqdlrssq lpqqnlysqq
      361 vehsretspn kvytkvsqsn iteakgwtrd dqnrivltaq tsklmaydsr rptvnc
//
LOCUS       WP_010476010             167 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DinB family protein [Streptomyces].
ACCESSION   WP_010476010
VERSION     WP_010476010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Newton,G.L., Leung,S.S., Wakabayashi,J.I., Rawat,M. and Fahey,R.C.
  TITLE     The DinB superfamily includes novel mycothiol, bacillithiol, and
            glutathione S-transferases
  JOURNAL   Biochemistry 50 (49), 10751-10760 (2011)
   PUBMED   22059487
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Cheo,D.L., Bayles,K.W. and Yasbin,R.E.
  TITLE     Cloning and characterization of DNA damage-inducible promoter
            regions from Bacillus subtilis
  JOURNAL   J Bacteriol 173 (5), 1696-1703 (1991)
   PUBMED   1847907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..167
                     /product="DinB family protein"
                     /calculated_mol_wt=18914
     Region          16..163
                     /region_name="DUF664"
                     /note="Protein of unknown function (DUF664); pfam04978"
                     /db_xref="CDD:428232"
ORIGIN      
        1 mtrtdmpaap derthlttfl dyvrdtavak ceglsaedar raplphsplm taagvishlr
       61 wvehywldfv flggedrapw apedpdremr ialdvplprl vaeyaeqadr lrrvvaehdl
      121 dveaerpvrd gvrvtlrwil lhlieetarh nghldairel tdgrtgt
//
LOCUS       WP_010475964             203 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010475964
VERSION     WP_010475964.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..203
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22963
     Region          26..191
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          113..203
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 madlgifrsk dsaidgaryi srvdasfrlr tlkpkdlpev aallcrcfyp eegwqswfnp
       61 imqmgifhdl qsrysvrlmp ftsligaqia ressveselv gtvevslksl spwmpfapsv
      121 pyisnlavap qcrcqgvgkq llfaceemvr qwghhrlylh vmddntparr lyakagyqlv
      181 dspptwpnil faspkrlllc krl
//
LOCUS       WP_010476020             114 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Streptomyces].
ACCESSION   WP_010476020
VERSION     WP_010476020.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..114
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12365
     Region          1..99
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrtdavrghl dglllavlep gplhgyaiit avqqrsggal elrtgtiypa lqrlerlgll
       61 rsswdavger rrrcyeltea grrslaqert awrefttaig svlnppspst glat
//
LOCUS       WP_010476055             244 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476055
VERSION     WP_010476055.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..244
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27044
     Region          14..211
                     /region_name="yflN-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Bacillus
                     subtilis yflN; MBL-fold metallo hydrolase domain; cd07721"
                     /db_xref="CDD:293807"
     Site            order(64,66,68..69,153..154,171,210)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293807"
ORIGIN      
        1 mtapiqtiat sfafnitvnc ylietddgyi lidtgmpnqr qaiedaleqa ncqigslkli
       61 ilthgdidhc gnaaylrqkf dapitmhadd vgmvergdmf wnrknpnlli kvlfrlffgl
      121 hkadqftpdl yledrstlse ygldaeaihl pghskgsigv lmstgdlfcg dllgntdkpe
      181 lwtivddpga ahtsvkklds lpintvypgh gqpfpieqfm hdhskdrsld sqatyvklgq
      241 lfny
//
LOCUS       WP_010476019             328 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476019
VERSION     WP_010476019.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 328)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..328
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36891
     Region          64..327
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mtrhspqqah dflhqsslgl aivgivlmtp fsinnflqgr yllgvgglli ngifafntwt
       61 itkrnyysdt ltlwvlvpiv ifflnlafiq qgiigvfwcy psviacyfml perkawlanl
      121 tllsitfpia whiiepalal rmistvvmvs ifsaifvrvi naqqqklklq aitdpltgll
      181 nrtslhetle qaiaqskrmg ismtlasldi dhfkaindaf ghatgdqvlr disgllkerl
      241 rrvdqvfrig geeflllfyg sdtesgylva eelrhligsq pflpdhsvtv sigvatlhpk
      301 edwttwmqrs ddylyraksa grnqvmcm
//
LOCUS       WP_010476145             303 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010476145
VERSION     WP_010476145.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..303
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32395
     Region          6..289
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mssqaarlyi llsiaaalit mglkfgayql tysvglfsdv aessvnliaa laafgaltva
       61 aqppdkehtf ghskaeyfss glegllilva aisiaitaip rlmdpqpive lelglglsii
      121 aslvnagvaw illragkrlr sitlradaqh lltdvwtsvg vvagliivkl tgwlildpim
      181 allvavhivw vaiklireti aglmdsalpe sdqaviratl tayqaqgivf halrtrvaga
      241 rnfvsfhvlv pgnwtvqkgh dlcdtleqsi mtalpgthvm thlepiedpv swedaeldrs
      301 hhp
//
LOCUS       WP_010476210             423 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Streptomyces somaliensis].
ACCESSION   WP_010476210
VERSION     WP_010476210.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..423
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=43894
     Region          8..268
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,60,65,70..73,85)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,34,36,68,84..87,91,93,130,132,
                     134..135,137,155..156,159,176..179)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,34,36,68,84..87,91,132,134..135,
                     137,155..156)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,91,93,130,132,134,159,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(155..163,172..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <252..>423
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
ORIGIN      
        1 markigsryt ahqilgrgsa gtvwlgegpd gpvaikllre dlasdqelvg rfvqertall
       61 glehphvvav rdlvvdgndl alvmdlvrgt dlrsrldrer rlapaaavav vadvaeglaa
      121 ahaagvvhrd vkpenilldm egplgpggah pavltdfgva klidtpgrtr tnriigtpdy
      181 lapeiveglp praavdiyal atvlyellag ftpfggghpg avlrrhvtet vvplpgipde
      241 lwqlivqcla kapasrlras elaarlhdla plvahmppld vdepgaepps epygddpypt
      301 lpdaprraav plvpgssads srdthtsmrv pgpdelsggp lgtarapras gqrrpgsarn
      361 kpsaarrrrl alsvagaala aaagvggwfa vggddaeapp gdsrqsapet apetapdtgs
      421 arp
//
LOCUS       WP_010476219             318 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476219
VERSION     WP_010476219.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..318
                     /product="MBL fold metallo-hydrolase"
                     /calculated_mol_wt=35097
     Region          24..237
                     /region_name="TaR3-like_MBL-fold"
                     /note="MBL-fold metallo-hydrolase domain of Myxococcus
                     xanthus TaR3 and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07715"
                     /db_xref="CDD:293801"
     Site            order(87,89,91..92,171..172,192,237)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293801"
ORIGIN      
        1 migltadsvq aihkpfmqek ltvrfwgvrg siacpglhtv ryggntpcve vqaghqkfif
       61 dggtglrvlg qellkhlpve ahiffshthw dhiqgfpffa pafmpgnrfh iygtrgsdgk
      121 tiekrltdqm lhpnfpvplq imggsldfyd leagqtveve ditirnailn hpggsigyrl
      181 ewqgltvsyi tdtehfpdal dpnvlaladq ahvliydaty tdaeyheagn skvgwghstw
      241 qeaikiaeaa kvdqlvlfhh dplhndvfld digrkaghrf tnsiiaqegl sitltpngqs
      301 slqyaelgra issvpdra
//
LOCUS       WP_010476213             438 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010476213
VERSION     WP_010476213.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..438
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=46625
     Region          9..36
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <25..178
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Region          43..72
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          127..414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          147..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(149..150,153..155,157..158,162,165,174,176,178,
                     182..183,186..188,190..191,195,198,207,209,211,215..216,
                     219..221,223..224,228)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          176..207
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293,297..298,301..303,305..306,310,313,322,324,331,
                     340..341,344..345,348,350..351,355,358,367,369,371,
                     375..376,379..381,387..388,392,395,404)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          293..322
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          324..367
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          369..404
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mskesngqal iaaiqqrdcn qvcslldagf spdtwddcni pglviaaqkg ytdiveillv
       61 aganfaspgi aepqgskgef gdfrasgpma iwaaavaghq dilqilksam pemlgqvlvg
      121 icergslaal htllavidvh qyysygplqa asqagrpdvv qilvqsgidv nrpsitketp
      181 lvvaadqgyv evvktlveag alvdswtsde dsplfgaayc ghlevynylf plvseetqry
      241 aeytlhkalk rkareqntdv eafikgamlg qmdviqwglr rgidinaiga snqtalmyaa
      301 ssglqqivqi lleagadpni qsdddgpdag ttalmkvash yachfaenvq eiikllvaag
      361 adpnlqdkag rtalihsvtw gyskpaieal ktlisvgadl nihdnagkta liyaqdrcqe
      421 qagfsvvvel lersglse
//
LOCUS       WP_010476261             333 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010476261
VERSION     WP_010476261.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..333
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37393
     Region          15..328
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mgkslppkai islgkfvwtt mwnvmmsnma prskagayir pesqfrntvg sesfpaesqr
       61 yrlyvglgcp wahrtlvvra lkglqdvidv vvvqpsdteg gwvfasehqg crnlrdlyll
      121 aqpgyegrct vpvlwdtqtq kvvnnessei ivnlnsafnd laqqpdldly pealrppidq
      181 wnekiyhavn ngvyrcgfaq tqtaydqacr elfevldeid talaqqrylc gdtltladvr
      241 lfptlfrfdv ayyglfkcnr rriqdyqhlg pylrdlyqlp gvadtcnlea vkqsyygflf
      301 plnpggiipa gpditslsdp hgreqigkap qav
//
LOCUS       WP_010476284             193 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010476284
VERSION     WP_010476284.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..193
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=21001
     Region          <31..171
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mmanpehvae lkkgvqswnq wrqrypdvip nltssnwvev dlsnanlqma dmsganllgt
       61 iligaelrca nlantdllgg llngadmsra hlcwtrlfga nldsatlaga dlygvdlgra
      121 ilsksnlmga slmetdlcea nlqraqllgt nlynanlhra vlrkvegltv sqiktahnwd
      181 gaffseefrm rlg
//
LOCUS       WP_010476303             440 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476303
VERSION     WP_010476303.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..440
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47723
     Region          5..382
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(15..16,19..20,23,55,119..120,122..124,127,147,
                     150..151,154,230,233..234,237..239,242,264,268,322,326,
                     330,346,349..350,353..354,357)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtkvfyailv nslvalltnt fvwfaatfwv ylqtesvvam smmagiylit vsisgfflga
       61 lvdsyfkktv mllssfcslv lyllaygvia fsqvevftnp anprlwgfil lalagviagn
      121 lrsialptlv tllvhkskrd qanglvgtin gvsflvastf sglvigflgv nwmleiaial
      181 tllailqlvt ipipeqkilr tesetrnvdl qgtirsiylv pglfaliffn tinnflggvf
      241 mslmdaygls lvsvqvwgil wgflslgfil ggigvarcgl gkiplrtlfl anlsiwgvai
      301 fftiqasivl lamgsfvylc ltpvveaaeq tilqtviple rqgrvfgfaq sieqaasplt
      361 afmvgpiaql lfipfmttga gvellgpwfg tgrargiall ftvtglvglm itvlamrshs
      421 yrilskqyrr akthqlearv
//
LOCUS       WP_010476360             287 aa            linear   BCT 01-JAN-2025
DEFINITION  uroporphyrinogen-III synthase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476360
VERSION     WP_010476360.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schubert,H.L., Raux,E., Matthews,M.A., Phillips,J.D., Wilson,K.S.,
            Hill,C.P. and Warren,M.J.
  TITLE     Structural diversity in metal ion chelation and the structure of
            uroporphyrinogen III synthase
  JOURNAL   Biochem Soc Trans 30 (4), 595-600 (2002)
   PUBMED   12196144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..287
                     /product="uroporphyrinogen-III synthase"
                     /EC_number="4.2.1.75"
                     /GO_function="GO:0004852 - uroporphyrinogen-III synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006780 - uroporphyrinogen III
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0033014 - tetrapyrrole biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30968
     Region          13..252
                     /region_name="HemD"
                     /note="Uroporphyrinogen-III synthase [Coenzyme transport
                     and metabolism]; COG1587"
                     /db_xref="CDD:441195"
ORIGIN      
        1 mtdlllstar lplgnkrivi taprpyagrl ataiiqqggl pivmptiety aldpapdldh
       61 alqqlrdfsw vaftsrtgiq avmlrlqqld iplfllnqch icaigqdadq lqalgvrvdl
      121 ipkesspagl vaelaqipdi dtqrilvpip qveripepdi vpnfladlqq lgltvvsvpa
      181 yvtrrleata yaveveqirq gkvdaiafss taeisallqm vdaetlmkhc viacfgpyta
      241 gnakdlglsv divsqdfssf tgftaaiaqf fhpasadipr qdpvilp
//
LOCUS       WP_010476374             703 aa            linear   BCT 01-JAN-2025
DEFINITION  M3 family metallopeptidase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476374
VERSION     WP_010476374.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..703
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=78992
     Region          8..702
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 msndtpiaaq dnplllcegl ppfdqieaeh vlpaitqlla eleqdlqtle aevqptwtgl
       61 vepleqlgdr lswswgiigh lmgvknspel reayeagqpk vvefinrlsq srpiynaykq
      121 lqqspdwsql dpaqqrives airdaelsgv gltgeakerf nqiqlelanl stqfsnhvld
      181 atkafnillt npkevaglpp sllslaaqaa ravgekdstp ehgpwlmtld ipcfgpfmqh
      241 sqrrdlrekl yrayisrasa gefdntdiid rilelrkeea kllgfetyae aslaskmapt
      301 vsavetlqeq lrqasfdqat aeldtlktfa qeqgseedsd lkhwdisfwa erqreakfdi
      361 tdeqlrpyfp lpqvldglfn linrlfgvtv taadgqapvw qedvryfqva neqgepiahf
      421 yldpysrpae krggawmdec lgraqfrrgd tvktrlpvay licnqtppvd gkpslmtfre
      481 vetlfhefgh glqhmltqvd yagaaginnv ewdavelpsq fmenwcydrq tlmgmakhye
      541 tgeslpeeyy qkllaartym sgsamlrqlh fgmvdmelhh nyepggseqv kqvrdriakt
      601 ttvlpplped sflcsfghif aggysagyys ykwaevlsad afsafeeagl endaairetg
      661 rrfrdtvlal ggsqhpmevf ksfrgrepst eallrhsglk aev
//
LOCUS       WP_010476392             138 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal-responsive transcriptional regulator [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010476392
VERSION     WP_010476392.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140950
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..138
                     /product="heavy metal-responsive transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15454
     Region          7..133
                     /region_name="HTH_HMRTR"
                     /note="Helix-Turn-Helix DNA binding domain of Heavy Metal
                     Resistance transcription regulators; cd04770"
                     /db_xref="CDD:133398"
     Site            order(8..10,24,40..42)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133398"
     Site            order(54,57,61..62,71,82..83,86,89,93,99,103,106..107,114,
                     119..120,130,132)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133398"
     Site            order(82,117,130)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:133398"
ORIGIN      
        1 mvvatrlkig evskqtntsv galryyeslg llasdrgeng yryypqeavq qvlfikkaqa
       61 lgfsledihe vlnvhqqgdv pcefvqsllq dkieqleaqi qkmmafkael edyrdrwsts
      121 qpppqpgdic plistvpl
//
LOCUS       WP_010476407             366 aa            linear   BCT 01-JAN-2025
DEFINITION  saccharopine dehydrogenase family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010476407
VERSION     WP_010476407.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..366
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39697
     Region          40..357
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 msfepktrsn nnnrlliigg ygqvgqivaa qlaplfpssv vvagrnleka ntaaseigyg
       61 aeaqaidlfa tyskdalldi alvivcldqt dtrfveqclm hgihyvdisa nydflsqidr
      121 lddlaltnna tvilsvgvap gltnmlarrv seqmesidqi divlefglgd hhgqaavewm
      181 fdnldvaytv qengqpisvr sfsesidigl pgqdierpay rfnfsdqhvi rhtlnvptvs
      241 twvrfddpis twliaklsqa gfggllkqgw gravaiwllm nthigtnicg vavqakgkak
      301 dgantltlgi igqrealmta vitaeiarqt lfappppgvh hseqviyldp viaslrrelp
      361 dlvval
//
LOCUS       WP_010476473             138 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal-responsive transcriptional regulator [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010476473
VERSION     WP_010476473.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140950
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..138
                     /product="heavy metal-responsive transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15421
     Region          7..133
                     /region_name="HTH_HMRTR"
                     /note="Helix-Turn-Helix DNA binding domain of Heavy Metal
                     Resistance transcription regulators; cd04770"
                     /db_xref="CDD:133398"
     Site            order(8..10,24,40..42)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133398"
     Site            order(54,57,61..62,71,82..83,86,89,93,99,103,106..107,114,
                     124..125,130,132)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133398"
     Site            order(82,117,130)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:133398"
ORIGIN      
        1 mvvatrlkig evskqtstsv galryyeslg llesergang yryysqeavq qvlfikkvqa
       61 lgfsledihe vltghqqgdv pcefvqsllq dkieqleaqi qkmmafksel eqyrdswsta
      121 qlhpqpgdic pliqsvsi
//
LOCUS       WP_010476501             212 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010476501
VERSION     WP_010476501.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..212
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23705
     Region          5..198
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mslnlyflrh getshsqtgg ycgeldpelt psglqmaqaf rntyqrilwa avytspmkrt
       61 iatamplcea tgvdlqlrdg lkeisygewe drspdyvqan yaedyvrwlt epawnpltgg
      121 etavqvasra slviaeieet fpagnvlvvg hkatirimlc sllgidlgry rdriemlvas
      181 vslvefdrhg pmlkrlgdrd hlpyqlrnri gt
//
LOCUS       WP_010476532             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cell division protein FtsQ/DivIB [Streptomyces].
ACCESSION   WP_010476532
VERSION     WP_010476532.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..269
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=27897
     Region          58..265
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 magpttverg aegaagaspg rpskgsgpgr gggvrhlpar sralfllaal alaggatwll
       61 ygspwlrved vsvsgtrvlt pgevrsaaav pvgsplvsvd tdaigerlrr alpridsvev
      121 vrswphgigl evterepvll irqggahiev daggrryatv taapagvpll hlpagrspsl
      181 rrfgadrltr eavgvtaglp erigrdlrsv rvrsydsltl eltrgrtvfw gsgeereaks
      241 rallalmkav pgaghfdvss psapaasrs
//
LOCUS       WP_010476575             357 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476575
VERSION     WP_010476575.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..357
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39497
     Region          1..157
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          190..351
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlkkilvald hsafsqktfm qslvlakath aklmlfhvis steegyppyp lmpgvleefd
       61 lsyagvansy lndldvfkas slellrsran qakekgltvl yqqsmgdpgr eicdiarqwk
      121 adtiiigrrs rnllskillg svsnyvthha pcsvlivhhq dvpefipkqs intldanqps
      181 feewrgklsy rsilvaldgg dinqpifnra inlakrmsta rlmmlhvlpp dvakvhisst
      241 pptaiaqqrl dnypslrddi lysqqqqwna ydsdclpqlr sytaiareag iptefiqqpg
      301 spgevicefa knrssdlilv gnrgrsglse lllgsvgkyv anhascsvmv vrpqqpa
//
LOCUS       WP_010476696             471 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476696
VERSION     WP_010476696.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..471
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52346
     Region          2..398
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtltfsqlgl sqtrvdclea lgfttptqiq aeaiphllag rdiigqaqtg tgktaafslp
       61 ileqldptvk tpqaliltpt relavqvsea iyqfkadgal rvvaiyggqs idrqisqlrr
      121 gaqlivgtpg rvldllsrge ivldqlswfv ldeademlnm gfipdvrkil ervpgdrkta
      181 ffsatmapei yklskqflnd pvtvtveqpk aaptrinqva yriprtwars tvlqavlele
      241 dpesaiifvr trreaatltq qlqtagysad eyhgdlsqsq rerlldrfrq rrirwvvatd
      301 iaarglhvdd lshvinyepp dsvesyvhri grtgragneg taislvhald rwklheieqh
      361 irqeiptlpt ptrsaiegrr leklteelhs iltgerlasf lptvsqlged ydtqtiaaaa
      421 lqmafdrypa itanlddwss knknggrssr kakpvlnkrr ssnrseisas t
//
LOCUS       WP_010476700             505 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein, partial [Streptomyces somaliensis].
ACCESSION   WP_010476700
VERSION     WP_010476700.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003535
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         <1..505
                     /product="LCP family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
     Region          79..363
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
     Region          388..478
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 ppaqgggrra aapaaagrrr gkektrtrka lvwtggvtaf vllatgagay ylyerldgnl
       61 stidiagagg ghgfkkdqai nilvigtdkr tgqgnsgygd knspghadtt illhvskdrt
      121 natalsiprd litdipectt kledgsekri paqsgvrfnt slgqmdrnpg ctmatvhkmt
      181 gvpvdhfmmv dfnavktlss avggvevcve qavkdkksgl dlpagtstie geqalafvrt
      241 rqafgnksdl sriqtqqqfm gsmfrkmkss dtltspskll dladaatkal tvddgigsvk
      301 klqelgmeia kvdpknitfa tvpvldnpae qvkatvvlde akaeplfsii rndislteve
      361 qkekdvqnar keaqaallkg praepgdvrv dvyngsgvrg gaqatlnwlq nsagvlkstn
      421 ranapaeiak ttleyapnqa dqartladlm glpagamkqg tadagerepm tltlgkdfkg
      481 agvpltgpak apegamaadk qvcak
//
LOCUS       WP_010476735             479 aa            linear   BCT 01-JAN-2025
DEFINITION  TldD/PmbA family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476735
VERSION     WP_010476735.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..479
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52573
     Region          1..476
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mkfdlhqaln tldinadwvg lrqvnekttt havrdgrpqs ngrdftqgvm vevlaegqfg
       61 yaatnrldpa slqgaaeqay qqaiatskwa vhsftpevrp kavgqyqspf qqpldlisva
      121 dqldllvkvc dtlhvsdqiv ktsaftqtle teqifvssng tdthqtfgfv itnyeataqd
      181 gsiiqkrtdn gplarcyqag sevfdpdqvl araqqvgeqa iallaaedcp tatttlvlap
      241 dqmmlqihes vghpleldri lgdernyags sfvklsdfgh lvygsplmni tfdptvpgef
      301 agyafddagm paqreylike glllrglgsl esqvraqvpg vanfrarswn rapidrmanl
      361 nlepgqssfe emistiesgv ymeanrswsi ddyrnkfqfg ceyarliekg kltkvlrnpn
      421 yrgitnqfwg nlaqvgdast famygtpycg kgepnqcirv ghasptcvfk eievfggaa
//
LOCUS       WP_010476751             187 aa            linear   BCT 01-JAN-2025
DEFINITION  Uma2 family endonuclease [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476751
VERSION     WP_010476751.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..187
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21212
     Region          2..179
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mtfaktqtlt leeflkfpnl eqspaweyvd geaaqkpmpk vrhsllqkrl ltkledsegr
       61 yltlpelrct fggrsvvpdl vvvsldkikl ndwgepednf tqppdwsiev lspdqnanrv
      121 idnllhcirh ggllgwlidp ddysvlvltp hkeieiyrgd qqlqgldgmd lnltaeeifs
      181 wlklgtn
//
LOCUS       WP_010476824             351 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476824
VERSION     WP_010476824.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..351
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38962
     Region          20..335
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mpapyrkyfl nrltnsvlir flllfasswa tlqvfayfqs illififaai lafllnyptq
       61 wlkrflphgv aatvvfmvgl lllfgllitv lfavlsqgqe lvnsvtefln ameqlsrqve
      121 qmlaardvqi dfgaieakfr dqviesigss vgviqgivnn lidlilvavv sffmlldggr
      181 iwkwllrglp kasrtrftla mkrnflgffw grfllalffa vssffvflsl svpvplilav
      241 vagifdmipg igatigigli slillpqglw ramqvliaci vlqqieenil mprvmqnslq
      301 mnpvvlffal ligsrlsglv glflsipiag vllslmdndt edddndfskv s
//
LOCUS       WP_010476906             819 aa            linear   BCT 01-JAN-2025
DEFINITION  CHAT domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476906
VERSION     WP_010476906.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Classification of the caspase-hemoglobinase fold: detection of new
            families and implications for the origin of the eukaryotic separins
  JOURNAL   Proteins 46 (4), 355-367 (2002)
   PUBMED   11835511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..819
                     /product="CHAT domain-containing protein"
                     /GO_function="GO:0004197 - cysteine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=91656
     Region          118..819
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
ORIGIN      
        1 mlklffrrrf gflvlliftq tlltpavase dsvkqanaln qqglqlldag npnealqilt
       61 qsqtiykkln ntagiygtli nqslaykqmg qyhsactrlt qvlnldtnic rrwkqtsqee
      121 lktsleksnn iiqsqqiial hnlgnilrll gqleaselvl kqglphssll sgedrhsiel
      181 alantyqsly kqaynqlsis idsdsqansl ntaqeyaqaa lanyqsvtes qsadriraql
      241 ntlqillhlk ksdssplkgi yqqsqnligs yfnnliaadf sqfpanesin lqlklsylla
      301 easlleipss ennlslayem trdalrqaea fgdkrlvsqa ygifgtlylq sdqledatqv
      361 ftkalklaqt iqddylayqw sweiaqihqq rgertqaiaa ysstlqhldk vrtllisana
      421 dlqfnfkesv epvyhnylql llsspnpdlq lvltthkqlq vaelenylkc gklttaqtnn
      481 qqtpytstih ifelngqvei iaktqdgifr hqpdssvvqe elsrlfnflh sdsfeeisea
      541 hfrrnsqvly eqiiapledh lpptgdllfv ldsnfqnlpl smlhdgqkyl verysvtnal
      601 ntqlqqvqpq sleelnvlfa glsedspsft kpdvpwnlea lpevedelas vkeasnktis
      661 llnndfttnr lqsklqgdtp ivhlashgqf ssdpeqtmil afdapikane fhdlisqkie
      721 lgqssielli lsacqtakgd rksalgiagl svqagsrntl aslwlaesea tselittfye
      781 gldnnmpkar alqqaqikli gseeywhpyf wgnfvlvgs
//
LOCUS       WP_010476993             300 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010476993
VERSION     WP_010476993.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..300
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32117
     Region          67..269
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 msqkeleqii tqlqdlswgn tlaemranft sgfsmpahpt aevqpmtasg vtaewitcpn
       61 sstdrvilyl hgggfimgsl aayrrlasdl aaaagasvll ldyrlapenp ypaaledalt
      121 ayrwlienqn fqpkqisiag dsaggnlalg lllslkekar pqpacaalls pycdqtrtgs
      181 tmvshadrdl mvtaplldti adcyapgkdl rspllsplya dlfglpslli hvgasevlld
      241 dalrlarqag ladvpvtlkv wadmihcfhl fapvleegrv aiaeagafls krevlddtll
//
LOCUS       WP_010477040             485 aa            linear   BCT 01-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010477040
VERSION     WP_010477040.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..485
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53633
     Region          20..481
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mqtqdrdtqr dqfaqgkplw araiatpate fgpislplls gqipeglkgt lyrngpgrls
       61 rqgqtvdhwf dgdggilavh vdnggvtasy ryvqtqelqa eeakdqflys gygqmapgpv
      121 wkrwgvppkn vantsvlalp dkllalwegg nphaldpvtl etqgldtlsg ltpkltysah
      181 pkrdphtgni ynfgvifgpk tyiqiycsha sgdiyrqasi plpglsmvhd fvlagrylvf
      241 ivpplrlqml pillgtksls dalqwqphqg tqiividrdt fkevtridtd pwfqwhfsng
      301 hedaagnivv dyvryddfqt nqwlkevvtg ypqapatgkl wqlqinpqsg qvlhneplfn
      361 fgcefpvisp letgqkttai ylnhhshtqr pveemfdcia ridgktsavt smafpsgcyp
      421 meaiyapdpn nfdqgwlltv vfdgnqdqst vqifsanqld agpiavlglp eiipfgfhga
      481 wqara
//
LOCUS       WP_010477087             200 aa            linear   BCT 01-JAN-2025
DEFINITION  Uma2 family endonuclease [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010477087
VERSION     WP_010477087.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..200
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23070
     Region          2..198
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mtlasqrnls ftefldqype dgfyelvnge ivrilatrqh ediagfiadv fkaevsrcqm
       61 nykvsdrivl atqtqtgqeq grhpdvsvvd qaiwrsnrta ytalrepiql avevvstnwe
      121 ddyedkldey qrlgipeywi vdylalgsrt ylgfpkqpav fvyqldaqsh yqfqrfqend
      181 liqsltfpel qltlgqilma
//
LOCUS       WP_010477107             210 aa            linear   BCT 01-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010477107
VERSION     WP_010477107.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..210
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24417
     Region          <21..111
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(25,28,75,104,107)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 marfvggtvn dqgdlvelgl wekeerqhsp alqrlytqls glklmplphd pkpyeptdnl
       61 hqdlfehglh rvateygatc lyvwlmahst gplhqvlael lideinhmtk fwgfgrwayp
      121 htsmfkilvt llcpqsrttk qkpssfsrtl krmmqvlhwe awslpnklsl lwtfvyvlwh
      181 lwrwsrslnp dqlnrwfgqs petpcpstgi
//
LOCUS       WP_010477298             521 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010477298
VERSION     WP_010477298.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..521
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=56931
     Region          22..264
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(28..29,31..34,36,49,51,86,102..105,109,111,147,149,
                     151..152,154,165..166,176..177,182..183)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(28..29,31..34,36,49,51,86,102..105,109,149,151..152,
                     154,165..166)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(32,109,111,147,149,151,176..177,182..183)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(45..46,78,83,88..91,103)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Region          <264..519
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mrpplptmvl lplgtllqkg tyrleqlvrh qglqltyegt hlpsqqtvli ntlnpsrqnp
       61 kkivlhrdaf iqeaqawqnl khpslepird ifvdavlpfl vreklsgqtw atkaktqplp
      121 eaeaiaqitq iadglnqahh qqllhrdiqp knivihpqtn hpvlgnwvwq psppggsssl
      181 lhaytapeva qgqqtvttdi yglaatlytl vtgkipiaas qrqhirleir hpdlsqativ
      241 allrgmamqp qhrpqsisew lkllpkapsp pvsfpiksgn igaaslssne aepqssakfv
      301 tpeisslpds dpsdpeissp seelslapea edlptastvp rqepsqtvst trlqpysvpp
      361 rfpyrvliic svlsgvvgia fglllrfhyq nqftnpqvpa kappvqnedf lpkpgttrrq
      421 letlptptet plespvpspl eeptvdprfe qgdigpdptl qkpvplspvp adpldpdpal
      481 qtpiesypds lapspepspf dpfaqpdfst pppsespesf q
//
LOCUS       WP_010477524             123 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010477524
VERSION     WP_010477524.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..123
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14220
     Region          18..112
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mnfqdifsyf qspppiylnr evavccilti likngesygs almqyvetey ppyrlsdtvl
       61 ynslnflthe givtsywknf pgrgrprrml iipssrqnea nqlsklwldf lelnsrkyal
      121 ati
//
LOCUS       WP_010477584             303 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010477584
VERSION     WP_010477584.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..303
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32435
     Region          6..289
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 msskaarayi llsiaaalit mvlkfgayql tssvglfsdv aessvnliaa laafwaltva
       61 aqppdqehtf ghskaeyfss glegllilva aisiaitaip rlfnpqplae lelglglsil
      121 sslvnagvaw vllragkrlr sitlradahh lltdvwtsvg vvaglvivkl tgwlildpim
      181 allvalniaw vsskliretm sglmdsalpe adqaviratl tayqaqgiqf halrtrvaga
      241 rnfvsfhvlv pgnwsvqkgh elcdileqsi mtalpgthvm thlepiedpv swedaeldrs
      301 qhp
//
LOCUS       WP_010477625              48 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2256 domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010477625
VERSION     WP_010477625.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..48
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..48
                     /product="DUF2256 domain-containing protein"
                     /calculated_mol_wt=5686
     Region          2..46
                     /region_name="COG4338"
                     /note="Uncharacterized conserved protein, DUF2256 family
                     [Function unknown]"
                     /db_xref="CDD:443479"
ORIGIN      
        1 maprkrdlpt kicpvcglpf twrkkwrncw ddviycsekc rrnrksss
//
LOCUS       WP_010477648             421 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010477648
VERSION     WP_010477648.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..421
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45968
     Region          1..142
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
     Region          276..421
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mdnqaylvfq lqelrygida elvqeifplp eltplaeapp diigmlnlrg kivlvmhlac
       61 rlgqsqptct lkdavilmdw qgiqvgivvn qvqdvltfdt aaidtsidyg rpqgspyikg
      121 vtkelevpvv llnpdslirq pdqvaslvwk seldtvepel peislnldtd tsaealeevd
      181 dpdeiaalhq qweallndsd sepmlmadle vansgsdhrl eadleeavap apppsqppkl
      241 gtfferycpd asevdqdvfr qraanlreal tdtdpadlrs lavvglgnqy fgldlswvre
      301 finirsvtpi pccpqhivgn inlrgevmtl vniqtvlnls gelsespqka vvfevndvva
      361 gltvdevvnv talssaqiap ipaavsaayr eflqgtilyd nqylnildlp kmisqgvlnv
      421 a
//
LOCUS       WP_010477890             383 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010477890
VERSION     WP_010477890.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..383
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41860
     Region          150..375
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mnhshkllak agrvllglli slvllvmvlh glqiinawql plkpvlaflg ggslscwiaa
       61 qimkgwhqsp raaprtlrwr rrvlfislfl lislnastyl aaytlthvrd pgqwglgfpk
      121 ptnirtpqer glsysthrlp inssawleaw lipatgtpaq gtvvmfpgnr stkdrqligp
      181 aqtfsqlgyn sllvdyrgvg gssgysttvg mreaedvvva fnalpaldlq ppviaygvsm
      241 gsaailnaia tqnlqpdaii ielpfarfid avrsrlqhhq ippfplaell vfwggvqhgv
      301 ngfshnpvef araiqcptlv mqgqqdpwtt vaevktlfqq itapkqlvia pdgghhqlig
      361 idralwetsl shflqsinad res
//
LOCUS       WP_010477983             138 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010477983
VERSION     WP_010477983.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..138
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14976
     Region          1..137
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mfntilvald speiservml alksfqldtv gkvilthvis tnetgeeqpa drpysdpqgv
       61 frhieeelqt ykaslpcdss leivtgdpae eiirvaniyd adliligsrg ltgvtrilqr
      121 svssqvvsda scsvmvvr
//
LOCUS       WP_010478056             354 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010478056
VERSION     WP_010478056.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..354
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38853
     Region          1..353
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 makleikhln ktynpkvvpv kdlsltvedg efltllgpsg cgksttlrli agleqptrgd
       61 vvigpdvvth ksagdrdiam vfqsyalyph mnvydniasg lklrkmsstd iqqrvaeasr
      121 vlnlddlmrr kpgqlsggqr qrvalgralv rnpavfllde plsnldallr eqvraelkql
      181 fekqnapvvy vthdqteamt lsskvavlyq gdlqqldppq qiysrpanqf vagfigspqm
      241 nlltlrcenq sailgetrip lpssagnpre ivlgirpeht rlatsgdatt vtgqvylven
      301 lgmsnllsik vqggeetira llptdqtwsg dtisvalptn qlhwfdvqtq krle
//
LOCUS       WP_010478083             292 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010478083
VERSION     WP_010478083.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..292
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=31639
     Region          <179..285
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mnlkslnqvs dasqapqddg pttktplsgh qdqllqlaqq rnlealttli dqklaeqvvk
       61 vaeiefkndl lqlsvessev peqsvtvpli rdflsqlrlp evtavtiygq klgqelpfwm
      121 eevaldllil dtqalmpqtm aagsaevtae epsplpeaap lpsetaldit akyeagernf
      181 arinlkdeal pginltladl qeanfvwcnl resslshanl tsaqlrhadl tnanlqgakl
      241 qgtdlqgakl qganlswavl rgtnltdadl tdvnlqnatl ervimpdgtm ld
//
LOCUS       WP_010478246             180 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010478246
VERSION     WP_010478246.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..180
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19407
     Region          3..177
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mgtkvsvfia tsldgfiart ngdidwlnea navvpegedc gfqafmasvd vlvmgrktye
       61 qvlsfgawpy gqtrvivlsr tpiqfpdalp acithsadpp lmlynrlvqe gaqhlyidgg
      121 atiqrflaag lideltitvi pillgegisl fgslakeipl tllsshsydf gfvqlkyavp
//
LOCUS       WP_010478321             240 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010478321
VERSION     WP_010478321.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..240
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25819
     Region          1..238
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkrhliaiag rkggvgkttt acglasifas qkykvliidl dpqsnagyvl gtdptapgtv
       61 ellqgkkpip ikasenlyvl pggpnlaght iqsldpldla daieslqydv iifdcppgve
      121 ylerlglvaa kialictdah plavmgasrv iqdlqvrqkk nrkgasrlgl ilsridlrrs
      181 mdqsldqqla eaypsikrfi ihqdaslawa aaervpliey dskgkaandl mtvsnwvvne
//
LOCUS       WP_010478379             381 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010478379
VERSION     WP_010478379.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..381
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42758
     Region          100..378
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 madltrille afevdgslre flielglrvg lfavgvvlsp lvgrilpfli wwllrlinrf
       61 iplgisktyg efirpvrnsl ittgtfgfia lcanllrrye gfykflglfi ylalaismaw
      121 lasrlaqrvi rlyvvnlvqr lgvevnelvl iietlvnili vlfsvvifaq glelnllals
      181 asiglggvgv afaakealeq lvgtielyld rpylpgeyir vnfnphnedv ygriesiglr
      241 stkirtvarn tvyvvpnaim ankeienitr gkkvmamlfl nfpqvlktse ealvkrivve
      301 sidnfggvdk sstrvrfsqt eekntrarvn ffimgsseds lrlrklliel anetistell
      361 ayglrftmpe pmvyidspmt i
//
LOCUS       WP_010478386             203 aa            linear   BCT 01-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010478386
VERSION     WP_010478386.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..203
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=22469
     Region          15..189
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mapfysnkti tislfladrw wmtalrglla ilfglaimiw pgislaillt lfgifslfsg
       61 cllllialqg rmvegnwmii legflgvglg lltlfrpett glfllllvav wailtgifqi
      121 gvalrlrrdi dnewlllsvg iasalfglll alrpvagata mlwlvgayai algillivla
      181 frlkrwrrqk lklqiersld qef
//
LOCUS       WP_010478427             181 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010478427
VERSION     WP_010478427.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..181
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20472
     Region          3..125
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,63..64,67)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(62,106..107,109..110,114)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(68,73..74,102,105..106,109..110,113,116)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91..93,102..103,106..107,110,114,117,121)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,107,110,114,117,121)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(115,121..122)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          137..178
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(138..140,172..173,175..177)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mavvgyarvs svgqsldvql eklkhcdkif kekrsgvsnk rprlkacley vregdtlvvt
       61 rldrlarstl hlcqlaeqld kkrvnlqvid qsidtgdatg rllfnmlgai sqfeteirae
      121 rqmdgiqnak argvrfgrkk qltqaqcsel rrkradgvli ktlmeeynls kasvyrylgq
      181 e
//
LOCUS       WP_010478392             331 aa            linear   BCT 01-JAN-2025
DEFINITION  sodium:calcium antiporter [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010478392
VERSION     WP_010478392.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..331
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35540
     Region          53..322
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mnlilwtlvl lasvwaahwg adqlanplqk lrkqwglnea agaalvalat aspeigtnta
       61 salqglsdig lgnllgsnii svpvivgvay iasqgktssf mknwsnrkvl qlksealsvq
      121 aipyvvicll aailllpepw qglqpidgwi mllvygiyvg qailrkrqkr qsvrwqrqel
      181 ivsilgvvvl aggayltvta tekiveilqi sqilgglfit stlsiapevf atwsvaksgq
      241 vtaattsvia dntvtmtlal fplamvslpi kdiqlfsvnl afviilgcfy agfvqwgtpn
      301 ysfslrevav liliygiyla vmlfgvfrvl g
//
LOCUS       WP_010478703             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Acaryochloris].
ACCESSION   WP_010478703
VERSION     WP_010478703.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris
  ORGANISM  Acaryochloris
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Acaryochloris"
                     /db_xref="taxon:155977"
     Protein         1..308
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=32983
     Region          6..304
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mdlvldlaql fingiavgsi ialaavgltl tygilrlpnf ahgdfmttga fltflfntqv
       61 lnhvvfgvdw ldslfaqanv wisiilativ tiggflicef liwakmrdrr atsttliiis
      121 iglalfirng iifiwgggnk sydlpvakaa eilgvvkipy yrliviglai lavvglhcll
      181 qytkigkamr avaddidlas vsgidvnrvv lwtwvlaggl talsggmygl itavrpnmgw
      241 flilpmfasv vlggignpyg aiagamvigi aqevstywlp teyklaiall amvlvllvrp
      301 qglfrgti
//
LOCUS       WP_010478893             324 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010478893
VERSION     WP_010478893.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..324
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36721
     Region          38..299
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 masrrsltlr kgkdteaale sfvlnddlln skgqpawsks piveikldki ilpefqlrly
       61 ydrekieqik atiqsvgire plllrpipgk gkyfeliags qrrlaaeelg hrmvpakvde
      121 vddlialkia iienearsdi npfertrgii qllstglqms ndevaqilts lfnaenrrsd
      181 nnviindeqk rfilsvfeem glnwksfvan klqlinlptd vvtflesgkv sytkairiar
      241 vkdedireel lkrvvaeelt vkqlqslitt vssktnssee iilrdrarav lkratspkll
      301 kdkkirkkve sltnqlesli sece
//
LOCUS       WP_010478916             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein
            [Acaryochloris].
ACCESSION   WP_010478916
VERSION     WP_010478916.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris
  ORGANISM  Acaryochloris
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Acaryochloris"
                     /db_xref="taxon:155977"
     Protein         1..161
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=18588
     Region          58..161
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msivlrdpfr sfermyplgw epfqeleswr remdrmfgrl mpisksdgek sltfmpsaem
       61 detdqeihlk felpgldakd ldievtkdav yirgerktei eaesegtvrs efhygkferv
      121 ipmpspiktd nvqaeynngv lsltlsksee dmkksvkvev s
//
LOCUS       WP_010478923             787 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010478923
VERSION     WP_010478923.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 787)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 787)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 787)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..787
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86539
     Region          132..396
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          543..786
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mvaldqkllr dlrhlrgqvi aialivacgi aclvtmlsay dslqlsqqty ydryqfadvf
       61 aqlkrapdsl ieriaelpgv qqvqtrvvvd vnldvpslpe patgrliaip eqqtpmlndl
      121 firqgqyiep grrdqvlvse vfaqanhlel gdtlgavine rwqqlrivgi alspeyvyei
      181 rgvelfpdnq rfgviwmgre algtafdmdg afndvalslm psanpasvif rldqllkpyg
      241 glgayeradq ishqfinsei eslaatavmv pfvflgiaaf llnlvlarlv stqrdqiavl
      301 kafgydnlav gwhylklvlv itllgaglgt ivgiglgavi tenyarfyhf pvlryraglq
      361 imvtaivvsg gaavlgtfta vkqavslppa eamrpeppas frrtiiermg mqkfippvgq
      421 iilrnlerrs lqaslsilgi aaavailvig ryfedatnym ieaqfrqvqr edvtlvfnep
      481 lssraryelt hlpgvmqaep fravparlrf qhqthlsglt glepqgelrr lldqdfypvp
      541 lpdqgvvltt klaeilgvtp gdpltvevle gerptrtvpv vgfvdeligl gaymdihaln
      601 rlmregptls gayltvdahn leqlytqlkq tpavasvalr ervitefekt iggsfaiftt
      661 vlvifssvia fgvvynvari alserdrela tlriigftqg eiavillgeq aivtvvaipf
      721 gfalgfglaa litraydwel frfplivtpa syafafviif laalgsggli rrqlnhldli
      781 avlktre
//
LOCUS       WP_010479079             192 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010479079
VERSION     WP_010479079.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..192
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22748
     Region          15..184
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 myevlfqrln qlvflnprqq qelrdvlqvi krpkddcfle vgqvsnhiyf vqagilrsfy
       61 tfegkevtqw fcfpnhfaas yfsfayrqps kdclssltev tllaisynsl qqlihqdkvw
      121 adlnrrlleh yytmslqria sfqvlstaer yeqllyehpt iesevplgyl asylgmtqet
      181 lsrirrrkkk rk
//
LOCUS       WP_010479102             444 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010479102
VERSION     WP_010479102.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..444
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=47854
     Region          158..436
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 masrkqlsag lidavllvgl ligsvaptla qesdvltppp tsttptsasq svyfadilvr
       61 grpvfqvgsl sdmdatnrae iinrriasll srsealgevs vqdinqqvat lrlnqrvlmt
      121 vtqqdsedyg qtvqslatdw anrlnqaldk pplaidvaqr lsttirdagr ntidmlpalv
      181 galivvvttw lvavgvryia frwaqqtegd rsteiligrl gyggvwviga vialgvlgld
      241 fgallgalgl tsvaigfslk dvlsnyisgv illaarpfrl gdqvviedfe gtitqvqlrg
      301 ttlrtydgri vyipnqevfs asitnntasp qrrssvmvgi dydadinqat qviqtavthl
      361 dlvepspppe vlvrelaast vnlevrfwvn sqrgefltmt skvaqtikea lqqaqvempt
      421 diytlvfrns pfpaseaqai pvqp
//
LOCUS       WP_010479143             295 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010479143
VERSION     WP_010479143.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..295
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=31905
     Region          19..295
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mkrlkwfllg glgllgllva wglvephvln leeetaiipn lpkawegqki gqlsdfqigm
       61 wadnpgtarr gvktlveiqp aavlisgdfi yhanpdpaae ieevvgivrp lveagiptya
      121 vlgnhdygms sktaeprikl asrlatelet agivvlenes iemqlpdsnd tlilaavnsl
      181 wanqadvdaa lkgiptnrpt valmhnpdtf effpansapl avaghthggq mripglpqws
      241 wlrfvqkdkv yadgwakgyg nlgnnlyvnt gigmsnipir ifcppevtif tlkss
//
LOCUS       WP_010479288             529 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010479288
VERSION     WP_010479288.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..529
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59114
     Region          249..525
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mpairrrlil alvsviltll lhipvwaqap spvanpstqq pliipnlsnp lvsdwiwldg
       61 rrlfkitatk gnlaeriqav qdsletskrk ylrsdsadpk vdirisnnlp viyvddqhlm
      121 titsldaelr gldvttlddq iksiletalr rarterqpqf lrqqgiltaa vigcavllnr
      181 lvhfwqrrlr rpakavaapk tdgslelppv qfwvgflgvl rqvlsilqis igiicllicl
      241 drfpytrpin iwllkslpip ltltgvglvt yllirlswal vnrfalaltv tpflspmasr
      301 rmllristia nvikgiavpi wislgiival illkvdvgpl lagvglvgva lslasqsiik
      361 dalngflviv edqfgvgdvi tvdrytgvve tlnlrmtqir naegqlitip nseirivanl
      421 ssewsrvdln ipipyhtdid qmldliqsta qamadepdwq kqileppqlm gvddfdhrgp
      481 vvkvwiktqp lqqwavsrel rrrlklafde anisipvpqq qlwlyrshp
//
LOCUS       WP_010479328             120 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010479328
VERSION     WP_010479328.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..120
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=13360
     Region          14..120
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 madtllllnh nacnqilltq fleghgyhtv gatsyegled alasphflrl alidisgfdp
       61 qiwthcrrlr qrqipfiils arrstglene sfahgahgvl ikplvqevll nllhsfleep
//
LOCUS       WP_010479812             140 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010479812
VERSION     WP_010479812.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..140
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16048
     Region          3..137
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mqrqtdriiq klkskglrvt pqrfavyadl larsdhptad qilshlnqdr ptssqatvyn
       61 slqalrevgl vqeilleegv cryeanieph hhfrcqscga iediaweqlq dldfkelrpg
      121 lqvnhyeitv hgycnrchsq
//
LOCUS       WP_010479865             191 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010479865
VERSION     WP_010479865.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..191
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21198
     Region          2..188
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mreltyfvac svdgyiahid gshdgfsqdp eyfadvfatf petvpshlrd algvhgknkw
       61 fdvvlmgrkt yeiglkegvt spyshlkqyl fsrsintspd envelvsnnt ielvtslksq
      121 sgkgiwlcgg gdlattlfah hlvdqlilki npflmvsgip lfsgviqqta leltdhkiye
      181 ngvlllyyrv k
//
LOCUS       WP_010479918             251 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010479918
VERSION     WP_010479918.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..251
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=27106
     Region          57..236
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mklnqchspl llkageesay pvsgsnavee vlsayargvr nfsgseiywe slyqaelqgi
       61 iftnsnltvd lceaklmdad fsncdlnhse fiwadlsqsn lsgsdltrvi fieadlrgan
      121 lkdaclknac lngahlgean leganlegik afyawfcegi yrgasfagat lqnvtfddsd
      181 crgvdfsgad ltgaefqntd lkganftnaq lkdacfdsad lvdadltgan vqdaklldvr
      241 mvrsepeyec i
//
LOCUS       WP_010480154             193 aa            linear   BCT 01-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010480154
VERSION     WP_010480154.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..193
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=20512
     Region          15..177
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 msnqdiqksq ptfgkwsial gallvvlgfv aiampfvstl atelviagvf fssgiiqliy
       61 ayqsranvks lafkillgag yigssvlllf yplqgvlslt lavgtfilve givqaimair
      121 mredesswyw tlgsgvfavv fglsimlgwp adsawilgll iglnlisdgw pmvvfgltdt
      181 dlfgsgpqqp qas
//
LOCUS       WP_010480069             255 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010480069
VERSION     WP_010480069.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..255
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28785
     Region          49..145
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mitankqvtq alyndtavrw vrgepsslsd ftarpailem capvteqkil dlgcgegycs
       61 rqlrqlgaas vlgvdlsqrm ieaaqaqeeq eslgityqvg catdvrhytq dkfdlvvavf
      121 lfnyltvaqt qacmaeifqv lepggrfifs iphpafpymr qaefpfyfev dgnnyfsgrd
      181 qqcpgriwkr dgswldvqli hktlqdffea lqmagftsmp tvrelrvlpe hveldpdffg
      241 plvdyplhma ievhk
//
LOCUS       WP_010480394             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010480394
VERSION     WP_010480394.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..231
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25360
     Region          2..173
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(56,60,112,130,133,137..139,173)
                     /site_type="active"
                     /db_xref="CDD:293810"
ORIGIN      
        1 mlfrqlfdpe tstytylian anleailvdp vqeqverdln llqelgltlr yclethihad
       61 hvtgtgqlrg qtgcqgivpe raaadcadrl irdgevldlg evnvraiatp ghtdshmayl
      121 inqdriltgd sllirgcgrt dfqsgdagtl ydhvvqrlfi lpdttlvypg hdykgqtvst
      181 igeekrfnpr fvgkdraafi qlmgtlnlpd pkkiaeavpa nqqfgqvatv s
//
LOCUS       WP_010480406             307 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010480406
VERSION     WP_010480406.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..307
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35027
     Region          26..258
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mtkrrnnfsk mrgieaflep ppeaakkekk vdllpinelq lplkqprryf dpskmrqlva
       61 sikehgviep llvrlldegq helvagerrf raateaglek vpvviqvlsd qealqlslve
      121 nlqredlnpv eetegildlf sieqsiskee viallnlsan akkrgqeltd nvvrqlesmq
      181 etltvlgqtt lesfrvhrlp llnlptdile klregaiayt kakaiarvkd krkrrrllke
      241 aiekqmslvq ikerikslcc dpkpdsprve fesltrkiak sklwenpkkw kraqtllaql
      301 dalased
//
LOCUS       WP_010480437             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Stenotrophomonas].
ACCESSION   WP_010480437
VERSION     WP_010480437.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24566
     Region          11..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnpaylpval dardervfda vrellaqqgm qmsmdavaqh agcskqtlys rygskqellr
       61 rvmqrhvgha tgamvralrt ddlrasllqf atdflehfnq phvgqacrli aadasqfpee
      121 artlyrhgag altlhlaewi etvcmrgqlr hddphfmael llsmiagqdf dkqrfhtphr
      181 ddaqlrrrwa efsvdsflra fapqpspaps snqprsss
//
LOCUS       WP_010480412             291 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Stenotrophomonas].
ACCESSION   WP_010480412
VERSION     WP_010480412.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..291
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32365
     Region          10..228
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnstasesvi targlrkayk ttvaldnasf sipsgrivgl igpngagktt alkallglts
       61 vegelsvlgr dprlhrdelm ndicfiadva vlprwlkvre aidfvagvhp rfdrarcerf
      121 lantklqpkq rvrelskgmi vqlhlalvma idarilvlde ptlgldilyr kefyqrlled
      181 yfdeqktiiv tthqveeieh ilsdvmfird grivldaemd dvgrrytell vnadqldtar
      241 alkpidersl afgktvmlfd gvprtqlstl getrspglad lfvaimkgty a
//
LOCUS       WP_010480510             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SGNH/GDSL hydrolase family protein
            [Stenotrophomonas].
ACCESSION   WP_010480510
VERSION     WP_010480510.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10139723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..262
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=27854
     Region          79..255
                     /region_name="SGNH_hydrolase_like_4"
                     /note="Members of the SGNH-hydrolase superfamily, a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site closely...; cd04501"
                     /db_xref="CDD:239945"
     Site            order(86,112,141,235,238)
                     /site_type="active"
                     /db_xref="CDD:239945"
     Site            order(86,235,238)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239945"
     Site            order(86,112,141)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:239945"
ORIGIN      
        1 mrgsvelaaa tvvtlglala splgaaeava vnpllqtpid qlrpdeirfm qqrladwpql
       61 qryrdanarl paavpgqprv vffgdsiteg wgregsagff pgkgwlnrgi sgqttaqmlv
      121 rfpqdvlalk pqvvvilagt ndiagntgps tqamiednlh ammelarahg iavvlasvlp
      181 vseypwmpgi tpapkvraln talkryaeak qlvyldyytp manaaggldp qlaedgvhpt
      241 akgyavmapl aeaavkralq qk
//
LOCUS       WP_010480565             195 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FMN-dependent NADH-azoreductase [Stenotrophomonas].
ACCESSION   WP_010480565
VERSION     WP_010480565.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..195
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20802
     Region          1..184
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mkllhldasv lgensvsrhl taavvarfkq qieglqidyr dldanpvphl rssslakada
       61 aeaadaeqvl eqflaadivv igapmynfsi pstlkawidr vavagrtfky tengpiglag
      121 gkrvivvssr ggiytdspad fqepflrqtf afwgindief vraegiaysp qhredaiaga
      181 laalpsheaa eaaaa
//
LOCUS       WP_010480643             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Stenotrophomonas].
ACCESSION   WP_010480643
VERSION     WP_010480643.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28827
     Region          9..264
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mgilsvfgkh rsltfelsqr evlgryrgas fgllwslisp flmllvytla fgfvmkgrwp
       61 gstgsttdfa lilfagltvh gffaecftra pqlivantgy vkrvvfpldi lvwsmtfsal
      121 fhllmnmvvl lllqlaikgs ipataillpv vviplvilta gvgwivsslg vylrdigqfa
      181 gvmaaamlfl ssaivpvesv pesyrivfel npltfiidqv revviwgrlp dwaglgvytl
      241 iacavallgh rmfnklrvgf advl
//
LOCUS       WP_010480615             145 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010480615
VERSION     WP_010480615.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..145
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15999
     Region          1..140
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mnilvaldls pssqeivkqv eelfnlphvk fwllhvadpe pefigyadgp qyirdavaqe
       61 fhaehkaiqa iatemrnaqi dctalliqgy cpdtilseaq rlkthlivmg shgknmmkql
      121 ilgstsqavi qdskipvlvi ptktn
//
LOCUS       WP_010480691             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MlaD family protein [Stenotrophomonas].
ACCESSION   WP_010480691
VERSION     WP_010480691.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..308
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32906
     Region          1..302
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 metkanyvli gaftlitgla llafglwaak yssdrtwqey rvvfreavtg lsvgspvqyn
       61 giavgsiiel nlvpddprqv varirlnstt pvktdtrakl aitsltgpsi iqlsggtpqs
      121 palttvnkdp apiipttpsa lqnitdvanr ivermdqils drnvasinat lanletisgg
      181 ladrdqgtqa lllsardaar sldttlkttn gtierldknl vqqlpgiidk ldatlaklds
      241 aagnadsilg enraainsfa ndglgqlgpt ltelrglird lrrvsdrlen nparyllgrd
      301 apkefepk
//
LOCUS       WP_010480723             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RDD family protein [Stenotrophomonas].
ACCESSION   WP_010480723
VERSION     WP_010480723.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..163
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18497
     Region          11..159
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 msrpaidtap aaatelprpr alllwralam vydalpvlal wmlagtlftl aytfsghaqr
       61 eniapfsawq wllwavcwai tgwyataswr rggqtlgmrp wrlklhasdg aplrrsqlwl
      121 rfavgtlsll lgglgfwwaw vdrerltwhd rasgtrlvrm pkr
//
LOCUS       WP_010480871             481 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Stenotrophomonas].
ACCESSION   WP_010480871
VERSION     WP_010480871.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 481)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..481
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51196
     Region          207..465
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mpvvlamlyv lchglvvafw pspagvgsfv fltgapllaa aaclvraqrd raalgwrata
       61 malllwaggm tfnmvdalga gradftprvs lllyvlygvp lvfilararr erlsislida
      121 amaallgvlf fvhtasfaar vevdahamsn mqrmfdiqnl ciagfavvrw lagdvperrr
      181 ffralalyal ayllvayyin hytsddafga fndllidvpf lliaclaldt apdtgttahp
      241 rlartvqaag piilpllllv vgtlvvdhar plavagfvva tlgfglrsvl lqadllerqa
      301 aldqlarqdg ltgvanrref darlmsewnr arrsgtelgl llvdidhfka fndqhghpag
      361 drclqavagv lkaiagrggd svaryggeef avivpgspls gvlalaerlr eavaalplpe
      421 gsvsisigvg ylhppalasa dqlladadag lyaakragrn qvilhahvld degsahgrmd
      481 c
//
LOCUS       WP_010480890             138 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Stenotrophomonas geniculata].
ACCESSION   WP_010480890
VERSION     WP_010480890.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..138
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14932
     Region          10..126
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mdtptatfiv nldvpdlaaa edfyirafgl rigrrlgpga vellggptpl yllhndagsa
       61 atedgdvrdy erhwtplhld wvvddidaal vravaagatl eqsvrerrwg riavladpfg
      121 hgfcliqfsa egydalve
//
LOCUS       WP_010480893             220 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Stenotrophomonas
            geniculata].
ACCESSION   WP_010480893
VERSION     WP_010480893.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23884
     Region          23..182
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgamnsttls esttptrrrg rparpeaevr hvvlqatlel llaqgyeatt ieavaahagv
       61 akktvyrhas nreelvglav rewtdgfapq lqrdahgade vlpllqdilq avctqalsaq
      121 avqvfrllat dfpgkdallq ayldngierg ralladwlar qqqrgllreg dpvrmarlll
      181 amavaeplre rvigvvaeda pvevhlrecl allapvlrgp
//
LOCUS       WP_010480903             134 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system VapC family toxin [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010480903
VERSION     WP_010480903.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..134
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /calculated_mol_wt=15306
     Region          4..132
                     /region_name="VapC"
                     /note="Ribonuclease/mRNA interferase VapC, contains PIN
                     domain [Defense mechanisms]; COG1487"
                     /db_xref="CDD:441096"
ORIGIN      
        1 mngilidscv lldlftddpn waewsesile rysltntlyi nsivyteism gfekieeles
       61 aievlhlkvl emprealflt gkvflqyrkn kgtktsplpd ffigahasvs efdlitrdvs
      121 kyktyfpqva liyp
//
LOCUS       WP_010480753             680 aa            linear   BCT 01-JAN-2025
DEFINITION  ribonuclease R family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010480753
VERSION     WP_010480753.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Domingues,S., Moreira,R.N., Andrade,J.M., Dos Santos,R.F.,
            Barria,C., Viegas,S.C. and Arraiano,C.M.
  TITLE     The role of RNase R in trans-translation and ribosomal quality
            control
  JOURNAL   Biochimie 114, 113-118 (2015)
   PUBMED   25542646
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..680
                     /product="ribonuclease R family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=76577
     Region          272..560
                     /region_name="RNB"
                     /note="RNB domain; pfam00773"
                     /db_xref="CDD:459934"
     Region          <568..>632
                     /region_name="GT29"
                     /note="glycosyltransferase family 29; cl45931"
                     /db_xref="CDD:480271"
ORIGIN      
        1 mekgtliefk rrgdcaegqr pfqlgvldrp egkknwvvvd qtgqthtlhp rqftfvvsgk
       61 tytpseiaef qleaesyidp sslevaweil ledsqsvapa dlaqllfsdq spplcyashc
      121 llsddriyfk qkgdrfeprs asqvaelqhq leqqakrqqe qqafyqkleq viagdtvewq
      181 gcdrtylqal ekfaalgdea ttrstatevl stlkrgtspd aafqllvdvk vwephqnlhl
      241 yrsktpvqfs ssvlaavdql lkmpppdlha erhdltslkv ytiddestse iddglslefl
      301 pggkqrvwvh iadpsrwitl gdeldqeaqr rgttvylptg mipmfptels tgpmslvqgq
      361 iccalsfgvi ltaegaiesy eircsqvqpt yrltyadvde mlelgveaes ellalahwak
      421 qrqawrksqg aisiqmpess ikvegekvdi qvlydssarn lvaemmiltg evaarygqdn
      481 dlplpfrhqp qpelppeeel lqlapgfvry cairscmprs evsisparha slgldcycqv
      541 tspirryadl vahfqikahl rdeelpfskt dlttlipsvt taayeatlle rqtnrywsle
      601 ylrqhgqtvw pamvlrwlre henlalille dlglelvmrl dhpvvlgdrl dvkvasvnpr
      661 ldriqlqecf taspdtaqeg
//
LOCUS       WP_010481003             192 aa            linear   BCT 01-JAN-2025
DEFINITION  Uma2 family endonuclease [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010481003
VERSION     WP_010481003.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..192
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21553
     Region          5..192
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mdtlivsvpp stqltdrqfy dlclanpdlk iertaqgeli fmpptggetg krnatltsrf
       61 viwnesanlg evfdsstcfk lpnganrspd vawvcqerwn alspeareqf ppispdfvle
      121 lmspsdtltv tqakmheyid ngvrlgwlin rqqsfvevyr phqpvsrlds pqtlseeevl
      181 pgftldlsai wr
//
LOCUS       WP_010481063             133 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010481063
VERSION     WP_010481063.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..133
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14866
     Region          1..>101
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mkylgschcg aiqfeveapk dlkvdecncs icskagflhl ivpqskfnll qgqdtlttyr
       61 fntgvaqhtf cricgikpfy iprsnpdgyd invrcldtqp dsmevvpfdg vnweqnahkv
      121 ahksqenqsl lqd
//
LOCUS       WP_010481253              83 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: UPF0175 family protein [Acaryochloris].
ACCESSION   WP_010481253
VERSION     WP_010481253.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris
  ORGANISM  Acaryochloris
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Acaryochloris"
                     /db_xref="taxon:155977"
     Protein         1..83
                     /product="UPF0175 family protein"
                     /calculated_mol_wt=9205
     Region          1..82
                     /region_name="COG2886"
                     /note="Predicted antitoxin, contains HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442132"
ORIGIN      
        1 mtqvtlnipd dlvvnqadng esfahrlqla aaiywyarge isqgkaaqla gmnrkeflkr
       61 lahenmdvfq vdfddlaqel arg
//
LOCUS       WP_010481285             510 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp70 family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010481285
VERSION     WP_010481285.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Fernandez-Fernandez,M.R. and Valpuesta,J.M.
  TITLE     Hsp70 chaperone: a master player in protein homeostasis
  JOURNAL   F1000Res 7 (2018)
   PUBMED   30338057
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Mayer,M.P. and Bukau,B.
  TITLE     Hsp70 chaperones: cellular functions and molecular mechanism
  JOURNAL   Cell Mol Life Sci 62 (6), 670-684 (2005)
   PUBMED   15770419
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Bukau,B. and Horwich,A.L.
  TITLE     The Hsp70 and Hsp60 chaperone machines
  JOURNAL   Cell 92 (3), 351-366 (1998)
   PUBMED   9476895
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Rensing,S.A. and Maier,U.G.
  TITLE     Phylogenetic analysis of the stress-70 protein family
  JOURNAL   J Mol Evol 39 (1), 80-86 (1994)
   PUBMED   7545947
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..510
                     /product="Hsp70 family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
                     /calculated_mol_wt=54734
     Region          4..482
                     /region_name="DnaK"
                     /note="Molecular chaperone DnaK (HSP70) [Posttranslational
                     modification, protein turnover, chaperones]; COG0443"
                     /db_xref="CDD:440212"
ORIGIN      
        1 mgkavgidlg ttnsvvaaid ngqpwaipde dgetllpscv gittkgklli grealrqyaa
       61 apertaksik rqmgtdhktv lgektyspqe isaillrtlk qraedalgea vtqavitvpa
      121 fftdaqrqat keageiagle vlqvlnepta aaltydfrse eteqvlvydl gggtfdvsiv
      181 eitgdvtevl ashgnnrlgg ddfdrrlqly lteqfrqshd tevpadptvq arllraaekv
      241 kidlsehafa tarepylvsq gktalhleve varesfedli qplieetlea idraltdakl
      301 dkqdldrvil vggstriplv qrmitahleq apidgiqpdl cvslgagiqa gvlsgasvda
      361 ilvdviphsl giaaamstaf gtmpgmfsti iarnsvipis rsevystlsn gqetveievf
      421 qgenavaren vplgsfrveg lpprpaggvq vevhfdfdhn giltvtatek gkgqqntliv
      481 ddagtsrlss heltqsraei eslfaqdeei
//
LOCUS       WP_010481320             389 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter permease [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010481320
VERSION     WP_010481320.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..389
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=42779
     Region          5..389
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mpklrlgpkw rqsrirngli qglvllligv avvyfganlv qnlqrlrlpf gfdflfsksg
       61 psigetliey sptdniaraf gvallntlrv vvlgivlatv vgigvgmarl sdnwlvrkla
      121 tfyvetlrnf plllqllfwy lavflklptf enriqlpgpi ilskngvafp wlkgnpatlp
      181 wilalaigsv cafllwryli rlqieqgrit faglwsllll vgigggaalf tqrfpfdvsl
      241 pyvdqrvvtg glqltsefsa lllgltlyta afiaeivrag irsvsigqse aaralglkpt
      301 lvmrfvvfpq alrvivpplt sqylnlakns slavavgypd iyyvasasle dtgrsveivl
      361 llmaiyltms llisilmnly nrsiqlver
//
LOCUS       WP_010481329             128 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GtrA family protein [Stenotrophomonas].
ACCESSION   WP_010481329
VERSION     WP_010481329.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..128
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13886
     Region          1..128
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 msllrqgsay liigvlqlll dwavfvlvta aglpvvqgnl agrvagmllg fwlngritfa
       61 tadgeqrlgw rrfarflplw lllttastll vssadhalgl qyawlakplv egglavisfl
      121 llrhvvyr
//
LOCUS       WP_010481337             432 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Stenotrophomonas].
ACCESSION   WP_010481337
VERSION     WP_010481337.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..432
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47458
     Region          4..>357
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mfayyarlav rsfrrnkvlt almvvaialg igasmttltv fhvlsgdpip gksdrlfyvq
       61 ldaatgayva geepetqltr fdgeallrea kgerqalmsg gggtiepdns tlkpfsidtr
      121 wtsadffpmf evpmqygrpw treddegrar vvviskalnd klyqgansvg rdlrmegqsy
      181 rivgvmkews pephfydltt gsygknedll lpistsfdlk lgnngnmncf genpdgnsys
      241 lnapcawlqy wvemdpakad dyrrylenys tqqreagrfk hppnvrlrtv mewldfngav
      301 psdvrlqlwl algflgvclv ntvglllakf lrrsgeigvr ralgasrgqi flqclveaga
      361 vgvvggvlgi glallglfav rqqpveyakl ahldgnmlll algltllasl aagflpawra
      421 mqvtpaiqlk sq
//
LOCUS       WP_010481378             142 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010481378
VERSION     WP_010481378.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..142
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15506
     Region          24..123
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mtpsnstpty tnlspqkwgq lphppllidv rsgaeyamfh aphavnfslh rlllgkipgl
       61 rrwawpawfr dlthdqpial icltahrspi aasqlskagf tqifnitggm mqwrqlglet
      121 vsgsqpipdt paqgcveegs ka
//
LOCUS       WP_010481446             162 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010481446
VERSION     WP_010481446.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..162
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17233
     Region          <25..162
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(41,43,47..48,51..53,55..56,60,63,72,78..79,82..84,
                     86..87,91,94,103,105,107,111..112,115..117,119..120,124,
                     127)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          41..70
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          71..103
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          105..133
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msdtddryet fqdfvrvgsl tqvsdylvrg eidinktiwp nsetpleiaa ekgrdkivpi
       61 llsagfspda gntdpplyca agegflgivq llieagadvn irssdgltpl msaaagghld
      121 vvrllvesga dvqfetedee talscaemnq hsqivsylng qg
//
LOCUS       WP_010481467             211 aa            linear   BCT 01-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010481467
VERSION     WP_010481467.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..211
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23144
     Region          6..34
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          <7..68
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          40..67
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtvqdtaiei lcevlltdts plircyaaqa lgeidqdnaa aitalgiaar qdpeaivrtm
       61 avlaisnlcr stqpqkkmpe nntpkvqmtf napvnypvgn vegdmvvnan sseqtqavsd
      121 maqllqdlyq qhphvsqagv tdllqteikq iqqdqpqrwq aiwrgllnpk rwrsggkaal
      181 ikagehftee slwgkaaiaf leqfseetds e
//
LOCUS       WP_010481471             365 aa            linear   BCT 01-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Acaryochloris sp. CCMEE
            5410].
ACCESSION   WP_010481471
VERSION     WP_010481471.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..365
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=40912
     Region          3..128
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          5..32
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(57..58,61,64,88..89,92,95..96,99,119..120,123,
                     126..127,130,156..157,160,163..164,188..189,192,195..196)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          71..99
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          101..131
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          141..164
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mlpatipilv hflddpegdi agraatilge iarelnstaa isalgaaith qsayvrnnii
       61 dalgssyskt aipfleaays dpewenrrrv mdamaqipse eviptiveaf qdyhvkvrya
      121 amealryisg tntgykvais hsnnvllhns dpvmrtiave alqhsgdksv lplleasltt
      181 ednpfirski knaidrfeel panirslppw drirwrikrt tgkhndktyq kslsldsqid
      241 ediliqklqt kghaarceai rllkecnnse fmystaikii rnhlfqvkds eeiyniveel
      301 qsiqkqcnfy hnnfyqlake fpleifstcw gisaininvk naygiaghvs gnqvihssls
      361 kedtv
//
LOCUS       WP_010481483             134 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF805 domain-containing protein [Stenotrophomonas geniculata].
ACCESSION   WP_010481483
VERSION     WP_010481483.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..134
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=14610
     Region          8..126
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mipallplrr cfdfsgrsnr kefwsyslsa alvvaasytl mdggywltgt vllvgeafep
       61 frmlgwgmtv cavivllppm lalavrrlhd idesgwyvvi afiplgvfvl fpvmllpgne
      121 eenrfggisg lpga
//
LOCUS       WP_010481490             135 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010481490
VERSION     WP_010481490.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..135
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14216
     Region          26..135
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtttstnsnl smqafsllll rlvvvaifly hgfpkainwa masekfigfg lpgflgpitg
       61 iveviasili ligfqnfwan wvlvaimaga iatvqfpkai segafiagle rdlmilaact
      121 vsaafgpgal alkkr
//
LOCUS       WP_010481564             428 aa            linear   BCT 01-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Stenotrophomonas geniculata].
ACCESSION   WP_010481564
VERSION     WP_010481564.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..428
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=45053
     Region          1..428
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 msdpqwqlet lavhggyrpd pttravavpi yqtvayafdd tqhgadlfdl kvpgniytri
       61 mnpttdvleq rlaaleggig alalasgqaa ityaiqtiae agdnivassa lyggslnlla
      121 htlpqygiqa rfadpadpaa fadlidertk avfvesignp rgnvtdiaai aevahaagvp
      181 livdntvatp fllrpfehga divvhsltky lgghgtslgg aiidsgrfdw aaqpkrfarl
      241 nqpdpsyhgv vytealgpaa yigrarvvpl rntgaalspf naflilqgie tlalrmerin
      301 analavaqyl kahakvawvr yagladdpeh aaaqrylggh gsgvltfglp ggreagarfl
      361 dalklftrlv nlgdakslat hpastthrql daaelakagv sedtvrlsig iehigdlrad
      421 leqalaga
//
LOCUS       WP_010481596             160 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010481596
VERSION     WP_010481596.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..160
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17293
     Region          <44..>147
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          44..69
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(45..46,49..50,52,76,79..80,83..84,86..87,110,
                     113..114,117..118,121)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          74..104
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          109..135
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnrkrvhayl taaiaaflfi sqgmalvshs plataspnpl tnphfaaats lleqkdfega
       61 mrelnqaiql dpslataysf rgilhldakn yqeatddfaq vtrlqpksae ayvnlaqsql
      121 ilkdyqaalq satkatqldp qnqaasllvk mipnlakpsq
//
LOCUS       WP_010481883             168 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Stenotrophomonas].
ACCESSION   WP_010481883
VERSION     WP_010481883.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..168
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18405
     Region          4..149
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mstelkthql smtvlmspem anfsgkvhgg ailrlldqva yacasryags yvvtlsvdqv
       61 mfrqpiavge lvtflasvnh tgtssmeigi kvvaedilkr svrhanscff tmvavdeegr
      121 ptpvpplqpa tsdekrrqaa aqirrqlrqe meqrhlella snppspee
//
LOCUS       WP_010481875             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Stenotrophomonas].
ACCESSION   WP_010481875
VERSION     WP_010481875.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32541
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..295
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(105,109,148,164,166,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(106..107,111..112,114..115,118,122,124..130,193,
                     224..228,235..236,239)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mlpterlrgi eafvatadag sftaaaerlh ltssavgkti arlearlgar lferstrrlr
       61 lteagegfyr tcvrvlgela daesvlvsha dapvgrlrvd apatfgrlkv wplllqlaae
      121 fpqlhpqvtf sdrfsdlaed gvdlavrigg peplpatlgs rqlgyeclrf caspayllrh
      181 gqprsaaela ghdgvlfgra dgsigpwqva dggqrstplq ararlvvgsa eaqvaaveag
      241 fgiaqlatwl vddalargsl vsilpsldcr glplrllwpq grqrlprvdv aldrlgaglq
      301 idppr
//
LOCUS       WP_010481961             846 aa            linear   BCT 01-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Stenotrophomonas
            geniculata].
ACCESSION   WP_010481961
VERSION     WP_010481961.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 846)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..846
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=90154
     Region          35..824
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mqkrafpcrn hcrlisrplr vaiavamama vashahavdg eplqfsagfl iggkaidmqr
       61 yaqgnpmepg dypldvvvng qflenrdirf veapapvgat pclpmallgr lnlkdsylad
      121 lqedaegcia lpalvegatv efdagnlqll vsvpqaaqar nargyvaphq rdhgvtaaff
      181 dynvnhnraq gqdatylgln tglnlgawrl rhrssfsqss hgtrhdviss ylqrdlpawn
      241 sqlllgqgnt ggelfeslsf tgarvasder mlpdslrgfa pvvqgiaegn alvtirqngn
      301 iihevsvapg pfsiedlypt nfggdlevtv teadgrtqrf tvnfsavpqa lrpgasrfsa
      361 tagelrdarg erealrfaeg tyargisnhf ttlggvqiae dfqaalfgga vntpvgafga
      421 dvthsrarlg ngeqvtgnsf rvnyqryvaa tgtnfglaah rystrgymtl ndfalsrsdd
      481 wghagrarqr fqvnfsqrlg ersslslsgg hvrywgdspq qndlqlrfqs slgratysls
      541 amryrlgdgr qdtrytasls iplgtaprap rlstqlahsa rgeqgqlgls gtlgesqqls
      601 ysvgasdgtg gqrstsayat yngghgtlta gysrsgdysa vnasaagsvv lhrdginfga
      661 pvgdgfaliq adgaqgarig ygdevrigrn gyallphvsp yrwnqieldp sglpmdvell
      721 qtsqrvapta gsivrvafna krertlfida tdalgqplpf aarvedesgr aygavgqggv
      781 iqlrgapeqg glivdpegpn rcrlqyttpd apdayglsws qavctplppp spglqaalda
      841 asestp
//
LOCUS       WP_010481704             141 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator [Stenotrophomonas].
ACCESSION   WP_010481704
VERSION     WP_010481704.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..141
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=15168
     Region          10..128
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mllskrfvep rvlliedaee tqelsrlale sqacqvtavs saeaalglln agepfdllft
       61 dvclggisgi etanrvrehl pqlpilvtsg mdqhrvlpql ragihflpkp ysmselldai
      121 rlcfrhaada almpppqasa a
//
LOCUS       WP_010481785             359 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P) transhydrogenase subunit alpha
            [Stenotrophomonas].
ACCESSION   WP_010481785
VERSION     WP_010481785.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Bhakta,T., Whitehead,S.J., Snaith,J.S., Dafforn,T.R., Wilkie,J.,
            Rajesh,S., White,S.A. and Jackson,J.B.
  TITLE     Structures of the dI2dIII1 complex of proton-translocating
            transhydrogenase with bound, inactive analogues of NADH and NADPH
            reveal active site geometries
  JOURNAL   Biochemistry 46 (11), 3304-3318 (2007)
   PUBMED   17323922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..359
                     /product="NAD(P) transhydrogenase subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37273
     Region          9..355
                     /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 mavallgike tapgerrval tpetarklga lgitvwyeag aglaagftda ayddagarvf
       61 dagrwgeidi llcvqappal vleqlkpaas vvgllapasd palaalaagd rlqlfplqql
      121 prttraqamd vlssqagmag ykaaliaaer aprffpmltt aagtvrpakv lvigagvagl
      181 qaiatarrlg aqvegfdvrp etreqiqslg arfldlgvsa ageggyaral tdeeraeqqr
      241 rladhlrgvd vvictaavpg rpaptivtaa mvegmatgsv ivdlaaesgg ncaltqpgqc
      301 iehrgvtidg plglasrgat qasemyarnl lnfvalfvre gqlgfdwdde llaktrwqa
//
LOCUS       WP_010481105             507 aa            linear   BCT 01-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Stenotrophomonas geniculata].
ACCESSION   WP_010481105
VERSION     WP_010481105.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..507
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55109
     Region          42..504
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mdrrrflrtl lsssaclalg atalrsapaf agdparfaqg mqehpwllgw rsvgseslgp
       61 atvqlqgklp sglagtlyrn gpawterdgf rydhwfdgdg mvhgwrfngd gslthhgrmv
      121 atpkftreqk agrfqypaag tsvpgalavr nnddanvant svtmingrlf alcesgsafe
      181 vdpdslqtlg pvtwrpdlaa lpfsahpltd rdgslwnfgs islmgghgll vwhigadgql
      241 rsanvietpe hgylhafamt dqhlvfvmmp fdftgaggsf fermqfapqr pvriavvakd
      301 apdkaqwfea pfaaiyhfgd aftrdggivl ravrhddine arspmkeama gdgahaansg
      361 aslvelhldl rrgqarwetl gisavefplf dprstntrga rlyaptidgp atapyfnava
      421 afdidrgrrq rwnygqdima eehvfvprpg sreaddgwli gtlldpvnkr sglavldarh
      481 vddgplaqaw lpyavplgfh gtfaahg
//
LOCUS       WP_010481962             172 aa            linear   BCT 01-JAN-2025
DEFINITION  fimbrial protein [Stenotrophomonas geniculata].
ACCESSION   WP_010481962
VERSION     WP_010481962.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..172
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=17150
     Region          1..172
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 msntlnmlva galalavspa afaekleitg elmtstcavd avggtitvpm gkvdvasvna
       61 seragmknfs iqldctgsga tqdvgvrfgg tpdgstgnla lnpdpsaasn vgvalydaag
      121 nhqklgedpl qwvtipaagk gqldysawya spgqnatagv anasgdfvvl yk
//
LOCUS       WP_010482000             854 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fimbria/pilus outer membrane usher protein
            [Stenotrophomonas].
ACCESSION   WP_010482000
VERSION     WP_010482000.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 854)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 854)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..854
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=92101
     Region          31..854
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 msihqalcll vagvacpgwa laapanlgeq almaqsgaan arapesaqfn ssflsgqakq
       61 vdlaafsngn pmvagnyrvd vyvngawqgr rdlqfkadaq grvdaclplp mleemgvdse
      121 avllqqdpsv ptdktscvpv qqrmanaygv ydsgnlrydl sipqvflrre argyvnpalw
      181 drginagfvg ysfnaidsds rveggqrnrs aylglnagmn lggwqfrhds nltwsegdgr
      241 hwqsiatyaq rgipqvrgml tigeayttge lfdsigyrga slasddrmlp dslrgyapvv
      301 rgiaetnari evrqneqliy sstvspgsfv iddlyptgyg gdlevsviea dgrrrefkvp
      361 fgsvpqmlre gvsrysltag qvrnkllade pwlvqgtyqr gignqltlyg gsalsdgyls
      421 llygvglstp vgafaadvth arttfdhygn htgasvrlsy snmigetgtn ltlaayryst
      481 egfyslqdal ygrdsdkrgi dpttrgrqrs qfqvtlnqpl grrggalyvt gsvrdfydrs
      541 gtskqyqvgy nnawrsvnyg fsalrteegv lgrsdtqyll smsvplgrgt hpvsfsadlg
      601 vrdrggydns rvgitgsagv dnnfsygaal sdsregstta ignveyrsry salnasyshs
      661 rdfrqasvga ngsvvvhpgg ftftpqrgdt mvlveapgar daivsnapgl rvdgrgyavv
      721 pyvspyrlnt vtldpqgmah dvelestsqs iapfagaisy lrfdtrkgna lliqvrnpdg
      781 rtmpfgaqvk deqgqpvgmv sqggrlyvrs eknqgrllve wgagadqrct vdyqvpagad
      841 asktgfiple aacr
//
LOCUS       WP_010482008             198 aa            linear   BCT 01-JAN-2025
DEFINITION  PAS domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010482008
VERSION     WP_010482008.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12091914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..198
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=23241
     Site            order(48,53,59,74..77,104,109)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Region          49..135
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(71,75,83,86..87,116,118)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          <122..>196
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
ORIGIN      
        1 mklaedshyl rielyeliqn dpsvfdflqg atldgvwywd lvnpehewms pefwlflgys
       61 ptqkkhltse wqdlihpddl vvvsknlekh lanpahpydq ivrytkkngk ivwvrcrgia
      121 irdqfdqpvr mlgahvdvtk lmevtellei qlqrldackm rlsleqqkvs qlaheksqle
      181 gqlqqkekei qvlkqrvl
//
LOCUS       WP_010482050             128 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010482050
VERSION     WP_010482050.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..128
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=13945
     Region          7..128
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 misvqvasnh srygqdisir hlhlaadepp slggddvgpt ptelilaglg sckaitlqmy
       61 aerkgwqles vgvelsydsd dqpptiqakl slegdldeqq rqrlrdisdr cpvhkllttp
      121 isiqtqlt
//
LOCUS       WP_010482194             176 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: gamma carbonic anhydrase family protein
            [Stenotrophomonas].
ACCESSION   WP_010482194
VERSION     WP_010482194.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..176
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18815
     Region          3..175
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mnplrpfrdk mpvlgervyi dpactvigdv eladdvsvwp gtvirgdvny vrigartnvq
       61 dgtiihvshh spynkagypt ligegvtvgh gciihactig dysligmgac ildgarverh
      121 gfvgagavvg pgkvvgegel wvgnparpar tlsdkeiesl hysadhyvrl kdeyrg
//
LOCUS       WP_010482249             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Stenotrophomonas].
ACCESSION   WP_010482249
VERSION     WP_010482249.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..322
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35628
     Region          18..240
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mgakasslas qndmapalrv rdlrktydng tqalkgvsle vapgdffall gpngagkstl
       61 igiisslvnl segqvevfgs dlvrnrsatm rliglvpqei nfnlfekpfd ilvnyagfyg
      121 vpreeaeqra eeelkrahlw ekaqvmsrtl sggmkrrlmi arammtrprl lildeptagv
      181 dieirrdmwr vlkeinaagt tiiltthyle eaeylcrhla iinhgqiveq gpmrallakl
      241 dvegflldid gelpaqlpvi egatltapdp htldidmpra mdlnrvfatl nesgirvrsm
      301 rtksnrleel fvrltgnlek pa
//
LOCUS       WP_010482267             285 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Stenotrophomonas].
ACCESSION   WP_010482267
VERSION     WP_010482267.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..285
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30579
     Region          30..285
                     /region_name="COG4798"
                     /note="Predicted methyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443826"
ORIGIN      
        1 mmpasslrgc rlllasalla avpafaapat vapakievsp aidaavkapt rdannvkrdg
       61 frhpaqtlsf frvapektvi eitpgngwys eilapllhdk ghyvaavvdp mavpegrgrd
      121 yqqrsrdsle kkyagapaqf gktavvaydp akpvfgpans advvltfrnv hnwrkagqaq
      181 gmfqgffnvl kpggvlgvve hrakadvadd ddtgyvgqqq viamaeaagf kldarsevna
      241 nprdtkdhpn gvwtlpptnq hdkaddakyq aigesdrmtl rfikp
//
LOCUS       WP_010482273             301 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Stenotrophomonas geniculata].
ACCESSION   WP_010482273
VERSION     WP_010482273.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..301
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31277
     Region          4..293
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnpdvlivgg syagiaagli lararrpvtv idagsprnrf aghshgvlgl dgisgaellk
       61 tarqqlldyp tvrwvhaeav qataraegve vrtadgqvla arklllasgi adqlpalpgl
      121 aerwgstvlh cpychgyevg ggaigllggh pmsaskaplf adwgnvtffs qglpiteeer
      181 aamqqrgvqi etapvvgvqg dqptwlevel adgrriaqra lfvpatqtma tplvqqlgct
      241 lvesplgvli evdamkqtsl pnvyaagdat tvgnitlaaa egvragigvh halvtedsva
      301 r
//
LOCUS       WP_010482335             217 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Stenotrophomonas geniculata].
ACCESSION   WP_010482335
VERSION     WP_010482335.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..217
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23816
     Region          33..213
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msllgealsa lrghrrhdaa ataapaapld adqalvraii dgsqaafsql vethqrtcah
       61 vigrmvgdrd qvadllqetf lavfrqlhrf rfesslrtwv srvayttalq hlrrrrleaq
      121 wmvavevpee lgigdegpgp aelsealqag rhlgaalerl sapqrlivgl hyledfdlae
      181 ieqvtglarg tikshlhrar qvlkqeltrh aaagell
//
LOCUS       WP_010482338             789 aa            linear   BCT 01-JAN-2025
DEFINITION  S9 family peptidase [Stenotrophomonas geniculata].
ACCESSION   WP_010482338
VERSION     WP_010482338.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..789
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=88582
     Region          352..516
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          538..789
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msrvlplsll lsavlaapaa haaptpitie qamadpdwig ppvekawwsw nsqqveyqlk
       61 rngspvrdtf rqplaggvaa qvaddqrgtl dvaepvydrs rsrsafvrng dvfvrdlrsg
      121 altqltrsne ragnvnfaad ngviwrvgqn wfhwtaasgv qqvaslkaek dprtapkadv
      181 lrdqqlrtle tlrrdrdqre alkdqdqrwr qadptrapgp vylgadveia dsvlspdlth
      241 livvtkpkdf ddgrggkmpl yvtesgyeet edtrtrvgrn gfephtlwyv dvrtgkaekv
      301 slaglpgist dplaelrrka gkdalkgers lqvmsdfmgg girwsadgqq aavmlrandn
      361 kdrwiisvna adgrvqnrhr ltdnawinwg fndfgwmadg rtlwllsees gfshlytqag
      421 takpqaltsg kwetsapvps adgkgfyflc nqqaphdyev cavdtgsrqv reltslngve
      481 dfslspdgqq llvrysgayl ppqlavlpsa ggqtrvltdt rtadykarqw iqpklvavps
      541 khgagvvwak yyepenkepg kkypivmfvh gagylqnvhq rypayfreqm fhnllvqkgy
      601 ivldmdyrgs egygrdwrta iyrnmghpel edykdgldwl vdtqqgdrdh agiyggsygg
      661 fmtfmalfrs pgtfkagaal rpvvdwhqyn hgytsnilnt pdidpeayrv sspieyaqnl
      721 qdnlliahgm mddnvffqds vnltqrliel hkdnwsiapy plerhgytra dswldqykri
      781 lklfeqnlk
//
LOCUS       WP_010482428             296 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010482428
VERSION     WP_010482428.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..296
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=33927
     Region          6..290
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msskvlatva teflnrpgya astlksyelt llpllqqygs lplelltrev ledylnslqq
       61 lsytthrrhq ailqsllnfa lerghiksnp iahlkqrkpd vqqgesgtde lvryltpqql
      121 qrlyqrvkpd rrmhalvrll hrtgariael laldlanvdl qdckfqvvgk gnkrrwcfys
      181 ddaaqvlaey iqyyrhpssp alftaqqpks glitrvsytt iykswkklte qdpvleglrl
      241 hdlrhtfate rvglmgieel ralmghqhlq ttlryqkvts sraekvakqa lqklin
//
LOCUS       WP_010482528             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-dependent oxidoreductase [Stenotrophomonas].
ACCESSION   WP_010482528
VERSION     WP_010482528.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..193
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=21863
     Region          5..193
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 msrsvlillg hpdrhslcga laqryataae naghrvrlia lgdlefdpvl rhgyrqiqpl
       61 eadlqdaaea ieacdhlvlv yptwwgampa llkgffdrvl lpgyafryrr dsvwwdrlla
      121 grsarvittl dtppwyyrwi yrdpgisqir atilqfcgir pvrvsrvgav rssspeqrnr
      181 wlalaaelgs rar
//
LOCUS       WP_010482551             462 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Stenotrophomonas geniculata].
ACCESSION   WP_010482551
VERSION     WP_010482551.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..462
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49527
     Region          1..461
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mtdsriaslq qacpglklkt dpadlehygr dwtrrwtpap laialpatve evqalmrwsa
       61 gegvavvpsg grtglsggav aangelvlsl ermnkalayd pvdrtlvvqa gmpleavnna
      121 aldhgliypv dfaargscti ggniatnagg irvirygntr ewiaglkvvt asgellelnk
      181 gliknssgyd frqlligseg tlgviveatv kltdpppasn vmllalpsfe vlmqvfaafr
      241 arlqlqafef ftdralehvl ahgaqapfde vhpyyvvtef aagddaqeaa amaafedcmg
      301 ngwvsdgvis asdaqaaqlw rlregitesl arykpykndv svrissmpaf laetqaligq
      361 ayphfdvvwf ghigdgnlhi nvlkpddtsd aeflaqcehv tkllaqvlar fdgsisaehg
      421 iglvkkgyld strgpaeial mkavkrafdp qarlnpgklf dv
//
LOCUS       WP_010482578             243 aa            linear   BCT 01-JAN-2025
DEFINITION  copper homeostasis protein CutC [Stenotrophomonas geniculata].
ACCESSION   WP_010482578
VERSION     WP_010482578.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..243
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25029
     Region          26..243
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mstrltleia snslasalaa qaggadriel fdnlaeggtt psfatiaiar erlsiplfvl
       61 vrprpgdfhy daletelmlr diaqcralgc dgvvigaldv qggvdvalcr elmqaagplq
      121 vtfhrafdaa rdlpvaleqv iglgcqrvlt sggqvsaeag advlaalvtq aagritvmag
      181 aglapgniat varqtgctel hasakglrrs amqfqnpalr gldpdwsqta tatvaalrqa
      241 ldg
//
LOCUS       WP_010482595             250 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Stenotrophomonas].
ACCESSION   WP_010482595
VERSION     WP_010482595.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..250
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26897
     Region          35..245
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msrpsgappa tndpaspsct tldclhcsvr hlavcsalsp devqaleqvt vsqqvsmgst
       61 lartgeerdh vytltagalr lvrtladgrr qingfvlpgd ylglsgsdhh rydieaiads
      121 rvcrvalpqm kalrsrfphl erkllqracq eldaaqdaal alarlqpaek ladfllrlaa
      181 reaklggdgl rvslpmgrgd iadhlgltme tvsrtftklr qqglialphl nvveildedg
      241 lrtlagegli
//
LOCUS       WP_010482623             154 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Stenotrophomonas geniculata].
ACCESSION   WP_010482623
VERSION     WP_010482623.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..154
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16631
     Region          41..152
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mepnlrpvqp snyatvaswp esagatqrwa gpgvpfplpp erfaqvlele vrpgwallde
       61 qgvcvgfgqy wmtgagtahl griivsplar grglgrllvq slsaqalres giqrltlrvy
      121 ldntaavaly rdlgfqqvea sstpellfmq rtsg
//
LOCUS       WP_010482789             216 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Stenotrophomonas geniculata].
ACCESSION   WP_010482789
VERSION     WP_010482789.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..216
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22802
     Region          1..204
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrfsqlivlg vllgvglgww lrrdagefva astpaaqpsv attpsmqaaa prataptgid
       61 aasgtlllpv qgvlpsqlrd tftdarsegr vhdaidimad agspvlavad gtveklfdsk
      121 rggltiyqfe psgrwcyyya hlqryadgls ekqvikrgdv igyvgstgna saeaphlhfe
      181 vhvlgpekqw wkgesinpyp llksaastpg aasaar
//
LOCUS       WP_010482867             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [Stenotrophomonas].
ACCESSION   WP_010482867
VERSION     WP_010482867.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..197
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22038
     Region          40..>184
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mmlslkdhlp awthpwlnya gvavqivlvl lvawllrvla rrlirrfaeh ytlppemvmg
       61 arritsfvvy fsallyilsl lgakpsvlwt aftgfaavga vaffaawsvl snifctllif
      121 ttrpfrlhdy ievlengekp glkgrvidvn liyttlqetg dghegtvlql pnnlffqrtv
      181 rrwrdpaqap ggiqgdg
//
LOCUS       WP_010482532             621 aa            linear   BCT 01-JAN-2025
DEFINITION  ferrous iron transporter B [Stenotrophomonas geniculata].
ACCESSION   WP_010482532
VERSION     WP_010482532.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Marlovits,T.C., Haase,W., Herrmann,C., Aller,S.G. and Unger,V.M.
  TITLE     The membrane protein FeoB contains an intramolecular G protein
            essential for Fe(II) uptake in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 99 (25), 16243-16248 (2002)
   PUBMED   12446835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     gene            1..621
                     /gene="feoB"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0015093 - ferrous iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
     Protein         1..621
                     /product="ferrous iron transporter B"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0015093 - ferrous iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66720
     Region          7..619
                     /region_name="FeoB"
                     /note="Fe2+ transporter FeoB [Inorganic ion transport and
                     metabolism]; COG0370"
                     /db_xref="CDD:440139"
ORIGIN      
        1 mtvtattapl rvalvgnpns gktalfnqlt gsrqkvanyt gvtverkegr lrapsgrefa
       61 vldlpgaysl hpasldeait rdlcrgfypg eaapdvllcv idatnlrlhl rfalelrelg
      121 kpmvvalnmv daaqrrgiqv dvaalerelg vpvvetvavr kqgakalver ldamvphlda
      181 pvpgpeggid yhakvreils vavrmparta kiddaldrwl lhpvfglvsl avvmflifqa
      241 vyawatplmd gieagfawlg efvgsvlpeg plaslltdgi iagvggvvvf lpqililfff
      301 ilvleesgyl praaflldrm maaaglsgrs fipllssfac avpgimstrs iqdprdrlat
      361 ilvaplmtcs arlpvyalli gafipqktvw gvfnqqglvl fglyaagils alamswimkk
      421 wrrdksehpl mlelpsyrlp hardlavgly ergmiflkrv ggiilaltil lwvllsfpaa
      481 pagatmpaid ysyagqigha mavffaplgf nwqicialip glaarevavs slatvyalsa
      541 adddaasqal tplisdgwsl atalsllvwy iyapmcistl atikretnsw kqmgfaafyl
      601 faaayvaali tyqvtkalgg g
//
LOCUS       WP_010482872             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Stenotrophomonas].
ACCESSION   WP_010482872
VERSION     WP_010482872.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..192
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20919
     Region          17..190
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mldttmpalp aandavdepa lvraaaagdt aayellyrrh aprvfavlwr lcggqqarae
       61 dalqeaflqa wkalpgfrfe sslstwlhrl gvnaalmelr graggqdhds ldevdgglqe
      121 lavhdrcagt erdleralst lppraravlv lhdiegwkhq eiaeqlqmav gsskaqlhra
      181 rgllrarlgd mt
//
LOCUS       WP_010483075             285 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide deacetylase family protein
            [Stenotrophomonas].
ACCESSION   WP_010483075
VERSION     WP_010483075.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181070
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..285
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32184
     Region          26..261
                     /region_name="CE4_Ecf1_like_5s"
                     /note="Putative catalytic NodB homology domain of a
                     hypothetical protein Ecf1 from Escherichia coli and
                     similar proteins; cd10969"
                     /db_xref="CDD:213026"
     Site            order(68..69,157,161,204..206)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213026"
ORIGIN      
        1 madartvpvl mhhhvspspg mitvspenfe sqiawlagng wtsltldqya gflagkpvpr
       61 rsivitfddg yldnwvyahp ilqkygmhav vfvvtgwmge gperphagia gatlpptpdh
      121 rgceaaiyeq drsddvmmrw searaaiaag tfevhchtht htrwlrrddl draqrragls
      181 rdlaisrevl qdklgdvsdt lcwpygdfdq dhievareqg frylhtthpf grnviggdpe
      241 riyrfairnr panwlrkrir lsynpliapl fngfkarqkk mvpgp
//
LOCUS       WP_010483111             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MOSC domain-containing protein [Pseudomonas sp. S9].
ACCESSION   WP_010483111
VERSION     WP_010483111.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..268
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29630
     Region          1..268
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mlhlsglyry plksgaaepl qgtqldslgv qgdrrwmvvd aqsgrfitqr llgtmnrita
       61 rwqnaeqlll sapgmpdlpv avpqgdgdlr gvhiwrdslr vpdagdaaaq wlsqflqrdc
      121 rlvyvapera rqidpvyaei gqkvafpdgf pllligqasl edlsrrvgrd lemlrfrpnl
      181 vvqgsepyge dswkriaigg iefkvakgcs rcimttldpv tgersadrep lttlktyrqi
      241 egdvffgqnl ialssgqlel gmpvevle
//
LOCUS       WP_010483124             163 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Stenotrophomonas geniculata].
ACCESSION   WP_010483124
VERSION     WP_010483124.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..163
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17619
     Region          23..161
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
ORIGIN      
        1 mpaktatact aphhhvhdas dfvavvervs rerglrltpi ranvlkliae agkpvkayel
       61 lewvrngkgv gadapptvyr aldflmangf vhklesvnaf vachhpssaa hsvpflicns
      121 chnaveledr eivtqlekra kelgfqpqaq tlevhglcar cag
//
LOCUS       WP_010483241             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HD domain-containing protein [Pseudomonas].
ACCESSION   WP_010483241
VERSION     WP_010483241.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..190
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21979
     Region          31..184
                     /region_name="COG4341"
                     /note="Predicted HD phosphohydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443482"
ORIGIN      
        1 mnmharfthm engtqddwai iakdfrafad qlpdrilthl klldgdfggf pvdrlthslq
       61 tatrahkdgr deeyvvcall hdigdtlgsy nhadiaaaml kpfvsaenhw mvekhaifqg
      121 yyffhhlgmd rhlreqfkdh pqyqatidfc akydasafdp eyeslpleff epmlrrvfaq
      181 pknsiyrdak
//
LOCUS       WP_010483340             405 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Stenotrophomonas geniculata].
ACCESSION   WP_010483340
VERSION     WP_010483340.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..405
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=42810
     Region          16..186
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mttfaasidq tlerelpaaa sgcqhaygri vlacqntvta ialaitrdrq asediaqeaf
       61 vkgwqqlhql rsatsflpwl rqitrnlard wlraqrgrpl tgeaaevamg maadpspgaa
      121 drlqrveeei aaediisalp adsrevllly yregqrsqqv adllglsdaa vrkrlsrara
      181 lvrdgllqrf gefarssaps aafatavvsm vlvaapgtas aaillstgvg vggsklglgg
      241 vsaaggaamg sltaaasqlh lipasnwaav aggvvggiig sylggrfllr fadtpqeraa
      301 vrrfvhlntf tamvvctsll vslmlqvplw lqlailvigl gtvnyqclvp lqrvmapmia
      361 rdsarrgrsg tnwqyesvyg rtgiiganvf vialvvyalm rsgnv
//
LOCUS       WP_010483345             404 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein
            [Stenotrophomonas geniculata].
ACCESSION   WP_010483345
VERSION     WP_010483345.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10505910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..404
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44043
     Region          41..297
                     /region_name="Exo_endo_phos"
                     /note="Endonuclease/Exonuclease/phosphatase family;
                     pfam03372"
                     /db_xref="CDD:460902"
ORIGIN      
        1 mnmtrrhpli lalallcgat apafatspam tekpstalrl atyntslysd dagglikele
       61 gdseharkia avlqqvrpdl vllnefdfdd ahraadlfqk rylevaqpgg gkplhfayry
      121 lapvntgvps gldldnngvv ggegrsrgnd awgyglhpgq ygmlvlsryp idgakvrsfq
      181 llkwsampga irpvdprtgq sfyndqvwsq lrlsskshwd vpvktpagvv halvshptpp
      241 vfdgpekrna arnhdelrlw qeylskgdkp wlcddkgqcg glaqdarfvi lgdlnndpvd
      301 gdgrheaive lienarvlry ptprsvggeq tslayaakgi erkgapfhat gdfgpksgtm
      361 rldyvlpstg feyigsgifw panespeaki adgsdhhlvw vdvr
//
LOCUS       WP_010483369             400 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Stenotrophomonas].
ACCESSION   WP_010483369
VERSION     WP_010483369.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..400
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44192
     Region          151..386
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlgvlshtrv lrlaglftwv mvglplaysq fenlhsrsdm gswaillfva ylsfgaayyw
       61 ltrllrsdsd shttwldrgl lllltvsalg vsylsgsglg silmmvaagv ipwmlsarlc
      121 vlwllvsqla vapvyymllh fplfeavmqs llyggfsmfi fvtslvarqq tqardeqrrl
      181 nselratral laesarvner trisrelhdl lghqltaltl nlevaghlae gqaldhvkrs
      241 halaklllgn vrevvsqlre tgaidlaaal rpltenvpsl diqldiedpl nvedpqrahv
      301 llrctqeiit navrhagarh lwikvyreap drvvveardd gvgadmvnvg nglrgmrerl
      361 qqcggqlqve trpgegfrlr atvpatvlva tltkvpegvr
//
LOCUS       WP_010483407             138 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Pseudomonas sp. S9].
ACCESSION   WP_010483407
VERSION     WP_010483407.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..138
                     /product="VOC family protein"
                     /calculated_mol_wt=15088
     Region          3..133
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(3..8,24,61..62,65,83..88,92,121,131)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mkinsyltfd gnceeafnfy adclggkvea lmrfsempaa agdvppelae rilharlvvg
       61 dqvlmasdac pmspyegirg nsvainldci ekgerifnal aqggtiempf qqtfwatrfg
      121 svkdrfgvpw lincevse
//
LOCUS       WP_010483414             399 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid aminotransferase [Pseudomonas sp. S9].
ACCESSION   WP_010483414
VERSION     WP_010483414.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..399
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43300
     Region          3..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(104..106,132,184,215,244,246..247,255)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(107,142,208,253..255,291,294)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            247
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mnhfasiarv pgdpilslme ayradnrpek ldlgvgvykd gqgltpipka vklaeqrlid
       61 settksyvgg hgdpvfcqll aelvlgtdsq alaeqrvgat qtpggtgalr laadfishhl
      121 agrgiwlsdp twpihesifa eaglevshyp yvgadnrlnv eamltalgqi pqgdvvllha
      181 cchnptgfdl shedwqrvle vvkargllpl idfayqgfge gleqdawavr lfaqalpell
      241 itsscsknfg lyrertgall vcaadteklv dirsqlafla rnlwstppah gaavvaiila
      301 dpelkaiwsh elnsmreria slreglvnal ephglaqrfa hinqqrgmfs ytgltpsqvt
      361 rlreafsiym vgsgranvag idaerfpqla raiaqvcte
//
LOCUS       WP_010483425             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator
            [Stenotrophomonas].
ACCESSION   WP_010483425
VERSION     WP_010483425.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..239
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26586
     Region          6..223
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 maiapapqsp kkraplyeev aehvreriyd yrlppgewid epalceelsi srtplrealk
       61 llaaeglvqi dagrgsrvtr ltledlnqlf pvmamlegrc aheavrhidd agvqrledlh
      121 aametaaaeg niaeyyrnny lihetvqhya gnpwlirith dlhrilkmhr grqlltpgrt
      181 aqslaehrel mecfrmrdaa aaertmerhl lsqgqalaay vaaggllnvp aplpteggg
//
LOCUS       WP_010482674             321 aa            linear   BCT 01-JAN-2025
DEFINITION  sodium:calcium antiporter [Stenotrophomonas geniculata].
ACCESSION   WP_010482674
VERSION     WP_010482674.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..321
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=32832
     Region          21..311
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 miaiaiawfl lgllllalgg dsivkavcgl aqrfgaspft agllllgvtt slpelavnar
       61 alavgqpela lgnavgssiv nlgltlavaa maaplllrar lqtvlwwsll aagvllilfg
      121 ldgglarweg gillagfivv qvlllrrgrs esaevqaaia esalsrtslp lnvlrvliav
      181 lalywgarlv vgaaadfgva lgwtpllvgl lpvaigtalp evataiaaar rghgdmvlgh
      241 vlgssvvnll lvigamavlq plalpasfvr lelpallafa lvlypmlrgd lkisrgegvi
      301 llvafvgwlv lelllvgapa l
//
LOCUS       WP_010483442             399 aa            linear   BCT 01-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Pseudomonas sp. S9].
ACCESSION   WP_010483442
VERSION     WP_010483442.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 399)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..399
                     /product="acetyl-CoA C-acetyltransferase"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41153
     Region          1..393
                     /region_name="PRK05656"
                     /note="acetyl-CoA C-acetyltransferase"
                     /db_xref="CDD:168156"
ORIGIN      
        1 mndvvivaat rtaigsfqga latvpapelg aavirrlleq tridgalvde vilgqvltag
       61 sgqnparqas iiaglphavp amtlnkvcgs glkalhlaaq aircgdaevv iaggmenmsl
      121 apyvmqgart glrmghsklv dtviqdglwd afndyhmgit aenlvdkyai sreeqdafaa
      181 ssqqkavaai eagrffeeit pilipsrkgd pvtfatdeqp rpgttaeslg klkpafkkdg
      241 tvtagnassl ndgaaavllm satkaqalgl pvlariasya nagvdpaimg iapvsatkrc
      301 lskagwtled ldlieaneaf aaqalavgke lgwdsqkvnv nggaialghp igasgcrvlv
      361 tllhemikrd akkglatlci gggqgvalai erpdqgrde
//
LOCUS       WP_010483447             295 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010483447
VERSION     WP_010483447.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32104
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..286
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(107..108,110..111,114,118,120..126,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 mtikqlrafl avaqtlsfaq acqhlhlsqp alslaiktle eslggpllvr ttrsvaltre
       61 gevllpmarr lvadwdnaee hlrqhftlql grvaiaalps faasllpval rafrdehpni
      121 nvtvhdvine qvvemvrnhr velgvvlepe sleglafipl yldrfiavvp gtsplasype
      181 lqwsdllgep fialqrpsav rslleksvse chgrlpvafe shqlvtvgrm vsqglgvsvv
      241 pglcreqmla lgaccvalsq prveqrvglv hlvgstlsaa akalieklie ttnrr
//
LOCUS       WP_010483465             355 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Pseudomonas sp. S9].
ACCESSION   WP_010483465
VERSION     WP_010483465.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..355
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=40563
     Region          36..293
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(41,44..46,49,60,62,94,113..116,216,218,220..221,223,
                     236..237,240,255..256,259)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(41,45,49,60,62,94,113..116,216,220..221,223,
                     236..237)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(44..46,216,218,221,237,240,255..256,259)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 maltdqstri regeeldaat idsylkahip gltgtprisq fpggasnlty lleypdkefv
       61 lrrppyghka ksahdmgref rilnqlndgf pycpkayvhc tdesvigaef yvmervngii
      121 lrsdipaeln fdaqktrqlc msfidklvel hnvdyqacgl gdlgkpegyv qrqisgwsdr
      181 yekaltpdap lwepvkawlc dkmpadhhkp aivhndyrfd nvildpnnpm qiigvldwel
      241 ttigdplmdl gntlaywiea ndcapmqlmr rqpsnapgml trqefadyya eragikiasi
      301 dfyytyalfr lagivqqiyy rfyhgqtqdk rfaqfiqmnk lleqmslqvi nksql
//
LOCUS       WP_010483477             374 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Stenotrophomonas geniculata].
ACCESSION   WP_010483477
VERSION     WP_010483477.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..374
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39883
     Region          1..373
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mpklgiaivg agmigavhrr aallagaevr gvaasspqrs heaaqswnva rayrdieevi
       61 aapqvqvvhv ctpnhlhram aqaaleagkh vicekplats ledaqalaal aasrglvatv
      121 pfvyryhpvv rearariaqg dlgplhlihg sylqdwlldp asnnwrvdpa lggtsrvfad
      181 igshwcdlve wisgerfaev saafstviae rgavsgqsfs tptaasamqa vtsedvaaam
      241 frtdagtlas ltvsqvsagr hnrlwfeidg akasvafnqe daerlwiglp dqrekifvrg
      301 pgagsddqrr lsvlpaghaq gyaqcfeafv adtyraiege rpqglptfed glrsaqivdr
      361 viasarsraw ttig
//
LOCUS       WP_010483544             794 aa            linear   BCT 01-JAN-2025
DEFINITION  arylsulfatase [Pseudomonas sp. S9].
ACCESSION   WP_010483544
VERSION     WP_010483544.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..794
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=87275
     Region          64..571
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(74..75,112,170,172,265,372..373,433)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(74..75,112,170,172,265,373,433)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
     Region          644..787
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
ORIGIN      
        1 mtstrlwtpc vilvlstlsg avtaqdwpdr sklpqplspf kgeishtyeg skpgwqkpis
       61 apegapnivl vliddlgfgq pgtfggpvpt peldrlasgg llynrfhttg vcsptraaml
      121 tgrnhhsvgf gtivelstgf pgynsllpkd avtvahtlrd ngystamfgk nhntpdwesn
      181 pvgpfdhwpt gwgfetyygf ngaatsqwep qlyhntnave petrpeegyh lttdlvdrai
      241 dwievqesvn pekpyflyla pgamhaphha pkewidkfkg qfdqgwdklr eqtllrqkql
      301 gvvpqdtilt prpkeieawd sltaeqkrly thqmevfagf lahtdhevgr fieavnkspd
      361 adntliiyia gdngaspegt ptgtlneimt qngipdsvea qlakidelgs plhenhyavg
      421 wawagsspfq wmkrvpshfg gtrngmvvsw pkaikdkggv rdqfshvvdi vptllnaaki
      481 papeyvdgvk qvqmagvdlg ptfasaqaee vhntqyfetg ghraiyhegw vaanfhgapw
      541 kltgsvgftd peyntwqlyn veedfsqskd iaaenpeklt elvtlfdtea kkyqvypldd
      601 rfaergiipr psvvagrtef tysagisrip egsapptyqr shkitakvni tdantegviv
      661 acggagggyt lyvrngklhy tysffgkesy hlvseeqlpq gnvevtmnye qlpfkpfves
      721 tggtaelfin gksvakgavd nsvparfsat etmdigkdlg spvssdyreq apfaftgkie
      781 nvrfniastq pvkk
//
LOCUS       WP_010483492             108 aa            linear   BCT 01-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Stenotrophomonas
            geniculata].
ACCESSION   WP_010483492
VERSION     WP_010483492.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..108
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=11446
     Region          10..102
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mnaltlpepi aayfaaehdp ealgrcfttq ailkddghtl tgvnaikafl aeasakyrat
       61 svpcaiarqe hchvvhatvs gnfpgspill tyrfelqrgl iaaleita
//
LOCUS       WP_010483593             323 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Stenotrophomonas geniculata].
ACCESSION   WP_010483593
VERSION     WP_010483593.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..323
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=34558
     Region          16..314
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mtdplldiar lggttmgttw svslvaprqr dlhplhagiq arldevvaqm stwepgsdls
       61 rynranagqw calpaetrqv lacaqaiaaa sdgafdptvg plvalwgfga hagerrqpda
      121 atvqatrerc gwqrlqwrsd allqpgglel dlsaiakgfg vdhvaawlrd qgiaaaliev
      181 ggelagygrk pdgqpwrvlv esapeedaht etpprvlale dkavatsgdr whqyqadgqa
      241 fshsldprtg mpvrqvaaav tvvaddamha dawataltvl gheqgmalae reglaarylq
      301 raadgprefl ssafqrllde qda
//
LOCUS       WP_010483658             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Pseudomonas].
ACCESSION   WP_010483658
VERSION     WP_010483658.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..158
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17088
     Region          1..141
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 msesailera qrflsalrhc qvlglqvhqa taegltlclp yspqiignpe tgvihggait
       61 tlmdttcgis tvcvlpefei cptldlridy mhpaephknv ygfaecyrvt pniiftrgya
      121 yqddptqpia hvvgtfmrmg kiaqgggnlk kdiqggaq
//
LOCUS       WP_010483665             243 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Pseudomonas sp. S9].
ACCESSION   WP_010483665
VERSION     WP_010483665.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..243
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25946
     Region          4..238
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 msnmkvqaia yevdgvqfeg qlvfnsaikt prpallmapn wmgvsdgaid iarkvagddy
       61 vvfvadlygk dlrpgnadea gaammplkdd rallrkrmqg slktllaqad kvalddsrqa
      121 tfgfcfggcc slelardgap lqaavsfhgt ldtpnpadak kikgavlvld gaadplvpre
      181 qlaefakemt eakvdwqlvt yggavhsftd phanmpgtaq ydektaaraf tamrnlldec
      241 fsa
//
LOCUS       WP_010483690             220 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Pseudomonas sp. S9].
ACCESSION   WP_010483690
VERSION     WP_010483690.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..220
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24685
     Region          1..201
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 midfytaatp nghkvaiale elglpykvha lsfdkkqqks paflrvnpng ripaivdrdn
       61 ddfavfesga vlvylaektg rlipqdvkgr srvmqwlmfq mggvgpmqgq anvfyrylpe
      121 kiqvgidryq hecrrlyevl dtrlaeeefl ageysiadia tfpwvrlhdw agvsidglds
      181 lqrwldaiaq rpavqrglai phseddgvkv vksaqtmlar
//
LOCUS       WP_010483711             134 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Stenotrophomonas geniculata].
ACCESSION   WP_010483711
VERSION     WP_010483711.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..134
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14573
     Region          15..119
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mgitsvagvp vqprhratch cgtvellldl pdgivdprrc dcsmcrrrga iaasvaragl
       61 qvvrgqnhlq lyqfntyvae hyfcgvcgiy thhrrrsnpd qygynvacle gidpfalgii
      121 pvndgvnhpa drta
//
LOCUS       WP_010483737             232 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Stenotrophomonas].
ACCESSION   WP_010483737
VERSION     WP_010483737.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..232
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25439
     Region          4..207
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtpilfygvp sgcsfgsiva lewlrqpyql cridmpgqvq gedyrrlnpl getptlrtpq
       61 gellseslai lnhlaakgia qglgfaqgta gfdrlnhrla ylntsffgay aplwhaleha
      121 egdeaevlga ygttkvrhah qaleqmigtg pwllgeqrsf adayfagiar wndyhqvvdr
      181 refprvqqlf erlqddagvq fahaieaqqp atssggflge vrledvleaa aa
//
LOCUS       WP_010483820             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thioesterase family protein [Pseudomonas].
ACCESSION   WP_010483820
VERSION     WP_010483820.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..146
                     /product="thioesterase family protein"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16244
     Region          21..140
                     /region_name="4HBT_2"
                     /note="Thioesterase-like superfamily; pfam13279"
                     /db_xref="CDD:463826"
ORIGIN      
        1 marltlsfpq dqfcfsthlt vrvtdinaan hlgndsmism iseararflf dfgieeasee
       61 gvgiivtdla ttyraeahar dqllfevgvm dfnkyggdit fritrpades liamaksgfv
      121 ffnyktsqva qmpgafsdkf prvnwl
//
LOCUS       WP_010483874             331 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010483874
VERSION     WP_010483874.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..331
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36005
     Region          5..330
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mdalktiacl iypdfmslda igplqvfasa nverqrqglp ayyrtlllae qagpirtsag
       61 ieviaaqald eiqaseidtl lipggigehq qvcnqrlldw lrsaepqirr lgsvcsgali
      121 laasglldgr ratthwadve tlrrdhpnie vladqlhtyd ahdtqgnahl ftsagvtagi
      181 dlalaliead lgrvialava rrlvmflrrp ggqaqfsall spepsrtprl aalldwiptr
      241 igedlslevl aaqacmtprt lsrvfiqelg vgpgkyvekv rleaarnllq daqasistvs
      301 rltgfghpen lrrtfqkhls vspqeyaqrf t
//
LOCUS       WP_010483887             198 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Pseudomonas sp. S9].
ACCESSION   WP_010483887
VERSION     WP_010483887.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..198
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21628
     Region          2..>107
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mlniaivags srnnsqsgkv arflrkrlmq mnltseaqsq vidlglaplp lwpaeddgpw
       61 glyseqlksa daviivapew ngmacpaikn ffiyasktel ahkpgllvgv ssgiggsspi
      121 selrassykn crlcylpehl ivrhaeqvln mpepqseddq rlraridysl dilgkyaqal
      181 kpvresidmt qaaftngm
//
LOCUS       WP_010483921             141 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas].
ACCESSION   WP_010483921
VERSION     WP_010483921.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..141
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15668
     Region          12..138
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mnkisvrlad wskdnadirr ireavfiaeq svapelewds edaqashfla cegdypvgta
       61 rllddghigr vsvlkdwrgl kvgdalmeaa iaeaekrglr rqmlsaqvha safyerlgfn
      121 iiseeyleag iphvdmvrns d
//
LOCUS       WP_010483990             166 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Stenotrophomonas].
ACCESSION   WP_010483990
VERSION     WP_010483990.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..166
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=18572
     Region          4..160
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mssnaaslte llirerpall rrvqrilggd ngaedviqav wfkargvdds qaidnprayl
       61 yrlaanlatd hgrestrrnr lladhylwgp devisteera maqdelqrvl daaghlpept
      121 rtifrlnrlq gltqaeiarr lgvsvttven hvrtalqrla warsgr
//
LOCUS       WP_010483998             239 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Stenotrophomonas geniculata].
ACCESSION   WP_010483998
VERSION     WP_010483998.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..239
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25324
     Region          157..234
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 msglrrwats laivllvhal lvsvacwwaa rapavaaaap paalmlelap maqappvppr
       61 evatgplqqq qqrqapkpal reqpkapvqp qgdlppprtp eptpspdtae anvaqtsapp
      121 qvaadaaary tapqttager sraeatwegr llghlqkhrr yprqaerlrq qgvvyvrfav
      181 aqdgavsglt lgrssgfall dqetldtvrr aspvpappae vagdpvdvmv pvsfflrgr
//
LOCUS       WP_010484105             309 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Stenotrophomonas].
ACCESSION   WP_010484105
VERSION     WP_010484105.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33652
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..287
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,222,239,266)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrltamtvf vevaergslt aaaevldmsr amvtrylaev egwlgarllh rttrrisltg
       61 pgeaalarfr qmlaigeelq gelasddpep hgtlrvtasv sfgqshlara vagfvarhpa
      121 arielllvdr tvnlveervd lavriarqid psliarrlat crsvlcatps ylqargtpta
      181 pehlaahncl thhyvgkslw qlhrdgrsls vavggnisan easllleavr agagiamlpt
      241 yqvapllrsg eliellpefs ldelgihavy asrrqqpaim rrfldflgec faspafqdld
      301 wrppgkent
//
LOCUS       WP_010484106             212 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Stenotrophomonas geniculata].
ACCESSION   WP_010484106
VERSION     WP_010484106.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..212
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=22140
     Region          2..212
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mkialvgstg nigrqiarha largheltvi vrsaqdlpae lagahpvvas lddldalvaa
       61 iaghdvlasa ygprpgddig rvgevaaqla aaarkagipr lvvvggagsl evapgvqlvd
      121 tpdfpeaykp yalahreafn rlqavddldw tffspaaeig pgeergqyrv qpkafladts
      181 ghsrisyady gaafvaelea hqypkqiita ay
//
LOCUS       WP_010484113             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [Stenotrophomonas].
ACCESSION   WP_010484113
VERSION     WP_010484113.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..233
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25854
     Region          1..223
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mklvklianl gygsrkqvqw mfregrvtda dgevlyaddq vpheairvdg epldppvgls
       61 ialhkpagyt cstkdtgrli ydllpprfrd rdpvlstvgr ldretsglll ltddggllhr
      121 iispksklpk vyevelsedl rgdevalfas gtlmlesekt pllpaelevv darrarlvlh
      181 egryhqvrrm faatgnhvqa lhrsrvggld lqgldegqwr qltstdldtl fap
//
LOCUS       WP_010484114             354 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Stenotrophomonas].
ACCESSION   WP_010484114
VERSION     WP_010484114.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10524380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..354
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=38364
     Region          176..345
                     /region_name="MTS"
                     /note="Methyltransferase small domain; pfam05175"
                     /db_xref="CDD:428349"
     Site            order(213..219,235..236,262..264,281)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 massddaplq tlflpfsqga lrwpegpvaf lrardgwplr eaagsrevhc eqsfapfaqp
       61 lqqaagwtvs gqlddvagkg ryplvlvlpp rqreearalf aralalvadg grivacqsnn
      121 egarsgegdl kqltglggsl tknhcrvywt apmqgqhdad lakrwsalda vrpivggrfl
      181 srpgvfawdr idpasallae hlpadlagra adlgagygyl srellercpk italdlyeae
      241 qralalaeln lappprplpl rflwqdvtag iepgydviis nppfhtpsra drpdigqrfi
      301 avaaqalrpg grlyvvanrh lpyeytlnes fgavrviaer dgfklveavk gkgk
//
LOCUS       WP_010484174             381 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YncE family protein [Stenotrophomonas].
ACCESSION   WP_010484174
VERSION     WP_010484174.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..381
                     /product="YncE family protein"
                     /calculated_mol_wt=40234
     Region          1..217
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          146..381
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mfrnplfrsa alavavslsl gvpsafadna paasataavq rqavakglye layspkqnav
       61 fvassggfgd dagpaqvlrl npstlavetr iplerkafgv vlddahnrly vgntvdlsvt
      121 vvdtaqnkav gtiqlmekkt gkdgkaayth dlrelvvdsa anrlyvtghs sqpdvssvlf
      181 vidtttlkvi ntidglgnak apglaldaan krvytsnlla dlvvvgtesn kvvaqhriaa
      241 eqpmnialdp agkrlfvtdq gseflrgyqa kssglvskhp gqrvlvldrs tgkelasipt
      301 dagplgilld aprkrlyvtn reagtvtayn sdsyqkvaty kvpthpnsla ldaknnvlfv
      361 sikngekddk gadesvariq l
//
LOCUS       WP_010484256             776 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Stenotrophomonas geniculata].
ACCESSION   WP_010484256
VERSION     WP_010484256.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..776
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86083
     Region          40..755
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mrrhllaaai lfavhtaqaa deptlptlqv qasqpsridt rvtvdnpqaq nrtlgglleh
       61 vsgvqssafg pnagapvirs lsgnrvqilq dgqsilgmna isgdinipfd plfvrsvtvn
      121 kssdtvrygg naiggsveid pglisrsmed kdqsmelvlr kgfnaadaqg frmnfnnqrn
      181 lstnlqvsrq rishydipgn skasvcntrl fpptggvnsa ladscqkear vqqiynkasq
      241 pyidqfmten pdwadgdfsf ytnnptsvwq rrtyinpvnp ayvagtpsyv qkqinndvtp
      301 dyhhrlgnsy arnsqvafgs tlffdrgyvg vsidakdsey gvpgfsmqnl sfgsnyanal
      361 pvgvvikqer yaleallrdp lpwferaelr vskldntsge rlgatrandy dfestqaell
      421 lsrqrvgpls gllgyshqsr dvtgsgslry lpdvdtrsna vflketldfg wasfdagvrh
      481 ervdhelqps rfktarnaan tklqdrsyrl nsyglgsyve lgplfaakvr ysssqrapei
      541 nelyasnahy svmtqeegnq nleperaknl eltglfhigg felsatayrt kyenylylgy
      601 sgvqtanrlp lkywkqtdtt vkgfeidasq aldlgrygtl nisafadlvk nkadhpdslr
      661 ahndgeylpn mptnryganl qwqregwkaq lsstyydtqk ylgrnvseev pldafnlvdl
      721 qvsrelpvrn syiagmevfv ngsnllneea rphnsplkyi aplpgrgfqv gvtvrl
//
LOCUS       WP_010484274             372 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Stenotrophomonas geniculata].
ACCESSION   WP_010484274
VERSION     WP_010484274.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..372
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40120
     Region          90..348
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mkrlllllla caglwlaacs psinasstsl adrliapggv stlldrpria aaiaelpnrh
       61 gfapgrdgvp ifwrvfdpgd ygaryhylpq rhenglpldt glslavpqpf raqaprgtvv
      121 llhgwmmngd smlpwslqla ksgyrvvtld lrnhgqsgag psgygtyesd dvvdvinelr
      181 argevtgply lfgvsygaat avftadklgd qvegvvames fanagvairt miphlmglqp
      241 eglkaqavas yarwryggqd inqviaaasr ridvdldrvd varaladtra cvlllhgqgd
      301 qhipvsqgre lalanprahy iemrgedhit lplrldllag vvddwmarde hhpksacpap
      361 qlpaqaewlt rs
//
LOCUS       WP_010484278             233 aa            linear   BCT 01-JAN-2025
DEFINITION  pirin family protein [Stenotrophomonas geniculata].
ACCESSION   WP_010484278
VERSION     WP_010484278.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..233
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25311
     Region          10..231
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mlqirksatr glaehgwlss rhtfsfanyy dpryvsfgpl rvinedkvig gqgfgthghs
       61 nmeiisyvlg galehkdsmg tgsvlrygdv qrmsagsgvt hsefnhsvde tvhflqiwif
      121 pdaeniapsy eethftpdsk rgqlrliasp dgadgslrih qdarifatil dggqklhhal
      181 gngrgayvqv argqlqvngi tleagdalqv sdeaqltlen gndaevlvfd lpl
//
LOCUS       WP_010484317             141 aa            linear   BCT 01-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Pseudomonas sp. S9].
ACCESSION   WP_010484317
VERSION     WP_010484317.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..141
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=16165
     Region          12..102
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mndflkdfar efaalnkhnl erlvdlysed avfqdplhtl hglanirgyf aelyanvsdl
       61 sfdfkgydqv gsgegylrwt msyrhprlag gnliqvegcs hllwhtrvyq hrdyfdagsl
      121 lyehlpvlgt viswlkgrls q
//
LOCUS       WP_010484369             367 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Pseudomonas sp. S9].
ACCESSION   WP_010484369
VERSION     WP_010484369.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..367
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40510
     Region          16..354
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mnvifeefps lhgvsigvat ldaekslnal tlpmiealds qfaawaddpq iacvmlrgng
       61 pkafcaggdv vqlveecrah pnqvpplarr ffadeyrldy rihtfpkpfi cwahghvlgg
      121 gmglmqgast rivtpssrlg mpeiniglyp dvggswflar mpgalglffg ltasgmnard
      181 aldldladrf lldsqqdall dgliqlnwqi qpetqlhsll kaleqqaiae mpeaqwlprr
      241 sridqlldqa dlpsaynall alqndddkll araaktlagg cpltaylvwe qiararhlsl
      301 aevfrmeyam slnccrhpef pegvrarlid kdqapkwrwp diasispetl aahfepvwqg
      361 dhpladl
//
LOCUS       WP_010484413             125 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Stenotrophomonas].
ACCESSION   WP_010484413
VERSION     WP_010484413.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..125
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13946
     Region          12..112
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mahqsrlagf iidcqdtpad egarfwaaal glqaqpsyae dgaeyadlqg apaglnvevq
       61 rvdhpsrvhl diesddidae adrlerlgar rigfvkrwwv meaptghrfc ivrmrerevp
      121 anhwp
//
LOCUS       WP_010484523             229 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Stenotrophomonas].
ACCESSION   WP_010484523
VERSION     WP_010484523.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..229
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25739
     Region          1..225
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mrivhhlens rslrvlwmle elgldyelrr yprdpktlla ppelrnvhpl gkspvlqdge
       61 lvlaesgail dyladrydtq rqlspspmpa dgaeriayry wlhyaegsam ppllltlvmg
      121 rirnapmpff arpiarsiad kaergfigpq rrlhldwmer rlaespwfag erfsaadiqm
      181 sfpiqaaaar ggglddkpal rgflkriger payqraeahg ghlqalsgn
//
LOCUS       WP_010484640             695 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. S9].
ACCESSION   WP_010484640
VERSION     WP_010484640.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..695
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76801
     Region          7..695
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mqfcrtiast afatlafspl sakanesfel pgqqvtgqrl nteyssdtas tasksavpim
       61 qeaqavqvvt eqviedfqvn slddamnfvs gitqsntlag sqdgfvkrgf gtnadgsilr
      121 dgirsslsrn fsattervev lkgpasllyg alepgglinv iskkpeylwh sqisgetssf
      181 gggsamldvt gpladsgfaf rfiaerqhed dwrnsgedeh tliapsvswt gndltlslay
      241 erkeystpld rgtvivngkp ahvdynkrfs eswskaegtd elvtakaeyq inpnwltrlt
      301 ygwnqedydy aearpaslde stgdltrrad gsefknqthy lawdwighsq lfdqrhdvli
      361 gadtervdnf rgdtyrgrns tgfniynpqy gnlgepslis qaqsdrsdel hsqsvyfkdn
      421 whlndqwivv lggryqrfeq yvdqgrgdey vkttdrtdnt flpfaglvyq lnqqvslygn
      481 ysrsfvpnss dadtgesfdp eegrsyelgv kldlqpgisa svalfdieke nvvvsnngss
      541 eaagkvgsgg veldingria ehwnllgtya ytdteikddp qnqgnelvna aknvaslyls
      601 hdldinpetg nwrvgggary vgeragdnsn sfwldsytva dafiawdstl lgdktrvqln
      661 vrnlfdqhyy pssggnlrvn vgepreirlq asvdf
//
LOCUS       WP_010484806            1024 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudomonas sp. S9].
ACCESSION   WP_010484806
VERSION     WP_010484806.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..1024
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113270
     Region          4..1020
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfnlsrwal qnrqlvlyim illsvigals ytklgqsedp pftfkamvir tnwpgasaee
       61 vsrqvtdrie kklmetgeye klisysrpge sqvtflasdy lkadevkely yqvrkkvgdi
      121 rhtlpqgiqg pffndefgdt fgniyaltgk gfdypilkdy adriqlqlqr vkdvgkidll
      181 glqdekiwie lsntkaatlg lslaavqqal nqqnavttag ffetptdrvq vrvdgrfktp
      241 eeirnfpirv agrtfrlgdv aevkrgfndp aaprmrfmge dalgiavamk dggdilqlga
      301 alqnefariq qtlpagmqlh kvsdqpaavk tgvgefvrvl aealvivllv sffslglrtg
      361 lvvalsiplv lamnfatmyf lgiglhkisl galvlalgll vddaiiavem maikmeqgyd
      421 rlkaasfawt stafpmltgt litaagflpi ataqsgtgey trsifqvvsi allvswiaav
      481 vfvpylgakf lpdlaklhal khggsetghd pyatpfyrrv rriiawcvrh rktvivitva
      541 mfltslamfk lipqqffpas nrlelmvdlk laegaslrat eaqvsrledm lkehdgidny
      601 vayvgtgspr fylpldqqlp aasfaqfvvl tknieqreei rswliktmne qfptlrtris
      661 rlengppvgy piqlrvsgeh idkvralarq vavkvrenpf vtnvhldwee pskvvrvnid
      721 qsraralgit sedvanflrs tlvgnsvsqf rdddelieil lrgtdqerrs ldmlpslaiq
      781 tssgksvals qvatleygfe egiiwhrerl ptvtvradvy gkeqpssiiq qilptleqvr
      841 eqlpagylln vggtvedsak gqksvnagmp lfivvvltfl mlqlrsfsrt amvfitaplg
      901 ligvtlflll fnqpfgfvam lgtialsgmi mrnsvilvdq ieqdisagqd rwnaiidatv
      961 rrfrpialta laavlamipl srsiffgpma vaimggliva taltllflpa lyaawfrvke
     1021 qpqg
//
LOCUS       WP_010484817             245 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Pseudomonas sp. S9].
ACCESSION   WP_010484817
VERSION     WP_010484817.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..245
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27180
     Region          9..245
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mnglklgsdq rlplyqrlrd eilakiasge wrpgepipte aeltktynva igtvrkavdt
       61 lvvdgllqrs qgrgtyvrrp dfnsslfrff rqtnssgehq vpqsrivtlg lepapqtvvn
      121 alklsasdtv irmqrvrtsg eraifteviw ltasrfakll evdpqdfgnl lypfyeqqcg
      181 qlvasaketl tveladtqts aalgidsgkp vvviertals ydntpleyri srgaadtfry
      241 qieis
//
LOCUS       WP_010484842             559 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type IV secretory system conjugative DNA transfer
            family protein [Stenotrophomonas].
ACCESSION   WP_010484842
VERSION     WP_010484842.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..559
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62809
     Region          138..542
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mlpskkylli aittlatlll gfvfsgyltl lflgldtklf twntyyqyfn aldqpqvapf
       61 vgkikwagyv gfglpllall vtglvlllkk dkrslhgdar fatgadlskh gmfkktgqsi
      121 vvgshsgklv rldgqqfvil aaptrsgkgv gvvipnlley geslvvldik qenfdltsgw
      181 rasqgqeiyl fnpfaedrrt hrwnplsyvs ddpafrvsdl msiaamlypd gaedqkfwvs
      241 qarnafmaft lylfenwdde rssgfpggsg tptlgavyrl ssgdgtdlkk ylkalsersf
      301 lsgnarsafa nmlsqadetf asilgtfkep lnpwinpvld katssndfll tdvrrkkmti
      361 yigiqpnkla esrliinlff sqlinlntke lpksnpdlky qclllmdeft sigkveiias
      421 avsymagyni rllpiiqsms qldatygrev srtiitnhal qilyapreqq dandysdmlg
      481 yttirkknvt harekthnft eerralmlpq elkamgpdke vflyegiphp vkcdkiryyk
      541 dryftsrllp kvdvpmlnv
//
LOCUS       WP_010484865             159 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TlpA disulfide reductase family protein
            [Pseudomonas].
ACCESSION   WP_010484865
VERSION     WP_010484865.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..159
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17299
     Region          26..141
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(56,59)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 maaqlqwvir ivlgvfavvv ltacsdatgv dqygrkvpve riegqwlvin ywaewcapcr
       61 teipqlnald kelagkgvsv lgvnfdnlqg aelekvseal gitftvlasd paeryklprs
      121 ealpvtyiid dsgrtrerll geqtaegikt klaqlkaeg
//
LOCUS       WP_010484893             255 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Stenotrophomonas geniculata].
ACCESSION   WP_010484893
VERSION     WP_010484893.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..255
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=29066
     Region          2..219
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mralillahp eprsfnahla aqaaeqlrhd hsqvdvvdly aegfdpleaa whhprrlqpe
       61 rfdaqreqrh saeleqlpad vrrhlhllrv adlvilqfpl wwfaapvilk gwldrvlvyg
      121 pmynsrqrhe hgvmqgkral lsvttgssar acavdgregd trlllwplmy slryvgfevm
      181 epcvvhgvrs glaaervqah dealvaatls yrerlthwrq wpivpfndsd dfedgvvlra
      241 datahspfir hrdag
//
LOCUS       WP_010484921             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peroxiredoxin [Pseudomonas].
ACCESSION   WP_010484921
VERSION     WP_010484921.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..157
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17311
     Region          7..149
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(42,45,120)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mtvkidapvt dfqaqatseq qvqlsalkgk qvviyfypkd stpgcttegq gfrdqfsefq
       61 aantvifgvs rdgvkshenf kakqgfpfel isdkdeslck lfdviklkkl ygkeymgvdr
      121 stflidkdgv lrqewrgvkv pghvdavlaa aqalnka
//
LOCUS       WP_010484945             207 aa            linear   BCT 01-JAN-2025
DEFINITION  CGNR zinc finger domain-containing protein [Pseudomonas sp. S9].
ACCESSION   WP_010484945
VERSION     WP_010484945.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..207
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23252
     Region          8..202
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mntadnrhwt tsdfiaddpv ldflnttgak gkqrinerlh scralidwal aaqlvtedeh
       61 qrllqlsqae tatagreldq iilwrealya lmhaasheqk pegaalhcve nvikqalasa
      121 qlhytvgepg fwgvdsekag iatirhrlal qlnkgitggk yqqtkeceac twmfidtsrs
      181 rrrrwcsmst cgnrakarrf yqgenka
//
LOCUS       WP_010485030             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Stenotrophomonas].
ACCESSION   WP_010485030
VERSION     WP_010485030.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34544
     Region          19..78
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          107..304
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(117,121,160,175,177,239,256,283)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(118..119,123..124,126..127,130,134,136..142,204,
                     233..237,244..245,248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mawiyndali apgtgmdsfn lmrafrrive rgglaraaed lgmspaglsk qlrtlethlg
       61 vvllqrttrr msltetghay yreccrllde lealergiae qrgevagrlr vnapqsfals
      121 tlspllprfl qqhpqlsldl vmedrlldav gegfdvslrl raelddsrlv arrlaslqqv
      181 lcaapsylrq hpapqavddl qahsvlaysl sdspgswpll gpdgqvtitl parvtvnnsl
      241 llrdllvagm gigalpsfla apalaqgelq qvlpdhrypp rfvhavypts rhlqpkvraf
      301 idflhaelpg caglds
//
LOCUS       WP_010485028             231 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Pseudomonas sp. S9].
ACCESSION   WP_010485028
VERSION     WP_010485028.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..231
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25529
     Region          1..213
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mgsmsvsakq vevqrivdvl skaiaqhrlr pgtrlveaqi vetlqanrnh vqvalqrlam
       61 qrivtiepnr galvsqptak earevfaarr aieraivesi sprmmaehaq rvsthlsner
      121 catnatdrra ivrelsefhl llgelsgnsv lseilanlmv rsslivalyq rndvpscasd
      181 ehqeiitalq qgdtdkavrv mlehldeleg qlaldeqepe evnlrqalag l
//
LOCUS       WP_010484981             267 aa            linear   BCT 01-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Stenotrophomonas
            geniculata].
ACCESSION   WP_010484981
VERSION     WP_010484981.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..267
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29116
     Region          31..>118
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
     Region          136..266
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mssvgpvpmp vvlilvcvll amavarlwpr rkdgmplpsa psmvldmllv gllcgrisfv
       61 alnfalyrea pwsilqiadg gyhlavvlva glawglwrlr pwralrapvl gaalagvllw
      121 aggsqllsaw qerrmplpvl qvadlqggrv dlqqfrgkpl vlnlwaswcg pcrrempvla
      181 aaqqahadvq fvflnqgetl eevqgfvare rlllgnvlld ddaaastvlg vqaypstlff
      241 daegrlrelh lgeltaagle hklrrlr
//
LOCUS       WP_010485032             292 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Stenotrophomonas geniculata].
ACCESSION   WP_010485032
VERSION     WP_010485032.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..292
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32304
     Region          104..244
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mlrlyaplfl lgfvatavvw vghchgdplw llallaiaia vsfvaerawp ydpafnrdhg
       61 drvrdalhal vneglnllsi aavpllaaii pwqlwplqwp falqllvaii aadlgitlvh
      121 yashrigwlw rlhavhhsvt rmygfnglmk hplhqaaeav ggvlpllllg lpmpvaavla
      181 faialqlllq hsnvdmrpgv lgrvmawapl hrfhhmrygt agdvnfglfl tvwdhllgta
      241 fdapgyrlqh rdlgigsqpd yprdypgqll apfrelphge vpelpeglrr rg
//
LOCUS       WP_010485052             265 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas sp. S9].
ACCESSION   WP_010485052
VERSION     WP_010485052.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..265
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29659
     Region          34..264
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 msradttasi lyhrvvvwll flilllplag tllyslstsw satilpdglt fkwyfelwge
       61 prflkafgqs llicfsalfl asililpllf vvhyhfprld glmnilillp famppvvssv
      121 gllqvygsgp vqlvgtpwil igcyftialp fmyraitnnl hainlpdlmd aahllgastl
      181 kaaflvvlpn lrkglmvslf lsfsflfgef vfanmlvgtr yetlqvylnn mrnssghfns
      241 alvisyfffv liftwaanrl nkdks
//
LOCUS       WP_010485101             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Pseudomonas].
ACCESSION   WP_010485101
VERSION     WP_010485101.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..201
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=21782
     Region          9..188
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlkrfaplvp ialtvllaac agqapqtqin qpeplaeaan patedftdft dalaaqksyq
       61 lpqladsile hglslvgtry rwggssvksg fdcsgfigyl feeeagmqlp rstreminld
      121 apivkrdele pgdvvffstn grgrvshagi ylgddqfihs asrrsggvrv dslqspywkr
      181 tymeakrvla mastgqgvtv r
//
LOCUS       WP_010485213             209 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Stenotrophomonas geniculata].
ACCESSION   WP_010485213
VERSION     WP_010485213.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..209
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22849
     Region          4..202
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 msyslpplpy aydalephfd artmeihhsk hhqayvnnln aaieqagiae qpvealianl
       61 davpeaqrga vrnnggghan hslfwtvlsa sggapddela aaidrdlggf dafkdaftka
      121 aqtrfgsgwa wltsdrdgrl qvessanqds plmgeavgls gntpilaldv wehayylhyq
      181 nrrpdyigaf fniinwaevg rryrqaras
//
LOCUS       WP_010485249             279 aa            linear   BCT 01-JAN-2025
DEFINITION  ion transporter [Pseudomonas sp. S9].
ACCESSION   WP_010485249
VERSION     WP_010485249.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..279
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31396
     Region          26..231
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mdntlslrrr iyriifftdt pagqrfdnil lvtivasliv vmldsiqaih sqyrawmsgl
       61 ewmftalfav eylvriycsp kplryifsfy glidllailp glltlffpsa qyllivrvir
      121 mmrvfrvlkl spylrqanfl mtalrgskqk iivffsciai lvtvfgtlmy viegpehgft
      181 sipkgiywav vtlttvgfgd ivpqtvlgqf lstlvmitgy siiavptgif taelatamhg
      241 gellerecps ckkdvhepha afcnrcgnpl fpreadkte
//
LOCUS       WP_010485215             506 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thioredoxin family protein [Stenotrophomonas].
ACCESSION   WP_010485215
VERSION     WP_010485215.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..506
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=54144
     Region          33..146
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mlpmrvalsm lllasalsac tpapvsians aevpapakai awrqgdvdda faeaadsgkp
       61 vllywgavwc ppcnqlkagl fkdpafialt skfvpvyldg deegaqawge rfgvrgyptl
      121 ivldpkrnei trvaggndat eltraltvaa grrsavaatl atalatpdrl aaedwqvlgd
      181 ygwevdanrl agerssedvl rqlskaapda alqrrfalla lataekpdas ptevrellqa
      241 vlaqpaevrr nrellgyagv qlvkqasagp atsntlgqql lvaleradae rgdraddals
      301 raltevslar qqqpkgalpa alvdrvkqrv aaadaaatda harqatissa vyalrqvgdd
      361 agaeslllae lkrseqpyyy mpelaelaeq rgdtagalew lkraydgaqg patrvqwgvl
      421 yvegllklap ddaprieqat asliaeleaq psgyhqrtrq rferlagqlk twsgkhqgae
      481 tlarlqqrmq qacgdqvdga ckdwls
//
LOCUS       WP_010485305             154 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Stenotrophomonas
            geniculata].
ACCESSION   WP_010485305
VERSION     WP_010485305.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..154
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16608
     Region          14..146
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mnekiiakvv draqaaidpa egiaavsdpg fggidvfvgk vrdvnigrpv tgitydlfep
       61 lvlnefkrla aeveatfgpk lklyvahakg rlgigdvavv vaagsphrde afracrqlie
      121 vvkhqcpiwk qehyedgdse wsegcslchv dsep
//
LOCUS       WP_010485324             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AzlC family ABC transporter permease
            [Stenotrophomonas].
ACCESSION   WP_010485324
VERSION     WP_010485324.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 243)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..243
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25649
     Region          21..224
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mdarttlplp dtcdtaprae flrglraavp vmigfipfal vlgaqaaqkg lsalevplmt
       61 glnfaggsef aavelwtspp hialivaita lvnsrhllmg aslapllqhl prrrvlpalf
      121 fmcdeswamg vadarrralg fslayylgvs aglytvwvac talgaivgpm lgdihaygfd
      181 mafpavflvl lrgmwqgmka arpwlvsliv aaatyllipg awyvasgala glaaawllae
      241 dae
//
LOCUS       WP_010485361             132 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Stenotrophomonas].
ACCESSION   WP_010485361
VERSION     WP_010485361.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..132
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14399
     Region          11..127
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mayarivsta dnylhhisng sfdvdadepa slggqgkgfa pfdlylasla actaitlrmy
       61 aqrkgwelge fhaelrserd adgrfhvhrv lhasaelsda qwqrllevve ktpvtlvmre
      121 garisserga aa
//
LOCUS       WP_010485395             130 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Pseudomonas sp. S9].
ACCESSION   WP_010485395
VERSION     WP_010485395.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..130
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14045
     Region          12..>130
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mmqtnqrrnt aviavvddde pirialesll rssgyqvksy csaldfinsn gpwethclis
       61 diqmpgmsgv emleqlnaqg ftipvifitg ypgaapcita atphlvaclp kpfaadklls
      121 hiettlqakr
//
LOCUS       WP_010485466             213 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor
            [Stenotrophomonas].
ACCESSION   WP_010485466
VERSION     WP_010485466.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..213
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23241
     Region          15..209
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mrkpaapaid papivyvidd dpsvraaled llasmglqvr afastqafle heledapacl
       61 vldvrmpgqs glefhrtmgs hglqlpvvfi tghgdiamgv naikdgaief ltkpfrdqel
      121 ldaihkgiei drqrrregdv lgalqqrwds lnagerevvd gvvrgrlnkq iagdlgvsei
      181 tvkvrraqvm rkmgartlvd lvrmydrlqa gsa
//
LOCUS       WP_010485484             194 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Stenotrophomonas].
ACCESSION   WP_010485484
VERSION     WP_010485484.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21006
     Region          14..136
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msphsdptap trgrpptitp erladigirl glpnltmanv aaelavtqaa lykrvanlea
       61 lkrlvaeavf qrwqiprasv dapggleayl mrfveslcev vkahpglppy llrrtvatap
      121 mlekiashqa hvadvfglpv dkarwllati afyciagadt iyaiaddeeg qvitefkqgm
      181 ralvigslev srlr
//
LOCUS       WP_010485406             307 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Stenotrophomonas
            geniculata].
ACCESSION   WP_010485406
VERSION     WP_010485406.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33745
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..292
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(100,104,143,157,159,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(101..102,106..107,109..110,113,117,119..125,187,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdrftamraf vriverrsft rasedlglpr atvtdaikal eqrlgvrllh rttrvvvptl
       61 egeafygrcl rliadmddae aafrdapprg plrievhgtl grhllfphlp eflqrypeie
      121 ldisegdryv dllregvdaa lrvgtladsd laarrlsmlr evtvaspgyv qahglpdtie
      181 slqdghqmvg yrssatgqli plefqqggqv ryvplparvr vsgaeaflga alaglgiiqa
      241 pryrmdpyia rgqlaellpe tpptpsplsl vyprnrtpsp rlrvfidwva gvfeqtgvag
      301 qqpglpg
//
LOCUS       WP_010485513             319 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Stenotrophomonas
            geniculata].
ACCESSION   WP_010485513
VERSION     WP_010485513.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..319
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34047
     Region          7..303
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 msvptgsrlv iyaalagnla iaiakfiaag isgssamlse gvhslvdtln ellllyglrr
       61 agkapdpvhp fgygrelyfw sfivallvfa agagvsayeg iqhirrpepa snhalsysvl
      121 gisilfegas wwvalrefrr tkgrlgyfea frrskdpstf tvlledsaal lglvfaligl
      181 vaaqaldmpv ldgvaslcia gvlaatafll aretkgllvg epahpavaer imavaetdpd
      241 lrrangvttm qmgpqqvvam lsaefeddrr tpqieacitr ietavkqefp elvtlfvkpq
      301 tpevyaarra alatppapd
//
LOCUS       WP_010485520             762 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Stenotrophomonas geniculata].
ACCESSION   WP_010485520
VERSION     WP_010485520.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..762
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81743
     Region          46..731
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mrhatlhrpl ltlaiaaalp alahaeespt adasasadaa rtvvaldqvm vtaqkratnl
       61 qetpisvsvv daealkdrsa islgslsdgs ipslrvtpfa trssalnigi rgvgasgdan
      121 qpardagvgi yvdgvfmgra qglgsmlydv erievlkgpq gtlfgrnteg gavsivtkap
      181 tgelggsvsa gvsnfsgyns avhldlpklg dvsfkidavq akrggttdnp mrgerdfnsy
      241 dkrgarlsal wqpsddfsll yafdrsydat tpyhtqvlvp gaylsplqka gasqdrrdsa
      301 ilggpqkdni grtsghllsl swtlsdalel ksissyrelt qgqfdmglvd aisayggagt
      361 pfgryslaqv yqhqysqefq ligntsqvqf lggafyyhet agdnaqtpnm lvwgpggnsy
      421 tvnpatspld lsrvridras kawtdslgvf gqatwtpeal qrlhltaggr ytrddkkgsl
      481 yivngaatnl afkdrwsrfd pmvtiaydlg ehamvyakys tgfkaggans rstnysafgp
      541 eevaayelgf ksqfwdnrar lnlavfdsti ahkqmdfslp fdpnsgetrt tmvttnalsd
      601 gksrgaelef nvmpvdnltl glnyaytkid aqtatdpfga gvqvtvqpll apknagslsv
      661 dylvpfanfs alkfhvdgnw sdgyytseyd qmltdssfvv narvalvdvp vnstgatmsf
      721 slwarnllde qhlfykinsa algqsgifnd prtfglemav nf
//
LOCUS       WP_010485541             250 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Pseudomonas sp. S9].
ACCESSION   WP_010485541
VERSION     WP_010485541.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..250
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=26664
     Region          9..246
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 msrlpiigvt sdtkqigphp yhvtgdkyvr avvlgaaglp viipslgell dqptlldnlh
       61 gllftgspsn vephhyngpa sepgtlhdpa rdsttlpllk aaiaagvpvl gvcrgfqemn
      121 vvfggtlhqk vhevegfmdh repqdeplev qyaprhalhv qpggilagig lsaqievnsi
      181 hgqgvqrlap glrvealapd glieafsveg aksfalgvqw hpewqvrsnp nylaifqafg
      241 eacrkragqr
//
LOCUS       WP_010485571             139 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RidA family protein [Pseudomonas].
ACCESSION   WP_010485571
VERSION     WP_010485571.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..139
                     /product="RidA family protein"
                     /calculated_mol_wt=15334
     Region          26..135
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mpthtrirmf ntkdtypnqs ldndlcqavr agntvyvrgq vgtdfdgnlv glgdpraqae
       61 qamknvkqll eeagsdmshi vktttyltdp rfrepvyqev gkwlkgvfpi stglvvsalg
      121 qpqwlmeidv iavipeeqa
//
LOCUS       WP_010485586             464 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Pseudomonas sp. S9].
ACCESSION   WP_010485586
VERSION     WP_010485586.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..464
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50862
     Region          1..463
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mtnpalidel kslvevgkvl tdadsldayg kdwtkhfapa plaivfpksv eqvqaivrwa
       61 nqskvalvps ggrtglsaaa vaangevvvs fdymnqilgf nefdrtvvcq pgvvteqlqn
      121 faeeqglyyp vdfasagssq iggnigtnag gikvirygmt rnwvaglkvv tgtgelleln
      181 kdlikdatgy dlrqlfigae gtlgfvveat mrldrapqnl tamvlgaadf dsimpvlhaf
      241 qskldltafe ffsdkalakv margdvppaf etdcpfyall efeasteeva naaletfehc
      301 veqgwvldgv msqseaqlqn lwklreyise tishwtpykn disvtvskvp aflhdideiv
      361 gehypdfeiv wfghigdgnl hlnilkpenl skdeffakca tvnkwvfeiv qkyngsisae
      421 hgvgmtkrdy lgysrseaei aymkpikavf dpngimnpgk ifae
//
LOCUS       WP_010484721             408 aa            linear   BCT 01-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Pseudomonas sp. S9].
ACCESSION   WP_010484721
VERSION     WP_010484721.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..408
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42533
     Region          21..408
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mqptastldt apgqqrsvmr gaifimatss igpafltqts fftakymasf afailislli
       61 digaqlniwr ilsvsnlrgq dvankvlpga ghlisgfivl ggiafnigni ggaglamnvl
      121 fdvppvlgsi iaavaiigif mmrnaarvmd kvmqllglvm lcmigyamlq snpplleals
      181 qsinpddpml lllpivtlvg gtvggyisfs gghrlvdagi tgienvgavt raavigiatt
      241 gavrvclfla algvvsqglm ldpgnpaasv fshsmgtigy kmfgvvllaa sitsvigaay
      301 tsvsfmyslh esikrhnqrv viafilcstl iyslvgkpvk vlvvagtlna lvlplalgci
      361 liaakksniv gkdyrhpnwm lgfgilavia tcvgvalsfn sfikfwms
//
LOCUS       WP_010485644             724 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Stenotrophomonas geniculata].
ACCESSION   WP_010485644
VERSION     WP_010485644.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..724
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78842
     Region          32..699
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 migallasgp vlaqeapqat ptagrtaspt nldsikvtar kreetlqevp vavtaftsea
       61 ldkmnvqdis dldaqvpnlt iyaargasst vtayirgigq sdptwgadpg vgiylddvyi
      121 arpqgalldv fdvsrievlr gpqgtlygkn tiggaikyis rglptqadgf aqitvgnysq
      181 ldakaaiggp iggadsglra rvavasmnhd gfgentfngq pvsdkqinaa rlnlgayagd
      241 dfdvqfaldw iddqsgmrgs kmlapnpflr ayppmdsryd irsgmrnlnn veskgasatv
      301 nwrpnedial kyviakresd seanidfdta pvkladvggt yhddqvsnev qlnydaggrv
      361 rgvvglyqfs geaggqiqnn yfsaqfadnq gkvltdsial yadwtfdlts rlkldvgary
      421 tdedkraivl nrlyadpgfs rpvavtadfd kktnfknvsp kvsldyqitp dimvyglatr
      481 gfksggynir anavavprsa epfddetvds yevgskmafl dqrlflnlsa fynkykdiql
      541 svftgldtng dgiddsffgd ftnagagtvk gleveyqylp sqhwlisgnl awldtkydey
      601 mdrginvarq mkftnapefs gafnveyrtd langsnlsar vsysyqsevw pttdlspvir
      661 qqgyglvnag viwrlddawt fslqgtnlad keyrttgyni pavgtligfy gppreyslsv
      721 rydf
//
LOCUS       WP_010485620             236 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Stenotrophomonas geniculata].
ACCESSION   WP_010485620
VERSION     WP_010485620.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25715
     Region          2..236
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mltathlvke hgthralddv sftvapgeif cllgangagk sttiklflgf leptsgsaev
       61 dglsawqrpq evrrrllyip envalydelt gyenldyfar laaveqrspa rlkdalrsag
      121 lapeafgrrv glyskgmrqk vgialaiike arallldept sgldptasae fhelivrqrd
      181 rgtailmath dlfrarevat tiglmqagrl crtldastit andleslyle emsrsa
//
LOCUS       WP_010485699             469 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar porter family MFS transporter
            [Stenotrophomonas].
ACCESSION   WP_010485699
VERSION     WP_010485699.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..469
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49610
     Region          16..458
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(28,146,149,153,276..277,281..282,285..286,382,
                     386..387,391,414..415,418)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 mnqaagsgen trlivlisvv atiggflfgf dsgvingtqd glhqafrsge wmqgfeiasm
       61 llgcavgafs agrladrlgr rnvlilsavm fllsalgaga avssgwfiaa rvvggfavga
      121 asvispayia evaparyrgr latvqqiaii tgltaaflsn yllaaaagas teplwggqaa
      181 wrwmfwmqaa psllflllll tipesprylv vkrrkddalr vltrllgsdk aratleeida
      241 slsndhhrpr lsdlksratg rirpivwvgv glacfqqlvg invvfyygav lwqavgfsen
      301 dallinvlsg alsigacvvt vllidrigrk pllwfgsagm slslalvvva fasgsladgh
      361 lqlpgrmgtl alvaanayvv ffnlswgpvm wvmlgemfpn qirgsalava gaaqwtsnfv
      421 vtvtfpmlla aaglaatygi ylvaavisvi fvvrhvhetk gkeleqmeg
//
LOCUS       WP_010485740             197 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Stenotrophomonas
            geniculata].
ACCESSION   WP_010485740
VERSION     WP_010485740.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21871
     Region          5..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mskattdthq kilataeali yqngihatgm dllvktsgva rksiyrhfen kddvaaaalr
       61 ardvrwlawf rqecdkadtp earilgmftv lkgwfqsegy rgcafintag evgdpadpir
      121 eiarnhkqkl ldytlelteq laveqpadla rqllvlmega itlsrvmgdy daadtakdva
      181 kllleqakrs awvpqir
//
LOCUS       WP_010485824             342 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Stenotrophomonas geniculata].
ACCESSION   WP_010485824
VERSION     WP_010485824.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..342
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37043
     Region          57..321
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mkhfvppsrr gplarglaal mmglllatpy ayaqqrnplq kightvldep aasyrfehfv
       61 vdspdqqrrw rvnlaipaka gktpspvlya ldgnavamvl dqpllaelat rkappvlvli
      121 gydndlrids kartrdytaw idraddesgt tqavgggaaa fldvierrik peverrarid
      181 aqqqalwghs lgglfvlnal ytrpaafqsy laaspslwws qgaalgdpeq qfvqnvhgqp
      241 aklwlmlgga ervgdrgkrd mnnprvvahl rriggatpda amqlserlak vpglsvqyre
      301 fdglghgpml pasfhaalhe lygvtdrsag dgapnggdna ae
//
LOCUS       WP_010485830             129 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF805 domain-containing protein [Stenotrophomonas].
ACCESSION   WP_010485830
VERSION     WP_010485830.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..129
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=14109
     Region          2..128
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mqemilplkr yaqfegranr reywmyqlfl flvatavmll agvlaillrn sadalagili
       61 gmvvllcvmw lvtivpliav tvrrlhdcnq sgwlfllalv pgggivimif sllpgtpqen
      121 vygpvpsgp
//
LOCUS       WP_010485948             248 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Pseudomonas sp. S9].
ACCESSION   WP_010485948
VERSION     WP_010485948.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..248
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=27649
     Region          48..241
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mtiwqrlkhq letlqpclkc llcdettesk rlpictdcer elpwlrahcs vcalpmhgae
       61 wicgecqknp psfdkvvapw sysfpvqgmi nrfkhqaqwp lgrllgdlls dhmqhsfadg
      121 lvrpdlllpv pltkqrqrer gfnqaqmlan slgkalhipl lshglsriid tpaqqgldal
      181 trkknlrnaf fvapevelqg rhlalvddvl ttgataqtls klllkagaar vdvyclartp
      241 kpgtlldl
//
LOCUS       WP_010485961             128 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Pseudomonas].
ACCESSION   WP_010485961
VERSION     WP_010485961.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..128
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=13622
     Region          1..128
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtdlpeelts safsqllgve plsvadgear vrleltdplr nrhkklhgga lfslidiamg
       61 lacssahgfd qgsvtleckv nyiraidqga vicvakvlhs grrtlvveaq vhqddklvat
      121 aqgtfarv
//
LOCUS       WP_010485981             186 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [Pseudomonas].
ACCESSION   WP_010485981
VERSION     WP_010485981.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..186
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20076
     Region          6..164
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mskqytvavl vgslrkasin rklalaladl appslqlkii eigalplyne didvepapda
       61 ytefrnqvka tdallfvtpe ynrsvpapmk naidvgsrpy gqsvfsdkpg avlsaspgav
      121 ggfganhhlr qsmvflnvqm mqqpeaylgg agsffddngq lsdsvkpflq kfidayakwv
      181 elhhka
//
LOCUS       WP_010485994             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Pseudomonas].
ACCESSION   WP_010485994
VERSION     WP_010485994.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..158
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=17906
     Region          7..>127
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mnkqpdarle ralatlalvi islislanvv vryftnasfa fteefsvfll viltfagasa
       61 alrrnrhiri gmlermfpal rtplivlqwl aavtvlgliv wyggqfalee yqwdsespgl
      121 glpnwwyvvw lpllallmlf rltqmtldrl rgrlsdep
//
LOCUS       WP_010486064             242 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Stenotrophomonas].
ACCESSION   WP_010486064
VERSION     WP_010486064.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..242
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26082
     Region          8..233
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtslravapt lqadalekgf msgdvqvpvl rglsldiypg eltlvsgpsg cgkstllsll
       61 sglsspdggr vhalghdvgh msrseverfr lhhvgfvfqg fnlfpaltal eqvqlplgyr
      121 gmsnresepl arkaleevgl shrshmrpaq lsggekqrva varafakspt lifadeptsa
      181 ldaengqrvi dilhryarah gatvlcvshd prlirhadrv iamedgmvrg drrqnqtves
      241 ap
//
LOCUS       WP_010486106             192 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Stenotrophomonas geniculata].
ACCESSION   WP_010486106
VERSION     WP_010486106.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..192
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21706
     Region          4..188
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mpvelpalpy lpgslqphls aqtvelhhvr hhrayvdavn agilgtewee asleeivrha
       61 qgtlfdaaaq awnhafywqc lrprgggepq grlgelvkrq ygdvqrlree fnrtalglfg
      121 sgwvwlvqhp ggqlglqatr nagtpltges tpllccdvwe hayytdyqnd raryldafwq
      181 mvnwefaesq lr
//
LOCUS       WP_010486108             423 aa            linear   BCT 01-JAN-2025
DEFINITION  YeaH/YhbH family protein [Pseudomonas sp. S9].
ACCESSION   WP_010486108
VERSION     WP_010486108.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11148708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..423
                     /product="YeaH/YhbH family protein"
                     /calculated_mol_wt=48446
     Region          13..420
                     /region_name="DUF444"
                     /note="Protein of unknown function (DUF444); pfam04285"
                     /db_xref="CDD:427839"
ORIGIN      
        1 msyvidrrln gknkstvnrq rflrryrehi kkaveeavsh rsitdmehge qisipgrdih
       61 epvlhhghvg rqtnvhpgnk efsagdlipr pqgggggqas gkasnsgegm defvfqitqe
      121 efldfmfedl elpnlvkrhl tgtdtyktvr agissegnps rinivrtlrs aharrialsg
      181 ssraklklaq aelerlkree pdnfgdiqal eeeisklhar inrvpfldtf dlkynllvkh
      241 pnpsskavmf clmdvsgsmt qatkdiakrf fillylflkr nydkievvfi rhhtsarevd
      301 eeeffysret ggtivssalk lmqevmaery pvnewniyaa qasdgdnwnd dspvcrdili
      361 nqimpfvqyf tyveitpreh qalwyeyqqv cdafadtfaq qqlvtagdiy pvfrelfqrr
      421 lta
//
LOCUS       WP_010486156             325 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF805 domain-containing protein [Pseudomonas sp. S9].
ACCESSION   WP_010486156
VERSION     WP_010486156.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..325
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34310
     Region          173..277
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mtqtrfkivf sgelmpgval etakdnlakl fksdsarvnt lfsgspialk rdlhedeadk
       61 ylaalhnagp katkepdlaa slslvdtdeh kqapesaetm qcpkcghrqd kaiecsacgi
      121 viekflarqa lqeqaaktas aattvapppa ahtpyappka pvgerlpefg elkpfttdgr
      181 igrlrflawt fvlmllcapi fgiaaagsai satvgailmi ivsialvivg vminvqrlhd
      241 igwsgwllfi tilpivgsif sllmlfmpgt qgpnrygppp ppnstsvkvl sgfvivcsal
      301 allgaiiall tipdalqllq sgavn
//
LOCUS       WP_010486179             433 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Stenotrophomonas].
ACCESSION   WP_010486179
VERSION     WP_010486179.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46559
     Region          16..419
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(28..29,32..33,36,75,133..134,136..138,141,161,
                     164..165,168,251,254..255,258..260,263,291,295,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mstitaaapp vnspsrvlla sligttieff dfyiyataav lvfphlffpd sseqaallqs
       61 latfavafia rpvgsavfgh fgdrigrkat lvaalltmgl stvligllpt haqiglwapa
      121 llalcrfgqg lglggewgga vllatenapp gkrawygmfp qlgaplgfll sagiflvlgr
      181 clsqddflqw gwripfvasa llvglglwvr lnihetpdfk kalerkapvr lpmwtvlrdh
      241 pvpmllgtlg afatfvlfyl mtvfslghgt avlgysreqf llmqmagmlf falgiplsar
      301 ygdrwgtrrt mivasvlivg fgvlfaplfq phspwlvtgf lclglflmgl tygpcgtfla
      361 eiypvevryt gaslsfnlag ilgaapapyl atwlaerfgl vavgyylclt avatlcalva
      421 lhrralrlnq rsa
//
LOCUS       WP_010486192             316 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Pseudomonas sp. S9].
ACCESSION   WP_010486192
VERSION     WP_010486192.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..316
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33788
     Region          1..310
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 masvlsiilp ifalilagfa crklkllgpe aaseinrmvv wlclpamlfe atatavwshi
       61 wqpgfiwvyi lgtllvfigt liwrlrksgd ladasiqgls asyantgymg iplcllvfgd
      121 dglepalias livicvlfal svvcievalq geknmlravr kvalalaknp lvispvlggf
      181 wavsgaplpe svhsfltlls natapcalis lglflahkqs gqsqgsvalv llklflhpll
      241 vwvlafwvfq lpplwamsav llaalptgtg pfmlaefyrr daavvsssil lstigslitl
      301 slclywieti rqasgm
//
LOCUS       WP_010486288             217 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Pseudomonas sp. S9].
ACCESSION   WP_010486288
VERSION     WP_010486288.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..217
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23561
     Region          60..190
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          117..154
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          159..187
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mptfirnaac illclaslpa lalssegqdn lkqlqqrwae inyslpadqr eaafeklsvs
       61 aeqavksepd saelliwngi ilstyagakg glgalglvkd akakleqalq idpralsgsa
      121 ytslgslyyq vpgwpigfgd dskaetmlkq alainpsgid pnyfyadflf rqkhyqdark
      181 falkaqqaap rpgretadkg rmqdislllk kidaele
//
LOCUS       WP_010486305             118 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudomonas].
ACCESSION   WP_010486305
VERSION     WP_010486305.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..118
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13283
     Region          4..105
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mpmqrhierh qlpyylkvyn rvtdkpmgyi gnvsvdgmll vsqlpmlvgg rfdmrikipg
       61 qsaqcfidft atcqwsredv tpgcydsgfs lvappteyie mvealrvyfs fhplsasa
//
LOCUS       WP_010486312             791 aa            linear   BCT 01-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Stenotrophomonas
            geniculata].
ACCESSION   WP_010486312
VERSION     WP_010486312.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..791
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=84762
     Region          19..782
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mgallaalap aaiqaadvsg aaataadvsg isadailppp tpltanqtly ldvalnstpr
       61 glmpfienrg rlqaspdvlr qlgfnangda pvyldqisga vvrydarlqt laldvpldql
      121 tlpttvlsrp qtrapagsas pglllnydvy gsrvdtlgnl slsselrlfg vgngtfenta
      181 vsrryqqpgd rrwrgesvrl dtrwsldfpd kamtlevgdf ysgfvdwtrp vrlgglqigr
      241 nyglqpyrvl tptpsflgqa vvpstvelyv dglrqysgqv pvgpfqlaaq pgisgtgnaq
      301 vvvtdafgrm qtldfsfygt qqllakglsd wsvgvghlrq dfgqrsfayd drtvasaswr
      361 ggisdtftge ahaeggggla qagiggwwll ggagvfnaay ahsnhhglqg gqwalgyswn
      421 nrrlnvnlrs vrshgdyrdl galqgnlpps iseqatvgld llrlgtlsas ylrlrypdge
      481 dnryaslfws rtwsqrwsay lsvnqnldqs ddrsiylsvt aslgnnrqas lssqrngdsq
      541 twvadvtqpv pgdgsaggig wraqvrhged gngglaevgi lndigrysfg asrqgglnya
      601 ygsasgslvw msghafatre vsdafavist ngvggvpvrl enrligvtdd rglllvspll
      661 swqrnrvsid tldlpeemra driedwvtpr qragthvtfq lrsrpslslt lqsmdgqple
      721 vgsevqlpdg rqatvgydgl lylediaags vlyittsrgq crvkvpdppk vvasgarpkp
      781 aplqcipeva p
//
LOCUS       WP_010486322             205 aa            linear   BCT 01-JAN-2025
DEFINITION  SOS response-associated peptidase [Pseudomonas sp. S9].
ACCESSION   WP_010486322
VERSION     WP_010486322.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..205
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=23067
     Region          1..205
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgryaffrw spafsglpgf psdqqphwsi spnsqvlllh reagesrlsr vrwgltpawl
       61 tdlsktpaqa raetvadqpm frdafrqrrg llpangfyew rgntrkrpyw lagdaptlyf
      121 aalweaypvd gavylsaavi tqaaanqrrp lilneaqqql wldeqtpldv lldilnspqp
      181 qlrervlanl vndpkldape cltpa
//
LOCUS       WP_010486371             118 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Stenotrophomonas geniculata].
ACCESSION   WP_010486371
VERSION     WP_010486371.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..118
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12827
     Region          1..>105
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 meyqgschcg riaftvqaea pisdvidcnc smcrrrgsll wfapreafql ttdpadvaty
       61 hfnkahidhh hcrecgvapy seavdrrtgt pmvavnvrcv pqvdlaglsv tsyngaal
//
LOCUS       WP_010486330             332 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Pseudomonas sp. S9].
ACCESSION   WP_010486330
VERSION     WP_010486330.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..332
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=35709
     Region          3..330
                     /region_name="rsmC"
                     /note="16S rRNA (guanine(1207)-N(2))-methyltransferase
                     RsmC; PRK09489"
                     /db_xref="CDD:181902"
ORIGIN      
        1 mdprsevllr qaqlfagpll laglpsddll ghlpnarsws whagdhglle srfagrnhfg
       61 vtpapvaapa avlflpksrd lteyllsala aqlaggdlfl vgekragier aakqmaafgk
      121 prkldsarhc qlwqvrvdnv ppapdleala qyyslqladg pltvaslpgv fshgrldvgs
      181 qlllqhldgl qpghmldfgc gagvlgsalk rrypdsrism ldvdafavas srltlahnnl
      241 eaevicgdgi daapfglsti lsnppfhqgv hthyqasenl lrqaarhlda ngqlrlvans
      301 flkypplieq hlgactilde akgfriydar kk
//
LOCUS       WP_010486508             554 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Pseudomonas sp. S9].
ACCESSION   WP_010486508
VERSION     WP_010486508.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..554
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60942
     Region          1..534
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msltydfvvv gagsagcvla nrlsengrys vclleagppd rypwihipig yaktmfhpvy
       61 nwgfytdpdp gmnnrriywp rgrvwggcss ingliyirgq qadydawaes gnqgwgwkdv
      121 lpyfrraenn dlgsgpthgt egplcassik arhpltegfi daakalgvpr tndfntgnqe
      181 gvgyyqlttr kglrcstava ylhparkrsn lsiislakvq kilfeakrat avvfekdghl
      241 qtiharrevi lsagalqspq vlqlsgvgpa ellkqfsipv vhelpgvgen lqdhlqirmi
      301 yectrpittn delrspwrkl rmglqwlftr sgplaiginq gglftrvmaq sktpdiqyhf
      361 gtlsadsagg kvhpfsgftm svcqlrpesr gyvrivssdp nqppsmqpny lsteldrqtv
      421 iagvrytrkl aetgplkeli krehlpgieq qsdeqilefc rqygatifhp sgtckmghdp
      481 mavvdsrlrv hgiqglrvvd csimptlvsg ntnvpvvmia ekaatmiled avkprpvvpn
      541 aiaaqsseal shal
//
LOCUS       WP_010486533             329 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Pseudomonas sp. S9].
ACCESSION   WP_010486533
VERSION     WP_010486533.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..329
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35044
     Region          45..299
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(60,144,146,148..149,177,231,252,255,268,270,299)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mttiqsftrr alltltvats tllaasasaa pvakqnnqvp gyyrmmvgdf evtalydgyv
       61 digtqllkga saddiqslla kmfldsskgv qtavnaflin tgnnlvlvdt gaakcfgpal
      121 gniqdnlkaa gytpeqvdtv llthlhpdha cgllsadgks aypnatiyip kgdadywlss
      181 aeqakapeat rgrfamsqka vapyaaadkm qtfnpdsklp egvavvpsng htpghtsymf
      241 sskgqdllvw gdivhshsvq fshpevtief dsdsakavqa rkklfaeaae dklwiagahl
      301 pfpgighvrk egdayawvpt efgpirsdr
//
LOCUS       WP_010486565             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Stenotrophomonas].
ACCESSION   WP_010486565
VERSION     WP_010486565.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20846
     Region          4..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 magrprefdr dqalrkamll fwqhgyegts msalvealgi asariyaafg skeqlfreav
       61 alyeegeggf apraleqatl reaigsmlre avmtytrrgr phgclvvssa ssvspdgegv
      121 rdwlashrrq rtaaiiarlq qaqaegelad daavqalgdh fatvlhgisv qardgisrer
      181 llamvdvalt plp
//
LOCUS       WP_010486610             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_010486610
VERSION     WP_010486610.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..254
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28812
     Region          14..252
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mseaikkpea vesmiqmqgv hkwygqfhvl kdinldvksg erivlcgpsg sgksttircl
       61 nrleehqqgr ivvdgtelth dlkqieavrr evgmvfqhfn lfphltvlqn ctlapmwvrk
      121 mpkrqaeeia mhylervrip eqankfpgql sggqqqrvai aralcmkpki mlfdeptsal
      181 dpemvkevld tmiglaedgm tmlcvthemg fartvanrvi fmdkgeiveq aepdkfftnp
      241 enertqlfls qilh
//
LOCUS       WP_010486673             164 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [Pseudomonas sp. S9].
ACCESSION   WP_010486673
VERSION     WP_010486673.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..164
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18737
     Region          7..146
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mrkrqlspqg dfpsaglprr faamfydfll cvallivvtf iyklilmgfy gaeqlkqmsd
       61 sgaldgdpil stllficlfg ffskfwtyng qtlgmqvwgv raqnadgtai slwqallrfm
      121 vsiaswlwlg lgffwvlidk qhrtwheiys esqtvqlpkn ihkk
//
LOCUS       WP_010486760             208 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhomboid family intramembrane serine protease
            [Stenotrophomonas].
ACCESSION   WP_010486760
VERSION     WP_010486760.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..208
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23229
     Region          1..188
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mtpvnlllia itailswmaf nnrkladrli lwppaidrhr qydrlvtygf ihadwshlif
       61 nmitlfffgg fiesvmvqlt gsyltypafy igallvsilp sylknqknpn ylslgasgav
      121 savlfafili kpwsiilvff ipapaivyaa fyvgysiwmd krggdrinhs ahlagaafgv
      181 ifmlamqpsi fthflrelsn ptfrlggg
//
LOCUS       WP_010486783             149 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Stenotrophomonas].
ACCESSION   WP_010486783
VERSION     WP_010486783.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..149
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16027
     Region          15..149
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msdhtsprvp ytrlaaeafk gllatsqavh dssidptlme lvflrvsqln gcgycmdmhg
       61 talrkggiep rkldtlpawh esrffdarer aalgwaealt rltdgapsqa afdalaphfd
      121 ekgisdlsmg iavinawnrl gagllpplp
//
LOCUS       WP_010485818             285 aa            linear   BCT 01-JAN-2025
DEFINITION  glycine betaine ABC transporter substrate-binding protein
            [Pseudomonas sp. S9].
ACCESSION   WP_010485818
VERSION     WP_010485818.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..285
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30965
     Region          31..285
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(40,42,88,116,146,150..151,196)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mrrikslclq glgvaalalg mssamaadkp elkigfvngw ddsvavsnva aevlesklgy
       61 svklqavepa imwqgvargd ldvtlsawlp tthgeyfkrf kdkvevlgtn yqgakigliv
      121 pdyfaaksie dlnkyskdid skitgidaga gvmrrtedai keynldiklm pssgpgmata
      181 laraekdkka ivvtgwiphw mfakwklrfl edpkkvfgdd ehvdtvanpa latkapdaaa
      241 flkkiswsge evgsvmlair egadpkdaak kwiadnperv aewlk
//
LOCUS       WP_010486844             298 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Stenotrophomonas geniculata].
ACCESSION   WP_010486844
VERSION     WP_010486844.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..298
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32447
     Region          15..139
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mvrvqqvsha dahvaihdvr qrvfvqeqgi aaelerdald pvsahvlald sdnqpvgtgr
       61 lapdgrigrm avlashrsqg vgeallealv eagrrlglae lhlhaqlpar dfyarqgflp
      121 egevfeeagi ghqqmrrrlg aagaidgrae avaittaiih rarrqlwlhs rqldpglldt
      181 ppvqaalrrf vtarhdkhlr vivhdaaava sagapllala qrlpsviqfr evtdpvdral
      241 asacllndag dfyfrlighr ldgeagialp arsqpfeqql qrvwdrsrdc selralgi
//
LOCUS       WP_010486956             298 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Stenotrophomonas geniculata].
ACCESSION   WP_010486956
VERSION     WP_010486956.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..298
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32073
     Region          10..220
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mdpiapslar lqqvqvryrd htalhgidlq vragqvlall grngagksta isvllglrha
       61 dagqvellgg dpqqrasrlg lgvmlqstnl ppmlqvdelv aqasacypdp mplpevlqra
      121 glqalarrry gqlsggqqra vqfaialcgr prvlfldept tgldiqarqa mwqairqlva
      181 egcgvlltth yleeaealaq rvvvleggrv ladaplaelr ladrprrirc rsalavedvq
      241 hwagvqqvqr dgehlqllas paepvvarll aadaqlrele vqgaaladaf ldltreaa
//
LOCUS       WP_010486960             438 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Stenotrophomonas geniculata].
ACCESSION   WP_010486960
VERSION     WP_010486960.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 438)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..438
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46177
     Region          86..278
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          191..437
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnkfkkwagn altvlllvig lvlwislpwi gvlavavlva lwllltrggr lalaatrigv
       61 aslpqrwgas svivvgiagv vgvlvamlam gegfqatlnn tgddttaivl rggsqaetns
      121 vitreqvptl stlpgitrda egrpllspel sqvvnlvsks dgtdvnaqfr gvgpqawavh
      181 dkvkivegrt fatglreivv gqgakgqfrd ldvgrtltlg nqtwtvvgvf atgdahdsel
      241 wtdadtlatt yqrsawqsis vrtdgkagfe qfkaavaadp rlkldvettr vyyskqgggl
      301 tklidilgkv igtimavgav fgalntmyaa vatrareiat mraigfrglp vvtavmletm
      361 llallggllg cavawllfng ysvstigsnf savvfkfhvs pellwtglkw algiglvggl
      421 fpalraarlp ittalret
//
LOCUS       WP_010486964             444 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Stenotrophomonas].
ACCESSION   WP_010486964
VERSION     WP_010486964.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..444
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48307
     Region          24..434
                     /region_name="MFS_KgtP"
                     /note="Alpha-ketoglutarate permease of the Major
                     Facilitator Superfamily of transporters; cd17367"
                     /db_xref="CDD:340925"
     Site            order(34..35,38..39,42,79,137..138,140..142,145,165,
                     168..169,172,258,261..262,265..267,270,299,303,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340925"
ORIGIN      
        1 msttsqpavp andraalrrs isntlkgsag nlvewydvyv ysvfavyfes qffspddkns
       61 tmyvwaifaa tflmrpigaw ffgrfadrhg rrlaltvsvt lmalcsflia itptaasigi
      121 waavillfar llqgfatgge ygasatymse aaipgrrgfl ssfhyvtlvg ghvlaqltll
      181 lmltfwgkpe isewgwriaf giggiaavvv fwlrrgmdes lsessieaar egkaqksgsm
      241 yelfvhqwrp lllcflitag gtvafytysv ngpkmiqsaf agndpmtgtl inlgvlaflm
      301 vlqpvggwls diigrktllv ffgvggvlys wylitqlphq hdatlafltl amafviltgy
      361 tsinavvkae lfpthvralg vglgyalans lfggtaplly qgalktghvd wfaiyvtati
      421 avslvvyvff ltnkgpnwld gtrk
//
LOCUS       WP_010487017             501 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [Stenotrophomonas].
ACCESSION   WP_010487017
VERSION     WP_010487017.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..501
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53288
     Region          8..484
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(65,67,71,74,78,111,114..115,124..131,136,139,142,
                     235,239,242,245,247,420,422..423,425..426,429,432..433,
                     435,437..440,449,453,455,469,476..481,483..484)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(151..154,162,177,180,210,227..230,233,251..253,285,
                     385,387,413)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(154,251,282,285)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mtvaaprirm lidgqfiesa tshwqdvinp atqdvlakvp fattgevdaa vaaakeafkt
       61 wrktpigtra riflkyqqli rehmselahi ltaeqgktlp daegdvfrgl evvehaaaig
      121 nlqlgelann vangvdtyti mqplgvcagi tpfnfpamip lwmfpmaiat gntfilkpse
      181 qdpmvtmrlv elaleagipk gvlnvvhgge evvnaicdhp dikavsfvgs trvgthvynr
      241 aslagkrvqc mmgaknhavv lpdankeqtl namvgaafga agqrcmaast lvlvgearnw
      301 vqdlvtkakt lkvsggtvag tdvgpviscs arerveglia sgveqgaklv ldgrkpqvdg
      361 fekgnfvgpt ifagvtpdmr iyqeeifgpv lvileaetle daiamvnsnp ngngtalftq
      421 sgaaarkfqe didvgqvgin vpipvpvplf sftgsraskl gdlgpygkqv vlfytqtktv
      481 tarwfddetl shgvnttisl k
//
LOCUS       WP_010487028             303 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Stenotrophomonas].
ACCESSION   WP_010487028
VERSION     WP_010487028.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32711
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,225,242,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnllqlirsf trtaetgsia aaarilgisa tavgqninrl eahlgvrlln rstrqlalse
       61 agalylaqvr hieadlaraq amvtagdiep agplriasss afgrhvlapl lpslqqrypq
      121 lqlelrltdr avqhgpeavd asirigaqle dgvvarqlar vpfvfcaspa ylkahgtpqq
      181 pselsghrgl lhrfptdgrp lrwgllkdgq rvdaalppsm vcddidalat laatgagitr
      241 laafvaepyl rdgrlqavfg adtawrpepm evyfcvsdrr dftakiralf ehlqagmapa
      301 wrv
//
LOCUS       WP_010487054             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Stenotrophomonas].
ACCESSION   WP_010487054
VERSION     WP_010487054.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21734
     Region          10..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maykrsalme erlagareri llatrelvat ggwrnapvta vatqagvstg liyrhfpska
       61 elfvevlnaa vahevaimer iasgpevase rlrlaitafv rralagpgla hafivepvdp
      121 eveaermrgr rafgdvflrl veegvaagel paqdahvaaa clvgafteam vgptapsrea
      181 hrdedalvda icsfclraig apakr
//
LOCUS       WP_010487036             211 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Stenotrophomonas geniculata].
ACCESSION   WP_010487036
VERSION     WP_010487036.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22372
     Region          4..210
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpalsdllaf alvslamvit pgpnmiyvis rsicqgpmag lislggvalg fvfymlcaal
       61 gitallmtvp faydalrigg alyllylawq alkpggrspf avrdlpqdsp rklftmgflt
      121 nllnpkvavm ylsllpqflh pdsegsvlmq sivlgstqil vsvsvngmia ltagsiagfl
      181 aahptwqmvq rwvmgtvlag lavrmtvegr r
//
LOCUS       WP_010487090             457 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Pseudomonas sp. S9].
ACCESSION   WP_010487090
VERSION     WP_010487090.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..457
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47747
     Region          2..448
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msnnkkfarv lgstdviala fgamvgwgwv vlagtmisna gtggtmlafa iggtavimig
       61 layaelaaam pqnggehvya hralgagasf fctwaiilgy vsvvafeava lptvleelip
      121 gykvglmysi agwevyftwa lvgivgaigm twlnirgvks salfqavitv lilavgimli
      181 sgslfngssa nteplfiggv ggvfsviimt pflfvgfdvi pqaaeeidlp frkigiiliv
      241 svlmavawyi limyatgral dvqalagskl atadaatavl ggswagkllv laglggilts
      301 wnafliggsr avyamaeakm lpaflaklhp tyktpvnail ligalsiiap lfgrqalvwl
      361 vdagglgivv ayamvalsfi vlrrnepdme rpfragrgpw vgyvalllsl glvllytpvs
      421 psallpvewl lvgvwailga vlygysrkay gsveigh
//
LOCUS       WP_010487098             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: O-methyltransferase [Stenotrophomonas].
ACCESSION   WP_010487098
VERSION     WP_010487098.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..192
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20718
     Region          32..190
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mlqalkdelt rfgadndare sargrrmlni tpetgeflsv lvrfgaarrv leigtsngys
       61 tlwlaeaaaa idghvttley aedkvamard tfarsgladr itlvhddagp wlalaadasv
      121 dllfldsdrg qyagwwpqlr rvlrpggllv vdnatshaeq meplrallea dpdfstslvp
      181 vgngellavr sa
//
LOCUS       WP_010487126             558 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Stenotrophomonas geniculata].
ACCESSION   WP_010487126
VERSION     WP_010487126.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..558
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60275
     Region          23..382
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          455..556
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 msaeanalpp revmefdvvi vgagpaglat airlrqraie agrelsvcvl ekgsepgahv
       61 lsgavmdpra ltelfpdwae rgaplkqkvt rdeflflset garstpnall pecfhnegny
      121 iislgevtrw laqqaealev aifpgfaaae vlygdngevi gvatgdmgie kdgsigpafe
      181 rgmalqakyt ifaegarghl grqliarytl degkdpqayg igikelwqid pakhepglvv
      241 haagwpldsd tyggaflyha dggkvaigyv vgldyknpwl spfeefqrfk thpsirkhle
      301 ggtrigygar aitaggllsl pktvfpggal vgceagylna srikgshaai ktgmlcadaa
      361 fdalaadrqh delsaypkaf easwlftelq qaknfkqwfk kgqtvatlmt gveqwllpkl
      421 gvrnppwtlh rtqpdhvcle paskhtriay pkpdgvltfd rlssvflsst nhdedqpshl
      481 tlkdpsipvk vnlaeyagpe arycpagvye fvgeadsarl qinaqncvhc ktcdikdptq
      541 nivwvtpqgg ggpnysgm
//
LOCUS       WP_010487134             211 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pseudomonas sp. S9].
ACCESSION   WP_010487134
VERSION     WP_010487134.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24033
     Region          4..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mklryddtrq hlldtghrmm vvkgftgvgl neilqaanvp kgsfyhyfks keqygqslle
       61 dyfrnylasm derfavtgnt arerlmgywq kwldsycepc ddqkclvvkl saevadlsep
      121 mrltlrdgad qiiariseci eqgqrdgslt mgdafhtata lyqlwlrasl lsklhlnsrp
      181 lknamattqt lltsdniwwr gcppvgghff h
//
LOCUS       WP_010487218             203 aa            linear   BCT 01-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein
            [Stenotrophomonas geniculata].
ACCESSION   WP_010487218
VERSION     WP_010487218.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..203
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=21650
     Region          1..197
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mqlsshsltn gapidrefaa gdaagfapdr nphlawngap egtrsfllvc vdpdvptvpe
       61 mvgrsdmtvp rdqprcdfvh wvmadipasv qeiaagscsd gfvvkgktap agpagsrqgl
      121 ndftgwfagn pdmagdylgy dgpyppfnde rvhryffrvf aldvaslelp arftaadayr
      181 amhghvlaea tlhgtytlnp alg
//
LOCUS       WP_010487224             438 aa            linear   BCT 01-JAN-2025
DEFINITION  bifunctional DedA family/phosphatase PAP2 family protein
            [Pseudomonas sp. S9].
ACCESSION   WP_010487224
VERSION     WP_010487224.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..438
                     /product="bifunctional DedA family/phosphatase PAP2 family
                     protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=46978
     Region          4..195
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
     Region          222..395
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(301,308,323..325,367,373,377)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mnqwidpltg wlssnpqwla aavflialte claivglivp gtfllfavaa magsgvlslg
       61 etlllayagg llgdalsyal ghffhkdirr lpglrqrehw leyaenyfqr ygiasllvgr
      121 figplrpmlp mvagmlnmpl prfilvslla aagwsvayll pgwatgaalr lplppgfwte
      181 aaivaagvgl fvliaaqsnl rdqrhaglit acsglialia mmigwphlde ldnglmtliq
      241 eqrgshadml aqsithlgdf ttqfaaaall clllvaakqw rsalfsamtl lgtalsntvl
      301 kltfarqrpe vlaeplssfs fpsghssaaf afflvlgvla grgqparlrl twsivsclpa
      361 lmiacsrvyl gahwptdiig gallastlca aslaisqikh pltplsmkaw wlivpactal
      421 lagisiwqls intlqyry
//
LOCUS       WP_010487316             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M48 family metallopeptidase [Stenotrophomonas].
ACCESSION   WP_010487316
VERSION     WP_010487316.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..259
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29934
     Region          19..251
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 msrllrrlis ptppatvqrd tvrlrledae ievlrvrdpr arriklsvde rgarltlppr
       61 aslamgerfl eqhrdwlalq lrqyqgqglp aplqpgedgv lplrgellpl rwqegryarl
      121 eidahgacvq wptrggdatl rrllrefyea qtradvgrwl pkylptlpra psrlrlkvms
      181 sqwgslapdg smaldlalvl grseafeyvl vhelchliqp nhspafwhev eqrfpawreq
      241 rdyfqlegrr lkamlrqll
//
LOCUS       WP_010487361             755 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Stenotrophomonas].
ACCESSION   WP_010487361
VERSION     WP_010487361.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 755)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..755
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82326
     Region          43..736
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msptrtsrgr lpvarplvaa lsallplvaa aqetpaakdp valdalqvta qrrvenakdv
       61 pvalsaiqge kldvlgsagd dirflaarvp slniessygr afprfyirgl gntdfdlnas
      121 qpvslvyddv vqespllkgf plfdlanvev lrgpqgtlfg rntpagvvkf dsarpsqdad
      181 gyvrvgygsy nswnvqgayg gpltdrwsar vsaiyqrrdd wvdntragap nsgfegydea
      241 agrvqflyeg ddfealfnlh krklngtarl franiiqkgg nglvenfdrd kvandgvnfs
      301 dletwggsar lqwnlgsvtl hsitgyetae slnrgdidgg ygeaslgagn ygpglipfas
      361 esadglphhr qwtqefrves newgrfdwqa gvfyfdedvt idsfnydslk pgnpqtghav
      421 qsqrnkawav fasgdfdvtd rfklrggvry tqdkkdftar vlqavpfgtp vsgpylantd
      481 vndvswdvsg vykltddina yarvakgfra psiqgrlafg gvsqadsekv isyeagikad
      541 lferrarlgl svfrynvdgq qliavggtnn tatllnadkt igqgveldle ayladnvllt
      601 fgssyndtei kdkdlavavc gggctvtdpi tmiggkpyal vngnplpqap kwihnatlrv
      661 gfplsdgsel yaytdwayrs avnffiyesp efrgrssleg glrlgynwdy gqydvavfgr
      721 nltnqtrvvg aidfnnltgf lneprtwgve ftakf
//
LOCUS       WP_010487396             236 aa            linear   BCT 01-JAN-2025
DEFINITION  2OG-Fe(II) oxygenase [Stenotrophomonas geniculata].
ACCESSION   WP_010487396
VERSION     WP_010487396.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..236
                     /product="2OG-Fe(II) oxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=26243
     Region          134..224
                     /region_name="2OG-FeII_Oxy_3"
                     /note="2OG-Fe(II) oxygenase superfamily; pfam13640"
                     /db_xref="CDD:463943"
ORIGIN      
        1 myeqgpvdfi evihnavpse vcaaiverlr atrglqpgav gsgvfpelkh skdlrisgld
       61 gwqdvdqqlq iavfngllty lrrypqalia plmlqiqdsn gqpqrlsaed fpdmppqqla
      121 dlartclrpg ainlqwyaag eggypywhce lypkdaqaet lhrhvlwtly lnddfdeget
      181 eflfqgrkia prtgslliap tafththrgn rpqggdkfia tswilfqsaq klfggg
//
LOCUS       WP_010487400             361 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Pseudomonas sp. S9].
ACCESSION   WP_010487400
VERSION     WP_010487400.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 361)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..361
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40650
     Region          89..354
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mpsflsgmer dpldtdfirm nfrsfvqrgi liimvvnplh alvlwlnhsa wwqlslmamf
       61 iqlpfyplcg qqrsfavflp svlalfsmva vyiwlfsehf gssagfhyli msliplvifa
      121 griglrlkvl icllmaigmf iaelklpgta tnsmsteale qlrilnllic fisismltft
      181 hfvtvsriqs klqylaaydp ltqlvnrrrm gqlaeqevlq srrqqyplsv iladvdnfkm
      241 indrhghpvg dvalqhvsel isaiardtds ccrwggeefl vllphtnlqg amqvaerirq
      301 qvaatplnah dlelemqltl gvamlmpnek laelikradt alyegkrasr ncvvksdpqs
      361 s
//
LOCUS       WP_010487423             281 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Stenotrophomonas].
ACCESSION   WP_010487423
VERSION     WP_010487423.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..281
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=29188
     Region          173..275
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 msasapvsap ppvppasaap ravsplagff idlgiaavtl fglslisgll wglyrgvvvg
       61 yanaqagaga peassvaasl gqpgalaqil malfatggaa lllyfwrrpa ntaerhasrq
      121 alrrpstwgw tllvatlivl gsngiaflak qfgiepvptn lalmqsaiar fplflvlfav
      181 vlapayeell frrvlfgrlw kagrpwlgvv lsslafalih eipgtsangp aeiaqlwlvy
      241 ggmgaafcwl yqrtgtlwaa iaahalnngv alaalvffga t
//
LOCUS       WP_010487432             343 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Pseudomonas sp. S9].
ACCESSION   WP_010487432
VERSION     WP_010487432.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..343
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38950
     Region          18..337
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mshfyaldnd qqvsclhela ntalhqwegs fseltlvkyr enavfsarrd dgqrvalrvh
       61 rhnyhteaal rselqwmeal aagglqgpev iptrdrqqlv svysesigep rhidmlawla
      121 gktlgtsehg vnaddstpdv fhaagalaar ihthgerweq pdefvrhawd eeglighqpf
      181 wgrfweldal ttdqrqllla arrraridlr rygrnlsnfg mihadlvpen llldkaklrl
      241 idfddagfgw hmfelatalf fclddprydq mqasllagyq svraltrqdl amltpfltlr
      301 gmtylgwvht ragsptalel tdfliertck lagryldsal pet
//
LOCUS       WP_010487433             426 aa            linear   BCT 01-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Pseudomonas sp. S9].
ACCESSION   WP_010487433
VERSION     WP_010487433.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..426
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46190
     Region          1..423
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mqtstllqrr fqvmgnqspl fyetplhlvr gegvwlydad grryldvynn vpsvgqfqph
       61 fvaalskqaa tlnihtryld egiveyaerl satfaeplnt lmftctgsea nelalriarf
      121 ttggsgvivs dynyhgntas laevttalps pepfarhara vpipnlyhap egmspeqmae
      181 qyaarvadai aslkadgiqp aallidtlfa neglprlpvg fvdkavalir eaggvfiade
      241 vqagfartge hlwghqahna vpdivtlgkp mgnghplagl vcsrerveaf grnamyfntf
      301 ggspvsaavg mavldviene nllanartvg ahlqqrlaql kdkheiigdv rgkglfyale
      361 lvrertrkep agiearrivn smrdrgvlis kigagdnilk lrpplvftqa nadlfvdtld
      421 dvlngl
//
LOCUS       WP_010487446             320 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TerC family protein [Stenotrophomonas].
ACCESSION   WP_010487446
VERSION     WP_010487446.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..320
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=35346
     Region          6..314
                     /region_name="R_switched_Alx"
                     /note="integral membrane protein, TerC family; TIGR03718"
                     /db_xref="CDD:274743"
ORIGIN      
        1 mqtignvwlw ggfaavvvia llvdlvlmrh ggphkvtfke alwwsigwva lallfnaglw
       61 yylnetagqv vankvglefl tgylvekala vdnifvflmi msyfavpeeq rqkvliigil
      121 gaivlrtimi fagsvlisqf hwllyvfgaf llftgwkmwf aagqepdlet npalrwmrkh
      181 lrllpdyagn alsvkrdgvr wftplfavli liavtdvifa vdsipaifai ttdpfivlts
      241 nvfavlglra mffllagmad rfhllpygla lvlgfigikm miidlfkipt pvslgvvavi
      301 iaatvvlslk yppkegegqa
//
LOCUS       WP_010487589             488 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Lacticaseibacillus zeae].
ACCESSION   WP_010487589
VERSION     WP_010487589.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..488
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53797
     Region          2..488
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mnnsegrtfm ghprglltls mtefwerfsy ygmrailiyy myysvekggl gfdqptalsi
       61 msiygslvyl sstiggfisd rllgsrrtvf wggvlimlgh ivlsipigsi glfgsivliv
      121 lgtgllkpnv semvgslype edlrrdsgfs ifvmginfgs liapifvpwm adkvnfhagf
      181 slaaigmfig lifyvvdgrk yinptdnvap dplkpedvrp lvlrvvgavv ivgvilavma
      241 gfkaltianv itlitvvaig lpvwyfilmi rskkvtkter srviayiplf laamifwaie
      301 eqgsvvlalf aaqqtkldfg ffkilpgnfq tlnplfilly gplfawlwmk lgkrqptspk
      361 kfylglifag asylwmvipv mlfgssakvs plwlvmswai veigemlisp vglsvttkla
      421 pkayssqmms mwfladasaq avnaqivrfy tpshevayfa ivglvsvafa iilafytpri
      481 eklmqgvn
//
LOCUS       WP_010487501            1050 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Pseudomonas sp. S9].
ACCESSION   WP_010487501
VERSION     WP_010487501.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1050)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1050)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1050)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1050)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..1050
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=117999
     Region          1..1044
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mtqqprserr tqnrvvalft dktrpdcldy dylgewskrg qnrnieaell qanlkqrgys
       61 dahisaalqr lmaaadatgi tlyqanlrty qllrygvpvq vavgqahetv hlvdwehper
      121 ndfaiaeevt lrggherrpd lviylngiav gvielkrssv dvgdginqli tnqeeifnlg
      181 ffstvqlvfa gsdsqglryg tattraeffv ewkatavnpe pdelniqrei panyhllpga
      241 elgqsgylld nplaqmceks rlldlirnfi ifdagikkvp rahqyaavka aqervrikeg
      301 gviwhtqgsg ksilmvliak wllehdpdar ilvitdrdel dkqisgvmrn agvigsdsps
      361 pritsradlv qklsattprl lcallhkfep dlsvppppmr gsfyvfvdec hrtqggdmnr
      421 qmkqwlanal figftgtpll rkdkqttrdv fgtyihtykf heavadkvvl dlkyeardvp
      481 arltsreaid awferatral nnyqksilrk rwatmealms aqerkqriia siiedfslkp
      541 rlnndrgtai lvaasiydac hyfrlfdgtm fgqycgivts yepnhnaisr epaksderyk
      601 fdtytqyvlk qgesttayee etkrrfieep anlkllivvs klltgfdaps csyiyldnel
      661 rdhnlfqaic rtnrldgddk dfgyivdfke lfgnvqdais vytsdeldid tggggsnnve
      721 lknwlvegkk qldaareals ylcapvappr eveqfihyfc gmaadangld etealrisfy
      781 kavasfvraf adlaqhltea gyseaeagrl qtevqfyadl reaikkhage eldikpfead
      841 mrhllntyiq adpadplstv dnfslvelii qtgvhdaiak klnakgqlsk daiaegiinn
      901 vrktiireql tdprfyegms rlledlikqs rddaaayeef lrkaevlvrl lghkgpgnsp
      961 aalnghrgat vlfnnldnid astfqcpqde dekvrlaldl dlamrgsapa swrgdtarea
     1021 qvlnalyplm grdrvatqai feiiknqsgy
//
LOCUS       WP_010487606             887 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation-translocating P-type ATPase
            [Lacticaseibacillus].
ACCESSION   WP_010487606
VERSION     WP_010487606.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 887)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 887)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 887)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..887
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95234
     Region          2..883
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 makkppyals sqevlqeeqt qltglsketa qtrlgengpn elaqaekksm larfldqfkd
       61 fmiivllaaa liagfllsew adagiilavv llnavfgvfq eskaeeaida lkemstpnah
      121 vrrgdqvlti pssqlvlgdi vlleagdvvp adlrlvesan lkieesaltg esvpvdksta
      181 pldaddvgig drtnmafmns nitygrgvgv vvatgmktev griagminaa eetttplqen
      241 lkslgktltv milviavivf avgiwrnaas lpemfltavs lavaaipegl paivtiilal
      301 gtqkmakrha lvrklpavet lgstdiiasd ktgtltqnkm tvekvyydgq lnnasdgihg
      361 gnplmtimnf andtqvqddg kllgdpteta lvaygktqsf dlnhaladep ridevpfdse
      421 rklmstlhrr adgkilvttk gapdellkrv telatgdqaa pmsdserdai lkankdmatq
      481 alrvlgmayk vidavpepvn setvennlif aglvgmidpe rpeaeaavae aksagirpmm
      541 itgdhrdtae aiavrlgiid qgdddavitg aeldqqsdee faknvgkysv yarvapehkv
      601 rivnawqkkg kvvamtgdgv ndapalkaad igigmgitgt evskgasdmv laddnfativ
      661 vaveegrkvf sniqkaiqyl lsanlgevlt lfmmtmlgwd ilapvhilwi nlvtdtfpai
      721 algveptepg imkqkprgrk snffsggvgp aviwqgileg lltlgvywfa itypvhsgqa
      781 amhadaltma yatlgliqlf hafnvksihq slftvgafrn kafnwailas fvllavtilv
      841 pgfnglfhvt tldwhqwltv lsagvtmivl veivkifera rrkrrgl
//
LOCUS       WP_010487681             452 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Lacticaseibacillus zeae].
ACCESSION   WP_010487681
VERSION     WP_010487681.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..452
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49718
     Region          23..438
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mgsdpdgqiw gqliliiflt linagfaaae iavvsssrtr mqaqadkgdr kaaklvaimk
       61 dssrflatiq vgitfagffa sasaattlad riapifgnws faheaavilv tlilsyfslv
      121 fgelypkqva lqraervakl svtpiswlat lmrpfvwlls astqllmklt pmefthqges
      181 vtreemvami engrnagaid pdeyqmfegi islsdtmare vmvprtdafm idaeepdqka
      241 idailnniys ripvyeedkd hvigivhikn llkearrvgf ehvkiesvmt epvfvpetit
      301 vdallkemqt rqqqiailld eyggvvgivt iedlleeivg diddesdqae qlytkqtehd
      361 yvvsgrmpis efndlfktsl dvpdvdtiag yvltqlgaip sthhseklel apgvvlstgk
      421 vegsrlvnvh ihltdmptle tstevssket ds
//
LOCUS       WP_010487690              90 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HU family DNA-binding protein [Pseudomonas].
ACCESSION   WP_010487690
VERSION     WP_010487690.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..90
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9525
     Region          1..90
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mrkpelaaai aekadlskdq anrvlnavle eitgalnrkd svtlvgfgtf iqrhrgartg
       61 knpqtgepvk ikasntvafk pgkslkdavn
//
LOCUS       WP_010487733             339 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Pseudomonas sp. S9].
ACCESSION   WP_010487733
VERSION     WP_010487733.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..339
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=37670
     Region          51..319
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(51,75..76,111,116,121..122,125..126,138)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(58..59,61..64,66,85,87,119,137..140,144,146,184,186,
                     188..189,191,200..201,204,226..229)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(58..59,61..64,66,85,87,119,137..140,144,186,
                     188..189,191,200..201)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(62,144,146,184,186,188,204,226..229)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(200..206,212..213,222..229)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mtsqnaadqp valndepndl tyfafaenaa rsappqapeg lsemaeilgs ryklerllgv
       61 ggmgvvyrar dllreqfgdp dpyialktvs ddfaeypdan allfsefalt srlqhanvvr
      121 vfnfdvdiss krafitlell kgptldqllc dkphglpwde lrsiaiplie alhyshqkgv
      181 lhgdikpsnv lladdglrlf dyglgqpmeg lltglprlsr trfnawtpry aalelinges
      241 ltpaadiyal acvllelsng khpfqrlsar qamnikldqq lqrpdkipql cwdallkaia
      301 fepqhrsqcc tellhafqrp eparrtgwln hfsskgtqg
//
LOCUS       WP_010487781             160 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA thioesterase [Pseudomonas sp. S9].
ACCESSION   WP_010487781
VERSION     WP_010487781.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..160
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17929
     Region          5..147
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mapgnaqlsm tvlmtpdman fsgkvhggtl lkyldevaya casryagcyv vtlsveqvtf
       61 repihvgelv tflasvnftg ttsmevgikv vtenirersv rhtnscfftm vavdeqgrsi
      121 kvpprqpetp eeqrrftkgq qrrairqeme hrykqlkeqg
//
LOCUS       WP_010487810             743 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Lacticaseibacillus zeae].
ACCESSION   WP_010487810
VERSION     WP_010487810.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 743)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 743)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 743)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..743
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79402
     Region          <24..>78
                     /region_name="PRK10965"
                     /note="multicopper oxidase; Provisional"
                     /db_xref="CDD:236810"
     Region          102..739
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     Archaeoglobus fulgidus CopB, a Cu(2+)-ATPase; cd07552"
                     /db_xref="CDD:319850"
     Site            order(392,394,696..697,724,728)
                     /site_type="other"
                     /note="putative HM ion binding site [ion binding]"
                     /db_xref="CDD:319850"
     Site            order(436..438,501,517..519,546,586..588,608,611,614,632,
                     635)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319850"
ORIGIN      
        1 mknskmehan ettgktsemq hddmadmpmd heqmghqagm etmamdqgam ahgqmnhgdm
       61 hmshgdmshm dmhhgdmshm dmdhggghmm hmgnlkqkfw vslivmipvl llsqfmgmni
      121 hlgalqlpiv fpgsdwlvli lssflffygg wpfltgakse lqqrqpammt liamgitvay
      181 gyslyafvmn hfiapngmvm dffwelatli vimllghwie mnavmaagna veklaallps
      241 qahvvhgdhv mdmplaevqv gtrlrvlage qmpadgqivs gsssvneslv tgeakaihka
      301 egdrviggsv ngdgvieikv tgtgesgyls qvmklvqsaq ankskaegma dkvagwlfya
      361 alavgilaff iwlsdgaaia fermvtvfii acphalglai plviarstsi gatngllirn
      421 rqaletakha kfilmdktgt ltegkftvak tvafanhdea qvlalmaale shsehplatg
      481 ikaaakeqql nvpaaqnvqv lkgiglqgev dgqaytivna rylkdhqlsy dqaqadqlaa
      541 agnslafllq kdqvlgmvae gdqlkpsskp fvaalkrqgi tpvmltgdnh etakkvadql
      601 gltdfqaelk pedkvaqvka yqqrgvvmmv gdgvndapsl aqadigvaig agtdvaidta
      661 dvvlvhsdpa dilnflslak atnrkmvqnl wwgagynila iplaagilap igfilspavg
      721 aaimslstiv valnamtlhl nra
//
LOCUS       WP_010487818             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Lacticaseibacillus].
ACCESSION   WP_010487818
VERSION     WP_010487818.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28082
     Region          2..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mailevsnls kifgqrhdrv ralndlsfqv aagefigimg psgagkstll nilatietps
       61 tgkvkiagyd lealnesqqa afrrdhlgfv fqdfnllddm tvaqnvllpl tlqrhvqpdr
      121 aerlrtvsqh lnldpllkaf pgelsmgqrq rvaaaravit qpsllladep tgsldslaat
      181 dflrylqqln qqekttilmv thdpftasfa sriifikdga ffaevtrgks reqffdriid
      241 meatvsgggh srvatd
//
LOCUS       WP_010487852             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HIT family protein [Lacticaseibacillus].
ACCESSION   WP_010487852
VERSION     WP_010487852.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..144
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15953
     Region          3..138
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 midcifckiv rneipnvpvy eddvvkafld itqvtpghtl ivpkkhvpdi faydtdlaaa
       61 vfervpkiar aikasnpaik gmnilnnngk vayqsvfhsh ihliprysdq ddfgmhfgdh
      121 saqydnakle avaakirnql eaqa
//
LOCUS       WP_010487881             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParB/RepB/Spo0J family partition protein
            [Pseudomonas].
ACCESSION   WP_010487881
VERSION     WP_010487881.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..290
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31963
     Region          32..290
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 maakkrglgr gldallggts vdalqeeaak vdsselqylp ldlvqrgkyq prrdmdpaal
       61 eelaqsiksh gvmqpivvrp vdqgrfeiva gerrwrasqq agldtipamv reladeaaia
      121 malieniqre dlnpieeama lqrlqqefql tqqqvaeavg ksrvtitnll rlialpeeik
      181 tllshgdlem gharallglp aeqqvegarh vvargltvrq tealvrqwls hkeepkavak
      241 vdpdisrleq rlaerlgspv qikhgqkgkg qlviryssld elqgvlahir
//
LOCUS       WP_010487956             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Lacticaseibacillus].
ACCESSION   WP_010487956
VERSION     WP_010487956.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..135
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15889
     Region          36..125
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mltyllifvg lfliywgfsw lwsyyqkskf kaiggeispe efehtmrkaq iidlrernef
       61 kaghilgard lpytqlrerl gemrkdlpvy lydktgvlsl raarrlrkng fekiswlkgg
      121 ydnwsgkikk sptny
//
LOCUS       WP_010488117             180 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: gamma carbonic anhydrase family protein
            [Pseudomonas].
ACCESSION   WP_010488117
VERSION     WP_010488117.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..180
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19386
     Region          1..174
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 msirtyqqft pqlgerafvd ssavvlgdve igddssvwpl tviradmhsi rigqrtsiqd
       61 gcvlhithag pfnpagypln igddvtiahk vtlhgcsigs rvlvgmgsiv mdgaviedev
      121 vlgagslvpp gkrlesgfly vgsparqvrp lsdkersyfc yssknyvnlk dqhlmegygh
//
LOCUS       WP_010488130             141 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Pseudomonas sp. S9].
ACCESSION   WP_010488130
VERSION     WP_010488130.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..141
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14591
     Region          3..136
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mkktasahwq gsikqgkgti stesavlsks pygfntrfkn epgtnpeeli gaahagcfsm
       61 alslqlgeag mtaesidtka evtldkdgdg fsitavhltl hakvpgadra afekavqnak
      121 tgcpvskvln atitleatle t
//
LOCUS       WP_010488145             133 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Pseudomonas sp. S9].
ACCESSION   WP_010488145
VERSION     WP_010488145.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..133
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14644
     Region          5..127
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mtqlhsggcq cgamryqfda plqdiahchc svcrrssgai vttwitvpla sfawlkgear
       61 qyassasctr yfcadcgaql alfttlspht ldvtiatldh pelaaadrhi wvqsrlpwlr
      121 ldpelpeekq kll
//
LOCUS       WP_010488179             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010488179
VERSION     WP_010488179.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 265)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..265
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29326
     Region          4..265
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 malsmarsvw tyrgfvlgsv krefqtryqn sllgaawsvl nplsmiivyt vifsqlmkar
       61 lpgvdnglay giylcagilt wgffaeiigr sqsvflehan likklsfpri clplivvlna
      121 gvnfaiifal flgflvatqn fpgwavlavi pllmiqvlfs iglgvmlgvl nvffrdvgqf
      181 vgiflqfwfw ftpivypasi lpdwvkplls anpmapliag yqgifvygnw pdwsslvptv
      241 iiagalcgla mrlfrkrsge mvdel
//
LOCUS       WP_010488241            1179 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Lacticaseibacillus zeae].
ACCESSION   WP_010488241
VERSION     WP_010488241.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 1179)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1179)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1179)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1179
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..1179
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=132157
     Region          4..1152
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mglqfilgda trdhaqtmat miqeqlaadp qnqifflvpn hikfeaeidl lkrlrqlqqg
       61 eanayaqsrv qvlsfsrlaw fylkntplyq qprldqasnt mlvakiladr qddltiyage
      121 aqhtgfvtql adqlselmig ritaedlmht vsalapgnrh raklrdlgii ldqyeaeigp
      181 yattasllsg lqqamrtqdl shtfiylnhf nvfsasesal vetmletaae vtlglvlnkp
      241 yplnppvapn lflpagrlyq rlyqkaktlq vpirpdrfaa prqisrgmqq vanwweantd
      301 lqpstaptse taeqihlaia tdpyqelrhv aqhiyravrh garyrdflil arrlepyatv
      361 ipaifaefsi pqftdlqrpm kdhplvvlme slfaiqkhdy qyqdvmrllh telllpegmt
      421 laefrdavdt tdnhlvrtgi agkqrwtqaa awryfqrnpd addpqmdpea vktaqinaik
      481 tliaqtvptl lkqwqtaktg aeaasdlyrw ldangvvdql rawrqtasde gdltrsrahe
      541 qawttftall ddyvtilgsa kfdreqfhel laagfasaty tqipatldav visetglvrl
      601 akakhvfvig atntampdvp tddgvlnsee rqllaaqlpd drflpeqgpa ttlgdpfiny
      661 lgfmaasdel tlsypvqnaq ennenqaspy fqqmgnalhl tptawapvsl ttpvetvlgs
      721 pramlsdfvr aagdaqqqkl plgkawqnvl aalkqtalat lsrrlsgslt yqndpghldp
      781 dlaiqlygrd mnvsvsrlet yylnhfeyfl kyglllqprp efelspadtg slfhavldry
      841 ltqlreehmt ladvdpsais aavpplvedi asqpgyeilg sthrmlyltr rlsqlliqvl
      901 vnmrqqqqrs gfrpmrtelq fgrigdtkgl pglswplphg grvnvrgkid rldvyrepda
      961 rrfiivdyks tqhrfndsda yygialqmlt yieamtnvpv dppfvaagal yfhlqdptlq
     1021 ytptlepvie rlkkfkylgf lvanhgdelt avdrtispes ggasevaplg fkkdgsfnrs
     1081 qsniltpddl raylahnqal iidaatqils gnidltpfqy gqssevvsrs dyqsimlfdp
     1141 atgfdhyhhv pklkrkdvin rlttdpkqtp dskketpqs
//
LOCUS       WP_010488266             337 aa            linear   BCT 01-JAN-2025
DEFINITION  lipoate--protein ligase [Lacticaseibacillus zeae].
ACCESSION   WP_010488266
VERSION     WP_010488266.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000589
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..337
                     /product="lipoate--protein ligase"
                     /calculated_mol_wt=38379
     Region          2..249
                     /region_name="LplA"
                     /note="Lipoate-protein ligase A [Coenzyme transport and
                     metabolism]; COG0095"
                     /db_xref="CDD:439865"
     Region          251..335
                     /region_name="Lip_prot_lig_C"
                     /note="Bacterial lipoate protein ligase C-terminus;
                     pfam10437"
                     /db_xref="CDD:431286"
ORIGIN      
        1 myyvimkshd irenlateqy lmnakqfdep lllfyyekps vivgrnqntl eelnqkyvee
       61 hnivvtrrls gggavyhdlg nlcfsfvvds dseefgdfks ftqpivdaih tmgatsaevs
      121 grndmlvdgk kfsgsamytr ngktfshgtl mldvdmsvip kvlnvpedki kskgiksvks
      181 rvtnlrpyld kkyqdmtlpe frdilltrlf gvddvaeikd keyhvtdadq veikkiyddv
      241 ynnwdwvygh spefttkkrk hfdygtidar fdikdgkian vkfygdffgp kdvadvaaal
      301 kdkpytsqav ketldgintn dyftnipkdd vinllvp
//
LOCUS       WP_010488336             400 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Lacticaseibacillus zeae].
ACCESSION   WP_010488336
VERSION     WP_010488336.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..400
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43815
     Region          14..392
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(22..23,26..27,30,62,117..118,120..122,125,145,
                     148..149,152,228,231..232,235..237,240,264,268,321..322,
                     326,330,346,349..350,353..354,357)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mgqskigwqg qtaafllsqn lfvfgtstvf favlwdialk tssgawmtyv slatslpail
       61 islsagvlad rynrkwlivl savavtvltl vvayvfafvt qelwlllvia virsfgngle
      121 npaanallpq lvpakqitrv ngynqilmaa mlvmspllag yilsdlgifw ifvidaltaa
      181 lavlclsvvh vptptarrdr askrqngila glryvgntpl llafmlftga afiliapssq
      241 lstlyvnrtf gsevwyltfn ewswtigagl gglfiarhkk frdqlgliai gfagsgiafa
      301 emglkqpfit ylffmfisgi fypliqagqt iylqenvpad klgrvfslwa ilstgiypla
      361 mlaygpladr vpigwifivt gllligvayw fwqrlkklsw
//
LOCUS       WP_010488361             644 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudomonas sp. S9].
ACCESSION   WP_010488361
VERSION     WP_010488361.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..644
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=67230
     Region          209..644
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mfaiasllrs rllrpvfial glallvqvlv avvltrttvs tlvedlsarl gsdtrqlstd
       61 leaasaevrg gleglssrtq aslgaglker lsaeqvqlrg ilesnlkqsa ddlaqllaav
      121 apkaiwdndv paltelvrma hrnsnvlfav yvdaggerlt rhvnrtderv kaliakgqgr
      181 gsldkllnaa asdpgvyvve asinpmgsei gkvilgvstv dvdkvvtqld qrfaaliqss
      241 gqlvsdglsa aasdsaaala srlkgaqqta kamaensrqa iesaaqslrw nisiglglvg
      301 lvillvlalv lgrrvvsklh tliavmddwa agegdltrrv qmnsrdeigd maavvnrfvg
      361 klqpivreag diavrtgvei eslavrsaaa evsaarqrde vagslqalaq madeaqaesq
      421 smqealqrvg sirqatedns aiarrvggsi aelvdsvdtg aaviqrlarq seqievvltv
      481 ihgiaeqtnl lalnaaieaa ragesgrgfa vvadevrala sktqqstgdi qahigalqqg
      541 areavsaieq asrqaaqgla alneserlqg svqvsveevh gainaaagaa rhqaegavav
      601 rrrvevihae sqraaeavaa taksgrvldg lasqlslslg qfkv
//
LOCUS       WP_010488407             161 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase [Lacticaseibacillus zeae].
ACCESSION   WP_010488407
VERSION     WP_010488407.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10082841
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..161
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005542 - folic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18159
     Region          6..160
                     /region_name="DHFR"
                     /note="Dihydrofolate reductase (DHFR). Reduces
                     7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH
                     as a cofactor. This is an essential step in the
                     biosynthesis of deoxythymidine phosphate since
                     5,6,7,8-tetrahydrofolate is required to regenerate 5;
                     cd00209"
                     /db_xref="CDD:238127"
     Site            order(7,14,44..46,65,99..102)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(22,27,58,98,104,117)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mteflwaqdr ngiigkdghl pwhlpddlhy fraqtvgkim vvgrrtyesf pkrplpertn
       61 vvlthqvdyq apgavvlhdv pevfayakqh pdqdlviagg aqvftafknd vdtllvtrla
      121 gsfdgdtkmi pldwdaftkv ssrtvedvnp dlthtyevwk k
//
LOCUS       WP_010488450             401 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Pseudomonas sp. S9].
ACCESSION   WP_010488450
VERSION     WP_010488450.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..401
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42916
     Region          1..395
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnldipkkfs glvsqahqva eryyrpisrk ydkaehsypr eldllaglld gmnasspeav
       61 gatsaskrsv gnqdhanqng gnmaallgim elcwgdvgll lamprqglgn aaiaavanpq
      121 qlerfkgvwa amaitepgcg sdsaaihtta tklgdeyvln gekifvtsge radavvvwat
      181 ldkalgraai ksfvvekgtp gmtvtrlekk lgikasdtas isfndcrvpa snmlgrpevd
      241 vekgfagvme tfdntrplva gmaigvakas ldrtrqllgk scpldysapl lsvshaearl
      301 yeleanwqaa rlltlkaawm adnrianske asiakakagr manevtltcv elvgalgyge
      361 dellekward skildifegt qqiqlliiar rllgktssel k
//
LOCUS       WP_010488501             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Lacticaseibacillus].
ACCESSION   WP_010488501
VERSION     WP_010488501.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..249
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26890
     Region          1..227
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlteerrqyi lsqlqqhtvv kskalmaald asestirrdl deleaagelk rihggakrin
       61 glgdepdvas kstqnlrakq aiaraaahqv eqddlvflda gtttaqlipf ladlgvtvit
      121 tgvdnaslla dyqiptlmlg gmvksatkal igattaealh hyrfdiafig tngihpefgn
      181 ttpdpeeavi krlaihqarq pmiladpskf eqvsfvkfad igdvtiltss lqglpagyhr
      241 fqnikevhs
//
LOCUS       WP_010488519             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Lacticaseibacillus].
ACCESSION   WP_010488519
VERSION     WP_010488519.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..248
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27191
     Region          6..245
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mqhkpliqin hltkkfgdnv vlndisetin qgdvivviga sgggkstflr slnllnrptq
       61 geilfegtnl vdlsekqldn vrekmgmvfq sfnlfpnmtv leniklaplk vktvtdeeat
      121 ktakelleqv glgekadayp aslsggqqqr vaiaralamh pdvmlfdept saldpemvge
      181 vlkvmqdlak tgmtmvvvth emgfarsvad qvwfmdggki lekgtpeelf ehpkeartqd
      241 flskilaq
//
LOCUS       WP_010488520             826 aa            linear   BCT 01-JAN-2025
DEFINITION  penicillin-binding protein 1A [Pseudomonas sp. S9].
ACCESSION   WP_010488520
VERSION     WP_010488520.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..826
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=90551
     Region          2..826
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mmrllkffaw scvaifcgll lslsgaflyl spslpsvdsl rsiqlqiplr vfssdgklia
       61 efgemrrspi efkdippdfi nallaaeddn fehhygvdps slmraatqil ksgqiqtggs
      121 titmqvakny fltnersfsr kineillalq ierelsknei lelyvnkiyl gqraygieaa
      181 sqvyygkpig eltlsqlami aglpkapsry nplvnptrak errdwilgrl hllgkideqr
      241 yqealaepvn asyhvaapel aapyiaemar aemvgrygsd aytegfnvyt tvpsnlqeta
      301 nsalrsglls ydqrhgyrgp esrlpgmtke twlaelakks qlgglepaiv tqveksgilv
      361 ltrdgkeeav nwesmkwarp flntnsmgpr pkqpsdvaqv rdlvrvqrqe dgslnfvqmp
      421 aaqgalvsld pkngailalv ggfsfeqsny nraiqakrqp gssfkpffys aaldkgytaa
      481 tlvndapivf assntdevwr pkndnntflg pirlrvalyk srnlvsirll qaigveyarn
      541 yatkfgfnkq dlppnlslal gtadltpmev aggwsvfang gyktepyliq kiddrhgktv
      601 ftanpptvps veqtedeqlq elaqdsagqa apeapalete vaapteatdp qapvepavak
      661 riidartayi mtsmlqdvik rgtgrralal grddlsgktg ttneskdswf sgynadyvtt
      721 vwtgfdqpes lgrhefggtv alpiwmkymg aalkdkpsnp pkeppgiltl ridpfsgrta
      781 spgtpgayfe lfknedtpps mgeidpnlgv pgsplpadds apidlf
//
LOCUS       WP_010488554             396 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: elongation factor Tu [Lacticaseibacillus].
ACCESSION   WP_010488554
VERSION     WP_010488554.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     gene            1..396
                     /gene="tuf"
     Protein         1..396
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43458
     Region          1..396
                     /region_name="TufA"
                     /note="Translation elongation factor EF-Tu, a GTPase
                     [Translation, ribosomal structure and biogenesis];
                     COG0050"
                     /db_xref="CDD:439820"
ORIGIN      
        1 maekehyert kphvnigtig hvdhgkttlt aaitkvlaek glakaqdyas idaapeeker
       61 gitintahve yetekrhyah idapghadyv knmitgaaqm dgailvvaat dgpmpqtreh
      121 illarqvgvd yivvflnktd lvddpelidl vemevrells eydypgddip vlrgsalkal
      181 egdkeqekvi melmdtidey iptpvretdk pflmpvedvf titgrgtvas gridrgtvkv
      241 gdeveiiglk pdvlkstvtg lemfrktldl geagdnvgvl lrginrdqve rgqvlakpgs
      301 iqlhnkfkge vyiltkeegg rhtpffsnyr pqfyfhttdv tgvielpegv emvmpgdnvt
      361 fevdliapva iekgtkftvr eggrtvgagv vseild
//
LOCUS       WP_010488665             216 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pseudomonas sp. S9].
ACCESSION   WP_010488665
VERSION     WP_010488665.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23677
     Region          6..146
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtglrarqka qrrqeiadsa lavfselgfs aatldqiatr agvssptvvn yfggkqeill
       61 ellrapdtaa ieriryraer asslvnalce idtevamlql eafppklwae iapaliagdl
      121 qdifkrwndg vvfelkqilh syqrigmlkl svsvdataci vsdlsnmafv rvvtqpqpdl
      181 hnhaiqmrkt fdvlcagiet tgesdllrpp aevsqk
//
LOCUS       WP_010488719             255 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Pseudomonas sp. S9].
ACCESSION   WP_010488719
VERSION     WP_010488719.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..255
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28392
     Region          18..219
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mneklqplkk qsralknsrt gtqddvvyah ifdaileqrl apgtklseea lgeifgvsrt
       61 iirralsrla hegvvllrpn rgavvaspsv eearqifyar rmveraitel avqyatvdql
      121 nelrqmvede qisfsrgdrg agirlsgefh lklaeaakna plvsfqrslv sqtsliiaqy
      181 esgsrshcsy dehnqlidai eardaeravs lmmhhmdhid sklnldedsa sddlhavfsh
      241 llqtkkkpgk ailnn
//
LOCUS       WP_010488750             217 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Lacticaseibacillus zeae].
ACCESSION   WP_010488750
VERSION     WP_010488750.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..217
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24275
     Region          49..138
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 mvaytiknyq pemleswlrc ralaymrssf qdeitaeket isddtgvslv aikdqqvigi
       61 aeaifldqgq araasyglpe gtvlttldtl avhpdyqhig iakallkqlr grlkmrggvl
      121 liytlddeaa nglyqaigar lcyqasivhg hssknhvpew thfrvtndkq vavydehdhe
      181 iaygqdmety yvgksenikq ltdvhkvvte nvytlel
//
LOCUS       WP_010488759             296 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lacticaseibacillus zeae].
ACCESSION   WP_010488759
VERSION     WP_010488759.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..296
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32439
     Region          5..219
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mttiiqtehl kfnydkkqvl kdinltvhsg eiigligvng agkttllnil lgllsgegav
       61 svfdkkpgdp nskarigsml qgdmiipgit vgdmlklaae qtehaldpds lladlnltql
      121 ktqrlgnlsg gqlrrvtfav aligqpdllf ldeptvgmda narkafwdqv eqlrqqgkti
      181 vitshyleei qqiadrllil qngrfifdgt lqqlqkqhlg atitcetdlq paifsgladv
      241 dqvhsmgdkl vihsrngdqt lkalvpmldr lhqislnres lediflqltk qevpqs
//
LOCUS       WP_010488791             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010488791
VERSION     WP_010488791.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22985
     Region          29..75
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          98..205
                     /region_name="TetR_C_24"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17932"
                     /db_xref="CDD:465574"
ORIGIN      
        1 mddlkaqavm qelvanglvt dpdsargkll qtaahlfrsk gyerttvrdl asavgiqsgs
       61 ifhhfkskde ilrsvmeetv ryntammqaa ldeattlrer vlalircelq simggtgeam
      121 avlvyewrsl sdegrahila lretyeqiwl evlaqakaeg yfkadpfiir rfltgalswt
      181 ttwfrsegpm sldqlaeeal slvlkd
//
LOCUS       WP_010488801             264 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Pseudomonas sp. S9].
ACCESSION   WP_010488801
VERSION     WP_010488801.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..264
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27899
     Region          9..258
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mqlpdlktll vnleqgvltv tlnrpesrna mslsmveelt qvfsqlnqdr qvravvlrga
       61 gghfcaggdi kdmanaravg idayrelnra fgsmleqaqr lpqvvialle gavlgggfgl
      121 acvsdvaiaa ddakfglpet tlgilpaqia pfvakriglt qarrlaltaa rfsgqeaarl
      181 glvhfseasa aaieqrldet laqikrcapq anaatkalll dtelqplgql lddaaqsfan
      241 avlspegieg tmafvqkrtp gwae
//
LOCUS       WP_010488827             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit beta/FixA
            family protein [Pseudomonas].
ACCESSION   WP_010488827
VERSION     WP_010488827.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26351
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkvlvavkrv vdynvkvrvk adnsgvdlan vkmsmnpfce iaveeavrlk ekgvaseivv
       61 vtigpttaqe qlrtalalga drailvesse elnslavakl lkavvekeqp qlvilgkqai
      121 dsdnnqtgqm lgaltgyaqg tfaskvevag dkvnvtreid gglqtvalnl paivttdlrl
      181 nepryaslpn imkakkkple sltpdalgvs tastvktikv eapatrsagi kvksvaelve
      241 klkneakvi
//
LOCUS       WP_010488864             350 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Lacticaseibacillus
            zeae].
ACCESSION   WP_010488864
VERSION     WP_010488864.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..350
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38170
     Region          7..343
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 msdqavvtlk dvdvefhgkt rsvhavdhvn ltvnrgdiyg ivgysgagks tlvrtinllq
       61 rptsgsvnvl gqdmlalsaa qlrkerkrig mifqhfnlmn srtiadnvaf plkgikskqe
      121 ikkkvaelld lvgltdrans ypaqlsggqk qrvgiarala sdpeilisde atsaldpktt
      181 ssildllksl nerlgltivl ithqmeavkq icnrvavmda gaiiergdll qvfsnpkqql
      241 tkdfidttlq ldqaiesvlq qpavknlgpn drllrltyvg asadqplvak lfksyhvtan
      301 ilfgdiqilq dtpfgnlivv lsgdqaqvdt giqylkqqdv kiedilkkea
//
LOCUS       WP_010488875             401 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FtsW/RodA/SpoVE family cell cycle protein
            [Lacticaseibacillus].
ACCESSION   WP_010488875
VERSION     WP_010488875.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..401
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=44252
     Region          14..393
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mesheiksns egdridygii lsvmllalig lvsiylaash dgstsqnpvr atimqaawya
       61 iggvgiffvm rfdaeqlwri apylygigif lmiavlifyd rateintgak swfalgpisf
      121 qpseimkpay ilmlsrvvtq hnaayshtiq ndwkligrmv lwtlpiailm klqndfgttl
      181 vflaifagvt lvaginwril lpialgaaai gtlaillvtq swgraflgsi gfktyqfari
      241 dswlnpsgst sgdsyqlwqs mkaigsgqlt gkgpfhmava vpvresdmif svigeafgfv
      301 gaavlillyf mliyqmirvt fdtknefyay istgvimmil fhvfenigmn igllpltgip
      361 lpfisqggsf llanmlsvgm vlsmryhhts ymfsrdtedf e
//
LOCUS       WP_010488933             155 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Lacticaseibacillus zeae].
ACCESSION   WP_010488933
VERSION     WP_010488933.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..155
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16718
     Region          6..>123
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 myqksfmeia neearanvng sdggpfgcvi vkdgkivsra hnkvlvdhdp tahgeitair
       61 kagqalgthd lsgcelytsa mpcpmclsai iwanikqvyy gntaddaaai gfrdaaiynf
      121 indglkgkml tlsqhdrdmt igafkayqta qkkly
//
LOCUS       WP_010488563             195 aa            linear   BCT 01-JAN-2025
DEFINITION  2-hydroxychromene-2-carboxylate isomerase [Pseudomonas sp. S9].
ACCESSION   WP_010488563
VERSION     WP_010488563.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..195
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21737
     Region          5..194
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            13
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mskqvefffd fgspasylaw tqlpkiaana gaqinwrpml lggvfkatgn sspvqvpakg
       61 rymlhdldrf akrykvplrf npnfpintlt lmrgaagyld derfelfvrt ifqamwvdgk
      121 nladpqqiaq vltaagfepe efvrlvadet vkerlkante eaigrgvfga psffvdgelh
      181 fgqdrldfva ealar
//
LOCUS       WP_010488944              95 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [Lacticaseibacillus].
ACCESSION   WP_010488944
VERSION     WP_010488944.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..95
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10844
     Region          3..92
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mkvinvtlkv kpeltdkyrh fisllvegsr aeagnlsydh fqsltdpnky eiiehwqdaa
       61 avelhnqtah fqkflagidd flaepleivr mdyae
//
LOCUS       WP_010488953             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VanZ family protein [Lacticaseibacillus].
ACCESSION   WP_010488953
VERSION     WP_010488953.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..201
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=23263
     Region          102..192
                     /region_name="VanZ"
                     /note="Glycopeptide antibiotics resistance protein
                     [Defense mechanisms]; COG4767"
                     /db_xref="CDD:443799"
ORIGIN      
        1 mlflgpfynw instslsrvn hfplvrlvvy sldktilyll ifaalrcfwl ltthrrtsfg
       61 helklglfvg ylillfaltv frdvyypwql tfhwdrplsv inlqplvetl klrqaashfd
      121 lwyqslgnia wfmplgfgvp wisthrrrlg saigiglvts lsietlqfll isgvadiddv
      181 ifnligailg ygfyrmwhlh r
//
LOCUS       WP_010488986             363 aa            linear   BCT 01-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas sp. S9].
ACCESSION   WP_010488986
VERSION     WP_010488986.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..363
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39711
     Region          10..>45
                     /region_name="DUF1501"
                     /note="Protein of unknown function (DUF1501); cl19855"
                     /db_xref="CDD:473233"
     Region          71..358
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mndkpvigns rrlflkhsla ysaaaisids llpqlaraae plsarypdpa vaalddsfld
       61 lrlfnasvek latglrwaeg pvwmgagryl llsdipnnri vrwdeisqsl gvyreqsnfs
      121 ngltcdnqgr litcegstth eqgrritrte hdgsitvlad nfegkrfnsp ndivvkrdgs
      181 vwftdppfqs gneyeghkiq telphgvyri dgeslkvtrv iddlagpngl cfspdeksly
      241 ivegrakpnr lvwayavned gtlgarkkhi eataygaldg ikcdeagnlw cgwgsngspq
      301 gkpeeldgvr vfnpqgkaig hislpercan lcfggpqgnr lfmasshsiy sifvntrgat
      361 fak
//
LOCUS       WP_010488996             214 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Pseudomonas sp. S9].
ACCESSION   WP_010488996
VERSION     WP_010488996.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..214
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23965
     Region          12..207
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mqalqtdktk pivyivdddq alrtslawll esvsiasqcy agadeflrhy daslpaclvl
       61 dvrmpetsgf qlqemlnarn iqmptffvsa hgdipmtvka mqngaidfve kpynpqqmld
      121 riqnalksav hshaqqqqrq qlkdklallt drerevlmmv idgkaskvia relnisvktv
      181 dvhrtkikdk mevgsiamlv revlslnseq vlad
//
LOCUS       WP_010488987             201 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Pseudomonas sp. S9].
ACCESSION   WP_010488987
VERSION     WP_010488987.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..201
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21498
     Region          1..201
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mesllpfllf afvasvtpgp tnilvlshss rrglgatlpi iagacvaaal mvlvvglgvg
       61 etllrfvrvq qvmtwcavlw lswlawqifn sppaplevdg prskgvsllg iaalqvvnpk
      121 vwmmamavis lfvgdgdrtp qvlllslsfl lvslpcmtlw allglgsarl lrspralqrm
      181 nqvlalllli sawlplliqg r
//
LOCUS       WP_010488999             166 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aromatic-ring-hydroxylating dioxygenase subunit beta
            [Pseudomonas].
ACCESSION   WP_010488999
VERSION     WP_010488999.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..166
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=18296
     Region          14..166
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mtehntlaal naplakaief iwheaalldn kdyaawaqlw sedgvyvipi dpdtrdfass
       61 lnyvyddarm ralrierlsa ghspsavdaa rtlrtvsrfn llessgdvve vtsaqllfay
      121 krgvhtpmaa elthrirfgq ggprleqkvv rlinstdsls algfll
//
LOCUS       WP_010489006             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aromatic acid exporter family protein
            [Lacticaseibacillus].
ACCESSION   WP_010489006
VERSION     WP_010489006.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10532842
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..321
                     /product="aromatic acid exporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35923
     Region          1..141
                     /region_name="ArAE_1"
                     /note="Aromatic acid exporter family member 1; pfam06081"
                     /db_xref="CDD:428756"
     Region          147..308
                     /region_name="ArAE_1_C"
                     /note="Putative aromatic acid exporter C-terminal domain;
                     pfam11728"
                     /db_xref="CDD:432028"
ORIGIN      
        1 mhigmrtvkt avgtavamli ayalhleywt aagiitilsv qnttkasfrl vayrllatvl
       61 gfviaigafl vlgynalafg vfllifiplt nvfevqsgiv mtavlvthfm makscswfwi
      121 rnellllavg agvalvanlf mpsleakite fqaqveaemr eiidhmsqql gpehlksadn
      181 wanlsdlkmt ldaavawanr hsdnqlwsen dyyqayfemr anqyellrqm qdsldrietp
      241 vlqaavisda lsmtasvlne dnpatqlvtm vkkiqrnfaa splptdrasf esrarlfyfl
      301 edfsrllqlk rnfnhiissq n
//
LOCUS       WP_010489102             290 aa            linear   BCT 01-JAN-2025
DEFINITION  SPFH domain-containing protein [Pseudomonas sp. S9].
ACCESSION   WP_010489102
VERSION     WP_010489102.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..290
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=31606
     Region          15..290
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mnpielkpks iigyvvafvv gilvlgvlfg swytvdeter gvllrngalv givdpglsfk
       61 mpfiesvsfi siqsqatsyn kvqayskdqq taeltvsisw hvpasevakv ytqykdldgl
      121 ltrlisrqvg tqienvfgqy navtavqqrg rfgadvskai tdsikgpvii dsvqvenidf
      181 sddyersiaq rmkaevevkt reqmlateqv qaqirvtqaq aeadskvaqa kadaeatrlr
      241 geaeadaika raqalasnqn lveltkaerw ngvlpttvlp ngtlpfidak
//
LOCUS       WP_010489105             348 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Lacticaseibacillus zeae].
ACCESSION   WP_010489105
VERSION     WP_010489105.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..348
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39151
     Region          7..216
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 maahealisv itpvynaeky laqaldslla qdysnfeilc vddgsvdtsk iilaayarqn
       61 arlhvirvkn ggqararqvg iehakgsfla fmdsddlvhp qwlstmaegm qtprvdmtvv
      121 nyynyiggtk ikarsfhapv ftiegddkyr ywledhdlrg ylwnkmfrad lfkepvpvan
      181 fnlledayfi gqllpridqi hfvdqpryyy rfnatssvha kfqkrdleai hqlgavfltl
      241 arekpeltsl avrryaalsl fvlskmsprq lvanwgyaqq lgmvlaqyar efqgiisagd
      301 analaadkpg kasllgklra wshllglptf ddlnklagre sdepkkes
//
LOCUS       WP_010489111             333 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YihY/virulence factor BrkB family protein
            [Lacticaseibacillus].
ACCESSION   WP_010489111
VERSION     WP_010489111.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..333
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=37584
     Region          32..313
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 marknhrkkr pllsteqqam irsgqmalae mklprrtkfw vfvrlamnrv aesnigqsaa
       61 aiayyallsl fplilfvana lpylgltyrs latyltqavp snvmkwldpv ianllntssg
      121 gllgigavat lwaaslgvng lkmgfnqvyg vdatqnfiiq rllsmlmtfm liivmgtili
      181 afafgrqfle wlipllrlnd dwlktfntlr wpvtvtalfi iimfldyflp nvkikiwtvl
      241 pgtaftvigw lliaqafsly mhyfgtryls ygtigtfiai mlwlnfsalv llwgavinal
      301 taeyfigrlh rskgkvhdfv krrvktprpk ees
//
LOCUS       WP_010489114             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Lacticaseibacillus].
ACCESSION   WP_010489114
VERSION     WP_010489114.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22950
     Region          2..125
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 markktithd qilnaaydlv veqgfksfta rniakkmncs tqpiylefkn maelkqavmd
       61 rikellalkm akhytndpvv dlglayiyfa lenrplyrav fvedhfgvde mreyamstam
      121 rvfdayepak nlseaqlrnt icgvwivatg ianlmapgfi ditrdqmvdi ltavtqdfiv
      181 ngrfsddpri swfekaqiaq gy
//
LOCUS       WP_010489131             307 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SPFH domain-containing protein [Lacticaseibacillus].
ACCESSION   WP_010489131
VERSION     WP_010489131.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..307
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33341
     Region          21..296
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mnvvlisiav ivlviviavl ftsvaiihtg evgiverlgk yvatlqpgfh vvppfiyrit
       61 eivnmkqipl kvdeqevitk dnvvvriset lkyhitdvna yvyqnkdsvl smvqdtranl
      121 rgiignmdln dvlngtetin qtlfqqiaet tagyglnvdr vnidsiqvda tiqdsmnkll
      181 rasrekeani meaeghkqaa iakaegekqa aileaeankq tqilqaqgha esqrliaaav
      241 kdqinsinag lidngdlylk yknveaieal akgtantvvl pstaidslgt lpalgklfnq
      301 ksdtken
//
LOCUS       WP_010489136             271 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Lacticaseibacillus zeae].
ACCESSION   WP_010489136
VERSION     WP_010489136.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..271
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28916
     Region          5..264
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,195,217..219,221..222)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mryrlilsdi dgtllnsqhq ltagvkqaiq ayvaaggifv lasarpplam ttlarqmgla
       61 vplvslngal igqpegeqlr ilaatswpeg vgprvyhvls mlplslnvfs gthwyvaafd
      121 kwtdqeavit dvkpttapir dmlsdnlsvq kmlcmgdpai vdqaekiila hpewqlvasr
      181 skatyleivr qgvskrsalq tlsslynvpi petmalgdge ndlpmlqaag lgvtlanalp
      241 qvsaviktvv pdndhdgaav aiqryamgea q
//
LOCUS       WP_010489196             121 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Pseudomonas].
ACCESSION   WP_010489196
VERSION     WP_010489196.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..121
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13406
     Region          9..116
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mkieqivdfa qinsplesyr paaekilkgd paqsvrnhya spcgqfntgi wegavgqwtv
       61 nyseheycei lqgvsvlrdk dgnaktlrvg drfvipagfs gtwevlepcr kvyvifeqag
      121 d
//
LOCUS       WP_010489257             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VanZ family protein [Lacticaseibacillus].
ACCESSION   WP_010489257
VERSION     WP_010489257.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..163
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=18919
     Region          <72..161
                     /region_name="VanZ"
                     /note="VanZ-like family protein (function unknown)
                     [Function unknown]; COG5652"
                     /db_xref="CDD:444373"
ORIGIN      
        1 mhsfkrhwgl wltavllfil fvsssmtyke qttvplmerl lqsepfkpfl stihfdyage
       61 tqsvaevgyf kfveffirkg ahvtiffllg lgltqgtfmy qknrwlhwpl vtlsctgiaa
      121 fdefhqmltg grtplfqdvm ldtvaaaiav tvmwgwlwwr krr
//
LOCUS       WP_010489265             216 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Lacticaseibacillus
            zeae].
ACCESSION   WP_010489265
VERSION     WP_010489265.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23941
     Region          23..182
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mivqphnltd lfssslaesq lsakqqavlk ailslfsekg fdrastkdia hlagvsegtv
       61 ykqfktkesi rqallapmiq hvipsaftef iheigeqklp dlhtfltfiv hnrmafaien
      121 qaqlrilaat llqdaalsqa laekfqkqfm dkaihllavy qqegalvdwp ltrilryifg
      181 tilsyllpvv lgmqssfdle tavseavafl erglqa
//
LOCUS       WP_010489272             236 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Pseudomonas sp. S9].
ACCESSION   WP_010489272
VERSION     WP_010489272.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..236
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25939
     Region          3..227
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtiklitfdl ddtlwdvtpv mqdaeaalrn wltmyapklg avpvehlwei rnqllaqepa
       61 lkhrlselrr rillnallga gyvekeasal aetgfqvfld arhqvelfae vhptlealas
      121 qfqlgvitng nadvrrlgla dyfqfalcae dlgigkpdpk pfqealrhan vsaelavhig
      181 dhpsdeiaga qaagmraiwf nplnrtwpqq papdgeissl aqlpallnsw lkpsgn
//
LOCUS       WP_010489302             223 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Pseudomonas].
ACCESSION   WP_010489302
VERSION     WP_010489302.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..223
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24537
     Region          1..209
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mlklygfavs nyynmvkfal lekgmafeev pfhpdqseqs lnisprgkvp algtdqgyms
       61 etsvileyie etgsgksllp sepfaraqvr almreielyi elparlgypq affgmqiapa
      121 lqekcklell agvaalkrhg kftpyvagds ltladvyfly sldlacavaq klfdidllad
      181 fpqagkllaq lnrlesvqki aadkeanmpe fmamikaraq ana
//
LOCUS       WP_010489379             149 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NfeD family protein [Pseudomonas].
ACCESSION   WP_010489379
VERSION     WP_010489379.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..149
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15997
     Region          24..149
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mlnflqhltf wdwlalgtll lilevfgagg yllwigvaaa gvgiityvip alpwalqfvl
       61 favlsvlsav lwwrrqrnag kisdqpglnd rgsellgrqf alheaissgr gkikagdtlw
      121 lvsgpdlpvg savrvtgqng vlllvepik
//
LOCUS       WP_010489381             307 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SPFH domain-containing protein [Pseudomonas].
ACCESSION   WP_010489381
VERSION     WP_010489381.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..307
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33044
     Region          6..287
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 meigsviflf vglaiavvfm gfkvvpqgsq wtverfgryt ntlkpglnii vplvdrigrk
       61 lsvmetvldi ppqevisadn aivqidavcf sqvinaaqaa yevnnldhai rnlvmtnirt
      121 vlgsleldam lsqrdainer llrtvdeata pwgikitrie ikditppadl vnamasqmka
      181 erlkraqile aegsrsaail taegkkqaqi leaegerqaa fleaearera aaaeaeatrm
      241 vseaiangnv qavnyfvaqk yvdalgklas sdnskvvlmp leasqiigsv ggigeiikat
      301 fgdkqak
//
LOCUS       WP_010489390             232 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Pseudomonas sp. S9].
ACCESSION   WP_010489390
VERSION     WP_010489390.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..232
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24973
     Region          3..201
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mkigilntgn vgsrlarawa gaghqlvlak dgedrkiapl laelgnratl stlkqaadfg
       61 davlfsvywp rtdalvdeig daldgkivie tmnplgvtkd fvhfhdvefm rdnstaeylq
      121 krlpnarvvk afsqlaapvl eaaawasspt kanvfyatdd qqagqivrql iedagftpin
      181 agplkvarql eqlgvllhqi aeheysgdad lirlgaaive anpgpilrqr tv
//
LOCUS       WP_010489443             283 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas sp. S9].
ACCESSION   WP_010489443
VERSION     WP_010489443.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..283
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31137
     Region          13..255
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mtkapayfgf wyrlgswllk stswlvlffl impilaiipl sfntepffsf tkgmltfqpe
       61 ayslrwysai fsdpkwilai qnsffigica tiiatalgtc aavglarddm parrlitall
      121 lspmivplii taagmfffys dlglagnylg vilahaalgt pfviitvtat lagfdyslvr
      181 aglnlgarpv rvfwdiimpl irpgvisgal fafitsfdev vvilfmagpq qrtiprqmfs
      241 glreqinpsi laiatlliil siimlvtiel lrrrsarlrg vea
//
LOCUS       WP_010489450             372 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudomonas sp. S9].
ACCESSION   WP_010489450
VERSION     WP_010489450.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..372
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41174
     Region          7..365
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 madqagdkpf lqftnvkkty dhkslvvkdf nldvakgefi tllgpsgsgk ttclmmlagf
       61 edvtsgeili ngrpvtsiap yqrnigmvfq qyalfphmtl renlayplkv rkmakdeina
      121 kvdeylelve lqdfgnrhpg qlsggqrqrv alaralifap divlmdeplg aldkklreqm
      181 qfeikrlhdq lgftviyvth dqtealtmsd riavfnngiv qqcaaphvly erpanlfvag
      241 figesntlrg tiasvetdtv tvrledgaqv sclkanctei gapttisirp ekltftdrlg
      301 ttgnqikarf varhyvgeyi ryqfetadkt elvvknlnds sapqfsaqee valawlaids
      361 qaldrpqaqa at
//
LOCUS       WP_010489477             425 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Pseudomonas sp. S9].
ACCESSION   WP_010489477
VERSION     WP_010489477.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..425
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44970
     Region          16..425
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtttlliiml vlllcgfpmm ttllaasaag ftlfftmgpe fivqqmiagi rpaalvavpm
       61 filaadiitr gatanrlldv amafvghvrg gmavttalsc alfgalsgst qatvvgvgsi
      121 mrpkmlqqgy kdsfamalii nasdiallip psigmiiygv vsgtsvaelf iagigpglll
      181 mcllcgyfyi yagitgipsg ekftwmqrlv tcrrailpll lpvmtiggiy tgvfspteaa
      241 avsvlyalil evlifrrvkl nelssialst glitavvfil vaagsafswv isfaqipqqi
      301 lsgigimsas ptellviisi affigcmfvd pivvmlilvp ifapavrmsg ldpvlvgtii
      361 tlqaaigsat ppfgcdifta iavfrrpyfe virgslpffa illlmsvlli mfppitlflr
      421 dlafr
//
LOCUS       WP_010489445             410 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010489445
VERSION     WP_010489445.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 410)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..410
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45407
     Region          <187..377
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mssltttear qaasaqrkkr itafmfvvpl lvfilltfva piasmlwrsv hhptvaelip
       61 htlealkdwd gkavpdqhtl qifavelngl akerlsgkla eefnraytgm ssvvkstark
      121 vaklkgddlr dkgaqtllda npkwqrtdlw yaiqrageky tydyyltald lelkpdtgiq
      181 vreetqiylq lysktltmal vitllcaalg yplsyylagl senranlllv lvllpfwtsl
      241 lvrttawial lqtngvinsf lmgvgltnep femlytsfat vvamthillp fmilplysvm
      301 rgidpsymra alslgdkpip afakiylpmt lpglsagall vfiisvgyyi tpalvggtdg
      361 qmisniiafh mqrsnnwela aalgslllal illlywlydr fvgasniklg
//
LOCUS       WP_010489481             531 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Pseudomonas sp. S9].
ACCESSION   WP_010489481
VERSION     WP_010489481.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Khan,M.W. and Murali,A.
  TITLE     Normal mode analysis and comparative study of intrinsic dynamics of
            alcohol oxidase enzymes from GMC protein family
  JOURNAL   J Biomol Struct Dyn 42 (19), 10075-10090 (2024)
   PUBMED   37676256
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17335521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..531
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57704
     Region          49..531
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
     Region          78..297
                     /region_name="GMC_oxred_N"
                     /note="GMC oxidoreductase; pfam00732"
                     /db_xref="CDD:366272"
ORIGIN      
        1 mpvpdlfaeg lsrgwktyng srleqdltle adivivgtga gggtsaeils aagykvllve
       61 egplktssdf kmqeaeaypa lyqegigrms kdgaitilqg ravggttlvn wtssfrtphq
      121 tlehwakehn vkghseaema pwfermeqrl gvapwamdpn anndvirsgc eklgyswkvi
      181 prnvrgcwnl gycgmgcptn akqsmlvtti patlekggel lylaraerli hdgnqvsale
      241 clamdercva ptgrkikika rhyilagggi ntpailmrse apdpyeragk rtfihlvnfs
      301 talfekvinp fygapqsiys dnfqwnqgta gplsyklevp plhpalastl lgefgvenal
      361 rmeqlphtnm vlalmrdgfh pesaegtvel radgrpvldy kmtdytwdgi rrafhsmaei
      421 kfaagaksvl pmqadaksat slaqvrsqid slsmelyrtr lgsahvmggc amgedaklav
      481 tdspgrhhql gnlsihdgsl fptsiganpq lsvygltaql ssllaerlkt a
//
LOCUS       WP_010489521             211 aa            linear   BCT 01-JAN-2025
DEFINITION  copper homeostasis protein CutC [Lacticaseibacillus zeae].
ACCESSION   WP_010489521
VERSION     WP_010489521.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..211
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22148
     Region          1..204
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mlrevaveny thipqalaag adrielndnl avggttvskg vmaesakyvh ehgrslvtmi
       61 rprggnfvyn dtelkimead lfeaqalgvd gvafgaltad glidedamts liaasagmsv
      121 vfhmafdaip edqqpaaidw laahhvdril thggplttpi eatlphlqtl iahaadqiti
      181 lpgggitsqn aaaiadklgv kelhgtkliq f
//
LOCUS       WP_010489622             280 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Pseudomonas sp. S9].
ACCESSION   WP_010489622
VERSION     WP_010489622.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..280
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31248
     Region          1..274
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mldsrmerle gkltpaertl layiqanqet lafetgatla aksgvspntv srflrrlgyk
       61 glkslkeelr ddvrmqslln ttliermqqp edlvahlhqe vaalnefadq lgsqywrdiv
      121 akvsqaervf vcgfqtirgl aedfanrlal vrsgvefldl ysgvlgqwid shdqrccvil
      181 idiapyadag isfaqnclrq gtdlvvftde ygiakhidtp siitmktktg lilestgglt
      241 salnvllhcv atqhkdqlke rlnayrdrve slrlyratsk
//
LOCUS       WP_010489547             492 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Lacticaseibacillus zeae].
ACCESSION   WP_010489547
VERSION     WP_010489547.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..492
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52825
     Region          20..473
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(27..28,31..32,35,67,117..118,120..122,125,145,
                     148..149,152,276,279..280,283..285,288,316,320,372..373,
                     377,381,397,400..401,404..405,408)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 mdvkdingkq vnvpmmvitl ivgtfitvln qtilstafpt lmkafdista tvqwlstgfm
       61 lvngimipvs aylsakvpsk wlymsamgtf fvgtlvafia nsfavllagr liqalgvgit
      121 mpllqnimms ifppnrrgaa mgmagiaigv apaigptlsg yvidnfgwrv lfgmilpiag
      181 lvliaalfff knvlplsnpk ldvpsliess igfgallygf sevgndgwgd pmvlgsiavg
      241 lifivifgyr qlhlkepfve lrvfkskifa lstvlgtian mamvgvemil plylqiihgk
      301 salesgltll pgalliavms pvtgqvfdri gakrlaqlgl flltiatlpy fflttntpsi
      361 fitviyavrm fgismvmmpl ttngmnaltp dmirhgtavn ntvrqvatsm ttavlisvls
      421 nvtnlakpaa slvksnplqy kqdffnatln gyhaafllav gfslvgwilt fflnshamsq
      481 evtikdekkv ka
//
LOCUS       WP_010489628             296 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010489628
VERSION     WP_010489628.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 296)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..296
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32809
     Region          7..294
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mstlegrkrl qllgllspat fviglffiap lvimatysml epglyggvew nfypdnfgrv
       61 lgwadgtlee fdpvyleiil rsfklaaitv fltllvcypa afwvarqpek mrnfcmflit
      121 lpfftsliir lyawvlilrp sgfinttlla lgintpinli ytetavligm tyifipfmfm
      181 pvyasvekld rrlleasadl gasrwqsfwk iifpmtlpgv aagsiivfip slgnfivpsl
      241 lggaqvlmig slveqqflaa rnwpfgaala mllmvavlic lilnvlaqnr nkagvs
//
LOCUS       WP_010489630             111 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease [Lacticaseibacillus].
ACCESSION   WP_010489630
VERSION     WP_010489630.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..111
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13083
     Region          21..88
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mtntsytgdv hshagrahfy rspewkalre qvlerdhyec qwckaegrvt tgndmtleid
       61 hiktleerpd laldpdnlrt lcrdchnkrh grfnykrlgr pknpyasder w
//
LOCUS       WP_010489645             351 aa            linear   BCT 01-JAN-2025
DEFINITION  c-type cytochrome [Pseudomonas sp. S9].
ACCESSION   WP_010489645
VERSION     WP_010489645.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 351)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 351)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..351
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38205
     Region          60..321
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 mpinkawlfl llaasgfara evpmadmqde ipaqpkaanl dyfkprelse ipkgafgdki
       61 rkgyqlfvns qqlsgqyvgn qlnctnchld agskayaapm waaylaypef rkknnrisnf
      121 aervqgcfnf smngkapaid spelvaisay sywllmggll dafgmqdqpv pemsdkalqe
      181 ggnvasfklp gpltdkvkld arghmpgraf aaldnpaqap spargakvye qhcalchgse
      241 gqgrvmadlp vipalwgaqs ynwgagmhrv ntaatfifen mplgkavqlt pqqawdvaay
      301 mnsrerpqdp rftkdvatta ktfhaddngy ygkeldgsvl gsqafpatrv k
//
LOCUS       WP_010489738             311 aa            linear   BCT 01-JAN-2025
DEFINITION  ADP-ribosylglycohydrolase family protein [Lacticaseibacillus zeae].
ACCESSION   WP_010489738
VERSION     WP_010489738.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..311
                     /product="ADP-ribosylglycohydrolase family protein"
                     /calculated_mol_wt=33173
     Region          4..300
                     /region_name="DraG"
                     /note="ADP-ribosylglycohydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG1397"
                     /db_xref="CDD:441007"
ORIGIN      
        1 mgimesrlih atvgfaigda lglpvkgqtq aelaaspvtg mkgygtfnqp agtysdetgl
       61 tlagldalqh gfdqdalvna yqawfkngey apygkrnpdi wssvettltt gkataapnep
      121 galirtlpfa ffayqtfetn lfqkaegsrl fqnfvtltnl dpenmvasav ytqiaiella
      181 dapdlptait tgisktaayf adqptyqpaf aafqtnleaq asdgtatdpl sllarvlhal
      241 qtwpdyhdav lnalmlggat dtaaaltggl aglaygytsl phrwclmlae yaqivdlcrq
      301 aeksgffpky d
//
LOCUS       WP_010489767             293 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Lacticaseibacillus zeae].
ACCESSION   WP_010489767
VERSION     WP_010489767.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..293
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30668
     Region          5..284
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 msplklgfig tgvmgtgiik nflkagqevi vynrtkahaq avldagavwa esphavaaqc
       61 hvvmsmvgfp qdveavyfgc dgilagtqag dlvidmttst ptlakqiaek akekgviaid
      121 apvsggdiga ekgtltimig gqkdllpklk elfapiassv nyfgpagsgq hakmanqimi
      181 agtmtglsem lvygkaagld lneilkvvgs gaaanwslsn ygprmlqady tpgffakhfl
      241 kdlrialdea kkmhlqlpat elaedlyakm vaagkgdlgt qglvtmnerw dea
//
LOCUS       WP_010489819             436 aa            linear   BCT 01-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein
            [Lacticaseibacillus zeae].
ACCESSION   WP_010489819
VERSION     WP_010489819.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..436
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46760
     Region          1..421
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mkkllrglia amvavlmigg aapavsvaaa essdtnvvda kaavaieptt gkvlyaknad
       61 svlpiasmtk mlsielvlda idsgkikwdd kvtldktiws lsqdrdlsnv plrrdgsysv
      121 relydasliy sanaammlla ktvagsqekf vnqmtaklks wgitdakivn vtglnnsqlk
      181 dakvpgtgdq aenemsakdm aqvaqhllkd hpevlkttsi akqtfrkgtd dainmenwdw
      241 mlkglvsydk nlpvdglktg tsdaagdcft gtvkkngmri itvvlhangd aktrrfdqtk
      301 klmnhvlenw ktvqladagq gikgyrnvtv nrgkartapi apvtkavavv psdtskqdlk
      361 ytytpakgvk kntieapvkk gatighlevt akgdslgfvg gakregitlk ttkadpkanf
      421 fvlifrgigd ffgnif
//
LOCUS       WP_010489862             206 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Lacticaseibacillus zeae].
ACCESSION   WP_010489862
VERSION     WP_010489862.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..206
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21499
     Region          3..192
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 msigiigsgn vgralgqlfs hvgekvilsh rhgvaslapv iaemrstvea gtvaeaadqd
       61 ivvlavpfna ldelptkvka davvidatny fpsrdgersa ltehhttsse lvaqhfgtkk
      121 vvkafntiam tkirslakpn qssdriaipi agddaaakqt vtnliekigf davdlgglad
      181 sypaqadgpl flftgdadqv raqank
//
LOCUS       WP_010489973             485 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Lacticaseibacillus zeae].
ACCESSION   WP_010489973
VERSION     WP_010489973.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..485
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50669
     Region          1..483
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 menffhlkqn kttpmtevma glttffamsy ilfvnpqvls qtgmpaqavf latiiasavg
       61 tlvmglfanv pyalapgmgl nafftytvvf algfswqeal alvficgvin ilitvtkirk
      121 liivaipeti qhaigggigv fvayigikna gflqftseas sintingqpl kagaltlkhg
      181 vesvvsnggi vpalvnftqa gavlaliglv imvilnvkkv pgailigill ttiigipmgv
      241 tdlhlsaans fgstfaslqt tfgaafsakg mgslftnpdk ivlsimtifa fsfsdifdtl
      301 gtfigtgrrt gifsdadeqa leegsgfssk mdralfadsi atgvgsifgt snvttyvesa
      361 agigaggrtg ltsvvvagmf lissifapfi aivptqalap alilvgimmm stfkeiewed
      421 lsqaipafma sivmgfvyni sygiaagfif ycliklitgk akeihpvlav vtvgfilnfv
      481 ilaal
//
LOCUS       WP_010489948             387 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Pseudomonas].
ACCESSION   WP_010489948
VERSION     WP_010489948.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..387
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42769
     Region          1..385
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnpnnnpeln airegvralc aefpaeywrk ideekgfpea fvkalteagw lsamipeeyg
       61 gsglglaeas vileevnrcg gnsgtvhgqm ynmftllrhg seaqksyylp klasgelrlq
      121 smgvtepttg tdttkiktta vkqgdkyvin gqkvwisriq hsdlmillar ttplaevkrk
      181 segmsiflvd lreaigngmt vqpianmvnh etnelffdnl elpadslige egkgfryild
      241 glnaertlia aecigdgrwf iekasqyard revfgrpigq nqgvqfpiae ahieveaadl
      301 mrwracdeyd agenagasan makylaakas weaanaclqt fggfgfacey dierkfretr
      361 lyqvapistn lilsyvaehl ldlprsf
//
LOCUS       WP_010490008             425 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Pseudomonas].
ACCESSION   WP_010490008
VERSION     WP_010490008.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..425
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44376
     Region          1..425
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtvavflssl lgfmafgmpi afalmltgav lmwyldfwdv qllaqnllag adsfpllavp
       61 ffilagelmn aggisrriit maqafvghkr gglgfvaiaa avllasmsgs aladtaalat
      121 lllpmmrqrg yplhssaglv aaggiiapii ppsmpfviyg vvtntsisql fmaglvpgli
      181 mgaglifawt liargfteps ppkaskavrr aalidgasal mlpviivggl rfgiftptea
      241 avvaatyala vstllyreld wktlieamtr asrttasvmf lcaaatvsay mvtlaqlpde
      301 iasmlgplad hprllvaaim llmiaigmvl dltptilila pvlapiaaka gvnpvyfgvm
      361 fvligsigli tppvgtvlnv vggigklrme ilvrgvmpff liylaivlll iafpaivtvp
      421 lawlr
//
LOCUS       WP_010490105             277 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase
            [Lacticaseibacillus zeae].
ACCESSION   WP_010490105
VERSION     WP_010490105.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..277
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=30593
     Region          112..205
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mtialvfvia fawsllsqii pfltglfgll kddvnipqsf dllflfgeai giismviyyr
       61 gdrdilpfak dhvarnyslg llfgfmmfsl iwgiitlfgg yqvlvifqgs nllwlilfff
      121 gyaiqsmfee llcrgyvmgy wlkqnkvima vllnailftl lhmanpgfnl paaiglflfa
      181 iamsqfrllt gsiwlcgafh aiwnfaegpi fgvavsgtss esfilkslpt tsfqpltggt
      241 fgleassvsn vvhlllvill tliilkkrrt altisan
//
LOCUS       WP_010490107             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Lacticaseibacillus].
ACCESSION   WP_010490107
VERSION     WP_010490107.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..219
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24056
     Region          12..218
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mvhsctavvp lfkklddkar aaidalther qvekgtvlis pdtdarllvv aqgklktyql
       61 atngkeqllr vdgpgdyege agllniaspn vytealttat vctisaadfq qllmkqpqis
      121 lqlltentrk mqalekqagy lgndsinvrl thylldlrta agkdtvtvpm awtqladylg
      181 ttpetvsrtl krlaneklir rtgkqvtiln aedmedfvw
//
LOCUS       WP_010490143             460 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Lacticaseibacillus zeae].
ACCESSION   WP_010490143
VERSION     WP_010490143.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..460
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49753
     Region          1..412
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mkkkigfwsi vllainsiig sgiflspgav vqssgskali lygiaaffaa ilavtfaaaa
       61 kyvahsgaay iyakaafgeh vgfyvgitry iatciawgvm atavvktvlr ifgfdqndlm
      121 lvtislillm lsllvincfg pkffelvnnl stigklaall vfiifgigvi attgvnhfaq
      181 idrltsagtn atlstlvmgv iaafyaftgf esvasgaddm dkpeknlpia iplaisviav
      241 vyigvvwiam mvnpqammat kevvalvavf nnpliqnivl ygalismlgi nvaasfhspr
      301 vleaiakqgq lpswlagrta knfplpafll tialavllpm afrydmtsii ilssisrfvq
      361 fliiplcvmk ffrgrgdrrl inparpnvlt dmvcpavsli ltvlllikfd wigqftilda
      421 nnqhapnyfa ivamilgyiv ilfgmmlfny qtkkkryeyd
//
LOCUS       WP_010490157             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Lacticaseibacillus].
ACCESSION   WP_010490157
VERSION     WP_010490157.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22086
     Region          10..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 masipvpspi ieqavklfae rgyaetnlps iakaakvavg tiyrhfkske dilntaftdi
       61 mnffhnslae aadcdpddpe tmfgrlfdaa tasmeqypte lhfiqqnvfn ealnaesraa
      121 rgrvitlinn mlmdgqdrgv ivkadvrtql ailygsivsm idivwaqqqi eghvsnqkal
      181 aadlknqvwn gltserrvfn
//
LOCUS       WP_010490188             323 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Lacticaseibacillus zeae].
ACCESSION   WP_010490188
VERSION     WP_010490188.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..323
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34004
     Region          5..300
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(35..36,39,91,105,107,136,169,260,263,299)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(229,234,251,260..262,265,287,291)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mnecltigep lvvfaaeead vplaaakhft kylagaelnv avglsrlghs veyithlged
       61 pngifirqql taagigsdnv tttsryptgi efkarvthgd pntyylrags aaahfdpdai
      121 drvdlagvkl ahitgifpaa sastltatkr lmkrlitnhi mitfdpnlrp alwpdqrtma
      181 ttinelaksa tivlpgaaeg kilvgsddpe tiahfyldqs pqtqlvivkv gkqgayllgr
      241 nvpgqllpsf paahivdtvg agdgfalgvi sallegrspa eaasrgnaig alaiqsagdn
      301 tgyptrsqld kfmktslnet ghe
//
LOCUS       WP_010490200             327 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Lacticaseibacillus zeae].
ACCESSION   WP_010490200
VERSION     WP_010490200.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..327
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36733
     Region          92..324
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mssnwkktll iagaftglst alkvysqlry hrslsatlve galrlfvkdk rtglqvkqdl
       61 ahkkmvgekt yhipeqmhfl vaikktkfnn idiyelnper nsgtailylh ggayaahpti
      121 qhwkmlnkla qrtnariivp iytvipfaty hrayqtltal yqllknddrv rkiilmgdsa
      181 gggmalglae sfavkdlpqp dslillspwv ditlsnpetk kldtidpiln rqaliangql
      241 wagktdrkdy hlsplfgdva plknvtifvg treefypdil klnkklkkhg vvtnlfhgig
      301 qnhiypilpt wearnaiqqm iavifsv
//
LOCUS       WP_010490201             320 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Lacticaseibacillus zeae].
ACCESSION   WP_010490201
VERSION     WP_010490201.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..320
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36063
     Region          83..288
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 msyisndemn peiktigrii rrlppfhnpq nfyranwltd hfvkghfpkd lnvkqvfiqr
       61 pdnskmrili vspvspkpla tgvlwlhggg yavglpetdl hyarkiqnis nsvvvmpdyr
      121 rsteapfpaa ladayltlvw lkehatalgv nplqlfvgge sagggltaal tlyardqnqi
      181 kiafqmplyp mlddqptpss lhndapvwde rsnvnawkly lgndyghenv seyaaparak
      241 syenlpptyt figtiepfyq etltyifalr kagvkaqidi ykgafhsfdf fasrtqlaqa
      301 atkkwqkafk yasnhyystk
//
LOCUS       WP_010490227             388 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudomonas sp. S9].
ACCESSION   WP_010490227
VERSION     WP_010490227.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..388
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43125
     Region          1..370
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maeirlqnla hsysrtpssa aeyairemnh tweqggayal lgpsgcgkst llniisglls
       61 pshgqvlfds rvvndltpqm rniaqvfqfp vvydtmtvfd nlafplrnqg maepqvlskv
      121 heiaevldlh plltkkasnl sadekqkvsm grglvrddvs ailfdepltv idphlkwklr
      181 rklkqiheqf nitmiyvthd qleastfadk iavmyggqiv qfgtprelfe rpshtfvgyf
      241 igspgmnlie vercadgvcf antrlslgaa lnqrldsldy qqlkigirpe fvhlwdlpgs
      301 dlpgaeslve vaadsdafsa evvhvedlgt ykilslnldg qplkvrlqed qvvprhrasv
      361 sfpaqwlmvy addflvtvda qearhesa
//
LOCUS       WP_010490229             364 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010490229
VERSION     WP_010490229.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..364
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40498
     Region          2..349
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 msltlehvsr wvdnqvyidd aclsfepgsf nvllgrtlsg ktslmrlmag ldrpskgril
       61 mngadvtaip vrqrnvsmvy qqfinyptls vfeniasplr qarcseaeit ekvhatakml
      121 riegllkrfp lelsggqqqr tamaralvkd aslilfdepl vnldyklree lrqemrelfa
      181 arhtiaiyat tepnealalg gtttilhqgr iiqsgntpev yhrpqhilaa elfseppini
      241 lpgqisgtev sfadtvhfpl npdlqqlepg eyrfgmrpsh iglvpsnddd lelavtvdla
      301 eisgsetflh vrgeqfslvl hlpgvheydv dtpiliyipt hklfvfdvqg qlkqaparrt
      361 graa
//
LOCUS       WP_010490231             633 aa            linear   BCT 01-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Pseudomonas sp. S9].
ACCESSION   WP_010490231
VERSION     WP_010490231.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..633
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=69723
     Region          9..630
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 maesarilth qaivedswsr crefglthqt apsfgspvrg evsallerhq slvvtthqev
       61 lpyygnilan snclimladn rgqvlqswgd qrfldaersa gfvagaswqe rqtgtnaigt
      121 alncaqavhi qhdehylkan rfmtgsaspi fdeqrqviav ldvssdsylp pshtlgmvkm
      181 msqsvenrli lnlfkqhyfq ltfntslnnl espwaglvvf desgqvisan rradnllgts
      241 lalvniemlf dvplqqllnq psgqpfnlka ggrfrfhahi tqplqpvapt ardfrrqakg
      301 aaisqddhgl padnlsldnl smgdarvdka iqqaqrliek dipllihget gvgkevfvka
      361 lhhagsraaq pliavncaai pselveself gyekgaftga nqkgssglir kadkgtlfld
      421 eigdmparvq arllrvlqer cvqplgssen ypvdirlisa tnrplrndve qglfrqdlyy
      481 ringlslelp plrersdkta lfkrlwqqyr epqqwaglsn evlelfnahp wpgnlrqlss
      541 viqvalamad dqpirvehlp ddfiaelqah qpatassmaq antgagthgg msgasdlnqk
      601 lqacagnvsq larhlgvsrn tlykrlreqg vkt
//
LOCUS       WP_010490267              92 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HU family DNA-binding protein [Pseudomonas].
ACCESSION   WP_010490267
VERSION     WP_010490267.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..92
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9611
     Region          3..92
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mamtkdqlis diaeaidtpk ttvraaldql seivsdalen gdeitlpgig klkvtarpar
       61 tgrnpqtgka ieiaakkvvk yvpakaltda in
//
LOCUS       WP_010490287             203 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Pseudomonas sp. S9].
ACCESSION   WP_010490287
VERSION     WP_010490287.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..203
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22133
     Region          1..203
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 malqtwllyl iaitglsltp gpngllamth galyghrral wtvtggvigf tllmalsmfg
       61 idsllkasan altilkwlgg ayliwlgiql wrspppnldt lddthgrpas slfrqglfaa
      121 lsnpkvilff gaflpqfldp ganiwlqfai maltfvmveg lveyllarma qrirpwlqrs
      181 gkgfnrscav mfiaigsalp mtr
//
LOCUS       WP_010490290             203 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Pseudomonas].
ACCESSION   WP_010490290
VERSION     WP_010490290.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..203
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22785
     Region          4..200
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 meypedsall srllsgeesa yrelvatyqg smravalaiv gsrnsdevvq dawlavvnsl
       61 kgfqgrsslk twlltitant aktrlkhnrr evlmddlpgp hgtigddrfa ddghwlmaph
      121 ewhqdtpeam llqnelrecl ektlgslsnm qssvlvlrer qgleleeicn lldislsnvr
      181 vllhrarlkm fatlehfeet gqc
//
LOCUS       WP_010490332             438 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Pseudomonas sp. S9].
ACCESSION   WP_010490332
VERSION     WP_010490332.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12081071
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..438
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46357
     Region          41..394
                     /region_name="MFS_1"
                     /note="Major Facilitator Superfamily; pfam07690"
                     /db_xref="CDD:429598"
     Site            order(48..49,52..53,56,90,148..149,151..152,154,157,176,
                     182..183,260,263..264,267..269,272,299,303,357..358,362,
                     369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
ORIGIN      
        1 mpgknltddi ysklvdeeda rvctelsdsa chqvpgnfll milshffskl gdalanpkiv
       61 lpwvmetvha plyligflvp iresgslipq lfvasyiram kirkwvwvfg smvqalaiag
      121 iglvawtldg atagwaiial vslfsiargl ssvaskdvig ktvpksrrgq vngwsasaag
      181 lvtvglalvl lfssqaqpep iayalllaga gclwviaalv yaqisedpge tdgggnafie
      241 aikrldilrt dkafrhfvit ralllcsalt apyyvvlaqk nldsnaslla lfllasgaas
      301 lvsapvwgrf advssrkvmi laalmtaalg iilfildhfe hawlgfsgli palyfclsia
      361 hqgvrigrkt yvvdlaqgnr rtdyvavsnt ligvilllmg figalsmvvg vsavilllsl
      421 lgaagaglav alpetetp
//
LOCUS       WP_010490375             402 aa            linear   BCT 01-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Pseudomonas sp. S9].
ACCESSION   WP_010490375
VERSION     WP_010490375.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..402
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42781
     Region          12..379
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 msitpsanda vtglilsggg araayqvgvl aaiadllpdp qnnpfpvivg tsagainavs
       61 lacgamhfaq avqrlssvwq gfstasvyrs dwsgvlaqas rfignsmlgl ggqvpvalln
      121 ssplkellar eldfsgisaa vrsrklnava vtafgydsgq avtfyqgrst idswfrhrri
      181 giptrlgldh llassaipll fapvkinney fgdgavrqsa pispalhlga nrvlvvgvsd
      241 hfqqeraihm prhsgvakpp tlaqisghll nstfidrlea diellerinh lsrmitpeqq
      301 nssnlkpvev lviapsqpld eiaarhrrem pasvrlflrg pgatrdsgag vlsyllfepg
      361 ycrelielgy qdamaqkarl ctflslgtas dpialpvtqi pv
//
LOCUS       WP_010490408             241 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lacticaseibacillus zeae].
ACCESSION   WP_010490408
VERSION     WP_010490408.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..241
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26556
     Region          4..236
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtritiehlt kslsgrnilq vknlscesge vyglvgpnga gkttllkcic gliipdggei
       61 qlnelvldrr trstflkhig svfaqsdsif dltidtllte hyhyfclkrp kdwhellqnv
      121 aleitpkqki gslslgmrqr lllalaishd psilildepf ngldpdgvnl tkklinnlak
      181 dkvviitshs fadlndiitq svviahgqts gvkklaaiks dftdgladfy refvrhtnsl
      241 n
//
LOCUS       WP_010490433             246 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Lacticaseibacillus].
ACCESSION   WP_010490433
VERSION     WP_010490433.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..246
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26750
     Region          6..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 msqyrvemkn vhksfgdndv vkgvnlnvan nevvvmigas gagkstvlrm ingletvtsg
       61 eilvdgedia hkgtdinkvr ekigmvfqhf nlfpnmsvmg nitlaptelg iaskdeavkq
      121 akemlevvgl tdkadampaq lsggqqqrva iaralamhpd imlfdeptsa ldpemvgdvl
      181 gvmrrlakqg mtmvivthem gfakevadrv vffdngtile qgkpedifeh pkeertknfl
      241 nkvlna
//
LOCUS       WP_010490429             170 aa            linear   BCT 01-JAN-2025
DEFINITION  CinA family protein [Pseudomonas sp. S9].
ACCESSION   WP_010490429
VERSION     WP_010490429.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..170
                     /product="CinA family protein"
                     /calculated_mol_wt=17961
     Region          8..161
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mqanqseitr lavelgrklt dlhaqvstae sctgggiaea itrvpgssaw feagyvtysn
       61 tqktkqlgvg pelfvllgav srevveamvr gaqeqsgary avavsgvagp dggtkekpvg
      121 tvwlawgdse qlysvrkefa gdrqsvrrqt viaaleglir llekenptlg
//
LOCUS       WP_010490441             156 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Lacticaseibacillus zeae].
ACCESSION   WP_010490441
VERSION     WP_010490441.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..156
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17934
     Region          8..150
                     /region_name="YdbS"
                     /note="Uncharacterized membrane protein YdbS, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3402"
                     /db_xref="CDD:442629"
ORIGIN      
        1 mnetghalpa nikfvwradi fiwsfnffvv glllliashf whwpswlglg vigltvlqyi
       61 irralvpyry rflrynitpt avflqkgfff rkneaipiar iqnvtleqgp llrwqqlqqv
      121 nietastahv idgvtasvad qlrtriltla qearde
//
LOCUS       WP_010490460             226 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase
            [Lacticaseibacillus zeae].
ACCESSION   WP_010490460
VERSION     WP_010490460.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..226
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=25440
     Region          129..225
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mgkiisiggs llkhsllltg illldiltef hdfftisklq qdqyevlvie lilkgafiwf
       61 lhwlyfrqlk rfnpngyglk plsrkntlif ligvaslfal lcvesltpfn adnatnqvlv
      121 nkfirtapll asvdavlaap iieefilrgi ffnyfvnknt imskifvvlv sgfvfgllhe
      181 phftvnllvy ctmgwlfgsv yaltgdlrys ialhilnnvl afvsmf
//
LOCUS       WP_010490508             482 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein/permease
            [Lacticaseibacillus zeae].
ACCESSION   WP_010490508
VERSION     WP_010490508.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 482)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11705690
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..482
                     /product="ABC transporter substrate-binding
                     protein/permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52429
     Region          41..264
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Region          273..482
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mrgikhwava iiallamlig ftvqqptpta aasddlaaiq krgylivgls adyaplefha
       61 tlngadtivg adismskqia kdmgvklqik emnftaliga lktgkidliv sgmsktpere
      121 kevnfsqpyl yetqvmvirk adkakyksia dfsgkrvgaq kqttqeqlak tqlpgakvts
      181 ldkandviaq isynkldagv mastiadsyv artpslmvld phfatdkapt aiavnkqspa
      241 llaqvnktis kvkgakykqy lqaayklqdq nqgfwakygn yfirgaiytl ifaaltvffg
      301 tiigtllalm klsrnwlaka ianvyiefir gtpllvqafi vffgtqilgl dlsafiagai
      361 amainsgayv aeiirggins vpvgqteaar slglhqrqam ryvilpqamk niwpalgnef
      421 vtdikessvl svigatelmf egtvvqgasf kpflplvvva ifyfimtftl srllrliekr
      481 fn
//
LOCUS       WP_010490455             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Lacticaseibacillus].
ACCESSION   WP_010490455
VERSION     WP_010490455.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..248
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27011
     Region          6..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 masepliqvk nlkksfgnhe vltdinfnvq agevvsiigr sgsgkstllr ninlletptg
       61 gdilfhgksi lgedvklsty rakvgmvfqs fnlfnnmtvl qnvmvpqqtv lkrdaaaakt
      121 halellkqvg mdpfiaakpd qlsggqeqrv aiaraeamdp evllfdepts aldpemvddv
      181 lntmtalaht gltmiivthe mafardvsdr vvfmnngiia esgtpdqifg npqqtatkef
      241 lkrylnrv
//
LOCUS       WP_010490556             425 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Lacticaseibacillus zeae].
ACCESSION   WP_010490556
VERSION     WP_010490556.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..425
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=49126
     Region          65..402
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mayktlrvls ysqsipnise eyerrfnges avktnlwmsp nerdhksias hqifcvltpd
       61 iykmtismmq rsetikrris elsdvasdqf fletlvnelm stneiegvrs trkelysavm
      121 salkkektpm rfrslaniyl girrnrsiki ndvtqirtaw eyvtageikk sdlpdgkvfr
      181 skevyindaa sgqaihwssp deeqvrqdme aliqfmndne tpfilkalis hfffeyvhpf
      241 ydgngrtgry lacaylgkkl dyltgisfsn siskakkkyy kafaevehpk nfgdvtffve
      301 almhiietgq kdiiaalkqs qikledwfkr ilaadftnhq kailayliqp ylfgsrenst
      361 mddnalkell srqgfngrty sqvsikksid qlekdgwiel vkhrpkihav sqrfiaymte
      421 nhklq
//
LOCUS       WP_010490785             189 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Lacticaseibacillus
            zeae].
ACCESSION   WP_010490785
VERSION     WP_010490785.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..189
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21408
     Region          3..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mttkhrilnr eivldaartm vaqdgirdlt fqtlakelni rsqslynyfp nlpaviealg
       61 tefmhnlyqe lienvsgisg keairafaev ahryferqqs ldeiiyfvhq fpesspfvqg
      121 tgdvinllkr liahtelkqm akesfvqdfi ssvlgftvle vmgflpdnka srgtsfesll
      181 dmylneikg
//
LOCUS       WP_010490434             358 aa            linear   BCT 01-JAN-2025
DEFINITION  LOG family protein [Pseudomonas sp. S9].
ACCESSION   WP_010490434
VERSION     WP_010490434.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..358
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40067
     Region          87..266
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mpydaddyla rhfqasgidl rskvdeltsl iapanspnie lyremlitvi rmgqadrnrw
       61 dakimlqtlr emehafcvle qfkrrrkvtv fgsartpvdh piyqlgrelg aqlarhdlmv
      121 vtgagggima aahegagldn slgfnitlpf eqsanatvsg sshllsfhff flrklffvke
      181 adalvlcpgg fgtldeaiev ltliqtgksp lvpvvlldqp ggsfwseall fierqlkdsg
      241 yilasdlnlm tlvysaddav tqitrfysny nssrwlnrqf iirlnhslna qaltairstf
      301 adickaddfq lqdkakegqd tpelahlprl tfsfngrnhg rlrelldfin lrenwlsa
//
LOCUS       WP_010490857             486 aa            linear   BCT 01-JAN-2025
DEFINITION  catalase [Lacticaseibacillus zeae].
ACCESSION   WP_010490857
VERSION     WP_010490857.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..486
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55073
     Region          2..482
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mtdklttgeg qawadnnhsl tagergpvll qdyqllekla hfnreriper vvhakgagak
       61 gvfklthdmk aytkadlfng vgketpillr fsqvagesgy pdtirdvrgf alkfytqvgn
      121 ydivgnntpv ffvndplkfp dfihsqkrdp rthrrdnnmq wdfwahspes thqvtylmgd
      181 rgnpasyrtm ngygshtfkw vnaqgeaywv kyhfisqqgv qnmtdevaak iagtdtdylq
      241 ndlfsaietg nfpkwtvyvq ilpyqegldy kydifdvtkv vshhdyplie vgeftlnenp
      301 enyftdveea afspanfvpg ieaspdkllq grlfgykdae ryrlganyeq lpvnrplnpv
      361 hnyardgfma akqdrsvnye pnshggpeed hsarihqdav ngkignykpy dednfsaagr
      421 lyrvmseder trlvttivnn lkqvtsqevr vlaahnfyka dpeygsrvae qlglriedvk
      481 agkaea
//
LOCUS       WP_010490891             214 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Lacticaseibacillus zeae].
ACCESSION   WP_010490891
VERSION     WP_010490891.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..214
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23338
     Region          4..211
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 midwqaltay arsvsaqdhs ghgfdhierv iamakrlaae tpgvdsavvv aaatmhdtyd
       61 dklvndvaaa ksaarhamaa agltdeqiqa viaiidhmsf kanlgkrqpl slegqlvqda
      121 drldaigaig igrafmygga hggrmydpel aprtaltpsn yrtkestvin hfyekllklk
      181 dqlntpaakq laehrqrvme dflaefkaew rger
//
LOCUS       WP_010490914             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Lacticaseibacillus].
ACCESSION   WP_010490914
VERSION     WP_010490914.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..202
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21894
     Region          14..193
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mktkrlspva vtsivlgviv aiclifgigt ynslakqnqa veaqwsqven vmqrradlvp
       61 nlvnavkgqm gqeqkvfgei aearksyana ntttgkakad dqlnksvgtl invikenyps
      121 lqssnqvntl mtqlegsenr iaverkryid qvrdynqsvv tfpknifasm mglgkkdtfk
      181 atpsaqtvps vdfssnssss gk
//
LOCUS       WP_010490991             306 aa            linear   BCT 01-JAN-2025
DEFINITION  Ger(x)C family spore germination protein [Paenibacillus elgii].
ACCESSION   WP_010490991
VERSION     WP_010490991.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Cooper,G.R. and Moir,A.
  TITLE     Amino acid residues in the GerAB protein important in the function
            and assembly of the alanine spore germination receptor of Bacillus
            subtilis 168
  JOURNAL   J Bacteriol 193 (9), 2261-2267 (2011)
   PUBMED   21378181
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Li,Y., Setlow,B., Setlow,P. and Hao,B.
  TITLE     Crystal structure of the GerBC component of a Bacillus subtilis
            spore germinant receptor
  JOURNAL   J Mol Biol 402 (1), 8-16 (2010)
   PUBMED   20654628
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Hudson,K.D., Corfe,B.M., Kemp,E.H., Feavers,I.M., Coote,P.J. and
            Moir,A.
  TITLE     Localization of GerAA and GerAC germination proteins in the
            Bacillus subtilis spore
  JOURNAL   J Bacteriol 183 (14), 4317-4322 (2001)
   PUBMED   11418573
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..306
                     /product="Ger(x)C family spore germination protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=33506
     Region          1..>274
                     /region_name="GerAC"
                     /note="Spore germination receptor GerABC, GerC subunit
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG5903"
                     /db_xref="CDD:444605"
ORIGIN      
        1 mkrrkmmlai vallpmmpll agcwsqreid dlslvagial dkahetkvek altkngatrk
       61 kedlisityq iftsssgggq gkggggsaeq kryenftetg dlllestrei slrterpifa
      121 qhfktlvigd ellrttpirs fmdlmyrese frpsalvfva rglaretfel kgakeipafr
      181 ilkmvdnqyk strilppvsl aklltllqsk ssfllqaivk gggeikfaga gvvhgqsgkl
      241 vgfldedelg sitlitgnvr ggvvkfadee tgqktcmkfc riratlcrvw kgttshsrfe
      301 snpgag
//
LOCUS       WP_010490960             292 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Lacticaseibacillus
            zeae].
ACCESSION   WP_010490960
VERSION     WP_010490960.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..292
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31158
     Region          7..281
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 meqvqpnkaf fwgillnliy iiaeiafgig igsvalvada ihnmsdvlgl glawfsewls
       61 nrhptvqrty gyksssilaa lanaafllva mgaiiveait rlsqnapveg gwmmlvagvg
      121 ilvngatagl fhsgsqhdln irgafmhmaa dagvslgvvl agglimltgw ewldpvmsil
      181 vaivvligtw nllrdavnla maavpkeidp iavktlvday ptvaschdlh iwalsttdva
      241 ltvhvvrttp egndafldal slslresfdi ahttiqveyg pylpdnkmen py
//
LOCUS       WP_010491021            1055 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Lacticaseibacillus
            zeae].
ACCESSION   WP_010491021
VERSION     WP_010491021.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1055)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1055)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1055)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1055)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..1055
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=120277
     Region          3..820
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mlelsfekev vktlttgsnq wverkdlyga tpdqlwanfr dklinnnyak lqghpltdte
       61 fnqvkraiev rtpyeaakll aaengigkve verddaklgt vtlelfwkad vaggkssyev
      121 vrqavrprla gtqdvdpdrr fdvtllingl pliqlelkka tvelnqafnq iekyaqegky
      181 tgiysllqmf vimtpdstay fanaepdhfn kaflfnwrtr dnhpvengla ftrqvlnipm
      241 ahkmvseytv idqerqslil lrpyqiyaie avmhrihdhq dgfvwhttgs gktltsykta
      301 klaaqdpgvd kviflvdrrd ldeqttsnfs ayaanddiai neaqntgdlm rklqqndgkv
      361 lvtsiqklhr avkktqaqla tgkqsrfskt lkqrviffvd eahrsqfgkm qkeiraafvn
      421 snwygytgtp ifnenkkqlk gdlavtteel fdkvchvynl rdaledqavl pfnvehvtti
      481 gkdtlitral eketnrvkar rdkqgrmlst adeakiqaki qamsvkdlee tyltpadfet
      541 dehinqvvqy ilekgprkts lghgnynail ttssiemaqr yyqafkaakk tthnqldpnw
      601 priaitysls enedqsahkh dqmatilkdy nqqyhtnfdl adlnlynedv akraarreav
      661 fahlkpdqei nlvivvrrll tgfdaprlnt lfvdrtlayq eliqaysrtn rlqnrelkqe
      721 gqivtfrvpa imeanereay klysgegsfn viirptyqqa vlkfqkavvd lkaiaptrta
      781 addlkgttak vqfvkafrqv nqqlnslsmy ndftwensek afgiaqpeve sytgkyprik
      841 aavtnqepek vpeelaaldf slavgsvvlv dydyltqliq dwideqqqyt tpdqaqahmt
      901 dylqnsvkvq sslnklaetq pqqaqlirea mpyieqkmqq sqqqsdqnqa pvslnarelv
      961 adyaqrqlvk ktsvfahtwg ldqtallrva rehtvgtdew hheqeltqsa nlaaalqaqt
     1021 atgpkipail plyriksqad wrqfiehdla iylqk
//
LOCUS       WP_010491122             363 aa            linear   BCT 01-JAN-2025
DEFINITION  saccharopine dehydrogenase family protein [Paenibacillus elgii].
ACCESSION   WP_010491122
VERSION     WP_010491122.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..363
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39207
     Region          28..335
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mknkivvvgg yghvgttick qlgerypgqv faagrsaera erlsretggk vkpltldirn
       61 ptdsdilnda klvimcldqt dtdfvrscfr ngthyidvsa ngafltqver cgpeaaahga
      121 tavlsiglap gltnllalea sklleqvhei ditimlglgd rhgeaaiawt vdnlhasfev
      181 irnnrsvavk sftdgrvadf gtefgrkkay rfpfsdqqti artlnvptvs trlcfdsalv
      241 tamaaglrat gaagflkagw vrqaaiagig klhfgeerfa vkvdargskg nkeayaecyl
      301 qgihqsdmta kvavsvadal crktfphgvf hieqlfelsd mrewltkeaa veirldgnlh
      361 stv
//
LOCUS       WP_010491114             288 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus elgii].
ACCESSION   WP_010491114
VERSION     WP_010491114.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..288
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30870
     Region          <47..122
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
     Region          159..281
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mnepyalesm nagdsahlla ltrsvgwhfs akqpdlylrt gpvvghrdgd kwiscagfya
       61 ygealasigh livdpayqgq glgkrlmlhc laeaaktgsa vtlistksgf plysslgfqt
      121 vgyahrflcd vpaeglrder fssaegdpvr lneavlpevi eldqaaagvr rermlrside
      181 hkisgwavrd ssgamqgygf arakddilvv gplvsadadm avrllkvlia dwrggiqldv
      241 pgvqasfqdr lrglgfreas vspqmllgas slpgrrellf aladpafg
//
LOCUS       WP_010491159             445 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SLC45 family MFS transporter [Lacticaseibacillus].
ACCESSION   WP_010491159
VERSION     WP_010491159.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..445
                     /product="SLC45 family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48399
     Region          17..434
                     /region_name="MFS_SLC45_SUC"
                     /note="Solute carrier family 45 and similar sugar
                     transporters of the Major Facilitator Superfamily of
                     transporters; cd17313"
                     /db_xref="CDD:340871"
     Site            order(27..28,31..32,35,67,131..132,134..136,139,159,
                     162..163,166,262,265..266,269..271,274,313,317,365..366,
                     370,374,391,394..395,398..399,402)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340871"
ORIGIN      
        1 menknkttlp nlplstiwml sfgflgvqma fslqssqmgr ifqtlgadpt klgfffilpp
       61 lagmvvqpiv gylsdrtwsk rfgrrmpyll vgalvsvivm fllpnsgsfg fktstalwfg
      121 aiailfmdls snvamqpfkm vvgdmvnekq ksyaysiqsf lsntgsvlat ifpylltaig
      181 vantaaagqv pdsvrisfyv gavilvifsl isvfsvheyd ndtykkyhgv alnednanek
      241 sksmlqllke apktfwsvtl tqffcwmafq ylwtygagsv aatvyhaadp tssgyqagan
      301 wfgilsavya vaaviwslvl skipagknkl gytlslflga igfisfffih sqfgllfsfi
      361 ligiswagmm aypfimvtna ldgyshmgty lglfngsicl pqivasvasf aifpavgskf
      421 pamilisgil mligslsvsl ikeki
//
LOCUS       WP_010491301             211 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Lacticaseibacillus zeae].
ACCESSION   WP_010491301
VERSION     WP_010491301.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..211
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23382
     Region          4..166
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mvshigvilg ttrknalgar ifnylkhtfp dtsevhytwl dlrdyplply dhpetpledp
       61 iqaptatetk wltamtnqdg yviltpeydh alpgglknal dligpevayk pvqiigyshf
      121 sdggmlaaas lvpilqmlkm ivlptptllw sadpcfdeng qinsaaensq hfarrlhetm
      181 hdigfytrll kehpyqplgs dtaanqtsat r
//
LOCUS       WP_010491343             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator
            [Lacticaseibacillus].
ACCESSION   WP_010491343
VERSION     WP_010491343.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..231
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27010
     Region          10..227
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mnevvpavkk nldlsqnrpi keavyealrk tillgeipsg erineknlse nlnisrtpir
       61 yalerldeed lverktgigv vvkgisinda yeifdirkel dvlairkamr lmtpdqfkqm
      121 ralleetdrl ndagrvsevm akftefnnfi ydashmlrlk mivnqlqnyl iyfrdising
      181 ddrrnlaiqe hwllyrgmln rdddqiklit rehlehslqy ilkvmkakhi e
//
LOCUS       WP_010491353             287 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase,
            partial [Paenibacillus elgii].
ACCESSION   WP_010491353
VERSION     WP_010491353.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..>287
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
     Region          <19..275
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mtepmlpeaf kqkmegllea eysaflasyg eerhyglrvn tlklsveqfr gltrmeletv
       61 pwaetgfyyr egdgrpgkhp hyhaglyyiq epsamapael ldvrpgervl dlcaapggkt
      121 tqlaaklqgt glivandvhp drvkalvkni elsgvrnavv lnedpakleg tftgyfdkil
      181 idapcsgegm frkeedmakv wrpdwpekya emqrmllrqa armlkpgglm vystctfspe
      241 eneamiaafl dehpafavep apafggwapg rpdwlggrya rgaetag
//
LOCUS       WP_010491357             160 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Paenibacillus elgii].
ACCESSION   WP_010491357
VERSION     WP_010491357.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..160
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=18185
     Region          65..156
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(86,89)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkklgiflai ivvlfgalyf vnqqsnqakf gkyannvygi apdklnpatl allddpnyqn
       61 iilpdaldkk iaaqedfyly yfgstcphck vttpvlmpva kdfnidvkqf nleefrdgwq
      121 kynieatptl iyykggkeve rlvgeqkaet fkaffekhkk
//
LOCUS       WP_010491443             177 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Paenibacillus elgii].
ACCESSION   WP_010491443
VERSION     WP_010491443.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..177
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19465
     Region          1..159
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mkitiiagsn rkeatstqlc ryiarlleek hcqvtlfdly ekplpfyngd ldqtdanive
       61 lrqrlleadg ivlatpeyhg smsgvlknal dftgfdhfdg kvtlsvssag gavgvsslqq
      121 lqtivrnlhg incpewisvg gaqrsftpeg epedaktrer vlktvgyfaq mistfrk
//
LOCUS       WP_010491465             463 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010491465
VERSION     WP_010491465.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 463)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..463
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51470
     Region          5..461
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mklldyfklg wdqlkrrvvv tllctmgiai gsasivvals fgesinqysq tkislylksd
       61 eitvtsggra egadpndpns mkpyeltkak igmmrtfpyi kalatyrtln qfefevdskk
      121 gyidqifate ldtlpafgye lqqggpseqe ntiilsygat mglfdsqisk arqqqlqsms
      181 erdarnawre qqyiaypvyq kqivlkpqiy rsndvgetvd iqipvrvvgi lkkpegvsdd
      241 mlirqktafv spalgkrlqe aiiqmnggkv kedknssqta dynevkikvd ssahvkeles
      301 llkklkltvq tnlsqeesmq nelliirlif ggagifilfv asisiivamt mstyqrrrqi
      361 gimkvlganl sqirnmfmve sallgllggl vgilvsywvi wginiaimqf tpprpgsqae
      421 ilfispwilp vglffaimtg vlsgiypaik asrtdaltai krd
//
LOCUS       WP_010491463             230 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010491463
VERSION     WP_010491463.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..230
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25393
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mlavehlshs frsgsentpv lhdidfrvdr gemiallgss gsgkstllnl maglmkptsg
       61 silisgqaie kmsenrlaef rrthigfifq syeliphltv renvelplvf qglrgkhrre
      121 kamsllskvg lgektemfps qlsggqqqrv siarslitqp aivfadeptg nldtktekei
      181 idllielnqt lgitfvivth emevakrtrr viqlrdgylv edgawagdae
//
LOCUS       WP_010491474              65 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Paenibacillus].
ACCESSION   WP_010491474
VERSION     WP_010491474.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..65
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6997
     Region          2..65
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mkgtvkwfna ekgygfiqve ggddvfvhfs aiqgdgfktl eegqavefei vqgnrgpqaa
       61 nvhkl
//
LOCUS       WP_010491480             560 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-binding protein [Paenibacillus elgii].
ACCESSION   WP_010491480
VERSION     WP_010491480.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..560
                     /product="thiamine pyrophosphate-binding protein"
                     /GO_component="GO:0005948 - acetolactate synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0009097 - isoleucine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009099 - L-valine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59629
     Region          25..556
                     /region_name="IlvB"
                     /note="Acetolactate synthase large subunit or other
                     thiamine pyrophosphate-requiring enzyme [Amino acid
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0028"
                     /db_xref="CDD:439799"
ORIGIN      
        1 mspftladaa appvladknq ptaglsvsqf lleqlkawkv eriygvigda nlslldelgk
       61 qnairyvacr hesaaalmas aeakltgrta vclatsgpgv tnmlnglada amdrapvlal
      121 sgqvetakig trtkqyvdqq klnaavagks elvthtdalp elmeqalvrg llqgqvthls
      181 ipkdlyplkv kgevkpyaah lhqpldapds eiaelaamlt faerpvlyig rgvkqaaedv
      241 lqlaeklsaa vittlparpl fpndhecyag glgqagseas svllsesdli vrlgatwwpd
      301 dyvptqariv qvdwnreaig lghplykgvv gdlgqivpkl aatghlsakd rsawrarvrd
      361 vctgwkrqie aeartdgtpi ppqrvmktia dhvsdqaiva vdtgdhtlwf nrifqakagq
      421 dilisgrwrt lgfalpaaia aklcypdrqa iavagdggvv qtlmefqtav eqrlpivlvv
      481 lnngayameq drmnvagmnl tgsalqppdf aaiaeacggs gyrassvael eqslrqaltd
      541 skpalidvrt aatpvphaki
//
LOCUS       WP_010491571             266 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010491571
VERSION     WP_010491571.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 266)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..266
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30516
     Region          1..78
                     /region_name="cupin_MmsR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MmsR, N-terminal cupin domain; cd06986"
                     /db_xref="CDD:380391"
     Region          172..254
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlfaghaqta pqhkvgpqvl dyhlvhtvvs grgnfrcvhr dyrlergnsf fifpgelvty
       61 vsdasepway rwvgfkgera deflskagis pdkpvissdr lrrltalyyq lektlhlakp
      121 gcdmqaggyl rllfgeyaqd rmreevpkee gsviqqqveq aircltlqyy qpisieqmar
      181 tlgyhrthls kmfkqhtgls pmqfllkirm eraklllqgp ltieqvassv gfgdalyfsk
      241 qfkkycghsp seyrhnrqvy pydceg
//
LOCUS       WP_010491577             679 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Paenibacillus elgii].
ACCESSION   WP_010491577
VERSION     WP_010491577.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..679
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=77976
     Region          2..654
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mardlpigng nvlmnfdvhy nvrdiyfpyv gqenqaldhl shfgvwtaed ffwidhpelk
       61 kqsgylndtl itnvacther lglklqlrdg vdvqenvfmr kvvvendwdr erevklyfhl
      121 dlhlygngvg dtvyydpelr slvfykghry mslsgrgqdq kevgitsyat gqkemnrleg
      181 twrdaedgrl ggnpiaqgsi dgtvelvlrv pargakeawf wicfaredqe lrklertvrs
      241 atpqallqrt ynywgqwlgh drhdlkllep dmasfykrsl lvvrtntdnr gailaandsd
      301 ilkfardtys ymwprdgali ahaldrsgyh altkrffqfc krglsedgyl lhkynpdgsv
      361 gsswhpwvna rgekqlaiqe detalvlfal whhhrqartl deargdydnl vlpaadfmar
      421 ytdasglplp shdlweeryg vhlftvasvy agllaaagfa ehfgdklram hyrdkaasvk
      481 qavehslyse qeqrfirsly wndekqayep dltldasmya ifdfgmfepd dprvvstmka
      541 ireqlwvqte vgglarysnd yyhqvtkdva kvpgnpwfic tlwyaeyvia aakseaelke
      601 aadllrwtmn halpsgilae qvhpfsgepm svspltwsha tfvkvvqeyl aklklfrhre
      661 rgqedqsdak llhaagekr
//
LOCUS       WP_010491684             271 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Lacticaseibacillus].
ACCESSION   WP_010491684
VERSION     WP_010491684.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..271
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29277
     Region          1..268
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mayadimhkh yneltksekk vadyvlsvgq kviyatmtdi kkathvgdat ivrfcqklgy
       61 sgftdfkiei akedfpktkp atsvhyydhi aqhlsdaika taalikpetl qtaiqmmtna
      121 triwifgvgg sgeiahslss illrsglkct peadphfqaq iasllspndl vigislsgkt
      181 kdtydslkia hdngakviai tnatvspiaq ladvtlqtai eeflnggsva grvsqlyicn
      241 vlaegyeqmn hvdalalkek vlraiidksi g
//
LOCUS       WP_010491713             295 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Paenibacillus
            elgii].
ACCESSION   WP_010491713
VERSION     WP_010491713.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..295
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31702
     Region          8..295
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mgkgnnasil avwislvsni vltllkltvg flsgsqvlla dgvhnagdvi ataaalssmr
       61 iskrpadddh pyghgkaevl gsafvaivla laalfigyha taalfeepae asvlaliaaf
      121 vslawkqaly mytirigrqt nskgliatay dhladvyasl aavvgialam lgeawsipyl
      181 aygdplagii vsilvlklay smgqeafdvl mekavkpekl geyaaliiti pqvkridrlr
      241 arehghyilv dlrvsipgel tvqeghdisr qikraimerh advdevlihl npwye
//
LOCUS       WP_010491722             271 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acetyl-CoA carboxylase carboxyltransferase subunit
            beta [Lacticaseibacillus].
ACCESSION   WP_010491722
VERSION     WP_010491722.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..271
                     /product="acetyl-CoA carboxylase carboxyltransferase
                     subunit beta"
                     /EC_number="2.1.3.15"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016743 - carboxyl- or
                     carbamoyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:2001295 - malonyl-CoA biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29364
     Region          13..270
                     /region_name="AccD"
                     /note="Acetyl-CoA carboxylase beta subunit [Lipid
                     transport and metabolism]; COG0777"
                     /db_xref="CDD:440540"
ORIGIN      
        1 mfqpqltqea lareaalpen lwiqcpyckq gsyreslgda qvcphchygf ritakkrlal
       61 vatettewda dlvttdpldf pgydkklaag rqatglkdsv wtgqaniggq vcglgimdpk
      121 fmmgslgtvt gerltrlfek ateaslpvvl ycasggarmq egihslmqma kvsaavknhs
      181 nagllyisil tdptmggvta sfamqgditl aephsligfa grrvieqtin qklpqnfqra
      241 etllqsgfid aivprseqea yvgdllkmhr a
//
LOCUS       WP_010491723             351 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Paenibacillus elgii].
ACCESSION   WP_010491723
VERSION     WP_010491723.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..351
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37088
     Region          75..342
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mlhrdqmknk rsgfkpwrlg gtiallllat acgsqaapaa gpvdgkegka pagayprtiv
       61 tggkhevvvp akpariaals ldtaemalel adpsrfavap rsldneqlsv haeqgkligt
      121 kitgatkldp eqvlsykpdl vlmttihnge kdadpilkqa gipvltfkew gsvrqimdql
      181 dligqalgee ekakvvtdrm kskleavrnk vegrkaaskp tvlvlspvgp ntgpymmgpd
      241 nissdlvrla ggvpaaeamg lprttkatie qiiqadpdci llsdwegkke qafreltgnp
      301 gwsalkavke grvrvmaakq lvnanpavvd siaeiadvle passvkkeag a
//
LOCUS       WP_010491847             130 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator
            [Lacticaseibacillus].
ACCESSION   WP_010491847
VERSION     WP_010491847.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..130
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14148
     Region          3..116
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mrivisnqsg kpiyeqiedq vkaailsgql kvneqlpsir slardlrisv itttrayhel
       61 eaagfitnvq gkgayvlgqd salvrenalr dieaslnqai dtanmahiap selhtmldtl
      121 lqaeetdhgr
//
LOCUS       WP_010491904             341 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010491904
VERSION     WP_010491904.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..341
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37073
     Region          5..328
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msknilqvrd lkvsfrtyag evqavrgvsf dlkkgevlai vgesgcgksv taqtimrlip
       61 tppsiiksgs ikfdgkteit kisnremeki rgsemgmifq dpmtslnptm tigkqiaegl
      121 ikhqglsase arkraveilk mvgisnpegr itqyphefsg gmrqrvmiai alacnpklli
      181 adepttaldv tiqaqiielm kklseqteas iivithdlgv vaemaqrviv myagkvveqg
      241 tvdelfydsk hpytwgllrs vprldqdkdg elvpipgtpp dlfappkgca faarcpyamk
      301 aclevdpeht klsethsaac wllhpdapkv erpveaggaa r
//
LOCUS       WP_010491934             462 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [Lacticaseibacillus].
ACCESSION   WP_010491934
VERSION     WP_010491934.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..462
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51879
     Region          30..427
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mesgqivpnl lvmlvtfffa affvacefal vqsrpsalee midkgtgrka kieralrmvh
       61 nlneylsttq vgvslagiil gwigettvef llvdlfglth lslpngslha vgailgviil
      121 tylevvltei vpknisidyp iktlmlvvtp lhyfhilffp fvwllnvsat givkmmgmkp
      181 adegneafsq aeilnlskna vtsgdmeqnd viymqrafel ndktakdimv drtslfvidi
      241 nttvkealrd yltqgysrfp vvangdkdki lgyvyiydlv kqgqvdpsvk vskllrsiin
      301 vpevtpihni ltqmikkqtp ivvvvdeygg tsgivtdkdi yeelfgtvkd eiddvsdeyi
      361 rktddpkvfr vsgkttlwdf erffhtnika ftdseiitia gfimethpdl klhdkvkidh
      421 fnftvadfsr gfanwfdvtq dpkpvkqtva eevkeakdkk qe
//
LOCUS       WP_010492089             220 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010492089
VERSION     WP_010492089.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25323
     Region          20..186
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mlpesnedwi eqllklsdee pkmtekqtki lhaaieifae kgyaaastse iaqkagvaeg
       61 tifrhyktkk dlllsivlpi maklvapfvl rnftpvleak ytryedflrs lirnrlefar
      121 qhlpmikilm qeipfhpdlq eqfktevmne vltrikkviv ffqqegqiip lpaatvvrlt
      181 asviigflit rfllvpeqew deeeeaetci rfimhglatr
//
LOCUS       WP_010492066             407 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Lacticaseibacillus zeae].
ACCESSION   WP_010492066
VERSION     WP_010492066.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..407
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43843
     Region          12..385
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(22..23,26..27,30,62,112..113,115..117,120,140,
                     143..144,147,221,224..225,228..230,233,260,264,313..314,
                     318,322,338,341..342,345..346,349)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mtkkapshar livgigiawl fdamdvgmls fviaalhkew qlstvemgwi gsvssigmav
       61 gailfgmmad rfgrkailil tllvfsigsg isafatgygi flvlrfiiga glggelpvas
      121 tlvsesvpve krgrsvvlle sfwaagwlla aiisyfimpv wgwrvavfat glaglyafyf
      181 reginesraf krvarpglik tlttlwhppy vrstimlwiv wfmvvfsyyg mflwlpsvmv
      241 lkgfslinsf gyvlimtlaq lpgyfvaawl iekwgrklvl slfllgtaas alafgmatsl
      301 pmlltagmll sffnlgawga lyayspeqyp tivrssgsgm aagigriggi vgpllvghll
      361 ganwsvtsif aiftasilia ivaivflgqe tmgvklvdsi etapskp
//
LOCUS       WP_010492105             147 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleoside 2-deoxyribosyltransferase
            [Lacticaseibacillus].
ACCESSION   WP_010492105
VERSION     WP_010492105.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..147
                     /product="nucleoside 2-deoxyribosyltransferase"
                     /calculated_mol_wt=16009
     Region          6..142
                     /region_name="RCL"
                     /note="Nucleoside 2-deoxyribosyltransferase [Nucleotide
                     transport and metabolism]; COG3613"
                     /db_xref="CDD:442831"
ORIGIN      
        1 maevylaapf fdpaqierld qvlaalhane svtaifsprd dtnkagltpn spgwqrqvfg
       61 ediqglhrst vlvaildyvg enpdpgtafe igyayahhmp ivalqlgemk mnlmlagsit
      121 cfvndltelk sldldhvlvr pyvgpvf
//
LOCUS       WP_010492146             294 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Paenibacillus elgii].
ACCESSION   WP_010492146
VERSION     WP_010492146.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..294
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=31630
     Region          11..293
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mqaglekakq hsklslpklv kraviillga alvsvglenf lvpnniidgg ivgisiitsh
       61 lsgipigvfl llfnlpflfi gykqigktfa lstlfavslm svgtwllhpv pplttdplla
      121 avfggiilgi gvgmvirsgg sldgteimai lfskkmpfsv gevvmffnlf ilssagfvfg
      181 wdhamyslia yyiafklidi tiegfdesks vwiigensre lgdaimnrlg rgvtylqgeg
      241 gftggnklvi fcvinrleea klksiveeld qsaflavgni hdvkggrfkk kdih
//
LOCUS       WP_010492180             403 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase
            [Lactobacillales].
ACCESSION   WP_010492180
VERSION     WP_010492180.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillales
  ORGANISM  Lactobacillales
            Bacteria; Bacillati; Bacillota; Bacilli.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Lactobacillales"
                     /db_xref="taxon:186826"
     Protein         1..403
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44848
     Region          2..403
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mkfdivvvgg stagfylvka lrtkgfsgsi clidredalp ynryklsknw ltgkkldapi
       61 fkpesffaen eiklqlntev vavhdekkkv vtadhqeity gqlvlamgae srhlhlpndd
      121 aegifylrsy hdaikikqws eqvkdvvlig agfislelas sfrklglnvt vvehgqhplg
      181 rvvgpqasey fvkmhqeqgv kfvlgsgves fthdqqhqvt gvvtdtgati paqmvvvgvg
      241 avpntsikad hlelgqnivv neygetalkd vyavgdatiw pfqgeeihve hwenaqshgk
      301 nvaanliqpq sqpydvlpyf wtdqydqtfe ylghttkwdq tfirgnldsg kftiayvden
      361 qvplailfan gnderadvte lmsrrqplds erfadtnqpl stl
//
LOCUS       WP_010492287             123 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF423 domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010492287
VERSION     WP_010492287.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..123
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=12724
     Region          1..119
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mnrtfvalgg icaflsvafg afgahalkgk laadmlanfq tgvqyqmmhs lgliaiglaa
       61 sllpanghlr ragwsmfigi vvfsgslyvl sitgikqlga itpiggvafl fgwlslvlal
      121 rtk
//
LOCUS       WP_010492296             410 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Lacticaseibacillus zeae].
ACCESSION   WP_010492296
VERSION     WP_010492296.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45418
     Region          18..398
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(28..29,32..33,36,68,123..124,126..128,131,151,
                     154..155,158,233,236..237,240..242,245,269,273,326..327,
                     331,335,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mdrhvfgatf sslrstnfrr fwigqcisvm gtwiqrttqt wlvyqmtksa flvgllaaaq
       61 fvpimaltlv agtlidrypk rqillltqfg flvlgaimtt ltflkiiqyw qilaialgyg
      121 ilqsfdtptr qsyvielvgr kdlmngisln ssifnlakia gpslagilmv tigvapcfli
      181 dtlsyiaiii glfmihqehp varhtprhii advkeglvyi vhhdnvklsa elmliictln
      241 fnnnviipiy aqevlgrgaq gyanllsatg igsliaaflm sylarfglrr dlyllvalgt
      301 aliqtlmifv hvywlamifm iiigfcnmvf lnqsnaafqf sipnelrgri msvyvllnqg
      361 stpigslyvg glmdfagglw gfpscgllal vlviptlfgh rttvkrwlht
//
LOCUS       WP_010492264             300 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010492264
VERSION     WP_010492264.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..300
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34325
     Region          2..78
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
     Region          53..276
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <171..276
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mrnepaiqlf ewsprvhidp fhthdhleig yclsgsgtfy fgqkayaaqp gdvfvvnhle
       61 rhaaasdadn psyylflyfd pmvieqadre lllpfvylpt kfqnripgel dtarrigklf
      121 heladeqrhk qpgyhgmmrg kilqicalll rhysgqtssa ewnrtltsyy rikpaldyid
      181 erfresltle daaavlglsp srarhlfqek lgvgfkkyll rlrvneakrl lastelpmad
      241 vmfasgfqsh apfyrafrki vgaapleyre lsrklalfen gldenkttmr spagynestt
//
LOCUS       WP_010492347             138 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010492347
VERSION     WP_010492347.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..138
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15306
     Region          1..124
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 meldqtdiei irllrqnari qwkeigenvf lsgqavgnri krledlgiiq aytvqvneek
       61 mgrsvlafit vfmkstnhsg fesfiqeqea vieafrvsge gcytvkaavs dpaalnvlld
      121 ailqygnykv nlaigkvk
//
LOCUS       WP_010492425             277 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010492425
VERSION     WP_010492425.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..277
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=30275
     Region          1..277
                     /region_name="MalG"
                     /note="ABC-type maltose transport system, permease
                     component MalG [Carbohydrate transport and metabolism];
                     COG3833"
                     /db_xref="CDD:443045"
ORIGIN      
        1 mskfknnlvv tgiyavfavl lvttvypivw ivgtslnpgd nllvskmipd hptiahyiel
       61 iqttdfvmwy qntikialvn avvstalvaa tayafsrfrf kgrqqglmml lilqmfpgfl
      121 svmaifvlll qtklldthlg liliyaggav smgtwvmkgh fdtipkslee aafidgasha
      181 daffkiifpl slpaitfval nsfitpfmdf ilpqivlrss dkmtlaqgly amvanetnss
      241 ftlfaagavl valpitllym yfqkylihgi aagadkg
//
LOCUS       WP_010492407             122 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase, partial [Lacticaseibacillus zeae].
ACCESSION   WP_010492407
VERSION     WP_010492407.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         <1..122
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          <2..119
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 ephmiaqhsg qiittdsvag hivhpgtavy sgtkwaiqai mdglrqeqaa nhikttmisp
       61 gavntelfst isdpkrreav esdeknngls atdvanavly aidqpanvav nevlmrpvtq
      121 qr
//
LOCUS       WP_010492427             432 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010492427
VERSION     WP_010492427.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15767475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..432
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48783
     Region          14..>109
                     /region_name="DUF5683"
                     /note="Family of unknown function (DUF5683); pfam18935"
                     /db_xref="CDD:465918"
     Region          135..430
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mqsqpsarrh qvtaavcsaa figlgqlynr qyikgllfiv laqlffwnyy siawkgilgl
       61 itlgdvptri irgkivqgdh sifllingli tlvvillflg fyamnvydak kngelrdegg
      121 hvlgfvesvk qakfrhfpyl lllpaaffil fvtviplvfn vliaftnysa pshipdralv
      181 dwvgfrtfyd lfaqeawrst ffgisvwniv waaastftvf lsglllammv nhpqvrfkkf
      241 wrtvfilpwa ipqfisilvf rvllngtfgp vndlivklgf spvpwlsdpt makvsvilvn
      301 lwfstpflma lmsgilttlp rdlyeaadvd gasglqkfvk itlplvlmat apifimqfaf
      361 nfnnfnliyl ltdgkpnnpd yyyagstdil iswifkmtln qsqfnmasav siimfiliaa
      421 fslwnykrmk sv
//
LOCUS       WP_010492441             297 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter permease [Lacticaseibacillus].
ACCESSION   WP_010492441
VERSION     WP_010492441.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 297)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..297
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31557
     Region          14..272
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mnslieffna lgkydflqsa lvtaimvgim sgligsfiil rgmslmgdai shavlpgvav
       61 aymlgvnvmi gasvfgiiaa lligfvaans kiktdtsigv vfsafyalgf ilismaesat
      121 nlhhilfgni lavsdsdimt taivlgivvl fvvlfykell itsfdntfak tyglnttaih
      181 yalmlvltlv tvsalqtvgi ilvvamlitp aataflwtdr letmlimaas vgvissitgl
      241 yfsftlnwas gpaivlvaav lfaisfifsp kqaffsfskr qrtkeaattq taeeivr
//
LOCUS       WP_010492469             134 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Paenibacillus].
ACCESSION   WP_010492469
VERSION     WP_010492469.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..134
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13988
     Region          1..129
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtmfselgal ivrivlgvtf llhglqkfqs gidkaagffq svglpgflay avggieligg
       61 icmilglgvr vfgalfsiim lgailtvkms qgfiggyefd lalfamslhl lisgnrvlav
      121 dslfrkrsae gasa
//
LOCUS       WP_010492523             252 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lacticaseibacillus zeae].
ACCESSION   WP_010492523
VERSION     WP_010492523.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..252
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27033
     Region          4..228
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mdkqpvvtve nvtktygkrg ekqtpalkgv sfqvepgefv gimgasgsgk ttllnilstl
       61 dhptsgavri kgqdvtklkg nalsdfrakk igfifqdfnl lenltgreni alplalqnvs
      121 akkqqaavdq iaatlgitav ldhyptelsg gqkqrvaaar alvqqpdilf gdeptgalds
      181 kaarelldtm ddlnknhgvs illvthdpfs asyasrilfi kdgqigselv hgdksqeafy
      241 qeiletlgtf qk
//
LOCUS       WP_010492543             199 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Lacticaseibacillus].
ACCESSION   WP_010492543
VERSION     WP_010492543.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..199
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22047
     Region          5..>85
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnqreqrkka tiarilaaaq tlfmtngyas vttrmiaeas nvqqpllyhy fgtkeklyla
       61 vvmqvsdtma akiasaqtgs gslaakvnhl ghvltddndm nlqmvihdia nlkasargrv
      121 fkawqdslla pldrffagfq selleayqpr evtlyflnvl avylrpanta enggfqqqlp
      181 ldralqmfct gvsrteeek
//
LOCUS       WP_010492547             236 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Lacticaseibacillus].
ACCESSION   WP_010492547
VERSION     WP_010492547.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25874
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtnlveltqv tkiygsgrta vtalqptdfv lkagefaaii gpsgsgkttl ltiignlqrp
       61 sggkviinhq dtthftehqr telrfntfgf ilqasnlipf ltvkdqlalv drfnhhkphk
      121 mskselfdml gitdladnyp aalsggerqr vaiaralynd ppivladept asldtkralq
      181 vvqqladiah ntdrgvimit hdtrlldpvd tvyemrdghl kalpktslek iqetai
//
LOCUS       WP_010492721             795 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Lacticaseibacillus zeae].
ACCESSION   WP_010492721
VERSION     WP_010492721.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..795
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=89108
     Region          180..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mahnrigire fveltvrtgd lnpitsnsnn taiigsqihr klqaahrepd yekevylktt
       61 vtvededyql egradgvwtd gdktltveei ktsarpwedc pqntkdrywa qariyghllc
      121 qqrhldhati tlvyvqtstd tisrftetkt aaeladdftd llteftdwlk lrsdiikrrn
      181 esidaldfpf peyragqhef aaavykaiys sarlfvqapt gtgktistlf ptvkamgsgl
      241 iqrafyltak qstrrvaeqa malmagsglk aksitltakd titfadepdd psqnpymlgy
      301 ydrlkpalhd llahedqitr svieayarkh tvdpfefsld aslfcdviic dynylfdplv
      361 flqrffsdad dsqfflvdea hnlvsrardm ytasitdqdf tnlkqalvpy kgaaltklrr
      421 aitrivntls aiadqrlmkq spvfeeapld dltnvlakft etvhdwlaep ptpalqpavd
      481 lvlpvfflan qylrigdfyd etfkteitkd hgvvtvkelc ldpshfvdes lkkgrgavlf
      541 satlspmpyf qkllggvdns ltyalpspfd pknqaiivdt svnttyrrre qdlpqliasl
      601 ttlvsakkgh ylfffpsyay lkiayaafta anptlktcvq enamteadrq afldhfkagh
      661 epvigfavlg gifaegidlr gaqligvaiv svglpglnae tdqlrdyfdq nagqgfayay
      721 qlpgfnnvlq aggrvirgak dvgvillide rfvtpryarl fpdhwthaqv srnpaqlaql
      781 lthfweahhe nptha
//
LOCUS       WP_010492593             296 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Paenibacillus elgii].
ACCESSION   WP_010492593
VERSION     WP_010492593.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10116212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..296
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=33706
     Region          58..>147
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
     Region          72..235
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
ORIGIN      
        1 mlndffnetv werawkedtq tavnkmkkag mdavrifdhr aksfneeafs eegrqrtrri
       61 mnwlegqgvt fkdtsildig aasggftvpf aerganvtsv epslplaell kenatgltng
      121 nvelvtepfe ninieakgwg kafdlvfvsm cpvivdwesv ekvlscarrf cyislaagsr
      181 ehslvneiwt lvtdqpqkte hlemaylqhl lylkgysyes litremktre vssetalmev
      241 mdwlkilglp addrnrqiva eylertypsd kveirqggrf gkvlirlqdq nmytra
//
LOCUS       WP_010492727             644 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Lacticaseibacillus zeae].
ACCESSION   WP_010492727
VERSION     WP_010492727.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..644
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=71611
     Region          8..592
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mkdkkllild fllkhgtvhy dqiaeatgls ertvgnylnr ldadlspyav klvrkrnvgv
       61 sldgpadqka hllrsihgqe gftsqtareh ylmikllltn rpytlsklad dlfvsrrtid
      121 ndfksvkrvf renhvtvqts rtgiqvtase srrrhmlakl lrgywgesls vakqkdgevv
      181 qqihlpayln hlvnpattka vmqslaeflk qsdlifsdya lqslaihlii acerpkktap
      241 apvhpapllp etkqlltlvt khvhrtldna daqqinahia aildrqvsda paasiedqaa
      301 pvlrqqiagw ltgispdtrl lddlsvhlsg alarisqgmt ipnpyteeik rnfpmafdaa
      361 aqlsmavakh yhvtfnddes gflalhfesf ferqhaadri stvvvcssgv gtsrllaqrl
      421 eerfreklvi trtigladlm rqtipetlii stvpiqgmrq pvvivnplll qhdiekvaqq
      481 adrlrfgtdg daflslldpk lvlpnlpqtd qhaamqamir qltkngvfed etlplklaed
      541 reklattamr lvaiphispe mvqrpaialg lapegidwsg qkvkvvffla lnaaapgdqr
      601 riyqvmnrmi ddrlfcekla qsptpasalk tlseyvhkga ngfe
//
LOCUS       WP_010492732             238 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Lacticaseibacillus zeae].
ACCESSION   WP_010492732
VERSION     WP_010492732.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..238
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27018
     Region          1..234
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mekvpltkql vnqletfike klqpndklps erdlselyhv srntvrsaln elflrgfiyr
       61 stgkgtfvae rfdertdvsg sysftkqmla mdrqpvtkiq rlekiavpas iakrmridpg
      121 tpvyvldrlr iadklpmmie rsylpaltvp dlekdalaks plydwleehy gihiasvdea
      181 ffaglvsped akllrvapas aclnirrttf adtgeiveyt lsvaradqfv yhvhhvnh
//
LOCUS       WP_010492739             614 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Paenibacillus elgii].
ACCESSION   WP_010492739
VERSION     WP_010492739.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 614)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 614)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 614)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..614
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=69408
     Region          178..593
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mrlwpwlykr ytekiqlrlt vyfvlvlvpl vivslfanfr fqrilleqte ertkgaltss
       61 mdyidvtlqn veqistlaat nnnllkllne tgpsltaqsy vnfyevikel ssitsispmv
      121 sqislyhass rmllntangg kviehplqvl rlqelaeagg taityimpdm efpgrqtfgs
      181 vlntdsislv rtmdlnnpdr epnlliitln kdklldllls llpspqaqia lyndmgqlvt
      241 gtesagrmrs gvdedsgsgs vistkvdsay ykwslvltqp keelyretnl nrtytyiiig
      301 vsivlaclis wgvysgiasp vqrllkgmkr vgsgnfnvrl endradelgy ltrafnkmve
      361 eqrhlienyy eqqlqlante lkflqsqinp hflyntldsi ywtaknydad eisemvlnls
      421 sffrlslskg retfsveetv thlhyyirvq qlrfleaftv syelseeskn vpvlklilqp
      481 lvenailhgl ekrrdgrlli asrveegclv ltvqdngtgi pparlehirs elaklatyes
      541 grlsyrqsnp kdlfglrnvm srilivygqr aelkigsaeg qgttatlilp lekckenhel
      601 epphpglhqe vkla
//
LOCUS       WP_010492810             281 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Lacticaseibacillus zeae].
ACCESSION   WP_010492810
VERSION     WP_010492810.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 281)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..281
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29753
     Region          5..274
                     /region_name="ABC_perm_SloB"
                     /note="metal ABC transporter permease subunit; NF040927"
                     /db_xref="CDD:468860"
ORIGIN      
        1 mtltfwhdla efhflqnall tsitvgivag vigsfvilrg mslmgdaish avlpgvavsf
       61 mvgmptvvga atfgiaaail itlirqhsli ksdtaigiif ssflalgvil ialvhtttnl
      121 fhilfgnvla vqdkdmylti giaavvialv vlffrrlrlt sfdpvmaqam gihtnayhyl
      181 lmvmltlvav vsmqsvgtil ivallitpaa tiylfanrlr tmviasgalg glisfvglvi
      241 gysfniavgs civllgtcvf ivcfpfskkq nliklpiggr s
//
LOCUS       WP_010492814             460 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Lacticaseibacillus].
ACCESSION   WP_010492814
VERSION     WP_010492814.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..460
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49256
     Region          11..446
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(18..19,22..23,26,58,108..109,111..113,116,136,
                     139..140,143,263,266..267,270..272,275,303,307,359..360,
                     364,368,384,387..388,391..392,395)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mikqwlilit lglfffmvii dgtivvvavp tiakdlavsp srvnllltvy lttisvcllf
       61 fgqladqygr srlfiwgtyl fligsglagf gshfqlvlaa rvvqavgasm tmatsyaiva
      121 dvfppallgr algiesifis agalagpglg glilsrlpwg yifwvnlpig llclliewav
      181 fprvtaasgk kkadhrgflq liviggllll lqinhvpllt igllvliggg tylfwrherq
      241 apeamldtrl frnqrfsrnl aasflnyvaa yfftllapiy lqlilrvpva vsgyllmltp
      301 ltalvanpla gfltdrcdrr rlmvvgllll vvtnaafalv pnekvlwpfv ivsvvfalgt
      361 alftnpnsvv liqsvdasmr gqvgaatsla rqlgmsigsa vaglvfyqtl glirpnvtaa
      421 nagapallta qcvsfllaag lfliaamilg kkvkdakrtg
//
LOCUS       WP_010492877             188 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Paenibacillus elgii].
ACCESSION   WP_010492877
VERSION     WP_010492877.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..188
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21396
     Region          5..187
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 miehalmdkw lffykymrsp kqigsvtpss rflasklvsp iawdevkava elgagtgavt
       61 rfirqanrgr avtllfeqdp llrsklgqhy peaiccpdaa hmrqelerng ipqldavisg
      121 lpfynfteql rerlleeihs vlkpggqfia fqyslqmkra lqqkfvleki afvpwnvppa
      181 fvyvcrkk
//
LOCUS       WP_010492833             599 aa            linear   BCT 01-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010492833
VERSION     WP_010492833.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..599
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=67182
     Region          <199..287
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mslqvltdlh qevrrlfiag ssvaagdlrl trllpqlrkl genapvfnrl adgvqlvtea
       61 kpeqasakll elgtllhsil ytqgrteaqg tleevqvtdt rgvtaipyrk mralidalte
      121 rgpgrlevir egyedslfqd frthmpavaa ledgyaeiae fiydkvipsi gpavipilhr
      181 qlnlqggkgd arklylihhl qgpvnaelil qaageggaev riaavdilgd ypeqedvvle
      241 qsyerrkevr raalsalsrl gtgraadrlf ealtgkdrel avepiqassh paltqrildq
      301 aeawlngfdg ssakteaveq lsaavqclkg kndeavrvfl ekllsspafm vkettavqey
      361 aagllldmqr pegyrfvesl yrqwggkhis ysfqaalrcl speevydqfa plihhkqqaq
      421 akellntlyd lterlaltvy rdaedssvis wdprwvhlfl dineeelvcr fvqepdtkit
      481 dyllkkvrva pqqmkprtvs lffalfkigh eetpellmqa legskgrqfy yldrdklalm
      541 sllpgsyaer lekfadllsy esvkqqvlev aerlktktsd eaemgkgagw iewikskmy
//
LOCUS       WP_010492903             327 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010492903
VERSION     WP_010492903.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..327
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34096
     Region          19..327
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msavivekse arkiksngfi skfgaligli ilctvltils dnfltvdnvm niarqssina
       61 llaigmllpi ltagidlsvg silalsimmm givsvnhgln pylgivvclg vgallgwtng
      121 imltklklph pfistlgtmn iargialiit gaapiagfaa piqfagnqfv gpvpfsfilv
      181 ivvyilfdif lnrtstgryi yaiggnketa rlsginvnki lvivytlsgl maglaglvmv
      241 grvnsafpla gmgyeldaia aviiggasff ggvgtvwgtl igatiiavlr nglnllnvsa
      301 dfqmaiiglv ivaavyvdvl rqrsfkk
//
LOCUS       WP_010492919             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Cof-type HAD-IIB family hydrolase
            [Lacticaseibacillus].
ACCESSION   WP_010492919
VERSION     WP_010492919.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..272
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29486
     Region          4..268
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,199,221..223,225..226)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mfrliavdld dtlldshkql ssatirglka aqakgikivp ctgrplpgvr ttldalglhg
       61 ddqyvivqgg gvvqstngki iaqkflnhqd yqdfstfath vsaagidsnv itpagdvyta
      121 drniskytvl qawenhagik vrepqempdd fviakglllg epenlakiqp qaeaefgnrf
      181 tvirsmpfml eimprgvnkg wglaqltqyl glhpdnviaf gdehndldmf dfagtsiava
      241 ngqdvvkdqa dyvtasnded gvvqalkhfk ii
//
LOCUS       WP_010492966             489 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 32 protein [Paenibacillus elgii].
ACCESSION   WP_010492966
VERSION     WP_010492966.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..489
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55514
     Region          3..483
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mrdkyrpqfh ftpeknwmnd pnglvyynge yhlfyqyhph gttwgtmhwg havsgdlvrw
       61 ehrpvalaad ehgeifsgsa vvdwqdtsgf fggepglvai fthhrnpdsd ggrpvesqsl
      121 aysgdfgrtw tkyegnpvla dgsrtdyrdp kvfwheptkr wililasgqt iciyhspnlk
      181 dwtfasefge gegahlgvwe cpdlfelpvd gdetrtkwvm fvsmgsspeh pegsrtqyfi
      241 gsfdgtvfrn enapetvlwl dygrdnyagv swsdvpaedg rriyigwmsn wkyaqvtpte
      301 swrsamtvpr alslrcrger vtltqqpvre lerlrteayq wrdhilgegg nplsgmrlgc
      361 femiaefesg eadefgfkvr asdaretvlg ydtrkqelfv drtrsgeagf hedfpgrhaa
      421 klelrenrlr lhilvdassv evfggdgeav itdlifpese dqelavytkg gsakllsldi
      481 fplqsirde
//
LOCUS       WP_010492987             142 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Lacticaseibacillus].
ACCESSION   WP_010492987
VERSION     WP_010492987.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..142
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=15478
     Region          8..137
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 mqderwnhpl ytteaindeg leghayvpgg lkvqtsspmn dhpgtnpeql lglslstcle
       61 atleavekeh glphtgavrv kvafigarae yqflvhaqvm vkgvdldtak afteeienrc
      121 pvskllknsg nytietvtdf dd
//
LOCUS       WP_010493055             844 aa            linear   BCT 01-JAN-2025
DEFINITION  M1 family metallopeptidase [Lacticaseibacillus zeae].
ACCESSION   WP_010493055
VERSION     WP_010493055.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 844)
  AUTHORS   Evnouchidou,I., Koumantou,D., Nugue,M. and Saveanu,L.
  TITLE     M1-aminopeptidase family - beyond antigen-trimming activities
  JOURNAL   Curr Opin Immunol 83, 102337 (2023)
   PUBMED   37216842
REFERENCE   2  (residues 1 to 844)
  AUTHORS   Peer,W.A.
  TITLE     The role of multifunctional M1 metallopeptidases in cell cycle
            progression
  JOURNAL   Ann Bot 107 (7), 1171-1181 (2011)
   PUBMED   21258033
REFERENCE   3  (residues 1 to 844)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   4  (residues 1 to 844)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..844
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..844
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=94426
     Region          14..437
                     /region_name="M1_APN-Q_like"
                     /note="Peptidase M1 aminopeptidase N catalytic domain
                     family which includes aminopeptidase N (APN),
                     aminopeptidase Q (APQ), tricorn interacting factor F3, and
                     endoplasmic reticulum aminopeptidase 1 (ERAP1); cd09601"
                     /db_xref="CDD:341064"
     Site            order(119,121,253..256,289..290,293,312,316,370,376)
                     /site_type="active"
                     /db_xref="CDD:341064"
     Region          508..812
                     /region_name="ERAP1_C"
                     /note="ERAP1-like C-terminal domain; pfam11838"
                     /db_xref="CDD:463368"
ORIGIN      
        1 mseaahfyet fqpshydlyl dinretktis gktsiigeak qpniavhqky lkvesveann
       61 qavpfttddp aeavritlpk agdvkltity tapltdtmmg iypsyyevdg vkkqiigtqf
      121 ettaarqafp svdepeakat fdlaikfdeq pgetvisnmp evreingvhy fdttvrmsty
      181 liafafgelq skqtttksgv kigvfatkah kpneldfald iakrsiefye dfyqtpyplp
      241 hswqlalpdf sagamenwgl vtyreallti dpdntsletk ervatviahe lahqwfgdlv
      301 tmkwwddlwl nesfanmmey vavdalqpdw hiweafqtle vpmalqrdat dgvqsvhvqv
      361 edpaeidslf dsaivyakga rmlvmvrali gddalraglk ayfeahkfgn aagadlwaal
      421 gqashldvgk imqswleqpg ypvvtaavvd gkltlsqqqf figtgkevgr qwqiplnsny
      481 tvapqifadk qvtlgdyaql rqdsgkpfrv nvgnnshfiv qydqtlltdi ldhldqlnai
      541 dqrqilqdlr llaegrqnsy anivpllprf aeshsaivin alyrvandlk qfvtpdssde
      601 aqlkaffdql sagqfkrlgw lpkpgetndd qltrpyvlsm alyaknatai aqghdlftan
      661 kdqllqlpad vrmfvlqnev knfgttalfd qlltaykqtt dssykadila altstpdkal
      721 igkivdqfen adtikpqdlr swfrgvlnnh vgeqaawdwi rkewswlekt vggdmeftty
      781 itviagifrt anrldefkaf fepklptpgl treitmdtsv iasrvdliqa eqqavngava
      841 kavk
//
LOCUS       WP_010493060             473 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Paenibacillus elgii].
ACCESSION   WP_010493060
VERSION     WP_010493060.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..473
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51892
     Region          35..446
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(45..46,49..50,53,85,135..136,138..140,143,163,
                     166..167,170,282,285..286,289..291,294,321,325,374..375,
                     379,383,399,402..403,406..407,410)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mntthpmnst hpmnttnvkn rldrlplsrf hkmvlvilsf ayffdfcdln tfsyvapalv
       61 qewnittnti afitsvsyfg mflgasfggw fsdrfgrkrg lillvtwfsa fsllsalawn
      121 pvalgvlrfl tsvgigavti lastyiseff pskakgkyqa lcitigicgi paagwvaksv
      181 ipmapwgwra vfifggigiv fpfiarklee sarwheargq wdkaheimar iereveretg
      241 klpapepvsg dslhhaakka apysqlfkgp llgrtlmlmt mwatstiaiq gfgtwvptll
      301 vkqgitieks iayvtlgtlg aplgafiasr isdrverrwa iailsviimg lgllygmval
      361 plviivcgfl mhmfertfss iayiytpely pteargsgng ltygigrlan mvspfiisfl
      421 ysgygylsvf vffgacwllc aaaiavfgvs tryrgteeas sapelkanta dvm
//
LOCUS       WP_010493088             187 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Paenibacillus elgii].
ACCESSION   WP_010493088
VERSION     WP_010493088.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..187
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21263
     Region          1..178
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdqeklymkq crngdkeaff klvepllsrv ystsaailrs shlaedavqn alleayqaim
       61 ngknirnfks wfnhltacra ldlarqrskl asrtgdleei evpdeqaspi dalirkeagh
      121 ellesvmsld inhrtvvily yyqelsldei advldvkkgt iksrlhaarl klnekmmepn
      181 pkqvmec
//
LOCUS       WP_010493106             390 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Paenibacillus elgii].
ACCESSION   WP_010493106
VERSION     WP_010493106.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..390
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42932
     Region          30..390
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mspnqpsdmf irsereaela aladrlaarf aqrapehdre gsfpfdnfad lresgylrlt
       61 vpqeyggdgi slyelvlaqe rlargdgsta lavgwhvgqm lhfrctrswp ealfarfcge
      121 vvregaminh fgtepatgsp srggkpqtta vrteggwlls grkiystlcp vlnhftvtag
      181 iegedatgvf fvrrgpdirv eetwdtigmr atgshdlvle hafvpeaell grsdsgwprv
      241 ddgdgwllhi pacyigiaha ardfaigfar dyrpnslpgp iaelphirqq vgqmeadlit
      301 artllyamad rwdrdeagrp alkpelglvk yvatnhairi vdiamrivgg aslsrklple
      361 rmyrdvragl hnppmddval qrlaaralae
//
LOCUS       WP_010493114             136 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Paenibacillus elgii].
ACCESSION   WP_010493114
VERSION     WP_010493114.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..136
                     /product="VOC family protein"
                     /calculated_mol_wt=14712
     Region          4..128
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(4..9,24,57..58,61,76..81,83,87,116,126)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 maklipflvs edaraqaefy ihalggeirs vmthgqlpda sealkdkvlh mcvmaggitf
       61 fmsdsvfepl nhgngiqlnl efpteaeare afaklgeggt vklplepafw gslfgqiedk
      121 ygviwmitnq aqasqa
//
LOCUS       WP_010493158             214 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Paenibacillus elgii].
ACCESSION   WP_010493158
VERSION     WP_010493158.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..214
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=22813
     Region          5..210
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 miytalgdsi tfgenassla kaypqltvsa lnsdsrkvrg fvlarsgwss ddlldaviwr
       61 gasaialssv vsvwiggvdl anaalasftt kqplavkhli agyrrnvsai ltrikkgsra
      121 rivcctqynp fpntplavea igqlnrmise lahscnatva pthswfegkq aelvygyrsg
      181 kiedalsgsl pihpndrghr viaaglapyl iphk
//
LOCUS       WP_010493207             141 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Paenibacillus elgii].
ACCESSION   WP_010493207
VERSION     WP_010493207.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..141
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16063
     Region          8..140
                     /region_name="SRPBCC_CalC_Aha1-like_4"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of an uncharacterized subgroup of CalC- and Aha1-like
                     proteins; cd08897"
                     /db_xref="CDD:176906"
     Site            order(9,11,13,22..24,26..27,32,38,55,57,59,61,71,73..74,
                     76,79,85,87..88,94..95,97,99,109,111,113,115,119..127,
                     129..131,134)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176906"
ORIGIN      
        1 metsqptkvt vqaviqapve kvwrywtepd hitkwnqase dwhapraend lrvdgkfltr
       61 meakdgsmgf dfggvydvvn rheaigytme dgrrvdiafv dqgnetkvie tfdaessnpv
      121 efqqagwqai mdnfkayteq n
//
LOCUS       WP_010493240             189 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Lacticaseibacillus].
ACCESSION   WP_010493240
VERSION     WP_010493240.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..189
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21513
     Region          3..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mttkhrilnr eivldaartm vaqdgirdlt fqtlakelni csqslynyfp nlpaviealg
       61 tefmhnlyqe lienvsgisg keairafaev ahryferqqs ldeiiyfvhq fpesspfvqg
      121 tgdvinllkr livhtelkqm akesfvqdfi ssvlgftvle vmgflpdnka srdtsfesll
      181 dmylneike
//
LOCUS       WP_010493242             313 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010493242
VERSION     WP_010493242.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..313
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33521
     Region          9..312
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msehihvpvl evndlsvaft rydrglrqst vevirslhlt vgrgellaiv gssgsgksll
       61 ahailgilpd naavsgtlry egepltparq ealrgkeial vpqsvnflnp lmrvgdqvrs
      121 svregdadaa vrrifdryrl apgterrfpf qlsggmarrv lvstatvggp rlviadeptp
      181 gldpaavret lsrfrelade gcavllithd iesvlpfadn vavfyagttv etapagdfsg
      241 dgarlrhpys ralwqalpqn gftpipgvqp hpsalppgcl faprcaaagt dcsrerpemr
      301 elrggtvrci hat
//
LOCUS       WP_010493260             510 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Paenibacillus elgii].
ACCESSION   WP_010493260
VERSION     WP_010493260.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..510
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=54060
     Region          1..459
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mlaatvcqql rsivgdawfr ddtetlvsys ydatplyqsm pdgvifpast eevaavmrac
       61 aqhripvvtr gagsnlcagv vplhgglimv mtrmnrllei dqdnltatfq tglntkrfht
      121 aveetglfyp pdpssmiict mggnialgag glrglkygtt kdyvigleav lasgevlrtg
      181 gklvkdvagy dltrllvgsg gtlailteat vklvpkpayr ramiavfadl psaartvsqi
      241 ianritpctl efmdqatiev veafakiglp idaqailaie qdgdeaqvek dlqlieaicr
      301 regaiqvkva atseegakvm earrsalaal srlrpttile datvprskia dmvlevqria
      361 akhnvrictf ghagdgnlhp tamtdardae eihrvelafe eifdaairlg gtitgehgvg
      421 hvkapylewk vgasgislmk rlklafdpdg llnpgklfae trkrvvftse pgagneaggp
      481 aepgqsgage rglsgdsied grdpatkgga
//
LOCUS       WP_010493285             111 aa            linear   BCT 01-JAN-2025
DEFINITION  L,D-transpeptidase [Paenibacillus elgii].
ACCESSION   WP_010493285
VERSION     WP_010493285.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..111
                     /product="L,D-transpeptidase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=12061
     Region          5..109
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mayriivals qrtlhllegd rvirsypiai gkiltqspvg eyrivnkvph pggpfgafwm
       61 glsrphygih gtnnpasigh avshgcirmy nedvlalarl vpigtrvsir p
//
LOCUS       WP_010493313             151 aa            linear   BCT 01-JAN-2025
DEFINITION  DinB family protein [Paenibacillus elgii].
ACCESSION   WP_010493313
VERSION     WP_010493313.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..151
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17488
     Region          4..143
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 mlrlfrynwm vrdewfetfe aiseedmlle rtggvgsilk tlfhivdvec swirvikgep
       61 dpepafndfa sldkvrqlsv qyrievedfl vhwtnesdde pvttgmeetf tqgeilrhvi
      121 aheihhvgql svwakelglr avsanfirrg l
//
LOCUS       WP_010493398             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Lacticaseibacillus].
ACCESSION   WP_010493398
VERSION     WP_010493398.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..146
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16187
     Region          5..134
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 maerslyhty vrnenglvge syvegnqgla lgvssslida pgtnpeqfia falstcfnat
       61 irivqhregt aedsqlrtrv dierdkigyk fivdaqilmp shtreeaqki vtqaldecpv
      121 akllkenenv sfrivdeftd eptlge
//
LOCUS       WP_010493403             268 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010493403
VERSION     WP_010493403.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..268
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30359
     Region          <28..>66
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <52..268
                     /region_name="PRK10572"
                     /note="arabinose operon transcriptional regulator AraC"
                     /db_xref="CDD:236717"
     Region          181..262
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 meaevftcgy syhaqrfhth yktglplylf rlqtegasea vidgkthrlg qgdllllnpg
       61 rtyelfvdey ettskgrsis sgdyylicgg rwidqwwkrg dkptlaridp geqllalwrh
      121 liiekqrpad kqtgeligcl lqalclsler aatesapsyg rsftalrmkr fveehatstf
      181 kiedaarqag lsvsravhlf kecygktmle yaleirlaaa lermkytamt leqiaescgf
      241 ggysyfhrvf kekfgispga yrsgehrk
//
LOCUS       WP_010493445             187 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Paenibacillus elgii].
ACCESSION   WP_010493445
VERSION     WP_010493445.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..187
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21124
     Region          122..171
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 migaycslyk sckrcgqsky yrqfpprggr kvsgssrkni crkcerkkpa vpapqappvp
       61 raakllrqdr qgmirmkgks nngrpwmqei ewslavllve eqaavvvtpy mirrlysndd
      121 frsmimtrdh ytcrycggyg dtidhivpks kgghttpvnc vcscylcnqs kadqdaagfm
      181 ekqrfpv
//
LOCUS       WP_010493456             408 aa            linear   BCT 01-JAN-2025
DEFINITION  Ger(x)C family spore germination protein [Paenibacillus elgii].
ACCESSION   WP_010493456
VERSION     WP_010493456.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Cooper,G.R. and Moir,A.
  TITLE     Amino acid residues in the GerAB protein important in the function
            and assembly of the alanine spore germination receptor of Bacillus
            subtilis 168
  JOURNAL   J Bacteriol 193 (9), 2261-2267 (2011)
   PUBMED   21378181
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Li,Y., Setlow,B., Setlow,P. and Hao,B.
  TITLE     Crystal structure of the GerBC component of a Bacillus subtilis
            spore germinant receptor
  JOURNAL   J Mol Biol 402 (1), 8-16 (2010)
   PUBMED   20654628
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Hudson,K.D., Corfe,B.M., Kemp,E.H., Feavers,I.M., Coote,P.J. and
            Moir,A.
  TITLE     Localization of GerAA and GerAC germination proteins in the
            Bacillus subtilis spore
  JOURNAL   J Bacteriol 183 (14), 4317-4322 (2001)
   PUBMED   11418573
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..408
                     /product="Ger(x)C family spore germination protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=45037
     Region          27..389
                     /region_name="GerAC"
                     /note="Spore germination receptor GerABC, GerC subunit
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG5903"
                     /db_xref="CDD:444605"
ORIGIN      
        1 mvpgagwkgl rlvmtasaal lllllpgcwd rkevndlaii maagldkaeg glvklsvqlf
       61 vprvsggggq dsggsggggk tpasgqtilr satgntlada mtklqeklsr rifwghgevf
      121 vfgealareg irenidfimr dpgpreraem fickgraqdi ltllpplers saeslremak
      181 sqtglkvtvk dfaemlvsda gaaalpwiet lpaqpgsdpk rtdayingsv ilkkdrmvgf
      241 iddrvtrgll wlrdeveaat vtlapkegkg lisfkildsr tkllpliegd rwsvtvriqt
      301 eddviqnttn inlvdpkvte slekqlsaei ekrirvalvh pqkelhadif nfaeafrrry
      361 pqlwkkekqr weerfpqvev riesrarivr tgmatvqatr pknevkpk
//
LOCUS       WP_010493478             325 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010493478
VERSION     WP_010493478.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..325
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35927
     Region          5..325
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mnktlvefkh vhtyfhtesg vvkavndvsf riregetvgi vgesgsgksv talslmrlva
       61 dngkiesgtv emdgrdllsl kpeemrrlrg seiamvfqep msslnpvlti geqlmeplme
      121 hrllsrkeak aevlsligkv gipdavrvfa ayphelsggm lqrvmiasal acspklliad
      181 epttaldvti qaqildllrq vkeqyntail lithdlgvva etadyvvvmy sgkvieeapv
      241 velfrhakhp ytqgllkskp vigerkdrly sipgqvpnli glgdscyfsd rcehcmdicr
      301 tkqppmraqg aehrvacwly eeesr
//
LOCUS       WP_010493497             254 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator
            [Lacticaseibacillus zeae].
ACCESSION   WP_010493497
VERSION     WP_010493497.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..254
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28144
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlkderllti rnlvdrkgiv tvneigdslg vstmtvrrdl eeladrneli rihggaqsth
       61 fkpltelsrn ekrsihvnek rkiaatiadi itsgdtvyig pgttmelisq ylkkpevrii
      121 tnslpvfqsf qdradyfslk liggqlrers gafigslane mlahltttka fisvngiadn
      181 hisnaspeeg qtqrialnna gmkfvaadhf klnrqdfysf ydldqtdgli tddgisaddk
      241 qhfseytsvi vgka
//
LOCUS       WP_010493505             172 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator
            [Lacticaseibacillus].
ACCESSION   WP_010493505
VERSION     WP_010493505.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..172
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=19876
     Region          4..86
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          94..>145
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mnneqiilgl lykkdrtgye lnevfkdifs hfydasfgmi yptlrrlakn glvskkmvvq
       61 agrpnkniys itpagkkefe aslttptlpd trhsdflmrl yfgeyekpad ltrimqeqvn
      121 wlkeqidklq drlqewpnit ppqklsftig iaeyeaqlkv lqreltpaks td
//
LOCUS       WP_010493507             194 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Lacticaseibacillus zeae].
ACCESSION   WP_010493507
VERSION     WP_010493507.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..194
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=21919
     Region          3..187
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mtkfliiyth pysgsfnhav lekvqeklqr qgdttdvidl yrdefnptyd aeelklfhag
       61 qthdplvtqy lqkikaaeal iiitpiwwnd ipgmlkgfid kvmkegpglt hvvtkrgvqg
      121 tltnikkgyi lttstsptfy lrffcgnavk kvligatlkq lgirhvqwtn fggitnsteg
      181 qrrlylqsid kkaf
//
LOCUS       WP_010493567             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GtrA family protein [Lacticaseibacillus].
ACCESSION   WP_010493567
VERSION     WP_010493567.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus
  ORGANISM  Lacticaseibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Lacticaseibacillus"
                     /db_xref="taxon:2759736"
     Protein         1..135
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15231
     Region          1..127
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mrlklkqfis fglvgginti ltyliyltly qlinptaamg vgygltsilg lflndtwvfk
       61 vkdhrqlksv apryyfsygl tfilslvlts fwndalglpk plapmfslmv tvptnfllsk
      121 fwvfrekgvt ahekn
//
LOCUS       WP_010493647             450 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Paenibacillus elgii].
ACCESSION   WP_010493647
VERSION     WP_010493647.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..450
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48633
     Region          12..445
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mksiakkiel tppqilvigf aaiillgatl lslpissasg qptlfidalf tatsatcvtg
       61 lvvvdtgshy smfgqiviis liqvgglgfm tmatlfafvl rkrislkerl ilqeamnqgs
      121 megivrlirr vlvysltief vaavifsirw sfdlgiakgi yfgifhaisf fnnagfdlfg
      181 svvapftslt tyaddwivni vsmgliilgg igfvvmsdvv dyrkhkrlsl hskvvlsatg
      241 llivvgaivf fifeftnqkt lgslnwsgki lasffqsvsp rtagantvdi gamrqasqff
      301 tiilmfigas pgstgggikt ttfttligam iamirgkedi vlfhyrlgkd rilkaitltm
      361 ialflvifvt mlltttenqs flkllfevts afgtvgltmg vtpdlsffgk imisltmfag
      421 rlgpltlaya lgpkaekely rypegkitig
//
LOCUS       WP_010493568             142 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Paenibacillus elgii].
ACCESSION   WP_010493568
VERSION     WP_010493568.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..142
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15208
     Region          2..141
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mpyqnilaaf dgsalsvkal ekaikfaqdh aarlevihvc hipvpvfggp lyaapfneek
       61 dyllaaqaii deakrltsql pdvevtlkqg qpalavleya eesgcdliim gsrglgglre
      121 fvlgsvshhv vqhskvpvli vk
//
LOCUS       WP_010493648             782 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Lacticaseibacillus zeae].
ACCESSION   WP_010493648
VERSION     WP_010493648.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..782
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=83982
     Region          11..664
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(301..303,366,384..386,414,463..465,512,515,518,537,
                     540)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(597,601..602,604..605,630,633..634)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
ORIGIN      
        1 maaqnispdq glsaqqvqqr fdngqhnlpl kpltrsisqi iqvntftlfn lvnvvlgali
       61 ittgsyknll flgvaiinta igtiqeiqak rqidkmsila aahatvirdg qrqkidleql
      121 vmddmvllkr gdqipvdgtv vatnglesde spltgesrpi tkkvgdplls gafvvsgqat
      181 mqvtavgkdt faaklsleak aekasqsqll atinriirvl tyvlipigii lfsvsmirrg
      241 nynrailtts aamigmipeg lvlltnvala vsarnlavkr vlvralpaie alarvdticl
      301 dktgtitsgk lkvantlpaa ghtaedvtsa aaaivyalnd dnetalaika aigadanqqv
      361 tqtmpfssar kwsgavvdgr alfmgapqft fgdqlpadia tqikqaasng yrvlavgtak
      421 tlaqplvnpe llglilitde lrptaintfd ffksqgvalk visgddpitv aniakqahle
      481 gadrsvdmst iaadateadf qalvkqynvf grvtpdqkkq limayqalgh tvamtgdgvn
      541 dvlalrqsdc siamasgsda assiadfvll dsnfdamtgv lnegrrvinn iervasmylv
      601 ktmysvilat ifvflpldyp ivpinltpvs aigvaipsff ltlepnferv tgqfmqkvmt
      661 vaapaaisvv vytllltwme sflnlsfdtt stmvamligt islnvllvva rpfnrlkvgl
      721 laglsaalfl vffifnhvfs laslwqwqla liyvplmvst vpfylliqef lgrrvlskin
      781 wr
//
LOCUS       WP_010493663             314 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Lacticaseibacillus zeae].
ACCESSION   WP_010493663
VERSION     WP_010493663.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..314
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34779
     Region          57..309
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mrkhkkawli gilsvvgviv vgligaslyf yqyafvpskk sflsgkesri itdgkawlks
       61 vhketwtqqa vgdklklvad yvpaakpttk tvvvahgymt nkeymapqik mfhdagfnvl
      121 apddrgqgqs egnyigygwp drldylkwin qiikkqgkqs qialygvsmg gatvmyvsge
      181 klppqvksiv edcgytsiid elayqaksmf nlpkwplvpa valtatlkag ynvfdasaie
      241 alhkntrpil fihgakdtfv ptkmvyqnyr aatkakkalw vvkgaahars fpdhpqvyak
      301 rvvgwfnanw clta
//
LOCUS       WP_010493802             371 aa            linear   BCT 01-JAN-2025
DEFINITION  Ger(x)C family spore germination protein [Paenibacillus elgii].
ACCESSION   WP_010493802
VERSION     WP_010493802.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Cooper,G.R. and Moir,A.
  TITLE     Amino acid residues in the GerAB protein important in the function
            and assembly of the alanine spore germination receptor of Bacillus
            subtilis 168
  JOURNAL   J Bacteriol 193 (9), 2261-2267 (2011)
   PUBMED   21378181
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Li,Y., Setlow,B., Setlow,P. and Hao,B.
  TITLE     Crystal structure of the GerBC component of a Bacillus subtilis
            spore germinant receptor
  JOURNAL   J Mol Biol 402 (1), 8-16 (2010)
   PUBMED   20654628
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Hudson,K.D., Corfe,B.M., Kemp,E.H., Feavers,I.M., Coote,P.J. and
            Moir,A.
  TITLE     Localization of GerAA and GerAC germination proteins in the
            Bacillus subtilis spore
  JOURNAL   J Bacteriol 183 (14), 4317-4322 (2001)
   PUBMED   11418573
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..371
                     /product="Ger(x)C family spore germination protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=41960
     Region          1..365
                     /region_name="GerAC"
                     /note="Spore germination receptor GerABC, GerC subunit
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG5903"
                     /db_xref="CDD:444605"
ORIGIN      
        1 mkrwirtavl avcvamlagc wdqaniedlt lslstgidld ekdnlmvyma apvfskeakr
       61 knevyefrsk tlrvarnkfd svvtaltvgg ksqmlllgkr lveqadwfpl tdiffrdgkq
      121 tvnakvvlvn gpvsdvihhy pkdkprlslh ltrlldknnr rnftvrttiq klidqkyekg
      181 mtisiselkl seefevtgta lldkkgkykg slnqqessll lilqrrttge vpfnvhvpne
      241 rksgvfasdv vsfnagvekv kiktaynqgk frfdvgihls gavtqrlflf dfskkgeele
      301 atiekqldkq fselvkkfqs lkvdpvgfgi yarahqykey kqvqeqwgdv fakadvnvkv
      361 kltlkssgti k
//
LOCUS       WP_010493942             317 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010493942
VERSION     WP_010493942.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..317
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32991
     Region          1..312
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mqteakaggk ragkafslgp llglalivvv lsvinsdflt itnifnvlrq isinaliafg
       61 mtfviltggi dlsvgavlal ssaftagmma sgmnpwlavl vglgcgavfg avngllvtkg
      121 kvapfiatla tmtvyrgltl vytqgrpitg lhedfaiigk gyfleipmpi vwmvltfiil
      181 fiilkyttfg rrvyalgsne eatwlsgint srikvmvysv sgllaalsgi iltsrlnsaq
      241 ptagtsyeld aiaavvlggt slsggrgwlv gtligamiig vldnglnlln vssfyqlvvk
      301 gaviliavll drskaak
//
LOCUS       WP_010493880             305 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010493880
VERSION     WP_010493880.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..305
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33858
     Region          7..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mgnesiitth nlskhyrsrk avdkvgldir kcdiygflgp ngagktttir mllglirpte
       61 gtihifgkdl rkeqrailrk vgslveypsy yghltayenl etirrildvp ksridevlai
      121 vrltkeakrp vkgfslgmkq rlgiasallg hpellildep tngldptgil eirelikamp
      181 kehgitvlvs shllseielm atrvgiiqqg ammfedtidr lreraqssir ialsnperaq
      241 rtvaltgcha elressllie hisddtlaei vallvqsghs iyrveevkks leniflemvg
      301 egtsl
//
LOCUS       WP_010494043             200 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Paenibacillus elgii].
ACCESSION   WP_010494043
VERSION     WP_010494043.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..200
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22847
     Region          3..200
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mnllqvvqql feqygyfvll iglpldfial pippgnstla ytgylsfkgv lswlpafaaa
       61 ltgafigvtv tywighkvgm plierygkwl slkpahvekt rryydkygek llliaffipg
      121 irqflgyfig iirvpyrkvv iyayagttlw vtsffavgyv fgeqwehmfm liernlkvff
      181 iglgcvatgf llfrwvkrar
//
LOCUS       WP_010494083             359 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Paenibacillus elgii].
ACCESSION   WP_010494083
VERSION     WP_010494083.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..359
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39151
     Region          4..356
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msandkiqig vigagnignv hiqeflqipd aavtavtdvy qpmaiarake ynipnvyaty
       61 qellqdpsld avivavpnda hapiaiealq agkhvllekp mavnaasake ivkahlksgk
      121 vlmmshqmrw eslnmqvkeq idkgalgsiy nvktgwlrrk gipgwgtwft qmhksgggpl
      181 idigvhmldl slhlmgspkp vsvfgttyae fgpkkrgigt wgkpdwngfy dvedlatali
      241 kldngstlsl dvswaantdf idngpyiylm gseggaslra grgtlytelf ertadveltv
      301 dsndegprqr msrhfldcir ehrepltsam sgltnslvle aiyessrtgq lvtldwsld
//
LOCUS       WP_010494165              92 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase, partial [Paenibacillus elgii].
ACCESSION   WP_010494165
VERSION     WP_010494165.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         <1..92
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
     Region          6..82
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 erdhcvgmgt avaedgwsgf inivvhpqlr gqgigkrivh elarwsrdqg anrlylqvia
       61 dnapairlys gagyeklfay hyrtkpmdnl ll
//
LOCUS       WP_010494245             244 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010494245
VERSION     WP_010494245.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..244
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27297
     Region          4..185
                     /region_name="ABC2_membrane_4"
                     /note="ABC-2 family transporter protein; pfam12730"
                     /db_xref="CDD:403819"
ORIGIN      
        1 mvnllyteli kmkrakmfmv sllgavsapi mmflallnmk skkpetpief evafmntnmy
       61 villvgtlly gvitaylfhr eyaedtmknl ltipvsrvsl ivsklillfl wimvltftiw
      121 sltlilglig qfegltmall lqslkqfvig gallfllctp tmlitflfkn yvptiiftam
      181 itmanvvlse seykalfpws asyviangdf ipqyppafsy avilaaslig laatiiyfkk
      241 vdih
//
LOCUS       WP_010494293             286 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Paenibacillus elgii].
ACCESSION   WP_010494293
VERSION     WP_010494293.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..286
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32608
     Region          3..241
                     /region_name="AKR_unchar"
                     /note="uncharacterized aldo-keto reductase (AKR)
                     superfamily protein; cd19100"
                     /db_xref="CDD:381326"
     Site            order(19..21,50,55,80,111..112,147..148,168,199..205,211,
                     227..230,235,238..239)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381326"
     Site            order(50,55,80,111)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381326"
ORIGIN      
        1 mehryfgasd kqfpilgfga qrivdehqct eedairivnr aidegityfd tapsysdgqs
       61 eerlgkalrh rrsdvwiatk thdrtrdgsw rlleaslnrl qtdrvdewrl hnlvtmddle
      121 qcfakggame amleakeqgi ikaisvsght npevqleaie rfpfdsalva lsaadhfiys
      181 fahefvprav ekgvavigmk vmalgklapw yeqalrytfs lpvattiigm etmdqleknl
      241 aiakrfrpms dteqldflke iihlatpdvl rwkasewmsg ewyrrd
//
LOCUS       WP_010494300             233 aa            linear   BCT 01-JAN-2025
DEFINITION  TerC family protein [Paenibacillus elgii].
ACCESSION   WP_010494300
VERSION     WP_010494300.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..233
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24651
     Region          15..181
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 megdllvgll klilinivls gdnavviala crnlpaeqqk kaifwgsfga illrivltfv
       61 avwllkvpfv qvagalllly iavkllkged naetlksssk igeaiqtiiv adlvmsldnv
      121 lavagaaggn lllivvglai siplivwgsq llmrlmnrfp iivllgaall gytagemtls
      181 dkavghwiet sfpaghyvlp ialaalvvvv gklagrrqer ehakkeaekh avs
//
LOCUS       WP_010494312             139 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Paenibacillus elgii].
ACCESSION   WP_010494312
VERSION     WP_010494312.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..139
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14211
     Region          7..117
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mnkkyevsll lirlvlgisf lvhgvvkfqs gigniagwfe siglpgfaay vvaiievagg
       61 ialilglgtr lvstlfallm igaivkakwa ggflgspqma gyeldlaffv malalaiags
      121 sllslgslls agnskrada
//
LOCUS       WP_010494319             147 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus elgii].
ACCESSION   WP_010494319
VERSION     WP_010494319.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..147
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16702
     Region          11..147
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mdlsivpvht eeqlrdcfav rirvfveeqg vspeeemddy daspsaakhf limngnepaa
       61 aarwimydgk taklqriavm kpyrgyglgr qiiqameedi rtqdvpviil daqtqaepfy
      121 eklgyktvst epfldagiwh vrmrkel
//
LOCUS       WP_010494330             122 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Paenibacillus elgii].
ACCESSION   WP_010494330
VERSION     WP_010494330.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..122
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13593
     Region          1..114
                     /region_name="CatE"
                     /note="Catechol-2,3-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2514"
                     /db_xref="CDD:442004"
ORIGIN      
        1 mklthlnlcv ndlseatdff qhlfgfqlld qkgdalavms dgegftlvls rfgeetvtyp
       61 kdfhigfyve tmaevdefha klaaanipte hgprkmrggy tlyftalggv lfevtsffre
      121 se
//
LOCUS       WP_010494332             237 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010494332
VERSION     WP_010494332.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..237
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27307
     Region          27..>118
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          87..233
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 markrisppd silgwpeaea ahipldrvri lqtalqvlde iglkelsmrk iadklqvkta
       61 slyyhfkdke qlmqllsdki sgemvwpeas lpwkervlqw gvqfrkvllq hrdavelfnl
      121 tigvgyqrlt qieklyqlfv sagfadpqip wiasmlknyv lgfvaeesrl hafagdedhg
      181 sfeamgeqys rffrqlpeeh fpntirlaph itntdwekef tfglsvlieg fstfqqk
//
LOCUS       WP_010494346             173 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Paenibacillus elgii].
ACCESSION   WP_010494346
VERSION     WP_010494346.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..173
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20164
     Region          20..161
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mnpkqyqpas adgqkqlqpf rsfveslqdp iyrlayrllq drelaaqeve rtfvevfrry
       61 aeegfaptng smrtaayrml ihrckmskas gkrrlkprkl sprtileavd alpdevrliv
      121 slkyecqlsy eeigeilems pervkkgvwr srerlsewme eprsplsfgi imh
//
LOCUS       WP_010494424             254 aa            linear   BCT 01-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Paenibacillus elgii].
ACCESSION   WP_010494424
VERSION     WP_010494424.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..254
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28509
     Region          1..238
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mitqeqvdfy hengyllvkg vfnseeveam rtatdaiidr aakskfdrsd twqgdylppe
       61 qlkklvlkgf hdvhyhdavf tralchpnma avlsrligpn vqvhhskmlv kppekgaafp
      121 mhqdypyfph akhsmiaasi hlddsdmeng clcvipgthk hgpmphvgah ylnhkeypis
      181 sgtpcpasag dvlffnylti hgsdvnrsvr prrnvlvqyr dpedlpteev hvnwgqglmv
      241 cghnpifkey kgah
//
LOCUS       WP_010494418             278 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010494418
VERSION     WP_010494418.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..278
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32494
     Region          25..89
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(35,60)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(42..43,54,57,61..62)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          107..273
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mnnerrrkel adflrtrrlr lspqelglqv dtsrrrtpgl rreevaslsg islpwytale
       61 qgrdiqvsdq vleslvrtlr lskdernhlr vlanhsnvsk gtenetlsps lqqildrlgt
      121 ypayiidkhw nvlawnkits slcgdfngma eiernilwrv ftmdhekkri vnwenvatsm
      181 lahfrsryam ymndswyqel vgrlwdrsee frllwgrhdv sgslegdkvv rhpkaglltf
      241 ryntfplsen sdflmrvytp vepdgtdrql qellqesc
//
LOCUS       WP_010494428             133 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Paenibacillus elgii].
ACCESSION   WP_010494428
VERSION     WP_010494428.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..133
                     /product="VOC family protein"
                     /calculated_mol_wt=14226
     Region          5..129
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(5..10,25,58..59,62,77..82,84,88,117,127)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mkanltpfis senaraqaef ylqalggeiq stitfgeipg tpeehkdkvm ymamtvaggn
       61 vlfmsdsfgp vsknggiama lsfgdeaear eayanlgkgg tdkypfalqp wgayygevvd
      121 kfgitwqivk qgq
//
LOCUS       WP_010494476             272 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Paenibacillus
            elgii].
ACCESSION   WP_010494476
VERSION     WP_010494476.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..272
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=29223
     Region          118..221
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mslkrtivyy lgitlgitfm mqavtgaayt patillmmwv pgiaavvftl lgktprpgtl
       61 glrlcrpydl imaaaipvlt fvittagsal lfegsvrwgd yklmamtdsf tlnllvtilv
      121 vvaksclfal geelgwrgya qsrmiasfgs vkgivilgiv wgywhfgvtl tgatfkgapl
      181 lgalvlmpla cigmsfmfaw ltlksgsvwp aavahgitni lfdfsflltd ykgsaalyyt
      241 wivavmllvg gifmcliqrm rppvtegtns aa
//
LOCUS       WP_010494478             127 aa            linear   BCT 01-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Paenibacillus
            elgii].
ACCESSION   WP_010494478
VERSION     WP_010494478.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..127
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14776
     Region          3..125
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mnnpphitea esevmkllwq kepltaieii sklkdqmdws dqtiktflnr lhkknairfe
       61 ksgrnylyyp lvsydeyvka anrsfldrmy ngavgmlfak fleeeklses eidqlqqlld
      121 kkkkggs
//
LOCUS       WP_010494482             299 aa            linear   BCT 01-JAN-2025
DEFINITION  toll/interleukin-1 receptor domain-containing protein
            [Paenibacillus elgii].
ACCESSION   WP_010494482
VERSION     WP_010494482.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Nimma,S., Gu,W., Maruta,N., Li,Y., Pan,M., Saikot,F.K., Lim,B.Y.J.,
            McGuinness,H.Y., Zaoti,Z.F., Li,S., Desa,S., Manik,M.K.,
            Nanson,J.D. and Kobe,B.
  TITLE     Structural Evolution of TIR-Domain Signalosomes
  JOURNAL   Front Immunol 12, 784484 (2021)
   PUBMED   34868065
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Essuman,K., Summers,D.W., Sasaki,Y., Mao,X., Yim,A.K.Y.,
            DiAntonio,A. and Milbrandt,J.
  TITLE     TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes
  JOURNAL   Curr Biol 28 (3), 421-430 (2018)
   PUBMED   29395922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..299
                     /product="toll/interleukin-1 receptor domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=34976
     Region          2..>136
                     /region_name="COG4916"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443944"
ORIGIN      
        1 mydlfishas edkenfvrpl alllnrlsvr vwydeftlnl gdslsrsidk glidsqfglv
       61 vlskdfmnkk wpdyelrsli skelaygkvv lpiwhgidrd dllnfspyll dklaintsqk
      121 tieeialnic kivkpdifnn ftrfmmyeqi yrdssleege sfskeeiqkv ldnfpvrhkt
      181 lplhlvnrik iiyhlfkyfs sqtlektidn fkhdtnpere iiiweaicst yieilkfipd
      241 kettkkeafg lvlfistnqs rdllykrfri fdkdiietai skfgeslpvs sssilmmnk
//
LOCUS       WP_010494530             126 aa            linear   BCT 01-JAN-2025
DEFINITION  GtrA family protein [Paenibacillus elgii].
ACCESSION   WP_010494530
VERSION     WP_010494530.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..126
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14152
     Region          9..124
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mirklynnel irflfvggln tafgysifal fifvglhysl aslfstiigi lfnfkstgil
       61 vfnskknsli ykfiavygiv ylinvsllki lslfitnvyf sgaiillpla vlsyilnkkf
      121 vfkvdl
//
LOCUS       WP_010494536             566 aa            linear   BCT 01-JAN-2025
DEFINITION  ribonuclease J [Ligilactobacillus acidipiscis].
ACCESSION   WP_010494536
VERSION     WP_010494536.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..566
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=62958
     Region          1..552
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mseikisalg gvrengknmy iveikdeifi ldcglkypen ellgidtvip dfdylrense
       61 kivgvflshg hadaigalpy flsefnvpvf gseftialak ivcenedssk kfndfhvina
      121 dteidfenat vsffstthsv peslgivikt nkgnivytgd fkfdqtatds yrtdfgrlae
      181 igkegviall sdsanaenps epvdehviad lisetfeyhk grvvvacvas nlmrvqqvld
      241 aaaanerkvt ltgfdaekvi ntalkmkklq lpkkdllikp admskyapeq lvileagrag
      301 eplkslyrma tgkykginls dgdlafittt pshamdtkva ktrdmiyrsg aevkaisdey
      361 nssghaskrd lqllinllkp kyvvpiqgey rllvahaesa eqvgikpqni fllkngdlle
      421 ydkgkmimas sieagntmid gsgvgdigni vlrdrkvlsd dgifiavvti drkkhriidt
      481 pkitsrgfvf vkaskdlmte sgeivkkvvq nnldnkefdw shlkqdiren lnhylyeqth
      541 rhpvilpiim evnqhrhykk kkqask
//
LOCUS       WP_010494553             116 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system PemK/MazF family toxin
            [Paenibacillus].
ACCESSION   WP_010494553
VERSION     WP_010494553.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..116
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=12774
     Region          2..113
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mivkrgdvff adlspvvgse qggirpvlii qndignrfsp tvivaaitaq iqkaklpthv
       61 eidaeahgfd rdsvilleqi rtidkqrltd kithldeetm rkvdealqis vglief
//
LOCUS       WP_010494572             247 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerophosphodiester phosphodiesterase [Paenibacillus elgii].
ACCESSION   WP_010494572
VERSION     WP_010494572.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..247
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26907
     Region          4..244
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mtiqqpivig hrgaageape ntlasfelal rqgadaield vhlsadgevi vchdhtvgrt
       61 tdgtgaiael tvaelkqlda grwfderfag erlplleevf qlvplemmin vevkcsytpr
      121 laarlaella qynrldsvvv ssfnhkvlkq lqeaipnlra gllyvanfvs hrqmaaaaeg
      181 lnvysihpqh htidagdaae atgyglrvyp wtvnepqdlr riidagvsgi itdfpgrlrn
      241 llnegka
//
LOCUS       WP_010494613             218 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010494613
VERSION     WP_010494613.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 218)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..218
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23564
     Region          5..208
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mqtfagvfem mardwdkllk lmlehlymsl sgvllaaaig vplavfmtrn rkiaqtiqvf
       61 vnmvqtipsi alllivmiff glgyttaiia licysflpii qntyeglrsv dphlieagkg
      121 mgmtdlqllv kvkfplampv mmagfrvatv isigvatiat fvgagglgem iyrgiattdd
      181 vkvlagsipa allavsidfl lrwiekktgc nlhkaksh
//
LOCUS       WP_010494647             169 aa            linear   BCT 01-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Paenibacillus elgii].
ACCESSION   WP_010494647
VERSION     WP_010494647.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..169
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=19465
     Region          12..123
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 mkwkpldsti gedeiraves eysiqfpplf kaflmsyhyv slqfdnvevd geyigdcrfi
       61 elpslsseer lqpldfsina wepllsagyv pfaecedsqg pvcfdtmrrq edgdcpvvwf
      121 lhdhlhelge emsrnrdhlv pyvrpifgsf kemmtvlcnr eaaaedtee
//
LOCUS       WP_010494658             180 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010494658
VERSION     WP_010494658.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 180)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..180
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20408
     Region          41..177
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mnfeekvket khlfkghvid ldletvelpn gknaqreivr hhgavgival tpadkmifir
       61 qwrtplgket leipagkiel nesndpllta qremneetry qaqnyellst fysspgfsne
      121 lmylyhasgl spvktklpqd kdeflqieel ssaeidsaiq ngeicdakti mavlfwklme
//
LOCUS       WP_010494682             268 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010494682
VERSION     WP_010494682.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..268
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29571
     Region          2..249
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mrvevqglsy gvkgvpiiqg vdlriqpgef vgiigpngsg kstllkniyr vlkpqagwis
       61 ldgqqlselt hketaqrmav vsqetssafd ftvrdivlmg rhphkrmfaa dtreddalvg
      121 ealervgmea yarrsfssls ggekqrvlia ralaqqsqfl imdeptnhld iryqlqmmdl
      181 vktlgmtals alhdlnmacy fcdrlivmne gkvyasgtpe evmsaellrq vfgvsaqlav
      241 hpvtrklsit yfpeslqphl kpkgvlis
//
LOCUS       WP_010494685             291 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Paenibacillus elgii].
ACCESSION   WP_010494685
VERSION     WP_010494685.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..291
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=32805
     Region          39..273
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mykhlkslil iiptltigiw eyirhafllp yismdlgnwl apllvylvtm tllrklfamm
       61 eqlqgqlqqe raakaaleer ekvaselhdg iaqslfllsv rvdrmeqsha vpmgelyqsl
      121 qktvhevndy vrqaidglry pavpqaqpwm esvqhliadf rkdtgivvql ewelsedrmt
      181 vkekvelyat lrealinvfk hagaanvwiq gkdasgsdtg wrctvaddgq gfvsdplskk
      241 ngyglkiiqd raakmgwafa lrrengrtvl tvsrpddaaf ghkgvsrteg r
//
LOCUS       WP_010494351             439 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 125 protein [Paenibacillus elgii].
ACCESSION   WP_010494351
VERSION     WP_010494351.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..439
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50845
     Region          17..436
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 meqfrlpkip ipamelprav qdvlaeaevk lahrpkllql fkncfpntla tttkrmedgt
       61 tfiitgdipa mwlrdsveqv ihyvplaknd pelqqliagl ikrhiqyihi dpyanafnes
      121 andwhwnttd etemspwvwe rkfeldsicf smrlaykywk etertdifdt nfksamrktv
      181 dlwkteqrhf elspyrfmrn ndvptdslrn nglgmpvnyt gmiwsgfrps ddacdfhyni
      241 psnmfavvtl rqmremaewv frdlafvdel kkleadvdhg iqlygiyrhp efgpiyayet
      301 dgfgnyclmd dagtpglmsi pyigyttpdd piyqntrrfa lskqnpfyye gkvakgigsp
      361 htppdyiwhm alsmqgltav tkeeklemla mleatdadtg fmhegfhadd ptvftrswfa
      421 wsnslfsllv yeamkegiv
//
LOCUS       WP_010494725              69 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Ligilactobacillus acidipiscis].
ACCESSION   WP_010494725
VERSION     WP_010494725.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..69
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7328
     Region          1..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mltgkvrsfn kdkgfgfitp ddggddffvh fsailttgyk vleagqkvsf vsvegirgpq
       61 acdvtilte
//
LOCUS       WP_010494793             224 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010494793
VERSION     WP_010494793.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..224
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24675
     Region          103..221
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mvelpaargd dswsgilqvv vvfamiliff ggygwyvehk vkvgprfsvp vhighlissv
       61 ttglllivvl nlvlqfilqv lhivpetaqn qaginrmlel nsmskfvtlf lavivapvce
      121 etiyrlllig piktkqvkpt trhrkrlavl swvffilahm gqqlygvivs pswngtvaai
      181 tasltygvls fvlvreyylh gslarsmvih mswnalaagv llln
//
LOCUS       WP_010494795              93 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010494795
VERSION     WP_010494795.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..93
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10843
     Region          3..92
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mkivnasftv rpgwqpyyeh fisemvdrsr kengnvsydh fkklgvgney eiiehwaddd
       61 alqahkdsas ykefwrginh yvkteptvtv ldh
//
LOCUS       WP_010494824             134 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010494824
VERSION     WP_010494824.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..134
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=15307
     Region          1..109
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mkftddvpiy rqieqyiage iisgrfqsgk qvpsvrqlal qfsvntntvq ralremiikn
       61 ilesrrglgn fvtsdptiie dlrqnlinks llamykqlha lnisdveikg clddflekrr
      121 sedgkhdrte kcll
//
LOCUS       WP_010494844             158 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010494844
VERSION     WP_010494844.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..158
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17757
     Region          8..151
                     /region_name="YdbS"
                     /note="Uncharacterized membrane protein YdbS, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3402"
                     /db_xref="CDD:442629"
ORIGIN      
        1 miepqeqidr kaiivwrwsg fiasavsall aavvfylahr fhwpgwipvv laagvlaeiv
       61 ltvlvmpelr wkrwryevre deimlqqgvm fvkrtlipmv riqhvdthqg pllrayglag
      121 itfstaagsh qipaltseta ealrvriael akvshedl
//
LOCUS       WP_010494972             325 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Paenibacillus elgii].
ACCESSION   WP_010494972
VERSION     WP_010494972.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..325
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=38062
     Region          1..308
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mddlyetffn akiaegvskr tlesyeenyr flceylamtd tprevnsvtp evlrkyitwm
       61 lrskrkwegh ahkaerdktv glsavtvntr mkglrtmfnf lydedlietn pfhkvkpvre
      121 peneiqimst dqlerilkap drrtyagfrd yvfmtllvdg fyrinealkl kesdinfetg
      181 mtlisaervk trrskavple kstlrllrdl ikenadfete yifltnygsl isddrmrdri
      241 kqhakkagle vrvyphlfrh taatmfleng gdvrflaeil ghsdlrmvlr ythlskksvk
      301 eqhgkfspin nvmsglnkqr kikrn
//
LOCUS       WP_010494981             153 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010494981
VERSION     WP_010494981.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 153)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..153
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17365
     Region          8..143
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04677"
                     /db_xref="CDD:467560"
ORIGIN      
        1 mrdyikdird kvghmpiiln avagvvvnde hnillqertd thnwslpggy meygetflet
       61 lnremkedsg lkvevvdmig tfeqgfttyp ngdqaqvisr lylvepaggs llkertdetl
      121 slkyfsfsdl ppllnqqnmd mikaaakyfh eef
//
LOCUS       WP_010495103             197 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Paenibacillus elgii].
ACCESSION   WP_010495103
VERSION     WP_010495103.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..197
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21000
     Region          <11..144
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 msvtgvfdgw kltspygyrv dpfngsrsfh tgvdlvkyhk ypipafvggv vlfageggpg
       61 tgfggygnvv aikdakgyvh cyahldsvae aavkgraiqr gdivgyqgtt grstgshlhy
      121 evrakdtpgy gygshvdpga yleaclktee pvldsgvrdt iintwldpal qkanaagdkq
      181 qadyirwlta elrkasv
//
LOCUS       WP_010495029             140 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Lactobacillaceae].
ACCESSION   WP_010495029
VERSION     WP_010495029.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillaceae
  ORGANISM  Lactobacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Lactobacillaceae"
                     /db_xref="taxon:33958"
     Protein         1..140
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=15702
     Region          22..134
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 maittfkakv vstddpnkyi sysrdftvkf qtnelnngyd egitpnegil calgacediv
       61 aasfykkekf eysslyipvr geisgkrpgf dnigvdihfr tpkekteitk fvkfmedtcp
      121 vrdnlvntvp ivtkevksek
//
LOCUS       WP_010495143             197 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Paenibacillus elgii].
ACCESSION   WP_010495143
VERSION     WP_010495143.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..197
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23128
     Region          2..185
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtdsqlirei kdgnvqlyde lmrryerkil afifhmlksa qmeslaedlc netfykayrs
       61 lhsfreveat fstwlytiar ntvlselrkh kntqvsleqs gytpqtavet lpeqtalrne
      121 kvtmvrdain nlpekqrsal ilreydqldy qeianilgqt vssvksllfr arasvklqle
      181 pyflepifee yeemnrr
//
LOCUS       WP_010495236             194 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010495236
VERSION     WP_010495236.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22128
     Region          3..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mppdqmetkd kilqatldmi rkegfenvti rkiaahsdtn ialinyhfgs kdkliseaik
       61 imllgfrgtf dvlddsalpp kerlktflih yvqvirehpe lvsriiatgt amfasqveyg
      121 eflremgfhk iqaalqqitq edrpdqlmmm itqlfgaifl palmkpiles gagvkmlpvg
      181 eqidwffery fhdk
//
LOCUS       WP_010495220            1045 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010495220
VERSION     WP_010495220.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1045)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1045)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1045)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1045)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..1045
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=119042
     Region          5..1037
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 msrnsyiteq dvenmaldsl ekigyriyks dsytrpnnli damrnsdynn vflagkleya
       61 lrkinpgyel diykeavrqf erladnpdmm idnhrlhqli iggakvktld kgeprtitly
      121 pidfnkvdnn efiatnqftv rqnekerrpd vtlfvnglpl vtfefkdsan envgiqqafs
      181 qlqtykseis nymeyneilv isdginarag sltagmdrfm rwrapkniqe epgtlqleil
      241 ikymlnpkdl lniienfvif etnadqtvki ltayhqyymv nkalksaeht lndpddkrig
      301 vvwhttgsgk slsmvffsgm aarklgnpti lvindrndld dqlfgtfasa heylqqdpsh
      361 aetsedvrey msrnsggivf stiqkfspnf dngeeempvl tkrsnlivma deahrtqygm
      421 aaklsengir ygfakylrda lpnasfvgft gtpidkedks ttavfgnyid vyditqavnd
      481 natvriyyes hvfplklkes akekyqqlie eagldddpsl penerrnrky tqlealagar
      541 prlesiakhf vhhfesrqae qfgksmvvem srknavklyn eiikirpdwg nddlhkgkmk
      601 iimtsnasdg pemskhhtsk adrlvlqkrm kdnddelqiv ividmwltgf dvpamntmyi
      661 dkpmkghnli qaiarvnrvf knkdsglivd yigiaealkt alnhyskddq dqvginihea
      721 lsllkekyqi itedclfgid ysgfnsdnks vriktvtkia nelladseek qrnfydnvtq
      781 iqkifalvst qeeaqdfape iaffkavkvf iaklkanpgg degtqaidds evnyrmsqll
      841 dqsiisepdv diyrdlgler paldlisdkf lqqvgemqek dvaivllekl lkgkvkamqk
      901 tnivksrkfq emleesieky nkrgitselv irkliemake inaeqekgkd lglskeeiaf
      961 ydaladhdka ikelgeeklh liaaelvklv rkeagvdwer rknvqasmri avkhllrkyg
     1021 yppdiapqav ttvveqaekm alnes
//
LOCUS       WP_010495244             136 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Paenibacillus elgii].
ACCESSION   WP_010495244
VERSION     WP_010495244.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..136
                     /product="VOC family protein"
                     /calculated_mol_wt=15156
     Region          8..132
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(8..13,29,60..61,64,80..85,87,91,120,130)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mgnakqkitt ffmfegkaee amnfyitlfd rseiismqqy gpneagaegt vvqalfslng
       61 qvfmcidssv khnftftpsm slyvtcdtea eiervfgrls dggsvlmplg aypfsekfgw
      121 vqdkfgvswq lnlekk
//
LOCUS       WP_010495242             439 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Ligilactobacillus acidipiscis].
ACCESSION   WP_010495242
VERSION     WP_010495242.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..439
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=45749
     Region          137..424
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mdnkgqfdge ykevdpengs qnnsggsggp klwkiflial iagligggvv vgsyslvqnn
       61 qdeklnsdns kaktktsnvn vkvtsdaesa fekikgavvs veayskddts ssiagfygqs
      121 edddsssesd seqanegsgv iykksgntay vvtnnhvisg adrveilmsd ghklnasvvg
      181 hdsisdlavl kidakyvdqi asfgnsdkis vgetalaigs plgsdyatsl tqgiisakkr
      241 tidvtnssgv atgqatviqt daainpgnsg gpliniggqv iginsmklss sgsseasveg
      301 mgfaipsnev veivnqlaen gkvsrpalgi slldldyisa sdrkktlklt dsvtsgivvm
      361 kinsdsplkd aglkkydvit glgdkkvkdi vslrealyah kigdtvkvey yhegkeqtad
      421 vkltleands ntstasner
//
LOCUS       WP_010495253             399 aa            linear   BCT 01-JAN-2025
DEFINITION  Ger(x)C family spore germination protein [Paenibacillus elgii].
ACCESSION   WP_010495253
VERSION     WP_010495253.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Cooper,G.R. and Moir,A.
  TITLE     Amino acid residues in the GerAB protein important in the function
            and assembly of the alanine spore germination receptor of Bacillus
            subtilis 168
  JOURNAL   J Bacteriol 193 (9), 2261-2267 (2011)
   PUBMED   21378181
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Li,Y., Setlow,B., Setlow,P. and Hao,B.
  TITLE     Crystal structure of the GerBC component of a Bacillus subtilis
            spore germinant receptor
  JOURNAL   J Mol Biol 402 (1), 8-16 (2010)
   PUBMED   20654628
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hudson,K.D., Corfe,B.M., Kemp,E.H., Feavers,I.M., Coote,P.J. and
            Moir,A.
  TITLE     Localization of GerAA and GerAC germination proteins in the
            Bacillus subtilis spore
  JOURNAL   J Bacteriol 183 (14), 4317-4322 (2001)
   PUBMED   11418573
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..399
                     /product="Ger(x)C family spore germination protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=45239
     Region          24..389
                     /region_name="GerAC"
                     /note="Spore germination receptor GerABC, GerC subunit
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG5903"
                     /db_xref="CDD:444605"
ORIGIN      
        1 mmlrtfvrtg kllalaaacc slagcwdmve vnqlaivdlv gmdrepgngk yttyyqvinp
       61 pgiavqkgag ikapvytykv egfsavelae ktfdivprrp fydhyqaliv terfakeglr
      121 evlnflekrp drratihlli tdsplpdmmk tfiplerlpg raehsiielq skysgresrr
      181 srvkdlvenm egsmltvlpi vslsgskpmp tteryeqida nqgnfimkga avfkhdrmig
      241 rlepadlpwf ylldggigvl nesmiinger idleapkpev rrqlaivsgk pvlkmdiyaq
      301 aqifdneqnv klteqnlaei kaqfneqvkk kasefyektk rlgwdllgie aqmkrksgke
      361 wadikkeera wkktelqlav hytiraigtt idpykekrg
//
LOCUS       WP_010495275             206 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010495275
VERSION     WP_010495275.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..206
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22841
     Region          3..200
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 myfyfvrhgt tinnqnhtfn gggvdpvltg fgqaeaqklg hylqevhfda cfssplkray
       61 etaqlvlken kqaqpaikil paltemdlgd wdgvsitqln gapqienyfh kpdlfdghsl
      121 haesyhdlqr rgyraleqii ksasgkknvl iashgllltt llkslngtdl rdirkdglva
      181 tssvtifesk dgtefklkdw alkpae
//
LOCUS       WP_010495297             204 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Paenibacillus elgii].
ACCESSION   WP_010495297
VERSION     WP_010495297.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..204
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23411
     Region          5..198
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 meqftlpelp ygydelepyl dartmeihhs khhatyianl nkaledhsql knatveelis
       61 nlndvpedir mavrnhgggh yghslywsim spngggtpyg diakgiekhf gsfkqmkdel
      121 tkaaisrfgs gwgwlvvdgd klevtstpnq dtpfmenktp ilvvdvweha yylqyqnkrp
      181 dfvsswwnvv nweevnrryn eair
//
LOCUS       WP_010495321             193 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010495321
VERSION     WP_010495321.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21466
     Region          3..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvrprafded kaldaamrlf wekgyeatsl sdltsgmgik rpslyaafgd kkelfeaalr
       61 kythahssyv rsklqnassv kdafrsyfeg iaaeadeegp nkgcfcinvm velaphdakf
      121 evltrehqmy laalfqemie rgmrsgelkq vgsakalaht mlvsvigltv lmksrpkrsv
      181 adhfiatile llk
//
LOCUS       WP_010495348             387 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Ligilactobacillus acidipiscis].
ACCESSION   WP_010495348
VERSION     WP_010495348.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 387)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..387
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43452
     Region          1..360
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          190..362
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mrtlamikrv lqemlrdkrt lammfigpll iltlmyflfq snndqtadla vrnvdstlvn
       61 avdndnikih hvssndsakk lirthdyagv mtqkddklql tlqnsnqiks silkkslqaa
      121 qvklkthasm talrdqkqai qklqqeltmv skqagispgt qasmpkqqkn parnysvkth
      181 yiygdkdtnf fdtflpimmg fvvfffvfli sgiallrert tgtlkrllat pikrgeiitg
      241 ylsgygifal vqtllivlys tyvfkiqilg siwyvllinv lmafvaltmg lfistfaase
      301 fqmmqfipiv vipqvffsgi ipvdqmanwl qgighimply yganamsdvv akgvgfiqiw
      361 pnllalllla glflilnlga mrryrev
//
LOCUS       WP_010495346             246 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010495346
VERSION     WP_010495346.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26768
     Region          5..234
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mgetiqvkdl aqgygknivi sdinlsvksg eilgligpsg agkttlinsi mgmlkpkqgs
       61 vtvlgesmpn rkilakigfm aqadalyetl tarenltffg qmqgmsqknl paqikyattv
      121 vnlnedldkh vndysggmkr rlslaialva dpeilildep tvgidpelrq qiwqelhrlg
      181 kegktilltt hvmddaeesd sllmirngva iaqgqpdrli kefkvksvee vflkagrqqd
      241 ahtgnd
//
LOCUS       WP_010495362             483 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Ligilactobacillus acidipiscis].
ACCESSION   WP_010495362
VERSION     WP_010495362.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..483
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54640
     Region          13..473
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 meelqpnkhy mhwtvialld fvtiisfeni fypfqnqgls vviswifllf tyvipyelia
       61 sqmsltfdnq dgglaswvrr ssndtlgyvt swmywvqsvp yivdvsnsvi vsfswmilgn
      121 ntlgqkmspf wfglltfgli lifillenai knsleilsli gggamfimsa lfvllagyal
      181 tqgahiatqp fnwhsfmpnf slkyfsttgl lifamsgael aapyvvrmrd pkhefpkamw
      241 llaimtaflt ifgtlalavf fngnqiphdf kmngpyyafa llgqqlglgn ilmyvfavvq
      301 aifmmaqlav lldatsrvfa gdvadnfmpk wvtrknkngr pvnsylmttg lnlflllltg
      361 tlpdintiyn wllningivs pyktcwvffa fiavrlqdkk fhsdyvfikn ktgalliggw
      421 cllftfvcat lgfipqevkf gtwdfthqli lnfitvfvlf glglvmpwlr krelrkekdc
      481 gta
//
LOCUS       WP_010495377             427 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Paenibacillus elgii].
ACCESSION   WP_010495377
VERSION     WP_010495377.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..427
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46149
     Region          19..387
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(29..30,33..34,37,70,123..124,126..128,131,151,
                     154..155,158,233,236..237,240..242,245,269,273,328..329,
                     333,337,353,356..357,360..361,364)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mshspiahth pplwrnrvfq ivafadllqq laiwtrnial lfyvmemtnn dpvavslltm
       61 feylpififs figgtfadrw npkktviagd tlsaisigii alcmmsglwq avfvativsa
      121 vvsqfsqpss silfkkhvpe eqvglavsit qglmsifviv gpiigtaiyt mlgiqyslfv
      181 liglfllaai iqiglpsser ssesanntim qdmaegfryv kqnrnlvvia aiftliglav
      241 giiqpldvyi lierlglhke nlqwfyavsg igmllgglla aalssriqrf aktvmflgll
      301 ilaasiafev lsrwvfvtas mrffvgitea flqivlstfm iklvhadyig rtngilaplm
      361 tggvligsga agllmsstsl mttffisaal vaaaacislq lsfpsgqmtn epdtkagmak
      421 kesvptm
//
LOCUS       WP_010495382             508 aa            linear   BCT 01-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Paenibacillus
            elgii].
ACCESSION   WP_010495382
VERSION     WP_010495382.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..508
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=52973
     Region          1..501
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mdtlqyllsg fataliwynl lfafagvlig tmvgvlpgig pisgvallip vttsltsglp
       61 peaaatssii llagvyygam yggsttsill ntpgesssvv taldgypmak qgragsalsi
      121 aaigsfvagv isliglvlla eplsnvalkm gpaeefslmv lglcalsgla gksitkallm
      181 tvfglalati gidavsgvsr ftfdipelyq giefltvavg mfalgevfkt ilekdadtge
      241 iakinrilpt kqdmkdsamp ivrgslvgff kgivpgsgat lasflsylle kkiskhpekf
      301 gkgaiegvag pesannaasg gamiplltlg ipgtgttavl mgalimynvq pgpllfedhp
      361 siawgliasm fignvmllll nmplvkvfak iietpakyli piivtisifg vyavqmsvfh
      421 lilllacgva gyffskndyp iaplvlglvl gpmiennmrr altissgdfs ifvmkpvsli
      481 fliiavlwla ipfvmklrgk kvivneea
//
LOCUS       WP_010495405             170 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA thioesterase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010495405
VERSION     WP_010495405.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..170
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18770
     Region          6..147
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 msepmtcrqt lavtshrvlt gdlnehetvy ggrllemldg tasisasrla ksvsvtasmd
       61 qtnfiapfgl qdsfcietyv sgcgtrsiev fakiigehlq tgeryiglts fltfvvtdks
      121 vslrkiipet aeekminagy ekrqenriss lrtqkefnss lssdypwdln
//
LOCUS       WP_010495406             218 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010495406
VERSION     WP_010495406.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24052
     Region          27..182
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msdqdissna nsrvlktyqe arlqnienlr klvvdaaatl lqeegpeavt vrkvsqkmgc
       61 stkiiynlfv nkeglaqqly ldgckllane fegtpqgadp aqhlqnlgea fwqfgqryss
      121 yyklmfggaf adfkpdeesl ngtvtamrql ltvinnaqkq glipgqydte lvirvfwasl
      181 hgvihlfmgg hlgdvqsaha vyrqtlsliv ssllpdka
//
LOCUS       WP_010495502             477 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010495502
VERSION     WP_010495502.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..477
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=53136
     Region          6..464
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mhysrvsetd ietlrkfipa erffypttkh ydhdqfnykk sapdvavqpv sngevsavmk
       61 yanehqipvt vrgnatglmg anisvdhgia idmikmnkvl eydpdsltmt vqagvrirdi
      121 deyladqpfi yvpfpamkwa aiggnlntna ggmkavkygt trehvrglta iladgtqihc
      181 shktvknssg ydikdliigs egtlavvtev vlrliprprv ektmllsfpd ieraiscvpk
      241 ifaagltpts veyfseedvd kweeysvkkf pvkdgsgylm igfdgnddkl vdgelaevvn
      301 vanendvsnt lvltandpns qavwdarsef etaiqqtttk mdeadivvpi nkiplvlkev
      361 rkvsekenvr lpnfghagdg nlhiyiccdd ysddefavkk dhvfkalyqv akdsdgemsg
      421 ehgigfarkd yfedfygsdy velmsrikla fdpnlilnpd kifplhvskq enevvkn
//
LOCUS       WP_010495535             240 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010495535
VERSION     WP_010495535.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..240
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26865
     Region          19..228
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 metddrttpv aahhipqfls genmerltqi mypnkaaege ylfwegdtad rlyyvhkgtv
       61 klskstedgk alilqvaqsg dlfgefgsge pqsygydgiv medaslgvil ikdlevliwk
      121 hgdmalqlfk wmsqmqrfmq skfrdlllfg kngalastli rltnsygekd ergiritikl
      181 thtdlanmig strevvnrml seykaagaie sengrfvvtn lsffqamvrc aecpldacri
//
LOCUS       WP_010495597             185 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Paenibacillus elgii].
ACCESSION   WP_010495597
VERSION     WP_010495597.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..185
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21435
     Region          5..175
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mvapevikaa qsgdrdaqit llreienhvy rtayyilnne qdamdaaqea liriytkins
       61 yeekaqfktw vqrivtnlci dkfrrakptv sieqhdlsft dhktvedevm styiaqdird
      121 aidklpehhr svvvlrylqd fsyneiaesl dlpintvksy lfrarqqlqt ilreykkpsg
      181 davrg
//
LOCUS       WP_010495604             256 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010495604
VERSION     WP_010495604.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27765
     Region          4..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnnqaivsar dirkiyghkg ekqyealkgi tfdvkagefv gimgasgsgk ttllnilttl
       61 dqptqgtvei ngqditslkg navadfrake igfifqdfnl lenltnseni alplslqnvv
      121 aaeikpqiek lakqlsitgi ldkypneisg gqkqrvaaar alvsqpailf gdeptgalds
      181 ssttdlleml nevnqqqnvp ilmvthdpls asycqrilfi qdgkigqelk rggqtrkqfy
      241 kqiiddlgaf qgqead
//
LOCUS       WP_010495675             537 aa            linear   BCT 01-JAN-2025
DEFINITION  xylulokinase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010495675
VERSION     WP_010495675.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..537
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58636
     Region          15..476
                     /region_name="ASKHA_NBD_FGGY_BaXK-like"
                     /note="nucleotide-binding domain (NBD) of Bifidobacterium
                     adolescentis xylulose kinase (XK) and similar proteins;
                     cd07809"
                     /db_xref="CDD:466809"
ORIGIN      
        1 mniaeiakei qggntalgie lgstqikavl itkdfepvas gsflwenslk dgiwtyslde
       61 vwdgikqsyq qmsaevstky hvqvekigsi gvsammhgyl afnknnellv pfrtwrntit
      121 gdaageltkl fnfniplrws iahlyhailq keehvkdidf ittlagyvhw qlsgnknvgv
      181 gdasgmfpig kdgqfdqekm sqfedlelvk qypwklqdil ptvleagqna gnltkagakl
      241 ldpsgklqag svmappegda gtgmistnsv rertgnisvg tsefsmnvld kplkkvhrdi
      301 divqtpdglp vamvhinncs sdinawadif kefarrlgid lkpdelystl fldttkgded
      361 aggvvnysyl sgepvtktde grplfvrtpn snfnlanfmt aqlysafapl kigmdillhe
      421 egvstdvmia qgglfktpvv aqqvlsnaln lpisvmtnas vggpwgmavl aqyvasgake
      481 sladyldtkv fsdsetmtls peqegvdgye kyieryqagl lvedqaaile dpvekqq
//
LOCUS       WP_010495697             340 aa            linear   BCT 01-JAN-2025
DEFINITION  lipoate--protein ligase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010495697
VERSION     WP_010495697.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000589
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..340
                     /product="lipoate--protein ligase"
                     /calculated_mol_wt=39011
     Region          2..251
                     /region_name="LplA"
                     /note="Lipoate-protein ligase A [Coenzyme transport and
                     metabolism]; COG0095"
                     /db_xref="CDD:439865"
     Region          252..336
                     /region_name="Lip_prot_lig_C"
                     /note="Bacterial lipoate protein ligase C-terminus;
                     pfam10437"
                     /db_xref="CDD:431286"
ORIGIN      
        1 mqyiamntkd irtnlateqy lmnsgkmtpp fmlfyiekpc iivgrnqntm eeidpeycrk
       61 hnititrrls gggamyqdlg nmcfsmvipa kdqefgdfks mvqpvvaglk emgatnievt
      121 grndivlngr kfsgnamytr dgktfshgtc mfdvdtdvva salrvpkdki eskgiksvrs
      181 rvinikpylk eeyqnmdtfq lreelikkiw ktntieeaek nyayvldded kkeiakleqe
      241 iyynwdwvyg kspkftvqrr khfaggtida rfniengtie nvviygdffg penvdelqde
      301 lkgtkysqek ikeklnaldl srffagipqd eitellstqq
//
LOCUS       WP_010495720             168 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010495720
VERSION     WP_010495720.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..168
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19804
     Region          1..162
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(5,22,27,57,98,104,117)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(7,14,44..46,64,99..102)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mlafiwaeds nhgigyqgql pwhmpadmkf fkdtttgnti vagrktfesf krplhnrkni
       61 vltsrdekdf pegvvvyhsv kevleyytrq psqkmfiigg vrlfkeflpy atdlyrttid
      121 hefavdtymp eidynhfmls dfvegkvdek nkyphhfehf mrvepene
//
LOCUS       WP_010495727             373 aa            linear   BCT 01-JAN-2025
DEFINITION  S-layer homology domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010495727
VERSION     WP_010495727.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Gerbino,E., Carasi,P., Mobili,P., Serradell,M.A. and
            Gomez-Zavaglia,A.
  TITLE     Role of S-layer proteins in bacteria
  JOURNAL   World J Microbiol Biotechnol 31 (12), 1877-1887 (2015)
   PUBMED   26410425
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Mesnage,S., Fontaine,T., Mignot,T., Delepierre,M., Mock,M. and
            Fouet,A.
  TITLE     Bacterial SLH domain proteins are non-covalently anchored to the
            cell surface via a conserved mechanism involving wall
            polysaccharide pyruvylation
  JOURNAL   EMBO J 19 (17), 4473-4484 (2000)
   PUBMED   10970841
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Engelhardt,H. and Peters,J.
  TITLE     Structural research on surface layers: a focus on stability,
            surface layer homology domains, and surface layer-cell wall
            interactions
  JOURNAL   J Struct Biol 124 (2-3), 276-302 (1998)
   PUBMED   10049812
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Lupas,A.
  TITLE     A circular permutation event in the evolution of the SLH domain?
  JOURNAL   Mol Microbiol 20 (4), 897-898 (1996)
   PUBMED   8793886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..373
                     /product="S-layer homology domain-containing protein"
                     /GO_component="GO:0030115 - S-layer [Evidence IEA]"
                     /calculated_mol_wt=40975
     Region          43..82
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
ORIGIN      
        1 mkrvvplvvs mmlmsacspn antlvaaeqp ksaveskagv slsdisghwa esdikaivaa
       61 gyvdgypdgs fkpdhtvtra efitmaakaa slkpvqggdn kewyapyvaa lvqagihqyk
      121 dfssgdwntp itrmemarla vrasdkslqs pedstdakkf mflatqkgli tgmadgqlgk
      181 desatraqsv kiiqrildvs qgkklevdkr aasyaevelt gsnvqtmwgs hvvelpykmp
      241 lekttatvkv hqvlimdlke kdgafrsmfd gqiakvndkp igdeylvalr vditdgsytl
      301 fgqlapeetq ltirdstgkv dkrfypvgie snegwylfvr skeevksqkq rigyvnlwlf
      361 enngaqfnla kkq
//
LOCUS       WP_010495734             162 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Paenibacillus elgii].
ACCESSION   WP_010495734
VERSION     WP_010495734.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..162
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=18259
     Region          5..>159
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mklgkrigqg ytaevfewgs dkiikvfrph tgdlmehewr isrqvaglgl pvpavygiee
       61 aegrrgivye rvagptltqv iaakpwriaq aarqlaalha amhrreapgl pkqkemlerr
      121 iretsllsee tkarvierln rlpeevrlch gdlhpenimm ta
//
LOCUS       WP_010495771             450 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Ligilactobacillus acidipiscis].
ACCESSION   WP_010495771
VERSION     WP_010495771.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..450
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49798
     Region          3..444
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mkqpqksqkl srslqnkhiq miaiggaigt glflgsgsai hssgpaiils yiivglfcff
       61 mmravgelll sdlsqrsild fikiylgdrl efvvgwlywf cwislamadl tasgiyikyw
      121 fpafpqwatp liillclylv nhvnvrlfgd leswfslvkv laiiiliavg fflaifkfni
      181 dgnsagfenl wthggffatg gygflmsfqm ivfafvgiem vgltageted peknlptain
      241 slpiriglfy vgsmiaimsi ypwdkistst spfvqvfasi gipgaagiln fvvltaalsa
      301 tnsclfstsr tlhslsdsgs apkklarvnq ngvpyaslnf stvflllvvl lnylipdnvf
      361 elissvstis fvlvwlilvy chlkyrktnp vgsqifrmpg ypwtdyltll ffggflifll
      421 fdkttripll fallvsvalf lsykplytqk
//
LOCUS       WP_010495780             237 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010495780
VERSION     WP_010495780.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..237
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26848
     Region          4..221
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mvlkykkvaf eisrqitdgk ytdklpseae lvekyntsrn tirnamdalf eqglikrvqg
       61 sgyfvnvplh sdgyfmniag knglgslgkr tiikskvnal kvisagkeia ahldcdpddq
      121 vyyvsrlrfs nkdlvsleha yylkqqvpyl nkeicedsif sfivenydie vtnadeyvsv
      181 yslgeneaqe skqpvgtptl kieeinctkn ehpfnysnsf yfqkgmtvym hinnsls
//
LOCUS       WP_010495800             249 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010495800
VERSION     WP_010495800.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..249
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27562
     Region          5..246
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mqpllkvdkl tggysrkkpv lhelsfsvrp gemvgligln gagksttikh ilglmqphsg
       61 qillngrsve qdptayrqty ayvpenplly eeltvkehle maamaygipk dafeerattl
      121 ldefqmtasw nrlsahlskg mkqkvmimsa flvrpalyii depflgldpl girallelmv
      181 rvkesggail isshilstie rygdrflllh qgrltaegdv ealrkqadmp gaslddlfcs
      241 lvtrdvtlr
//
LOCUS       WP_010495804             418 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Paenibacillus elgii].
ACCESSION   WP_010495804
VERSION     WP_010495804.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..418
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44203
     Region          3..415
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtkrtitmaq gvalymgavl gsgililpgy tadaagpaai iswlllslls vpiaytfarl
       61 alkyenyggi ativqqafge rsgavvgwff fawvatgqav vgltgasyiv tvfglagewl
      121 ygfaflflva alaanllgmr isglvslgls givlvllvlt iafslpamea vhfrpfaphg
      181 ltgvgqacvl ifwaffgwes ithlvpefrn pqrdvmrctw asvfiigavy tllsavtigt
      241 htygdigtea plaalmnral glnaglatvv vacivclgtl nvylasssrl gyalavegkl
      301 prwfaktsns gtpnrsvffl fvtntltlaf syaasfsvdr lilvpttlgi lvyivasfac
      361 vkllwsdkag rlaaltssal claiapfsmq ylavpavvaa scllylryrr kvsavnsp
//
LOCUS       WP_010495819              90 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010495819
VERSION     WP_010495819.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..90
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10516
     Region          8..>70
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtskqdlrir ktkhkiyaaf wkllkeydys rikvsdilte aqinrstfyc yysdkdalln
       61 kieeqlingf kkvalkvprs elgslspkrn
//
LOCUS       WP_010495894             304 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Paenibacillus elgii].
ACCESSION   WP_010495894
VERSION     WP_010495894.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..304
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=32097
     Region          19..291
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mkqdrgtsgy graaafgvqm ayltigcllm aisynmfqhp hqiaaggvtg lstvleyvtg
       61 lkpaisqwli nvplllagaa vfgrgfavkt vlgsvllplc illtegvpsl tdnmllaaiy
      121 ggigtglglg lifkgnassg gftivallln rklgiglgka llildfavil taaivftpek
      181 alyawiglfl tkkalelihs asdskvafii tdqtreetlr aailleldrg ltrftswggy
      241 tgeprgvlmv vlrnadiapl krivstvdpq afvilsease vygqgfhsyp lvpragrdas
      301 kvfs
//
LOCUS       WP_010495878             400 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010495878
VERSION     WP_010495878.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..400
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44297
     Region          25..395
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mgntakgnry qyvvvgggvv agyaikgirk edpsgsilvv skeadvpyer palskklwld
       61 defteediri gaedhadvtf kfnttvnkid rqekevelgd ntvvhyeqll latggeprni
      121 kgpddphvlv frnwsdyrrl rkfsgknkhv viigggyvgt elassltqnd tkvtmifpek
      181 algegkfpee irqeyeetfk kngveilsgk mvesyqrqgd hltisiadgs eisaetiiig
      241 lgvtpriela kaseleladg gvkvdeylqt sdpsiwsagd iasypdkilg rqriehvdha
      301 rlsgelvgqn magahlayqh tpyfysmifd iswqaignid lslkkifdkr nsgtivyfln
      361 deklagvlvw nvpvdlddvr klladppadn deligsiken
//
LOCUS       WP_010495901             227 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Paenibacillus elgii].
ACCESSION   WP_010495901
VERSION     WP_010495901.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..227
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25367
     Region          1..116
                     /region_name="CatE"
                     /note="Catechol-2,3-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2514"
                     /db_xref="CDD:442004"
ORIGIN      
        1 mkirevilhs snyeatkqfy cdtlqlpvle enadslviqa geskltfiad dreqayyhia
       61 ftipdnkade alewvrsrgi eplakddavq ypfpnwnata lyfydpdgnl veliahhsls
      121 natnepfssk nilriseigl pvedlpaalr qlheslslek wsgdglkfaa vgdveglliv
      181 idikrpwfpd ermpgifptt vklqteragi ielgpkpyri esvsgqa
//
LOCUS       WP_010495954             424 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010495954
VERSION     WP_010495954.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..424
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=45589
     Region          7..415
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkhykffkps lgwqiligli lgvilgivfy knqaaitamq nigtmfinli qmivlpivvs
       61 cltvgianmg dikelgrvgl ktliyfeils tiaiilgmiv anvlhpgtmi nihslhgsdi
      121 sqymataksa khntgiwatl lgiiptnifk slsegnmmpv iffsvffglg isaigergki
      181 ivdfltavqq vmfkvtnwvm ktapigvcal igvtlaemgi nallplgyfv aityltmivf
      241 vivvmgivak ifkfklsdll hvikdeiila fstasseavl pkmmekmgkf gvnqgivsfv
      301 iptgytfnld gsaiyqslaa lflaqaygih lsfgqqltll vvlmltskgm agvpgasfvv
      361 llatiatigv pmsgltfiag idriidmgrt avnvvgnsla tvvigksene fddeksqkyi
      421 akfk
//
LOCUS       WP_010495960             189 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Paenibacillus].
ACCESSION   WP_010495960
VERSION     WP_010495960.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..189
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22241
     Region          1..179
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdndieiver ilngdkqafa qiidkykgrv fallrrmlgh spdtqdiaqe vfikaynhln
       61 eytpghsfsa wlyriaanrc idelrkrkrr pditgfdaef mqgetpetay lekerrqale
      121 qrimeldqsq ravfvmrymq hlsyqeiaer lsvpistvqm rlyrarqklr esmsnsgveg
      181 efiyevrqs
//
LOCUS       WP_010495998             312 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010495998
VERSION     WP_010495998.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..312
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35522
     Region          <99..242
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 miqlikaeql kiynrpmvli mgicliivtt lvavfnvgkt hkseindwks mlieenhslr
       61 edmkkapeem kqffetqikr ndyilergll pnqmtawkfv slmsnflpli tlfslivasd
      121 ivagefqwgt mklllirpvs rsrlllakyc svllfaalfl afmlliswli gailfgvkga
      181 mepfifsrdk qnfqdipmvm nisityglkm itlfvivtls fvisilfrss swavgisvfi
      241 lfsgnlvgpl lqhinagwsk fflftnlnle eyffgsrsve gmtlpfsigv llvhtfflcl
      301 vgwivfakre vn
//
LOCUS       WP_010496034             392 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-glycerol glycerophosphotransferase family protein
            [Ligilactobacillus acidipiscis].
ACCESSION   WP_010496034
VERSION     WP_010496034.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..392
                     /product="CDP-glycerol glycerophosphotransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=45546
     Region          2..386
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mlktvylwlv sfcskifskt nsdqivylls fagnenfivr laqrvkqepg gklvvlyrpn
       61 cvksahelra hniecrefsd nfyflthqlk timqaklifa dnyfaflggc qfdhdrtrvv
      121 qiwhangavk tfgweeprtk drsasskkrf qkvydqfddf ivgsakmgev fcnsyhqpie
      181 kmkvlgyprt drlfsnekkt qkrkqffaey pelaqkeiil yaptyretvt getyfdlpqd
      241 ftailanlsd eqvmlvklhp hvkeaishlk kqhlahvfwv ddfttddlll vssrlitdys
      301 svifdytlle narqiifycy dfekyaqivg iqkdfnewlp gkmvsnasdl qkllqiplpd
      361 aaadfsvfnh lwnkandgna ishvlenyfy gn
//
LOCUS       WP_010496101             656 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Paenibacillus elgii].
ACCESSION   WP_010496101
VERSION     WP_010496101.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..656
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=71974
     Region          11..570
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mklagamtlr qkliaglsam vvlfmgvalf nvnqmhriks qlgvqnekve lklmalelke
       61 vvqelniias gleisknpdy ipkynekrkl ydqmvqrige tadtdeksvw rsklilltge
      121 ytntfdvaak vvqdksltkt dvdknmeyly nesqrimgei ftyvdhfyvs yagdataavt
      181 atqdgldrtv avmitafalv avcvtaigvl virsftgqir rlqhavgria dgdlrhkigs
      241 rsrdelgqls qsfdhmvdqv rgmlhstkqi asslaghsls frefsgstaa anqdilraiq
      301 distgaeqqa hysehsayli nslaeeirki neytdtmqrk sreaafntht gsrsmealrq
      361 sadrsgdvlr qvtsametls qssvqigkiv gtiteiatqt nvlalnasie aaragehgkg
      421 fsviaeevrq lssqtaessk riglivksll iqmsemeasf eearrsfdeq ngkmdesvea
      481 fssirssmde lsghigqihe litdaqekng qlvdavqhva aiaqesaagv eevnssshqq
      541 dtairhiasq addmlsltrr lfeeidkfki ddieaeeage aeiplspemd esrgqkkedr
      601 evipeaksag qavtetaaap aastdtgtqa apqeqadhkd neavsreeee kklqpv
//
LOCUS       WP_010496111             383 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Paenibacillus elgii].
ACCESSION   WP_010496111
VERSION     WP_010496111.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..383
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42084
     Region          92..264
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(98..99,159,164,219..221)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mrklllqail laflglglif qplsaakstv lykdqvavii yhhidddaks ggtitaqllk
       61 dqltylkskg yqfitlkqfk aymegapvpn navlvtfddg yesfyvnayp llkqmrvpav
      121 nfvitgdlen plasyipsms rddimemtsd tnftdfqchs hrfhyklpgg gaalvsrlvk
      181 dgvketeeqy kqrvvsdtka cvgalselyt epvdsyaypf giydkpameh irqggikyaf
      241 tvvpematre vdrmqiprid agnsgvsper lhqailrrvv apmpptsevp laetvgaigg
      301 kvaqshdgtv qigfgahnws gaagstklta pdgrtlalhk qltwknnkif islkdleqav
      361 ggqivynpnv qsfalrqtid tkp
//
LOCUS       WP_010496188             378 aa            linear   BCT 01-JAN-2025
DEFINITION  Ger(x)C family spore germination protein [Paenibacillus elgii].
ACCESSION   WP_010496188
VERSION     WP_010496188.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Cooper,G.R. and Moir,A.
  TITLE     Amino acid residues in the GerAB protein important in the function
            and assembly of the alanine spore germination receptor of Bacillus
            subtilis 168
  JOURNAL   J Bacteriol 193 (9), 2261-2267 (2011)
   PUBMED   21378181
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Li,Y., Setlow,B., Setlow,P. and Hao,B.
  TITLE     Crystal structure of the GerBC component of a Bacillus subtilis
            spore germinant receptor
  JOURNAL   J Mol Biol 402 (1), 8-16 (2010)
   PUBMED   20654628
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Hudson,K.D., Corfe,B.M., Kemp,E.H., Feavers,I.M., Coote,P.J. and
            Moir,A.
  TITLE     Localization of GerAA and GerAC germination proteins in the
            Bacillus subtilis spore
  JOURNAL   J Bacteriol 183 (14), 4317-4322 (2001)
   PUBMED   11418573
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..378
                     /product="Ger(x)C family spore germination protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=41991
     Region          4..371
                     /region_name="GerAC"
                     /note="Spore germination receptor GerABC, GerC subunit
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG5903"
                     /db_xref="CDD:444605"
ORIGIN      
        1 mnlkrtaita amlllaasvt agclqtrvle rlglviaagy deapgdkilg tsvlyemdpg
       61 akersnvits taftskglry nnnaesrkkl tsgqlrvvvy hedlarkglt elvdtmlrdp
      121 eigsgvylav skgrafdlmt rrypeisnig eylfqsirqn veseemispi lhefirdlys
      181 pgkdpvlpyi vqrdneiily gaalfrgdqm vgtlplsklf ylrllrdrfh sgmteigips
      241 ealgsigsps kgqkqvylvl dsvksksrir ltdakqlaft vqvhmsgrlq eisspvnlrn
      301 rqviellere askavqanvm afikktqrln vdpvgfgeky raqhrgtglt pdkwkqlypk
      361 akvsvevstk ilrtgqsd
//
LOCUS       WP_010496231             325 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Paenibacillus elgii].
ACCESSION   WP_010496231
VERSION     WP_010496231.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..325
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35412
     Region          13..325
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkvvvvgcgg mgrihaihya smpevelvgv cdivvhlaer ladetncraf asyeemmsav
       61 kpdlvsialp tylhkeymvk taalgahvvc ekpmaltled aaemirsceq agvrlfvghv
      121 vrffpeyadi krkveagelg klgvahakrs gshpakvkew fgnfeqsggv ildlmvhdid
      181 fmrwalgevk svyalnrrdq emdyalatlv feqgavanle afwgypgpfh tkaeiagsdg
      241 ivrnssleaq slqmvrtsag qdgpaavevp gspgyhdpyy yelrhfvqci renresivtp
      301 ndaykaveia laaiasaktg savhl
//
LOCUS       WP_010496253             208 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Paenibacillus elgii].
ACCESSION   WP_010496253
VERSION     WP_010496253.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..208
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23852
     Region          <23..205
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mdsaayqdsv edditkssdl yvkyvktaid lilsiafilf llpvlimvai liklesegpv
       61 vfkqnrigkg gkpfviykfr smythvareg rspendqdpr itkvgrfirk tsldelpqlf
      121 nilkgdmsfi gprpeqksiv eqyytdkeng rfsvkpgitg lwqisedrka pihenlhhdl
      181 yyikrasfwl dikiifgtlr vmiksnth
//
LOCUS       WP_010496265             129 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010496265
VERSION     WP_010496265.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..129
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14976
     Region          12..96
                     /region_name="HTH_GlnR-like"
                     /note="Helix-Turn-Helix DNA binding domain of GlnR-like
                     transcription regulators; cd01105"
                     /db_xref="CDD:133380"
     Site            order(14..16,30,47..48)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133380"
ORIGIN      
        1 mkekelrrsl svlpigtvmk ltdlsarqir yyeqqglvip ernegnrrmy slnnvdqlle
       61 ikdylsegin magirhiyeq qkerehakqd qmqksltdtd vrrilreeik avggladrad
      121 klsvhkkkl
//
LOCUS       WP_010496320             244 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010496320
VERSION     WP_010496320.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..244
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26693
     Region          4..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mselleiqnl kksfgkneil kninetvaqg evvcvigpsg agkstflrcl nvlehpsdgk
       61 vifegqdltk isekqlsslr qkmgmvfqsf nlfpnmtvle nitaapmkvk gvskqeaeqk
      121 askllerigl adkaqqypas lsggqaqrva ivralamdpe vmlfdeptsa ldpemvgevl
      181 evmkdlansg mtmvvvthem gfakevadri wlmadgyiqe sgkpseifen pqtkrgqefl
      241 skvl
//
LOCUS       WP_010496331             307 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Paenibacillus elgii].
ACCESSION   WP_010496331
VERSION     WP_010496331.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..307
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32998
     Region          2..300
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydcivvggg iaglqaaiql gryrhrvlvi dkgrgrstlc rsyhnvlgwp dgvsgqelrh
       61 lgrthaerlg vefrrdevva aarngrgfqi aladgggavh tetllaatgv ldrfpplpgl
      121 eerlgisvyv cpdcdgyevg gkrtvvmgsg dtgagmalal rywtdriiyv nherqavgsg
      181 hadklkeadi phveaeiaev lggpdarfdg vrlsdgrtie gvrgfiafgg nevhtgwtva
      241 lgierlenrh ivtdprtkmt nvpgvwaagd igvhseqvti amgegsqaai wihkellkrr
      301 tntalfv
//
LOCUS       WP_010496339             397 aa            linear   BCT 01-JAN-2025
DEFINITION  NupC/NupG family nucleoside CNT transporter [Paenibacillus elgii].
ACCESSION   WP_010496339
VERSION     WP_010496339.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..397
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43037
     Region          1..397
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mkflfvvagl llvfavgylf snnrkgirsr pilamlvtqi vlsfiilntk iglelitfvs
       61 rlfsklmefg vggvnfvfgg lenqgastff invllpiifi siligilnyv kvlpfvikyv
      121 glalsklngm grlenyvavs aallgqsevf lttkkqlnqv tkqrlytlct samsavsisi
      181 vgaymtmlep kyvvvaivln ifsaliiani inpykldpee eqatvvadee hhpkesffqm
      241 isesimdgfk vaiivgamli gfialmnmin yvfelifhis fqsvlgyifa pvaflmgipw
      301 seavqaggim atklvtnefv amlsfkdias glsprtvgiv svflvsfanf ssigiitgav
      361 kalndkrgde aaqfglklll gstlasilsa tliglfl
//
LOCUS       WP_010496363             121 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010496363
VERSION     WP_010496363.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..121
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13611
     Region          3..116
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mniaisntse kpiyqqlfeq isaqilkgel esgyclppir qaalelrvsv itvkkaweel
       61 ercglintvt gkgcfvaefs sdemlqirne milkqmvsda syyksfgltl deviellkki
      121 y
//
LOCUS       WP_010496371             346 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010496371
VERSION     WP_010496371.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..346
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38126
     Region          1..340
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtapvqlsir nlskryktge gvtgisfdih hgelvtllgp sgcgkttvlr svggflepds
       61 gdiliagksv lhlppekrpt amvfqsynlw phmnvfenla fglkirkmkk dqiqeavdra
      121 lklvrlpgae kkrpselsgg qqqrvavera lllepevlll depfsaldak lraelreelr
      181 eiqsstkltm mfvthdqeea lslsdriivm nrghieqsds pqaiydapqt lfvanfigrm
      241 nmlegvahng sitlqnlelp dsrhlhgdvv vairpedvrw keasfpglaa tvkqvmvlgh
      301 yaeitlltea gvlrmflpre eavelsggqs vsltfskhaa ypkisa
//
LOCUS       WP_010496401             153 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010496401
VERSION     WP_010496401.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17277
     Region          1..114
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdqvdykivs llhensripm aelgriigmt qpavkervrk leeqgvitgy haaismpklg
       61 knttafvmfr tkkcaafvef crqspevtdm yrisgeynym lkvvtattee lvdfsercgd
      121 fgysytlmml tapfehkmmi eppiaemaep ssn
//
LOCUS       WP_010496421             457 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Ligilactobacillus acidipiscis].
ACCESSION   WP_010496421
VERSION     WP_010496421.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..457
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48913
     Region          11..433
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mkeltkgspi kliltfavpl lignlfqqly slsdtiivgq tlgvnalaav gstgsiqfli
       61 igfaqgmtag lsimtaqffg ahdyrkvres fatsivislv vtavltflsv yfihdilmlm
      121 ntpaeiehna qtfstiifgg igiqmaynll aniirslgds rtplyfliia avlnvllell
      181 fivvfhwgva gagfatlaaq lfsvllcvly iikkipllqi hwvdfkkvdr kmitshlnvg
      241 lpmafqssii aigsimiqsa lnalgttava attasskidq iatlpmssfg vamatytaqn
      301 ygaaeygril kgvksavlms vgfsvaagll miifgqnmvt vfvgnadqgv lslsqiyfnv
      361 nasfypllai lfifrntlqg lgksvvptla glaelamrig aalflatrfg yagacfaspl
      421 awigsclvli tsyvqsvkml rrrqkekdea aeivadn
//
LOCUS       WP_010496437             358 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Paenibacillus elgii].
ACCESSION   WP_010496437
VERSION     WP_010496437.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..358
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39900
     Region          <205..344
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 maasharllt aaalcaallv spaagglenr gfayapaaka palpkaskav ngmkavfaer
       61 kdlfdkvssi tgipwhylaa vdqyertinl akkrpapdgm iaiyftdlqw ggilnpdhed
      121 knansiqwfg gigrdgsgdg ladrmndldr lysmavnmlk kgsaeedlri glwdyyqntr
      181 sveriqqfar iyahfdtldl yehcfvmpls adysyrstwg asrgwggyri hegtdifagy
      241 gvpvrsatyg vievmgwnpy ggwrigirdl nnvyhyyahl sgfnkkevqq gtivkpgqvv
      301 gwvgssgygk pgtsgkfpph lhyglyrdng ltewsfdpyp hlrkwereer mrrktttp
//
LOCUS       WP_010496467             419 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Paenibacillus elgii].
ACCESSION   WP_010496467
VERSION     WP_010496467.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..419
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=45336
     Region          <22..419
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnwflglsfk kklqigcytl vvvysaamll lisasslspi lgfvflavma glsypfirwl
       61 eraltepisd israalsisk gdfsqkihir sddalgelgt afnrmteklr ellqetgras
      121 khvfdssrdi yfknekmktv leeasvaage laaganqise eisgvssatk dieqrvteyt
      181 estremnsra rqmmalvnkg lqsvetqsgg mrknvdatan vsqtidslar qtgsisqmtr
      241 tisdiaeqtn llslnasiea aragehgkgf avvahevrkl aeeatastke vfglvrsieq
      301 giqhalasma eneqivaeqt kligeteqvf aeivgsvrfi seqiaafadg teqmlagakh
      361 isatmenisa itqqsaagte evsasmidqi savqaivaqs eemtklvmkl qqtmsifkl
//
LOCUS       WP_010496596             551 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010496596
VERSION     WP_010496596.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..551
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62841
     Region          7..126
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          226..544
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mgisiqeaiq lpvmsktklv agfdgmnnii kwvtivevie didrlqegef littgfglme
       61 sevkrsqfhk llsnkklsgv amytgfylre ipqsfidian rsalplleip tdinfsvitk
      121 aileqivnnq frmfehsini hkeftrlvld nqgiqaitet lsrltdgsiv lfdsdasiis
      181 dqivhdavrr igqdrlllfs eplqppfdqq llhfnnhese ytislypvma nqtnygwiaa
      241 ikdkerwkdi dqiavehaat vyaieflrhk aildtelrfq gefldqvlsk nftnkaevie
      301 rgkklgfdps gsqavlqikv enlppdlerr tlddmldrly qvvnqtmnkh nhqfllrnrl
      361 dgcvvlmgtg skgaapeaae easllatrdi adkwsafype hplrigigks ytdladlaks
      421 aqeahralvf akllhkpksv vhyddlglyh fliqmqelgm dlrqfaeeql galmqnkrqg
      481 adllqtlety lyhnqslhvt aaelfihrht lkyrlnqiek ktrrnlqsse drlkleiaim
      541 aykltvssee l
//
LOCUS       WP_010496636             203 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010496636
VERSION     WP_010496636.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23239
     Region          6..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkrivkdpka rrqeiltvag elfrhhgyag ttveaiiqka gvakgtfyyy fkskeqimda
       61 lvhelvdrlc eayqqiaddp amgvmeklrh mlrgqhqlav neselmeglh rpenrelher
      121 vnieiivkis pllaqvieqg kkealfdveh pletvqflla gsqfllesgl fhwnqeeqtr
      181 rlksmqamie rslgakrgsf sfi
//
LOCUS       WP_010496648             330 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Paenibacillus elgii].
ACCESSION   WP_010496648
VERSION     WP_010496648.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..330
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38558
     Region          12..324
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mdpqikllfl dehvkegamr fglsqeklsf iggfqnfiys ytlegckyil rftpntlrtq
       61 eglkaeiewi rylagngmsv sepvpsargi dvehvsgkmv dfyvtsfrha pghkigypec
      121 lgnpllyeqc grmtgnlhel akryeplarr hswerneyll harkyipreh spilraldel
      181 kerlaslpdt pdnfglihgd invgnftvde tgeitlfdfd ecqyswyaed iaiqlyylly
      241 vfgedskser kvqyelfieh fergytedgr rlpdgwknql slflrlreii vvvgmyrswd
      301 lrqpddwtrd flqdsrmrii ngisliddfl
//
LOCUS       WP_010496688             188 aa            linear   BCT 01-JAN-2025
DEFINITION  cysteine hydrolase family protein [Ligilactobacillus acidipiscis].
ACCESSION   WP_010496688
VERSION     WP_010496688.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..188
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21332
     Region          6..184
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 msnkkallvi dytndfvasd galncgepgr aieddllqhv kefdekgdyi ilptdyhfkd
       61 dpfhpetalf pphniagtpg qelygqlasw yhkhqdqdnv ykfnknryss fqntnldnyl
      121 rsrdikdlyl tgvctdicvl htaiaaynld yhinvyedsv asfdqvghkw vlahfknslg
      181 anvlttdk
//
LOCUS       WP_010496706             144 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Paenibacillus elgii].
ACCESSION   WP_010496706
VERSION     WP_010496706.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..144
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16327
     Region          9..139
                     /region_name="SRPBCC_CalC_Aha1-like_4"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of an uncharacterized subgroup of CalC- and Aha1-like
                     proteins; cd08897"
                     /db_xref="CDD:176906"
     Site            order(9,11,13,22..24,26..27,32,38,55,57,59,61,71,73..74,
                     76,79,85,87..88,94..95,97,99,109,111,113,115,119..127,
                     129..131,134)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176906"
ORIGIN      
        1 mgtgnpvtit letivhspve svwkywtdpk himrwnkasd dwhtpyaend lrvggkflsr
       61 meakdgsfgf dfsgvydevs inesisytig dgrkvkivfi hqdsdtkiit sfeaeetntv
      121 emqqagwqai ldnfkkyvev akee
//
LOCUS       WP_010496769             314 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Ligilactobacillus acidipiscis].
ACCESSION   WP_010496769
VERSION     WP_010496769.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..314
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34541
     Region          21..314
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 msvflqsisg viiilvliiv gyvlaargwf pgstdkliak lvtqiglpcy midtitsrft
       61 ahqligiipd lvfpiismli lmvvallfar ifkvsgshrg lfssmffnsn tvfvglpinq
      121 alfgsksipf vliyymantt ifwtigtyfi qrdgmqdakf nlkttvrkvf sppllgfivg
      181 lllvllkikl plfvikdlsy lgnlttplsm ifigicvyna glkqlslkkd nllillgrfv
      241 lapllmtllv astnfptlmk qvfilqsamp vmtnapvvar lynadadyas vmvtettfla
      301 livvpilmal tqni
//
LOCUS       WP_010496816             328 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Paenibacillus elgii].
ACCESSION   WP_010496816
VERSION     WP_010496816.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37684
     Region          3..310
                     /region_name="UDP-GlcNAcDh_Arch"
                     /note="UDP-N-acetylglucosamine 3-dehydrogenase; NF040723"
                     /db_xref="CDD:468687"
ORIGIN      
        1 maikigvvgi gtmglhhvrn fyhhpevelv avvdpsedrl kqviekfpvq gytnfkdiid
       61 rvdavsiatp tsthfslake fiknkkhvll ekpiceeide akilidlaen yqvlfavghi
      121 erfnpvmqel enilrankpv yidihrespy dprifdadvi sdlmihdvdl llyllnerit
      181 lksaygisvh ssrndlvsaq fisesgilin vttsrtteqk irqwnltlpn qfiqadlmer
      241 klyitrrtng sleifhnnse vkykqeqlie kvlvanyepl qmeifdfiqa itkgrrpkvq
      301 gkeglkalei tkeiqlkvke tcinrkii
//
LOCUS       WP_010496907             391 aa            linear   BCT 01-JAN-2025
DEFINITION  Ger(x)C family spore germination protein [Paenibacillus elgii].
ACCESSION   WP_010496907
VERSION     WP_010496907.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Cooper,G.R. and Moir,A.
  TITLE     Amino acid residues in the GerAB protein important in the function
            and assembly of the alanine spore germination receptor of Bacillus
            subtilis 168
  JOURNAL   J Bacteriol 193 (9), 2261-2267 (2011)
   PUBMED   21378181
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Li,Y., Setlow,B., Setlow,P. and Hao,B.
  TITLE     Crystal structure of the GerBC component of a Bacillus subtilis
            spore germinant receptor
  JOURNAL   J Mol Biol 402 (1), 8-16 (2010)
   PUBMED   20654628
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hudson,K.D., Corfe,B.M., Kemp,E.H., Feavers,I.M., Coote,P.J. and
            Moir,A.
  TITLE     Localization of GerAA and GerAC germination proteins in the
            Bacillus subtilis spore
  JOURNAL   J Bacteriol 183 (14), 4317-4322 (2001)
   PUBMED   11418573
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..391
                     /product="Ger(x)C family spore germination protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=44058
     Region          1..381
                     /region_name="GerAC"
                     /note="Spore germination receptor GerABC, GerC subunit
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG5903"
                     /db_xref="CDD:444605"
ORIGIN      
        1 mlsaslflvs mtgcwdrvei edvgivlgig fdmpahkatn qengmpkgkq gkveriamth
       61 hfavpkqfsa kegvsaqkdy invfsegrvv fdninglstr lsrtpsyehl rviliseeva
      121 rsfdlrdiin fllrnpearr sirvlvcegk trtvlekkgi vanpalnlre lvegfrktlr
      181 ippimklgdl senltkkenf viqwvtaare ettlsgaavi rgkdarmagw ldeeetvgln
      241 wlkgekkrtg iiegrdpisg ekivyevrkf arsikprhkd grisfqveik tegrlredwv
      301 dsdnafkeef iaraeraaea siksslkrvl vkmqkklmld aagfgkrlqv eypqvwnkvk
      361 enwdstfsea sievkvnari vefgtrgsrg g
//
LOCUS       WP_010496887             642 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010496887
VERSION     WP_010496887.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 642)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468444
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..642
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71928
     Region          <50..189
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          <74..>342
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mnfrqlalkn iqgnwhryva fflssafsvm vfymfgsfiy hpeiangnik aasmvkqvlf
       61 acqilivifs fffvlyasfa flktrkkefg lltlfgmtrs qicrlmfyeq mmigllsigv
      121 gigtgmlfsk lfflaiarll qtdspirfav ptqallqtvi gflalflams lfamfnvgrs
      181 qiiallragk qpkkppvasl wltvlavvcl gggyylaftt svklimylml piifltvigt
      241 yflftqasva iigrlqrmtg lyynrtnlit isqlafkikd nartlfvvsv lsaviltasg
      301 tiyvfyknid qqlmeqfpnt isfteqgpgd rhaidadklk ailategasl akelkiagvk
      361 vplklddsrv sdttvllise sdynravegi eyavplqiap ghavfsypyr mgdvilmekg
      421 srrtvqlngq awplemdgqv tggvinlmga atgllvvndg eysrmmketp ddqrlvyygf
      481 elnrwqehaa avekvkqsvp eehrkrlsdr tsfyaavqqs wsltmliglf vsflffvasa
      541 smlyfklfte lqeddhqyra lmrigmsvpe irriinvqig llfllpvvvg aahaafaykt
      601 lanllsmnvw sygamvisvf allqfgyfll trraymgqmk sl
//
LOCUS       WP_010496917             237 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010496917
VERSION     WP_010496917.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..237
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26498
     Region          10..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..230
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 misartqrgp kremslkqiv dsaiaiadke glsalsmnkv aaslgfttma lyryvpsked
       61 lillmqdavl disipeensa hwrenmtafv ltimrcfqdh pwlcdipasg ipitpnnlri
      121 vdwalrmmsd lpldhrekis ivvlltshar vhsffqrdmd ravqtgvnsg pvpgvsykaa
      181 lehlvtserf phlspvilag ayspendykd ghsygfefdf gldrildgie hyvnskr
//
LOCUS       WP_010496989             428 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010496989
VERSION     WP_010496989.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..428
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47934
     Region          10..412
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnpkfveefe kekfaglspi qeavyeplsa gknvigyapt gsgktlayam plletllpkd
       61 gtqllvlvps qelavqvnnv mgrfasllgm ksiaviggan vkrqyeklkk hpevivgtpg
      121 rvldvikerk lkmhkltacv ideadqmlad easlalcrei vshahadiql sffsatdsan
      181 lsdvhhwfgv epevidvrqi dntqghvthy liespvrkrv emlrklanld dfaglvffds
      241 ttqvkdasek lafqhvaige lssgqssqkr kqaladlrkr kirlllttdv aargldiael
      301 pavvnfdipr dlttyihrsg rtgrmgaqgt vinlgnehdl rqfkqlvkdk dydlqtgyiy
      361 qhqlvtdlka aqaenkqqnk pkkkkkktkt eikqiraeek kqsikhkknr krdrknkgkp
      421 kpkkrqge
//
LOCUS       WP_010497021             154 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein, partial
            [Ligilactobacillus acidipiscis].
ACCESSION   WP_010497021
VERSION     WP_010497021.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         <1..154
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
     Region          6..140
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
ORIGIN      
        1 kvgwtvlavv illavgswaw gstlvqsrvq asfgnnaayq kkeydkqral akkkygdtae
       61 ntavvkekpt akesssaskt nsstkktasd qkyiyitvkq geylstiann ynttvdklve
      121 lndlesrdis agvqlkvpan gntstgnsad ssgq
//
LOCUS       WP_010497023             309 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010497023
VERSION     WP_010497023.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..309
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34725
     Region          5..285
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mdlgkkfqpv kkfvrlvikq fgevnignta ivtayyslla ifpmlifitn llpmlglkad
       61 tilpylqtaf pstvfstikp ivmdflnnss gslasvtgil tiwsasrgvn alkmsinqvy
      121 gvkdydnait srifsffmil lfaiivivaf vvnsfgqivl eyltpifhls lgwldafsky
      181 kslatlviif lvmvflyvtl tnakthlryv wpgalfaaag wmiltqgfsi ylkyfaksvl
      241 sygtigtfiv llfwlnfssw lillgallns tleryhygki epkktaikrl ydrvdpmnkd
      301 nskkkkstk
//
LOCUS       WP_010497031             454 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Ligilactobacillus acidipiscis].
ACCESSION   WP_010497031
VERSION     WP_010497031.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..454
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51059
     Region          9..434
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mdadpgqqwg llilalvlmv lgfcfaiyer alktttnqal esaseslsak kkekvaglik
       61 rlphefqmaq varlttclla liflvtavfl algesltsvl vsgivlgvva saineplfvk
      121 lplkvvvhdp vkaalkgyri lhwvislfip lvfainwfck llgrdkivav epsqvmswqn
      181 ivdlieegrs kgeidndeye miegilslhe kmarevmvpr idafmiditn dndrsiddil
      241 qmnysrvpvy hedkdniigv vhiknlvkaa rqfgfehtti rqvmrepffv petimidqli
      301 yemkkkqnqm ailldeyggv vglvtledli eeivgeiede sdepdqmmis ltpadflvqg
      361 kmalddfnde fgqdlqvpdv dtiagyvitq lgyipqesdv dsvtlddgst ivvhkmeddr
      421 lleleielsh eavdyrvere kskkkaqakl elnr
//
LOCUS       WP_010497035             740 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010497035
VERSION     WP_010497035.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..740
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81840
     Region          1..>79
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          98..725
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mlcqnchqnp atihlttsin grqtsidlcq ncyqklkdqa gnngrsssmm qdpfgfsnld
       61 dlframssdq qgaqrqgqvp ptqaaggngr nngsntilgq ygldltneaq ngridpvigr
      121 dkeierviei lnrrtknnpv ligeagvgkt avveglaqki vdndvpqklq nkkvvrldvv
      181 slvqgtgirg qfeermkqlm delkkeknti lfideiheiv gagnaeggmd agnvlkpala
      241 rgelqlvgat tlneyrtiek daalarrlqp iqvdepsvee tikilqgisg kyedyhhvkf
      301 seksleaaat lsdryiqdrf lpdkaidlld eagskknlti htvdpavmde kinkaeeekq
      361 aalkaedyek aayyrdqvsk fnkmkenstt destpeitek dmekiveekt dipvgelkek
      421 eqtqlknlan sleqhvigqd qavtkvarai rrnrvgfnks grpigsflfv gptgvgktet
      481 akqlarelfg tedamirfdm seymekfsvs kligsppgyv gyeeagqlte qvrrhpysli
      541 lldevekahp dvlhtflqil ddgrltdsqg rtvsfkdtii imtsnagsgd svssvgfgae
      601 asgethsiln slskyfkpef lnrfdgivef nalskenlhh ivslmlddvn emlaakgiel
      661 hvtgpvadkl vdlgydpkmg arplhrviqe qledkiadyy ldnpnnknls arledgviki
      721 tkndepveks aedssshtte
//
LOCUS       WP_010497108             676 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Paenibacillus elgii].
ACCESSION   WP_010497108
VERSION     WP_010497108.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..676
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=73362
     Region          114..676
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnllrsvggk lfliffisil ffvltvglts yniskgviqk kvadasegti mqagqkldll
       61 yatyedlsmq illdedlkkl ladmdtvnkn sydflqlrqk lgdklnvysy snktlksiyl
      121 fkasgepvas agsamskesl aqedwfkkiv egngkatwle srakgysdsl gnagtasfgl
      181 grvlkntttn avqsvlllei nleavgkels qismgeggkt vivtpdmnyi ynqdvavlgk
      241 psdlgvtkea faedkgnlqn ssrdmqlvyf ksaktnwlli gampvaelvk dagvifgmtw
      301 lmafvamiia ivigyfivrm igrpvvqlrn lmkegeqgnl kvrmtvtsqd eigqlgqsfn
      361 qmmekittlv qqtnhsaqev lqtagslsda skktatsake iavateeias gasslavese
      421 rgnelthnig mqmksvvdan ivmgssasev qasskqgiey mseligktna teamtrsmve
      481 kvdnlkestr sirkildvln nmtkqtnils lnatieaara gaagkgfmvv adeirkladq
      541 srqsiaivgq itetiqkeid etvnvlsqay pifqeqiesv keadsifkqv dsqmgefier
      601 lsevtesise leasqmvlsd amsnvsavae essatsqeva slsseqmsis sglvklsdsl
      661 edlsnslkeq lskfqv
//
LOCUS       WP_010497182             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010497182
VERSION     WP_010497182.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..282
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30915
     Region          1..280
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 menilvviqn vrnqvskker vlcdyilvsp tevmqlpvqs laqrcqisaa tvvrfcrrld
       61 ldgysdlklh lsaavqetqg qeygeikpge saseisgklq lhfenalkvt tkklddqvie
      121 tvvtalheah qvqlfglvss slvvqdmyqk lsrlglsavv nndihlaatt lasgstedll
      181 lvvstsgntk evvtllkfak eksittvlvt antnstgarl adhllesqnl gesvirpgas
      241 tslvteffva dvllfryvar yyaevlnslk dsrelikrln nd
//
LOCUS       WP_010497197             737 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-galactosidase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010497197
VERSION     WP_010497197.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 737)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16044983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..737
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83944
     Region          39..293
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          297..643
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Site            order(344,375,419,484,488,534,553,556)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          657..733
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mtkpsaksel ievssnpltf hlhnsqvsyv lgvedenila hhyygkavdh ysnlrryprl
       61 mrhfapsped ietrdfslst lpqefpgagg adyrepgivv qfpngsrtvn ftydsytisd
      121 gkpqlaglpa tfaqedeaqt ltvklvesda qlelylsyti frdlpvitrs arvknlgqqp
      181 vqvqrlvsfs ldspdnelnl lqlngryaqe rnvtieplnt gikildskrg asghtqnpfc
      241 alidphatef sgevfgfclv ysgshksiiq mdgynqvriq mgindqnfew wlepqksfqs
      301 peavlvhseq glnsmsqsfh elflnhlmks kyshqtrpil lnnweatyfn fdekklqdii
      361 asshdlgiem fvlddgwfge rdapnsslgd wvvdrkklpn glkplsdych nldmkfglwf
      421 epemisvksk lyqshpdwvl evpgqrrsid rsqfvlnlgr aevrdyller msyiiehadl
      481 dyikwdmnrn mtevydakls aseqgevshr yilglydlle rltdnypdil fescsggggr
      541 ydagmlyymp qtwtsdntda iarlkiqygt slvypvvsmg ahvsavpneq tgrmtplrtr
      601 glvassgnlg yelnplnlle nerqevklqv kwykahrrli qfgklyrlqn pfettrtawm
      661 fvsddkkeav amyfnifsea ssplhmlnfv glnpsqkysv ngeytaygse lmqigiyplt
      721 qndgdfdsav felkave
//
LOCUS       WP_010497254             183 aa            linear   BCT 01-JAN-2025
DEFINITION  FHA domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010497254
VERSION     WP_010497254.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..183
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=19993
     Region          78..182
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mlsekksvwv tvvnvlialv aaftlvytyi wntnvalklf vavffiiglt gmawrkygrt
       61 aasapeakke aaitklallg ddgdrikewy ihgetsllig rsssdlevqi dlsgteyaal
      121 vskqhavlny asgnwyiedl dssngvgikk rgesgkrlln gdepeqvhsg dtiyiantrl
      181 lvk
//
LOCUS       WP_010497374             260 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010497374
VERSION     WP_010497374.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28600
     Region          <4..258
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mnrlldvrql sktfiqngsv vmavqdvsfd igdgeclglv gesgsgkstl arillalerp
       61 dcgeitlagr sllalkgsal revrqhmqvv fqdptaslnq rlpiwrsvie pldnfpqvtp
      121 ffltevrhsr raaaarllem vglsadfldr yphemsggqr qraaiargis lgpkllicde
      181 ptssldvsvq aqilrllktm qaqlgmaclf ishdiaavqs vsdriivmkd grivdrfasr
      241 qlmdadrdey trrlvdavse
//
LOCUS       WP_010497379             157 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Ligilactobacillus acidipiscis].
ACCESSION   WP_010497379
VERSION     WP_010497379.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..157
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17978
     Region          7..149
                     /region_name="YdbS"
                     /note="Uncharacterized membrane protein YdbS, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3402"
                     /db_xref="CDD:442629"
ORIGIN      
        1 meksqhlper ikkvwkisal lslvvgsvmc aviywvvdhf dwpgwinyia wmlvlldfvv
       61 elliipyryr fwlyqitttd veiesgfflh kqtaipiari qnvtlqagpl fqlfhlqsvk
      121 ietaaaahei agvlpesavq lkqrlmeltq eedvnas
//
LOCUS       WP_010497388             287 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Paenibacillus elgii].
ACCESSION   WP_010497388
VERSION     WP_010497388.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..287
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30515
     Region          1..286
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 msnvtviglg pmgaalvqal lrkghrvtvw nrttakaepl vregamlads aasaisaspv
       61 tivcvanyet sysildtqev apalagrvlv qlstgspqqa rdneawarer gadyldgaia
      121 atppqmgrad ttiftsgtys ayqksepflk slagnvpylg dkvssasstd laflsylfgs
      181 mlgffhaari lesdglrvds fgsmiaeisp vigemvkhes eviqtetydq pqsslntcmv
      241 tvklfleqar eaginsefpt famglfkkal dagygneelg alikvlr
//
LOCUS       WP_010497394             394 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Paenibacillus elgii].
ACCESSION   WP_010497394
VERSION     WP_010497394.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..394
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42759
     Region          21..385
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,146,
                     149..150,153,225,228..229,232..234,237,261,265,316..317,
                     321,325,341,344..345,348..349,352)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mtlshersle spfqlrhylt litvviiagm nqglllpllt llldktgvst gvnglnaaal
       61 yigtfatmfw iekpvrrfgy kpvivvgili vlvtlflfpl fpnfwvwlvl rfmvgvgdsg
      121 lhyatqlwiv srspadkrgr yislygmayg agfslgplgi nllpygmwap flatmlctvv
      181 slmfvsrlpn alpetvkrep gaqaattypa vfrlawyall tsflygymes smnsnfpayg
      241 lrigmsdawi slllpvigig slilqlplgv wsdrwgrkpi lmaagligga afaavpfasq
      301 gnlllvlilf glagglvgsf ftlglayaad vvpkavlprt nviasvlfsi gsitgpnigg
      361 fsmqyfsvhs mfywlggayv lfallglwfr pkvs
//
LOCUS       WP_010497430             133 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Paenibacillus elgii].
ACCESSION   WP_010497430
VERSION     WP_010497430.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..133
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=14929
     Region          11..132
                     /region_name="Polyketide_cyc2"
                     /note="Polyketide cyclase / dehydrase and lipid transport;
                     pfam10604"
                     /db_xref="CDD:431388"
ORIGIN      
        1 mmtvlpsktl sitierrpee vyayvtnpen fpewvtsfvk sirrsgeewi vetteapitl
       61 kfvdnndygv adhwvtvatg qtilnpmrvv pngsgcevvf tafrqpgvse esfandtami
      121 ksdlrtlkri mek
//
LOCUS       WP_010496818              65 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold shock domain-containing protein [Paenibacillus].
ACCESSION   WP_010496818
VERSION     WP_010496818.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Horn,G., Hofweber,R., Kremer,W. and Kalbitzer,H.R.
  TITLE     Structure and function of bacterial cold shock proteins
  JOURNAL   Cell Mol Life Sci 64 (12), 1457-1470 (2007)
   PUBMED   17437059
  REMARK    Erratum:[Cell Mol Life Sci. 2007 Jun;64(12):1584]
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Phadtare,S., Alsina,J. and Inouye,M.
  TITLE     Cold-shock response and cold-shock proteins
  JOURNAL   Curr Opin Microbiol 2 (2), 175-180 (1999)
   PUBMED   10322168
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..65
                     /product="cold shock domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7048
     Region          1..65
                     /region_name="CSD"
                     /note="'Cold-shock' DNA-binding domain; pfam00313"
                     /db_xref="CDD:278729"
     Site            order(7,16,26,55)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:239905"
     Site            order(13..19,25..28)
                     /site_type="active"
                     /note="RNA-binding motif [active]"
                     /db_xref="CDD:239905"
ORIGIN      
        1 mqgkvkwfna ekgygfiere dggdvfvhfs aiqtdgfktl eegqsvefdi vegargpqaa
       61 nvvkl
//
LOCUS       WP_010497450             134 aa            linear   BCT 01-JAN-2025
DEFINITION  GtrA family protein [Ligilactobacillus acidipiscis].
ACCESSION   WP_010497450
VERSION     WP_010497450.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..134
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15702
     Region          1..129
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mkmlkryksf iiyvfwggva tlvnigtfml glkigwhyqt sniiawllal fvtyfsnkfl
       61 vfdspywgla qllreffsfl vvrlfallld mviiwlgikv lhynellvki fdntvvgian
      121 yivsrwfife nkni
//
LOCUS       WP_010497455             162 aa            linear   BCT 01-JAN-2025
DEFINITION  cysteine hydrolase family protein [Paenibacillus elgii].
ACCESSION   WP_010497455
VERSION     WP_010497455.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..162
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18363
     Region          4..147
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mkiallivdm qtvflkdkeq ssiekaceyi nytadllrsk ghlivhiqdi egrqesnkel
       61 ydiipeikae ehekrvtkvf snafwktele qlllenevgl vivsgfaaeh cvlftyngar
      121 ergfktvilq ngivgerdaa veatyrdrni isypviesfi gs
//
LOCUS       WP_010497466             400 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010497466
VERSION     WP_010497466.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18916554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..400
                     /product="MerR family transcriptional regulator"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45845
     Region          8..112
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(8..10,24,41..43)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(55,58,62..63,72,87,91,97,101,104..105)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          168..299
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mrsgdyattg qiakktgitl rtlryydqig llppsqhsqa sarlyskedl irlqkiqtlk
       61 yigltlqeik evireeslsg hdlrssltaq ketlrqklah mevvvkainq aigimknkse
      121 dvewsgliel ihavhsekdw veqyhtatrl qtriqlydkc svnpigwhrw lfghlieqsg
      181 ctvleigcgd galwarnmdr ipetwrvtls dfshgmleea rsslgerttq fkfvvadvqd
      241 ipfydeqfdt viannmlyhv pdmpkalsei hrvlkpggrl fastmskrhl qeveqlaaaf
      301 dpeirvldpv ierfnldnge qmlapwfsev rlytyddhll vnevrplldy itstpmnarq
      361 rltgaamhqf esflnsmier egkiriskds gfflgrkrsi
//
LOCUS       WP_010497475             161 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus elgii].
ACCESSION   WP_010497475
VERSION     WP_010497475.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..161
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19032
     Region          1..158
                     /region_name="COG5628"
                     /note="Predicted acetyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:444356"
ORIGIN      
        1 mlvtlekvke dgivtlnhlv elasydlsey ngrdvhengl fvadfdsksw ldsehfhlff
       61 iradekiagf vvirnlykeq vinlnhffvl rkyrrqgvgr eaaiqafnlf kgrwrvnqye
      121 wnvpaqhfwr sviqaytnqn ytetiredfk gpsqefsnhe m
//
LOCUS       WP_010497529             216 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010497529
VERSION     WP_010497529.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..216
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=22992
     Region          3..215
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mtkvgiigat gmagsaafke aqtaglnvta ivrnaakark elgdsiqile kdafslkked
       61 lagfdvvvda fstdpaqayl hvdltahlis lfreeksprf ifilgagslh tgddnhlvve
      121 dikkvpgaes fintpinqla elhflqdvtn vnwvgispas sfvagdaaen ilygteellt
      181 dkngksettg gtmakaivqe iqesshhqer ftvvng
//
LOCUS       WP_010497530             258 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter ATP-binding protein
            [Paenibacillus].
ACCESSION   WP_010497530
VERSION     WP_010497530.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..258
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29329
     Region          13..215
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mqtnarfgch qqivtiddif fsyenkpvis glnfsilerd fvglvgsnga gkttllkmiv
       61 gllkpvrgei rlfgqpidqf rdwervgyvp qknalnplfp atvrevvtsg lfgkknmfrr
      121 lskqerskad dalyamried ladrrigqls ggqqqrvfla ralinnpell ildeptvgid
      181 aetqagffrm irhmhqhhhi tfimvthdmd miqsylgeds vqksgglsfy vkhthepenc
      241 retdlthsmq qlretiev
//
LOCUS       WP_010497565             304 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010497565
VERSION     WP_010497565.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..304
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31564
     Region          1..286
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mqdaltgsle lgmlyaimal gvyltfrild fpdltvdgsf ttggaiaavl issgvspala
       61 tlaafggglv agactgllht kgkvnallsg ilmmialysi nlrimgkani pllgedtllt
      121 dvplllvmpi vvlvvkfald wfmhtdlgla lratgdnprm irsfgvntdn tiivgvslsn
      181 glvalsgali aqysafaeit mgvgmivigl asviigealf gaktvfratl avvlgaivyr
      241 livalalrvg leptdmklmt alivigaltl pmirgklrqk svirqraadl ensrarkvsa
      301 gggr
//
LOCUS       WP_010497606             267 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [Paenibacillus elgii].
ACCESSION   WP_010497606
VERSION     WP_010497606.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..267
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30834
     Region          10..164
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mnevnireas ivtpehvrlq frtagigsrt aaqlidnlll laafgaisll vglilmlldi
       61 glddalgeya aaflivlsfi ligcyyalae yymggqtfgk kwlglrviqe ngqpvtllsa
      121 iirnffrlid flpsfyfvgm lwmffhpmdk rigdlaagtf virdmqherl alrkrtrkwl
      181 dknnirltye lklseafrrr ieredwllls tfverlpsld kfkreelswq iaerlgtkle
      241 lerelyaaqs taflielyvq lseewtl
//
LOCUS       WP_010497707             111 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010497707
VERSION     WP_010497707.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..111
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12991
     Region          20..97
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mkiqvtadll dglvlallnr edyygyaltq emqkaisise stmypvlrrl kkdgylttyd
       61 qpfqgrnrry yqitdsgekh leqvykmwtd yknsldqvfi pdkehdsarq a
//
LOCUS       WP_010497731             243 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase family protein [Paenibacillus elgii].
ACCESSION   WP_010497731
VERSION     WP_010497731.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10065661
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..243
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=28255
     Region          7..196
                     /region_name="MPP_PPP_family"
                     /note="phosphoprotein phosphatases of the
                     metallophosphatase superfamily, metallophosphatase domain;
                     cd00144"
                     /db_xref="CDD:277316"
     Site            order(10,12,39,43,69..70,149,169,189)
                     /site_type="active"
                     /db_xref="CDD:277316"
     Site            order(10,12,39,69,149,189)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277316"
ORIGIN      
        1 mknrtlvisd ihgcydefvd llsvvkyept ddelillgdy cdrgfkskev ielilnlhke
       61 snaialrgnh dqmfldalng gddyiflhng gvntiesycg lnwfenyqgf dfnryleakk
      121 filkhykhhi eflnslpfyh eteefiftha glnpfyenwk eqpndnflwi rdifinnltq
      181 vdktvifght ptiniqdedc giwfggdkig idggccfgfq mncleiceeg ykthyvesks
      241 kkr
//
LOCUS       WP_010497774             283 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010497774
VERSION     WP_010497774.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..283
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31638
     Region          11..279
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mdltstytls ngvkipvvgf gtwqtpdgni aessvkaald agyrhidtae mygneksvgr
       61 aikasgvdrn slfvtsklnn inhtyerata aldksladlg ldhldlflih wpnpapyrnd
      121 nwekhlqetw ramedaykag kvqaigvsnf yqhhlevlek tqtitpmvnq ihlcpgdhnd
      181 elvdycrerg illeayspfg tgkiftdptl qkladetght iaqvclrwsl qhkylplpks
      241 vhaerieent hafdfelnde qmkkiddlvg vagyggnpde vnf
//
LOCUS       WP_010497750             170 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010497750
VERSION     WP_010497750.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20260227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..170
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19428
     Region          1..114
                     /region_name="Spm_actase_Thplmales"
                     /note="spermidine N(1)-acetyltransferase; NF041158"
                     /db_xref="CDD:469070"
     Region          86..170
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mielkkvtnd qikelqkisr qtfadtfgad ntdsdmelyl dqtygtetll aqlanpnsif
       61 ffawkdgnvv gylkvnlada qtekmgndsl eieriyvqkn fkrqgfgskl fqqalscare
      121 qkkakvwlgv wernyaalkf ynkqgfkqig ahvfqlgdda qrdlllqlel
//
LOCUS       WP_010497832             488 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Ligilactobacillus acidipiscis].
ACCESSION   WP_010497832
VERSION     WP_010497832.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..488
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54094
     Region          4..488
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 msgskepsfl ghprglstlf ftemwerfsy ygmraillyy myfavskggl gfdkptaasi
       61 msiygslvyl ssvlggfisd rlwgprrtvf iggilimfgh ivlstpfgsa alyisialiv
      121 igtgllkpnv semvgglyse edtrrdsgfs ifvfginmga fiapyivgwm gqsvnfhlgf
      181 slaaigmffg lvqytidgkk ylpkdslyas dpiqpeetka likkvsigvv aiilifvima
      241 lfkmfnvnnv inilsicavl ipvvyfinml tsgkvnkver srvwayvplf iasilfwsie
      301 eqgsvvlalf aedqtrlsia gfnfpaswfq sanplfimly tpffsmlwnk lgkkqpssgk
      361 kfsyglffsg asflwmmipl fihgtdtrvs pwwliaswal viigemlisp iglsvttkla
      421 pkafqsqmms mwflgdaaaq ainaqivrff tpsnemmyfg liggitvifg fvllffvpki
      481 ekfmagvk
//
LOCUS       WP_010497841             191 aa            linear   BCT 01-JAN-2025
DEFINITION  GbsR/MarR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010497841
VERSION     WP_010497841.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..191
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22033
     Region          7..176
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mnnwvgmtee qagivqkark rviesigknm dlygvtlstg hlygmmffqd kpmtldemge
       61 emgmsktsms tgvrtltdlk mvhkvwekgt rkdlyevepd wyqtfadffv ikwqksiemn
      121 vqalrksaae lkrlaesdpd nealqnfvat dtrkleeair yylwlgrlid tfesgeifkl
      181 vpkeepqtds h
//
LOCUS       WP_010497900             474 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Paenibacillus elgii].
ACCESSION   WP_010497900
VERSION     WP_010497900.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..474
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52911
     Region          3..394
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mntgfaalhi apqyvkrlqe lgitepsdiq adaipialeg kdvvaqsqtg tgktlayslp
       61 llhkidtsar evqalvlvpt relgmqivqt leqlvkdsdv rvqqliggas ierqidrlkl
      121 kpqivvgtpg rvqelvklrk lklhgirtvv vdevdqvfel gsmqdvealf kgmlrdrqll
      181 ffsatfpppl qdvidrwmre pvyvrvnpaq rtsetlehly fvcqerdkid tlrrivrlyn
      241 pkaaivfvne tddigeavak lqhvglsveg lygdsfkqer akamqafrag kfqlllatdv
      301 aargldlpqv thvinldppi dadhyvhrvg rtgrmgrkgt avsiitpreq fiidkfskal
      361 gieikqrtmf hgkvvdpeqe rairrdakkl verrvpdelp sgsekpeari aqagapklpr
      421 tegksvkpaq tgtgrpsapa spdkrkadre rdrknkgapr wlkekrdpsg kpkk
//
LOCUS       WP_010497852             243 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010497852
VERSION     WP_010497852.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..243
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26734
     Region          5..243
                     /region_name="EfiE"
                     /note="Predicted lantabiotic-exporting membrane pepmease,
                     EfiE/EfiG/ABC2 family [Defense mechanisms]; COG4200"
                     /db_xref="CDD:443354"
ORIGIN      
        1 mkawsviaae lykqkkgvlw klafggpalv svliflnmsl rydylmqrya gktpweamln
       61 evfflwaffl pigvtllaai vhfreysena wkhllslpvr rghvyaakwl vivlatvlsv
      121 lalmaglrlg glvigfpepf pfglygqyal ylifsslgit svqhwlssrf rntiipvavg
      181 vsgtvgamfl aqsewlrylp yaaplfalpg pdgdvsvsiv sgllfgtaal lagmlefgkr
      241 dil
//
LOCUS       WP_010497868             519 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Paenibacillus elgii].
ACCESSION   WP_010497868
VERSION     WP_010497868.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..519
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55447
     Region          25..410
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(26..27,30,61,111..112,114..116,119,139,142..143,146,
                     272,275..276,279..281,284,312,316,368..369,373,377,393,
                     396..397,400..401,404)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mvqkktntaw tvaalmlgll lasldqtivs tamptiigkl ggldkyvwvf saylianvvs
       61 mpifgklgdm ygrklffllg lvvfmigsal cgtsttmtql ivyraiqgig ggalmpitfa
      121 iifdifppek rgkmqglfga vfgissvlgp lagayftdhv nwtwifyinl plgivslili
      181 slfyhpvlpn npnqridwlg tfvfavsils lmfglelggk eyawdsvqii glfaiaivfl
      241 llfiriemra aapvvplplf gnrlftasmg vcffygalmm saatyiplfi qgvfqgsats
      301 aglvltpmml gvvassaigg rfigklsyrg imlgsvllll iatsllslvs vdtprwqitl
      361 ymilmglgig tgfpvtsiss lhnvdfrfrg tvtslvgffr sigsavgltv lgalqasaln
      421 rrlaellpag agaktpadpr allspefqan vpkpvleqmm vgladsiayv fqvtivmavl
      481 alifillmgk akmevptkgp rkeggssdeg sgihapqhm
//
LOCUS       WP_010497913             256 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Paenibacillus
            elgii].
ACCESSION   WP_010497913
VERSION     WP_010497913.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..256
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28029
     Region          1..250
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 msaiiryeki mellmadrev svadlagklg vtgktirqdl ekleskgllr rthggavlan
       61 egysgllagl apnpkhpdek reaaewalrf vepndiiald sgsttlemak lldnapltvi
      121 tndlhiisel ikkdrvrlvv pggfrsrnml vseeaaeflg rlnvqkafls ttgihpeygf
      181 tifthshvgq kramidsakq vfcvadhskf dkcalitfak lseigvivtd pylpeetars
      241 yeaagtrier srrsga
//
LOCUS       WP_010497996             342 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010497996
VERSION     WP_010497996.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..342
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37160
     Region          34..341
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mnrelewiqt vvpdmidvls rrflilkkik tdrpvgrrtl aaqlklsera lrtetdflke
       61 qglidssksg mtltengalv vrslgefmdq mltlqateke ltalfggirc lvvpgdsded
      121 eavtcsmgqt vneilqallp qghniiavmg gttmaavaqs ldselttgrd lmfvparggi
      181 gervdvqann isaqmaertk gqhralyvpe hvsektyepl lrepavrevi emirqsnavi
      241 hsigeaipma krrsmsqtai dslkqkgavg eafgyffnek gevvqklsri glqledlasm
      301 kcvvavaggs skghaiaaym klapsqtyli tdqgaanmil kg
//
LOCUS       WP_010498015             290 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010498015
VERSION     WP_010498015.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..290
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31410
     Region          4..283
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,214,236..238,240..241)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mlqliasdmd gtmlndhmvi sdynvaaikh aqekgihfiv stgrafkevk plldqagvsc
       61 plitmngalv idengktlss apipdqlaqk iiillkkagl yfevitshgv csddkaarie
      121 nfaellssid attpfklavs lasarmelmd inyvddyyel vndphiqifk ivafsphgqa
      181 glekvrqeis kydslvitss gsgnievnhi kaqkglalqs yadrlnipmd nvmsmgdnnn
      241 dlsmikiagi syamenatke ikmaanhlts kntdngagka ieeqltqlgl
//
LOCUS       WP_010498050             442 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Paenibacillus elgii].
ACCESSION   WP_010498050
VERSION     WP_010498050.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..442
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49463
     Region          1..438
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mnalnwsrgl temtlafhil fatvgvgipi fisiaewigi wkkdphyslm arrwtrgfvi
       61 tvavgvvtgt ciglqlsllw pefmrfagnv islplfletf afffeaiflg iylytwnrfs
      121 npylhwlltl pivigssasa lfitmvngfm ntpqgftien gkltsldpla amlnpatpsk
      181 vahvlssayl taafllgmia afsmlrgrnn dyykksirln mmtglllaaa tiwigdasak
      241 flaenqpekl aaaewhfets shaslviggq lnpvtneitg aikipwalsv latnhpngtv
      301 vglndfpede wpplyvhylf damvgigfyl lavpviflim trmkrrnayn rwmlwaifag
      361 gpfsllaiel gwfyaevgrq pwilrgymrv sdavttnphv gitfwlfaal ylllgivcll
      421 vlsrlfrnkp aeyeleerri il
//
LOCUS       WP_010498078             256 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010498078
VERSION     WP_010498078.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28291
     Region          2..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msmvyvngln ktypghiatq altdihltie kgefvgimgp sgsgkttllh mvstigtpss
       61 gtvlingtdp yqmkkdelav frrrqlgfvf qdfnlldtlt iaenivlplt ldnkplaeme
      121 arlqqvadrl nlseflnkrp yeisggqrqr taiaraivts pallladept gsldsnasri
      181 vmesleninr herttimlvt hdpvaasycs rivfikdgrl aaeihrgdnr qtffqkiidt
      241 lsfwgghthe lssirv
//
LOCUS       WP_010498054             205 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010498054
VERSION     WP_010498054.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..205
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24031
     Region          22..101
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mkktntiqrs pvalailall aeepmhpyrm qqllkergkd evinvrqrts iyqtidrllr
       61 dgliavretl kepgkpdrtv yestedgrkl frewlrdmls mpsqefpdfp vavsflsllt
      121 pddvlkqler rslllekeiq rvssdlqtyk dtiprlfmle teykravlaa ewqwvcsvsg
      181 dlrngelhwd eewlreiamr lnske
//
LOCUS       WP_010498106             298 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010498106
VERSION     WP_010498106.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..298
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33082
     Region          53..291
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 myfaqsnwfl aakgknffkf nvfqryienf dwdkaitsll qtlgslvlvs llffivnfvg
       61 krlirrgfes rkksnnqhls enrkatiftl sqnifhyail ffylyavlsi lgipvgtlit
      121 gagilsvalg lgaqgfvtdi vtgffillee qfsvgeyvkl gavqgtihai glrttqilgy
      181 dgtlhfvpnr sitivsnfsr ndmralidir vdpnkdinqm eriisqvndr ltpqyseiti
      241 ppqilgtvdp gngtlvvrvt iytkngaqgs iqreflaayl aalseagfei paapinle
//
LOCUS       WP_010498131             311 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010498131
VERSION     WP_010498131.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..311
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34357
     Region          4..223
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msfieikdvv kryggnisvd hlnlsirqge vfgllgpnga gksttikmlc gllkidqgem
       61 ridgisvaas pleikrrigl vpqeiaiygn ltarenvtff gklyglrgel lrervqeale
      121 fvglsdrqge kpgaysggmk rrlniacaim hrpkliimde ptvgidpqsr nhildsvrkl
      181 nqmgstiiyt shymeevaai strvgiidhg hliacgtqed lralvssdek llvkvaevkk
      241 eavselkahp riqqvavndr tleiylptsp nslqdilyil skhqvviqsl nrvepdleal
      301 flsltgrtlr d
//
LOCUS       WP_010498148             334 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010498148
VERSION     WP_010498148.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..334
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37118
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdnneyydl tiigggpvgm faatysrmhm aktqiiesld slggqvsalf paktlydipa
       61 yyqtsgkdli tnlteqtnaf epdiflketv esftkteqgf mikttkrtty skaiiiaagi
      121 gsfeprklrv dnapffegqq lhyfisdpti fknrnialag ggdsaidwal elapqarsvt
      181 vihrrdkfra lessvhalqq mpnvnfltpy tikdlkeaas gqlkvilqka rdkerknvlf
      241 ddlivnygfs ssntiieswg ldmerhaikv sekqetslpg iyaigdiayk egrpaliasg
      301 mgeaptavnn allyvypdrr qpahstelml kykh
//
LOCUS       WP_010498149             171 aa            linear   BCT 01-JAN-2025
DEFINITION  shikimate kinase [Paenibacillus elgii].
ACCESSION   WP_010498149
VERSION     WP_010498149.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..171
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=18885
     Region          6..168
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 meyrnivlvg mmgtgkssvg qalasrlnwv yedtdaaier tqgmsitrmf aelgepffrk
       61 aesetiertl qgrhqvvatg ggavlaehnr ilmqssglvv alkasaetii ervrsdqsrp
      121 llqggvedrv rhimesrkha ydfadlhvdt dgktvgqivd eicrslerer a
//
LOCUS       WP_010498150              97 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010498150
VERSION     WP_010498150.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..97
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=10717
     Region          1..96
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mhtitpqelk qrlengenlt iidvrepeev algmipgakh iplmevpqrl geipqhseti
       61 lvcrsgnrsg raleyleaqg ftglvnmtgg mleweql
//
LOCUS       WP_010498151             193 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010498151
VERSION     WP_010498151.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..193
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=21038
     Region          12..193
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mnypqsdlqn skgpkvkint tlgeieiqlf peqapktvkn fvslaqdhyy dgtifhrvip
       61 efmvqggdpt gtgmggesiy gapfedefsm dlfnirgals managpntng sqffivqstq
      121 vpadlieqmk aanypqevid myqnggtpwl dhrhtvfgqv ikgldvvdqm aaaptgaqdk
      181 pvddikiesi vve
//
LOCUS       WP_010498255             283 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Paenibacillus elgii].
ACCESSION   WP_010498255
VERSION     WP_010498255.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..283
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=30396
     Region          4..281
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 msqvrivtds tadipadlre rlgievvplk vlfgseafrd gvdmgpeqfy dklassgifp
       61 ttsqpspadf iqvyerlade gadsiisihl ssqlsgtyqs alvsksmide kadievvdsr
      121 sascgigmlv vaaaeaakqg kskseileri aslrqnigly flvdtleylh kggrigkaaa
      181 lfgsllnikp ilsvnddgvv ysvdkvrgqk kamnrivelm qkdfagkpid limayttgre
      241 taeeffsllk qhfdvksvqy thigpvigah vgpgtvaafa ipg
//
LOCUS       WP_010498230             280 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Ligilactobacillus acidipiscis].
ACCESSION   WP_010498230
VERSION     WP_010498230.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..280
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=30874
     Region          1..277
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mkiailtdsa amisskvrsq pnikvlqipl sldgetyypn elsevaglet lrdatlntvt
       61 eeqislttis avtdelqqag ytdilcihia ssisglgsnl stfakncqqs lkihlfdsht
      121 lgpaegalve raltlithgl kiadiltelt kyrqkqhtlv imenlknlrr igsisnnahl
      181 fsnnmlhykt llhfsengel evlmkssrtk kiatailnkf rssaskpela imadntmvle
      241 kyvsclkeim pqlqlvtdly spsifsfigp qaliiswqnn
//
LOCUS       WP_010498356             345 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Paenibacillus elgii].
ACCESSION   WP_010498356
VERSION     WP_010498356.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..345
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=40094
     Region          22..300
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mqaanvqsln idstqsdimi wankykgksr teylrdanef fyfmqgrrid eiskteieti
       61 nengkrtrll nkhvekykqy lkqknsdssi rrkiygirsl ykflringyd vdhmifetst
      121 lkkktkgygf yspvevkrla tealkerdge elstlillaa ttslrlnall glewlniikh
      181 eesglylvnt idkgdqeatr pfeqdlfdkl flirnrtgsd klfpnlkpdk veksiirlne
      241 rlglnpirkl rfhslrkaai kyemrttgnl rrakdqgghn saqvlledyt eaeddyasra
      301 gilmmktide svfdsvgkee llcmikeiny gvyqqlayri qkkei
//
LOCUS       WP_010498430             475 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Paenibacillus elgii].
ACCESSION   WP_010498430
VERSION     WP_010498430.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52057
     Region          11..396
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mgqdrhtdns svnskiilia mpwvifllfm qvfnenvfsl vtpkiaedfa itpgtvswvv
       61 tigglilgvg gaiyaalsds isfrklfvfg vvtfvagsll gfivqssfvl vvlaraiqcm
      121 gaavipgcfi vlvrrcapke qqplylgygt amyqlsagig hiiggyvaky fswtfsfllp
      181 lvvlitlpvf lkylpdetgk kgkldiigai iltvlstvli lavtrkdmvi gliglvilvf
      241 fvlyskkrtd pildlsvfri ktytplllvs iliycvqsaf ffifpffird vysagievig
      301 lmfvpanfga fisgmlagki tnkigklkaf yvgtsivlag mlmfgiflgm niiymwiala
      361 lfgigytiiy sgfytsftgl lpddrvgism svynlitkii lslfvalvgi lisqdtldfk
      421 llpvpeglkh vhlysnvcll fslmlvvgmv lfevfygrke rqklasetia eqeav
//
LOCUS       WP_010498437             242 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010498437
VERSION     WP_010498437.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..242
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27860
     Region          6..234
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 maelvykqii adlkkkifag efssmrlpde rslaeqysvs rssikraltr masdgvifkk
       61 rgsgtfinpl ylknesvfny eessnlgvsd nfemngkspq ikvlnfevir pteeiqrdlf
      121 lrpddfvyki drlrlfddqp fmietgyipi kilpslslkk iegsifsyve qafgqtvsks
      181 flsifaepst kydqkllhll pnepvgvmeg ifflnngtpf efsrmrlhyk ymkyntfvti
      241 sd
//
LOCUS       WP_010498446             151 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010498446
VERSION     WP_010498446.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..151
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17147
     Region          6..144
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mlrnqemlvt aaenlkehgi kntpqrqail aylmtshehp siemiyehvr qsgfsvslat
       61 vyntlellqa nklitevapd ndghmrydyl dkphyhvicv scnkivdvfd dsfkqlekka
      121 avetgyqiyn sqyevyglcp acqakqqaah e
//
LOCUS       WP_010498451             249 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Paenibacillus elgii].
ACCESSION   WP_010498451
VERSION     WP_010498451.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..249
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27682
     Region          4..199
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mkkrwlfvfa hpddesfaag gtiaklsgtg hevvlacats gckgksgefq fatreelarh
       61 reeelrsacs vlgvaelily ryrdgelksi dpealaerir stiaelkpdv vltfppdgvt
      121 ghpdhiaisq atekavalae aeypegrrps fyytsiphyy dhcqdsgpkd tcpitarvdi
      181 sgyrqhkgra lqayrsqvys vnraypgvme ddftvirnye yytlvrangq hvqdmtktal
      241 selptmdls
//
LOCUS       WP_010498497             115 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Paenibacillus elgii].
ACCESSION   WP_010498497
VERSION     WP_010498497.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..115
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=12694
     Region          13..109
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 msilviviqi ilagmfslss fmklkrtssm vqhwneyryp mwfltlmglg elagvvallv
       61 gfqfpallqy vglffvalml gaihahlfra khrpvmavna almlalsvvm iaiar
//
LOCUS       WP_010498506             271 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Paenibacillus elgii].
ACCESSION   WP_010498506
VERSION     WP_010498506.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..271
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29687
     Region          5..261
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,192,214..216,218..219)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mnyriialdv dgtllnddye vtdktvetlr tayeagariv lctgrgpgna ipvlerlglt
       61 gvlithngaa tvetpgpkll hqfgfevqti aelirycreq kvhfdvntal dmyvekvger
      121 eaamyekfma spervedvls mtvplvkltm fgseeemdav erelarvslp psihalrsgv
      181 hfvdvmskev skgralqala aqwdiapeqi vamgnyyndi dmirfaglgi amdnspaavk
      241 etadavtlsn nddgvhealr ryvlssgelr a
//
LOCUS       WP_010498556             416 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Paenibacillus elgii].
ACCESSION   WP_010498556
VERSION     WP_010498556.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..416
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=45293
     Region          219..410
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mqykilsrfw dvvlkryiep gemfdvpdde ldtfilkgli kkpaerkdsp rnlqavatrg
       61 shlgaglypt kpddptvtiq tsktyhefac dctdvaliyg nyydfdqltp nkitdkasie
      121 ypignttrte vfgpngsrem vvepgglves igtgirgkkg dglyvytgvs vpdggkfprg
      181 qvayssrgeg mkngdvvdsg atdthgqfvh hpvaivgrpk eptpavlivg dsiaggaqdn
      241 pqdrgfisla lgkdipwirv akgnessygf agtacrfrmr lakycthsvi hygtndflnk
      301 nlaqfqadli allqllsdyg lknyvctipp rtlsktdmtp vnpafalngd vmkantwlls
      361 nprpdliagv fdtakvlrnp ekpaewdpav lgtdgihpga vghtrmaaqi dlnrfk
//
LOCUS       WP_010498675             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010498675
VERSION     WP_010498675.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..249
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28351
     Region          7..235
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 maffgfkeld rlsevdmaiy rfftenvekv pymrvrdiat eahvsnssvm rfihklgyds
       61 fpefkvsfrs eqrrsqtndh eisfitaenf ppdiyekiel iadkmqqsdq iifcgigssg
      121 alaeyaarqt aavgfnsfcv kdpfyplitq lkntsnnlli tfsvsgktie liemlnnfvn
      181 dedvtlvavt adrssqlalm sryvlcysts qerlakyydl ttqvpamyli eqlistarrl
      241 aveqdhesi
//
LOCUS       WP_010498692             316 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Paenibacillus
            elgii].
ACCESSION   WP_010498692
VERSION     WP_010498692.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..316
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34181
     Region          20..296
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mteerykqaa agawigiagn lalallkgvt gymanskalm adafhsasdv vgsvavlvgl
       61 raakkppded hpyghgkaep iaaivlsvll lvvgveigis avksiyggvh eppegfalmv
      121 lilsiivkea mfqykfrlgk klasqalian awehrsdvys siaafigvgg amlgsyfgia
      181 ylyyldpiag lvvavmvlrm gyrllmdsvh stmdhvlhqe daadlletvq rikgviavdq
      241 lrarehghyv ivdvkisvnp risiqeghdi akivkhtlmk rflhvsdvfv hvnpydagyp
      301 ykstdsepdd mptllh
//
LOCUS       WP_010498766             332 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010498766
VERSION     WP_010498766.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..332
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36622
     Region          5..326
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtqklldvkg lktqftrdqg kvnaidgvdf hvnkgevlgl vgesgcgksv tslsvmrllh
       61 gtpgsivggt vrfqekdlva lsesemrsir gkdiamifqe pmtslnpvlk igkqlveair
      121 lhlkydkska rehavhmlkl vgipraedvi deyphqlsgg mrqrvmiama mscnpqllia
      181 depttaldvt iqaqildlmk klkdendmsi mlithdlgvv aemcdrvivm yagrvveegn
      241 vldifddpqh pytkglihsv pklrqnhrrl esipgnvpdl tnmptgckfa prcsavmdic
      301 rerepqlaqt tggrkcrcwl fendsakgvg ea
//
LOCUS       WP_010498947             253 aa            linear   BCT 01-JAN-2025
DEFINITION  pseudouridine synthase [Paenibacillus elgii].
ACCESSION   WP_010498947
VERSION     WP_010498947.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..253
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=28491
     Region          3..227
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mdrlqkvlae agvasrrkce elitagrvev ndkvvttlgv kvdpsqdfik vdgkpirrqs
       61 kvyvifnkpk gvitsaqdpe grktvteffk nikqriypig rldydtegll lltndgefah
      121 llthpkhhvp rtylatvkgv phgslldklk ngieledgmt apaeveyqdv rpenneavvk
      181 itiyegrnrq vrrmfdaihh pviklkriqf gplqlsgipr gkfrhltpqe vnelrqealk
      241 agegkshkiq kge
//
LOCUS       WP_010498958             368 aa            linear   BCT 01-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010498958
VERSION     WP_010498958.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..368
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41235
     Region          12..308
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mrllptrsce pgmrlgkciy neegvillne gveltggllg rleklgidyl yiadkatedl
       61 kieepladet riralteirt hfrsfmenes rskfsknhml grsfgnvmkm iindlnekqg
      121 taimllnmnv lnnylyqhsl nvciyttmlg mvsgynqdel malgmgallh digktkinld
      181 iikkpgplta eefeevkkht eigfrllkde pnmpllsahc afqhhereng sgyprgitgk
      241 diheyakwia vadsydamtt hrphrlamlp hqamevlfag vgtlydqrkv amfrdnvaiy
      301 plgltvnlst geqgvvvnin pavpqrpvvr vlidaygqvv gqpyeidlae kltvfinhad
      361 nltqashd
//
LOCUS       WP_010498999             170 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA (cytidine(34)-2'-O)-methyltransferase [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010498999
VERSION     WP_010498999.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..170
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=19448
     Region          3..159
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 mtnhialfep lmpantgnia rtcagtntel hlieplgfst ddkylkragl dywdhvkity
       61 hknlvdfies ipdlsylylv skfaehayte vdysdvsqdh yflfgkettg lpepfmrqyp
      121 dkciripqnd qniralnlsn saaiviyeav rqqgfpnlet thlydndklk
//
LOCUS       WP_010499113             232 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Paenibacillus elgii].
ACCESSION   WP_010499113
VERSION     WP_010499113.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..232
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24926
     Region          2..211
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 maplisviip awnesrllas tleavskaha saafsfdmql ivvddgsrdg tgdvacawad
       61 vvlrfpvnsg kgaamyagwq aasgeivvfl dadlgstaek fplllepvlr geadltvakl
      121 ppasipggfg lvrglagrgv rllsgydsga plsgqramrs evlrrcerky qgfgaevgmm
      181 vdavklgfri velevpfrhr etgrtwqgwi hrgkqlcevg ltlwqcwrkp ac
//
LOCUS       WP_010499178             162 aa            linear   BCT 01-JAN-2025
DEFINITION  HPP family protein [Paenibacillus elgii].
ACCESSION   WP_010499178
VERSION     WP_010499178.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..162
                     /product="HPP family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=16938
     Region          43..158
                     /region_name="HPP"
                     /note="HPP family; pfam04982"
                     /db_xref="CDD:461506"
ORIGIN      
        1 mnpssttpsa lrkgiayglq gagaflavla alllgqwsev tllmapfgas cvlafavpds
       61 plaqprsivg ghllstaigl vllhtagfha wsaalalgla itamqwtrtl hppagadpll
      121 vmmagsawsf lwspvllgsl livavawgyh rvcrrtypqr wl
//
LOCUS       WP_010499132             297 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010499132
VERSION     WP_010499132.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..297
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33617
     Region          4..217
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
     Region          <158..291
                     /region_name="Radical_SAM"
                     /note="Radical SAM superfamily. Enzymes of this family
                     generate radicals by combining a 4Fe-4S cluster and
                     S-adenosylmethionine (SAM) in close proximity. They are
                     characterized by a conserved CxxxCxxC motif, which
                     coordinates the conserved iron-sulfur cluster; cl18962"
                     /db_xref="CDD:450244"
ORIGIN      
        1 macieinnlt kdygqdrgif dislsvdqge vfgfaginga gktttirnlm gfikpdsgha
       61 tingldctkk saqvkqkvay ipgeinfpgn dsgevflkrq memigrgnwe hckkicdklq
      121 ldataniksm skgmkqktai aaafsaesdi limdepttgl dplmrdnfie llaeqkkmgk
      181 tifmsshifk emeetcdrva likngkivdi vsmddirynk nkrfklefkn dvsfkrfsel
      241 syhciniqpd dlqvtveind kdinelmndl sqydvlffke ikqtfedyfn qtfkeea
//
LOCUS       WP_010499195             475 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010499195
VERSION     WP_010499195.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..475
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53569
     Region          1..454
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdilslarfq fgmttifhff fvpfsigtgl vvaimetmwv rtkdkmylrm tkfwgnifll
       61 sfavgvvtgi iqefqfgmnw sdysrfmgdi fgaplaieal laffmestfl glwiftwkmv
      121 kpwlhatfmw lvtiasmlsa fwiitanafm qhptgyaikg gravmtsfpk liansqawye
      181 fghviagaia mggfliagms afkllndklk ekeffkrslk lglvigligs iavfaagdqq
      241 mkaliedqpm kfaategeke ntpdpapwkl vdfmdtkthk dkfsikipym lsilsyhkps
      301 gsiqgmdean kelqakygde nnyyppvntl fwsfhimalf gmamlgvavl glffarkksq
      361 llfrqkwmlw ivglftfvpf mtntsgwlvt elgrypwtvy glftikdsvs pnvsvgsllt
      421 sniiyfllfs ilgaimvalv vkelkkgped edselinapl ssdkevdpfn keafe
//
LOCUS       WP_010499237             237 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Paenibacillus elgii].
ACCESSION   WP_010499237
VERSION     WP_010499237.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..237
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25912
     Region          <8..139
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mkvfedwkit spygyradpi ngnqsfhtgi dlvkyhrypi pafiggvvlf agegvagagf
       61 ggygnvvalm dekgyvhcyc hldsvavakg qtlskgeivg yqgttgrstg shlhyevrsk
      121 dspsygygsh vdpgkyleal feneeddemm kekvaelesq vaalkgecqt llntaeahve
      181 qinalkallt dqnvpewftk efgedalngi vdspqgpnlf wrlaavafrl rknnnqs
//
LOCUS       WP_010499221             269 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase, partial [Paenibacillus elgii].
ACCESSION   WP_010499221
VERSION     WP_010499221.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..>269
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          26..269
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(26,51..52,89,94,99..102,116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(33..34,36..39,41,55,57,97,115..118,122,124,165,167,
                     169..170,172,182..183,186,202..205)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(33..34,36..39,41,55,57,97,115..118,122,167,169..170,
                     172,182..183)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(37,122,124,165,167,169,186,202..205)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(182..190,199..205)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msanerrgne vmlhyglqpg qtltgryrim aplgsggmsr vflaedlklk gkrwavkety
       61 igddpsages gqeaalrrhv llkeaetmsr lshpnlpdiv dyvpanahgf lylvmdyieg
      121 etllqrferl grrmnegqaa eiavqlcgll dylhslrpep iihrdlkpsn lmldadgrvr
      181 lidfgtarsf kaeqaadtvl lgtvgfaape qfdgrqsdph tdlfglgall yfllsggayy
      241 npqspyreae aaippglapi vlrllrasp
//
LOCUS       WP_010499246             108 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase, partial [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010499246
VERSION     WP_010499246.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         <1..108
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
     Region          <1..107
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 dkadekaihv llkredklva ytrivphtdq vhisfgrvlv vkeyrkhelg rkvvqatlnq
       61 iqkqfpakei kiqaqsylqn fyssfgfspv sdvylednip hldmilkk
//
LOCUS       WP_010499252             248 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010499252
VERSION     WP_010499252.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..248
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27043
     Region          56..218
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mysfyvilkr dfinlalnpv illtntvfpl vlvlvlgyls ngaysgedmn gydyygvtim
       61 vytavnvsmt aansfmertl kssnlrilys piprafvyls kitatvlfcg lsmlitlavl
      121 nwgmdvhlgg adigyvavll lllmlmsaal gvwlcclfks eeasnkllsm innvlallgg
      181 lffqldglge tvakasyfsp vkwvseaifr iiydhdpalf ataaalmlga tallllgckl
      241 tfktedyv
//
LOCUS       WP_010499261             182 aa            linear   BCT 01-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Paenibacillus elgii].
ACCESSION   WP_010499261
VERSION     WP_010499261.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..182
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=20954
     Region          72..170
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 mwssvfempy lmregateee leclvktwne klspqeiaei terqrnpfpa nhplhtqykp
       61 fdpslwglpq kklpdsyldf lrysnggefq tgeryfqffg tkqlreynla yefpeymags
      121 vsigmdgcgn hyildmredt dgdeypilaa hsgnlgyedc kqvarsfpel ckgttsmdee
      181 ld
//
LOCUS       WP_010499262             162 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Paenibacillus elgii].
ACCESSION   WP_010499262
VERSION     WP_010499262.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..162
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=18582
     Region          2..152
                     /region_name="SRPBCC_CalC_Aha1-like_6"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of an uncharacterized subgroup of CalC- and Aha1-like
                     proteins; cd08899"
                     /db_xref="CDD:176908"
     Site            order(14,16,18,27..29,31..32,37,44,53,55,57,59,66,69,72,
                     78,80..81,86..87,89,91,101,103,105,107,112..120,122..124,
                     127)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176908"
ORIGIN      
        1 mlasiqqadg gytarferhl khpvdqvwsv ltdndrlaew fpqlridelr kgglikfdmq
       61 dgtfkeltit dfamhsvlgy twgedrvrfe lypepegcll llveqlhkit ghtskdlagw
      121 hvcldvidal lsgratgfrk eewetwheqy vriltplgsa ne
//
LOCUS       WP_010499272             596 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Paenibacillus elgii].
ACCESSION   WP_010499272
VERSION     WP_010499272.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19960403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..596
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=67006
     Region          <142..392
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          <214..309
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          241..271
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mehahtegeh rfpspeqdfe iykaarsegd fqhalyhlac alstdpanae wldslnewid
       61 agedllpfvp veennyfavm avrayiyari nkfneafgll gqvvrvkpev pylvwvsewe
      121 priagvdhie edtiigfvsg alrsldmleg nvrhkalaal vsvlrkmcqa hpkaymlfwl
      181 lssmyrrqed vlaafaaakt ayklnkcwnt aigmalcfka qgnirkaagf ykkagrldpg
      241 neagyldlgd lylenglykk alkaynkavd iqpghewavp sllyceymik qdaerlgkie
      301 ayfkantsng rarellkpll pgselpfvdy ipepqeasin vlrqvaeqnp dlesggtisl
      361 tinhleapsa iramelylsk fgrsanppkl nltidnvpep dprqpiaeng amlwnyegpi
      421 aqpampepsg ravdavrrla mtpyqiedwy rtagelaqsl tpaylpdlfa vlthppeppe
      481 svsswhwlqr iqyaavflma rlspskpsea llslchgqsd wpvnaavavl ayeaqgdpel
      541 ekavselflr lmeripqegy cfftyalics wlqlssidvk lreqleqwkn dleqre
//
LOCUS       WP_010499278             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010499278
VERSION     WP_010499278.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..182
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20688
     Region          1..>182
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mriekyvnqh ydelnqteke iasfvmmqpk etiamsitel aqaclvsrsa ifrftkkigl
       61 sgfnrlkyil eddqmnkesq rdedyledai naigaaarqf knkdveriya sfdkakniyi
      121 cstgwvqeiv snqlqrdffi vgknayvlpg avdelgvvle kmnagdvlii isfngenerl
      181 ve
//
LOCUS       WP_010499298             287 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010499298
VERSION     WP_010499298.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..287
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32112
     Region          12..276
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mtilnekytl nngvkipklg fgtwlidndk vatvvqqaar igyrhfdtaq aygneegvgv
       61 glretglnrd dlfvttkvqa efkdystvkk sidqslqklg ldyvdlllih apepwtefhg
      121 enhyfkenle vwrameevlq agkvraigvs nflqtdltni lekgsvkpav nqllthignt
      181 sfdllkqakq ndvlveaysp vahgeilqne rikqmahkyr vsvpqlairy clelgtlplp
      241 ksedpehian nadvnfkiav edmqtlqnlp qdkdygnssa fpvfsgk
//
LOCUS       WP_010499359             823 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010499359
VERSION     WP_010499359.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..823
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91368
     Region          1..807
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mnesytpsak rvlelaqvna ngfrhqaigt ehlllalvse eqgiahkvla qfvitptdik
       61 eeierltgyg tlkrqapdny lpyspkakki ltravaqael lnsekigteh illalleddd
      121 ilssrildsl nidikrirqt vfrqlgisqt qvrrnakkkd kvegtptldg larnlnemae
      181 ngqidpvigr qkevtrviqi lsrrtknnpv llgepgvgkt aiaegfaqei indnvpvelt
      241 nkrvmmldmg slvagtkyrg efedrlkkil devyhdgnvi lfidemhtli gaggaegaid
      301 asnilkpala rgemqvigat tldeyqkyve sdaalerrfa tiivdeptpe etvdilkglr
      361 pkyekhhqlk lsdealqaav kmsdryitnh flpdkaidlm desaarvhia asggqqklar
      421 ashklkdaka akeqalvdee fedaakyrkq elkwkeklak leaqeegqdg hytkevgeed
      481 vanvvsewtg vpvtqltkse sdrlvnleni lhkrvigqne aiaaiskair rarsglgdpt
      541 rpigsfmflg ptgvgktela kalagamfgd ednmvridms eymekystsr ligappgyvg
      601 ydeggqlsek vrnkpysvvl ldevekahpd vfnillqvld dgfltdskgr kvdfrntiii
      661 mtsnlgatdi rdkkevgfga kattdeyqam sdkikgrlkq sfrpeflnri devvifhsld
      721 kqqlheivkl mthdvierik eqniklkitp aaidvvakag fdpeygarpi rravqseied
      781 rlsesllegk itpgstvtig aqkgkislkv keqetkepvt qsk
//
LOCUS       WP_010499366             282 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010499366
VERSION     WP_010499366.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31712
     Region          5..220
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mkpilevtgl kkdlgnfrld dvgfsliegc itgfivvnga gktttiklil glmlkdagei
       61 qffgkdvqkn erefknrigi vldegyfyde ltmlemksiv apsysnwdna lfnrhmerfg
      121 lplnqkigtl skgmrmkyai alaishqadl lvmdeptsgl dpqvrlelmd illdyvkdgk
      181 svflsshits dldkvadali lidngrivfs eekdilldrh gfvkgdpnel nettrkmflt
      241 lheteygfsg vtndkaavrq hvkhalierp tiedimlgyi rr
//
LOCUS       WP_010499444            1260 aa            linear   BCT 01-JAN-2025
DEFINITION  S-layer homology domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010499444
VERSION     WP_010499444.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 1260)
  AUTHORS   Gerbino,E., Carasi,P., Mobili,P., Serradell,M.A. and
            Gomez-Zavaglia,A.
  TITLE     Role of S-layer proteins in bacteria
  JOURNAL   World J Microbiol Biotechnol 31 (12), 1877-1887 (2015)
   PUBMED   26410425
REFERENCE   2  (residues 1 to 1260)
  AUTHORS   Mesnage,S., Fontaine,T., Mignot,T., Delepierre,M., Mock,M. and
            Fouet,A.
  TITLE     Bacterial SLH domain proteins are non-covalently anchored to the
            cell surface via a conserved mechanism involving wall
            polysaccharide pyruvylation
  JOURNAL   EMBO J 19 (17), 4473-4484 (2000)
   PUBMED   10970841
REFERENCE   3  (residues 1 to 1260)
  AUTHORS   Engelhardt,H. and Peters,J.
  TITLE     Structural research on surface layers: a focus on stability,
            surface layer homology domains, and surface layer-cell wall
            interactions
  JOURNAL   J Struct Biol 124 (2-3), 276-302 (1998)
   PUBMED   10049812
REFERENCE   4  (residues 1 to 1260)
  AUTHORS   Lupas,A.
  TITLE     A circular permutation event in the evolution of the SLH domain?
  JOURNAL   Mol Microbiol 20 (4), 897-898 (1996)
   PUBMED   8793886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1260
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..1260
                     /product="S-layer homology domain-containing protein"
                     /GO_component="GO:0030115 - S-layer [Evidence IEA]"
                     /calculated_mol_wt=138454
     Region          1058..1099
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
     Region          1119..1165
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
ORIGIN      
        1 mkrltnravs favivallvs mivpfsamaa ggslmkvkgy staaatptpv tsetvnisve
       61 idniddaqis siyyeienvt tspgspvenk snkgmktgpy evtfnsvkls agtnkitftm
      121 gdvtkissqp ayltftpttn itdlkfndva iddgqmypkd ptqtayvitg kspnattvqg
      181 yllgqanpit afrsnngdft fipnrntdfn mqagdnifki vasnntntyn ttkkfifnng
      241 kpflfngald tgsgkqklvn dpfpqlnqtt anltgkmkvd lapgsstvtq yvyaditvvg
      301 gspatqrvyf sgttpaplte ipaeststyk vfdlgsiplt lptnrnqtli vtfytgsglv
      361 gqapqqtftf nyfdpaapyv tkvtkdlgtd pvttqpveva lnqngdneis elpstfyiyt
      421 tgvdpagnvk afiggdttgi aatyvgpdgt qqkwkvqvng irdgraimsv vpngvtngkl
      481 dfplvitstp yiipvnfynn mviknaalet pyctpgtggt pclqakimnl peaeytnvev
      541 svngyvtklv agdfrdtnak stfmlnvska dtrwlpndnk dllnegrntv kinlrlngav
      601 vttvqyeifk ftlptpafvg dilpsplekf tkaqtpdkya tnansvsfvg nfvnadsikm
      661 tvrkkdalgn pvvtfdards gngwnypsap angqqnylns vgtgaintss iplpftgdvi
      721 fefmvsnktg itetrsitis repvpyrvie pilvrsgkdd vatingnfvd ikleaenads
      781 vsfgkdanvl skidpsdnkp yfyyryenlk agrntisftv nrgkdsskgs fvvnnvntav
      841 egaqmlmplq nkyklfegel elsfptntkl mrneptatnq yltgdrkllf glanvkdgrv
      901 nkayntdysa sfflqeptgk frpasklfwi nagavgqddy ldkdklkeal tgsgrdpyni
      961 dvnnanvrfy qknnendlkn sfvptkrgel tlkyddsirq dswkyvtvyq mdiyedyrgm
     1021 ttlawknigg evdpkkstit vpidhfgyfq vmymydsfnd itshewgrdt ldtlyskgfm
     1081 lnklqslfvp nesitrgefa tllvkafdlp lqysgnltfs dvqkfastnp lydykyieta
     1141 arvgiargna ggrfkpdeai trqdaavmia raaelkvnsd snksldslqk qftdakdidi
     1201 yalpaveavy kakfiegien vllsgqkkkt yrfdplqnft rvqaaavmer ilkqqkkfpk
//
LOCUS       WP_010499495             253 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Paenibacillus
            elgii].
ACCESSION   WP_010499495
VERSION     WP_010499495.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27599
     Region          7..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mtlhqlnqrq qmilnrmaed gevkiaelki mfdvtemtlr rdleklehwg yirrifggai
       61 llgkdialqe rtsvlieeka rigkraaslv epgdsifldg gsttlqvaky lqpdrqitvv
      121 tnalniaael qnkriptivi ggmmldstat lvgpvaaaal akmafnrvfi gttgitvkhg
      181 ysnsnmheae ikqlaiakat evnvvadhtk fgrqdlfsfa plhgihrivt dgspgeelra
      241 aleeasvdml lgs
//
LOCUS       WP_010499503             385 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Paenibacillus elgii].
ACCESSION   WP_010499503
VERSION     WP_010499503.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..385
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42825
     Region          6..276
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 martiirfgv igcglmgkef asaaarwchl tgvdfeprit avcdaneaas qwfrdhvpsv
       61 eavytdyksl ladsavdaiy cavphqlhaq iyvdiieagk hllgekpfgi dqaanrliqd
      121 aidrhpeviv rcssefpffp gaqqiyrwvq erkfgriiev eagfwhssdl dptkpinwkr
      181 riatngeygc mgdlgmhvlh lpmrfgwrpr svrallsqiv perpdgqggt vpcetwdnai
      241 laceahtedq qfpmllsmkr iapghantwf iriagtafsa efttkqpkqi vslpyspggv
      301 qawhvadapy ksaygtvtgg ifefgfpdsi lqmwaafcde lahgdrmqqp frcatpqeag
      361 sshqiftaal esnrtgrtis idwrs
//
LOCUS       WP_010499571             658 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Paenibacillus elgii].
ACCESSION   WP_010499571
VERSION     WP_010499571.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..658
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=75587
     Region          2..650
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mprhlvigng kflinldrnt ymrdlyypyv gqlnhvggyq criglwvdga ftwladpewk
       61 felsyiedsl vtevrashyh lgitllmndg vhqredvylk rvrvhnhwdt vrevrmffnq
      121 dlvinetevg dtaayypqnn tvfhykkdry fmfnglagtd giyqyttgvk rfynaegtwr
      181 daedghlmgn aiaqgsvdst vsfrlhvppn sdetlyywms agknleevkk ldnyvkeshp
      241 gklldrveiy wqrwvnkpee rdygnlseac vrlykhslli vrtqtdvnga iiaandsdim
      301 qsnrdhysym wprdgaliay amtmagyqgm itpffnfcae alspdgylhh kynpdgtvgs
      361 swhpylnggs mqlpiqedet glvlfalwqd yvrhgiielp qslyrtlirr aarfmsgyie
      421 qelslpkpsy dlweerygif tfttsavygg lvaaanfcsl fgdeerssry rhtaekiksg
      481 ilkhlwdeee qrfvrglvld ggvwvkdktl essvygifef gvlpaddprv vstmkvnrag
      541 ltiktdiggv aryhhdyyfq rssdidnvpg npwiictlwi aeweiecakt lkdlesprrt
      601 lewvvkhame sgilpeqldp fdggpvsvap ltwshatyvl tvvkytekyk kllaaska
//
LOCUS       WP_010499572              66 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Ligilactobacillus acidipiscis].
ACCESSION   WP_010499572
VERSION     WP_010499572.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7166
     Region          1..65
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 meqgtvkwfn adkgygfitr edgsdvfvhf savqgdgfkt ldegqhvtfd vedsdrgpqa
       61 anvvkd
//
LOCUS       WP_010499594             307 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010499594
VERSION     WP_010499594.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..307
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34196
     Region          7..250
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mettpvvqlq qvtkrigskt ivdglsfvvk pgevfgflgp ngagktttir mmvglmaitn
       61 gevliqghsv ktrfeqamlh vgaivenpef ygfmtgyqnl vhfarmmpnv tkeridevvr
      121 lvklenrimd kvktyslgmr qrlgvaqail hrpsvlvlde ptngldpegi relrdylrrl
      181 aaeeglaviv sshllsemel mcdrvaiiqn grlldvrsfk eapsetedie vrfevdrpda
      241 alellgeahr aktegselvv wlpnrreata elnarfvsag irvygirtlt ktleeqflev
      301 tggnriv
//
LOCUS       WP_010499674             855 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010499674
VERSION     WP_010499674.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 855)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..855
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94970
     Region          19..>156
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          128..418
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          <661..853
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mniihkltlr hlmknkkqtl vtvigvvisv amvtavitlg ssflvlmqkq tiqnygewhv
       61 lyknvnkdql eaikqdaatq qlitskergf allpgsqnin kpylfikafn aqgfnnfpia
      121 lsegrlpqqa neivlseaia tnakvtyrig drltldvgqr snpagsgntd ltqdeplrfl
      181 ngtsaetlih tttetytvvg fikrpsweqt wapgytalty vdenmvdank tvdasvvlkk
      241 vdgnvfahan dlstknnigs fktngtllry ygvmggglgk tynslffivv lvivigsisl
      301 iynafaisvs ersrylgmls svgatrrqkr nsvffegavi gvisiplgvi cgligigitf
      361 hfinsmleaa igvmekltlv vtpsslamtc lisivtifis tylpaqkask isaidairqt
      421 tdikltgktv ktsklvqrlf gieaefglkn lkrnkrryha tvfslvisiv lflsvsffts
      481 nlqkslnvsq kdynydigvy kndevatlde rlvksivsle gvteyslikq wsgvftwvae
      541 ksipegakpp wdpdqgryky nlqvnalsed klkayaqkvg ieyakltnpa hptailidvm
      601 syrdkkdnki ietrgiqgra gemldlvsmd fnkesvskve laavtdqfpm glvrssfeih
      661 lvvsepvfdq lmkkskdkay sglylnskdp lktqqdieem kkelevsnif qvrqhseqii
      721 lllsvfvygf valitalsma nilntistsi alrkrefaml rsvgmtpksf nkmmnyesif
      781 ygikaltygl pisavimvli yraisysfsy gfmvpwtsil yviaavfviv slsmyyasir
      841 vkkaniidal kqenl
//
LOCUS       WP_010499675             227 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010499675
VERSION     WP_010499675.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..227
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25322
     Region          1..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 meilriehls kvygkgdtav kalddvsfsv dkgefvaiig psgsgkstll hmlggvdkpt
       61 sgkvfvdrtd mysldetqla vfrrrqigli yqfynlipil tveeniqlpl lldqhkvdrk
      121 qfedivktln lqnrlnhlpn qlsggqqqrv sigralmnqp aiiladeptg nldskngsei
      181 idllkmfnks lhqtlimith derialqadr iisiedgkia kdevirp
//
LOCUS       WP_010499696             492 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Ligilactobacillus acidipiscis].
ACCESSION   WP_010499696
VERSION     WP_010499696.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..492
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=54089
     Region          1..457
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mkmqlaeiaq aldiepqngw dditvtsvsf dsrkisagal fvplidekdg hqyvesakdn
       61 gavatlwqed hpntptelpf lqvedslkal qklgsyylqk inprvvaitg sngktttkdm
      121 vagilstqfh vkktpenfnn eigvpmtclt mepntevlvv elgmdhfgql dclsrlvspd
      181 vavitmigea hieffgtrak iadakmeiln glkedgyfiy ngdeplller akdktmpqlt
      241 fgnnesndiv atdieghens tsfkvaaype tpfnipmigt ynvnnalaai svgkifqisa
      301 dnmsqalknf eitknraewv tgkkgekils dvynsnptaa rkvleafsqv ttsgkrivvl
      361 gdmlelgdqg aamhaglaqa idpqkiasvy lcgdlmgsla dalrtkfsnd qvhhykvdek
      421 erlfndldae lspndlvmlk gshgialekv lamlirdcif vfksasilwl cvlerktlqd
      481 rrrtiptgci ve
//
LOCUS       WP_010499725             198 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010499725
VERSION     WP_010499725.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21803
     Region          27..73
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          84..194
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mvttsnkser vpsdkvnsrv ersrhtvltt afellseggv asftvdevar rsgvakttiy
       61 rhwptrealv idacsrmiae qetpdtgsle gdvtailiei ahllptanws fvlpsivdta
      121 ernpefaeih sriqrghaap lrevlqravg rgelsadadv stivaallgp lfyrrwfsre
      181 piddqfvqai ikrvlasl
//
LOCUS       WP_010499708             200 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Paenibacillus elgii].
ACCESSION   WP_010499708
VERSION     WP_010499708.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..200
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22571
     Region          6..>199
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 meplakaviy arvsteeqah hgysiqaqlt elklhaeqhd meivdeyvde gvsgksinkr
       61 tqmvrllkda asgkfeyvlv ykldrvarnl kdamqindel gkhnikiifl kdnldtstsh
      121 gklhfqimgs vaeferntiv drvkmgmtqr arqgqynggi cfgynnvdkm lvvneaeaai
      181 vreifklakk gngyksiirl
//
LOCUS       WP_010499732             140 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Paenibacillus elgii].
ACCESSION   WP_010499732
VERSION     WP_010499732.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..140
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15492
     Region          1..121
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mhsmsfyant vlriltgvif fmhgkfklew gysnlsewlh sqgfplaaff ahvlpwiell
       61 ggiimiigig trylailfsl illvalfkvk iaagfisntn tgyefdlllm ivclhvavts
      121 pnslkqvwmt sgkggetkhv
//
LOCUS       WP_010499737             136 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Paenibacillus elgii].
ACCESSION   WP_010499737
VERSION     WP_010499737.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..136
                     /product="VOC family protein"
                     /calculated_mol_wt=15202
     Region          18..134
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mneqqqakes nsqaspvknk vgsifvpvrn ieksrswycq vlglneddck imnghlcplp
       61 megtgiildt mpkwggdqpg gapsietpaf mfmtedlrss fdymkkigve lvteiehdhw
      121 fvvkdpdgnk lmicre
//
LOCUS       WP_010499754             203 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Lactobacillaceae].
ACCESSION   WP_010499754
VERSION     WP_010499754.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillaceae
  ORGANISM  Lactobacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Lactobacillaceae"
                     /db_xref="taxon:33958"
     Protein         1..203
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23225
     Region          3..132
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,63..64,67)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(62,113..114,116..117,121)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(68,73..74,109,112..113,116..117,120,123)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91..93,109..110,113..114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(122,128..129)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          144..186
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(145..147,181..182,184..186)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 makigyarvs skeqhldrql aalkdvdklf tdklsgantn rpelqkmlay iregdivmvt
       61 eldrlgrnnh dltkimnsiq nkgatldvln lpsmtgiadp nlrqlmtnli ielykyqaes
      121 erkriierqq qgialakqqg kyhgrkpqyt qddprlqhaf klyqagmsdv dvarntgikr
      181 ttfiryrkkf nvkpvfsank icf
//
LOCUS       WP_010499782             311 aa            linear   BCT 01-JAN-2025
DEFINITION  ketopantoate reductase family protein [Paenibacillus elgii].
ACCESSION   WP_010499782
VERSION     WP_010499782.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..311
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35175
     Region          1..299
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mrvlvygagv igsylahvlv rggndvtvla rgkraeelek eglvirhyfq rkttvdpvrv
       61 irtleagdiy dlifvvmkyt dfqavlpila nnrssnivlv gnntdahdmq nylmehsdth
      121 kniafgfqis agsrengrtv cirggvqmvl gglngpipfk avldqafakt kyklvyheni
      181 dawlknhivp ilalgfvtii herqmtkiar ddkqlrqmia amdegfrvle aqgypltpae
      241 qaslirkhpt llrlllkiyh ilpfsrlvdg spyeiaalnr vfrdwkersn vptpnwdvle
      301 erfnasypfi h
//
LOCUS       WP_010499797             318 aa            linear   BCT 01-JAN-2025
DEFINITION  carbohydrate kinase family protein [Paenibacillus elgii].
ACCESSION   WP_010499797
VERSION     WP_010499797.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..318
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34805
     Region          16..312
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mfefkqvldf edrqndvlma gellidlisa dyedafegaa yhkffggspa niamnvkklg
       61 grsqiaaavg edrlgmflin qlriagiepe yvetvgnsts lvlltkskst pvpvfyrsad
      121 yqisytskle eallrskilh fscwpismlp ardtiekmld laakqnvlig fdpnyhpvlw
      181 qkgedgaayv ksiigkvdii kpsgddaerl fgkdtpynhi kkflslgakl viltlgkyga
      241 ivsngsetvt fktlatevvd ttgagdafws gfytalvkgy sihealslgf avsayklkyt
      301 gavvdlpele aiknlyel
//
LOCUS       WP_010499823             187 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010499823
VERSION     WP_010499823.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..187
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21882
     Region          25..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkvylnhklt rgarrtlnaf ssvllnllqq ekfekitvnq ictdacyprt tfynyfedky
       61 dllnycwfli vsdiqinntq hltpekaahl yfgnlydmlt erkdlldkil lhndiegqmv
      121 qsfanylkke vnqiigeles slehqvpkkl lvaylsetvm vlltwifidq hdlpketaid
      181 yleqlla
//
LOCUS       WP_010499831             385 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Ligilactobacillus acidipiscis].
ACCESSION   WP_010499831
VERSION     WP_010499831.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..385
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41274
     Region          1..377
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mefigslcli listaigghf sarlnlpavi gellvgillg pallnwlqpn dfihffseig
       61 vvilmfiagl esdlsllrrf irpstyvavv gmlfpiliay ltglyfhfsq lesiflgvtf
      121 aatsvsisvv vlqemkqlds hegttilgaa vvddvlaviv lsilisfsgg qvnssgnkqn
      181 lvlslllqig yfvllfvlgr wvipyvmqfs skllvpaset lislvlclgl adladitgls
      241 tvigaffagl aigqtdykvl idrniepigy avfipvffvs iglnmtftgi indfwlffvl
      301 siggilskll gaglgaklah fswpssfmig agmvsrgema liiaqlgiqs hllstdrysa
      361 vigaiiittl itpfllrgti skinh
//
LOCUS       WP_010499859             334 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Paenibacillus
            elgii].
ACCESSION   WP_010499859
VERSION     WP_010499859.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..334
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35718
     Region          38..331
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 menatkqtvv lnrpkinaks salaalmvla affpffsgpy wldvgflavf yivlglglnv
       61 vvgyaglldl gysaffavga yttgifmtqf hmnfflalal sglfaavagl iigaptlrlr
      121 sdylaivtlg fgeivkisak nleftggasg iygilspfpa pttfmgvtin nltycywail
      181 ilavvaivas krlgqsrigr swayireded aaeamginrv rsklaaysvg affgglagav
      241 favkmtaiap esfnfmqsvm illavilggl grisgvviga iivivlpesl rdlnklihld
      301 vdidryrflv fgvalvilmi frpqglvpes rgke
//
LOCUS       WP_010499882             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Ligilactobacillus].
ACCESSION   WP_010499882
VERSION     WP_010499882.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..268
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30639
     Region          1..268
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkiitftaik ggvgkttltl nygdwlakqg nkvllidldh qcnlttvfek trrnntiaea
       61 fkddeeaqev lidkvapnld lvagfidldv lgsrlennsn kemmlfmwfk nnlnklqlnq
      121 ydyilidthp dfgtitknai avsdyllspi tpsehgynak fdletrldkf rkslfdyrtg
      181 etyvdaklff ignmikhnts msrdllnhia ndetvatiip erelfnkata rhasifeltq
      241 qddsiykqnk kfveqanqlf qeladkik
//
LOCUS       WP_010499920             134 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin
            [Paenibacillus elgii].
ACCESSION   WP_010499920
VERSION     WP_010499920.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..134
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=15044
     Region          21..132
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mslktlentk tklhkvedqe yrrgdiwlvd fnggatgsem tgvrpaviis gnignrfssn
       61 vvllaissqi nkkllpthvy lkaeehnler dsivlcemit tkdkwnlmyk ltsldyktma
      121 dievaikvnl giey
//
LOCUS       WP_010500004             188 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Paenibacillus
            elgii].
ACCESSION   WP_010500004
VERSION     WP_010500004.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..188
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=21050
     Region          94..180
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mknadkqalk stgkslllfg atsvvfglil nksafiaqfk kpflfeeitt slllfailli
       61 stfifqnlnn spteseyvkq eedqsslvsi vcsvlagiie eicfrgslql vlnsllnswl
      121 siiivslifa llhrqykswk tlvyifyvsi vlgvyyqite siwvcvvahs lynmfvsisi
      181 sinknksn
//
LOCUS       WP_010500029             367 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Paenibacillus elgii].
ACCESSION   WP_010500029
VERSION     WP_010500029.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..367
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39058
     Region          1..343
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnklkagivg cgkisgiylq nltanpelev aacadlnvar arasadeygi pkactpaell
       61 adpaidivvn ltipaahaev clqaleagkh vyvekplavt reegrailgk aaekgrfvgs
      121 apdtflggsi qtcikliadg wigipvaasa fmigrghehw hpdpefyyak gggpmfdmgp
      181 yyltalvaml gpirrvtgsa gisypqrtit sqpkfgrtiq vetpthiagv idfrsgaigt
      241 iitsfdafgg telprieiyg segtlsvpdp ntfggpvrvr rydatefsdm plthgftdnc
      301 rglgvldmaa airqgrtnra ngelayhvle amhgfhdasm hrkhyemhss cerpaplkag
      361 laggifn
//
LOCUS       WP_010500071             272 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Paenibacillus elgii].
ACCESSION   WP_010500071
VERSION     WP_010500071.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..272
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29086
     Region          1..270
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 msilfytavg liaatfgslv glgggiiivp alvylgpmfv gqtisvstav gtslavlift
       61 alsstltfvk qkrvdfksgw llfitcgpga mlgsyttqfv naksfqlsfg lfmllmaill
      121 vlrdylkpln vkwhmqrtyt dssgntyhyg ysilpaliig llvgfisglf gigggslfvp
      181 amvllfqypp hvatatsmfv illsslmgsf thfslgevnl wmvlglapsa ivggwlgaki
      241 asrlsskkll wvlritfviv sfkmiveglv lt
//
LOCUS       WP_010500096             281 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Paenibacillus elgii].
ACCESSION   WP_010500096
VERSION     WP_010500096.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..281
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=32831
     Region          2..258
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdyiqafeah lrskdrsent iscylrdtlq fiawyrskte ygldklield gveykkylqq
       61 sdqavitinr kiasinvfcq wmykqgyike aihieavrnk virqykgled kdlwklrnei
      121 hrmgnrmhic mielligtgi rvselvgirl kdielsdrkg tlkvfgkgns frtipinkdv
      181 rkalaryiev rpdneseylf igqrgalern ainlilkkyg driqvkvtph mlrhtlayrl
      241 vkttplttiq qilghdhvtt tniytlttqq dmeivlanie w
//
LOCUS       WP_010500097             269 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Ligilactobacillus acidipiscis].
ACCESSION   WP_010500097
VERSION     WP_010500097.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..269
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30329
     Region          6..263
                     /region_name="HAD_YbiV-Like"
                     /note="Escherichia coli YbiV sugar
                     phosphatase/phosphotransferase and related proteins;
                     belongs to the haloacid dehalogenase-like superfamily;
                     cd07518"
                     /db_xref="CDD:319820"
     Site            order(11..15,46..48,68,113,115,187,195,217..219,221..222)
                     /site_type="active"
                     /db_xref="CDD:319820"
ORIGIN      
        1 mlnqckliav dmdgtflndq kdydrqhfaa lyrkmqerki qfvvasgnqy yqlctffadf
       61 pdiiyiadng ayirdlttvy fgsrfdpkqa kkilgqlnty pglfdelvvg gfksayiled
      121 sseefkkeah fynrklqivd sfaeiidest kysfnyttqd tisfmqklqe qlwgmaeitt
      181 sghgnfdiiq pgvhkasglr hlsqrlgipl sqmcafgdgg ndlemleavg dgvamancap
      241 evkkiaqhqt gtnneqgvlq yldklldnn
//
LOCUS       WP_010500123             365 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010500123
VERSION     WP_010500123.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13386660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..365
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39494
     Region          9..>150
                     /region_name="YhgE"
                     /note="Uncharacterized membrane protein YhgE, phage
                     infection protein (PIP) family [Function unknown];
                     COG1511"
                     /db_xref="CDD:441120"
     Region          170..365
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mnayihltla qlrlfvrnrq vlfwtllfpi ffmvmlgsfl gkgnpvsvtg aivdedrtaa
       61 sealvkalqd npilrlnaas alnpeletlk rgdyqlvlvi pkgyeeqtkp gvtaaaaaik
      121 vyydetnaat sqiglqvlap vvdgidkkls gytpkitirp egvqslklsy idflvpgiva
      181 mmimsnnlng vagqiaswre rgilrrmqst tlkastfias qitarlllng lqavivlvvg
      241 svffgtqvng swllllsfiv lgtlafmsig fiiaglaktp esagpiagfi sfpmlflggv
      301 ffpiknmpef lqpivkllpi shlttalrqv mnvgagfsvv wseaallggw llvafivasf
      361 tfrwe
//
LOCUS       WP_010500271             353 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenibacillus elgii].
ACCESSION   WP_010500271
VERSION     WP_010500271.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39453
     Region          1..352
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mallslenvs vaydhqyilq nfnltvekgq lisllgpsgc gktttlrlia gfleakdgkf
       61 mlngkdytrv pvnkrnfgfv fqsyalfphl svydnvafgl rlrkvpeaev kqrvlrilev
      121 vslagfeqrf pkalsggqkq rvaiaralvi epdlllfdep lsnldanlrv nmrveirriq
      181 qelgittvyv shdqeecfsi sdrvaimnkg iieqldrpst iykypktefv arfigfnnfi
      241 tfeerreagd gielkvkgyt fhaarqsgae gatskkgair pddvqlgtae eighgpnrvr
      301 ggikvstflg rsyqyvvetd lgdftvnkem evpyssgqqv hllfpadklv lvd
//
LOCUS       WP_010500286             278 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Paenibacillus elgii].
ACCESSION   WP_010500286
VERSION     WP_010500286.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..278
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30591
     Region          10..274
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mkhivsqpwl fehgtddhiv iadcrftlgk sesgkqsydi dhipgavyfd lerdlsgpit
       61 ehggrhplpd vqelaaklgq agihagstvv ayddqggama srlwwlltyl ghekvylldg
      121 gyskwkeagy pvtdeppllr eavftprvre dlavsveqvk erlgkpgvtl idsreakryl
      181 gieepidkva ghipgaksyf wkdaldetga wkseaaladr ferlrraeei ivycgsgvta
      241 cpnvialsea glnnvklypg swsdwisyeg npiatgee
//
LOCUS       WP_010500293             148 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Paenibacillus elgii].
ACCESSION   WP_010500293
VERSION     WP_010500293.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..148
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16143
     Region          11..139
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 maavktfkat ahlqegvkvk assrqfelti depkslggtd tgmnpveall aslgacqsiv
       61 arvyapkfgv klddfqvdve gdldldgffn rsevrpgyse irytfrvktd spkdkveefi
      121 rfieskcpvg dtianpvnlk lnsivies
//
LOCUS       WP_010500298             204 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010500298
VERSION     WP_010500298.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..204
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23264
     Region          9..198
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mdpkvqdkrm ekgeqtriri lhaaiaiise hgikevsaak laqltgvsks nifhhfksid
       61 eilhgalhil fddllepmaq eyrdleqflh qlgqsifrvp epylkafkaf fsfyhegmfn
      121 adfreallsc tdkitellgh qlnrlalrpl dektlesvta llfslmdgmg lhyllngnsq
      181 lyeqawrlqv smlcrhlaed dsla
//
LOCUS       WP_010500354             209 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010500354
VERSION     WP_010500354.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23106
     Region          6..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprtgrprsf nrdeavaaam llfweygfes tslaqlraam gdisaasfya afeskealfr
       61 eavdryisty ghvsesfrdt sltskaamel glrqsarmqt enthplgcll vlsavncspe
      121 qqhiqdllsk erervrgwik dcieravang efpestdism vvllfetflr gvstqardgv
      181 pyeaidaait qlmsvwdais vepgirgid
//
LOCUS       WP_010500467             205 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerol-3-phosphate responsive antiterminator [Paenibacillus
            elgii].
ACCESSION   WP_010500467
VERSION     WP_010500467.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..205
                     /product="glycerol-3-phosphate responsive antiterminator"
                     /calculated_mol_wt=22408
     Region          10..187
                     /region_name="GlpP"
                     /note="Glycerol-3-phosphate responsive antiterminator
                     (mRNA-binding) [Transcription]; COG1954"
                     /db_xref="CDD:441557"
ORIGIN      
        1 mqdldflerl rqsrmiasvk ehktlekaak aqvgavvlsi gnigniksfv dlykknripv
       61 flhverlggl sqdsegmafl atcvkpdgiv ttrnqlikla kkeglltiqq iflfdsdsvk
      121 sglksvqetq pnaieimpal lpeyirvyrq etnipiiagg liqtreqire alqsgavavs
      181 mgthelwrep igevlsdggp ggees
//
LOCUS       WP_010500468             160 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus elgii].
ACCESSION   WP_010500468
VERSION     WP_010500468.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..160
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18995
     Region          1..160
                     /region_name="COG5628"
                     /note="Predicted acetyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:444356"
ORIGIN      
        1 mevvvskaae eqksvlrnll elykydftef dpedvnehgl feypyldhyw teegrhpflv
       61 hvdgklagfa lirelgsder vysvaeffvm kkyrrhgvgr dlafdlfnrf pgqwevaqmk
      121 enepaqkfwr rivdeytkgs yqemtrddwe gpiqtfrslp
//
LOCUS       WP_010500522             406 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase, partial [Paenibacillus elgii].
ACCESSION   WP_010500522
VERSION     WP_010500522.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..>406
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          3..404
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mkknnfallg igsdlaeamq khgyneptpi qseaipvala ghdiiaqaqt gtgktlafal
       61 pileninpan pnvqalivtp trelaiqite eikrwaplkg lrvlsayggq dverqirkle
      121 gnihiivatp grlldhlrre tvqlhklsvl vldeadqmlh mgflpevvei isvtpsrrqt
      181 llfsatmppr irqlakeymr qpveievksk rvtldeieqv viqttdrgkl etlcklidee
      241 npylamifcr tklrasklmn elaergyscd elhgdltqak reqvmkrfre akiqllvatd
      301 iaargldveg ithvfnydip hdaesyihri grtgragqtg kaftfaaqrd amyleqierg
      361 ikatiakrsg kaaaergdag egaargrrgg adaeagkarg rrggad
//
LOCUS       WP_010500574             341 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Paenibacillus elgii].
ACCESSION   WP_010500574
VERSION     WP_010500574.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..341
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36355
     Region          8..333
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mnlqdyrgvw vfieqkngai apvslellga grkladkrgv plagiliggg vrplaadvia
       61 ygadtvylyd dpifhhyrte sfmravieac qkhkpeiflf gatstgkdla savatdlatg
      121 ltadttqldv daetglleas rpafggnima tilckkdrpq matvrpkvmk rlapdlkrkg
      181 diveeavsvr eedlrtkvle ivrdttqrvr ideadvivag gkglggpdgf elihrlaatl
      241 gatvgasrda veagwiehhh qvgqtgvtvt pkiyfaigis gaiqhlvgmq nsgliiaink
      301 dpaapifgsc hygivgdafv ivpllieafq kalqsevpqy g
//
LOCUS       WP_010500538             256 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Paenibacillus
            elgii].
ACCESSION   WP_010500538
VERSION     WP_010500538.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..256
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27936
     Region          1..252
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 miringihks fgsnhvlrgv dlqvqqgevv vilgpsgsgk stllrcinyl etydkgsvvi
       61 egkpigripm qgqagqsvem pqqdlnavrq dvgmvfqsfn lfphksvlhn itmapislrg
      121 mnkedaeqla rellrkvglq dkaearpssl sggqkqrvai aralamkpkv mlfdeptsal
      181 dpetvgevlq vmrtlakegm tmvivthemg fardvadrvv vidggviiee gkpseiftkp
      241 thprtqmfls qvlesk
//
LOCUS       WP_010500701             644 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010500701
VERSION     WP_010500701.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 644)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..644
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72043
     Region          <53..183
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          <116..>269
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mtlvqlagkn irknftnyfl yfasmifsiv iyftfvslky dstilatsdt spkissaftg
       61 asavlmifva ifiwysnaff trkrkkevgl ysllgvrkkq igrmlfyenl mmgllalvvg
      121 illgsllsrg fvtilmkvmg ydamanfhis pqavintivv ftvitvitsl hgyrliyrfk
      181 lielfqadke geqepkaslv mallavlfig igywlalqni lesavwrklg fmvtplvivv
      241 tviigtylly stfivyllkm arknkkrfwn gvqlistsql lyrmkgnart ltiiavlsat
      301 tltavgtays fyynnrssva ladpnsmmfi andqhianev qdrisrdqkh evvyheripa
      361 lqmkvditsl nskissdivs ytvisntafn klaelqqrkd slslqgkeaa vldagyyegl
      421 speyvgstvs lkakelaenv tftslkrynv lnlraanttv vvsdevfarl qkeaplmnle
      481 ayklthedea ksltseiqsm lpreahfssf ytdyasgmel sgliifmggf lglvflaatg
      541 siiyfkqlte anaekdryvi lhkigvnkke irksiakqil fvfalpliag iahcavalta
      601 lsrliqtnlv ipvlicigay acmyivyyfl tvntyykivt kssp
//
LOCUS       WP_010500739             158 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Gluconobacter japonicus].
ACCESSION   WP_010500739
VERSION     WP_010500739.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..158
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16517
     Region          1..146
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mttkfelngq pvsvdapddt pllwvlrdel nltgtkfgcg igecgactvh vggratrsci
       61 talssiegas ittiegldpe gnhvvqvawr dqqvpqcgyc qsgqimqaas llkdypsptd
      121 aeidgvmggs lcrcmtyiri rkaikeaaaa qqgganng
//
LOCUS       WP_010500738             140 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Paenibacillus elgii].
ACCESSION   WP_010500738
VERSION     WP_010500738.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..140
                     /product="VOC family protein"
                     /calculated_mol_wt=15476
     Region          5..136
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(5..10,26,64..65,68,84..89,91,95,124,134)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mtmqitpfim ldgqaeeair fyeqalgakv vfkqsfgqap etpgqpmpee vksriahsvl
       61 kigdaelfva dgfpgefgqr gdqlsicmts gdvetskrlf ealqqdgqvr mpleeiyfsp
      121 aygmvtdkfg vtfqiftkrp
//
LOCUS       WP_010500761             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Gluconobacter japonicus].
ACCESSION   WP_010500761
VERSION     WP_010500761.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..308
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33737
     Region          <22..308
                     /region_name="bifunc_ST_SDO"
                     /note="bifunctional sulfur transferase/dioxygenase Blh;
                     NF040641"
                     /db_xref="CDD:468609"
ORIGIN      
        1 mrdaaieaat aqirrvqnge vpspvvctff deatntashv vhcpvtrraa iidsvldyda
       61 aagrtsngsa qvivdyvrre gltvdwqlet hahadhlsaa pwlqeqlggk lgigadiirv
      121 qnvfgkifna gtrfardgsq fdrlfkdget fllgeipvtv lhvpghtpad mafvignsaf
      181 vgdtifmpdf gtaradfpgg darqlfqsir rllslppetr lflchdykap grddyawltt
      241 valerecnih vhdgisedef vsmrttrdat lampkllmps vqvnmrgghm pepeadgisy
      301 ikipvnrl
//
LOCUS       WP_010500769             217 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Gluconobacter
            japonicus].
ACCESSION   WP_010500769
VERSION     WP_010500769.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24069
     Region          35..184
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msqssslavk evfpphlgdm ragrspgrpi nlllkdtilt aiatvlteeg yqgltigkva
       61 kaagvstatv yrrwptkqam ffdairqwkt sltpdvdtgs flgdvdqlve arirflatpl
      121 grtygtllge avhnpefgtv lrevsiepar lemrrflera rqrgedgfcy paetvldmll
      181 stihframdt lwncpletea nirdikglvr cmigtrq
//
LOCUS       WP_010500821             392 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010500821
VERSION     WP_010500821.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42715
     Region          5..390
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mrttelitma lrtvlsnpmr tmltmlgvii gvssvvtlva igrgtsdqie kqyenlgtnm
       61 lvvnvlgtgr aqqldyndlm qleqlpefss iaptinkans nikydrtqek ytvtgtndry
      121 lsimkgqlet grfivdadle frnpvavlgs evsktyfgtl dptgeqinid gvvftvvgkl
      181 kskgtgaggt smdnavfvpl ttaqrtfklg nirttyidtp tkediykaqd tmkqyltykf
      241 ksdqgfnlin qdelmnarva asstltnqli svacisllvg gigimnimlv tvsertreig
      301 irksigakrr nilmqflvea tvisgiggli glllgsglal vwpminpsqt tklsmdigly
      361 aflfsvlvgv vfglypanka sklrpidalr fd
//
LOCUS       WP_010500843             246 aa            linear   BCT 01-JAN-2025
DEFINITION  creatininase family protein [Paenibacillus elgii].
ACCESSION   WP_010500843
VERSION     WP_010500843.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..246
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=26918
     Region          2..241
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mqlqyensfd vkekiaraqa ailpigavea hgphlplgtd nllaerlaak laertgsfvl
       61 ptlpygqvws lrnfpgsinv snealialls digeslfrqg frifvmlngh lgnatalkea
      121 arklaervpe lkvyyffypg vkditaqvre sssnhasyfh aceietsyml ylagehvdms
      181 raicdipdig veadctptpw etftstavlg datlatsekg railetsldv mthivndakk
      241 rhqptl
//
LOCUS       WP_010500878              89 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl carrier protein [Paenibacillus elgii].
ACCESSION   WP_010500878
VERSION     WP_010500878.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..89
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10252
     Region          1..76
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mfdtivqilc qikedpslre rlthetdlnn evgldslqml nfmvkveeel kieidydefd
       61 ylhlrsigtf idflnrcasv agayehave
//
LOCUS       WP_010500884             221 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010500884
VERSION     WP_010500884.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..221
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24594
     Region          8..221
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mpipgnfstp irlsakeral seiqrwiidg tlhpgeklld adlaealgvs rtpvrealql
       61 leaqglvelh pgketrvrli ekddilkmyp tlaslhalaa eqaaplvlpg hieqlkelna
      121 rfsdaiavgq pfqamewdeq fhnlivdiad npyiasfsas lqihirrfky vflkqpvaat
      181 qasvqehadv iqalekqdpe aaaammkqnl lrpmrelyel i
//
LOCUS       WP_010500984             234 aa            linear   BCT 01-JAN-2025
DEFINITION  pirin family protein [Gluconobacter japonicus].
ACCESSION   WP_010500984
VERSION     WP_010500984.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..234
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25668
     Region          12..234
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mldirpfssl ghanhgwlda rhhfsfagym drhrmhwgrl rvwnddrieg gtgfgahphk
       61 dmeiityvrt gaishedslg nkgrteagdv qvmsagsgit haefnketen ttlfqiwiip
      121 nepggtpgwg trpfpkdarn grfvtlasgf edddalpira earvlgatlk agetvtfetr
      181 renfsylvpa tgsleidgqt vetrdgaalt dverivitak edaeivlves gpld
//
LOCUS       WP_010500994             193 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010500994
VERSION     WP_010500994.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21950
     Region          3..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkykkptnr divlrvatdl fltkgylats mdeivveskv sktniyyhfk skdellsaiv
       61 etlvqtytgm ihdvisrknl tvqerittll hlltrqelec lggcpfltly sqmpqdahll
      121 rekisrffrd qvdlleallt egirsrqist qlparstaef ivsaveggli lqhvsqdpnv
      181 lehtlqflaf llk
//
LOCUS       WP_010501060             917 aa            linear   BCT 01-JAN-2025
DEFINITION  S-layer homology domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010501060
VERSION     WP_010501060.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Gerbino,E., Carasi,P., Mobili,P., Serradell,M.A. and
            Gomez-Zavaglia,A.
  TITLE     Role of S-layer proteins in bacteria
  JOURNAL   World J Microbiol Biotechnol 31 (12), 1877-1887 (2015)
   PUBMED   26410425
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Mesnage,S., Fontaine,T., Mignot,T., Delepierre,M., Mock,M. and
            Fouet,A.
  TITLE     Bacterial SLH domain proteins are non-covalently anchored to the
            cell surface via a conserved mechanism involving wall
            polysaccharide pyruvylation
  JOURNAL   EMBO J 19 (17), 4473-4484 (2000)
   PUBMED   10970841
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Engelhardt,H. and Peters,J.
  TITLE     Structural research on surface layers: a focus on stability,
            surface layer homology domains, and surface layer-cell wall
            interactions
  JOURNAL   J Struct Biol 124 (2-3), 276-302 (1998)
   PUBMED   10049812
REFERENCE   4  (residues 1 to 917)
  AUTHORS   Lupas,A.
  TITLE     A circular permutation event in the evolution of the SLH domain?
  JOURNAL   Mol Microbiol 20 (4), 897-898 (1996)
   PUBMED   8793886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..917
                     /product="S-layer homology domain-containing protein"
                     /GO_component="GO:0030115 - S-layer [Evidence IEA]"
                     /calculated_mol_wt=99979
     Region          49..90
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
     Region          184..226
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
ORIGIN      
        1 mksinsrqar rlaaavlals lafgspafaa aaetksnist gssvnsqrft dvgdqhwaik
       61 hvtklaslgv iegyekgeyr pensvsqqev ivmalrfmgl esevtkskag talpftvdnf
      121 fkpyvayaid rgliniqeet adgtnaktaw gskeasrewv aklviraigk qelanqqaqs
      181 sssftdnkdf sswasgyina avslkivqgf ednsfkpkdk vtraqmatfl sradkeatsr
      241 ssrvvtgyvm eitdrkisil nakgetteyt lssdtalysg kddsrislsn ikltnevylv
      301 qnqgaalyie ltndqqkmet yegtlaeift drmmasiqrn gknelydlfp tvtvtdkdgr
      361 glslssltpg sivelkkntl lkeskisqiv lkqtpvskts egtvlslnkd snqvtfleqg
      421 tgqnesftlt artvvklqdg tttdlsklrv gdavsyevka nelqvvsvkk padfsqsveg
      481 tmaslssdkr iltinkaggs lgayhiadna iimidgltnp slfdiesgdq lkmdlvndki
      541 vkvsvtsrsv kqfvyatils fdanskvvti stesdgvgay rltdnttirf mggpvqqsnf
      601 qstfigngnd kkrvdlkvsk dkivqiestm nvegtiaqin tsnitndlti rtaggqnltf
      661 kvnygapvem fnktngtisd lkvgdairlt ltgnqdfvtn lmakkkgvyk vlvtnsstnq
      721 vtakdetgsq ltfkvenndq iinpgkqsha fsdilideyv kasfsgtkld nlqllnsvrg
      781 kvtnvdvaag tltvqdfqgn iqvitvgqqf tirqnantsa alntikqndr veiirdandk
      841 aiiqvatatk rtvssydtvl nqlllkptan sdktsynlfa kaylhkgtqt vapstfmene
      901 evmvyviddk ifeiekp
//
LOCUS       WP_010501146             221 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010501146
VERSION     WP_010501146.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..221
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25008
     Region          1..221
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mpipkdyltp vrlsakdktl aqlqkwiieg tmqpdeklnd aeisaalgvs rtpvrealqi
       61 lemqglvqmf pgkdtrvtti dkanilklyp tlaalhalaa etaarliqpe qvqqlhelnd
      121 sfakyvednd lyqaveydek fhnmivdisd npyivcfsss lqmhirryky iflkrplges
      181 qaaaqehrei igaleahdse gaahfmkknl lrpleqiqqi l
//
LOCUS       WP_010501197             381 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Gluconobacter japonicus].
ACCESSION   WP_010501197
VERSION     WP_010501197.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..381
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40687
     Region          102..381
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          272..380
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(276..277,310..311,314,324..325,328,370,374)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mrlrtallam tsmvaapsla mastvtgpyv nigggynlvq nqhasfsptt qadgstsnag
       61 sssqfrhkdg ftgfgafgwg fgnglrveve gvynysqinh rnktaatgst kgsdqayggf
      121 vnvlydidla hfglnvpvtp fvgvgagylw qhynpittny sngavnrvgg tqgsfayqgi
      181 vgaaydipgv pglavtteyr figqqfadga yrstswnrng sglhkgnvnf dprfshqfil
      241 glryafdtap pppppapvvv ppaptparty lvffdwdksd ltgrareiva qaaqasthvq
      301 ttrievngyt dnsaahpgpr gerynmglsl rraqsvkael irdgvpaaav dihgygeskp
      361 lvptgpntre pqnrrveiil k
//
LOCUS       WP_010501220             140 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Paenibacillus elgii].
ACCESSION   WP_010501220
VERSION     WP_010501220.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 140)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..140
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15710
     Region          8..114
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cd02883"
                     /db_xref="CDD:467528"
ORIGIN      
        1 mfivnvegav crddqwlvit rsmkeehagg tlslvggkve vegntldile rtvkrelyee
       61 igieikdpvt fvysssfvte dgynvinvvy lceydsgtah rkspdeveav hwmtyeeimn
      121 hskappwtke svkraaaark
//
LOCUS       WP_010501520             579 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Paenibacillus elgii].
ACCESSION   WP_010501520
VERSION     WP_010501520.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..579
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66291
     Region          4..519
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mikverlsfs fpqkelynni sftldeaqhc afigtsgsgk stlidilmdp erylfdgkle
       61 idpdctigyv sqfseldntk ettvfeyige qfikiqneiq sictemetss diepllekyq
      121 laldafdamg gndfesnihk qlslanlmkr rdlkvtdlsg gefkliqvik emlnrpdlmi
      181 mdepdvfldf enlnalkkli nshkgmllvv thsryllnhc fnkiihlenm eiqefdgryi
      241 eynfsllqtk ielqelavae heeierneni innlraiatn nseasrgrtl karvkfherl
      301 earrikapfv dikqpnisfg idneiedtiv vnvnnysvgf dellldnvnf eikstdkvai
      361 igsngtgktt llreifknnh dsieinadvk vaylsqlqge mlkdsntile efidagfkty
      421 deirlylsny gfegeivsqk ieslsggekn ilqlakvsas kanvllldep tshldtytqi
      481 alekaikefk gailmishdf ysvvngmdyv liiddktirk msmpkfrrmi yashfdrdyl
      541 eteqkkksve mkielalkdt dferakglid eleelikll
//
LOCUS       WP_010501548             523 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Paenibacillus elgii].
ACCESSION   WP_010501548
VERSION     WP_010501548.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..523
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57398
     Region          <214..309
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
     Region          267..307
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          321..395
                     /region_name="G5"
                     /note="G5 domain; pfam07501"
                     /db_xref="CDD:462185"
     Region          361..523
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mkffkgadrl kglldklrat rsadrsnnld egvkpaamse vpgatalerm knriilhkwm
       61 viksvsalgl maavvvsghe lveanmndyy qvyangdlig ivsdpskvee ykqkkreqls
      121 kneadlrmvv tepkleltpe rvfshnvndq avldklggyf ssypvgvqlv vdgkpmgivk
      181 deataktvld qiknnaiasm qtkkmsgrvs ilsaspatst paqtelqkad fvqkvdlqev
      241 kiepkqlvnp edlrkkletg dvqptkytve kgdcvsciak kldipkqviy qnnptisddm
      301 ikvgqqldlt vlkptlavrt vekvvenqei ayetevkqdd nmrlgesevl spgknglkkm
      361 tyqltkvngl leaetvlsee vvqqpvkavv kkgtkvikge gtgkfawpvl sasisstfgt
      421 rwgafhkgvd ltgnrnimas dngkvvfage ksgygnciii dhmngyrtly ghlnqintsv
      481 gkivekgdki gymgstgdst gvhlhfevqk netpdnplky lnq
//
LOCUS       WP_010501527             395 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Gluconobacter
            japonicus].
ACCESSION   WP_010501527
VERSION     WP_010501527.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..395
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44172
     Region          113..348
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mtqhfvstlf avrsyftwlp apvvsvlmla vvgilafycg nlvtsltlri pgsrsaalir
       61 kivaalrrpt rimvallaml galpaatgfs yeteqdlklf flfllvltfg fsaiivfrim
      121 teaylnrlss reqtddimir thqtqirvlr rlteimvgiv tvasalmlfp svkqygvslf
      181 asagaasliv glsarglltn liagvqiavt qpirmedlvi ingdwcwvee inatyvvlrv
      241 wdwrrhivpi syflenqfen wthnsaaiig vvflwldyea pmdkvremln eiirtcplwn
      301 gkvfdvqvad cnaqvmsiri iasarnalqs wdlrcdirek iiarireecp ealprarfam
      361 mpprpgedaw psellspkid rpppgsymgp gtpga
//
LOCUS       WP_010501590             226 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase, partial [Paenibacillus elgii].
ACCESSION   WP_010501590
VERSION     WP_010501590.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..>226
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          3..200
                     /region_name="TTHA0252-CPSF-like_MBL-fold"
                     /note="Thermus thermophilus TTHA0252 and related cleavage
                     and polyadenylation specificity factors; MBL-fold
                     metallo-hydrolase domain; cd16295"
                     /db_xref="CDD:293853"
     Site            order(12,58,60,62..63,147,168)
                     /site_type="active"
                     /db_xref="CDD:293853"
     Site            order(131..133,139,155,157,162,192)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:293853"
ORIGIN      
        1 mqldiwggag ehgrscyllh ndrigvlldc gvkktgagqy plvdpnvipr lnavflshah
       61 edhsmalpll ykhgyrgvvw ttrataqqld tyfaswkkyv rgqsaelpyg dehveairfa
      121 yledagasge widaarhvkv cwgrsghlvg svwlmleleg krvffsgdys sesvllaadg
      181 pealppgaas qpadlavida acgmdaeaqp vllerlaari gqalaq
//
LOCUS       WP_010501746             166 aa            linear   BCT 01-JAN-2025
DEFINITION  DinB family protein [Paenibacillus elgii].
ACCESSION   WP_010501746
VERSION     WP_010501746.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..166
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18408
     Region          8..148
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 mfiktgdfia ewqqeaaatq rimdaltdea ldqavtpdhr tlgqlawhlt ttvhemlsrt
       61 glefasagdd qhapdsaavi aeayrnasqa asnavqtqwt daklaettdm ygdtwpnglt
      121 lriliqhqih hrgqmtvlmr qaglrvpdiy gptredwler gmqplv
//
LOCUS       WP_010501896             443 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Gluconobacter japonicus].
ACCESSION   WP_010501896
VERSION     WP_010501896.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..443
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46105
     Region          1..440
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mlstldrwfh isargstvpr eivagltvfg amayivavnp silsaagldr hdmvmttiag
       61 avagtllmal warlpialap amssnvlfaq vvvqqahvsp rtaftvvlfs glcftalsls
      121 qirqriirgf ppsivlgiqv algafiarig lttggiavpt aqgltfgsls dpsvllsmag
      181 vllcavlvvm rvpaglllai stltvaglfi htdkgtittl pahavdwphy ptnlflpfdf
      241 agffshlgll ipitlyflis dffdatatmm svahragldg tpekpaldhr afasdgaasi
      301 igaslgtctv sayveslagv eaggrtglsa lvvallfavs svfwplitai paiatapvlv
      361 lvglnmlgsl hrvadnpsda ippltmllia gvtgnfmlsl scglllytgl alalrdfkrl
      421 tpivlgldaa flfymvlqsh mgs
//
LOCUS       WP_010501981             451 aa            linear   BCT 01-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Paenibacillus elgii].
ACCESSION   WP_010501981
VERSION     WP_010501981.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..451
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48523
     Region          36..450
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mskvqsalas pevagsrgrg agaddrgqsk fremvthrkk gwrrilwliw almgpgliaa
       61 ianndaggai syaitgatfg iglfvplvlc lapltftiqe msmrlsavtq egfarlalrr
      121 ygkfwgyyhi stlafenlli litefigmta glvllglplw lssvlclllv vgfvlftgyw
      181 tkerialflg vlnviflvva gmthpsmaai ghafaawnvp aelqdgvmwf viatvgnava
      241 pwmiffqgsg tvdkgvtake lrlgridtal giviqviiaa giiiagaalh ghvqnindag
      301 padmisafnd vagrwpailf glglfnagfl asitvslsss wsiaelfgws kslndkisqa
      361 pkfyavyigs lvlaaiaili pnlplnyfsv iaqviggilm lpllifmllm tsdkklmgey
      421 rtkrfgkicg wamvtllvgl tlasfwntfi q
//
LOCUS       WP_010502047             111 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Gluconobacter japonicus].
ACCESSION   WP_010502047
VERSION     WP_010502047.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..111
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11907
     Region          35..111
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mysfilaaat glmlagspnl pensdlqqkp gagtpeypid afehgetakt evscdiseag
       61 tpsnchiaks nnphfnasal efvqrmryvp arrngkniav pnhiehvdft i
//
LOCUS       WP_010502098             247 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010502098
VERSION     WP_010502098.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..247
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27012
     Region          7..246
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 medgkltvra veraldillc fteaedlnlt eisarvglhk stvhrllasl egkgfiirdp
       61 aseryrlgfr iwelsanlth sddpalivlp emerlrdqvg etvslyvrdg mervrvqavq
      121 snqairrvap igarlplsvg assktlvafa dpdeqqqllr dpswptavsp aaylqqleev
      181 ktlgyatsve erepgaaava apifgraqrl vaalavsgpa nrltlkkmke hapalmeaar
      241 rmgkmlk
//
LOCUS       WP_010502107             286 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Paenibacillus elgii].
ACCESSION   WP_010502107
VERSION     WP_010502107.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..286
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30485
     Region          16..267
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(44,49,55,78..79,105..110,232..233)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(48,50,111..112,114..119,171..173,175,177..178,
                     186..187,190,193..194,197,201..207,215,219..222)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 mtnsnipsfa vgsksftava iniaskagew iqsklgdfnk lqtkysshdl vtevdkgaet
       61 mirnliqthf phhvvlgeeg vapgpdaskr aleqlsdaey lwivdpldgt tnfvhgfpff
      121 sislalahkg evivgvvynp vhnelyvaek gkgaylkgkr mqvssetkli dslvatgfpa
      181 dragalpvnm rgvqalapkv rnlrvagsaa lhmayvaagr lsgfweigln swdmaagall
      241 isesggkvtd tegkpyslhv rdvlatnghi hdeirqelsa asaigi
//
LOCUS       WP_010502351             349 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Paenibacillus elgii].
ACCESSION   WP_010502351
VERSION     WP_010502351.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..349
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38691
     Region          7..321
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkneelfdvt iigggpaglf asfysglrem ktklieyqpr lggkvhvype kmiwdvgglt
       61 ptlgeklieq lvqqgltfdp tmvlnqkver iergengvfv lhtstgeqhy tktvilaigg
      121 gilepqridl egaekfevsn lsytvkslrr fkdktviisg ggnsavdwan elepiakqvy
      181 ltyrkdtlsg heaqvkqlln ssakcffhtt itkliaasnq ekierveltn hetgevqeli
      241 ldeviinhgy erdrsllens evklemaney flagetnsat sepgiyaagd iisyegkvhl
      301 iagafhdaan avnqaklyiq peahasgmvs shneifqsrn relikqlik
//
LOCUS       WP_010502456             312 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Gluconobacter japonicus].
ACCESSION   WP_010502456
VERSION     WP_010502456.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..312
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35250
     Region          <16..293
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mseditdrsd dgrknsrglf glfgrrgrdq glresiatlv qeaaqpveet gdepeldrqe
       61 ralimnvlrl rditaddvmi pradiiampe sisfndaldh mrrenhsrmp vyrgqlddia
      121 gmihvkdlva yvddpeafdi rpllrqplmi aptipvldll lqmrqrrmhm alvideygsi
      181 dglvtiedli etivgdisde hddpvttpwv erpdgsfdid arlpvrqlee rlgavltdae
      241 reaeietvgg lvfrmaehvp ardevlthds glefrvldad arhiralrmr vpegwekkpl
      301 pdtgqqdder gs
//
LOCUS       WP_010502519             262 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Gluconobacter japonicus].
ACCESSION   WP_010502519
VERSION     WP_010502519.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..262
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27063
     Region          9..259
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 msfdpvavrl eaarsvvrda aqlalsmrpa pggptgtlkg rqdylteadg avealvskri
       61 qdlfpedgfq geeggvtrqg qfrwvvdpid gtsnfargrd rwcvslgllk gdepvagiie
      121 apalgevfta qkgkgaflng kpikaspisn pqeamiemgw scrvstelfg ekigaimalg
      181 amprsggsga laltdvacgr sdgyleiviq lwdvaaalii leeagaavsp flqtggltgg
      241 atilaaapgi akvlsdavqv ei
//
LOCUS       WP_010502524             317 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010502524
VERSION     WP_010502524.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..317
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35189
     Region          43..193
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <208..304
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msmqethslp tesqnkkgle tetarlarli dtytphdgif rqripgltlv rfsststgsk
       61 tfytpsfgiv aqgaisftvg qevyvsakpr ifmlpvalpl tlrilqgsps epflkaglsl
      121 dpkrigelal kmfprglppi rqrsagygfe adldfvsami rlidylgnpg daewlaplam
      181 dellirllrs pigvyvaemg fadsgvqrvs kaiewlrrnf aeamkveela glvhmsvsrf
      241 rehfkavtam splqyqktlr lqearrlmav shldaaaacq lvgyasasqf srdysrffgs
      301 ppgrdiarlr qqepfee
//
LOCUS       WP_010502533             258 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Paenibacillus
            elgii].
ACCESSION   WP_010502533
VERSION     WP_010502533.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..258
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29416
     Region          1..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mfqeerliai vqklnekqri tvteicewlq iswdtarrdl ikleeqgsii rtrggamlpt
       61 iskevpnyeq rlqldtpskq aigrlaatli hdgdylytds sttvryamea mrtrrnvvvt
      121 nsidlagmlt qkdeirihll gglldneqrl vygartleml seyqvdkall gtcgitphgl
      181 ttmfeeesyl irqvmrksdq vivladhtkf gkklfhrvag legidmivtd repsdemkee
      241 lhkhqvelli asegehhd
//
LOCUS       WP_010502561             254 aa            linear   BCT 01-JAN-2025
DEFINITION  lipase family protein [Paenibacillus elgii].
ACCESSION   WP_010502561
VERSION     WP_010502561.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wong,H. and Schotz,M.C.
  TITLE     The lipase gene family
  JOURNAL   J Lipid Res 43 (7), 993-999 (2002)
   PUBMED   12091482
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Cygler,M. and Schrag,J.D.
  TITLE     Structure as basis for understanding interfacial properties of
            lipases
  JOURNAL   Methods Enzymol 284, 3-27 (1997)
   PUBMED   9379943
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..254
                     /product="lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=28709
     Region          44..>224
                     /region_name="Lip2"
                     /note="Predicted lipase [Lipid transport and metabolism];
                     COG3675"
                     /db_xref="CDD:442891"
ORIGIN      
        1 mtiasnraiq laaivyqair qynnngkfel ppgyklaavl gskevpylgf ilesrksivi
       61 alrgtaavsd lkrdlqfdqi pfpfvrnagl thrgftelya salrepimsy lnkaspkkrl
      121 ylaghsiggs lvtlcaldlv yhtpfkqpvv ytfgapkvgn pdfvrrfnrr ikhsthianr
      181 ydlvpllpps fdktvyrhvr yryvirfqnk glrgshsiks yykelvrrra grsrpyyngs
      241 pkgllpapsv rlar
//
LOCUS       WP_010502565             191 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010502565
VERSION     WP_010502565.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..191
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23057
     Region          1..92
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mlelfilgel tgapmhgyll htilngiigp trkiswgvly plihslladg lieqvpdeqq
       61 egerqgrgkk kkmyritedg rrrffrlmee plpyspdyel qfyakfsnfd misrelqfli
      121 lhqykdylrf elrheeerve yvskdemmpd eerqynliwf rhrldklryd eewvlqlinn
      181 lrmngegler k
//
LOCUS       WP_010502642             584 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Paenibacillus elgii].
ACCESSION   WP_010502642
VERSION     WP_010502642.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 584)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 584)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..584
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=65701
     Region          209..571
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mtgkptiftk vlvlialllt pvlflyiytn qvsvnvvree iqssslnrls fflqqfdstv
       61 eqlamfpvil nsdpylrefi drrsdkpydk lkeqtrlmqk islqsvsaaw tndltvylpk
      121 dqivissnif ksydpgdiek faplkswtyd gtvrgdartp garftrqivd plgatdpsai
      181 qamiqvsfpv anisamldqv ktggkgdpfl yrsgfspigs atlndgsvqa ivrmldgqsl
      241 eesghfvatv agrqvavyyv ksrqldwylv dyvpvdsila pirktnllfy aalglllgms
      301 flaayllyrn vqkpigklln gvrllkkgdl sariryrpnn efdflidrfn emaeqiqdlv
      361 qrvyaekirl heatlkqlqa qinphflyns lffivntaml edtrsvvama hnlaeyyryt
      421 trmenraaal geemklvdny ltihnlrlgr lrceldvpet mlelhiprll lqpivenaiv
      481 hgienkrgea virvsgsmce gtyrivvddn glgmtdeaia rmeqqlalpq evasgfgmwn
      541 vhqrlryvfg egaglklshs plgglrvtlt wgrdsehgsa idrg
//
LOCUS       WP_010502663             317 aa            linear   BCT 01-JAN-2025
DEFINITION  S-layer homology domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010502663
VERSION     WP_010502663.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Gerbino,E., Carasi,P., Mobili,P., Serradell,M.A. and
            Gomez-Zavaglia,A.
  TITLE     Role of S-layer proteins in bacteria
  JOURNAL   World J Microbiol Biotechnol 31 (12), 1877-1887 (2015)
   PUBMED   26410425
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Mesnage,S., Fontaine,T., Mignot,T., Delepierre,M., Mock,M. and
            Fouet,A.
  TITLE     Bacterial SLH domain proteins are non-covalently anchored to the
            cell surface via a conserved mechanism involving wall
            polysaccharide pyruvylation
  JOURNAL   EMBO J 19 (17), 4473-4484 (2000)
   PUBMED   10970841
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Engelhardt,H. and Peters,J.
  TITLE     Structural research on surface layers: a focus on stability,
            surface layer homology domains, and surface layer-cell wall
            interactions
  JOURNAL   J Struct Biol 124 (2-3), 276-302 (1998)
   PUBMED   10049812
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Lupas,A.
  TITLE     A circular permutation event in the evolution of the SLH domain?
  JOURNAL   Mol Microbiol 20 (4), 897-898 (1996)
   PUBMED   8793886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..317
                     /product="S-layer homology domain-containing protein"
                     /GO_component="GO:0030115 - S-layer [Evidence IEA]"
                     /calculated_mol_wt=35684
     Region          32..73
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
ORIGIN      
        1 mkikkkillt aglsiallgv qsgpsyaess lfkdvpvtfw gyksikwsvd nkivdgypdg
       61 tfkpgqpvkr defiamlira yqpsdlkfsd dsagwaapyl nywtklgwea gantalsrge
      121 vaqilshaag knytiddsvn yvldtgiaqg kedksfegfk kddsvnraea vafierlkqy
      181 naklepkggg ptiaytntkh hftvqvpaqw egkynvetet ykdsameayh fynkanreyg
      241 gliftisvwp kdkwneesee iskiiriskv gergdrvftl sfpsdvqyrp ddeklkaayl
      301 smyedvknql vvfkldk
//
LOCUS       WP_010502689             289 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Paenibacillus elgii].
ACCESSION   WP_010502689
VERSION     WP_010502689.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..289
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31219
     Region          1..285
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mevsfiglgn mgfpmaqnll qagyeliifn rtpekaeplm hqgaryagtp leaakesnlv
       61 itmlsddaal eevvmgpngi lnglpekgih isastisvdl arklstshae rkqyfvsatv
      121 lgrpdaakaa klrillagpe qarqraipvl aamgqeifei gdhgeegnvv kigvnflias
      181 mlealseaql mvekygvepa rfmdvvnalf qspvyqnyga imteqrfepa gfkmklglkd
      241 velaikaaqs vhaplplgql iqnhfsvgma qgygemdwta lirclehss
//
LOCUS       WP_010502836             415 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Paenibacillus elgii].
ACCESSION   WP_010502836
VERSION     WP_010502836.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..415
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=45278
     Region          218..411
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mlrinkkgsy vydaygklia pgemyetfdp edpvtsprdv ltrsiqavat rgshlcngly
       61 ptkpedpvit vqtsrtyhef tedmaeiavv fgnyydqdvs tpnpisvrss ieypigntkr
      121 iplytmsgsr tfaldpgakq msdmasvngk kgtgfymytg ilipdggkfp rglvaynsrg
      181 egmknadivd sgtpdthgqf vyhpiaiigp snvpgniiva dsigqgagdt pqdrgfiaag
      241 lgtdfpwirv akggessydf rangkamfrv gllkygrraf vhygtndlmg ksfdqfkadi
      301 tatwqllkdf gieeiyqfti pprttstdaw attenqaavn tkfakgadrd qanawllsnp
      361 apglltgsid tasavqhpkd askwdagttk dgvhpseagh ermrqkfsey llrfk
//
LOCUS       WP_010502845             226 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Paenibacillus elgii].
ACCESSION   WP_010502845
VERSION     WP_010502845.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..226
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24545
     Region          <8..137
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 msvfdgwkvt spygyrsdpf tgsqvfhtgi dlvkyhkypi pafvggvvlf agegvagtgf
       61 ggygnvvalr ddagyvhcyc hldsvaaakg qtlskgdivg nqgttgrstg shlhyevrak
      121 dapsygygsh vdpgeylesi qtlpteeded nmaikaenwf wkqaynilgk aynegkidwq
      181 wcqkvldrtl saweyahvla vieartkgvd vdsenpaavg pdqrgk
//
LOCUS       WP_010502863             380 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Gluconobacter japonicus].
ACCESSION   WP_010502863
VERSION     WP_010502863.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..380
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39487
     Region          22..368
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mpisfsdpkd rdekeprare lsriagllri alavtlilla vwlmkdvlav vfasalmavv
       61 lhglarmvrr hitfipyqaa valvtviill avaglvwssg paigdqfirl kqalvqqsgd
      121 lkshlsgstl gqmvldhlpt avggndatsg slgslgsgla gsvtgilssa fgvlgtlavi
      181 liaglyfals paiyidgflr lfptqhrsaa rtllmaagtt lwawtagqal dmlvvgilsg
      241 iglsligvpl alalgvvagl cnfipyigai lgavpaillg lsmgtkealf vailysviqf
      301 fegnvlapli qrravhmppa vailsqtvfs tilgipglil aspitaalla mgdkataple
      361 dedqtkrdvg eiseteahke
//
LOCUS       WP_010502878             139 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010502878
VERSION     WP_010502878.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10644999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..139
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=16146
     Region          86..>127
                     /region_name="CbpA"
                     /note="Curved DNA-binding protein CbpA, contains a
                     DnaJ-like domain [Transcription]; COG2214"
                     /db_xref="CDD:441816"
ORIGIN      
        1 myndlmdeye llfqqfeydf legqlpveqe plervlndve ygfqdlynra parektnynr
       61 fygdsssfsk gsgyrqgeas fqtmigvseg asrdeirrqs rrllkklhpd rggsaylfnw
      121 vkkaydvnes nkptnsvle
//
LOCUS       WP_010502921             115 aa            linear   BCT 01-JAN-2025
DEFINITION  ester cyclase [Paenibacillus elgii].
ACCESSION   WP_010502921
VERSION     WP_010502921.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..115
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12776
     Region          11..114
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mktveqknie ivtafieate nrseldrteq ffaeqlgeaf adrhyaidei laqgekvtar
       61 iaitgthqga fagkaptgrs vkitqfrefr vvdgqivehr gwfdtgtllp qlqan
//
LOCUS       WP_010503054             185 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Paenibacillus elgii].
ACCESSION   WP_010503054
VERSION     WP_010503054.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..185
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21224
     Region          3..179
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mkrriildla vtldgfiegk ngevdwcimd semgfnhfln qidaifygrk sydlwgqftp
       61 eieptdseke fwelvhskek yvfsrtqkgt dnkavfindn ileevnkikn kpgkdiwlyg
      121 gaslittfin lglvdefrls vhpvvlgegk plfddikqrl nlkmvntrtf ssgvvqliyh
      181 fdank
//
LOCUS       WP_010503152             260 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Gluconobacter japonicus].
ACCESSION   WP_010503152
VERSION     WP_010503152.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..260
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28612
     Region          2..257
                     /region_name="COG4798"
                     /note="Predicted methyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443826"
ORIGIN      
        1 mlskyaflcl fplltvtsal agptldqavh spkrtpafva rdavrhpiee ltffglkpda
       61 hvleiwpsgg ywtqilapyl ydhgtytval gpadlkkqai sklqserpdi ygrirttqfd
      121 gqhldfapan svdlvltfrn mhnwmeagna pemlaaihrv lkpggilgie dhrgnttapq
      181 dpmakdgyvr qsyaidliqk agfklvgsse inanpkdtan wpkgiwtlpp tyalgatdha
      241 kyeaigegdn fvlkfqkvkd
//
LOCUS       WP_010503231             450 aa            linear   BCT 01-JAN-2025
DEFINITION  inorganic phosphate transporter [Gluconobacter japonicus].
ACCESSION   WP_010503231
VERSION     WP_010503231.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10475700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..450
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47969
     Region          30..442
                     /region_name="PHO4"
                     /note="Phosphate transporter family; pfam01384"
                     /db_xref="CDD:460184"
ORIGIN      
        1 mlhfapesiw siialglcfl lvcvfefang fhdtanavat viytnslkpk vavvwsglmn
       61 llgvllggia vaytlvellp pdvlsppngn pavpmlvslf gtalawnllt wwfgipnsss
      121 hcvigslvgi aigdsflhar dlghsvdwnq iwkvlttlav spplgfigag ilfllirkfv
      181 hlpalyqrpe phhkpnpivr allittctlv sfshgnndgq ksiglimlti iglmpaafal
      241 npqvpvqydv irqdvqaarp lvaefdrysf kadamasidr lekgaeihas paetrgdiyq
      301 vlsglrsvts npaasdkqkk eaaslakklr ptveyapfwv rllsalclgi gtmigyrriv
      361 qtlgegigka hlnpaqgaas evvgaglimt agytglpvst thiitsgvag tmvasgsgin
      421 mhmltkiala wlftlpvtit vsallfyila
//
LOCUS       WP_010503341             430 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Gluconobacter japonicus].
ACCESSION   WP_010503341
VERSION     WP_010503341.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=46730
     Region          7..412
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mkpqseiliv gggvaglsla aslgktlgkr rkaritlidk sfshvwkpml hcfaagtvan
       61 endrisfitq asehhfefwp gevvsidren rqvvlspfha sdgslvlesr tirydtiila
      121 igscandfgt pgvkqhclci dnlveanvfn ekfrmelmra fahgseldia ivgggatgtq
      181 laaelhkald ivdpyslhaf gktppklrvt llqsgprilp afpeavslaa qqelerlgvt
      241 vrtsarvaaa dstgfilkdg thipaklrvw aagvkapevt qtygnlslnp tgqilthsnl
      301 csidddrifa vgdcsfikdd plpataqvar qqalhlarhl pafvergvkv pgcvfknkga
      361 ivalgkyngw atlpggtvwg ggffhgfsar mahlflyrrh qielfgfyrg lislysdwie
      421 tfvrpsvrld
//
LOCUS       WP_010503358             258 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Paenibacillus elgii].
ACCESSION   WP_010503358
VERSION     WP_010503358.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..258
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=29478
     Region          1..>245
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mnvigyvrvs tagqardgys lsyqreeiea ycqqqgwnll hvfvdegisg akvdedalev
       61 dregfqnmls llstrcidhv vvlntnrlwr sdivkvlvhr efkkynvnvk sieqptysiy
      121 kkdpsdflin glmelldayq rleiamklgk grnkkakegg yaggratfgy kakkgskvlv
      181 ideqqavive rvfelkelfp qwtlseiayq lnlenyktqq gkaftkvqvk rildrrsfys
      241 gmyqyanvea igkhqaii
//
LOCUS       WP_010503564             404 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010503564
VERSION     WP_010503564.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..404
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43470
     Region          18..235
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          140..403
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 msllhmawrn lmnrrvqtli tiivvsigva mtlsimmlsa gikqgivkas epfgmivgsk
       61 gsanqlvfnt iflmdnplan isldyyhtle ndprvtqtvp falgdnfkgf rlvgttpsff
      121 alkgkpsdpp yfqladgrlf dkpfeavlga kvaketglkv gdrlvsghgv akslqhdegh
      181 kdhpytvvgi lhsvsapsdq giyvsmdsyw ishehpgeqk heedehgvta alvkprsyvd
      241 lmkmyqeinq gkeaqavfpg qviakifdmm gsgeqilkyi syvvlgmagl tvvlalygst
      301 verrrtvail raigasrsav vtivllesvl vvvfgcvlgt algggltwll sdyigsqisv
      361 tvavayswdv aaviggvall gmiagilpav sayrtetary lhta
//
LOCUS       WP_010503574             219 aa            linear   BCT 01-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Paenibacillus elgii].
ACCESSION   WP_010503574
VERSION     WP_010503574.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..219
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=24017
     Region          15..125
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 midlskikni klnppassdv ieavedelmv kfpnvykell kktngfqtde gvviygtedl
       61 iernltweve eyakgfvaig dnsggtvylm aeelgatell avdsgdmnpd natmitsdfi
      121 qwlssgcrha gqdfvndkqs ftqlhdiili nkpsndikdv lqikkilgvn mstsellkgv
      181 ktppfvlirg vpygkaikcl eelgdlskvl kllpsnvdv
//
LOCUS       WP_010503630             847 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paenibacillus elgii].
ACCESSION   WP_010503630
VERSION     WP_010503630.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 847)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..847
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94254
     Region          135..408
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          599..845
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mikvrnkkai rnlsdksfkm nkthnliaif aialtallft tlftmalgav envqrttmrq
       61 aggdghgvlk yvtdeefdhv kdhplikeia ydrslsdkvt nreffkrrae fryrddvglk
      121 lgfielaggh kpvkenevia dsitlqllgv pqevgapltl kldirgkevq rdfvlsgwwk
      181 sdpvfksgqi fasrayvdvh apelqntyke dhvitgiina yimfnnsmdl egklnkvite
      241 sgysldkdsa nyiasnvnws ylttnfsmga gtilaltsal llitftgyli iynifqisvt
      301 rdirfygllk tigttgkqir hiirrqalil siigipigli agffvgkwlv plmmhtmnst
      361 ieentvsvsl spwifigsal falitvlist fkpgriaaav spieavkytd gnpknrvklk
      421 kstggakmpr malsnlgrnk krsvlvvisl slslillnta ftlsrsvdmd kflskvhdtd
      481 fliahadyfq edftgsenat sesyiqvvqa qpgfekggrl ygganlftle vskpkknfsv
      541 tdavgnfpsn vygleelplh rlqridgeld fdklatgkyi leglesddhg npymenaifk
      601 vgekvtlhry mdtaeahlnk annpneftvl ghvavkrtns gisaasyttf ylpadiykpl
      661 vekpvvmsya fnesddqvea merflesyte ttepvmnyds ksiamnelsg mkntigmigg
      721 tlsviiglig ilnfvnavlt siltrrrefa mlqsigmtqk qlrsilvyeg lyyvigtslf
      781 sillgsvfsi tivrpicnii wflgyqfiiw pllavlpfll vlgiviplaa ystttkqsiv
      841 erlreae
//
LOCUS       WP_010503640             156 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase, partial [Paenibacillus elgii].
ACCESSION   WP_010503640
VERSION     WP_010503640.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 156)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         <1..156
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <7..156
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 qifakcsnik spalsaliqa kitqalkkri tldhhiinme qlslgaikst dlvkiisnli
       61 dnafeavetl peneryveln gcikqdklyf svyntgtpip seqigkmfek gfstkknsnn
      121 sglglfivqr iikqykgkil vmpmqegnkf eiiipl
//
LOCUS       WP_010503847             729 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Paenibacillus elgii].
ACCESSION   WP_010503847
VERSION     WP_010503847.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 729)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 729)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 729)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..729
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=83727
     Region          244..706
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          493..707
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 matklkskym pafvkvllii caalvlllai diakkrdyiy gnpffqsdlf ysvqvldavk
       61 eitsyyvehg edekkigmek kkvseetvqq wreefealal drmtperpdq plmasegvpl
      121 ytlqekefae wskqfenawq ryllenttky ieerksdyhn lkntvarldp lvkytitdkk
      181 nhktytnrta spdgelkteq dsetthtitl plqqpvkqlh wadnyfkqnq legkftfyat
      241 aepnmafate avafkdyitl igirkqlhye fagfaagsav livlfaymrk krekekiwgg
      301 tlttawqrlp idirmlvlll flitvfgygr tiydwripfs fayrwvllaa llsfigigln
      361 dalrlyrtkg afgeqwkkgy iltlnkllka altnkillfk svliflstvl lglflfaawk
      421 esgiwpilsf myalaylfia vpylakrvgt lnhmltgmne isagrfnfaf eengtgelsq
      481 mvrqlqsmkq gfqaaldvel rserlkseli tnvshdlktp ltsminyvdl lkkesplpge
      541 sdhyvqvlek ktnrlkmlie dlfevsqlss gtvvldletv nvsallqqal aelndkiets
      601 klhfrvhieh phifarldgk ktwrvfenli qnalhysmpe trvhlsltee qehtvlrisn
      661 vsayeiqfda eelferfkrg dssrhtegsg lglaiaksiv elqggrllia ieadyfkvtv
      721 ifnkqaedc
//
LOCUS       WP_010504041             434 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Gluconobacter japonicus].
ACCESSION   WP_010504041
VERSION     WP_010504041.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..434
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46552
     Region          1..382
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtsfaelnla epiqkalaee gyttptpiqa gaiphllegr dllglaqtgt gktaafalpi
       61 ldyllrnrrp papktvrvlv laptrelasq idesfgayar hmklshavvf ggvgqgrqie
      121 atrrgvdvlv aapgrlldlv gqgyidlsal evlvldeadr mldmgfvrdi rrimallper
      181 rqtvlfsatm pqsisdlahs llsdpatvqv tpesstvdri rqavmfvese kkkdatlmlv
      241 essnvvravv ftlmkheank vaeflnkngi taeaihgnks qgareramsg frngtvkvlv
      301 atdiaargid vddvshvfny dlpnvpesyv hrigrtarag rdgwavslcd aeqrawlkdi
      361 ekkidkaipv vtdhpyhsda aqnstmrppv lgggrgggqr gggnggggrr rsgppssvrg
      421 sagrrggars agqr
//
LOCUS       WP_010504044             279 aa            linear   BCT 01-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010504044
VERSION     WP_010504044.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..279
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32068
     Region          <66..189
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mvnfymwdgn tilhewktek aknkpgltse qlrqalhfds litwvfedgt fhplakftse
       61 ssygivsdyl gtpiemydet gekvwscdld iygkvqrqdl tgnrcacpfr ypgqyedeet
      121 glyynrfryy sphegmytqq dpiglagnnp tlygyvhdpl twidpwglin lnsnnakgkf
      181 gvykieikge lhkygkadls rvtqetglpt rlhqqvrklk eifgrknvig eviekgyett
      241 kkakaaetak lneyyeqtgk vpegnrrsfk pkegckklk
//
LOCUS       WP_010504130             437 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Gluconobacter japonicus].
ACCESSION   WP_010504130
VERSION     WP_010504130.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..437
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48651
     Region          8..421
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 msaehsvfrs ifrnvsvltv grvvnalcsf vyiaftvral glsdfgllil ihslastgsv
       61 lsrmqswqtl irfgsdaftk ndtdllrkvv hfcirldtls aafailfgli avqvygvtaq
      121 wsrhvrflad lyvivsplmy sgwangilrm agkfhlvpii dtcaavvktl gvllgyvlhl
      181 klgyflamwa lailidygfy fyyamdilrk kfrfryfqay rswrwqipgm wqftraasvn
      241 qtlgnisghv atllvgnglg paeaavfrvc rqiadgivtp aqlispvlyp elvkmrdkqd
      301 wkglkrvtwk mfgvltalsl lllllsavfg skifrlmlhv hvhhtslyis imlmaavfsl
      361 lvipleplli vvghvkflmt srtaimaiyf palyvltmqf glagacltta acnaaillsr
      421 fagvwmfggr igkpkpe
//
LOCUS       WP_010503096             264 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfate adenylyltransferase subunit CysD [Gluconobacter japonicus].
ACCESSION   WP_010503096
VERSION     WP_010503096.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Mougous,J.D., Lee,D.H., Hubbard,S.C., Schelle,M.W., Vocadlo,D.J.,
            Berger,J.M. and Bertozzi,C.R.
  TITLE     Molecular basis for G protein control of the prokaryotic ATP
            sulfurylase
  JOURNAL   Mol Cell 21 (1), 109-122 (2006)
   PUBMED   16387658
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Snoeck,C., Verreth,C., Hernandez-Lucas,I., Martinez-Romero,E. and
            Vanderleyden,J.
  TITLE     Identification of a third sulfate activation system in
            Sinorhizobium sp. strain BR816: the CysDN sulfate activation
            complex
  JOURNAL   Appl Environ Microbiol 69 (4), 2006-2014 (2003)
   PUBMED   12676676
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Malo,M.S. and Loughlin,R.E.
  TITLE     Promoter elements and regulation of expression of the cysD gene of
            Escherichia coli K-12
  JOURNAL   Gene 87 (1), 127-131 (1990)
   PUBMED   2185135
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Leyh,T.S., Taylor,J.C. and Markham,G.D.
  TITLE     The sulfate activation locus of Escherichia coli K12: cloning,
            genetic, and enzymatic characterization
  JOURNAL   J Biol Chem 263 (5), 2409-2416 (1988)
   PUBMED   2828368
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     gene            1..264
                     /gene="cysD"
     Protein         1..264
                     /product="sulfate adenylyltransferase subunit CysD"
                     /EC_number="2.7.7.4"
                     /GO_component="GO:0009336 - sulfate adenylyltransferase
                     complex (ATP) [Evidence IEA]"
                     /GO_function="GO:0004781 - sulfate adenylyltransferase
                     (ATP) activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0070814 - hydrogen sulfide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30333
     Region          1..264
                     /region_name="PRK05253"
                     /note="sulfate adenylyltransferase subunit CysD"
                     /db_xref="CDD:235375"
ORIGIN      
        1 mddldqleaq sifilreayr klkplsllws lgkdsnvmvw larkafmgrv pfpvmhvdte
       61 kkfpemyafr deytkkwdld lllgycppve eidpslppaa rsaarktagl aamidkhklr
      121 gviagirrde qatrakervf sprgaghrwd vrnqppefwd qyatpyedgm hirvhpllaw
      181 reidiwryie regiplvdly fakdgkryrs lgdqditspi esnaatvaev iaelenskts
      241 eragramdhe sedaferlrv agyl
//
LOCUS       WP_010504287             437 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Gluconobacter japonicus].
ACCESSION   WP_010504287
VERSION     WP_010504287.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..437
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46414
     Region          2..422
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtepdqlaqs lrtrhivmia lggvigagff igssaalsmg gpavivsyvl agllvwlvns
       61 mmrdlasvtp grasflgqir halgdrfgfv agwtywltwv tvigveaiav tsmltpyipv
      121 pyavlellvl gamtavnlls vkgygefeyw fsaikvlaii vfsgigfwal gvhsipvken
      181 lfshggvlph gllallavip tvlfsmggse iatvaavesd nterniarat rtiplrigvf
      241 ylvtislilc lvpwtdivpg qspfllvlnr fhvpfaglam gvvilvaals slnsgiyvts
      301 rilyelaetg dapstflvve pktqlprral lasvgssifv aatavlspgl ifavlvsltg
      361 gfmlfnnall vlgrlkimpr kpagayvala liamaiiamm iqpetrsqie mgafaiivil
      421 laerflprak slqnnap
//
LOCUS       WP_010504299              62 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Gluconobacter
            japonicus].
ACCESSION   WP_010504299
VERSION     WP_010504299.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 62)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 62)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..62
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..62
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7026
     Region          1..62
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mnnclkelra erswsqadla aaldvsrqtv naiekgrydp slplaftisq lferrieeif
       61 fp
//
LOCUS       WP_010505269             208 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SOS response-associated peptidase [Gluconobacter].
ACCESSION   WP_010505269
VERSION     WP_010505269.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter
  ORGANISM  Gluconobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Gluconobacter"
                     /db_xref="taxon:441"
     Protein         1..208
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=23270
     Region          1..208
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcnlyaqtss qdeiraiaev lndhtgnlpf mpdiypdyva pivrhgqngr elvlarwgmp
       61 spafalkgrk vdrgitnirn tasphwrrwl gvshrcivpf tafseqarqd dgsfhpvwfa
      121 adatkplrff agiwtswtsv rklkegevta dlfgflttea ngvvapyhpk ampvilesrk
      181 eietwltapt pvalqlqrpl qesslavf
//
LOCUS       WP_010505414             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Gluconobacter].
ACCESSION   WP_010505414
VERSION     WP_010505414.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter
  ORGANISM  Gluconobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Gluconobacter"
                     /db_xref="taxon:441"
     Protein         1..182
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=19740
     Region          3..128
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,66..67,70)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(65,109..110,112..113,117)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(71,76..77,105,108..109,112..113,116,119)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94..96,105..106,109..110,113,117,120,124)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94,110,113,117,120,124)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(118,124..125)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          140..181
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(141..143,172..173,175..177)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mtiygyarvs ttdqdltiqe qalkaagcqv irsekvsgts tagrrelqtl laflqagdvl
       61 vvtridrlar siadlqtimh tlkdkgaalr cteqpvdttt aagkafldml gvfaefetnl
      121 rrerqlegik aakergvytg rkssidadvv rklrdegigp aeiakrlgig rasvyrilsa
      181 dl
//
LOCUS       WP_010505505             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Gluconobacter].
ACCESSION   WP_010505505
VERSION     WP_010505505.1
KEYWORDS    RefSeq.
SOURCE      unclassified Gluconobacter
  ORGANISM  unclassified Gluconobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="unclassified Gluconobacter"
                     /db_xref="taxon:2644261"
     Protein         1..187
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20301
     Region          1..145
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mleaadtlfa qadvpervtm daiaaacgvg kgtlfrafgs rarlldalwa tkiealrasv
       61 esgvapfrqd tspqqrlaaf ldliltfkld nrhliralef gsgilqsphy rwmlgvtarf
      121 ieegtgsppe gaalynahal laalhidlie dmlanglsld tireaqarra ymamgitesd
      181 yktlvri
//
LOCUS       WP_010505517             237 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HD-GYP domain-containing protein [unclassified
            Gluconobacter].
ACCESSION   WP_010505517
VERSION     WP_010505517.1
KEYWORDS    RefSeq.
SOURCE      unclassified Gluconobacter
  ORGANISM  unclassified Gluconobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="unclassified Gluconobacter"
                     /db_xref="taxon:2644261"
     Protein         1..237
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25218
     Region          <26..205
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mpelqtllke vvrrpatcds qkgpplasll aqlargddgh gqrvgrlagl ighlagsglc
       61 asslelagrl hdagklllpd sllnhpgafs srqmtvmrqh psmglgalfh lsadvptivh
      121 eavllhhery dgkgypfglq gdaiplaari vgladvidal lsarsyksgw sprqvraflp
      181 eqagtafdpr laelaveafe dllairqsaa qpvrgyvplp aqvpfssrti nlrndtp
//
LOCUS       WP_010505594             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Gluconobacter].
ACCESSION   WP_010505594
VERSION     WP_010505594.1
KEYWORDS    RefSeq.
SOURCE      unclassified Gluconobacter
  ORGANISM  unclassified Gluconobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="unclassified Gluconobacter"
                     /db_xref="taxon:2644261"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33751
     Region          7..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(103,107,146,160,162,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(104..105,109..110,112..113,116,120,122..128,189,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mhddagdlrf fvllveagnl tavarhlnvs agassrrlar leerlgvrlv trtsrrfdlt
       61 degqtfyera aeimidieaa eaeisahqqe lrgvlrigap lelgrrrlad fisefadrfp
      121 klrvhlllsd egldvvnsrl dlairigmpn eagtvatkim nseriicasp aylerfgmpt
      181 tlaqltehrc iclmrghelg mldqwrlsrs gedqivevtp hlsttsgevv hdwalkgkgi
      241 vfkvlwdvgd dlqrgrlvrl fpeyqgetig lfatmpsrrn vplrvrafld nlrdflappq
      301 s
//
LOCUS       WP_010505622             371 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Gluconobacter].
ACCESSION   WP_010505622
VERSION     WP_010505622.1
KEYWORDS    RefSeq.
SOURCE      unclassified Gluconobacter
  ORGANISM  unclassified Gluconobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="unclassified Gluconobacter"
                     /db_xref="taxon:2644261"
     Protein         1..371
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39450
     Region          133..340
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mhililsdni andiecasqa drslidtefs imkclstaia lataiaaapa laapvleptt
       61 qhflnglada hapaipslsp hdaralldga qasvkvtaps aritdrvlpi gptgstriri
      121 yrpldapnha paivyyhgag wvmggpashd rlvrdlaags gavvifvdye rspearypta
      181 ieqdyavley varhpvefgi dpsriaiagd svggnmvavv salvaerhgp rpvaqilfyp
      241 vtdaamndgs yrefaggpwl takamdyfwn qylpagtdra qphvsplntp dsilhgqapa
      301 lvitdendvl rdegeayarr lveagvpvit trynatihdf vmlnalaktp astaaiaqat
      361 hflrdaftka k
//
LOCUS       WP_010505709             107 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system PemK/MazF family toxin
            [Gluconobacter].
ACCESSION   WP_010505709
VERSION     WP_010505709.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter
  ORGANISM  Gluconobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Gluconobacter"
                     /db_xref="taxon:441"
     Protein         1..107
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=11301
     Region          1..106
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mnrgdfvtva lqgdlgkprp alivqadrfe ttasvtvlpv tstlidapll rlsvppdern
       61 glrktsqvmi dkpstvsrdk igptfgiasd tvmlsvnral alflgla
//
LOCUS       WP_010505819             305 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Gluconobacter japonicus].
ACCESSION   WP_010505819
VERSION     WP_010505819.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter japonicus (Gluconobacter nephelii)
  ORGANISM  Gluconobacter japonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Gluconobacter japonicus"
                     /db_xref="taxon:376620"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33957
     Region          8..>53
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,192,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 meqslisler mrtfvriaer gnlaavaret gagqstvtrh lreleealgv slltrttrrt
       61 altdegtryy aqcvqilslv eqasqemrdt rqatagtvri sctgalgvlh vsrliyafqd
      121 enpdirvefg ltderidlvr dgvdiairlg plsdcamklr slgesqrmlv aspewlrrng
      181 pvrgpedlrq legvrmsrvh gsdrlvlrsa rgrnhavpfh grlivdhgla ardaflagrg
      241 ygpahrwlie dclrdgrleh vlpnytlspv plsmliaper tnltrvrlcv dflaeglrqv
      301 pgisr
//
LOCUS       WP_010506340             235 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Komagataeibacter europaeus].
ACCESSION   WP_010506340
VERSION     WP_010506340.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..235
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25131
     Region          8..229
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msdalnnapp lrmdgvarry isgeetldvl rgadltlhps eivalvapsg tgkstllhla
       61 gllekpdagc vmvagqdaga ltdarrteir rdrigfvyqf hhllaefsar envmlpqmia
      121 gvarrdarar adellsifgl ghrldhlpgk lsggekqrva iaralanrph vlladeptgn
      181 ldvntsdavf dalletvrah gvaaliathn mdlarrmdri vtlrdglvvp vapat
//
LOCUS       WP_010506395             419 aa            linear   BCT 01-JAN-2025
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme
            [Komagataeibacter europaeus].
ACCESSION   WP_010506395
VERSION     WP_010506395.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 419)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..419
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=45063
     Region          18..414
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mdqtvasptd iagslrhira dfpilsqkvh gkdlvfldsa asaqkprqvi damadtmrtq
       61 yanihrglyw msertteaye avrdqvaafl gaqareeivf trnsteainl vahsfgtllk
      121 pgqvvlvsem ehhanlvpwq mlrdrtgiel rvtpitddga ldmdalarnl sdgrvalvai
      181 thmsnvlgti tnaraiadma haagakvlfd gsqlavhrrv dvraldadfy vvtghklygp
      241 tgigvlwarr eildamppfl gggdmistvs ferstwasvp hkfeagtpai ietiglgaal
      301 ayiesigfda igaheealta halkvlgnvs glkvigtapd rggvisftmd dvhphdiatl
      361 ldrngiavra ghhcaeplmr rlgvaatara sfgiyttpge idflaatleq irsffclma
//
LOCUS       WP_010506620             152 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Komagataeibacter europaeus].
ACCESSION   WP_010506620
VERSION     WP_010506620.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..152
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16302
     Region          1..151
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslrarfmdd lkaamkagqs ekvgtirmit aklkdvdiag rakgedqvsd eavmsmlrgm
       61 iksrtesasm yekggrpela ekenaeiaii raylppdldd atieaavrea iertdatsmk
      121 dmgkvmaalk qqfgaaldpa rasavvrarl aa
//
LOCUS       WP_010506635             522 aa            linear   BCT 01-JAN-2025
DEFINITION  S41 family peptidase [Komagataeibacter europaeus].
ACCESSION   WP_010506635
VERSION     WP_010506635.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..522
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55128
     Region          60..386
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mkfrngllig caflagiaaa pqiahysagr wgdiapmaha adtvskddns pheieqlmfl
       61 fgyvlekvka nyvepvstrd litnslngml sgldphssym tekqfsdlqv qtkgsfgglg
      121 levqgedghv rvvspiddtp aaragikpgd fivaidgkni dgqpldqvvt qmrgkpdtri
      181 tltlirekap kpiivtltra iiplqviksa lydnvgyiri aqfneetqsg llaaykklqa
      241 qthnkmagli idlrsdpggl ltqaidvgsd firsgeivst rarhpqdsqr wdahntditg
      301 glpivvling gsasaseiva galqdhqrav llgektfgkg svqtilpipg egairlttar
      361 yytpsgrsiq glgimpdipv reahddagys iheadlahii knrggntaqa psrtdlpaia
      421 ksipaqppan wptfdptkpm tdfqlqeglr vvrsmaglpv aaeppihddr akatpvpsas
      481 vppkaaapaa pagtpatptt paapaapaek egptaptvpa hp
//
LOCUS       WP_010506739             396 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: elongation factor Tu [Acetobacteraceae].
ACCESSION   WP_010506739
VERSION     WP_010506739.1
KEYWORDS    RefSeq.
SOURCE      Acetobacteraceae
  ORGANISM  Acetobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Acetobacteraceae"
                     /db_xref="taxon:433"
     gene            1..396
                     /gene="tuf"
     Protein         1..396
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=42936
     Region          1..396
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makakfernk phcnigtigh vdhgktslta aitktlakag gaefkaydmi daapeerarg
       61 itistahvey etakrhyahv dcpghadyvk nmitgaaqmd gailvvsaad gpmpqtrehi
      121 llarqvgvpa lvvflnkvdq vddpellelv emevrellsa yqfpgddipi ikgsalvtle
      181 dgdpevgenr vmdlmnavde yipqperpid rpflmpiedv fsisgrgtvv tgrvergavn
      241 vgdeieivgl rptqkttvtg vemfrklldr geagdnigal lrgtkredve rgqvlakpgs
      301 itphtkfkae ayiltkeegg rhtpfftnyr pqfyfrttdv tgvvhlpegt emvmpgdnva
      361 mdveliapia mdeglrfair eggrtvgagv vasita
//
LOCUS       WP_010506757            1062 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Komagataeibacter
            europaeus].
ACCESSION   WP_010506757
VERSION     WP_010506757.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..1062
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113430
     Region          1..1052
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mngivvtalk rpytfvvlsi livvfgvrgl lrtptdvfps inipvvaicw tytglmpedm
       61 sgrvvyyyer altatvnnie hiesqsyygr givkvffqpg tdtavaqtqi tsvsqtvikq
      121 mpagmtpplv ltynassvpv ltlqvssdsm tasqiydmss nlirpalvsv agaaipnpyg
      181 gqpgnimvdl dqskllahgl satdignalg kqnivlpagd qqigafdwmv qtnaspeeid
      241 sfnnmpikqe gnsvvylrdv awvhaggppq tnmvlvkghq avlivimksg dastlsvvsg
      301 ikallpsivr tlppgvditv lgdastfvke avrdvvqemg taalltslvv llflgswrst
      361 viiatsipla mlcsviglgm agqtinvmtl gglalavgil vddatvmien idahlemekd
      421 letaiidaan qiviptfvst lcicivwmpl fqltgvagwl fmpmaeaiif amiasfilsr
      481 tlvptmakym laaqvaahaa akaagghqep rnifgrfqqg ferkfiafrn ryrailehli
      541 sirgrfvpif glgafcslvl lvfagqdffp einsnalalh mrapmgtkia eagkismlvn
      601 yeierllpgq venivnncgl pfsplnqafi ptptvgaqdc dltvtlkdee apvakyrtil
      661 rkglaekfpg teitfmpadl takilnfglp apldvqvtgr nlyanfdfae klaeklrhvt
      721 giadvavqep lntptlrvna rrtyalgtgl teadvannal avlsgsgqva ptywldpktg
      781 vshlvdiqtp lqflqtmndl etipidkgdg npsdkapqil gglsdivqtg tpgevshyni
      841 mpvfniyast egldlgavsr qvarvvddvr kdlpagsslt irgqaetmng aytqliggla
      901 msillvylii vvnfqswldp fiiitalpga lagiawslfl thtalsvpal tgaimcmgta
      961 tansilvvsf arermdvhgd alraaieagy erirpvlmta samiigmlpm slsnsqnapl
     1021 gravmggllv atcatllfvp cvfalihsrk skqsaagege ha
//
LOCUS       WP_010506921             790 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Komagataeibacter
            europaeus].
ACCESSION   WP_010506921
VERSION     WP_010506921.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 790)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 790)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 790)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..790
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82294
     Region          2..69
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          70..769
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msqtlsfpvg gmscaacaar iekilnrqdg vqasvnfatg rvqvvldtpa atidavvaai
       61 rkagftvdes svdlsitgms caacaariek ilnrlpltqa svnlaterah ivfvpgiada
      121 dtfitrieka gfgaslvnds apddtharrl aawraerahf llllalslpf faqmvlmpfg
      181 tmymmsgwlq lvlagvvqfy garhlyqraw navrggganm dvlvvmgtsi ayvfsatvvi
      241 ahlhqplyfe asvaiitlis lgrlmearar drtsaglesl lklqpplahv lvngtmvdrp
      301 vadvrvgdif vvrpgesipv dgqvsegtse vneamltges lpvlkqagar vfggtintng
      361 vlratatgvg hdtalahivk mveqaqgska hvqrlvdris nifvptviti alvtfvvgwm
      421 vtgnatwslv savsvlviac pcslglatpt aimvgtglga rcgilfrnad aleraqkltt
      481 iimdktgtlt egqptvsdvv papgvdasrl lsvacaleqd sehplaraiv dhataaglsp
      541 lpasdframp gmgvmatvdg vpaclgsprf madhgmtpdd avtarleheg rtviavaagg
      601 hpvghialtd rlrpdairtv salkaagirv mmltgdnprs aaivakqagv ddfmagvlpg
      661 dkaqavrach dqggmvgmvg dgindapala aadvgfaiga gaaialdtad ivlmkselts
      721 vldaislsra tlskirqnlf fafiynilgl plaafgllnp ivagaamams svsvvsnsll
      781 lnrwkpggri
//
LOCUS       WP_010506760             446 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA recombination protein RmuC [Komagataeibacter europaeus].
ACCESSION   WP_010506760
VERSION     WP_010506760.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..446
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=49245
     Region          85..403
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mpdlsaspvl wigmllaams cllslivlrr lslmagqged adqlarlcvm teretaarva
       61 eneaqrarma eieralstrl dqrhqemtet fnriarmmgr dlaemrvtqs ealremaeeg
      121 rrqsdelraa vnerlhqave kqmqtsfqrv leqigamqka mgevsamtaq vgdlkrlfsn
      181 vktrggwges qlrsilddvl pegayetnrr lrddsrevve favrmpvrat vppvlaidsk
      241 fpteayerll qavddcnpda eraarralet tlriearkia tkyivppvtv efavlylptd
      301 glyaevarip glldeigrty rvivmgpglm pamlrtihlg yvtlalerrt ddiarllgat
      361 rqemlrmdgv leklarnasa msssidearr rtglvtrrlr eldvdtaaap agddgvnpas
      421 amgegagaqa dmapswsreg vgghgt
//
LOCUS       WP_010506546             222 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division ATP-binding protein FtsE [Komagataeibacter
            europaeus].
ACCESSION   WP_010506546
VERSION     WP_010506546.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Hung,L.W., Wang,I.X., Nikaido,K., Liu,P.Q., Ames,G.F. and Kim,S.H.
  TITLE     Crystal structure of the ATP-binding subunit of an ABC transporter
  JOURNAL   Nature 396 (6712), 703-707 (1998)
   PUBMED   9872322
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..222
                     /product="cell division ATP-binding protein FtsE"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=24392
     Region          1..220
                     /region_name="FtsE"
                     /note="Cell division ATPase FtsE [Cell cycle control, cell
                     division, chromosome partitioning]; COG2884"
                     /db_xref="CDD:442130"
ORIGIN      
        1 mfrlhdvsya hggsagvaal shisldvpqg efrwllgpsg agkssllsil slevqasagm
       61 veilgvpvmq arrsnlarlr rrigtvwqdf rllpdlsvfd nvalplrlqh raedeiahev
      121 haimkwvgle nrldarplql sggeqqrvai araviyrpal lladeptnal derqagrlma
      181 mfhrlaelgt tivvathnda ivekypapai elahghmvrd yr
//
LOCUS       WP_010506976             399 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Komagataeibacter europaeus].
ACCESSION   WP_010506976
VERSION     WP_010506976.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..399
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42962
     Region          102..398
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          290..398
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(294..295,328..329,332,342..343,346,388,392)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mrlrmvllat algaapfata mattitgpyv digggydltq tqhahgfdkn qyennantag
       61 yldatdnarl lkeahsrerm ehgdgwtgfa tfgwgfgngl raeiegdynw saltgynsvs
      121 gsaygnnhqs gkssgsdrsy ggfvnvlydi dlkrlfnidv pvtpfvgvga gylwqnvdas
      181 tsvtrylnvr qngtngsfay qgivgaaydi pgvpglqmtt eyrmigqves famgnisqtg
      241 ggdrtlsydh rfnhqfivgv ryafnhappp pppapavapp apsaartylv ffdwdgavlt
      301 drargivaea aqasthvqtt rievngytdn tsahpgprge kynlglsmrr adsvkaelir
      361 dgvpaggidi hgygeahplv vtqpdtrepq nrrveiilh
//
LOCUS       WP_010507095             325 aa            linear   BCT 01-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Komagataeibacter europaeus].
ACCESSION   WP_010507095
VERSION     WP_010507095.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..325
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=35058
     Region          15..103
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(16,28..29,31..32,34..35,38..39,41,48..50,51..54,56)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          92..311
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 msvvtltvsd deadirldrw frrhyphltq galqklcrtg qvrvdgrrat aatrlapgqa
       61 vrvppipnas rppplavkpl darqvreinq mvvyrddhvi vlnkpagiav qggpgithhi
      121 dalldglrds pddprprlvh ridrdtsgll lvartpgvaa klaaafrgrd vhkvywavvv
      181 grpspatgii dqpltklgag agaisvvaer gdadavhals eyevldaagr klswlalspl
      241 tgrthqlrvh cealgnpilg dpkyggdiah vtgftdklhl harrleiphp aggtlmvead
      301 lpphmretfr qigfvapata qprrs
//
LOCUS       WP_010507132             133 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Komagataeibacter].
ACCESSION   WP_010507132
VERSION     WP_010507132.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..133
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14793
     Region          3..129
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 marmihsmir vrdeaaslaf ydtafglkva drlvfdtftl iylsndeqtf eleltvnhdr
       61 ttpydlgdgy ghlavsvadv daeharlaaa glsplavkdm scgerfvgrf ffitdpdgyr
      121 ievlqrgrpg rfl
//
LOCUS       WP_010507241             222 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Komagataeibacter
            europaeus].
ACCESSION   WP_010507241
VERSION     WP_010507241.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..222
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24483
     Region          6..77
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(16,18..19,21..22,25..26,70,73..74)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(16,55..57,68..69)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(55,67..68,70..71,74)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          90..204
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(91,98,163,166..167,170,174)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(91..92,95..96,99,137)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(98,102..103,106..107,171,174)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 msdgilvigt rrysswslrg wlavrlagld vreqviplad ngetpairti spngkvpyle
       61 hkgvavwesi aiceycaeqa pglwpedvrq rayarsisae mhagfravrq ampmnigrdn
      121 rplaagttpd idadiarida iwtearldfg kdgpflfgat fgmadamfap ivsrflsygi
      181 spspesraym aavrahplvd dwyqkaaqep aewrqsrfed ia
//
LOCUS       WP_010507247             221 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Komagataeibacter].
ACCESSION   WP_010507247
VERSION     WP_010507247.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..221
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23941
     Region          3..209
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 mpevmfagpd grlegryhhs sapnaplalv lhphplhggt mnnrityamy rafekmgfsv
       61 mrynsrgvgr sqgrydggig eisdaaaald wmqmvnpnas glwiagysfg afvgmqllmr
      121 rpeitgwisv appanhydfg flapcpcggl miagendelv pepavrklvd klntqkgvtv
      181 dyrifkgadh vfanhadqva ealedhvstv mnrkalalaa d
//
LOCUS       WP_010507331             539 aa            linear   BCT 01-JAN-2025
DEFINITION  amidohydrolase [Komagataeibacter europaeus].
ACCESSION   WP_010507331
VERSION     WP_010507331.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..539
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58471
     Region          2..537
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mpldlaiina dihghaqpvn avgimdghiv aigtssdima qcvpttvird lggmflmpgf
       61 idvhmhiama adylsaiglr dvrtmkalle rvaqwaaahp dapwirglew sygypdlpng
      121 efdarmidsi lpdrpvilts gmahaawans rameiagitr dtpdpengei vrradgtpsg
      181 wlkedavslv tshippmtgp emdhalglvl dtasrlgitr mqsaaydeay lpllsardaa
      241 gtlpvrigmm teiepdpglt pqrlrealdl racydnamvr ldgikffldg vleshtgymp
      301 egyadqpdar gtllwdcray idavragven gldiwthaig pgairlalda aenaghsper
      361 prirvehael pypddiarfa htstiasmqp vmiapadewm gmegvwkkrv gdnraqlafp
      421 mrslldagst lafgtdwpiv sldplrglrk avlrrpigap aseawiptqa irfseafdsy
      481 tskaavaagr eryegrialg yradiavlsg npfmtdpdsl pdlkcmltvt agrivhdli
//
LOCUS       WP_010507354             465 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Komagataeibacter europaeus].
ACCESSION   WP_010507354
VERSION     WP_010507354.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..465
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49522
     Region          3..462
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mtaietfiar iqplvgnris tnatvrqhha hgegwqspdp aaqpdvvvfa rtteevaaiv
       61 sachdlylpv ipfgggtsle gqltatkggv sldlsqmnai pdirpqdlsc rvqagvtrqq
      121 lngllrsdgl ffavdpggea tlggmcatra sgtgavrygt mrenvlglta vmadgkiiqt
      181 ggnvrksatg ydltglligs egtlgiitei qarlhplpet ilgatcqfst ladavdtats
      241 iiqaglpigr lellddvqmd aciryssleg yrplptlffe lhaspasvte qadllreite
      301 yhnglsfras aspeertrlw karhdafwac mayrqghkgm ttdavvpisa mtdmitlakq
      361 dieesglvap ivghvgdgnf htvilippep dgwaraqald hkiiqraldl ggsisgehgi
      421 giakqmfmhn qhgndaimvm haikraldpr nilnpgmllp aavsp
//
LOCUS       WP_010507384             156 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Komagataeibacter europaeus].
ACCESSION   WP_010507384
VERSION     WP_010507384.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..156
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16356
     Region          1..154
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mltlqingks vevdvdpdtp llwvlrdvlg mtgtkygcgi aecgvctvhv dgrpvrscsl
       61 pvgligprka iitieglqad pvaaavrkaw ldidvvqcgy cqpgqimaai allkkipnpt
      121 deqieagmsg nlcrcgtymr iraairnvaa aqgatp
//
LOCUS       WP_010507387             416 aa            linear   BCT 01-JAN-2025
DEFINITION  c-type cytochrome [Komagataeibacter europaeus].
ACCESSION   WP_010507387
VERSION     WP_010507387.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..416
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43471
     Region          179..393
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 mtmterglgr itgmlfalla stgihgaraa dapdgqyltr aadcevchtr pggtpfaggr
       61 afaipgmgvi yspnitadrq agigawtddq fvkavrdgvs pgwkhlypam pyrdyaymtp
      121 devkairayl atlpssaarp pentlkfpfs irsamifwnl vngpasshpd dpahtpswnr
      181 grylvegpgh caechsprtf tmgvsgtnay agadvggwqa ynitssktdg igawsaddla
      241 tylstghadg hgsasgdmgd vvshslrflt rqdidamvey lrdiparsst dgappaftqp
      301 tathdqadsh gamlyagaca gchlpdgsgr qnpvasiaga rttlgaangq nllqvlthgs
      361 alqtatgtaa mpafhggysd qdvadianfv mhhfarsstm vnaadvakak tasape
//
LOCUS       WP_010507478             270 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Komagataeibacter europaeus].
ACCESSION   WP_010507478
VERSION     WP_010507478.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..270
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28529
     Region          7..255
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mlknrqflge liseciavmi ivligdsvaa mytlydpspy klsywgvsiv wglgvtiaiy
       61 vtgsvsgtha npavsvalal yrgfswrkvp aycaaqvlgg mlgaalvytl yqpvidhynq
      121 lhgisradgg aagvffthpg efitplhafm detiltallv ggifaitcey ntvapqanss
      181 aliigllvas igacsgylea wainpardfg prlfcflagw ggsalpsadn fwwvpiagpl
      241 lggvigagcy qflirpfipr hasaimppap
//
LOCUS       WP_010507502             215 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Komagataeibacter].
ACCESSION   WP_010507502
VERSION     WP_010507502.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23917
     Region          16..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkpvaptisp kpglrerkqa rarttliaea mrlfsaqgyd qttvdeiada aevsrrtlfr
       61 mfetkgdivl awtrgmtqtl ndalatcpad mhpadammha ftslvpriaa nrqdtyafvy
      121 liektpslqt vslqkygkwe dclaeglakr iterknrrma arlmarggia ifrtaldewi
      181 rlkgrpalvp llqktyelqa slwpdhagtg pedaa
//
LOCUS       WP_010507546             534 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin monoamine oxidase family protein [Komagataeibacter
            europaeus].
ACCESSION   WP_010507546
VERSION     WP_010507546.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..534
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58800
     Region          49..532
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtdshppktp trrqlltrig tlagsaalyq amttmghaqg tdftappvls garrgtrvlv
       61 lgaglagmls ayelrkagya vqvlefqgrs ggrnislrgg dtvtelggav qkvgfasgny
      121 inpgpwripy hhqgllhycr efgvelepfv elnhnswlhs stafdgkpvr yrefssdftg
      181 fttellgkai dqhklddvvd aderehlrta meqwggldpd ltyrkgdtss qrrgytrpqg
      241 ggidgapips dpfarrdvlr sglwtwmafh erlemqttmf qpvggmdmig kgfnrqvhdl
      301 itlnckvtsi qqdehgvrvm yddmnhggva rqaqadycvc tiplsilsqm dvqvsaplka
      361 aimavpyass vkmgmefrrr fweeddqiyg gisftdqpis qisypshgyf srgpavllgg
      421 ymfgpaafdf agmtpqarle qalaqgevlh pgtyrkefsn gvslawsrvp walgccsmws
      481 eqarkthykt lcmmdnrivl agehasyvgc wqegailsal davtqlhkra qgas
//
LOCUS       WP_010507793             304 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Komagataeibacter europaeus].
ACCESSION   WP_010507793
VERSION     WP_010507793.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..304
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33204
     Region          1..298
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mhilfitstr lgdailstgl ldtllrrypq adftiacgpv aaglfahmpr rvrtiemvkq
       61 pwdrhwlelw rqcsgtkwdl cvdlrgsvvs yflrvgkrhv mrggrrrgrr ithignlldl
      121 dpaplpvvwt saaeraraae mlpggprwia lgptanwdgk iwpaerfvav fralqeddps
      181 vrpvilygpg egervraqav ldqlpdaldt ggnlsvtqva allgrctlfi gndsglmhla
      241 aacgiptlgl fgrsraseya psgpwarvam apgpvgnapm eglavaqvvt tarallrdrw
      301 grkr
//
LOCUS       WP_010507875             409 aa            linear   BCT 01-JAN-2025
DEFINITION  lactonase family protein [Komagataeibacter europaeus].
ACCESSION   WP_010507875
VERSION     WP_010507875.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..409
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43373
     Region          30..406
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mscnisrraf ttalaaagvp aisrravaqt atkprticyi ggytqhgppg gagngqgisv
       61 femnpdtssl splmtyvdia spsfmamsad frhlyalsei ndfnangegc vtafsvnrss
      121 geltklnvvr sggavpahls vhasgkyvlv anymggtvgv lpihpdgglg dptdvvhdtg
      181 prmpdraadn ppgnfaisdh ssahvhmvas dpsghyvlac dagldrvyvw tldlhtgrlv
      241 paktpfismt pgsaprhfsf nekgtmiyil geqdskvvaa tfnpqtgeiv pqqtvstvtp
      301 hfrgstlaag illspngkyl yvsnrlgdsl asfhvnddgt lnlveeiwmh adygrammfd
      361 psgtylfcan qrsdsvtsfk vnaqtgvldf twnftpvgsp ttfafmnti
//
LOCUS       WP_010507837             367 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Komagataeibacter europaeus].
ACCESSION   WP_010507837
VERSION     WP_010507837.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..367
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39236
     Region          1..367
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mgldgrvvaa ltrmglhqps liqrevippv magrdveara gtgsgktvaf aapvlstlmq
       61 pgdadnahvr clilsptrel agqtagvlrg largsglril qatggtarva qartlgegva
      121 ivvgtpgrvi dlvhggeldl stvgqfvlde adrmlepgfa eemlalaaal parhqtllfs
      181 atippamael aarllhrpvr ismevenapa priaqyaifv pmrhkaeatl aclkqygmqr
      241 vmvfvrtrqe adtiarsist ltpavaihgd hsqarrerml rdfrqgrvgv lvatdvmarg
      301 ididdialvi nhdipaqpea yvhrigrtar agrrgvaval capeerqalk dierltgqri
      361 riaslpe
//
LOCUS       WP_010507881             254 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Komagataeibacter europaeus].
ACCESSION   WP_010507881
VERSION     WP_010507881.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..254
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=27308
     Region          9..247
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
     Region          17..77
                     /region_name="DZR_2"
                     /note="Double zinc ribbon domain; pfam18912"
                     /db_xref="CDD:465906"
ORIGIN      
        1 mnhhahpwwr ragtrmldtl fpphclacga dvmqagllca tcvsqlhlit spychrcalp
       61 fpsraaggat ltctacaenp ppwregraam vyddlprqli lplkyadrte natllaryma
      121 aaarglvekd sifipvplhr vrlftrrynq aallacalar qtgasvlpdg lerlratpal
      181 kglgrtrrqa imqgvigvrg hrlgdiagrh vivvddvmtt gatlaacass llragaarvd
      241 vlaaaracgq heqq
//
LOCUS       WP_010507890             209 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Komagataeibacter europaeus].
ACCESSION   WP_010507890
VERSION     WP_010507890.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10154716
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..209
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=23700
     Region          144..191
                     /region_name="DnaJ"
                     /note="DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock
                     protein 40) proteins are highly conserved and play crucial
                     roles in protein translation, folding, unfolding,
                     translocation, and degradation. They act primarily by
                     stimulating the ATPase activity of Hsp70s; cd06257"
                     /db_xref="CDD:99751"
     Site            order(168..170,179,182..183,186..187)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mmkrrntrhr afdpepdapd rccdmhgcdq pagyraprsr dalnsyfwfc lqhvreynan
       61 wdfyrgmspg qieahiradt swnrpswklg qgnaahafse eevldpldll kgaakararn
      121 rarqqqaedr raeapqalky plgvldlgwp vsmeelkary kdlarqhhpd anggdrkaee
      181 rfkginiaya tvrahlvtta grdgmarsa
//
LOCUS       WP_010507978             282 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Komagataeibacter europaeus].
ACCESSION   WP_010507978
VERSION     WP_010507978.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..282
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29850
     Region          10..279
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mhplisatdl aqaiqhgdil vldasmalpg qafdpqqrfa nahvagavrf didtfsdpds
       61 plphtipgqa rfarlaterg mantkrivfy dqdgmacaar awwltrlfgh ervqvleggl
      121 pawksaglal etgpdlaapa pfvsrprygr lhgtgdvldi vhgrlpglil darsrgrfeg
      181 rdpepragie sghmpgarnl pytellddng rflpvdtlke kfaslgvtds tpvtcscgsg
      241 mtacmialal vsigggagep avydgswaew astpdspivc ga
//
LOCUS       WP_010508013             265 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Komagataeibacter europaeus].
ACCESSION   WP_010508013
VERSION     WP_010508013.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..265
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29233
     Region          6..262
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mtrtgltdsh chldhfsdee mpeilartrq agvdglvtig trlsradqqk klatldtpdl
       61 rvwctigthp dhvdeevlpd aaelvamadd prvvgigesg ldyfhgqpdi rprqhdsfrv
      121 hidaarrtgl plvihtread ddtlgilrde tarngafpfl ihcfssgpdl argalelggy
      181 isfsgiatfn raqsvrdvak dvpddrllve tdspylapvp rrgkrnepgy vaytarmlae
      241 lrgmedaafa emttrnfsrl fsrav
//
LOCUS       WP_010508028             154 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Komagataeibacter
            europaeus].
ACCESSION   WP_010508028
VERSION     WP_010508028.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..154
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16611
     Region          4..143
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mpcvtvrvqa etfdvtheta lllrgqdevg gvgaftgivr ggdglvalel ehypgmtesm
       61 mrriaesaca rfgltgctvi hrvgrlavgm pivlvlcaaa hrkaalegtd fmmdwlktsa
      121 pfwkreefan grsqwvqpra hddaatarwg tlgv
//
LOCUS       WP_010508124             300 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Komagataeibacter europaeus].
ACCESSION   WP_010508124
VERSION     WP_010508124.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..300
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32371
     Region          1..284
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 marilvirlg algdfiqsfa pfaairahhp hdvvdlltqa pfadlarhap wfdhvhvdrr
       61 ppwhdlravm alrrllrsyd fiydlqtsgr stryfhlsgm tawsgigrga qavhdspqrr
      121 amhtrarqrd qlrragidsl pvpdlswlar ggpvlpapyg vlvpgaaahr pakrwpvery
      181 aalaqqmhar gllpvivggr geralaavir dtcpaavdlt grtslpelgg vmaraacavg
      241 ndtgpmhlaa algvpctvlf sadsnpalta pvgqkagqvr viyvrdlatl rvdrvaatla
//
LOCUS       WP_010508123             287 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Komagataeibacter europaeus].
ACCESSION   WP_010508123
VERSION     WP_010508123.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..287
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=30075
     Region          159..277
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Site            order(174..175,177,201,204..205,208..209,211..212,235,
                     238..239,242..243,246)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          199..229
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          234..261
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 maagivvvvn magngcvraa dapggaplpa vsavpehdgp ghdeawsfah ctatvsddpd
       61 gardyaedwl ghgggleaeq cealarielg dvataaasld rlahvpgwpv gdpapahagt
      121 qpdtpqslrr raavaeqaar awqaddspkq afdsaayglt lepgdvplrl vyarvaveld
      181 qpqraidtlt plpsvpaerd ealvaraaaw rrmgrigqam tdinaalkdm prngaaller
      241 gilyqregqm aqaradwqdv vtlapdsdea dlarqdlsll etdpeap
//
LOCUS       WP_010508228             338 aa            linear   BCT 01-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Komagataeibacter
            europaeus].
ACCESSION   WP_010508228
VERSION     WP_010508228.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..338
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34489
     Region          103..309
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mirlhrkhtl vasaafaaml caasplaala qdaapaasda atapavsapa tdgsgaaatp
       61 apgadapapq aaapadaapa papaaeappa dappkapegn pyglgalwan gdfiargvll
      121 imvfmslgtw yimitkffeq arvmnaakqv msdfwtkgsi kdgaaalpan spfryiadtg
      181 vkaaehhegt mqesidlhsw ttmsiqrsvd viqtklqggl aflgtvgsts pfvglfgtvw
      241 giyhaltaig iagqasidkv agpvgeslim taiglgtavp avlgynllvr rnkgamdkir
      301 nfaadvqsil mggyrhgaei tihpdnsptt ttidnrva
//
LOCUS       WP_010508304             171 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase, partial [Komagataeibacter europaeus].
ACCESSION   WP_010508304
VERSION     WP_010508304.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..>171
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          13..>128
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 mpqdaagtpa sqirlvladv dgtlvtkdki ltprairave rlrergilft itsgrppkgm
       61 kmvidplkis epiagfnggm mvrpdftvie artlpadtar rvigiirdhg adpwvyngnd
      121 wivskldaph vareqwtvkf ppvvgnveak ldqvvkitgv sddlalmkrl e
//
LOCUS       WP_010508347             354 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Komagataeibacter europaeus].
ACCESSION   WP_010508347
VERSION     WP_010508347.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..354
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37886
     Region          3..332
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,225,286,306,308..310)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,173,176,178,225,232,286,306,
                     308..309)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,173,176,178,309)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mptlftplkv galtlpnrvv mapltrlrag pghvpndmma eyyaqralag lilseatpvt
       61 pqgigyegvp giwtdaqaeg wkkvtsavha vggrifmqlw hvgrisdpyf lngeapvaps
      121 aiaakghvsl lrpmrdyvtp ralrteevpg ivdafrrgae lakvagfdgv eihgangyll
      181 dqflqdstnh rtdryggsie nrarlmlevt daaiavwgkd rvgmhlsprc dlhdmgdsdp
      241 aatfghvate lgrrgiafic areaegpdsl gpqlkkqfgg vyianekftg asaekaiedg
      301 radavafgqa fisnpdlper lragveltpp dpstfythgp kgyidyptmg aagd
//
LOCUS       WP_010508478             389 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Komagataeibacter europaeus].
ACCESSION   WP_010508478
VERSION     WP_010508478.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..389
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41278
     Region          30..366
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mgspstpavp ttrqtpdala arfatraaah drsgeiaten ldecraagll gltiaradgg
       61 qggglrqvtd vvgtlatgdp ttalimamhf lqhmliaqsd hwpeaarrqv tetalhdgal
      121 inalrvepel gtpsrgglpa tritsdagkv vlngrkiyst gstalrwgtv wvatdeaqpr
      181 vgqvlvdlha pgvrierswh qmgmratgsh tfvfenvelp etalvdlrlp eqwhsndgal
      241 vtghalaiaa lydgvaraar dwlisflhar vptalgrpla tlprfhtllg qidallmtnr
      301 simdaalnqt engtypgtea nlakyvvten aikavelgva aignpalsed nplerhfrnv
      361 lcarihspqg dvalaaagra alteppqrs
//
LOCUS       WP_010508509             343 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Komagataeibacter europaeus].
ACCESSION   WP_010508509
VERSION     WP_010508509.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36313
     Region          9..330
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mpadrpapll dvrdlcvgfp argrmvpive hvsfslpeag ilglvgesgs gksvtamaim
       61 glidtpgvrv sgsvrfrgre lvglpprqmr rlrgrdiami fqdpmtaftp vytigwqide
      121 qirahervsr tqarartvri lgemgvpdpe rmarryphql sgglrqrami amalscnptl
      181 liadepttal dvtvqaqile lirslrathg ssvllithdm gvvaqtcdst lvlysgrvae
      241 tgpsgrvfdh pghpytaall dsipplygpr pdrlpaiaga ppvpadrpag cafgprcahv
      301 hatctaappa lvplgpghaa acvlpaegtp lpprtvargd acp
//
LOCUS       WP_010507708             297 aa            linear   BCT 01-JAN-2025
DEFINITION  complex I NDUFA9 subunit family protein [Komagataeibacter
            europaeus].
ACCESSION   WP_010507708
VERSION     WP_010507708.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Parey,K., Wirth,C., Vonck,J. and Zickermann,V.
  TITLE     Respiratory complex I - structure, mechanism and evolution
  JOURNAL   Curr Opin Struct Biol 63, 1-9 (2020)
   PUBMED   32058886
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..297
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=31002
     Region          4..273
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(10,12..15,34..36,78..80,93,116..118,129,133,
                     152..155)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(129,133)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mtrkvatvfg gsgfvgrsvv grlaragyvv rvagrtatda atlrmlgdvg qvvsvvasit
       61 dekacvaaie gsslvinlvg ilaphgadtf taihvegaar varlaaasgv erlihvsalg
      121 aradslsaya rskaegecmv grampeavii rpslifgvdg afpamfarma rflpvmpvfg
      181 attrfqpvwv gdvadgmiri atgadmagai fefggpqvlt mrqivawaar wgghprplfv
      241 vprwlatvqg mvlehlpgkm ltrdqvrlly vdnvvapgar tldmlgiaps pmglvmg
//
LOCUS       WP_010508548             213 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Komagataeibacter
            europaeus].
ACCESSION   WP_010508548
VERSION     WP_010508548.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..213
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24293
     Region          7..208
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mfssfkltsa erealnaist rihrpakrri yaqgdagnyi yrirsgavrl ehhlkdgrnq
       61 ifaflwpddm fgnleggayh tsaitlvdty lfqisypalk dlvqihpriq tlflrqaldy
      121 akmaerhlll atyplvvkrl agfllecsrq adffdrgsni ltlamdrkdi adylgfaiet
      181 tsrtlkeled mgliqrlsaq rikidrdrig aii
//
LOCUS       WP_010508277             425 aa            linear   BCT 01-JAN-2025
DEFINITION  Mrp/NBP35 family ATP-binding protein [Komagataeibacter europaeus].
ACCESSION   WP_010508277
VERSION     WP_010508277.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Vitale,G., Fabre,E. and Hurt,E.C.
  TITLE     NBP35 encodes an essential and evolutionary conserved protein in
            Saccharomyces cerevisiae with homology to a superfamily of
            bacterial ATPases
  JOURNAL   Gene 178 (1-2), 97-106 (1996)
   PUBMED   8921898
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..425
                     /product="Mrp/NBP35 family ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0140663 - ATP-dependent FeS chaperone
                     activity [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=43874
     Region          167..406
                     /region_name="ParA"
                     /note="NUBPL iron-transfer P-loop NTPase; pfam10609"
                     /db_xref="CDD:431392"
     Site            order(178..185,310,312,337..338,374..376,379..380)
                     /site_type="active"
                     /db_xref="CDD:349757"
     Site            order(178..180,209..210,212,215..216,256..257,287,289,292,
                     316,319,375,377..378,380)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349757"
ORIGIN      
        1 mprmpgmtcd rhaggcppfh dstttgrpfy trtgqiadsr erttmtspdr atietvlqrv
       61 rtadhaasva dmgsldafmv rdgvlhvaia tdrtragslq pllpeleral vtavpgctaa
      121 sviltahrpa paapapqaap apaggghrpl nlggktpkaa tgplppnvgv viavasgkgg
      181 vgksttavnl avglgleglk vglldadvhg pslprmmgvg dqpevrdgrl ipphkwgisa
      241 msigmlvdes kamiwrgpmv mgaigqllgd vewgaldvlv vdmppgtgda qltlaqktal
      301 agavivstpq dialldarrg vamfekmnvp vlgvvenmsy fccpncnhrt elfghggara
      361 eadrmgvpfl geiplladir asadngapvv vaapdspagq ayralahtvg galrrlleqk
      421 kkaar
//
LOCUS       WP_010508575             299 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Komagataeibacter
            europaeus].
ACCESSION   WP_010508575
VERSION     WP_010508575.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..299
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32519
     Region          37..298
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mktkkdagrp rlgrglaall geqvnmlpaa pavearktpe tisslpvdvm epgpfqprqq
       61 mepgaldela ssirvrgilq pilvrphpgr kgvyqiiage rrwraaqiag lhdvpvhirp
      121 ledgdamaaa lvenlqradl naieeaeglq rllddydltq delasaigks rphvanmvrl
      181 lqlpppvrda vrhqslsagh arallahddp vaalkvvlaq glnvrqteal arqqerkaaa
      241 ardkaektar npeiaalerd latrlglkvq iafdgkggsi ridyrsleqf dgllrllqq
//
LOCUS       WP_010508628             312 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Komagataeibacter europaeus].
ACCESSION   WP_010508628
VERSION     WP_010508628.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..312
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31832
     Region          2..311
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtvlvyldhe ggairqasrs aiaaaarlgd vdvlvtgpda aaaaksaaai pgvkkvlqvt
       61 dttgnselae pvaallaela agythilaas sataknvlpr taalldvqpi pdivaindad
      121 tfvrpiyags alatvrsada kkiitvrass fdpvaseggn atieevalpa gpggstfiat
      181 elskserpel esarvvvsgg ngmlneenfk llepladrlg aaigasraav dkgfvsneyq
      241 vgqtgkivap elyiamgisg qiqhlagmkd skvivavnkd peapifqvad ygivgdlfti
      301 lpqleaeldk ag
//
LOCUS       WP_010508626             546 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Komagataeibacter europaeus].
ACCESSION   WP_010508626
VERSION     WP_010508626.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..546
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=59924
     Region          1..>31
                     /region_name="mhpA"
                     /note="bifunctional
                     3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid
                     hydroxylase; PRK06183"
                     /db_xref="CDD:235727"
     Region          18..346
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          442..543
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 msetpretme fdvvivgggp sglaaairlr qvapdasvcl iekgseigah ilsgaviepr
       61 alaellphwr eegaplntpv teeqmlyltr kgsleipfld rvmphmsnhg nhivslgdfc
      121 rwlagraeel gveiypgfag aevlvddsgr vtgvatgdmg igrdgqpgdn yapgmelrak
      181 ytlfaegcrg sltkqvtamy nlrkgvdpqt yglgikelwe ipkemhrpgl vqhsfgwpld
      241 drtyggawmy hfgdnlvsyg fvtgldypnt wlspfdemqr vklhpafrpy feggrriayg
      301 aralseggiq siprltfpgg aligdtagfl nvpkikgtht amksgmlaae avaealatdr
      361 vepgsytrri rdswlwtelr svrnirpafa kfgmkggaly sgidamllrg rapwtlhtrh
      421 gdnevlepas isekisypkp dgkitfdrls svflsstnhe edqpvhlkvr nmslwktvnw
      481 dvfrspesry cpaavyevad eatdphlqin aqncvhcktc dikdpaqnid wvtpegaggp
      541 nypggm
//
LOCUS       WP_010508794             349 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Komagataeibacter
            europaeus].
ACCESSION   WP_010508794
VERSION     WP_010508794.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..349
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=37122
     Region          8..335
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 msgpgerldh fmaranaayy agcdpfadfi tapeisqvfg ellgawvavv wgqlgcpdpf
       61 mlvepgpgrg tlmadalrlv rrvapachka mrvhlietsp rlrdvqaaal rdatimpvcw
      121 hdrldgvpdg pmvlvanefl dalpirqfvr rgqgwderfv hdgaftlapg dfparhparl
      181 rpvpegevle tcqpaldfih algarllrwp gaavlidygy dapawggslq alrdgrpadp
      241 lldagradlt ahvdfgaiad hvpagvdvwg smtqgsflsa lglaarveql araapaqade
      301 iraaarrlva pdrmgqlfrv mglssglagd lpgfagrrag ngtgrggtp
//
LOCUS       WP_010508820             247 aa            linear   BCT 01-JAN-2025
DEFINITION  (Fe-S)-binding protein [Komagataeibacter europaeus].
ACCESSION   WP_010508820
VERSION     WP_010508820.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..247
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27036
     Region          <2..242
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mkiglfipcy idafypeagi atlelleklg qdveypldqt ccgqpmgnsg cnsdaaaaea
       61 lfvrnfakyd kivmpsgsct hhvrdnfdai pqtdevrhvr entyelvefl hdvlkvdafp
      121 waefnhtvgl hnscgtlral rtasmselge kpfskpmdll kkvkgirfvt pkrpdeccgf
      181 ggtfsvteea vsakmgvdkv rdhyqagady ivsadsscvm hqqgcaerag vpirfihiaq
      241 ilngaae
//
LOCUS       WP_010508906             736 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Komagataeibacter europaeus].
ACCESSION   WP_010508906
VERSION     WP_010508906.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..736
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81281
     Region          63..722
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mirlwfsrrp lspamlaamt aftpvyslva qtttatgtpt tttgttttqv tdgdvtrrss
       61 apdamtvtar ldrariqlqp stgatvhafs rkaletipgg dnagmnsvll qapgvaqdsy
      121 gqihvrgdhn evqfrldgvq lpeglnvfgq tlmtrfadnl slstgalpvq ygflqaavvd
      181 intkngstnk ggnvsiygga rdyffpsaqy ggqhgkwdyf ftadyvhdrv gienttpsfn
      241 aphdlsnqyh flghvrytvd entrisliag vsnaeyqlpn iggqpmfgdn yssllpqapg
      301 ssnlnerqke itdfgilslq ktigafslqt svfsrysslg yspdpnmgdl aymgisqhae
      361 rsvmstgtqs dvtwrvrpdh tirfgfqvfa ernitkadat vfndanqqvk ihtgngrtgd
      421 iyglyvqdew qpvrnltvny glrfdgvgey tdehqlspri nvvwrawkga alhagysryf
      481 tpppfevvgg tdlrqfants aatdvsrsdt vkaerdhyfd agieqvilpg wrvsfdayyk
      541 lahnlidegq fgapiilsgf nyrrgqvngy efstsydhgp lslygnfaws raigkditsa
      601 qfnfdaddlk yisqhwihld hdqrwtasag gsytffyrsg hptrisatmv ygsglrqdsd
      661 vpnggvipqy atfnmsvvqs frdlfhsrfl rttqlrldvt nlfdhpymlr sgtgvgvgap
      721 qyglrrtilt gisqsf
//
LOCUS       WP_010508925             205 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Komagataeibacter
            europaeus].
ACCESSION   WP_010508925
VERSION     WP_010508925.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..205
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22368
     Region          5..195
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtarlvlydw tpdvrcyavr lglslmgmty eiravdtdlp vgqrpvglra gerppvlvag
       61 svrlsrpgvi mqfiarqpev arawldpahe waildwldfg ttaldtmaaa rdaafgttlp
      121 vlppmgalva alrrmedhms arameghdwf aapaasiadv vlfvvfaltv dlgverdtcp
      181 alrrwarrmr glpgfvvmpg vpdya
//
LOCUS       WP_010509087             851 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Komagataeibacter
            europaeus].
ACCESSION   WP_010509087
VERSION     WP_010509087.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 851)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 851)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 851)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 851)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..851
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..851
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92914
     Region          498..799
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 msahyattvh saptrsrrgg iltllaafml allpwamqar aadtdpatqg itsqqaqqvl
       61 svmndpqkre eftrtldaia kglpapkpap aaapakkaaa padvslepds issetmselt
      121 hirdlalqqg qnfmglfkdl afvgrwvhsi lsnadsrril ldamgrasii filalvaera
      181 lsiamrkpla gvtaravate qrlnqrlkre dqadqnqpap ppastadaqa eqqteqarqn
      241 ddrqqhetlr iitripysll hllikllpva lfcglgygas alftsthqaa mvtitltnay
      301 viarviylll etvfvphspt irlcsasdat armvtrwwnf lvaapsivvc lstlggvfdm
      361 pargteaiir avvliehili aifiwrirhh vaaalqpsar lrekpfwifv grmvrfwwip
      421 amffdlalwl vwatqirggy awilrtlslt ivvilgarll svlafsmqnk ifhvpeatek
      481 rypglqarvd yyypiarral svlltfvtiv lllqswglpa irfflhgslg tkivgamlti
      541 miaytiaivv wevanatlqn qitrfetsdq asratrlrtv lpiirtvllt fiiiivtvtt
      601 lsqiginvap lltgagimga aiafgsqslv kdfitgffml venamqvgdw vtagsvagtv
      661 ehlsirtlrl ravngdlhii pfssvtsian tsrdynlvvv sfmldlsedp hrvaailkde
      721 lslmrkdpvy gpliksdfsf lgveqadgng akflgsirta agakwkvyre yysrlgarmv
      781 kekvafpipt svnllangps galrmnmeed patllaaraa qpdapkpaap kaqadgdgqa
      841 aspkgnepsh g
//
LOCUS       WP_010509142             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Komagataeibacter europaeus].
ACCESSION   WP_010509142
VERSION     WP_010509142.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32321
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103,107..108,110..111,114,118,120..126,187,217..221,
                     228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllsalhsf vrvaatgsfs avsretgasq ptisrhiall eahygatlfa rttrslmmte
       61 dgrsllphay evleiletae talgrrrasv sglvrlgvtt afglyltsrl stlleehpdl
      121 svelvmrdgf gdlveegldl airigsiaeg sliarrlgsv hrcvvastdy larrgtpahp
      181 rdllnhpcia ysyggtrhdw qfarkgeaet tvaasgpfra nsseavlqav raglgigmlp
      241 tfqveediaa grlkhllpew tipelpfyav htgprtlplr trtvldflie isdvlrqg
//
LOCUS       WP_010509175             854 aa            linear   BCT 01-JAN-2025
DEFINITION  penicillin-binding protein 1A [Komagataeibacter europaeus].
ACCESSION   WP_010509175
VERSION     WP_010509175.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..854
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91097
     Region          55..791
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtladgsgrd gridgpsrpg aggprrpryr mvrwlagstl avlllgggga allawgeyer
       61 lseglptvdg lrtyqppvms rlysgddqvm aelaaerrif vpysaiperv rdaflaaedq
      121 kffthggvdp mailragltd mmmhgtkhrp igastitqqv arimllgsna vsidrkikea
      181 llamrleqtl skeqileiyl neiylgegay gigaaaqtyf nkpldqldna eaaflgalpk
      241 sptnynphrf vqaatnrrnw vldrmadlkv itpeearaaq qeplvpanft rpgpvpgsew
      301 faeevrreli erygigttme gglsvhtsld shlqqvatta lrdgllrydr ahggwrgafa
      361 hidaadaggd wanalarvta ptamleqwrv avvlspatgr vgwlegrdpv iphtgdllar
      421 drawmrtgkg lqegdvilie pqadgggvav rqvprvegal atvdvhtgrv mamvggwsfk
      481 esqfnratqa arqpgssfkp fvylaameqg ispsqkfdds pvsygewhpn nyekdfwgpt
      541 tlhdalresr nlvtirlaaq igmkpvadla qklglvhsmp lvlpaalgav ettvmreaga
      601 yatianggrl vtptlvddik drngnivwrp dgvtwkagsm aadgpqmedt rpqvvsatsa
      661 sqivammqdv vrrgtgvrag agidrpiagk tgtsqdfnda wfagfspdlv tvvwigfdtp
      721 qslgknetgg aiagpiwnqv mktalasrpr ldfrvpegvq larydtgmgm aidafkpgqv
      781 pgvsvdlgag sgmaltaadt gaenmpdset dmatmpgspa aagdgstsag hpgapsrpaa
      841 sqpsggdigm ggly
//
LOCUS       WP_010509183             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Komagataeibacter].
ACCESSION   WP_010509183
VERSION     WP_010509183.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..256
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=27352
     Region          36..242
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mtrqhrnqvi aaalltalpa layatpaaaa dsnpyglgal wsngdfiart vliimvvmsv
       61 gtwyimitkf leqarilkda kevkakfwpa hdikegaall dtaspfryia dtgikaaehh
      121 egtmqetidl hswttmsiqr svdfiqnrlq gglaflgtvg stspfvglfg tvwgiyhalt
      181 aigiagqasi dkvagpvges limtaiglgt avpavlgynm lvrrnkgald evrnfaadvq
      241 silmggyrhe thdaae
//
LOCUS       WP_010509279             345 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Komagataeibacter europaeus].
ACCESSION   WP_010509279
VERSION     WP_010509279.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..345
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36780
     Region          86..289
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpdpatvsrp glltrlllgg mklraarrah ephtledmra rldrpcfpma lsslqvrrvi
       61 acrvpgsrgm lsarlyvpyg rvhgvvlfmh gggyvhcgln shhgiccrla rqsgaavlsi
      121 ayslapenhf pvavddcwaa lrwlageahr wggpiavagd saggtlaavl aqmardrggp
      181 elamqllyyp slygerdvps rqtyasgyml stklmewyae qyirtpadlr dprlapiyas
      241 slaglapavi glaqcdplhd egtgyaaamq qagsaaetrt wrgtvhgfln fyaflpagre
      301 airygahalr ralrgarvvs aaaggtppvt aspsvpsgqs drsaa
//
LOCUS       WP_010509425             208 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Komagataeibacter
            europaeus].
ACCESSION   WP_010509425
VERSION     WP_010509425.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..208
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23199
     Region          11..204
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpltqlhnpl agverhyvnr qefmtesmpa nmhfhvvsgg arlfkslpdg rrqiigfahk
       61 gdvlpaypct hyhysaeamh tlrvtcvptp ylrhlhetsp gacaaslhta rqvlvglhnr
      121 llmlgrqtar erlaaflvaq gtrmgrgalw pvdpaisrad iadflgltte tvsrllsafh
      181 reklisrqrr aihildldrl raivahse
//
LOCUS       WP_010509481            1102 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Komagataeibacter
            europaeus].
ACCESSION   WP_010509481
VERSION     WP_010509481.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..1102
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=119074
     Region          1..1083
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnlcrifilr pvattllaaa ivlsglfayr vlpvgdlpdi avpviyvman qpgaspqqma
       61 ssvttplerr lgqiagisei esdssqdnaf illtfndstn idsaandvea alraaradmp
      121 atlesqpqyw kanpsenpim ilaltsdtqp mselydiakt rlqpllsqvq gvgwvelmgs
      181 sapavrvein pwplfkyglg fedirsalas anantpkgvi endttrytla tndqarsaaq
      241 yrdlvigyrd srpvrlqdva yvhngvener qvgflnghra amaiilprag anvirvtdqi
      301 karlpalraa lpagvtltpa mdrsitiras ladtqwtllv svllvvavvl vflrtprstl
      361 ipaitvpisl agtlaimslf hfsldilslm altiatgfvv ddaivvleni arhmeagmgr
      421 measlkgsre igftvmsiti slvavflpll llggtpgkvf fefsmtlait vtvslvlals
      481 ltpmmcslll evshdtplpp dapwwrrwpr magdwleagy qnllrfyert ldvalrhhvl
      541 tavtlplsla imigvivlmp kgilpkedva mvmsffradq ttsfpamtek iraisnalta
      601 dkdtqevvaf sgdtniegqa faqmvdrtrr ddgpdemier ihkrlanipg ldvslfsagd
      661 isggggrqke gayrylltsd dadalytwvp altsalrtap alrdvttdvm nngaaihadi
      721 irdlaaryli tpqlvsntly dafgqriasn istslatyhv vmevadqyrt spdilqsfri
      781 staggspggg tvsntvrarm atttqastst qlsqqsfrne ianrlaggtg asngsavsss
      841 tetmlplsnv arleprptai tvshkagfvs aaisfnlapg malsdaatti adtmvrlhvp
      901 qtihggftgq aaqfqsaiin evlifiaalv tiyvtlgily esyihpltim stlpsagvga
      961 vlalwalgqe fslitmigmi llvgivkkna ilivdfalha erdrgldarh airdaciqrf
     1021 rpilmttlaa algavplitn sgygvemrrp lgitvvgglm msqlltlytt pviylymeri
     1081 rlwtrrtmgr llsrtkgqen fr
//
LOCUS       WP_010509503             249 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Komagataeibacter europaeus].
ACCESSION   WP_010509503
VERSION     WP_010509503.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..249
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27213
     Region          14..193
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(17,19,104)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(49,103..104)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            102..104
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 msgngaddrp ivsiiaavln egpnirpvcq eisdvlgqlp gaevifvddg stddtvaqle
       61 avrhdgilpd lrilghdtvy gksaglrtgi eaargewvil mdgdgqdnpa dfaamlemcr
      121 makgraplvv gvrtrrrdtm srrlasrfan glrrrllddg cpdtgaslka frrvdflglp
      181 qfeglhrflp slmgrrgvpl aclsvdhrtr lhgsskytnl nraivgirdi lgvmwlnnra
      241 ripkrvter
//
LOCUS       WP_010509635             430 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Komagataeibacter europaeus].
ACCESSION   WP_010509635
VERSION     WP_010509635.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..430
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46085
     Region          2..409
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msmtfadlsl apsllsalae egytsptpiq arsipllleg cdllgmaqtg tgktaafalp
       61 llhrlattpr papaggarvl vlaptrelvs qiadgferfg rhlrpsvtti fggvsqfhqi
      121 nalkagvdii vatpgrlldl inqglcdlsq lealvldead qmldmgfakp ierivaalpn
      181 drhtllfsat mpksitalae rllrdpakve itppsttvdr ieqsvmfvda adkkaallal
      241 lqtpgmgqav vftlqknian evcafiteag itaealhgnk sqgqrerald afrsgaaqvl
      301 vatdiaargi dvdtvthvfn hdlpslpesy vhrigrtgra grngfaitlc daeqrawlrd
      361 vereigrplt vqadhpwhse aarnstmrpp vlgggpvkqv kpqkkrerkv wteeeknaar
      421 aaaraaaeta
//
LOCUS       WP_010509646             418 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome-c peroxidase [Komagataeibacter europaeus].
ACCESSION   WP_010509646
VERSION     WP_010509646.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..418
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=45701
     Region          53..410
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mdtmisrllg valrgmyvis allmvtpasa qatqgapmsr iqarsraqal svlgrdlfhd
       61 vrlsasgyma csschddtha fapanslpvq yggpdmrqqg hravpslmyl qdvpqfaehf
      121 fdsedeades ldngptgglt wdgrvdtarg qgeipllspy emanasrrdv lrrvlaagyg
      181 prldtlvrpp tddrfalive alatyqqepg lfypysskyd avlagrarls pleargldlf
      241 eradkgncas chvsqpghdg tppqftdygl valgvprnra iglnanpayf dmglcgpdrt
      301 dlsdhpeycg lfrtpslrnv atrhvffhng vihslrqava fyalrdirpq lwyptgpdgr
      361 vriyddlpar fhaninmdpp fgprpgnrpa lsddeidavv aflgtltdgy fhpagnvr
//
LOCUS       WP_010509966             547 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Komagataeibacter europaeus].
ACCESSION   WP_010509966
VERSION     WP_010509966.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..547
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58919
     Region          10..540
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 matgtddfgd fdyivigags agcvlanrls adprnrvlvl eaggndnwiw ihipvgylfa
       61 mgnpradwmf rtdpethlgn rvlnyprgrl lggcssingm iymrgqaady dgwrqmgntg
      121 wgwddvlpyf ikaednfaga safhgvggpl hvdrqrlrwk lldafrdaaa qagiakiddf
      181 nrgdnegssy fqvtqkhgfr wsaargylhp vmkrpnlrvq tgalvhrvlf rdgraigvrf
      241 eangvvrsvh araevivsag aigtpailqr sgigpgerlq afgievvkdl pgvgenlqdh
      301 lqirsayrvs gvetlntevg sllgkarigl qylltrsgpm smapsqlgif arssaryata
      361 nleyhvqpls laafggdldp fpaftaavan vrpesrgsvh lksadpavpp aihpnylste
      421 edrrvaidsv rltrrivaqs alaryrpeef rpgpslesda dlekaigeia ttifhpvgta
      481 amgqgsqavv dhelrvhgma glrvadasim pritsgntna psimigekas amilnaarsp
      541 stpalva
//
LOCUS       WP_010510130              74 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase, partial [Komagataeibacter europaeus].
ACCESSION   WP_010510130
VERSION     WP_010510130.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 74)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         <1..74
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          <5..69
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 gvvmalerll gipasqmvtl gdqpndvlmf rksgmsiamg qaspevqkqa thvstsceee
       61 gfangiekfv lgda
//
LOCUS       WP_010510147             311 aa            linear   BCT 01-JAN-2025
DEFINITION  hydrogen peroxide-inducible genes activator [Komagataeibacter
            europaeus].
ACCESSION   WP_010510147
VERSION     WP_010510147.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Jo,I., Chung,I.Y., Bae,H.W., Kim,J.S., Song,S., Cho,Y.H. and
            Ha,N.C.
  TITLE     Structural details of the OxyR peroxide-sensing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 112 (20), 6443-6448 (2015)
   PUBMED   25931525
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..311
                     /product="hydrogen peroxide-inducible genes activator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34158
     Region          8..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..296
                     /region_name="PBP2_OxyR"
                     /note="The C-terminal substrate-binding domain of the
                     LysR-type transcriptional regulator OxyR, a member of the
                     type 2 periplasmic binding fold protein superfamily;
                     cd08411"
                     /db_xref="CDD:176103"
     Site            order(108,111..112,115,119,127..131,224,231..232,235,
                     238..239,241..242)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176103"
ORIGIN      
        1 mlpmpsaqql rylvtlaelr hfgraakaca vtqstlsagi lalerqmdvr lldrdvgkkv
       61 vftplgdkvv vrarvaleal qgvldvalas repmsgplrl gviptigpfv mptlvrrlpa
      121 aypqlrlsln edvthnvmek laagrldlvl lampcdcads etlplwrdpf mvvmprnhpl
      181 ahlpdvpvrs ivrermille dghclrdqtl amcrqvrgwt qpedeaecav sslytmvemv
      241 aagmglallp rlavesplma gqdvvvrpvt daqawrtigl awrprsprta dfqtiapffv
      301 pdsitdtilp l
//
LOCUS       WP_010509968             291 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Komagataeibacter europaeus].
ACCESSION   WP_010509968
VERSION     WP_010509968.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31733
     Region          1..>144
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..287
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,217..222,
                     228..229,231..232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdintlrlfi avvreggfsq aakavlstqs tvskavkrle delglvlidr aapgitltda
       61 gnvvlrrart ilaerddllv elrelrglkr gelrlglppi gsdtlfaptf vafrdrypgi
      121 gihliergcq dlkdllrage idlaglllpl sdefawqdvc vepvvavvaa ahplaarrsv
      181 pitafadsaf llfetgfsln qivlaacrrn gfmpkvtars tqveflfdli aaglgigflp
      241 rmmvetrqhd giraialdgp gmlwhmtlaw rrggylsdaa kawlelarrp d
//
LOCUS       WP_010510181             347 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Komagataeibacter europaeus].
ACCESSION   WP_010510181
VERSION     WP_010510181.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..347
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=36320
     Region          9..335
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(48..49,133,137,140,158,161..163,182..183,187,202,
                     226..227,248..249,251,274..276,324,329)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mtqaipdtmq avtfsqpggp dslcistlpv prptggdvlv rvmaagvnrp dimqrqglyp
       61 pppgaspllg levagevvat gpdvpadsfp aigarvcalv ngggyaqyct vpagqclpwp
      121 agfdaihaaa lpetfftvws nlfmtaglkp gesvlvhggt sgigtttiql vramggtvya
      181 tagtddkctl cttlgaaaai nyrtedfpqr ikaltqgrgv dvildmigga yldgnlrsla
      241 tagrlviial qggakadgvs larimtrrlv vtgstlrprs tayktaiarq leervwplla
      301 qrtirpiiha tfpfarvada hklmengthm gkimldlqhl pidmtgr
//
LOCUS       WP_010510234             325 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Komagataeibacter europaeus].
ACCESSION   WP_010510234
VERSION     WP_010510234.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..325
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34830
     Region          83..291
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mphnpvapef raalkvlpsf dglsdatlee trkafisair svrvaghpdv lvgechvpgp
       61 agapdvpvvt yrpvasspna palvyihsgg ivsgtpevdd arcrqmvsel glvifsvdyr
      121 lapeapcpaa iedcyavlkw ahdhapdlki drnrliiggd sagggltacl allardraei
      181 kvlfqlliyp mlddrtgttl mpspalgeyi wtrsanhyaw naylgntpgs pgiseyaaaf
      241 ratdltglpp ayigvgsldl fldedleyar rlmaagvpte vcvipgayhv fdvfipdapl
      301 srqfrasyft alkraisqdf senpt
//
LOCUS       WP_010510314             367 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Komagataeibacter europaeus].
ACCESSION   WP_010510314
VERSION     WP_010510314.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..367
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39609
     Region          5..341
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(24,26,58,100,228,295,315,317..319)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(24,26,58,100,102,109,176,179,181,228,235,295,315,
                     317..318)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(26,102,176,179,181,318)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            181
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtdllftpkf vgslllkhrv vmapltrmrs spgnlpndlm ltyytqratp gglliseasp
       61 valsgygfer aagiyddaqi agwkritdgv hakggrmiqq lwhvgrqsar ilqpggsapl
      121 apsairadgv awtlqgtvpf dtpralerde ipvlvaayra aaeralkagf dgveihgang
      181 ylpdqflqdg anrrtddygg pivnrarflr evtqaamdvw gparvgirls psgsygsmsd
      241 sdrhatfgyv ahmleemgag ylhivqprlg ldaednpvda aalrplfsrt iiaaggfahd
      301 sadrllasgn adliafgraf ianpdlverl rhgwplnayd rttfyggdah gctdypfhdv
      361 pvkemqa
//
LOCUS       WP_010509692             369 aa            linear   BCT 01-JAN-2025
DEFINITION  LptF/LptG family permease [Komagataeibacter europaeus].
ACCESSION   WP_010509692
VERSION     WP_010509692.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Owens,T.W., Taylor,R.J., Pahil,K.S., Bertani,B.R., Ruiz,N.,
            Kruse,A.C. and Kahne,D.
  TITLE     Structural basis of unidirectional export of lipopolysaccharide to
            the cell surface
  JOURNAL   Nature 567 (7749), 550-553 (2019)
   PUBMED   30894747
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..369
                     /product="LptF/LptG family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40425
     Region          16..366
                     /region_name="LptF"
                     /note="Lipopolysaccharide export LptBFGC system, permease
                     protein LptF [Cell wall/membrane/envelope biogenesis, Cell
                     motility]; COG0795"
                     /db_xref="CDD:440558"
ORIGIN      
        1 mklrlrlacg tvllgylsre llskvfttta ivvalmeila lleqateimh rklglsgvly
       61 yavlhlplll gnampiavli gtlltllqlt tsneisimra aglstpglvk lllpttvalg
      121 llcgivddqi tprteqalaq wwnattphaa knrhnywira dndlinityl sgggtmmdkv
      181 tvyhrdprsl lqkittladv hyihghwygt pthvlsvvsp srvdlldtpp dqsvrlnwpa
      241 sltpgyiiql tvsftqsint mldeqrgvlp ssqspsfflt eilgrimlpv tftvmlllav
      301 pvvyipprag trswlpiwcl gagllfivfq gllralgnag tlpslmaifv gilifilgvi
      361 tvllrieer
//
LOCUS       WP_010510316             304 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Komagataeibacter europaeus].
ACCESSION   WP_010510316
VERSION     WP_010510316.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33433
     Region          10..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(105,109,148,162,165,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(106..107,111..112,114..115,118,122,124..130,192,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mnktpslpel taflavarhq sfriaadela lspstlshmi raleerlelr lfhrttrsva
       61 pteagaqlva qlapilssle qtlatvgmlk arpsgtlrin asrhaarall rdimpffvhr
      121 ypdvhvdlvt ngrfidivae gfdagirlaq avpqdmiavr fgadgrfvav aspdylathg
      181 iprtpddllh hacirfrlpg grlyrwefar ygqdhvmdvt galtlddmdl mvdaasagqg
      241 iafvseetar ealekgrlai ilddwspafp gyalyypghr lvppalrafi dvvkelqarq
      301 ietp
//
LOCUS       WP_010510411             770 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Komagataeibacter europaeus].
ACCESSION   WP_010510411
VERSION     WP_010510411.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..770
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83811
     Region          76..755
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mrpyflrhsf rlltavpayv glpalsclll astsplaaaa tasanapsvd tkhvatrhst
       61 aaprqqgiaa rkasaeqitv trshaqryla tpgtvntisg qelrslhles pkdvaaftpg
      121 vtatnavsgs apifsirgvg lddyvgtnmg gigiyldgvf apfpvfytgq mldiesvate
      181 kgpqgfdmgr sttggsiniq svkpsdkfgg yaewgyssyn tnrgrfaint pitsrisnrl
      241 afnyvkgdgw qkdlstgary gsqdllairn ltrftiddts slllnlhytr dkgtstspqd
      301 igpvssgdtg mnpsanavsv gnavpqrnen ggglsinytk afdfgdfsst taidfyrrdd
      361 tdnydgsaih vsdyrwndta iaqshdmhlr mnpakifhlt vgvfesydki dgaytsdrmq
      421 svseidltnh fsqqnlstgv yvntvtnitk kldfiasgrf sydergfdgg siysaigads
      481 prllapynah vgdaltgvne rhdyhrftgr vglryqivpg tyaygtisng ykagsyfaap
      541 vlaagaldyv kpenliayev gikssllhdr levegslfdy eyhnrqtlff apitpttnsl
      601 tlgtiprart rggelsttlh nlvpnldirg sfayldaqvk spvnyingls ldpavahnsp
      661 lpfaprfsws aiarynidvn hyrvtlqasy twkdnmwtal gdnnaksski sslglrmevg
      721 pktgkwtaav yvdnlqnnkg slysftgsdn nrvqyiqtpr wvgcelhynf
//
LOCUS       WP_010510422             237 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Komagataeibacter europaeus].
ACCESSION   WP_010510422
VERSION     WP_010510422.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..237
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25124
     Region          4..233
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mnasslalvg fevdgwgrll vmaagltlaa alcsfavggm lgtagavlkl spvatlrwvg
       61 ifyttvfrgi peilvvylfy fggslalthl mhlagfpgff slpsfvigvl aiglvsgayq
      121 tevyrsaylr ldrgqveagl acgmgrvvll wrivapqtll falpalgniw qsvlketall
      181 siiglvellr qstiaagatr qpllfygaaa fvylvmgqvt gigirsverh lsrcrgr
//
LOCUS       WP_010510500             216 aa            linear   BCT 01-JAN-2025
DEFINITION  SOS response-associated peptidase [Komagataeibacter europaeus].
ACCESSION   WP_010510500
VERSION     WP_010510500.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..216
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=24164
     Region          1..215
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcnlyamtgs qqaireaarv mtdrtgnlrp lpeiwpntma pivrnaqdgr elvmarwgmp
       61 tppgylkghr vdrgvtnirn ptstwwkrwe gvahrclvpl tafseperlp dgtsrpvwfa
      121 rsdgeplaff agiwcqwtsv rkladgettd dlfgflttta nrevgaihpk ampviltrpe
      181 eldlwmqapl ddalqlqhpl pdnalkmvha ppvgsy
//
LOCUS       WP_010510539              93 aa            linear   BCT 01-JAN-2025
DEFINITION  HU family DNA-binding protein [Komagataeibacter europaeus].
ACCESSION   WP_010510539
VERSION     WP_010510539.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..93
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9663
     Region          1..92
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mkvsdlveiv ateadlsnad trkvidavve amtqaairge evtlpnfgkf kvkdvpareg
       61 rnpatgatiq iaasrklgft pakalkdaln ggk
//
LOCUS       WP_010510783             540 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Komagataeibacter europaeus].
ACCESSION   WP_010510783
VERSION     WP_010510783.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..540
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56891
     Region          62..458
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(69..70,73..74,77,108,158..159,161..163,166,186,
                     189..190,193,318,321..322,325..327,330,358,362,416..417,
                     421,425,441,444..445,448..449,452)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mldalragfs fsmirdvalp alhdwlhdrf ltlqdpfvqp sptvatvsay tpatrilvfs
       61 gliltmvmaa ldqsivstal ptivtdlggl ahmswvvtaf mltstiatpm ygklsdmfgr
      121 rpllafsiga flaasllcgm aqdmwqlivf rglqgigagg lmtlsqtvig dmvtpqqrgr
      181 yqglftgafa vssvtgpflg gvltsalswr wvflvnlpvg glamalvmlg lptaraearp
      241 ridyagaall gvatagflll fnsvgttlgw tspltfallg asvaffvlfi rqerrapepl
      301 vslgllrias fsvcvaatgi msfammgslv flplyyqlvl gqtpetsglm mlpqvgtmmv
      361 ssvvggyvss rtqryaplla lgvgieftal tlialcahhg apalffllsl gglgvgmgig
      421 mpnatviiqn svppgmlgia tammsfirsl ggslgvalsg gvmaltlqnr lhalpekidv
      481 taflekgmaa vhglspemrl qvreayktai saslsvsssf mflaflmivg lmvrnrrpsa
//
LOCUS       WP_010510847             833 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Komagataeibacter europaeus].
ACCESSION   WP_010510847
VERSION     WP_010510847.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..833
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90507
     Region          102..806
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mcldgksltg sypsrrstpl lrfsvrvssh rfflalttal vlitprgvtl artisthaah
       61 aqharpvtap htgtaqpqgv ratggteqir vgasvvhsad gvtgrapggg liqkqtapka
      121 rstvtpdyim kqspaqnayn avkllpgivv antdpaghek salsmrgltq dqianvwegm
      181 plssiggynl dvawvtdsen igsvsvqpgs snldtpaing sggmfefktr dpskkfgglg
      241 dvgvgnrdyt rqflrvdtge wgktgirsyi sfsnqhdtfy hgpgqedfkh idfkvlkewg
      301 dgnrvslvgg ftrgiignep ywdmtmaswk qkglknelag synlndaagg tdywklnwlh
      361 sktfniaaps hfnfgrlald vtpyvaanqk vygsgfnlnd qvydgygssp qsisipgqva
      421 gqtygvteqy sslnemrggv naklsykvgh hhiylgywfd ydnstnlvgy tgvssagdpt
      481 tswgrardsl rltngkvfys qnysdistvn giyagdtvtl lngrlvldgg mrvtmihrdg
      541 tdnipglqrk vsanefmplp tlgghfqlnk yvqvfggvst gakappdsam ittinpntgq
      601 ianqgqthih deyniteevg mrytgkyiig sftyfhynls hhqvstsmfl gneaigqvid
      661 agnqttngfd aeigtrpihh frpyasmqyl hstidnniqg lptkgkmavd tptwaaslgv
      721 dwdngiffwn yglnyfskqy stfmnqealp slytmnatvg arlprnslvg rglsflkspe
      781 imlwvnnmid thaysainsi sltnttigkv qgtaptyntl grfsavvtfr agf
//
LOCUS       WP_010510823             300 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Komagataeibacter europaeus].
ACCESSION   WP_010510823
VERSION     WP_010510823.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33547
     Region          8..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdnrigemqm flrvvesgsf seaarlsmtt pstiskliar vetrlgvrll erstrrlsvt
       61 pegqlyyera qaliaelddm ehaltkgavr pggivrinas vafgalalep llpefwdayp
      121 dividlslsd eltdlyldrt dvafrvgplq dsnltarhig tarrkivgsp dylnrfgtpr
      181 siddldhhkc lgfnfrraap vwplqekgri vdrivrgpll anngetvrrl tlrgaglarl
      241 gdyhvrddik agrlvevlah adaqdeeeih alylgskqtp qrvrvfldfv iprlqaylra
//
LOCUS       WP_010510909             124 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YidH family protein [Acetobacteraceae].
ACCESSION   WP_010510909
VERSION     WP_010510909.1
KEYWORDS    RefSeq.
SOURCE      Acetobacteraceae
  ORGANISM  Acetobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Acetobacteraceae"
                     /db_xref="taxon:433"
     Protein         1..124
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13001
     Region          2..118
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 miprytdhaa nertflawlr talaivafgg vlakfdlflr laadqhdaaa prpygvtael
       61 gvvfvalgvv lfaaayrrfq atrtaiaadt thysvgpgme raltialgal gcavlvaltr
      121 avvs
//
LOCUS       WP_010510947             462 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Komagataeibacter
            europaeus].
ACCESSION   WP_010510947
VERSION     WP_010510947.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..462
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49841
     Region          9..406
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mstserdalk rifgntgfli agratnaics fvyiawavra lglsqfgvlm lvttfgaavs
       61 qathllswqp llhygtdpft ngrqaqfsrv lafciradyi sggvgwlvgt lgvalfgaym
      121 gwpaadqgaa faymltiafm ntswsagvfr lcnsfwltml tdlsgalvrt vgsgigfmyh
      181 mgldyyllvw smtqlvmfis stslgwlqlr hagatqrfsl faplkagdap giwrftlsts
      241 cnhllgsvfn qfgtllvggi lgpadaavyr vsrqigegia kpaqlmmpal ypefirlree
      301 qdwygikrvt iklflmiggf sillmgvamg vgnilltwml hvhwhggrsl imlmlgsail
      361 glgvvplepl ltvigqvsqv lkgriivtlt ylplvygmtm awhlegaaaa avvaglimlg
      421 vclrpvvvwf rrmapgrrpt gmvkgeaapa tvppvpekgt gt
//
LOCUS       WP_010511049             288 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Komagataeibacter europaeus].
ACCESSION   WP_010511049
VERSION     WP_010511049.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..288
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29900
     Region          7..262
                     /region_name="AztB"
                     /note="zinc ABC transporter permease AztB; NF040871"
                     /db_xref="CDD:468808"
ORIGIN      
        1 msilsvlwdp fasfgfmrra lvasmtlgmg agpvgvmlql rrmsligdam shailpgaav
       61 gfllagglsl tamgiggiaa glgvallagl vsrrtqlaed asfasfylts lalgvlivsa
      121 rgsnidllhv lfgtilgida salclmggit tlsivmlsii wrplvmecvd pgfmrmtggr
      181 ggiyhmvflf lvvinlvagf ealgtlmsvg mmmvpaatar lwtrrllpmm vlsaatgmaa
      241 gligllvsyh yrlaagpsii ltcsvlyils lvmspaglra grhvhets
//
LOCUS       WP_010511053             209 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Komagataeibacter europaeus].
ACCESSION   WP_010511053
VERSION     WP_010511053.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22644
     Region          1..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtfhtwllfa atafvlsamp gpnmmhvmst sirygllrsv gvmtgcmlai vlvviaslag
       61 magilvaspr lfmvlrviga aylvflgvrv wrardvadsd gadmgcvpvv tmralfrdgf
      121 ltgisnpkll lfaaaflpqf inpaaprmpq yvtlvmtfam vevfwyvvya sggrvlsawl
      181 rtpevhrifc lvtglvfigf gamllltqv
//
LOCUS       WP_010511212             278 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Komagataeibacter europaeus].
ACCESSION   WP_010511212
VERSION     WP_010511212.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..278
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30865
     Region          12..273
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mttsipllkl ndghkipamg fgtypldnpq aekavreala agyrlfdtas rygnesgvgt
       61 glvsfdigre difvttklrg adqgydstlr afdeslerlk msyvdlylih wplpakdqyv
      121 eswkamirlk kegrirsigv snflpehlqr lidetgvtpa vnqiemhadf aqselvalhk
      181 klgilteaws plgrgkllen pvvkrvadrh gkstaqvllr wvidygavpi pksahpdrmr
      241 anlhafdfql tpddmsdlat ldsphnrtgg dpatyvee
//
LOCUS       WP_010511348             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Acetobacteraceae].
ACCESSION   WP_010511348
VERSION     WP_010511348.1
KEYWORDS    RefSeq.
SOURCE      Acetobacteraceae
  ORGANISM  Acetobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Acetobacteraceae"
                     /db_xref="taxon:433"
     Protein         1..205
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22703
     Region          4..>196
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mgqraviycr vstadqsctr qkdelqrfae ragyevlgvf metgsgvrvd raerrkvmal
       61 aqareidail vtelsrwgrs tidlistlqe lesyrvslia itgmtfdltt phgrmlatvl
      121 agiaeferdl iservksgla aarargkvlg rqkgerpksd rlapkvmalv aekrsyrwia
      181 rdlgiskntv aaivqrdkvr pslps
//
LOCUS       WP_010510443             524 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat-containing sulfotransferase family protein
            [Komagataeibacter europaeus].
ACCESSION   WP_010510443
VERSION     WP_010510443.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11929146
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..524
                     /product="tetratricopeptide repeat-containing
                     sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=58364
     Region          6..>253
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(114..115,117,141,144..145,148..149,151..152,175,
                     178..179,182..183,186)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          139..169
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          279..471
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mtgnirqary alsrgepvqa rniaamilar epglaeayfl lglsevtlgn irpgtahmeq
       61 avalgrsaef faqlvrclll lrrdadaaaa lreaeiclea geksdaltrd tigcayarlg
      121 ehtasvphfe aavrgqphhe qflynlaval sfvgrvread qtferllsca pgharahhal
      181 srlrrqtaes nhvprlnaah aatrdpedrl llgyalskel edlgdtqasf rtlwdanagh
      241 rknlpysfdr daaifdaiek nwplfaqapv snpsdeapvf vmgmprtgtt lvdrillsrp
      301 dmvsagelqa fpiavkiasr vrtpmvldpe tvahaagrdl gtigrayler ahphipkgss
      361 rfsdkfpgnf myagliahal pharliclhr hpmdtvlsnf knlfattsry ydysyciedi
      421 aryyvrfdrl mrfwqkvipg rvleiryedi vedqegatrr llshcglpws eeclafhtna
      481 spvstpsaaq vrrpiyrdal arwkcheadl eparvifeen gisv
//
LOCUS       WP_010511525             401 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor, partial [Komagataeibacter europaeus].
ACCESSION   WP_010511525
VERSION     WP_010511525.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         <1..401
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <11..374
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 lfsplqdrav hiwvlggfyn dlksdydrhe ytpgyaqwag idrpdnleya sivhnktqer
       61 avygeltyhi ikglqitggf ryfdydalvt ggtalplfqt ypgvnysmnh gttgangtiw
      121 kanvsyrfnp nimayftyst gyrvgganrv apcqmpmnpn tqhacalpne mfyepdktrn
      181 velgvrgnff hrrlvftlag ynidwtnvqv pgqtkygnvs itkngaaavs rgfdasvnvr
      241 vtpnftvsat yaytdahltk yspdlvsnvl gsypgrpgdr lpgstknsgs iianytipld
      301 ngrslqlnwa ttyvgsiysr vglegygyrm psyvthraal tyntkqwsld lfvnnltnqy
      361 avtavsndss smrsrdgvte ryyaysvltp rtfglegrvh f
//
LOCUS       WP_010511550             309 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Komagataeibacter europaeus].
ACCESSION   WP_010511550
VERSION     WP_010511550.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..309
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33464
     Region          32..261
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mrlphlhlpy lhvhvhdrpl agdphphnpf hwklyfceai atailmilgl savilltapg
       61 spfssplmhh pyiqtalcgl cfglsgtaaa mtpfgkvsga hinpsvtlaf slakriggvd
      121 alnymiaqvi gaflgtavvy eagrliawwg nmavavryga tvpygqisiw wamwsemfvt
      181 aaliamlywl aahpkwkfit pwsgglffli mnpvtawlsg nsvnfartla palfagqwtg
      241 lwiyvvgpfa gaslavmair mnllgklhll earlvnfghh grvpglddph rklnhpddpd
      301 hvppgagpa
//
LOCUS       WP_010511651            1024 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Komagataeibacter
            europaeus].
ACCESSION   WP_010511651
VERSION     WP_010511651.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..1024
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=108049
     Region          10..998
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mthaylatli rarmlvlggl glllaagima vlglpveavp disprqvlvs vvapglatee
       61 veklitfpve tsmtgipgmt dlrsvsrggv svvyvqfadd tdinldrtrv nermqqarsn
      121 isvpgitvsm gplatgmgei mqfqirgagr slmelnrimn wtvvpqmrlv pgvvdvnvng
      181 gaeetyevtl dparligsnl svgevyravd agnaasgggw ithhaeqqsv vgrglvgsla
      241 dfgniavrtn pdgsavrlrd lgrvragart rlgavtrdgq geivigvvmm esgassnatl
      301 aainralpgi rqalpagvti epyytratlt gqtiatvrdn lvmgavlvvg vlvvvigswq
      361 aalviasvip valvcamagm rqfgisanll slgaidfgmi vdgslvvieh vlsrreeepd
      421 aefiplviss vqqvmrpvgf ailviimvyl piltlqgieg hmfrpmaqtv imallaslay
      481 cficvpvlaa lalggvrpag dtrliaflrr pythmvtwge thprilfggt lvvlalsagl
      541 amrlggefip qldegalavt ttrlpsasld tvlasvtkqe qilrhfpevr avvsntgtsa
      601 iptdpmgvne tdsfiflnpp stwktartqa elvaamddtl rrelpdalys wsqpvqmrmd
      661 dllsgvrtqi avsifgddla mlaelgdrvv aamsgvkgaa dvaaagdgtv plivvdidrt
      721 qaasrnvavq dildtveavg ghigtrpviv dnaiistqvr ldpkrvasta aigalqvrrv
      781 dgqgnvllsq vahvhevdgp prisrdgvrr rmvvqanvrg rdlasyvaea qarvardvkl
      841 pagytmqwdg qfrnlqsamq rleivlpial glifallvva fgavrpallv fvnlpvaatg
      901 givaltlrgl pfsisagigf ialfgvailn gvvlvseiaa lrargmavaq aafaaaesrf
      961 rpvmatalva slgffpmafs esagaeverp lasvvigglv sstlltllvl pslyarvmre
     1021 kdqd
//
LOCUS       WP_010511901            1080 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Komagataeibacter
            europaeus].
ACCESSION   WP_010511901
VERSION     WP_010511901.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..1080
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113686
     Region          1..1069
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mkfiawfvrr pvatllllls avlsglmalp llpvsdlpdv dlpvisisas naggspevma
       61 rtvaaplerh lgniagvtqm mssstrgqts islgfelgrd lngaardvea airaarrdlp
      121 ttpgsdtqyh ranpnatpvl ilavtpgmqs maklydlvnt tlrpmllqvq gvgdvtlmgs
      181 sapavrvemn pllffkygig fedlraalas anahtpkgvi dmgdrrfqla vndqaehada
      241 yrdlviayks grpirlrdva tvtdsmqdvn aaaffdekla ltlmvraqpg anlvgivdav
      301 karlpqlrtl mpsgadiava rdgsavirss lhhtlvtlla scvlalavvw vflrswtasv
      361 aaaiivpccl iaslgpmhla gfgldnlslm altvvtglvv ddaivvieni irmrergmsv
      421 eeaaiagase vaftllsitv svlavflpig lasaltgrlf refagtvgia vtvslvlscv
      481 vtpcltalcm rfaenrttvh tgvgaadlld yekhsgslyr hileiclshp gktalllplt
      541 llvgvfvftr mpkvvfprqd igivsggsrg sgsslaqtkt rlehfsqvll sdpavnhvia
      601 yldtgegash gmvfatlrdl stgrasgtev aarvvarmgk dihaeyhaqa pgnimmrvgs
      661 nssgisyilr seddrllgpa trklakalrr hreftdvdpd vdppgqgitl aidrdtaarv
      721 gvtpqvignt lsdalgqtta svvytthgqy nvvltvenrf qrdpeilkqf wvspsggsas
      781 gssasntirv vtsatastta stgatafrnq ianslaggan astgsavatg aetlvplsvv
      841 aritpsldpv avthigyass aslalelapg aslsqaqsvi dqewrslhlp esitgelqsd
      901 eedvgksthd seiliigavl avyltlgmly esvwhpltil stipsagiga ilalnlfglp
      961 fsgmaviaml lltgislkna illvdfaiha erergltsrd aireacllrl rpivmttfaa
     1021 algalplvlm ggygmelrqp lgialiggll vsqaqtmftt palyllvarc aslsrkaeap
//
LOCUS       WP_010511950              97 aa            linear   BCT 01-JAN-2025
DEFINITION  HU family DNA-binding protein [Komagataeibacter europaeus].
ACCESSION   WP_010511950
VERSION     WP_010511950.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..97
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=10011
     Region          1..89
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mkstdlidri aeatggtkad aktaletvlt sivqaaevgd evslpgfgkf tvrhtaarmg
       61 rnpatgaemq isasrklvfa pakavkdrlt ganqkka
//
LOCUS       WP_010512240             266 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Komagataeibacter europaeus].
ACCESSION   WP_010512240
VERSION     WP_010512240.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..266
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30430
     Region          27..240
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msitapwmat gqtaftfrsr rkkpadlvsi cvtnfnygry ipealdsiaa qthmaldlvv
       61 vddhsdkdds valitawmee nrerfwrctl ivhprnqgps earntafkha vgafvfvmda
      121 dntiypraia rlheaardgg fdatysqley fgkeqrigsa diwdpaqmar enyvdvmali
      181 rrqawtdvdg yshidqgwed ydfwlkfidh gfeaayvpei lcryrmhgns rttndawaah
      241 eslraimafr hpeltaryql lpdvka
//
LOCUS       WP_010512287             313 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Komagataeibacter europaeus].
ACCESSION   WP_010512287
VERSION     WP_010512287.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35293
     Region          9..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mlrdvnrsee mevfvavvea gsfseaarrl nmspsavskl msrlearlgt rllnrstrsi
       61 dlttegerfh reslcileqm taledsllhe tprptgdvrv nmnlpfglqc vldllpgfla
      121 cypgvrlcvd ltdhvvdlve hhadvairig pmrdsgllqr klmethfvtv aapsyleshg
      181 ipetvneler hncltfsfqr htpewkfrde tgqlrtfnpk gnlllgdges mrcltlagtg
      241 iaqlslfqvq edlaagklvp vlerfaahep qtvhavfmgp nrympqrvrv fvdylaknlr
      301 adrrisrdmk svw
//
LOCUS       WP_010512305             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Acetobacteraceae].
ACCESSION   WP_010512305
VERSION     WP_010512305.1
KEYWORDS    RefSeq.
SOURCE      Acetobacteraceae
  ORGANISM  Acetobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Acetobacteraceae"
                     /db_xref="taxon:433"
     Protein         1..204
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22114
     Region          2..131
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(7,9,68..69,72)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            9
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(67,114..115,117..118,122)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(73,78..79,110,113..114,117..118,121,124)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(96,100..101,110..111,114..115,118,122,125,129)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(96,115,118,122,125,129)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(123,129..130)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          149..187
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
ORIGIN      
        1 mligyarvsk adgsqsldlq hdalraagie pgniyddras gsrddrpgla aclkslrdgd
       61 vlvvwkldrl grslahlvnt vkdlsdrrig lrvltgkgaq idtttasgrm vfgifatlae
      121 ferdlirert maglaaarar grkggrkfal tkaqvrlaqa amaqrdtsvs dlckelgier
      181 vtlyryvgpk gelrdygkrv lsla
//
LOCUS       WP_010512407             397 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Komagataeibacter europaeus].
ACCESSION   WP_010512407
VERSION     WP_010512407.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..397
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43290
     Region          43..373
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mkredlaggi reylqqlpap yaqhygvvpp pppeagvmlg daaarhgqal salgeiaala
       61 rtlpdpylis rvlscqeals ssalegthst lnellmvded dqgashatrq vrdyartleq
      121 flpqacsegp alfrlptvla lhqavmqhdp ayrgtpgtlr rdvvwiggtg hiaystynpp
      181 ppdqvaacle aslnymqadg mqqmtqslit rlaiahahfe avhpfsdgng rvgrlllplm
      241 maadgqvply lspyieahrq dyyaalkraq qrldwpplig flsdaiirtv tevqvtrqat
      301 qalkatwrqr rafrkgsaal raldlltdyp vltasrlghl lditppaaqt alaqlcqvgi
      361 ltertgharn riyvaeevlt ilnrpfgeep alpdpss
//
LOCUS       WP_010512438              77 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator, partial
            [Komagataeibacter europaeus].
ACCESSION   WP_010512438
VERSION     WP_010512438.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..>77
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          14..>77
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msspprsspl apkrqrgrdr veailaaatt vfgeksyeaa tmteiaaras taigslyrff
       61 ptkdvlaaav lerygar
//
LOCUS       WP_010512584             232 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Komagataeibacter europaeus].
ACCESSION   WP_010512584
VERSION     WP_010512584.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 232)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 232)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..232
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25949
     Region          17..229
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mqivhklqal ktdcsiqihv iyalimreih trygrenlgf lwvlgepilf cggvailwta
       61 irpshehglp mtaivvtgyv pltmwrhcls hsikafesng sllfhrqvtp lsiilarail
      121 eitgtimagl lvtcgaiflg fmkppqyygm lylglgfhml fstacamifa alsemseive
      181 kmmavvgyls lpftgafsmv nwlpvkyrwy mmlspsvdni emiregqfgl ra
//
LOCUS       WP_010512631             261 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase, partial [Komagataeibacter
            europaeus].
ACCESSION   WP_010512631
VERSION     WP_010512631.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         <1..261
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          4..255
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(4..8,38..39,186,208..210,212..213)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 vladvdgtlv tkdkiltpra iraverlrer gilftitsgr ppkgmkmvid plkisepiag
       61 fnggmmvrpd ftvieartlp adtarrvigi irdhgadpwv yngndwivsk ldaphvareq
      121 wtvkfppvvg nveakldqvv kitgvsddla lmkrlehdlq qalgdtasaa lsqpyyvdvt
      181 nrdankggvv malerllgip asqmvtlgdq pndvlmfrks gmsiamgqas pevqkqathv
      241 stsceeegfa ngiekfvlgd a
//
LOCUS       WP_010512814             799 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LPS-assembly protein LptD [Komagataeibacter].
ACCESSION   WP_010512814
VERSION     WP_010512814.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..799
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89724
     Region          66..798
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mdrpapstra psltrltavl rqfprgllls atmlggmmca lgprdahada ppdgprrsmp
       61 ihapksqpqs panfsgtvsn tdpmtfqadh vaydsrngia twtgnvqlwq ndqimradkv
      121 vydrntgvas argnvamvep dgtvlfteya elsngmrdgi mtrmyarmed narmaangmr
      181 rtgakvndlt rvvytaceic arhperapfw qlraydathd lqhkrlefrd afvdffgvpi
      241 fylpafsmtd psvrrqsgfl tpgftphdry lgtyvtipyy wvidrqsdvt lqglfstrtg
      301 peltanyrry fsnarlnltg giaydthrdi dyintfgqnv dsadnhgiqg yifangqvsi
      361 nrtwragani rwasspnfmr dyrvsgygqd tlnsniyleg fgtgsysrid aegyqgmnqg
      421 iihnqdlpwv lprytysyfg qpdalggrfs ldttdfyvyr engtsdqrgq lslnwdrpfh
      481 nslgqiwnlt lhvesaihra telnqqpnya rttraqvegq vlptvglkmn wpflrsfnhn
      541 tgtqilepiv qflaapntgn stsrnipned slsyeftdst lfalnryagt drldgglran
      601 vglhnnwtwn ghqidvlige sfqehvdhnr ipysglshhl sdvvmgthmv pnqffdfdgk
      661 mrldpyggkv dfadalgsag frhfrvtggy lfepvtpyyy yvrqpydtaa pdiyykpvse
      721 ltvgaasnwd nwhiaaylrr slsrkesvav ggdagyqndc fgldvmylkq yttiggqqsn
      781 stvmfsltfk tigtfging
//
LOCUS       WP_010512841             229 aa            linear   BCT 01-JAN-2025
DEFINITION  YdcF family protein [Komagataeibacter oboediens].
ACCESSION   WP_010512841
VERSION     WP_010512841.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..229
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24956
     Region          22..202
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 maappamtpt pstnrarpsl yrwlagagml aallawlggl awfihdamra ptrpphvdgi
       61 valtggqgri deslhllaqg dadrllisgv dlhatlgdfl rhqarpvplt lwthttlghs
      121 atstlgnade taewvrayhi rslvvvtagy hirramleis rtvpdvrlyg ypirspalrh
      181 llhpatmrlm vteydkwlla clnvarltrp lhglinhadt rpgappvmg
//
LOCUS       WP_010512849             560 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Komagataeibacter oboediens].
ACCESSION   WP_010512849
VERSION     WP_010512849.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..560
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60271
     Region          25..560
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mtianrllfg fmvgvllmvs lgiyalgqir evrdemtiiv trdlsvyrel thiranendl
       61 varrlailah yyahdfetap avledaiagw dekargadsl lagvlsraee agrlarsddq
      121 remfntvasq lrdistqfqm dthgaamlfq airagndagv reqasridsr eqsidllvgr
      181 aaslldhgvq vaetqgaasy dysrrslaig mggavvvali vtfwtrrsim epissimhvm
      241 ervgqgdlat rakvggmged rdevarlaag lnrmidglre iarqsgevtq nldaavaeir
      301 astqqqaasv eeqfaavqet aatvdeiths gaqiskrare vissaevivh ssasgleave
      361 etaramahth dgaeavasni valserteai seiiasvndl sershllaln aaieaaaage
      421 hgrsfavvaa emkiladqsr datqnvrail gdiqrgints vmlteeavkr vsagkertdi
      481 ayrtiermtg gieegvhafq qivastnqqq igieqvmtal qsirqasqqt sagtrnlevs
      541 asnlgklskq lltisaryrt
//
LOCUS       WP_010512862             186 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease [Komagataeibacter].
ACCESSION   WP_010512862
VERSION     WP_010512862.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..186
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21612
     Region          75..134
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mpcdsqylpa lvlnadfrpl syfplslwsw qdairavwld rvsvlseydt vvrspthslr
       61 lpsvialkdy ipsarkpaft rfnvflrdnf scqycntrfp tqeltfdhvi prsrggrtsw
      121 envvtacspc nlikgsymph qirmypastp arptsrrlqe ngrafppnyl heswrdylyw
      181 dtelen
//
LOCUS       WP_010512873             125 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF423 domain-containing protein [Komagataeibacter].
ACCESSION   WP_010512873
VERSION     WP_010512873.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..125
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13004
     Region          6..109
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mptvvrfllc faalaafsgv mggaltahlp drffaeggre marqaiqmqm whalaiigis
       61 vlmiqqgcrv lvsvsgclma vgtvlfstgv altafwgihp gpvaptggsm lmlawlllav
      121 gvmrs
//
LOCUS       WP_010512929             424 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Komagataeibacter
            oboediens].
ACCESSION   WP_010512929
VERSION     WP_010512929.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..424
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=45098
     Region          9..414
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 menavtnair vvalgndgdg maqtpqgrif vpgtvpgdei llaaqngthg tldrivvpga
       61 drvdapchlf gacggcrlqd malpallewk tgrvtetlqr arfdpipalq ahqvsphgrr
      121 rvdlafrrae kqivlglhrr rgdvvdmsec tlldptlfal lpplramlhs lpavraggdi
      181 qinlldsgpd llitmdgtpd andrrilaqf gkkhgipris lqgrppetla ltgpvfhhfd
      241 dvrvvpppga flqparagea fiksavlagl prkglkagii elyagcgtls fslaehakvh
      301 ayegdraala clkqasggtr vlpalrdlnr qpvmatdlak aaavvldpph agagaqiaqi
      361 aagrppcviy vscnpaamlr dltplrdagy rlasvtvidq flwsaevesv cvltlpgasr
      421 rnrr
//
LOCUS       WP_010512990             367 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Komagataeibacter
            oboediens].
ACCESSION   WP_010512990
VERSION     WP_010512990.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 367)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..367
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39815
     Region          53..339
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 meednragqp mrllrravvp llvgagcavv ggqwlqsrqq arivrhddel ldgephdltl
       61 swpsaqastl ynvalrqdff sqyhldvhlq pgaltgrdai adllagrsma avapvlswlq
      121 ayqanadlpa rlvmglqagt frllvrrrlr iakiedlvgr riavlnadma drlffsvilr
      181 rkglnpdtap dwvilppdqi ddalaagtvd avalhdplaw qllnnraldm velvnsvkgl
      241 yaertnlalg vstdlldrtp gaavalvlal shaarwlpeh maeaatlldg rvdgmdqdtv
      301 lqmmrhevlg ispvgndlki qiaryvdelk llgqfpdsld sagyarrisa dilhhghggk
      361 ggavqag
//
LOCUS       WP_010513016             463 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Komagataeibacter oboediens].
ACCESSION   WP_010513016
VERSION     WP_010513016.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..463
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=47821
     Region          4..446
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mtllwnradl laatsghfps ashadiagtg vsidtrtlqp gdvfialkge nsnghahvaa
       61 aldagaaavv ahepcgddpr ilhvddtlva mqdmarfarm rfagrmvavt gsvgktsvkd
      121 mlrhalqacg pthyavasyn nhwgvpltla rlpataaycv ceigmnhpge iaplaamvrp
      181 dvavvttvas shlglmgsid aiarekaeil lalprggtgi vphdvtgaay frdnaataga
      241 tlwwagttad ctvqatdvks dahgsgfdlr lpgwqgharv napgrhmagn amlalaaaha
      301 lgadmghava glatfhpgag rgamarvmhd kvtlldesyn aspasvqaal dllglvatgr
      361 riavlgdmle lgafarhehv sllpavrana divfccgpnm ktlfdtlpss lqggwtpdsr
      421 qlaplvhaal ragdtvmvkg slgsrmrhvv aaiaaddawv gqa
//
LOCUS       WP_010513194             545 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Komagataeibacter oboediens].
ACCESSION   WP_010513194
VERSION     WP_010513194.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..545
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60544
     Region          8..545
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mpseqdlsad vvivgsgvag ssianelara gisvivleag prvdrqhfvd nfrnlenkps
       61 yqgpfpcvpw aehppnqitp nkylhttgpd aeayqqvylr mmggttwhwa gcawrylpsd
      121 felktrygqg rdwalkyddl epfyyqaevm mgvcgpdpav edlgsprrqp ypmealpisy
      181 aaeqfrnlir ektpyrvvhe pqarntrpyd nrptceghnn cmpicpigam yngsysvyha
      241 eaagakfvpn avvyrierds ankrvtavhy ydpdkgshrv tgkyfviaah cietaklmlf
      301 sadeqspdgi anssghvgrn mmdhtgvqvt fisgdkalwp grgpletnvi dnfrdgdwrn
      361 ergaylvhmv ddnqvdlata laiskgyvgr eleeqiryla shtvrlfshn egladpdnrl
      421 tlsatykdal giphpevyyk lpeytvkscd htrglfkdli glmhgtdeqw tpgyfpqdhp
      481 agstimgtdp kdsvvdgfcr thdhenlfia sssvfssvgt gnitltvaal alrvadtlkk
      541 elaha
//
LOCUS       WP_010513280             374 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Komagataeibacter oboediens].
ACCESSION   WP_010513280
VERSION     WP_010513280.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..374
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40410
     Region          8..339
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtqpthdrki ryavigcgqi slqsfipgle raanstlaal vtgdmhkgqa letrygvrvw
       61 hyddlpdlla sgevdavyla tpnalhrrya vpvleaglhl llekpmatsv edceailqar
      121 rrgggrlmia yrlhcepgtv elvsrcrngd fgapvgfssv fgqdvpqsnh rahggywsgp
      181 vpdlgnypin avrhmfgaep vevtatgtrt pgrtfnfddt vsvvlrfadg riadfmvsya
      241 capvegltlf gsrgsvramp cytfgpsvai tyttlidgke drrshgpveq fggeafyfse
      301 cilnnrdpep dgedglrdvr vlvaveaalr tgkpqslppl agregiredq vvilpplaea
      361 cesdltgvmp qavs
//
LOCUS       WP_010513288             309 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Komagataeibacter
            oboediens].
ACCESSION   WP_010513288
VERSION     WP_010513288.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..309
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34278
     Region          28..300
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 msfrmdgqet mkvsekkqaa ttqvppatye elirvihdry arlsnsyqki alymtqnpnd
       61 vavdsvhvaa gkcgvhasgc vrfaqsfgyq gyrdlqtifr hrlstaalgf sarvraleee
      121 ldtredrsem gfmrdlivrd isslqellan vtaqqiarav dlmeqadtiy ligqlrsapv
      181 vellrymltm lgkravllda agglathmar vmlptdmlfa vsfrfyasev vniveetvtr
      241 nipvvaisds tlsplarnad vlfsvpehey tfsrslaapm cltqalvval asrlqnesrk
      301 pripvatqk
//
LOCUS       WP_010513291             156 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Komagataeibacter oboediens].
ACCESSION   WP_010513291
VERSION     WP_010513291.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..156
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=16995
     Region          52..156
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 miarptfvat pvrattarva dpfavlqrqv grliddyrap dtfgsgriga tditedatgy
       61 hiyievpgcs ekyitlnasn gvlsisgekk spmaetdhkm hvstrsfgaf sehfnlpegv
      121 dedkitarik dgvlkvtlpr repakpterr idiqpg
//
LOCUS       WP_010513298             195 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Komagataeibacter
            oboediens].
ACCESSION   WP_010513298
VERSION     WP_010513298.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..195
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21133
     Region          1..188
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 miilygmpls ghvhrvrlll smldleyrfe vvgasapell rlnplgqvpv lrdgdlvlad
       61 snailvylak aygagthwlp ddavgaahvq rwlsiaagel rqgpaaarmv alfgkagepa
      121 dararaagll tfmdrwldgr aylaaacptl adlacygyta hapegsvsle pyphvrawle
      181 riealprfvp lpwwd
//
LOCUS       WP_010513353             317 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hydrogen peroxide-inducible genes activator
            [Komagataeibacter].
ACCESSION   WP_010513353
VERSION     WP_010513353.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Jo,I., Chung,I.Y., Bae,H.W., Kim,J.S., Song,S., Cho,Y.H. and
            Ha,N.C.
  TITLE     Structural details of the OxyR peroxide-sensing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 112 (20), 6443-6448 (2015)
   PUBMED   25931525
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..317
                     /product="hydrogen peroxide-inducible genes activator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34638
     Region          11..69
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..295
                     /region_name="PBP2_OxyR"
                     /note="The C-terminal substrate-binding domain of the
                     LysR-type transcriptional regulator OxyR, a member of the
                     type 2 periplasmic binding fold protein superfamily;
                     cd08411"
                     /db_xref="CDD:176103"
     Site            order(111,114..115,118,122,130..134,227,229..230,233,
                     236..237,239..240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176103"
ORIGIN      
        1 msyiplsgls lrdieyvvav ddlrnfsraa ercgvsqggl seqvrklesl lgvvlfersr
       61 rhvtvtpdga rliamgrdvl aaaramieaa rvrtgplegl vrmgviatlg pyyvpdllpl
      121 lrgaypqlkl qltdsltdtm lrmlrhdeld vvfaalpvgg dgfecaplfr epflaafpag
      181 hplaqrrtla mpdlrgpdll lledghclrd qaltlcgmpp qrdqprlats lemlwhmiga
      241 gegysliprl alrhraaweg litvtalpsa yrtiglvwrt sdprgpafse farflrdnpp
      301 egctpvdtvs sapaprd
//
LOCUS       WP_010513345             510 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Komagataeibacter oboediens].
ACCESSION   WP_010513345
VERSION     WP_010513345.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..510
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54949
     Region          29..499
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,153,
                     156..157,160,287,290..291,294..296,299,327,331,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 mstqpadasg ptppqkadaa awlavaagti galmatldts ivnsalptiq geigassseg
       61 twvttaylva eivmiplagw ferifklrnf lliaavlfti fsmwcglspn lmhmiigrvg
      121 qgftggamip tamtivatrl ppaqrpvgia lfgmtavlgp vigpviggwl tenlswhyaf
      181 flnlpisigl mvllfvglpk gridwgefrn tdyyglaglv lglggltvvl eegqrerwfe
      241 sdmirelsim sllgmillvv gqfrsrqpvi hlkillqksf fgvfvlslgv ggalygilyl
      301 ipqflaavpd ynseqsgiia aisgiptllm lavfpilvrk ldirlaiafg mflyvvscfm
      361 nahlspdsag phffwsqvvr gfaqffsllf lnqaatsavp iqyaedasgl fnaarnlggs
      421 fglaavatlh drrmdlhtar ieetitansp lgqefmqhyg larlsalitr qatvmtygdl
      481 fwifgiallv mmplvilikp mpkdagmtvg
//
LOCUS       WP_010513359             383 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Komagataeibacter oboediens].
ACCESSION   WP_010513359
VERSION     WP_010513359.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..383
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40559
     Region          12..366
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mgsplppspa vtqqaldala arfapragay drsgeiamdn lddcraaglt gltivradgg
       61 qgggirqivn vtgtlatgdp stalilamhf lqhaliarat swpettrrqv ietalrdgal
      121 inalrvepdl gtpsrgglpa trislasgrp vlngrkiyst gstalrwgmv wvatdeaqpr
      181 vgqvlvdlha pgirierswh qmgmratgsh tfvfedvelp etalvdlrap dqwhsndgtl
      241 vighalaiaa lydgvaraar dwlisflhar vptalgrpla tlprfhtllg qidallmtnr
      301 silagaldrt esgdypgtea nlakyvmten airavelgva aignpalsqd nplerhfrnv
      361 lcarihtpqa dvalaaagkv ala
//
LOCUS       WP_010513399             309 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MIP/aquaporin family protein [Komagataeibacter].
ACCESSION   WP_010513399
VERSION     WP_010513399.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..309
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33704
     Region          32..261
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mrlphlhlpy lhihvhdrpl agdphphnpf hwklyfceai atailmmlgl savilltapg
       61 spfswplmhh pyiqtalcgl cfglsgtaaa mtpfgkvsga hinpsvtlaf slarriggvd
      121 alnymiaqvi gaflgtaavy eagrmitwwg hmavavryga tvpyghisiw wamwsemfvt
      181 aaliamlywl aahpkwkfit pwsgglffli mnpitawlsg nsvnfartla palfagqwtg
      241 lwiyvvgpfa gaslavmair mnllgklhll earlvnfghh grvpglddph rklnhpddpd
      301 hippgagpa
//
LOCUS       WP_010513490             477 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpP1/FadL family transporter [Leptospira licerasiae].
ACCESSION   WP_010513490
VERSION     WP_010513490.1
KEYWORDS    RefSeq.
SOURCE      Leptospira licerasiae
  ORGANISM  Leptospira licerasiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Leptospira licerasiae"
                     /db_xref="taxon:447106"
     Protein         1..477
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53139
     Region          32..440
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mnlginitre qkagrskngl arfllilllf fssahsyvhg fqgimptsfg arqagmggaf
       61 qavggsvmdl esnpshlarl ttpkwefgts vhfakieysd sfidqdpnls yrntitetpr
      121 avfpyvgyiq pvtdrlgigf alytqggggg sfsnitrvsp gkqtlnetlg gdvpfgterk
      181 iqedlkfkfm ltkltvgagy rfgnlsvgig ldlayafmem kktnldlsrt velpgsisyn
      241 sdpaysyggk lgfsydlssn iriaysytlr nvlhmdgqmk ieaddpivkn gsrvsrymvw
      301 pdrhifgisy rknswifdfd vkfipwsqsf rtnrfildqp llttpigles nvmqmnfrwr
      361 dqycfalgae yewkygfrfr agysyaktpm tpqglnpmlg ttnehhlagg lgyysvngsa
      421 iqlaveyafp ksmrgsgssd walshsifsd keiqlaqfqf nksvsvlsvs lgiekni
//
LOCUS       WP_010513563             411 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Leptospira licerasiae].
ACCESSION   WP_010513563
VERSION     WP_010513563.1
KEYWORDS    RefSeq.
SOURCE      Leptospira licerasiae
  ORGANISM  Leptospira licerasiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Leptospira licerasiae"
                     /db_xref="taxon:447106"
     Protein         1..411
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=45221
     Region          146..410
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mefdlqrlvi flsvftvill igysyatsrl iapfelgtfq evslwigvvf lvlltpsayl
       61 lslffrethw qkfwaysaft tlgfatilvs fvvfkdlgnl vwkgvvylsd llqpnsisva
      121 saeteallgs ekfgradfla rfssfallgi aggltafgfy qakktptikq vrikvkdlpd
      181 gldgfkivql sdihigptik gkflegvvsk tnslqpdlva itgdlvdgtv gmlkhhvspl
      241 knleskhgtf fvtgnheyys gviawirele dlginvllnq nklidhngak iavagvtdyk
      301 ahtvipghrt dpkqaslgte dahykvllah qpnsifeaak vgydlqlsgh thggqyfpgn
      361 lfihlfqkfv aglskwedtq lyvsrgtgyw gpplrigaps eitllvlekq s
//
LOCUS       WP_010513548             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RlmE family RNA methyltransferase [Komagataeibacter].
ACCESSION   WP_010513548
VERSION     WP_010513548.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Hirata,A., Okada,K., Yoshii,K., Shiraishi,H., Saijo,S.,
            Yonezawa,K., Shimizu,N. and Hori,H.
  TITLE     Structure of tRNA methyltransferase complex of Trm7 and Trm734
            reveals a novel binding interface for tRNA recognition
  JOURNAL   Nucleic Acids Res 47 (20), 10942-10955 (2019)
   PUBMED   31586407
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Caldas,T., Binet,E., Bouloc,P., Costa,A., Desgres,J. and
            Richarme,G.
  TITLE     The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S
            ribosomal RNA methyltransferase
  JOURNAL   J Biol Chem 275 (22), 16414-16419 (2000)
   PUBMED   10748051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..254
                     /product="RlmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=27317
     Region          45..248
                     /region_name="RlmE"
                     /note="23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ
                     [Translation, ribosomal structure and biogenesis];
                     COG0293"
                     /db_xref="CDD:440062"
ORIGIN      
        1 mkqrsstrip gkartssltp gtgdsstdgr aaqanrtktv tvkkargrtt aqhrwlqrql
       61 ndpyvqaaqk qgwrsraafk lielddrfql irpgarvvdl gaapggwtqv avkrgaaevv
      121 gvdllpvdpv pgatiiegdf ndpdmpdrlt gllggradvv msdmapnttg haptdhlrii
      181 glaelaldfa vrilapggtf vakvfqggse kqmladlkrm ftqvrhakpp asrkessely
      241 vvatgfrgld rted
//
LOCUS       WP_010513601             246 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Komagataeibacter oboediens].
ACCESSION   WP_010513601
VERSION     WP_010513601.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..246
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /note="Members of this family of hydrolases with an active
                     site Cys residue belong to MEROPS family C26.; Members of
                     this family of hydrolases with an active site Cys residue
                     belong to MEROPS family C26.; Members of this family of
                     hydrolases with an active site Cys residue belong to
                     MEROPS family C26."
                     /calculated_mol_wt=25807
     Region          21..243
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mkphfpligv tldseppatd drdgysrfpw yairqnymdm iaacgglpva lghdaqqaaa
       61 mvarldglvv tggafdvppd lygasdqhas vqtkprrtia etalvraama rglpvlgicg
      121 gmqllavvlg gklvqhipdt yptalaheqp nprdeaghmv dviagthlar lvgggrlavn
      181 sshhqavada gravicatap dgvveaielp ghpfcigvqw hpefgisagd rllfeglida
      241 arqirt
//
LOCUS       WP_010513603             274 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Komagataeibacter oboediens].
ACCESSION   WP_010513603
VERSION     WP_010513603.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..274
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28931
     Region          12..264
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mndtengsaa fpriialanq kggvgkttta inlaaalats glkvllvdmd pqgnastglg
       61 vgydarrsgt yamledsara aavvqpsavp glsliaadte lagaelelvm adrreyrlhd
      121 alaqigadyd tilidcppsl glltlnalva aqsvivplqc effalegisq lvrtvnsvrq
      181 slnpalkldg ivltmydrrn nlselvadda rsffgdrvme tliprniris eaqshgqpvm
      241 nydhrssgsl ayqalatevv drlglhaark gkas
//
LOCUS       WP_010513623             352 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Komagataeibacter
            oboediens].
ACCESSION   WP_010513623
VERSION     WP_010513623.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..352
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37596
     Region          14..334
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mdnglidirh tgrlgritln rpaalnalnm dmldridacl rawrddgave tvlidsaspr
       61 afcaggdira irdrlathgl eagampfrrs yrlaatlagy pkpvvsfmdg iamgggiglg
      121 ghvryrivte ravlampeta ialtpdaggs yllsrapgms glrlaltggr mnatmaldag
      181 fadrmahstt ldairqalth tpagrvmdsl ppcppmpggp dtaaiatvyd apdlpdllrr
      241 lqahkadwar ddlaamtrac pfslcltlaa yhaartlpdl dhvleqefql vchlllrpdf
      301 aegvrarlid kdnapnwrpe cvnavsphei aaclhdhacs plglgtagpd rr
//
LOCUS       WP_010513646             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Komagataeibacter].
ACCESSION   WP_010513646
VERSION     WP_010513646.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..255
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27469
     Region          39..251
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msdmpscqfe srprrivigs sgvqtdfctt csvrptsvcs vigpddisrl sdaavetiip
       61 pgrgfieega patdffnvts gtvklfkalp dgrrqitgfa spghflglav sdnyafgaea
      121 vdtvrvcrfs rdkmadlldd fpklerrlle easnelvaaq nqmlllgrkt arervasfll
      181 dqmhasqlpg hesnggrlhl pmtrgdiady lgltietvsr tlswmrsqgm ievgkgyait
      241 ivsaakldvl aagnt
//
LOCUS       WP_010513650             215 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira licerasiae].
ACCESSION   WP_010513650
VERSION     WP_010513650.1
KEYWORDS    RefSeq.
SOURCE      Leptospira licerasiae
  ORGANISM  Leptospira licerasiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Leptospira licerasiae"
                     /db_xref="taxon:447106"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24858
     Region          12..178
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkkavkesp ktrdlqktre kilytafqkf fqsgfqatsm ddlvketdls kgafyhqfpt
       61 kfilgyavve evirplilnr wirplqdydd plqgildlmq khicdikpdl irygcplnnf
      121 mqemspvdkg fqtrlksalq lwiqelekel vrakenglil enintqeaas fivmfhegvy
      181 gflkgsgdrk lcghflnmmk nylqsistak rnsir
//
LOCUS       WP_010513681             249 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Komagataeibacter oboediens].
ACCESSION   WP_010513681
VERSION     WP_010513681.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..249
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27393
     Region          14..193
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(17,19,104)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(49,103..104)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            102..104
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mtgngvedrp vvsiiaavln egpnirplcq eiaavlgqlp raevifvddg stddtvaele
       61 avrrdgilpd lrilghdtvy gksaglrtgv eaargewvil ldgdgqdnpa dfipmldicr
      121 ttegraplvv gvrtkrrdtm srrlasrfan alrsrllndg cpdtgaslka frredflalp
      181 qfeglhrflp slmgrrgvpl acysvhhrnr lhgtskytnl nraivgirdi lgvmwlnnra
      241 ripkrvter
//
LOCUS       WP_010513708             296 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Komagataeibacter oboediens].
ACCESSION   WP_010513708
VERSION     WP_010513708.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..296
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31390
     Region          31..259
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mdmtaprqpg srpiedrpla gsphpdhpfh wklygcelva tvvlmicgiv svtvlttpyt
       61 aigrvlgphp ivqtalcglf fglsgtvaaf tpfgrvsgah vspsvslafs lagrlgivdl
      121 cgyvaaqmag aclatvllaa lghvlpgwgr mvqasayaat vpfsgvaivw plvtevvlta
      181 llvlmlcyla ghpvlkwltp wagglfflfc npvsawlsgn ssnlarsfgp avvagqwesf
      241 wiyalgpftg aalaiwlirs rllgrievee arlvnfghhg ripsllhpgr hredni
//
LOCUS       WP_010513749             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dienelactone hydrolase family protein
            [Komagataeibacter].
ACCESSION   WP_010513749
VERSION     WP_010513749.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..220
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23628
     Region          1..217
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mgaditvtaa dghtfsayra grpdaarcvv vvqeifgvtp yirsvcdsfa aegyqaiapa
       61 lfdrvrrnti lpydgtgmqe gltlrsqiaq ddtlkdlvaa admlpaekkg ivgfcwggkl
      121 aweaachtka faaavawygg giaqtrnqvp ncpvqlhfga edahipadev dairaahedi
      181 eiftydgadh gfgctdrpsy neaaatlamq rtlsffehwl
//
LOCUS       WP_010513765             323 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
            [Komagataeibacter oboediens].
ACCESSION   WP_010513765
VERSION     WP_010513765.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..323
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=32889
     Region          5..317
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
ORIGIN      
        1 mthsariavi gagawgtala lqatragaev slwarnpatm sagrvmprlp ghalppritv
       61 sdvmprqadl illacpmqhl rtiarnvppc apliacckgv eeatgllplq vlgemfphsv
      121 lgvlsgpnfa hevaaglpaa avlactdrtq arrladlltt pafrlyasdd ptgvqvggaa
      181 knvvaiaaga tigaklgena raalitrsia elsrlshalg grpetlsgla gigdllltct
      241 gaasrnyrlg laigqgtpaq qaadalegva egratapall rlarqhgvst pviatvtsll
      301 agtidmedas qlllsrpvgh efa
//
LOCUS       WP_010513882             152 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Komagataeibacter oboediens].
ACCESSION   WP_010513882
VERSION     WP_010513882.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..152
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16250
     Region          7..148
                     /region_name="CFF1"
                     /note="Predicted sugar epimerase, cupin superfamily
                     [General function prediction only]; COG3542"
                     /db_xref="CDD:442763"
ORIGIN      
        1 midlrdpstp pesvrqalgl qphpeggsyr eiwrdtpadg prgavstimf llaagershw
       61 hrvdaaeiwc wqggsplvle iapradgpie rftigplpeq gqvmqavvpa gawqaafpeg
      121 awsltgcqva pafvfssfel appgwspqge ae
//
LOCUS       WP_010513896             323 aa            linear   BCT 01-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Komagataeibacter oboediens].
ACCESSION   WP_010513896
VERSION     WP_010513896.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17003057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..323
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=34741
     Region          19..64
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cl09940"
                     /db_xref="CDD:447867"
     Region          87..320
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mndtvppapv iattgdagqr tdrfianvve glsrsrvksl mesghllrdg splrdpaepv
       61 ragmcyeihi ppaipatpqg qdialdilye drdlivldkp agmvvhpapg nedgtlvnal
      121 lahcgegltg iggerrpgiv hrldkdtsgi mvaaktemah qalslafaer ridrayqaic
      181 wgvpspasgs fdgaigrdrr drkrmavian gggkmalthy rvldtfhggl ahvecrlatg
      241 rthqirvhfa haghalvgdp vylrripaas rslppvakda aldfprqalh arrlgfvhpr
      301 sgeemlfeta ppedfrhlls sia
//
LOCUS       WP_010513900             651 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Leptospira licerasiae].
ACCESSION   WP_010513900
VERSION     WP_010513900.1
KEYWORDS    RefSeq.
SOURCE      Leptospira licerasiae
  ORGANISM  Leptospira licerasiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Leptospira licerasiae"
                     /db_xref="taxon:447106"
     Protein         1..651
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=72058
     Region          89..650
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mknwkiwqki lflsaflslp ypfvlyflis eqniriefae kelsgvhllr svmylwkdqk
       61 tdwptkikif dqeneksdlq eglvstweas krefskgiss erqttillel nnrigdisnl
      121 ildpdldtyy lmdivlirip mfhkllgeie slnllqqetk lesiqarlia ksglltetis
      181 gmdrglsvil ekspeygehl qvpyskfksg veslnglisd tngskdyrgr mseellknsl
      241 ntealysaas asleaglikr inglkirnys ilgfifills ipaiglaitl fkvssqignv
      301 vkrmegiaig kgdltqrlde nagaefgeia igfntfveri rlilsdviqv teglkeiadl
      361 nmsvsyslek tstdnfssiq elsatteeia sssefvtstv eeeieslsfl tekagelsnl
      421 iekissgiql vktttesmkq vanesesdls slvktidgis essdkigkiv diineiaekv
      481 ellainasie sarageagrg favvaseitk laeqtsqsil eirkivtnns eearagkvav
      541 dtsvnswrki tsgvdsiflg lnemilllpe emkikdkles sivgikeksm sisastseqk
      601 salqeiaskv yrindsiees ngsakslkvr asemnsqtnk lrelvdsfri q
//
LOCUS       WP_010513952             133 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Komagataeibacter oboediens].
ACCESSION   WP_010513952
VERSION     WP_010513952.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..133
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14840
     Region          3..129
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 marmihsmir vrdeaaslaf ydtafglkva drlvfdtftl iylsndeqtf eleltinhdr
       61 ttpydlgngy ghlavsvadv daeharltaa glsplaikdm scgeqfvgrf ffmtdpdgyr
      121 ievlqrgrpg rfl
//
LOCUS       WP_010513991             247 aa            linear   BCT 01-JAN-2025
DEFINITION  TlyA family RNA methyltransferase [Komagataeibacter oboediens].
ACCESSION   WP_010513991
VERSION     WP_010513991.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..247
                     /product="TlyA family RNA methyltransferase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26244
     Region          5..247
                     /region_name="YqxC"
                     /note="Predicted rRNA methylase YqxC, contains S4 and FtsJ
                     domains [Translation, ribosomal structure and biogenesis];
                     COG1189"
                     /db_xref="CDD:440802"
ORIGIN      
        1 makrrvdqml vdrglvetrt raqalimagl vhtpdrriak ageqipedtp ltlkgqdhpw
       61 vsrggiklah glehfglspa gltcldvgas tggftdvllh egaakvyavd vghgqlawkl
      121 rsnteqvvvl ekcnartldt tiipdpiqal vcdasfiglr tvlpaglelc vpgawaiali
      181 kpqfeagrda vgakgvvrdp avhdavcami hewwsglpgw tvlgidpspi tgpegnrefl
      241 iaarkdg
//
LOCUS       WP_010514362             737 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Komagataeibacter oboediens].
ACCESSION   WP_010514362
VERSION     WP_010514362.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..737
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82807
     Region          11..686
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mdsliptgra pdylnrlnpe qraaiettdg pllvlagagt gktrvlttrf ahillsgrar
       61 pnqilavtft nkaaremrer vsallgepae glwlgtfhal carmlrrhae yvgltssfti
      121 ldtddqlrll kqilepyrid tkrwppqaim gviqrwkdrg lvpdaitaae dtdfangrca
      181 eiytdyqlrl rqinacdfgd lmlhmteilr rhpdvlaqyh rffryilvde yqdtntiqyl
      241 wlrllahrgg qpsniccvgd ddqsiyswrg aevenilrfe rdfpgakvvr lernyrstrq
      301 ilgaasglia hneerlgktl qpgredaege kvrvisvqds ddearmvgse ierlradghp
      361 maeiailvra gfqtrafeer litlglpyrv vgglrfyera eirdaiaymr vvnqpsddla
      421 feriinvprr gvgttglqkm hmharerqip ltaavlemlg agdikgrare qlaalmrtla
      481 ttrdmlgreg hvvaidylle dsgyidmwka dkspdapgrl enlkelvrsl adyenlsgfl
      541 ehvalvmdte drsgedsmsi mtlhgakgle fdtvflpgwe egvfpsqrtl degglkglee
      601 errlayvgit rarklaiish aanrriygnw qsaipsrfve elpgehvetr gdtsnsrrsf
      661 lgrpavfgst pfplvasrrv hdvtpsttat sgmkvgvrvf hqkfgygtit svegnrleva
      721 fekagpkrvi dtfveqv
//
LOCUS       WP_010514295              72 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Komagataeibacter].
ACCESSION   WP_010514295
VERSION     WP_010514295.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..72
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7607
     Region          1..64
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mkvhnslrac rtaqgltqaa laervgvsrk tintvensvf mpsvglaltl arslgvmved
       61 lftlapdepe kp
//
LOCUS       WP_010514036             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Komagataeibacter].
ACCESSION   WP_010514036
VERSION     WP_010514036.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..265
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29186
     Region          6..262
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mtrsgltdsh chldhfsdee mpeilartre agvdgmvtig trlsradqqk klatldtpdl
       61 rvwctigthp dhvdeevlpd vaelvamadd prvvgigesg ldyfhgqpdi rprqhesfrv
      121 hidaarrtgl plvihtread ddtlgilrde tarngafpfl ihcfssgpdl argalelggy
      181 isfsgiatfn raqsvrdvak dvpadrllve tdspylapvp rrgkrnepgy vaytarmlae
      241 lrgvedaafa elttrnfsrl fsrav
//
LOCUS       WP_010514437             206 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Komagataeibacter
            oboediens].
ACCESSION   WP_010514437
VERSION     WP_010514437.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..206
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22930
     Region          50..139
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 msppswsrtv ferlhrrrpd pwgvgtraye hdkyrqtlav lsgrhfsfal elgcsigmmt
       61 arlarrcerv lavdvaeaal erarrrcagl ngvsfyrgqv pdgfpplpar acdlivvsem
      121 lyflsrrdir rlaahclrvr qagapivlvn wtgptdtpct gdeaarhfin acragglhvt
      181 harrypryrl dvvngpdsap pvtdpt
//
LOCUS       WP_010514439            1063 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Komagataeibacter
            oboediens].
ACCESSION   WP_010514439
VERSION     WP_010514439.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..1063
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115031
     Region          1..1058
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnaivvtalr rpytfvvlsi livvfgimsv lrtptdvfpn ikipvvsvvw tyggmlpeef
       61 agriiynyel mvtstvegie hmesssyygr givniyfqpg tdigkaeaev taisqtvikq
      121 lpenipspmv msldassvpv ltlqvtsdkq tpsdlfklam irvrpllvtv pgavvpqayg
      181 gmdsfvmval nqqqlqahhl samdvqnalr gqnivlpagd qkisatdwmv qtnatprsmk
      241 elgdipvkrv gnaviyvhdv aevyrgghpq tnlvlvkgkq gveivvmksg dastldvvag
      301 akallpriqr llppdvkvsi lgdasvfvkd sifdvvreml taaaltgmvv llflgswrpt
      361 viiatsipla ilcaitglhw agqtinvmtl gglalavgil vddatvmien idahlemgkt
      421 lepaiidaan qiviptfvat tcicivwlpl fglsgvagwl fmpmaeaiif amiasfilsr
      481 tlvptmakyl laghsvaghg dshhcqpqvh nlqyprrlpe rfqqafergf nnfregyagv
      541 leraiagrrr fvavflgvsv cslglylvag rdffpetksg tiqmhmrapl gtrievagre
      601 aslvedrinq lfpgkvesmi encglpegah nqafiptpti gtqdcditia lkdeetpvwn
      661 drtilrhdls arfpgtvftf qpadltakil nfgspspidi qisgpdlrdn ydyarllvnr
      721 lravpgaadv viqqtmktpt lfvqgnrtfg qatgmteadl annelmtlsg sqtvdpqywl
      781 dpatgitfpl nvyvsqdqlt hfnnlmtipv dkgdgdpqgr hmqllggisn vsatgtpgqv
      841 shfnsmpevd iyvsaegadl gqvttgvqhv ldqthdrvps taavvvrgqt etmrhayvel
      901 vfglvvsvll iyllivvnfq swldpfiiit alpgalagia walflthtrl svpaltgaim
      961 cmgtatansi lvvsfareri eehgdalraa leagygrirp vlmtalamvi gmvpmamsns
     1021 qnaplgravi ggllvatvst llfvpcvyai lhnrpsrire emn
//
LOCUS       WP_010514461             411 aa            linear   BCT 01-JAN-2025
DEFINITION  NupC/NupG family nucleoside CNT transporter [Komagataeibacter
            oboediens].
ACCESSION   WP_010514461
VERSION     WP_010514461.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..411
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42541
     Region          3..410
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mhirgfigii flicvamvfs tdrkrinlri igaclllqag igllvlrvps gqaalraisd
       61 mvtqvlsygs egarflfggl vgprmhdlfp dgsyvfafqv lpslvyvsal iavlyhfgim
      121 qafarllgrg lqwllgtspv esfgaiitif vgqselpval gpylasmsts elasvmcsgt
      181 asvsgatlvg yfglgipady lvaasfmaip gglmfakmle prapdspvsp idagraayhr
      241 affeavmega mkgaqtavav aamlvacigl ialvngmlqg igghvglpal sleyimglll
      301 aplawmlgvp agecdavgsv lglkvvlnef vaylrlgpdi qagrlsaraa aiasfalcgf
      361 anlsslglav aafgsqcpdr reeiahksar avlggmlsnl msaaiagiim p
//
LOCUS       WP_010514468             453 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Komagataeibacter oboediens].
ACCESSION   WP_010514468
VERSION     WP_010514468.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..453
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49138
     Region          1..441
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mtldtflndl phvaaqtepa ivkrksrdfy wyspalkarl hglaaqavvm prttddvldi
       61 araarrhnvp ltvrgggtgn ygqavplqqg vivdmtemnr vlkvehgvar vqaganilal
      121 drelrgqgle irmfpstkrt asiggfycgg sggigsvrwg glsnpgnllg arlvslavep
      181 evqdlrgrev fclqhaygtt givtevdvpv epviawqdla igfadfaaaa afgrslamqp
      241 gidrklvsvi darlvpyfph lsdvvppgha iviamvapaa vavvddlarq qngsicyraa
      301 mheaeddptr mplyeltwnh ttlqvlkkdr sftylqclhp aqdmlesvdt mtrllgeevm
      361 fhlefmnvgg qiacaglpvf rfttqdrlda iialfrahgv svanphvytl edgsprqqia
      421 pellaakqrn dpmgllnpgk mrsftpvaqe tpa
//
LOCUS       WP_010514480             539 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Komagataeibacter
            oboediens].
ACCESSION   WP_010514480
VERSION     WP_010514480.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..539
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=56257
     Region          31..531
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mqertlargl ltavlatatg mlaapaaqaa tpsvtapvgv isgmtqgnad iflgvpfaap
       61 pmgqgrwqps tplasypapv rattarmgca apisadvget vnedclylni yrpagvdaha
      121 slpvtvfihg ggnqtgtpas ydgtefatrt hsivviptyr lgvfgflalg gergqpqgdl
      181 alsdiisalk wthdniaafg gnatgmsvvg esagaanicd vltapaahgl vtqaimqsgf
      241 cpgrptravm eaigtataqa agctgpdpls cmkrlpvpal laawntvwqq ptvrlkdgts
      301 vsrplfpvtp sgstlqpkpv daairagavg svpvligfnr delrtflagy yplstdryha
      361 llkqdysgfa adlqkeyplt pgqdpvytls alrtdqmlic palraaavln gpthvavyef
      421 adrtappfrs lamklpdapg fdrgashtae llylfgyksv agplspvqqa lsaqmmdmwa
      481 tfgrsgttap wpawtpqapd vtvlalpadg girvehdvat rhhcgfwgrh paipnslfp
//
LOCUS       WP_010514472             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Komagataeibacter].
ACCESSION   WP_010514472
VERSION     WP_010514472.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..265
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28932
     Region          1..257
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mspvvglwgv ekvfgsgvra lapvdleiqp gefisligps gcgkstllkv iasihpptag
       61 lvrwwgrdft hvgseghrma fvfqdptlmp warvednvrl pldlervpvs taapqvraal
      121 eqvglghvlr hypaqlsggm kmrtsiaral vtrpdlllmd epfgaldeft rdrldgemar
      181 lcyenglttv fvthslyeav flssrvivma anpgrifgey hidpairrdd afrlsdgfah
      241 mcrdlsqmlt eathatfaga egvnp
//
LOCUS       WP_010514495             193 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Komagataeibacter oboediens].
ACCESSION   WP_010514495
VERSION     WP_010514495.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..193
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=22103
     Region          2..190
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mkvhviyahp ltdsfnaalh elavrslkqa ghevddldly renfnpvlsa edreiyhdpa
       61 inqkhvanyv rrlqtaealv lchpvwnfgw pailkgyfdr vflpdvsfkl idgvlssgfs
      121 nirrvstitt ygsprhrafi lgdpprkngt rflravmnrr vkvdylalyn mnnttlaard
      181 rfmgrvrntm lsy
//
LOCUS       WP_010514499             399 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Komagataeibacter oboediens].
ACCESSION   WP_010514499
VERSION     WP_010514499.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12081071
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..399
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42133
     Region          11..399
                     /region_name="CynX"
                     /note="Cyanate permease [Inorganic ion transport and
                     metabolism]; COG2807"
                     /db_xref="CDD:442057"
ORIGIN      
        1 mnrdktfnig liliiylyaa asmavvglvv pfihtiadiq hvspgvvgkg lsffalpaai
       61 lsfifgmtvd rigvsrsfal svfltvagdv llmsahdiwp friglmlagc gfayatttsp
      121 allmnylpqd mrsralafws tfapagysag lllavpflhn gnwamaclfh iglmvialvg
      181 gwmflmrlre dgpareaaat entpqvrpaf arvltlslsv alpngiaygt slvaptylah
      241 ahsvslgtts tevalikivv mllggglisl lastqqralm lfvimaavgt gaqfmlffpp
      301 sgiilasvgl fvwmfayssl sgsamsllpa vagsgnargv vsgivgqfis vssvlvpsly
      361 fstttwtdyf lfavialvaa tallfltyra irqprlava
//
LOCUS       WP_010514503            1082 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Komagataeibacter
            oboediens].
ACCESSION   WP_010514503
VERSION     WP_010514503.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..1082
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=116647
     Region          1..1078
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnicrpfilr pvgtvlmama llfagvvgyr ampvadmpnf svpviyvias qpgsspqqma
       61 ssvttplerr lgtiaglrti qsdsndgfaf llmffddtrn idgaardvea aiqaaradmp
      121 ptlritpqyy kanpasmpvm iasltsptrp lyqlrdmaet rllpmlsqih gvgwvqvagt
      181 akpavrvdvq pwmlykfgig yedvraalas anantpkgvi etgdrrftla tndqarnaaq
      241 yrdlviayrs grpvrladva hvedgpener ragwanddpa vvaiirpqpg anviaitdqi
      301 karthllqqa mpadvrltft cdrsltiraa lldtqftlff aivlvtvvvl aflqswrstv
      361 ipvitvpisl agavagmylm gfsldtlslm altiatgfiv ddaivvveni vrhmeagasr
      421 mqatlagaee iaftivaitv slvavflpml fmggtpgkil fefamtlvla vsvslllsls
      481 ltpmmgahll hrhapargdr wrdrlgqald rgfvrctawy ggsldyalrh rwlvilslpl
      541 tlvgsviima hipktmipaq disimqgyar adqnisfqam sartrevvrr lradpdirdv
      601 ialtgeeatn qsqffiqlvd rdqrhstpde isqrlraslr tiggiqvnls nagdmngggg
      661 rqhdgnysyv lhsdnaddvy twvprladal rqepdlmgvt trvednadsl mvdiardtaa
      721 rylitpqlis nslydayger tasnistpft ayhvvmetaa ryrenpdivh dmwistaggs
      781 agggtvsnti rvtrtdaasl tglaaisqqs frnsianrla ggagassgsa vssstetmip
      841 lsnvtylrrq gtplsishqg gaiagtisfd papgrslsqa eeaiqrsmlr lhipsgvhga
      901 fvgesadfha aivnqvlafl saivvmyitl gilyesysqp ltiistlpsa mlgatgslwl
      961 cgqafslvgm igvimlvgma aknsilvvdf alraqreggl pvataiemac vkrfrpilmt
     1021 tlaaamgavp lvlgnsygve mrrplgiail gglvvcqvmt lystpvvylv mdqcarrfrs
     1081 kg
//
LOCUS       WP_010514521             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: inositol monophosphatase family protein
            [Komagataeibacter].
ACCESSION   WP_010514521
VERSION     WP_010514521.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..262
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27425
     Region          8..258
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mtqailtrfe aarsvvrdaa dlamkmrpap ggpkgtqksa qdwltetdga veafiserig
       61 mlfpedgfqg eeegrtrtgt lrwvvdpidg tsnyargrnr wcislglmdg dmpvagiiea
      121 pmlgetytav rghgaflngq rihaspvtdt assliemgws nrvppgvfqq kidailnlga
      181 mprsggsgai alaevacgrq dgyleicinl wdvaaalvll deagarvspf lrdggltggv
      241 cilaaapgia dalsnavgvs lk
//
LOCUS       WP_010514638             587 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Komagataeibacter].
ACCESSION   WP_010514638
VERSION     WP_010514638.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..587
                     /product="DEAD/DEAH box helicase"
                     /calculated_mol_wt=63159
     Region          1..388
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          468..536
                     /region_name="RRM_DbpA"
                     /note="RNA recognition motif (RRM) found in the DbpA
                     subfamily of prokaryotic DEAD-box rRNA helicases; cd12252"
                     /db_xref="CDD:409698"
     Site            order(475,480..483,485..487,489..490,496,499..502,
                     530..531,534)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409698"
ORIGIN      
        1 mpfpethpal qraldergyd nptpvqtavl dvaaegrdll vsaqtgsgkt vafglamadt
       61 llggaerfgp agpplaviia ptrelamqvt reltwlyapa ggrivscigg mdarrearal
      121 qmgahivvgt pgrlcdhqsr grldmsqlrv vvldeademl dlgfrdeleq lldampktrr
      181 tllfsatiak eiaslarryq ndavridtls gakqhadiey raivadarel ipavvnvlry
      241 tdsqttmvfc atremvrhmq aalvergfss valsgelgqn ertraidslr kgqanvcvat
      301 dvaargidip alalvihatl ptdpatllhr sgrtgragrk gvcvlmvpms qrrraerlmq
      361 gakitatwsg vptaaeiran dakrlladpv lnedvaeadk elvgqlvegr tseqlaaall
      421 qmyrarlpap envrhitpda prpprerser dgtrptrdsy asaepgawfa mnvgrqekad
      481 pkwliplicr lggvrkadig airindtqtl feitpdstek frsciaaien devqispasa
      541 paggaprrsg pprggrpfgr kpgggrpggg fggpprsgas srkrprs
//
LOCUS       WP_010514637             101 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Leptospira].
ACCESSION   WP_010514637
VERSION     WP_010514637.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..101
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11764
     Region          7..74
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mdfttfrrkv glrlkelrie rnlsqedlds gddgipyrti qnieagrssi nlrtiykicr
       61 klkvnamelf dleklsnhpp kkrarkktly kkvttksnln k
//
LOCUS       WP_010514654              89 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HU family DNA-binding protein [Komagataeibacter].
ACCESSION   WP_010514654
VERSION     WP_010514654.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..89
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9273
     Region          1..89
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mskafiaavi qdsidctgva anqaasdlia aivkelkreg gftlpsfgtf tvkktkarka
       61 lnprtgepvk vkagktvrfk aspnlkkav
//
LOCUS       WP_010514656             470 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: lactate utilization protein B [Komagataeibacter].
ACCESSION   WP_010514656
VERSION     WP_010514656.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..470
                     /product="lactate utilization protein B"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=53312
     Region          1..453
                     /region_name="LutB"
                     /note="L-lactate utilization protein LutB, contains a
                     ferredoxin-type domain [Energy production and conversion];
                     COG1139"
                     /db_xref="CDD:440754"
ORIGIN      
        1 msnkpvnhar aaehfledap hlqfhderlw dmrqkrdgqm hmlpewqdlr eeasrikeht
       61 lsrlpeyleq feenakkngi hvhwardgae hnrivgeilk ahnarnliks ksmvteecdm
      121 rpylekqgvt vtetdlgeri qqlddqlpsh ivvpavhklt sdvakifakd yhtdpnirdp
      181 hllaeaqrqa arpvilhada gmtggnfvva etgtfvvctn egnadlsatv pnlhiatigi
      241 erlvprmadl gvfirllsrs algspitqyt thfrgpqkgg emhvvlvdng rsarlgmedf
      301 wtslkcircg acmntcpvyr rsgglsygav ysgpigaiid ptfnerkyst lpyastlngs
      361 ctnvcpvkin iheqlykwrr vlvqhhempf vkreimhmag klmgqpkmyr aaikmtevsl
      421 gsmprfvlyn wlnpwgkhre nphpvkqtfn dwyrknreka kpaaasetkk
//
LOCUS       WP_010514687             362 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: XdhC family protein [Komagataeibacter].
ACCESSION   WP_010514687
VERSION     WP_010514687.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..362
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37952
     Region          8..360
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 mtqvsstrdp ldlliewara gqpcalatvt stwgssprpa gsmmavcang riegsvsggc
       61 vegavieear gvmdtghpaa lsygvssdda wavglacggl ldvyvaavrt pahpqgtldl
      121 amletvaekr rarvpvivat dmatgasrll yrtdaapggd tscdldarla araqevfetg
      181 rslrledang qalwflhlip mpprlliaga vhiaqvlapm aqttgfsvtv idprtqlatp
      241 erfpgitlet dwpdetlarl gvdnqtaivt lthdaklddp tlhyalngda fyigalgsrk
      301 tqasrverlr eagfseaqia rihgpvglai gavgaaeial silaeivavr hnrplgrvsg
      361 ws
//
LOCUS       WP_010514921             507 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Leptospira licerasiae].
ACCESSION   WP_010514921
VERSION     WP_010514921.1
KEYWORDS    RefSeq.
SOURCE      Leptospira licerasiae
  ORGANISM  Leptospira licerasiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Leptospira licerasiae"
                     /db_xref="taxon:447106"
     Protein         1..507
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58208
     Region          29..468
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkkilgtivc llftqsffak tvndgvemdl ekavllglan nvilknlerq nevfqmtvre
       61 kwreylpklg vsyfglrnln qnqqdsvynd irltiqqlvy dggengrlie sarlsaeink
      121 aeiqvqarka kidvvrqymk iisnrgkyls arrlyrsfeg qlsdttleyk nglksrldfl
      181 evsakfneak lsllkaetef knsitelkli lqledsddfv iqenifydyy iedpkpilda
      241 degnleenrp dlkkskiivn rlkleresld sawkpklfag gyygkntndv lpvihdnygf
      301 nfsvvvplgs stlqsqsnyg iqtdgtgiqr ipgygpqfvg qgansfnsan lqlfdnlsqa
      361 rkvlegelkf vdakssyefa rkqakfevik ardkllenys visvlsqkvl lylenfrinr
      421 vkfksgqlkr tdllkseyef sktqddlaea yseylrscye yfyvtgrdia dlpfykvnlg
      481 rgnsiiaklv ketrenedff pekgrkk
//
LOCUS       WP_010514995            1057 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Komagataeibacter
            oboediens].
ACCESSION   WP_010514995
VERSION     WP_010514995.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113176
     Region          1..1039
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnaivqlala rpytfvvmai liamagvlca irtpedifpe igipviavaw tysnlspqdm
       61 sgrielpfqr vltttvnnie hieglsltgi gvtkvffqpg tdiriantqv taiaqtilrq
      121 lpigttppli lnynastvpi vqlalsgegm teqqlydygf nfvrnrlitv pgaaipfpyg
      181 gkvrqiqmdl dpaklqsrgv saqdvgtals tqtqitpagf vkigeyqynf rlnnaplsvd
      241 llnmlpvrtv ngavvrvrdv ahvrdgstpq qnvvhvngqr salltvlksg atstiaivqg
      301 iramipdatr glpkqlkirp vndqslfvra avngvmrega iaagltslmi llflgswrst
      361 livatsipls vmgaiaalaa lgqtlnvmtl gglalavgil vdeatvtien ierhlemgqd
      421 vhaaiidgsa eiivpaflsl vcicivfvpm fflpgvagfl fvpmalsvmf amvmsfilsr
      481 tlvptmamfl lrahedvnhr etvltrfqhg ferrfdalrt ryaallgsvm ayrgrfvigf
      541 vcfsvlsmgl lpflgrnffp qvdagtmtlh vrgpigmrie etaalfqrie klirqripag
      601 eldsitdnig lptsaintay nasgtigpqd gdilvalken hgpteryira lrrdlprafp
      661 easfaflpsd ittqilnfga papidiqvsg inpdetrqfa qkilhairri dglvdariqq
      721 pghypelrfe adrtrisqlg ltegdvttai atsiagtvqt aplywldphs mvtypiavqm
      781 peyrisslad iiglpvtgvs tpqlqvlgal gtitrgatsp veaqynirpl idvfaggdgr
      841 dlgaiasdvl avlrhldher pgtvtvtlrg qyqamttafs gmgfgllgai vliyllivin
      901 fqswidpciv ilalpaalag icwmlfatht plsvpaltga imcmgvatan silvisfcrd
      961 qmgehgdasr aaqaagstrl rpvimtalam migmlpmalg lgeggeqnap lgravigglm
     1021 fatcaslffv palftiihgs radgaagdaa dgarang
//
LOCUS       WP_010515002             319 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Komagataeibacter oboediens].
ACCESSION   WP_010515002
VERSION     WP_010515002.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..319
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34036
     Region          83..291
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mspnpvapef raalevlpsf dgisdatlda trkafiaair nvrvrhypdv tvttghvpgp
       61 pgapqvpvvt yrpvashpga palvyihsgg ivsgtpevdd arcrqivsel gmvifsvdyr
      121 lapeapypaa iedcyavlkw vhghaaeldi drqriviggd sagggltacl almardraev
      181 pvlfqlliyp mlddrtgttv mpppvmgeyi wtraanhyaw naylgqipgg agvpgyaaaf
      241 raadltglpp ayigvgsldl fldedldyar rlmaagvpte vcvipgayhv fdvfipdapl
      301 sraftqsyfa alkraitrd
//
LOCUS       WP_010515035             404 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdopterin molybdotransferase MoeA [Komagataeibacter oboediens].
ACCESSION   WP_010515035
VERSION     WP_010515035.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..404
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.10.1.1"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061599 - molybdopterin
                     molybdotransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=41796
     Region          10..401
                     /region_name="MoeA"
                     /note="Molybdopterin Mo-transferase (molybdopterin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG0303"
                     /db_xref="CDD:440072"
ORIGIN      
        1 mktnsfarqv dyatalrlvr draarvmppa trvpvaqatg rvaaadimar tcrppadisa
       61 mdgyafahda mvahgrlpva grtvagdaai plppgharai ltgaripaga dcvmaaerma
      121 vvdgnvapaa plpasganir rqgeefasgt rlvaagqrld wrhvallssq gvgdvavirr
      181 prvsvvsnga elaadapgac pdsnapmlas mltgigarvt thaaptdnva rqaaclhaar
      241 rgadvmvttg gisvgdtdhm ldilrdagar vmfrgvairp grpltvlehd gqtifclpgn
      301 pgaaaicalm fvwpylrtim gqdmprpgvc atadftadap pgvtlfipvs lhpgpqgwlc
      361 rrvptvgasd iiafsradal lavtqdspir agqpawgmpl radm
//
LOCUS       WP_010515064             325 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine recombinase XerC [Komagataeibacter oboediens].
ACCESSION   WP_010515064
VERSION     WP_010515064.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..325
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=35752
     Region          1..320
                     /region_name="xerC"
                     /note="site-specific tyrosine recombinase XerC; Reviewed;
                     PRK00236"
                     /db_xref="CDD:234698"
     Site            order(152,166..167,245,247,266,301)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271175"
     Site            order(166,266,269,292,301)
                     /site_type="active"
                     /db_xref="CDD:271175"
ORIGIN      
        1 mmatgardaf lhwmeterra saltltayrg dldrflaflt khlgaepdmg alaglsltdl
       61 rawlahehaa alggrrpttq draartrarr vsalrsfyry laryhgvdnp apgllatprt
      121 rrplprplpk tqalevpegv sdiahtpmar vrdgalfmll ygcglrisea laldvrdldl
      181 artlgdgtkg dgvlrirgkg gkermvpvlp qvmqalsrwr sthplpqpda plfvgvrggr
      241 lqagiaqram rtwrhmaglp ehatphalrh sfathlmegg adlrviqdll ghaslsttqr
      301 ytladearlm dvwtrahpha tdtar
//
LOCUS       WP_010515090             444 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Komagataeibacter oboediens].
ACCESSION   WP_010515090
VERSION     WP_010515090.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..444
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=47614
     Region          20..444
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mkpspspssr ptgrrpnagr pdrrggkvap dptrdiafdi vegvivhrrm ldtsldhsaa
       61 araaeprdra aghrlaatvl rhmgtanevl apflkreppe pvrvvlligv aqllfldtpa
      121 haavatsval arrrglvpfa glvnavlrrv aaggtqaleg ldqarldvpp wlwqswgkla
      181 rpiaralghe ppldlsirpg aepppggevm pngsvrfaag tvkvvdlpgf aegtfwvqdm
      241 aaslparlld vkagervadl caapggktaq lafagaeifa ieregrrier lranlarlgl
      301 davkvihada aqwrpdapld ailldapcsa tgtirrhpda mwikrprdia tmtegqdrll
      361 aasrdmlrpg grvvyavcsl qpeegeqrar aaeamgllpd pftpeelafl pqartpegwl
      421 rthpgmladh ggmdgffaar frra
//
LOCUS       WP_010515192             734 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Komagataeibacter oboediens].
ACCESSION   WP_010515192
VERSION     WP_010515192.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..734
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81133
     Region          61..720
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mtrlwfsrhp lspamlaamt vltpvfplva qtttgtgvlt tdttttqvad tdatrrssap
       61 damtvtarld rariqlqpst gatvhafsrk aletipggdn aglnsvllqa pgvaqdsygq
      121 ihvrgdhnev qfrldgvqlp eglnvfgqtl mtrfadnlsl stgalpvqyg flqaavvdit
      181 tkngatnkgg nvsiyggard yffpsaqygg qhgrwdyfft adyvhdrvgi enttpsfnap
      241 hdlsnqyhfl ghlrytvden trisliagvs naeyqlpnig gqpmfgddys sllpqapgsd
      301 nlnerqkeit dfgilslqke igafslqtsv fsrysslgys pdpnmgdlay mgisqhaers
      361 vmstgtqsdv twrvrpdhti rfgfqvfaer nitkadatvf ndadqqvnih tgngrtgdiy
      421 glyvqdewrp lhnvtvnygl rfdgvgeytn ehqlsprinv vwrawkgasl hagysryftp
      481 ppfevvggsd lqqfantsaa tdvsrsdtvk aerdhyfdag ieqiilpgwr vsfdayykla
      541 hnlidegqfg apiilsgfny rrgqvngyef stsydrgpls lygnfawsra igkditsaqf
      601 nfdgddlkyi sqhwihldhd qrwtasaggs ytffyrsghp trisatmvyg sglrqdsdvp
      661 nggvipqyat fnmslvqsfr dlfhsrflrt tqlrldvtnl fdhpymlrsg tgvgvgapqy
      721 glrrtiltgi sqsf
//
LOCUS       WP_010515205             281 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Leptospira licerasiae].
ACCESSION   WP_010515205
VERSION     WP_010515205.1
KEYWORDS    RefSeq.
SOURCE      Leptospira licerasiae
  ORGANISM  Leptospira licerasiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Leptospira licerasiae"
                     /db_xref="taxon:447106"
     Protein         1..281
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=32284
     Region          40..280
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mkrpvyyfli iilfyfigsv iytivsaykv pennldsflk sedktpkryv vflgdsithg
       61 tvsynyvqsl senpklknft fvneginsrl tyqilekvdd tirlspehif iligtndaka
      121 alneeeykgy nslwnlpevp nistyeknlk vivallkaet kakihlisip vlgeslnsip
      181 lkqsiaysnv irniakesns yyiplnetlv adlknrpdqt egeytrntlk mywiifkhfg
      241 lfqswdkisd qsdlifmtdg ihmnsragki leemiqkdlk e
//
LOCUS       WP_010515496             341 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Komagataeibacter oboediens].
ACCESSION   WP_010515496
VERSION     WP_010515496.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..341
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35613
     Region          10..324
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtmpspthtt dvaiigagpa glfaafecgm lklgciiida ldeiggqcaa lypekpiydi
       61 pahpaiegga lidaldrqia pfdvprllgr rveslegtrg gfrlgtssgd viaahaviia
      121 agagafgpnr ppldglaafe qtggvqyfvr rradfadrdv liagggdsav dwalslrdva
      181 rsvklvhrrd rfraapeslr qldeavarge vekiigyqlh glhgadgqla gvdlatldgt
      241 vrhvacdhll pffglatdlg piaqwgldti rgtipvtpst cesslpgifa vgdvatypgk
      301 lklilqgfte gamaahaihp ivhpdtalhf eystskgvpa g
//
LOCUS       WP_010515579             215 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Komagataeibacter oboediens].
ACCESSION   WP_010515579
VERSION     WP_010515579.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..215
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24319
     Region          1..215
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mlrcidivkd yhvdnghrri ldginlqvek geklgilgrn gagkstliki iggvelptsg
       61 riehtmsisw plafggafqg slsgldnlrf icriynldyt rtrkyvddfa elgkqlmdpv
      121 ktyssgmrar lafalsvvie fdcylidevi mvgdarfyer creelfvkra draliivshd
      181 mhfvkeicdr svvihdrkmv ecssvqegid lyhsl
//
LOCUS       WP_010515629             282 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein
            [Komagataeibacter oboediens].
ACCESSION   WP_010515629
VERSION     WP_010515629.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..282
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30855
     Region          12..282
                     /region_name="COG2374"
                     /note="Predicted extracellular nuclease [General function
                     prediction only]"
                     /db_xref="CDD:441941"
ORIGIN      
        1 malalmvlpv gaqaggslkl stwnldwltt rpqgdpdlpe dvtprttael drlayyarrl
       61 apdiaaleei dsaqlaarlf papryrills ddtvvqkval avradlpvir hpdvtaldvy
      121 pstaprhlra gldltvgsga dslrilvvhl kagcrdssat trnrpvcrtl lrqiaivqdw
      181 imerqdegev fvvmgdfnrl lapddpawrs ltengpltla taghaspcaq gsyfidhima
      241 ggpardwlqp dslrvmlyre ngrddtmrls dhcpvsvrls pp
//
LOCUS       WP_010515691             319 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Komagataeibacter].
ACCESSION   WP_010515691
VERSION     WP_010515691.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..319
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33990
     Region          7..298
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mahssssrtv ifaalggnll vaatkfaaaf mtgsasmlse aihslidtgn qglllvgmrr
       61 atrpatamhp fgfglelyfw tfvvallifg lgagvslyeg iihiihpqpv ahvlvnyvvl
      121 masivfegsv wlmalrafrk egkgrrgwve avqmskdptv ftvlfedtaa lsglgvallg
      181 nilaewldmp vldgvasiii acilavtatf laresqsllt gegvapevla alrrmalaas
      241 gverlneirs lhfgprdvlv visldfrndm tagqvevvvs alerqikqay pevtrvfiea
      301 qdsrtqppgt adsgsmptp
//
LOCUS       WP_010515716             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Komagataeibacter].
ACCESSION   WP_010515716
VERSION     WP_010515716.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..158
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17290
     Region          5..154
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 mpdrthryqv sllwtgnggn dgasrqahhr dyelhcvgrp vidgsaapaf rgdsqkwnpe
       61 klllgalcad hqlwfihlct amgigilsys dsaealidey edgsfsitqv ilrphaaist
      121 phdiqqvidl hqdatmrsci arsvsfpvlc eprvtgaq
//
LOCUS       WP_010515813             209 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SCO family protein [Komagataeibacter].
ACCESSION   WP_010515813
VERSION     WP_010515813.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..209
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22681
     Region          51..205
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mmrnerdrff vivglvilav ssvagyfgyr yssnapvplt tygnpvggsf rlingadgsv
       61 mdtdfrgrwm miyfgdthcp dtvcgatvka madgvealgr drahlvvpif isldpmrdtt
      121 evlrtyalrf gthvtvmtgs pkmleavake yhapyvrhdg engeysmepa tqivimsptg
      181 ryagslpsta taaevtarmt elmnapgkh
//
LOCUS       WP_010515888             150 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Komagataeibacter].
ACCESSION   WP_010515888
VERSION     WP_010515888.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..150
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16561
     Region          1..139
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkldaidrri lnvlqedgrc pnnelarrvg lspspclrrv rlleesgvie gyvavvnpak
       61 agfgvtafvr iwltgederq sehfveeigk lpqvteahvl agdcdfllrv vaedlpglrc
      121 fqsehlarik gvrsmktdip llkvknasfa
//
LOCUS       WP_010515889             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Komagataeibacter].
ACCESSION   WP_010515889
VERSION     WP_010515889.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33578
     Region          8..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdnrigemqm flrvvesgsf seaarlsmtt pstiskliar vetrlgvrll erstrrlsvt
       61 pegqlyyera qallaelndm ehalttgsvr pggivrinas vafgalalep llpefwdayp
      121 dividlslsd eltdlyldrt dvafrvgplq dsnltarhig tarrkivgsp dylnrfgvpr
      181 niddldqhkc lgfnfrraap vwplhekgri adrivrgpll anngetvrrl tlrgaglarl
      241 gdyhvrddik sgrlvevlah adaqdeeeih alylgskqtp qrvrvfldfv iprlqaylrt
//
LOCUS       WP_010515892             690 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Leptospira licerasiae].
ACCESSION   WP_010515892
VERSION     WP_010515892.1
KEYWORDS    RefSeq.
SOURCE      Leptospira licerasiae
  ORGANISM  Leptospira licerasiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19960403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Leptospira licerasiae"
                     /db_xref="taxon:447106"
     Protein         1..690
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=77434
     Region          <133..685
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          141..167
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(143..144,147..148,150,174,177..178,181..182,
                     184..185,208,211..212,215..216,219)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          172..202
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          207..235
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          245..269
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          277..307
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          312..340
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          316..573
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          345..375
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          381..408
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          419..445
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(421..422,425..426,428,452,455..456,459..460,
                     462..463,486,489..490,493..494,497)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          450..480
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          485..508
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          519..546
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          592..624
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          631..662
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 menpirknri fleteepkps yyygdepeef rpkrhynpta fawgalaasl llliglaiwy
       61 sffregrpgf gtngvadgks plmpkgslaq elqrpylpdg tnnplltkcv tlykqnyrkq
      121 sfdycteflt gpatsqeksl altvlgviyd edgrfpqaid slqkaitldg nnvyayynlt
      181 layahsgqns aarstalkar eiapndpria lmagnlfnei ndpdaaiday kqglssspdd
      241 pyltynlals yfkkgeipqa eehfklvvmr arggklaals nsylgnisyn rgdyvsaehy
      301 freaatltpn dakalynlsi vlkkngklee svkylelanq agsndpelfr siaegfeqln
      361 qgeqsinalq kglkynpnnl dllfqlaety ynkgdllaae etyrrivdst pgdsftetal
      421 lnlgvvldqm erygeaityl nrvldlnpkn akayynlglv ykhtgngtqa ienfrkasyl
      481 dpddikpkea lgdyylenkf yreaieeysa lfkqkedyyk valklaeaym gtgesssaek
      541 illqvlnrsr nsneikqahk klallynksk dpdlknrakd eayrsahmdp edyegrlvls
      601 killdsnsvl drekaieelt aivrsevkpk tastaynylg vafykngeyk kavrsfqnai
      661 dldpsnteay dnkraataal edsskrdglf
//
LOCUS       WP_010515900             742 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Komagataeibacter oboediens].
ACCESSION   WP_010515900
VERSION     WP_010515900.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..742
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81893
     Region          57..711
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mtgttkarha asatsraaps gkagqganav qatstseilq vssgrsgggg mmrqeraphs
       61 iqtvtrqfmd mrspagtald mvknlpslnv stqdtsgmtg gsiesrslnd gdmallvdga
      121 vvtsgteylq edidtenmdr ievtpgtsai dqpvtsaalg vmnvvthtps hkfggltdfs
      181 ygtndmsrqf irlesgdigk tglrsffsfs hthadnwiga gasdkkhidf gvqkdigtds
      241 yikfflswnq erygiynypt adqfyakkhg tgtwgassdp nspnfwgnhq egpwnelfmt
      301 lpvhlrltnr lhfdlvpyfa ygrgwsssvs geagsgltya ngsavspsql svnyydqrtp
      361 ttgatiklty disrhnqmtf gywygytqsr qwgpnsavnq ngfsnnpddl stayfqngqr
      421 yysanqqtgd qihalfiqdt akyfqdrlvv sagfkfammn ywfdnylthq tmgsnsvvpl
      481 prfstsytfn rhhqiyvnaq gdfrapdpsn ltentslprn qytikeelgy rynnryiifd
      541 lslfnyaitn rllsvynann systvnagnq targfdvmls thpfhhfspy vsfeylnarq
      601 dsnvqygtsy lptkgkeaim aphvmanfgl tydnrhffan atvhytgpqs vtlvgderip
      661 gyvtdtislg yrfspflvak sptfrlnftn ltgsmvrtgt tgvadnyhav tllngqsiag
      721 stgaqfyvep rfsmtgtist af
//
LOCUS       WP_010515909             501 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Komagataeibacter oboediens].
ACCESSION   WP_010515909
VERSION     WP_010515909.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..501
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52311
     Region          25..421
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(32..33,36..37,40,71,121..122,124..126,129,149,
                     152..153,156,281,284..285,288..290,293,321,325,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mqpdpsldpa stytpatrll vftglimtmv mgaldqsivs talptivtdl gglahmswvv
       61 tafmltstia tpmygklsdm fgrrpllafs igallgasll cglaqgmwql ivfrglqgig
      121 agglmtlsqt vigdmvtpqq rgryqglftg afavssvagp flggvltsal swrwvflvnl
      181 pigllalgli mfglpagrse aepqvdypga allavatagf lllfnsvgta lawtspltvl
      241 llagsvaffv lfiwqerrap eplislgllr iasfsvcvaa tgimsfamlg slvflplyyq
      301 lvlgqtpevs glmmlpqvgt mmvssvvggy vssrtqrytl llamgvgief saltliafca
      361 hhgapalffl lslgclgvgm gigmpnatvi iqnsvppdml giatammafi rslggslgva
      421 lsggvmaltl qgrlyalpek idvaaflekg maavqglspa mhlqvreayk aaisaslsvs
      481 ssfmllaflm ivglmtrgrr a
//
LOCUS       WP_010515915             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Komagataeibacter].
ACCESSION   WP_010515915
VERSION     WP_010515915.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..181
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20305
     Region          <1..113
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkvapanfyn hygslndlll eiaadyfevf reqaahisrt satrtealkr tvlyfvdfar
       61 lrpqlyrlmf gyipdaytyp ryrltasaaf edlmelmygy rvftsrddfg pgdmatlgsk
      121 vqigygmyam lcglsnlfia npvegpfskt dnpresiatf ltgildafir gdlpkvlgak
      181 p
//
LOCUS       WP_010515914             470 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Komagataeibacter oboediens].
ACCESSION   WP_010515914
VERSION     WP_010515914.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..470
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51808
     Region          15..460
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mvpapspsps vhkqtiaqtg ltrlqtwlfa fpalpaafii lpmnifipaf yashtavtll
       61 qigtatslcr vidalldpai gflsdrsrtr fngrgtwgia sgviccvalf flfqpsshat
      121 ilyygvwafv lyfgyslfei prsawsaelg stpplrtrin aaiglftvag slifwlvpvi
      181 lfrfygttgf tqgtlrvivw lyavlmlpav icimryvpdr psartiaptl rdlarslkqn
      241 rplalyflai alwgvgqgiw fsttflflnd ylrvgsvfpl imivfflsti vaiplwgrae
      301 rrmerhalwa ismilsaltr plallpapgm hslpfimllt aaggalsapa nfmpyailad
      361 vidydiwktg tsksstlyal ntlitktala mgsgagfiil gwvhyhagqa nhgppltgll
      421 lcytvicsip qliaamiify fpigrrahtl irhrlnrrrt dtripvrndp
//
LOCUS       WP_010515946             185 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide biosynthesis/export family protein
            [Komagataeibacter].
ACCESSION   WP_010515946
VERSION     WP_010515946.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..185
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19660
     Region          8..183
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mmmqavgvta llalsccasa reqsfetvda rvyhlgpgdq vrvityndpq lsntftvsdn
       61 gnidfpllgv vpaagaappe laarisasle kkgiltqpsv svevaqyrpi filgevnhpg
      121 qypyqpgmtm ltavalaggf tyravtshat dvrqedlsta phegrisrat vllpgdvvti
      181 derff
//
LOCUS       WP_010516012             112 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF736 domain-containing protein [Acetobacteraceae].
ACCESSION   WP_010516012
VERSION     WP_010516012.1
KEYWORDS    RefSeq.
SOURCE      Acetobacteraceae
  ORGANISM  Acetobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Acetobacteraceae"
                     /db_xref="taxon:433"
     Protein         1..112
                     /product="DUF736 domain-containing protein"
                     /calculated_mol_wt=12201
     Region          1..109
                     /region_name="COG5489"
                     /note="Uncharacterized conserved protein, DUF736 family
                     [Function unknown]"
                     /db_xref="CDD:444240"
ORIGIN      
        1 mtqigsfirt pdgfagrlrt laldaeltfl svgagtaena pdyrihlgdg dagpevgagw
       61 trtgeragey vsvllddpif tqpiraslfq vgrggrdwql vwnrqvkrdd rr
//
LOCUS       WP_010516040             216 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Komagataeibacter
            oboediens].
ACCESSION   WP_010516040
VERSION     WP_010516040.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24049
     Region          16..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkpvaptlsp kpglrerkqa rarttliaea mrlfsaqgyd qttvdeiada aevsrrtlfr
       61 mfetkgdivl awtrgmtqtl ndalatcpad mhpadammha ftslvpriaa nrqdtyafvy
      121 liektpslqt vslqkygkwe dclaeglakr iterrnrrma arxmarggia ifrtaldewi
      181 rlksrpalvp llqktyelqa slwpghdddg peedaa
//
LOCUS       WP_010516051             311 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Komagataeibacter].
ACCESSION   WP_010516051
VERSION     WP_010516051.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..311
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32425
     Region          2..308
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mlstiiaaml plivvfllgy ragwhhdftg eqvsvlnrmv mqyafplnlf vgiagmprti
       61 lagqlplaas vflimcgsfg vayglsrhvf rrdaatatlq glamgapsvp figsamlpvl
      121 vghastavai ssavfamvlv qtpvcmvmla ksahkgpseq arlvpqiias frepivwapi
      181 vatllvvsgi hlpksllnag ellgntaagv alfasgivlf lqrvsvtlpv vvtvavrniv
      241 ipavswlllt llglshevir tavlslsipv gtvvvilavr fgtdeqeaas tlflsavvsv
      301 vtmalfiacv g
//
LOCUS       WP_010516099             180 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peroxiredoxin [Komagataeibacter].
ACCESSION   WP_010516099
VERSION     WP_010516099.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..180
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19762
     Region          4..174
                     /region_name="PRX_Typ2cys"
                     /note="Peroxiredoxin (PRX) family, Typical 2-Cys PRX
                     subfamily; PRXs are thiol-specific antioxidant (TSA)
                     proteins, which confer a protective role in cells through
                     its peroxidase activity by reducing hydrogen peroxide,
                     peroxynitrite, and organic hydroperoxides; cd03015"
                     /db_xref="CDD:239313"
     Site            order(4,51..52,55,115,125,138..140,142..144,148..149,156,
                     167..170)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239313"
     Site            order(49,83..84,106,108,120)
                     /site_type="other"
                     /note="decamer (pentamer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:239313"
     Site            order(50,53,126)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239313"
     Site            order(53,167)
                     /site_type="active"
                     /note="peroxidatic and resolving cysteines [active]"
                     /db_xref="CDD:239313"
ORIGIN      
        1 mltvgdkfpa fnlsavpggp eglkgdfvqi tdesnegkwk vvffwpldft fvcpteivaf
       61 gklagefkdr davvygvsid safvhlnwrl nhaelknlei pmlsdikrel iescgvmaqq
      121 agaalratfi vdpqgiirhv svndlsvgrn pqeilrildg lqsdelcpcn wkkgdafika
//
LOCUS       WP_010516114             310 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Komagataeibacter].
ACCESSION   WP_010516114
VERSION     WP_010516114.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33860
     Region          9..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..301
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,231,248,280)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mrkqvvdyft alrvflrsaq igsfsgvaae qgmevstvsr hisrleadld valfnrttrg
       61 lhlteagtlm qerasrilad ldnareevtl hnssprgtlr invptafgrr hvmphmsafl
      121 tsfpeirvdv tltdttvdli esgtdvairi galpdstlva krlagqsril vgapgyikha
      181 glpvcpenlt dhsclfftvq tgnawyfrpg irpdapfekl svsgilkand sealleatls
      241 eiglallpsw ligedikagr lvrvleqfew vlapgaerai wavyppkkvv apkvksfinf
      301 macqlkdslg
//
LOCUS       WP_010516212             170 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA thioesterase [Croceivirga radicis].
ACCESSION   WP_010516212
VERSION     WP_010516212.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..170
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18811
     Region          5..150
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mrtktpsesr timtdmvlps etnplnnlfg gellarmdra asiaarrhsr ritvtasvnh
       61 vafnrsvplg svvtveatvs rafnssmeiy idvwmedris gekvkaneai ytfvavdetg
      121 tptevpklkp eteleqqryd aalrrkqlsl vlagkmkpnd atelkalftk
//
LOCUS       WP_010516241             261 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Komagataeibacter].
ACCESSION   WP_010516241
VERSION     WP_010516241.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..261
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26984
     Region          9..261
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mhlpesinll yvlsglgvgf lvgmtgvggg slmtpllill fkvhpqsavg tdllyaaltk
       61 tvgtlahgrr qsvewrvvgr lamgsipati ltigmlhwag spsaqvthvi svalgialli
      121 tapsvlfrqr lqtlsrqkag svspamtgrl ttllgavlgi mvtlssvgag aigmaalifl
      181 yprlelrrlv gsdiahavpl taiagmghww igdidvallt sllcgsipgi ilgslciglv
      241 pdraqrfila ailvtvglkv v
//
LOCUS       WP_010516269             259 aa            linear   BCT 01-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Croceivirga radicis].
ACCESSION   WP_010516269
VERSION     WP_010516269.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..259
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27949
     Region          3..246
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mftgkkiglv lsgggirgma higllkvlqe rgvkaqsvag asigalvgal yangnsidem
       61 laffketplf qysffaigkp glidteryfs vfqqffphds feqlniplhv vatdllqgte
      121 kvfnqgalim pllasaaltp vfspveidkv lyadggimnn fpkeyveqga dlvvgsnvsv
      181 ngklqkkdls nslqltsrit glmiyascre kicecdilie paqldqigvl dkkgiekaft
      241 igydaanfam dayldknkp
//
LOCUS       WP_010516348             228 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Komagataeibacter oboediens].
ACCESSION   WP_010516348
VERSION     WP_010516348.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..228
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25535
     Region          10..>167
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mgssareear iadalrkavl erklapgskl peeelaqifr snrakirrvl lslsrshivt
       61 lepgrgafvs rpspqeardv lasrrlievs llarpyrkls tqgvtrlrri maqeaeahek
      121 hdaiamihvs gqfhltliee lgnevlksit eelilrmsli itmyerhntt cclssdhhdl
      181 ldlllaekya easllmarhl egiescldfh rdpvtatils qilqpvqg
//
LOCUS       WP_010516377             134 aa            linear   BCT 01-JAN-2025
DEFINITION  HIT family protein [Croceivirga radicis].
ACCESSION   WP_010516377
VERSION     WP_010516377.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..134
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14877
     Region          1..125
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 masiftkivn geipsykvae teefyafldi npnaeghtlc ipkkevdkiw dldealynrl
       61 mtfsrkvala iesvvpckrv gmsviglevp hvhvhlipln kmadatfqsk vslekeafea
      121 laqkitkayl asnk
//
LOCUS       WP_010516380              86 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF2274 domain-containing protein [Acetobacteraceae].
ACCESSION   WP_010516380
VERSION     WP_010516380.1
KEYWORDS    RefSeq.
SOURCE      Acetobacteraceae
  ORGANISM  Acetobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Acetobacteraceae"
                     /db_xref="taxon:433"
     Protein         1..86
                     /product="DUF2274 domain-containing protein"
                     /calculated_mol_wt=9480
     Region          1..74
                     /region_name="COG5639"
                     /note="Uncharacterized conserved protein, DUF2274 domain
                     [Function unknown]"
                     /db_xref="CDD:444364"
ORIGIN      
        1 mtklriteip dekpvrvtvd lpadlhrdlv ayaalvsqng qsvdparlvp hmirgfitsd
       61 rafrklrqep rrapvktqsp aapeng
//
LOCUS       WP_010516368              64 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Trm112 family protein [Komagataeibacter].
ACCESSION   WP_010516368
VERSION     WP_010516368.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   van Tran,N., Muller,L., Ross,R.L., Lestini,R., Letoquart,J.,
            Ulryck,N., Limbach,P.A., de Crecy-Lagard,V., Cianferani,S. and
            Graille,M.
  TITLE     Evolutionary insights into Trm112-methyltransferase holoenzymes
            involved in translation between archaea and eukaryotes
  JOURNAL   Nucleic Acids Res 46 (16), 8483-8499 (2018)
   PUBMED   30010922
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Bourgeois,G., Letoquart,J., van Tran,N. and Graille,M.
  TITLE     Trm112, a Protein Activator of Methyltransferases Modifying Actors
            of the Eukaryotic Translational Apparatus
  JOURNAL   Biomolecules 7 (1), 7 (2017)
   PUBMED   28134793
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006712
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..64
                     /product="Trm112 family protein"
                     /calculated_mol_wt=6818
     Region          10..64
                     /region_name="Trm112"
                     /note="RNA methyltransferase activator Trm112/YbaR
                     [Translation, ribosomal structure and biogenesis];
                     COG2835"
                     /db_xref="CDD:442083"
ORIGIN      
        1 mtekppappl dprllsilvc pvtkgplvyd reageliskr aglafpvrdg ipimlpdear
       61 klda
//
LOCUS       WP_010516404             860 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Komagataeibacter
            oboediens].
ACCESSION   WP_010516404
VERSION     WP_010516404.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 860)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17596983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..860
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90224
     Region          11..62
                     /region_name="YHS"
                     /note="Heavy metal-bindng TRASH/YHS domain, predicted
                     Cu/Ag metallochaperone [Inorganic ion transport and
                     metabolism]; COG3350"
                     /db_xref="CDD:442578"
     Region          79..105
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          148..174
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          191..843
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(490,492,798)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(534..536,599,615..617,646,686..688,709,712,715,734,
                     737)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(799,827,831)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mtdtrqddrq mmvprtvhdp vcgmsvdtvt akfhtlhdgh dyyfcsehcq rkfgadpaaf
       61 vadeasithd qslagqtawt cpmhpeiret hpgkcpkcgm alepaektgn apampamehg
      121 qksgsntghd hhtstnemps lagnhtiwtc pmhpqirqdh sgdcplcgma lepedptghn
      181 eenpelrdft rrlivagvla iplmliamgg dvglhlvppv lspwvqlalt lpavcwaglp
      241 ffqrglaslr tghfnmftli mfgvgaafgy slvatifpda fpatfrmpdg slpvyyeaag
      301 vvvalvlvgq vlelraraat gnairalldl tpkqahriga dgqendvave diatgdrlri
      361 rpgesvpvdg kvlngassvd eamltgepap vakkpgdavt ggtingtgsl eiearavgsd
      421 tmlarivamv ataqhsrapi qsiadrvsdw fvplvlgisl vtfvvwyfvg ptprfghall
      481 naisvliiac pcalglatpm simvgtgrga regvlvrnae alqaldkvdt lvvdktgtlt
      541 eghprliald vapewqeddv lrlaasveaq sqhplaqavv ralkerhgtl vqvsdfgsqp
      601 glgvsgtadg rqvvignaer lkqagadpap leadatryrq sgagvmfvai dgkaagtiav
      661 adplredtka alaalhddgm rivmltgdne ttaravaqaa gniaevhagl kpqdkadiir
      721 qlesvgrhva mtgdgvndap alaaasvgia mgtgtdvaie sagitlahgs lgalvrarkl
      781 ahaimrnirq nlafsflfng igipvaagvl ypvfglllsp miagaamals svtvvtnalr
      841 lgrisdgghs ardartgnll
//
LOCUS       WP_010516443             202 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Komagataeibacter oboediens].
ACCESSION   WP_010516443
VERSION     WP_010516443.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..202
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21426
     Region          8..>199
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mpnpapparr vgfaimglgr lalgqilpvf aecrqarpia lisgdsakyr aiaarygita
       61 dacydyasig rirdnaaiea vyvvtpntlh rdnviaaara gkhvlcekpv atsvaqtqnm
      121 vaachdagrl lmiayrcqye ncnaevacqa ragrfgdirl idavnvqhqg dphqwrqsra
      181 lasggalpgi glyclntara ag
//
LOCUS       WP_010516461             177 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Komagataeibacter oboediens].
ACCESSION   WP_010516461
VERSION     WP_010516461.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..177
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18396
     Region          15..170
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtsvssavsg arlvtgqsvl gavqvvtgdg gvaaiilgdd pvalhdaalk rfpdavpagk
       61 aeadrvlaav rtcietpwat fglpldmrgt pfqcqvwqal raipcggtat ytelaahigr
      121 peavravaga cganplavvi pchrvirrdg slsgyrwgvs rkqwlldrer tgmargq
//
LOCUS       WP_010516478             380 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Croceivirga radicis].
ACCESSION   WP_010516478
VERSION     WP_010516478.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..380
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44343
     Region          18..244
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mskslftffl lctlalnaqv kkeifesfkl qerrdvsyyf pedysedkky plivvldadh
       61 lfdlavaytk fyskfhrmpq sivvgvhqle ndirwedcdf eqstglptek gklfyeflgt
      121 elipyletqy nvapfkmfmg yditanfgny flfkdrslfn ayilispvla pemesripar
      181 lsdldqelfy sliiekdkte drnrvlqlkn avssiekesl hfsfdeyeep dhtsiaaygl
      241 skvfdntfkm frpitpreyk eqilksedsp mqyltnkyem iekflgyksd ielndimaiy
      301 aaslkkedfe sldalskick aqypetmlgf ylegealele gepkkamkaf eksflmneid
      361 fltkdmalek idalkadfgf
//
LOCUS       WP_010516482             346 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Croceivirga radicis].
ACCESSION   WP_010516482
VERSION     WP_010516482.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..346
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=39378
     Region          13..337
                     /region_name="AKR_Tas-like"
                     /note="Escherichia coli Tas protein and similar proteins;
                     cd19094"
                     /db_xref="CDD:381320"
     Site            order(19..21,26,48,53,87,130,178..179,205,233..239,242,
                     244,253..255,289,306..310,314,318)
                     /site_type="active"
                     /db_xref="CDD:381320"
     Site            order(48,53,87,130)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381320"
ORIGIN      
        1 mkytrlpntn iriskiclgt mtwgrqnsee egyeqmdyal dqgvnffdta elypvpakke
       61 lyavteeiig nwfaktgnrd kvvlaskiag ngdytkfirt tgfakdalkt avegslkrlq
      121 tdyidlyqlh wperntnyfg qrgynaeqhd fwednfhqvl etlrdlvqeg kirhvgisne
      181 tpwgtmryle eakvhqdlpr mltiqnpynl lnrtfevgls eicmrerigl laysplgfgt
      241 lsgkylgevp prkgritlfp qynrysnena vqatrryqel atenglslaq malafvnsrp
      301 fltsniigat smeqlkenia sigidlpenv mkgieeihns ipnpsp
//
LOCUS       WP_010516489             697 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Komagataeibacter oboediens].
ACCESSION   WP_010516489
VERSION     WP_010516489.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..697
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77698
     Region          18..556
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mksqssipsv svsyahtgas tqanalgmrp mqerayekrg eqyllikspp asgksralmf
       61 ialdklenqg lkqviivvpe ksigasfhde plskfgfwad whvepkwnlc dspgtdggkv
      121 navgtfless dqtlvcthat frfavekfgi aafdqrlvai defhhvsanp nnklgqqlaq
      181 liehgsahiv amtgsyfrgd aaavlseede rkfervtyty yeqlngykyl kqldigyffy
      241 vnsyaddilk vldpaqktii hipsvnsres tkqkvkeveh iiealgewqg rdektgfhlv
      301 ktpegrvlri adlvddnsdr drvsaalrdp tqkhnrdyvd iiialgmake gfdwiwceha
      361 ltvgyraslt evvqiigrat rdapgktrar fsnliaepda tseavneavn dtlkaiaasl
      421 lmeqvltprf efrpkspqnn eepgfdygpe gydpkktnvg fseeqgvyhi evkglttpks
      481 eeairicred lneitatfvq dkptieqglf neelipeeit qvrlgkiike kypnldaedq
      541 eavrqhaiaa lnftqqgkqy alegvtqeea gpsggtglas ddqhprnnal ingvrqfals
      601 vreldidlid rinpfgeaya ilasamtees lkqvaaviaa krttltpeda kelalravrf
      661 kkernrlpsi tstdpweqrm aegaaafvrf kdegrye
//
LOCUS       WP_010516501             229 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Croceivirga radicis].
ACCESSION   WP_010516501
VERSION     WP_010516501.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..229
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=26161
     Region          1..229
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 msniindins illpkvcfgc ngklyrgehf lctvcrhdlp ftefnftqen avdrifygrc
       61 hikkassfly fynpgkvkql lhylkysrqk kignflaqwf gqqilaentl ptidfivpvp
      121 lhpkkqkkrg ynqlegfgke laillntkyk enaliktant ktqtkknrln rwlntknlye
      181 pnpsvdlsnk tilliddvit tgatiesctn alskhenisi yvatiafvp
//
LOCUS       WP_010516506             156 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Croceivirga radicis].
ACCESSION   WP_010516506
VERSION     WP_010516506.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..156
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16609
     Region          <11..156
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(36,38,42..43,46..48,50..51,55,58,67,69,71,75..76,
                     79..81,83..84,88,91,100,102,104,108..109,112..114,
                     116..117,121,124,133)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          36..67
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          69..100
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          102..133
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 meekkeffnd irngdantva qklkakpsli nakdergstp lilaayyghl avvevllskn
       61 ipidvkdgtg ntalmgvcfk gysevaklli dkgadvnqtn smggtcliya atfnhiaivk
      121 lllangankn akdarghtal dharmqgate lvnllq
//
LOCUS       WP_010516572             104 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thioredoxin family protein [Flavobacteriaceae].
ACCESSION   WP_010516572
VERSION     WP_010516572.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..104
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11686
     Region          8..86
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(29,32)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mlleleqdnl qeiiaensnv vvqysaswcg ncrimkpkfk kearenenvt fvlvdaekfp
       61 esrklatvdn lptfaafqng slknqvqtnk ydvlktlvhe vaan
//
LOCUS       WP_010516576             152 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Flavobacteriaceae].
ACCESSION   WP_010516576
VERSION     WP_010516576.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..152
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17500
     Region          1..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 meldatdkkl lnllqqdckk ttkayalelg lsttavferi krlernaiit dyvglvdkkk
       61 vqksftvych ikliqhtken vlrfehqiqq lqevqecqhi sgdydyivlv nvanmqeyre
      121 fmvnkltaid qigstqssfv inqvkkttav yi
//
LOCUS       WP_010516449             120 aa            linear   BCT 01-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Komagataeibacter
            oboediens].
ACCESSION   WP_010516449
VERSION     WP_010516449.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..120
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=13771
     Region          10..115
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 msdrsdddil tvwydggcpl clreialmrr ldranhihfv dvadpaqpcp ldrqllldrf
       61 harkgtviyd gaaafaamwr aipvlrppge larlplvlwg levayrrflr vrpilqrwvr
//
LOCUS       WP_010516678             216 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Croceivirga
            radicis].
ACCESSION   WP_010516678
VERSION     WP_010516678.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..216
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23717
     Region          15..187
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mlnlhiatia iiaanvlvsl rgfkdqlffd rykfqigaiq agqkermfts gflhvdiahl
       61 ffnmftlyff advviawfgp skffivyvis llagsllaly fhknetyysa vgasgavtgi
      121 lyaaillqpn mqlgllfipi plpayifgia yllysiygmk srlgnighta hfggaiggya
      181 ttllfrpsll ttdplmvfll aipivilfvl aktgki
//
LOCUS       WP_010516694             444 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Komagataeibacter oboediens].
ACCESSION   WP_010516694
VERSION     WP_010516694.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..444
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47482
     Region          8..417
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mssitsevsl rekvaygcgd lssnlmwgmt ssylmfyytd iyglpvvavg willvarvfd
       61 afcdpaigyv idrqggqivp rlirslalpf gvagfvcfvs lplspngkil walltyivlg
      121 aiyscintpy galgtmitrq ahdrvglnaf rmmgcqggqf ivslftipai twlgggngmv
      181 qrqhgmalya lclaiaatil wryvgrvcit ryppaparhs pvvllralaq nrcwwlcngl
      241 vflqfaglaa lygfalyyar iilggtdemg gvlltvatim gfagaiicph ivrrlgvigs
      301 aaacggvqvm aylllglagg cvpfffaafa mltlaqgits plyyvllahg idvgrmtspv
      361 ntagmaysin tlvtklsmgv tgfilatfla hghyagdvht fspalkhwim agfvwlplga
      421 aalqlvllai wprgvaspvt rrnp
//
LOCUS       WP_010516784             153 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Croceivirga radicis].
ACCESSION   WP_010516784
VERSION     WP_010516784.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..153
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17460
     Region          90..148
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 maksqqtfnk rekekkklkk reeklkkkea rraeakdsdg gipfayvdkf gnltdtppep
       61 teeeeidase ivlgipqkee teedkfdpir kgkvsffdhs kgfgfiidse nnekyfchvs
      121 glndeitend kvtfelekgq rgmnavrvnl dks
//
LOCUS       WP_010516806             296 aa            linear   BCT 01-JAN-2025
DEFINITION  pirin family protein [Croceivirga radicis].
ACCESSION   WP_010516806
VERSION     WP_010516806.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..296
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33099
     Region          16..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msntdliiee raanignfmv grllpfrqkr mvgpfifidh mgpahmtaeq nmdvvmhphi
       61 glstltflfe gsvfhrdslg taveikpgav nwmtagkgvv htertpdylr nqsktlhglq
      121 iwvalpkdqe ecepsfthvr aeqlpswved gvefkliage afgkqsavpv ysplyfieik
      181 stttktvaig eylygesaly ilegaikleg nqygpkqilv aknstlcafe lqanttvyif
      241 ggdpfpeerf iewnfvasdr alikkakedw vnnkfptvpn etmrvplpqp kglknk
//
LOCUS       WP_010516829             374 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Komagataeibacter oboediens].
ACCESSION   WP_010516829
VERSION     WP_010516829.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..374
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40789
     Region          6..355
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,235,309,329,331..333)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,235,249,309,329,
                     331..332)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,332)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msssslfepv rlgdlslenr iflppltrcr stqpgdipna lmaeyyaqrt qagflitegt
       61 qieprgqgya wtpgiyspeq vagwklvtda vhakrrpifa qlwhvgrvsh ralqpgheap
      121 iapsavaatg vnvfipmgsg tgklvppdvp ralsipeihe lvelyaqaar nalsagfdgv
      181 eihaangyli nqfiseranf rtdayggsls nrlrflrevv eavsavvtpd rlgvrfsplf
      241 gttteervyl gllednpaet ytaavrvlad agiayvslae adwdnapemp dafrasardi
      301 fggrilcagr ydlhkaqhvl ahdwadmigf grkfianpdl ptrlkhgwpl nsldpttmyg
      361 ggahgytdyp fhnq
//
LOCUS       WP_010516819             296 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Komagataeibacter oboediens].
ACCESSION   WP_010516819
VERSION     WP_010516819.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..296
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32782
     Region          24..174
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <186..283
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 metqlqelrr laawaenrrt etgiprvamv qgeipehqla avydpminli ltgsktmtvg
       61 srtlrydpat yfvmsvdlpa vgalhpsekg qpylavsltl tpaiiaslla dlpepagsdp
      121 sspgfsvapv tpelldawvr llrlmehpde iaalapayer eilfrvlqgp lgwmlrdiat
      181 pdtalsrvan tvhwirenfa rplrvsdlae maalsistfh rhfkavtals plqyqkrvrl
      241 lharslliag egnitfaafh vgyespnqfs rdyarqfglp psrdvvrlrr mtsgrd
//
LOCUS       WP_010516869             173 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Croceivirga radicis].
ACCESSION   WP_010516869
VERSION     WP_010516869.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12134272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..173
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19443
     Region          13..154
                     /region_name="Acetyltransf_3"
                     /note="Acetyltransferase (GNAT) domain; pfam13302"
                     /db_xref="CDD:379112"
ORIGIN      
        1 mpihllenvt terllfrkva psdfqawlpf yhdpsstlyw nglpkdpiia cneqfyrife
       61 ryalnlggmn avihkntgel lglcglllqt vdgvseweig ysllpkfrkm gyateaakac
      121 ktyatknkla pslisiihin nnpsiqvaik ngmrldkatt yknnpvaiyr iql
//
LOCUS       WP_010516898             197 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Komagataeibacter
            oboediens].
ACCESSION   WP_010516898
VERSION     WP_010516898.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21827
     Region          4..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkiaekhraa rqhileaarp ligqrgfsav glaqildvag ipkgsfyhyf eskeafgeal
       61 lqtyiddyli kmddilgndd enaaqritry cqfwrdthie gqignkcliv klaaevsdls
      121 ermraildvg trtvidrisa viakgqeegs igstqpalml aaslyqlwlg stlmvkiths
      181 sppfdhawea srqllei
//
LOCUS       WP_010516904             751 aa            linear   BCT 01-JAN-2025
DEFINITION  S41 family peptidase [Croceivirga radicis].
ACCESSION   WP_010516904
VERSION     WP_010516904.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..751
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=85207
     Region          <472..748
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mknflplffl siwftvcngq vnqkienqka fakvygyvky fhpsdeasti dwdkfaiygs
       61 sqvencksda elldtfkrif epiapsvrfy tdedsgdydf keitpkdlen ydlvywqhng
      121 vsfgmtnngr pyssvrvnre feidksssvg nimtsvaase ysgkefkysg wvklakgsqg
      181 tgnlwfrvdk sdgsmgffdn manspitdsn wqryeitgti dslasrlafg cflmgkgkll
      241 lddvelsykd nekwtiiplg nngfegekit degqwktsgl gyvfntsetd kneggksaii
      301 qyqgnvekgl gkklfdnqpe fgelinkkih kniychipiv vygskehtyp ipnakdlsll
      361 knnvegists ntdltlrlgn viivynifqh fypyfdvvkv dwekelekal lrcytdktek
      421 dhlitlqklt aslkdghvrv snknmerfvp piswewvenk liitdiyddi dglaigdevl
      481 kidgknsvdf fdeinsrisa gtdgwakyra qteslygpkd sklvmtlqdk tielsrdkdi
      541 yranrqnsip kipykeinkd vfylnldman mdtintlvpn mkdytsiifd lrgypkgnhg
      601 vishllktkd ttkgwmqvpq iiypdqenia gwtkyewelk takpylgdkk iifitdgrai
      661 syaesfmgyi egyklgtivg qptagtngnv npfqlpggys mswtgmkvtk hdgsqhhgig
      721 vlpniyatrt iegikagrde flekaveltk k
//
LOCUS       WP_010516936             596 aa            linear   BCT 01-JAN-2025
DEFINITION  T9SS type A sorting domain-containing protein [Croceivirga
            radicis].
ACCESSION   WP_010516936
VERSION     WP_010516936.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..596
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=66055
     Region          528..593
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 mkkslligfl fiatgvyaqe ltvqitrlin wnkdynksfg flqsgfvtds ngnkivvggf
       61 dgldvdfgtd dtlssdrnld vfivkydsld nlvflknigg iffqeggysn dyasdvkvds
      121 enniyvmati dagtlqkvdl dpehpennsv istshgndfs iynhnaylik yspegkllwy
      181 reikddfidr sfslyidtnn dvwatgyvgg ftganidfdt nneypdnrdi iqgefyrlgf
      241 varynsdggf igvkgigggt fsnlhvcvap tgnmylagsf sanitdrwqg lslfknddvp
      301 vyiesqgyfe ftpqntdvfi lkcnalgnve wvktisstls nevtdialdd kehvyisgyf
      361 sgnnvdfdne nnlsfdtkss asngsgfvae yntngnlnvl ntidggartr iqslavsnng
      421 tialgghfeg nvkmgdfsfd sssstsnpfi avidsignwn nakeieknsf asitnveisa
      481 nndvqfvgfe atnydeeyni ksifygnaes eifetptpdv sdkkniivyp npssdivnie
      541 tdknvekiai ydlngklimt kkdsnwigvr flpdgvyiir lhldnnedyi klilvr
//
LOCUS       WP_010516923              91 aa            linear   BCT 01-JAN-2025
DEFINITION  HU family DNA-binding protein [Komagataeibacter oboediens].
ACCESSION   WP_010516923
VERSION     WP_010516923.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..91
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9553
     Region          1..91
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mkiadlvdhi atatdtsktd trkvldalve amttaakagd eitlpnfgkf kvrevaareg
       61 rnpatgatiq iaasrklvft pakalkdsln d
//
LOCUS       WP_010516970             203 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Croceivirga radicis].
ACCESSION   WP_010516970
VERSION     WP_010516970.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..203
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23833
     Region          42..197
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mrdffsaeet ilfnffnqvy plsendfrpl akaikkkklk kgenllnigq ietktsfvlk
       61 gfihqyvtie gelftidfal egmsfnnfts ymenspsnqv qealtdteil yfekediehl
      121 llqshpfsys ytklfeqvhl erekrslllq hknaykkyel flttipkaki fleqvpqkli
      181 anylgitaet ysrvkkeylk nkn
//
LOCUS       WP_010516986              66 aa            linear   BCT 01-JAN-2025
DEFINITION  CsbD family protein [Croceivirga radicis].
ACCESSION   WP_010516986
VERSION     WP_010516986.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..66
                     /product="CsbD family protein"
                     /calculated_mol_wt=7514
     Region          6..65
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 msapwkdkak gnwniakgki kqewgeltdd dldyqegked elvgriqkkt geskekvndf
       61 lnslky
//
LOCUS       WP_010516989             279 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Croceivirga radicis].
ACCESSION   WP_010516989
VERSION     WP_010516989.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..279
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32878
     Region          90..249
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 meildavlni npnyviigll alfftleqia ktpfvfksrg mhlaqnilfq lvltvlnlff
       61 valqvyciew lnahkiglly lveipfwakl flsvvlydft tywihrashk vpvlwrlhrv
      121 hhsdttmdss ttfrfhplel iliyqtgnil talifgtdvm amavyylfly vffflehsnl
      181 nypswlnnsl glifvmpdhh rvhhhqeqyy tdsnfadifi iwdrifgtfk lipvadiryg
      241 lkefesekkq sflylmkspf iqveseiekp ieenrnqds
//
LOCUS       WP_010517035             780 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Komagataeibacter oboediens].
ACCESSION   WP_010517035
VERSION     WP_010517035.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..780
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84907
     Region          131..564
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mvkretggpq vhqqlkhgst yrdtrpftvr iaeelqsgss gfilvilagl gvlapaiigi
       61 tfplalclml wvmtrhpvlp fhlprysglk drhdldpktr rprmaagiiy lgtdgltgqq
      121 lwlssdagrq haavpgttga gkttsaisll anplahgsgf ilidgkgdnt vhgdvlalar
      181 rfglddqvln lnfltasgir qsntfnpfat gnadaireml vsqlgepssn dangvfrdra
      241 vglagtiapv ltwmrdthgv pinietmrya melrwigtla rhrvflirnp gsdhpieisv
      301 peipddilyp aqaylgelpg ydsslawneq kenrpseqhg yakmyftrvf tqlgvslghi
      361 fraqipdidm rdvvlnrril vvtlpalens sdtlaglgki vvaagrgvma qllgarldgp
      421 aeqvfklkag sgdapfhffy delsayvtdg mdrqlamgrg lncmfwlgfq dlpglttrig
      481 dkaftllgna nlthamrlqd amrtrewiek qsdrievsqa thfegnsags yregrgaevr
      541 evaripwadl qsliegeait myagrivhsk tffaavngrs gairmaqpvm laapldlnrv
      601 ppdqqllall atiegglfqs elttlhdepd vralqeavdr lgsgsqdilr nfaqigaava
      661 aaprrvatan ddeeneraag tdmltpfsym lrdaaaipkp gfqtpprtip pidghllgrl
      721 eaierrvdrq pgvarrqafl imgvrdamtk gtptdgaast gmtekeilaq irilrektaa
//
LOCUS       WP_010517036             166 aa            linear   BCT 01-JAN-2025
DEFINITION  Dps family protein [Croceivirga radicis].
ACCESSION   WP_010517036
VERSION     WP_010517036.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..166
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=19282
     Region          1..154
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mnylnldeek vlpvvielnt lladyhlyyq klrnyhwniv grnffdlhek feelytdarv
       61 kideiaervl tlryhpmsnl ssyletssie ettkilndne mvedllkaha ilikqmgnvv
      121 aeadkiedeg tidligayir eleksswmld awtktttdtl krsvpa
//
LOCUS       WP_010517069             186 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Komagataeibacter
            oboediens].
ACCESSION   WP_010517069
VERSION     WP_010517069.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..186
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20342
     Region          8..185
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 masdqtssrr fdpdrkqrii daaldvivah gvqgtthrrv amaagvplgs msyhfagmdd
       61 llhmafrqva qaasaafvaq lskarnrqda ieaiidiiag niwstprtll lsyelyafaa
      121 rkpelaavmr dwmqasrdal grffdpltcr aldalvegmg ihdsvdhspl grgdiadivh
      181 ricrqd
//
LOCUS       WP_010517195             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Croceivirga radicis].
ACCESSION   WP_010517195
VERSION     WP_010517195.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..269
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29997
     Region          50..260
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mnwksafyas ltcvflfscg nkkksenskp dhlakednsk qlvtkttsal tinpiehatm
       61 vlekngtvvy idpvggaekf esyklpnyil itdihgdhln vetlsglsld dakiiapsav
      121 aeklpedlkg ktivldngdt kqlntelsvn aipmynlree alkfhakgrg ngyvlnwide
      181 riyisgdted itemrnlkni dkafvcmnlp ytmpvasaad avtdfeptvv ypyhyrgtqg
      241 lsdieefkrl vlaekpniev nflnwypaq
//
LOCUS       WP_010517109             975 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Croceivirga radicis].
ACCESSION   WP_010517109
VERSION     WP_010517109.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 975)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..975
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..975
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=108950
     Region          130..205
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          200..923
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtirglsnll lslvffcfst fntaiyaqnl ksetnlvtll hqlskdynvy fnynpedlkd
       61 lslntsgleg vrlkkklkqi eqltelkies lgsryyviys skdlnksnnk ikgrllthqn
      121 klrlqnkvig kitdlnglpl agvnirikgt tigttsnfdg nynldanpnd mlvysyigfk
      181 tkerkadknv inivliegis lnevvmignr skprtvinsa vpidnisavd lsstgqstld
      241 qmlnykipsf nstnqaisda tahfdpadlr glgpsrtlvl ingkrknqsa lvyindtpgk
      301 gevgvdlksi paaaiervev lrdgasaqyg sdaiagvlni vlkknkqytq ietqtgittr
      361 gdgfsngvsi nsgipfqnsd gylnltaafy qqdftsrtnn lgfdalynit endtewanwl
      421 qkypdlgmtv gqpktknynl nynfelpvsp tcswysfggl syrigesfal yrapywiedp
      481 nnlfheqnea yegfqptfet dirdnyftlg fkcqilgfkt disatqgrna vdylvansln
      541 qslgansptr fdvgsyafdh iltnmdftka fgktninfgw evrresfrst agepasylge
      601 gtvsfpgiqp rdqliatrnn fgsyaevdhe fskrfmlgta iryeyfsdfg kniswkassr
      661 ytfkedkgal rasvstgfra pslhqiylsn tqtlvsgesv snqgtfsnqd piirdnlgvk
      721 qltaersrni tagitikpld nlffsadfyn vyvknrvlft neigfdedla qinpvesili
      781 annitslkff inavntntng ldlvgnytni klgeawgklt laanfnktri vddiaaptil
      841 knnnyeifnr keqarilsar prskvllgfn ynlrrlnlgl nntffgsvkw qhaedpgkdq
      901 tftgkiltdi tlnyqlntni sfycavnnif nvypdeldnk gdvltdlggr fkyawevnqf
      961 gfngttlngg lrikl
//
LOCUS       WP_010517202             542 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Croceivirga radicis].
ACCESSION   WP_010517202
VERSION     WP_010517202.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..542
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58926
     Region          15..533
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mdlnfnkned ynkllrsdln rrlakvklgg gtkriekhka kgkltareri aylldsdeea
       61 ieiaafaged myaehggcps ggvvvkigkv kgkqcivvan datvkagawf pitgkknlra
      121 qeiaienklp iiylvdsagv ylpmqdeifp dkehfgrifr nnavmssmgi tqiaavmgsc
      181 vaggaylpim sdealivdkt asiflagsyl vkaaigesid netlggatth ceisgvtdyk
      241 aaddkdaldk iksimgkigd fdkagfnrep sklpaknqed ifgilpksrg dqydmleiie
      301 rlvddskfeq ykqdygktil tgyaridgwa vgiianqrkv vktgkgemqf ggviysdsad
      361 katrfiancn qkkiplvflq dvtgfmvgsk sehggiikdg akmvnavsns vvpkftvvig
      421 nsygagnyam cgkaydprli cawpsaelav msgnsaakvl lqiekaslek qgeafdaeke
      481 kalyskikar ydnqispyya aariwtdaii dpmdtrkwis tgieaanhap iekqfnmgvl
      541 qv
//
LOCUS       WP_010517214             310 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Croceivirga
            radicis].
ACCESSION   WP_010517214
VERSION     WP_010517214.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..310
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=34878
     Region          134..238
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 myieqgykst pglwkffvlp fgfigfmlln yiatlmsnmd veasmamlid klgknitlif
       61 llaplvvglf vvlgwvllvh gqsitaltts rkkidwkrvf fafgvwgtlt viltmtdifm
      121 spedyvftfq lnkfipmavi aillvplqts feeylfrahm mqglgllakn rwvplfttsi
      181 ifglmhianp evgklgmgim vyyigtgffl giltlmdegl elalgfhaan nlisalllta
      241 ewtafqtdsi ytdvsepilg wdvlvpvlvi fpillalfgk iynwknwkek lfgrvltkee
      301 ffakenatts
//
LOCUS       WP_010517233             212 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Croceivirga radicis].
ACCESSION   WP_010517233
VERSION     WP_010517233.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..212
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24950
     Region          24..202
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mdrkvvsyts tnnyetlnrn tpyteniwlv fhgigylsry firhfsnldp lknyiiapea
       61 pskyylkddy kyvgaswltk eytqreinnn fnyldaiwae erinkdkklv lfafsqgvsi
      121 llrwlahskv pcteiillag sipkeleqkd ylhlektkik yvygvndqfi taekimieke
      181 fmktlfpnev evitfpgghe ipknwmqivf np
//
LOCUS       WP_010517269             289 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Croceivirga radicis].
ACCESSION   WP_010517269
VERSION     WP_010517269.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..289
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33681
     Region          175..286
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 msnnyvysll lagflslnaq qkdmqafipl lgktwiaega wgngstfkqe qifkitldsn
       61 lvitetkgfl dpeqkafghr ahgirkfepr tgkikfwefd iegnttegkv yitdkdiwys
      121 ydyggtqvtd hweylndhty nytvgvydkg aweqiflktq flalnnqfef tikqvnlftt
      181 didntakfye rifgfrtsgn ehekfkllyl daqtqikllk kdsltsienn iinlttpyln
      241 rvishlksnn ipyyksakke rypldkseyl erifiqdpng qwieisnvn
//
LOCUS       WP_010517270             334 aa            linear   BCT 01-JAN-2025
DEFINITION  pirin family protein [Croceivirga radicis].
ACCESSION   WP_010517270
VERSION     WP_010517270.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..334
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37899
     Region          59..297
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mnaihkifpl gfpwqtqdpf lfcvyhqdny pegtetlgpd qkhlegrplg ndfqkkngfr
       61 myhgktipgf pyhphrgfet itvvnkgycd hsdslgaagr fgmgdvqwmt agrgvqhsem
      121 fpllhqdkpn tlelfqiwln lpqkdkftep hfkmlwredi pivtengtel qliagtyhgn
      181 kapspapnsw anlsenevai wtlklkpnst ftlpttnati nrtlyfyege qlqinqepik
      241 vnhgidlnpn ikteistnak sasllllqgk piaepiaqhg pfvmntkkei eqafeeyrlt
      301 qfggwpwpya dnvhesgrgr fakypdgtiv ekel
//
LOCUS       WP_010517300             319 aa            linear   BCT 01-JAN-2025
DEFINITION  PhoH family protein [Croceivirga radicis].
ACCESSION   WP_010517300
VERSION     WP_010517300.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..319
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=36123
     Region          1..318
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 mneliielte isprdffgnq neniellkky fpklkivarg nkikvygdee lleefdrrfd
       61 mitehfakyn kidenaierl ltsdskeeiq ssaasgevlv hgvsgrlika qtvnqrklvd
      121 aimkndmvfa igpagtgkty tgvamavkal kekqvrriil trpaveagen lgflpgdlke
      181 kldpymqply dalrdmiape kldkyiedgt iqiapmafmr grtldnafvi ldeaqnttha
      241 qmkmfltrmg knakflltgd pgqidlprrv isglkeaili lknvegikii ylddkdvirh
      301 klvkkvieay kdiehqnqf
//
LOCUS       WP_010517361             214 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Croceivirga radicis].
ACCESSION   WP_010517361
VERSION     WP_010517361.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..214
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24648
     Region          <1..188
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mklykflfkr iidfitaffg lvlllpvfil vtvllwidfk gspfftqerp gknervfhil
       61 kfktmndetd ksgkllpdnq ritkvgafvr ktsldeipql vniikgdmsl vgprplrtyy
      121 lpfynevekk rhlvrpgitg laqisgrnfl tweerfdldv eyvenigflm dakillqtfk
      181 kaisgkdvae dpdafiesfd vhrkkqlega vkst
//
LOCUS       WP_010517367             315 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Croceivirga radicis].
ACCESSION   WP_010517367
VERSION     WP_010517367.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..315
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37735
     Region          <96..292
                     /region_name="BcsL"
                     /note="Acetyltransferase involved in cellulose
                     biosynthesis, CelD/BcsL family [Cell motility]; COG5653"
                     /db_xref="CDD:444374"
ORIGIN      
        1 mtslpkhytd hclfqlylnk tlhaahqgkv qnllvnryls ltpsiyqene ksfyiikdvp
       61 dylyfqehip ldhgfikvpq yhghlvnlys yqnlseylnd qlskrniknl kskkrklesl
      121 gkieykvlsd dlgeleyaki fnhfkellsn rfdqkgilnr dlshwqqlyr ftlpklcsge
      181 akmfiiynne lpicialnyi vdhvmfshiq tydtdyskyn lgdihmqfql ewcfsnnidi
      241 ydvskgtnpy kekwcnhryr lfheivyskk svtgtlrskl kkmelnilqr frnigilgsl
      301 iqmdkwlyki ykwrk
//
LOCUS       WP_010517279              90 aa            linear   BCT 01-JAN-2025
DEFINITION  HU family DNA-binding protein [Croceivirga radicis].
ACCESSION   WP_010517279
VERSION     WP_010517279.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..90
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9277
     Region          1..90
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mnktelidam aadagitkaa akkalesflg nvegslkkgg rvslvgfgsw svskreareg
       61 rnpqtgqtiq iaaknvvkfk agselsdavn
//
LOCUS       WP_010517500             447 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Croceivirga radicis].
ACCESSION   WP_010517500
VERSION     WP_010517500.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 447)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..447
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49795
     Region          1..443
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
ORIGIN      
        1 msklgliikr eylakvrnks fvimtflspi lmvgmivlia yltkvndses rtiailnqsd
       61 yfsnaftpte sisyvsfkdi tleeakdstq sldyyallhi pkedsleeta estflyakdn
      121 pnssvlnrle gifeqrlrqa rlqdlgiske qfatvdtkfq mhagtfkgee nlkginelka
      181 iigggfgyli mmfiiiyggf vmrsvieekt sriieviiss vkpfqlmlgk iigtslagit
      241 qftiwiisas mllfvallll didlatltqg qplgpgamag mgdfadaknq kmllyaaeff
      301 kipwvlivvs fliyfvlgyl iyssiyaaig aavdnetdtq qfifpiilpl mlaiyvgffs
      361 vfsnphgpia vgfslfplts pivmlmripg glgeggvpiw qfvtsiilli ltflaivwla
      421 akiyrvgilm ygkkptykel fkwlkyk
//
LOCUS       WP_010517527             525 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Croceivirga radicis].
ACCESSION   WP_010517527
VERSION     WP_010517527.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (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   5  (residues 1 to 525)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..525
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58131
     Region          82..487
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkndiklkka varflilcvm lpfagcslee etysiytpet fyaneqqils slsgvyrffa
       61 sttgmgveyr clelsadqvv vhekiqgwwg ganfsqlmeh ewdashgyig gawntyfrtv
      121 gqtnalissl ensgldgslv dgpiaelrtl rayayfflmd lfgnvpvftd pkvdplnlpt
      181 qntrtevfqf vttemeaale nlptkseagn ayygrftkea vnallsiiyl naevytgnam
      241 ydkaitnada vinsgaysll pnyfdnfvyn ndnnaefifg avyspdisgg ighplvqkvl
      301 pgiqgglfgl pytpqngfgt rpsvmnkyed eddrksmfig ygpltdprng evvmverivp
      361 dnnstlynpd tstegpvpye iipatgirlq pmnagikwvk wgldpntngg nagndiafvr
      421 yadillvkae allrngdagg alplvnqvre rsnatlltav tlddilderg relafemsrr
      481 rdlirfgkfg dawefkevse dfrtlypipr aaieanpnlq qnpgy
//
LOCUS       WP_010517613             830 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 3 protein [Croceivirga radicis].
ACCESSION   WP_010517613
VERSION     WP_010517613.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 830)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 830)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 830)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14303124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..830
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88910
     Region          63..>461
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          429..633
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          667..817
                     /region_name="Exop_C"
                     /note="Galactose-binding domain-like; pfam18559"
                     /db_xref="CDD:436577"
ORIGIN      
        1 mftkavlrct lvialfflac kqqtktpepl leskamltdw pvfepqpldp kiearidril
       61 pqltleqkvg qiiqadsesv tpeevkqyrl gsvlsggnsa pgnkayadaq twlqmadqyy
      121 nasvdaegva vaipiiwgid avhghgnleg aivlphnigl gathnpeliq klaaitahel
      181 tvsghdwtfa ptlavpqdvr wgrsyegfse apdlanryad kivlglqgqr gdagfmgagr
      241 viscakhfla dgatengvdq gdakidesel lnvhaagyys aipagvqtvm asfssyngrk
      301 lhgdyellte vlkgklgfng fvvgdwnghg qvpgctnedc pnainagvdm fmapdswkgl
      361 yestlkhvke gtitlerldd avrrilrvkl asgifekgap strpfagden qlalpahcal
      421 arqavreslv llknnnqllp ldasktilvv gdgaehiika aggwtlswqg eghtndefpn
      481 gesilegike avakkggkli fspeadtnlt advviavfge dpyaefqgdr khldfvpngf
      541 dteklatyke kgipvvsvfl sgrpmwtnpe lnnsdafvaa wlpgsegggv sdllfqrdsg
      601 ydftgklsfs wpatavapqt kdvlfglgyg lnygstekvp llledaglen vtvastgvff
      661 dkgqatapwq lqlqsaelek qvasfptsig gllvaktdhk aqedalklew tstellqaql
      721 vtaspvdmar esngamelaf yarnfgqeta tvqiglcgtp glcnqtlavt isgqewkayr
      781 lslscfeklg vdmsnittaf sisapqgtql glaaiqlatd adakpgcngq
//
LOCUS       WP_010517614             247 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Croceivirga radicis].
ACCESSION   WP_010517614
VERSION     WP_010517614.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..247
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26857
     Region          17..224
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mknlsylfll lsllaeilgt iggfgssvff vpianfyftf eavlgltaiy hlssnlskia
       61 lfkkglnktl llqigipsvv fvvsggllan yfkssnlelv lglflvvlal afliksnwvv
      121 npnkknalvg gslsgfsagl lgtggairgl tmamfnlekn vfiatsafid fmidfsrtfv
      181 ywyngfihka tlvyvpflll igfigtwlgk klldyipqer fkrislglil liglatlvkv
      241 fttsvpt
//
LOCUS       WP_010517619             243 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Croceivirga radicis].
ACCESSION   WP_010517619
VERSION     WP_010517619.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..243
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27356
     Region          163..240
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 merkknpqad lnrnsglyfv iglaivlftv wrlleyktyd tvkeydtvln vmdnmdeevp
       61 itemiktvtp ppppaapdvi aivedmveve etiiestess qetyvedaiv sveeveveev
      121 eeeisvpfav iedvpvfpgc enlatnaerk acfnemiqeh iktnfkypst aielgiqgrv
      181 yvqfeinqyg kvskilergp dklleaeagr iiallppmkp gmqrgrpatv ryavpinfvm
      241 qmq
//
LOCUS       WP_010517785             119 aa            linear   BCT 01-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Croceivirga
            radicis].
ACCESSION   WP_010517785
VERSION     WP_010517785.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..119
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=13750
     Region          1..117
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 menltnkeee imkvlwklek afvkeileam ptpkphyntl stivrnlqek gfvaheafgk
       61 thryyptvtk enyrnsfvnt aiagffndsy knvvshfake ekisvdelke iialieknn
//
LOCUS       WP_010517749             151 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Croceivirga radicis].
ACCESSION   WP_010517749
VERSION     WP_010517749.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..151
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16880
     Region          3..136
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 meikldplsk eilnclqena rasyaeigrk vgltspavae rikkledlgv itgyqakiay
       61 aklgyqlkam vtlrafvgkl kpfleqvksy eevincyrit gneniimevv ikdqmhlenf
      121 idrlivygea rthivlskva gsnslinpkk q
//
LOCUS       WP_010517773             141 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Croceivirga radicis].
ACCESSION   WP_010517773
VERSION     WP_010517773.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 141)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..141
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15789
     Region          1..122
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mkrivyiall lplgllaqnw qtdfaaatsk anseqknill vfsgsdwcap cikldrkiws
       61 tpifkkaaak nwvlyradfp kkkknklkae vlnqnktlae kynskgyfpl vvvlrpngtv
      121 vgtagfndmd vesyiehlks l
//
LOCUS       WP_010517808             209 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Croceivirga radicis].
ACCESSION   WP_010517808
VERSION     WP_010517808.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 209)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..209
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22574
     Region          1..209
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 missnsltyq ypssssvlaf pnlnldeaes llilgksgvg kttllhllag llspatgnvt
       61 inhtnittls akaldafrgk qigmvfqnnh alrsltvlen lkarlyftkk tsnknalvel
      121 lnvlgiadcq nkktnelsig qlqrlgiala vvhqpklils deptsslddt nctkvmqllq
      181 eqatankanl ivithdqrik anfknvltl
//
LOCUS       WP_010517814             470 aa            linear   BCT 01-JAN-2025
DEFINITION  alkaline phosphatase [Croceivirga radicis].
ACCESSION   WP_010517814
VERSION     WP_010517814.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..470
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51312
     Region          1..467
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mnrrkffrnt slgalgtsll apfnsleaae taasfknkka kniillvsdg mstgtlnmad
       61 lhltrktgig shwmnlyren kvtralmdta sassivtdsa aassawgggv rvpngrinid
      121 angkanlpiw qkfksagkka gcvttvpith atpagfcini ksrndqdtia ekyleqdfdv
      181 lmgagnehfa adkrkdgkdl yhafatkgys vvkdkktmqn assqkpllgv fydsglpyak
      241 dqentkelan svptlaemtk kaidnlkdak ngfvlqveag kvdwaahand itgllydqia
      301 fdeainaamd faekdgetlv iittdhgnan pgviygsnan tnfdsiqhyk ftnswilngl
      361 gkessintvk eriayangia iddeaaklll syyknlntda gwynpkklpf rplaelqkeh
      421 nsvgwismqh sadyvelamy gpgselltpf ikntdlhylm lnatevqnnf
//
LOCUS       WP_010517828             229 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Croceivirga radicis].
ACCESSION   WP_010517828
VERSION     WP_010517828.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..229
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24774
     Region          2..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mlkavnvtks yngkvalkdi sfsvekgeif cllgqngagk tttiniflgf ikkdsgqafi
       61 gdkevgkdnt nlltayipet vqlygnlsgv enldffsrla gytyttqele aflaktdlqa
      121 eahhqrlssy skgmrqkvgi avalaknaev ifmdeptsgl dpkataeftk ickelaamgk
      181 vifmathdif navelgttig imkegvlaqq lkaseidagq lnqlyleti
//
LOCUS       WP_010517848             216 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SOS response-associated peptidase [Komagataeibacter].
ACCESSION   WP_010517848
VERSION     WP_010517848.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..216
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=24175
     Region          1..207
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcnlyamtss qqaireaarv mtdrtgnlrp lpeiwpntla pivrntpdgr elvmarwgmp
       61 tppgylkghr vdrgvtnirn pistwwkrwe gvahrclvpl tafseperlp dgtsrpvwfa
      121 rsdgeplaff agiwcqwtsv rkladgettd dlfgflttta nrevgaihpk ampviltrle
      181 eldlwmkgpl ddalqlqrpl pddaltvana svgrny
//
LOCUS       WP_010517978             800 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Croceivirga radicis].
ACCESSION   WP_010517978
VERSION     WP_010517978.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..800
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90118
     Region          36..120
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          107..744
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mqkyyssnpl kyaqllllfv fsyysntgya qekytlsgvv keassnetli gvtvavanls
       61 tgtvtneygf ysltlpqgsy qivvsymgfk eeyvtvnleq ntkmdfalte eaeqlaevmv
      121 sedverldvr kpqmsvntls aatikkvpvv lgeadviksl vllpgvtnag egssgfnvrg
      181 gavdqnlill deatvfnssh lfgffsvfnp daikdlklyk ggiparyggr vssvldiyqk
      241 egnskefkvn ggvgavasrl liegpiqkdr tafliggrss yahlflplfd idskayfydv
      301 ntkinhrine nnslylsgyf grdlfslnes fvnvygnavg nlrwnhlfnd rlfsnlsliy
      361 sdyyygleld fvgfewdsgi qnfnvkydlk hylnnklqin yglnniyyvf npgeitpnrs
      421 nsgiiedqlt kkyaneaaay idveheisnk lsinyglrvs hfnrlgqdef fvyqnnqavv
      481 fderqqvyke atpidtltpg rggslakftn leprlaiays indnssikts ytrlaqylhl
      541 lsntssptpl dvwtpsgpfv qpqlldqyal gyfktinggd ytlevegfyk diqnridyid
      601 gadliannai eqvilngqar aygleflfrk negdltgwls ytlsrseqrt pgrtaietgi
      661 nnsnwyasay dkthdlsina nyelndkwsf gsnfifqtgq ptnypvgqfq qqglvvpiyg
      721 ernktrlpay hrldlsatlt prknknrklq gewvfsiynv ynrrnaasin fsrnedngrn
      781 eatrtaifgl ipsvtynfkf
//
LOCUS       WP_010517986             463 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Croceivirga radicis].
ACCESSION   WP_010517986
VERSION     WP_010517986.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..463
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=50041
     Region          102..373
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mrrtaqlffv allaggvtlg ayklffekeq ftfvaqnett pflttsmpts pkgaginevd
       61 ftvaaektin avvhvknmtv spanplaeff ygfkggqtpq igtgsgviis pdgyivtnnh
      121 vidkanslei tlnnnksyea eivgtdpssd iallkieven plpylafgds dnakigewvl
      181 avgnpfnlts tvtagivsak arsistnrdq sfiqtdaavn pgnsggalvn tngdligint
      241 aitsqtgsyv gysfavpsni akkvvddlle fgkvqkgilg isalsldspq akemnidqvn
      301 gvyvagvede sgaeeaglke gdiikqvgni kvskfseltg ylsskrpgdv vevlvdrgge
      361 tktfevelkk rqteilpvmg lqvknlsked qkkyktkkgv kitnvperyr gyeledkvmi
      421 liddneirdv edakelfqki trygrtsitl lgengererl ifq
//
LOCUS       WP_010518044             295 aa            linear   BCT 01-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Croceivirga
            radicis].
ACCESSION   WP_010518044
VERSION     WP_010518044.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..295
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=32047
     Region          1..281
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mnkiavigag tmgngiahvf aqngyrvnli disqesldkg iatirknldr llakekitet
       61 vkentlgnit tftqleigvk eadlvveaat enlevklnif reldticdan silatntssi
      121 sitqiaavtk rpekvigmhf mnpvpimklv eiirgyntsd svteqimals kalgktptev
      181 ndypgfvanr ilmpmlneai etlyngvagv eeidtvmklg mahpmgplql adfigldvcl
      241 silnvmydgf knpkyapcpl lvnmvtagkl giktgegfyd yseskkaekv skqfv
//
LOCUS       WP_010518082             264 aa            linear   BCT 01-JAN-2025
DEFINITION  undecaprenyl-diphosphate phosphatase [Croceivirga radicis].
ACCESSION   WP_010518082
VERSION     WP_010518082.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..264
                     /product="undecaprenyl-diphosphate phosphatase"
                     /EC_number="3.6.1.27"
                     /GO_function="GO:0050380 - undecaprenyl-diphosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28442
     Region          13..260
                     /region_name="UppP"
                     /note="Undecaprenyl pyrophosphate phosphatase [Lipid
                     transport and metabolism]; COG1968"
                     /db_xref="CDD:441571"
ORIGIN      
        1 meiidaiilg iiqglteflp vsssghlelg kailgaqaip eesllftvvl hfatalstlv
       61 ifrkdvleil kglfqfkwne qtefslkiii smipaafvgf fledymevff dgailivgvm
      121 llvtaillyl admskttnkd vsyrsafvig laqmvamlpg isrsgatist svilgidktk
      181 sarfsflmvv plilgkvakd flsgdiafes sqmgamgagf iaafvaglaa ctwmiklvkq
      241 skltyfaiyc lvvgliaigw siwg
//
LOCUS       WP_010518168            1034 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Komagataeibacter
            oboediens].
ACCESSION   WP_010518168
VERSION     WP_010518168.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..1034
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112261
     Region          16..1023
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mkpmstpepr apgginlsdw sirhralvlf fmiligvagi qsyfrlgrne dppftvktmv
       61 veaflpgasv eetthqlter iekklqetpd ldyvksytla gkttifvnll sgapkaevpd
      121 iwyqvrkkvg dikaqlpqgt vgpffddefg dtygiiygft adgfshrelr dyvetvrdel
      181 lhvpdvakid tlgaqdekiy vdfsthhlar lgingatiaa allaqnatvp sgvidtgreq
      241 iqvqptgqfg svqdianvtv yagsrkvrlg diatitrtys dppqtmfrvg gqdaiglals
      301 mrsggnvlel eknitakmae lharmpigie ahlvanqpkv vhdavgdfte alfeaiaivl
      361 gisflslggr agtvvafcip fvlavvfvcm klfgidlqrv slgaliialg llvddamitv
      421 esmvskleeg wtltraatya yvstafpmlt gtlvtvagfi pvgfaksvag eytfslfavv
      481 gmaliaswfv avlvaplvgv tilkqrpaaa phappegrll rvfsrallft mrrpratvla
      541 slaalvvaiv lsplvprqff pasdrpellv dlslrqgasi katadvsrrl dailrndpdi
      601 dhwssyvgrg avrfylslne qlpndfftqt vivaksavar drlrkrldga lsrdmpdvvh
      661 glfplelgpp vgwpvqyrvt grdpdrvwhy ahdvakimad snqlhmvnfd wgdparklki
      721 dvrqdeahrl glssgaiala insavtgvta tqvrdsiylv dvvlranhaq rlsiedlrnl
      781 dirlpndqtv plstvasisy vedypliwrr drlptltiqa qlrdgvqadt avgtlapkia
      841 afnaslpsgy hvavggtvee saksqksvva vvplmilvml gvlmiqlqdf krlalvisva
      901 pfgligvvga llltqhpmgf iamlglvali gmiirnsvil vhqiqiekdl gqsewdavmn
      961 aakirfrpim ltavaailgm lpiassvfwg pmadvimggl avatvltlif lpslyvlwfr
     1021 vketpspqve gatr
//
LOCUS       WP_010518173             242 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Croceivirga radicis].
ACCESSION   WP_010518173
VERSION     WP_010518173.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..242
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25097
     Region          1..229
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mtpfiaeiig tallmllgig vnanvtlnkt ygqgsgwivi ttgwafavyv gvvvaaphsg
       61 ahlnpavsig lavankfdwn lvpiyilaqf igamlgalli withkdhfdv tvdgdskrgv
      121 fctgpaipnt tinlfneilg tfvlvftvly ftdaiisdsa tiiglgslga lpvallvwai
      181 gislggttgy ainpardlgp rivhallplk nkgnmgwgya wipvvgpiig aslaallglv
      241 la
//
LOCUS       WP_010518212             448 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Croceivirga radicis].
ACCESSION   WP_010518212
VERSION     WP_010518212.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..448
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50996
     Region          1..413
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mehiviigng iagvtaarhv rklsdkriti isgetpyffs rtalmyvymg hmkfehtqpy
       61 engfwkknri dllqafvekv dtdgkilhla tgntinydkl iiatgskpnk fgwpgqdlqg
      121 vqglyskqdl elleenapnk kvckravivg ggligielae mlrtreipvt flvredsfwn
      181 gvlpagesam inehikehhi dlrlstnlet ilddgagrvk avttdqgeti ecdlvgltag
      241 vspnidfled stmetgrgvl vnrkletnip dvyaigdcae qhsgignrrp ieavwytgrm
      301 mgetvaqtic gnpteykpgh wfnsakfldi eyqtygwvfg rkgkpeyeah yhwrhpeeki
      361 cvtiaydknt ekflgintfg mrmrhqifdr wlteekdidy viahlkdanf dpefykpyer
      421 limadynqtr nkkikqksks lkrifqlg
//
LOCUS       WP_010518206             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [Acetobacteraceae].
ACCESSION   WP_010518206
VERSION     WP_010518206.1
KEYWORDS    RefSeq.
SOURCE      Acetobacteraceae
  ORGANISM  Acetobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Acetobacteraceae"
                     /db_xref="taxon:433"
     Protein         1..239
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24930
     Region          36..110
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
     Region          142..220
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mkmqilqtca alalittsat aqdnpmenht asyiampaae gqtaafaefl asaapivget
       61 epgtvlwfal qaddtlaifd ifadeearda hfsgavaaal nqnadalvdr gwddgvvani
      121 nnsdvlsvka pvdlytatta tyikleaapg kgpelaallt aagpivadte pktlfwaalq
      181 idennfaifd ifadnsgrea hfagqvagll nekaselvsg gwddgvvtnv rnfdilaak
//
LOCUS       WP_010518192             269 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Komagataeibacter oboediens].
ACCESSION   WP_010518192
VERSION     WP_010518192.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..269
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29443
     Region          8..263
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(12..16,46..47,194,216..218,220..221)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 msepeirlvl advdgtlvtk dkiltprair averlrergi lftitsgrpp kgmkmvidpl
       61 kisepiagfn ggmmvrpdft vieartlpad tarrvigiir dhradpwvyn gndwivsnae
      121 aphvareqwt vkfppvvgnv edrldqvvki tgvsddldlm krlehdlqqa lgdtasaals
      181 qpyyvdvtnr dankggvvmt lerllgipas qmvtlgdqpn dvlmfrrsgm siamgqaspe
      241 vqkqathvst sceeegfang iekyvlgda
//
LOCUS       WP_010518262             748 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Croceivirga radicis].
ACCESSION   WP_010518262
VERSION     WP_010518262.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..748
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84265
     Region          40..108
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          100..699
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkntywlfai llqilnlgha qdkvegmime gnaagkhlvl pganvywlns pigtitneeg
       61 lfaipytgey dklvvsyigf ktdtltitqp kmvhhtlqps nqldevvveq krdavqkafl
      121 ssenivtins aellkaaccn lsesfetnpa idvnfndalt gtkqiemlgl tspyilitqe
      181 nipmvrgasq tfgltftpgt wvesiqitkg agsvvngyes isgqintelv kpftdhklfv
      241 ngyanqngry evnthlnakv aekwstglyv hgnkrsqked nnedgfldap laeqlnvfnr
      301 wqyqdaakgw vgflgarflv ddkqvgqvnf npetdkfttn awgseintkr ydlsgkmgyv
      361 fpdmpfqsmg vqiayskheq dsyygfnqyd ishaslysnl vfnsilgdtr ntfktgitfa
      421 ydkydelvnt vdfnrvdrsv gvffeyaytn leklsltaga rvdshnrlgt fftprlhvry
      481 tpwenaslrg sfgigrraan ifaenqrlfa snrqlllnss tgpiygfepe katnfglsfl
      541 qgftwegrkg nvgldfyrtq fnnqvvvdwe npsqvifsnl egdsyansfq velnyeilpr
      601 ldfrtaykfy svktnyqngl lqkpltaknr yflnigyttn pkengaqwri dytlhtvgqq
      661 rlpstvvfeq nyqlgdasps yalmnaqvtk vfsnafevyl ggenltnftq dnpvlgandp
      721 fgpnfdtsiv yapimgrmfy agfrykln
//
LOCUS       WP_010518263             119 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Croceivirga
            radicis].
ACCESSION   WP_010518263
VERSION     WP_010518263.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..119
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13261
     Region          23..92
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mkklilflgv almaltttaq dknkklnfev ngkcgmckar iekaclnvkg vkyaswdipt
       61 helsliider ktnsmeiksa iaavghdske lkateeayak ihpcckyred ntddskhye
//
LOCUS       WP_010518290             635 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Croceivirga radicis].
ACCESSION   WP_010518290
VERSION     WP_010518290.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..635
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72621
     Region          4..532
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          559..634
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mlnvhnlsvs fggeylfnei tfklspgdkv gligkngagk stmlkllake mpldegtiat
       61 dkeikigflk qdidfkqgrs vleesyqafe eiklveqkle sintqlaert dyesegynql
      121 midlndythr yeilggynyq gdtekvlqgl gfkredfekq tetfsggwrm rielaklllq
      181 nndillldep tnhldiesil wlesflknyv gavvivshdk mfldnvtnrt ieislgriyd
      241 fnkpytqylt lrseikeqql naqknqerei qqaerliekf raksskasma qslikkldki
      301 erievdqddn svmnlrfpis kqpgkvvlei tqlgksygak kvlervdlmv ergskvafvg
      361 qngqgkttla kiivdeldyt gnlklghnve lgyfaqnqae yldgnktild tmidaanesn
      421 rakvrdilgs flfggddvek qvkvlsgger nrlalaklll qpfnvlvmde ptnhldiksk
      481 nvlkqalqqf egtlilvshd rdflqgltdt vyefkdgnik qylgdidyyl eqrnvedfra
      541 iekkeesipe kvktdsgald ykrqkkiksl knklsaleke iskleqqiad ydhellmnyd
      601 etiaktdffd kyngckkkle dsmlewenvs leles
//
LOCUS       WP_010518324             163 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase [Croceivirga radicis].
ACCESSION   WP_010518324
VERSION     WP_010518324.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..163
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18645
     Region          4..162
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(7,24,29,59,98,104,117)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(9,16,46..48,66,99..102)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mnqliliaaa aennalgkdn dlpwhlpddf krfkalttgh kiimgrktle sfpsplpnre
       61 hiaitrdkny kpkfpckvvh sleealslia ptedafiigg geiyalalpy atkieltrvh
      121 aeveadaffp efdkdswqle qeefhdkddr heyaftyrty trk
//
LOCUS       WP_010518362             248 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Komagataeibacter oboediens].
ACCESSION   WP_010518362
VERSION     WP_010518362.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..248
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26064
     Region          1..244
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msikgkvalv tgassgigaa tarklategv ivglaarrkd rldalvteit gvggkavalp
       61 tdvtdlasck aaadfliarf gridvlvnna glmplsnvds lkvdewqrmv dvnvsgvlna
      121 aaavlpqmia qhsghifnms siagrkvftg lavycatkaa vaafsdglrm eigpkhnirv
      181 tciqpgavks elyeqitdat yrkqmddlaa smtylegedi adtilfalna psrmdvaelf
      241 vlpteqgw
//
LOCUS       WP_010518313             483 aa            linear   BCT 01-JAN-2025
DEFINITION  NupC/NupG family nucleoside CNT transporter [Croceivirga radicis].
ACCESSION   WP_010518313
VERSION     WP_010518313.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..483
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=51142
     Region          57..483
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mkptkiwcll llglfvlplt aqepvvidsl annlpnvgln ttsadlvpnq gftlktllrg
       61 ilgmaalvli aflfsanrra inwkttaigl giqlliaigv lkvkfvqvif etigsvfvsi
      121 ldftragsqf lfeglvvdmd tfgyifafqv lptiiffsal tsvlfylgii qkvvkglawl
      181 ltkslgisga eslsiagnif lgqteaplli kaylekmnrs eillvmvggm atvagavlaa
      241 yigflggddp elrlifakhl laasvmaapg aiviskilyp qtetintdvq vsqdriganf
      301 ldaiangtte glklavnvga mllvfvafia mingilggvg eyttfntwis antpydsfsl
      361 eailgtvfap lmwligvnne dvmlmgqllg iklaasefig yiqlaelknv ansahftynk
      421 svimatymlc gfanfasigi qiggigslap gqrktlsefg mkavlggsla sllsatiagm
      481 ilg
//
LOCUS       WP_010518437             170 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma carbonic anhydrase family protein [Croceivirga radicis].
ACCESSION   WP_010518437
VERSION     WP_010518437.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..170
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18053
     Region          1..170
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mliktvngkt pvwgadcfia enativgevs mgsqcsvwfn avlrgdvhfi kignkvnvqd
       61 gavihctyqk spttignnvs ighnaivhgc tiednvlvgm gaivmddcvl esnsiiaaga
      121 vvtkgtrvps gtifagmpar kikevspels rgeidriann yvkysswfke
//
LOCUS       WP_010518446             277 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Croceivirga radicis].
ACCESSION   WP_010518446
VERSION     WP_010518446.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..277
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30929
     Region          12..274
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mleefqdyek hinkaiewfw dlvpnlilai iilfaglwfi kiinklvrkf fakkdydetl
       61 esflqsfisi glkvmlfvlv vtqlgvqtss liamigaagl aiglalqgsl snfaggvlil
      121 lfkpfrvgdf vsaqgvdgtv keisifntkl ntfgnqlaiv pngqlangni vnysaepirr
      181 dnyivgigyg snikkakdil lalceqderi lkepkpevyv aeladssvnl slrwwaknen
      241 fwgakfnlie qsklqfdeag ieipfpqrvi hseeidd
//
LOCUS       WP_010518503             233 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Croceivirga radicis].
ACCESSION   WP_010518503
VERSION     WP_010518503.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..233
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26196
     Region          158..232
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mnvkkhpkiq leplrnlffv sglalilcls ylalewktyk plprykqist qltrleetpp
       61 ityhtlqepp kksytaptii kieaddggii edlieipstt tnnilavnqi tvieepedei
      121 ipinvveeap ifpgcenatd kkacfqemml lhvkntfkyp eqaiamnlqg rvhvlftidk
      181 ngvitnlqlr gphnileqea srimaklppi kpgkqggrpv kvpfsipitf klq
//
LOCUS       WP_010518521             325 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Flavobacteriaceae].
ACCESSION   WP_010518521
VERSION     WP_010518521.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..325
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37270
     Region          131..300
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mskvkyyydp dtlsyrkiep kkskryrnvf lflaaaalfg flgltvllnt nlvntpkels
       61 lerevqnyel qyeilnkkmd qmeqvlanie drdnniyrly feanpipeeq rkagfggvnr
      121 ykslegynns emivnttkrl diiqkqmviq sksldeitll aeekekllaa ipaiqpvrne
      181 dltrmasgfg wrtdpflktr kkhwgmdfta prgtpifasg dgkisradnn ssgygkhiri
      241 ehghgymsly ahlskynvtp gqkvkrgdli gfvgntgrse aphlhyevwk dgerinpinf
      301 yygslspeef esmlkfatqe nqsld
//
LOCUS       WP_010518553             444 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Croceivirga radicis].
ACCESSION   WP_010518553
VERSION     WP_010518553.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..444
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49625
     Region          340..442
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(344..345,378..379,382,386..387,390,433,437)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mkfplrtvgl maflflftap vqsqflkklg kkakeaaert verrverets kktdqtldsi
       61 lepgskkpep kslphppnqd ddtldtdttn gngatkntnn nkaneepnle vyskfdfvpg
      121 dtplffddfs ndfigdfpak wntnaggevv nfsdssekwl elksgyniyf ipnspklped
      181 ytiefdirtv gvdkktssqa ylrvdlsddd kfkegqnfvq ghiplcqytp igitaenrin
      241 gsreiystve adirdeilnv phisiavnke rfrlwvnetk hidipklvap navlntlkfh
      301 lnnlkegker vfltniklne ggvdlrrkli aegkistngi lfdsgsanik pesmgiirqi
      361 yqvlqqdssi klkivghtda dgddttnlkl sdaraqsvkk altdvygvaa nrlttegkge
      421 lepiadntsi egktqnrrve fikl
//
LOCUS       WP_010518666             743 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Croceivirga radicis].
ACCESSION   WP_010518666
VERSION     WP_010518666.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..743
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=83427
     Region          1..735
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mknrsfsivf vllvtllmgq kkpvdyvnpf igtsnfgttn pgpiavrgma nvspfnvagp
       61 qnlpmekdsr wfstpyvnen pyltgfshvn lsgvgcpelg viitmpttga lvtdheqygs
      121 tysneaakpg yytntldkyg vkveatattr tgvskyhfpa geanvllnlg lgltneegaq
      181 vkvvspteie gmrmvgsfcy ykseesypiy fvaqfsepaq eygvwkkprk ynglesqwmv
      241 tngetrikkg frqtvvgdsi gaymrynfkq pktvsvkvgv syvsienare nlkvetqnkd
      301 fetllaeaqd kwnkqlstie veggteadkt ifytalyhtq ihpstlndan geypkmqtre
      361 tlktndtryt afslwdtyrn yhqlmslvyp kqqsdmvksm lqvydesgwl pkwelnatet
      421 ttmvgdpagi vladtylkgi qdfdvelaye amlksadqle gnplrpglkd yiekgylttk
      481 ttksgsvstt qeynisdfai aqlakalgkk edykrfskrs isyrklfdke fnllrpkndd
      541 gswltpynpe tganfvknlg fiegnawqys fmvahdvkgl mnlmggsksf tnklqqvfdk
      601 nqfdmanepd iaypylfnyv kgethrtdql vsellktyfk nepaglpgnd dtgtmsawav
      661 fsmmgiypvs panpiytftv pvfdkvtiql ddsyygggtl vikkedsagl nnerevfigk
      721 kkitkpfvsh qellakkeit iky
//
LOCUS       WP_010518668             749 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Croceivirga radicis].
ACCESSION   WP_010518668
VERSION     WP_010518668.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..749
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=84933
     Region          1..729
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mrhgfwvlsv ifvlacknqp kpksleslts yvnpfigtdg pgntypgatv pfgmvqlspd
       61 igipgwdria gyyypdsilt gfshthltgt gagdlydili mptnsrfkdt lkannykpys
      121 hfnhvgegas pgyywvqlkd ygikaeltat prvgihkytf pkdtlsqihv dlgyslnwdr
      181 ptntkitvvn dsvlqgfrms egwarnqqly femtfskpfs syyvkenkeg qatkiilnyq
      241 teedevitvk tglssasvgg askaikeeak qdfesirkqa navwekelsk irittqnker
      301 ktifytmmyq smlaptlysd snqqykaand angqylpetd siamakgfnr ydtfslwdty
      361 raahplytii qtervpdmik sllahyqetg klpvwsmqgs etnmmigyha vpvivdayfk
      421 gfefdanlay qacktsamvk erqidefaqn gyiataaghe nwsvsktley ayddwclaqf
      481 akdldkeedf dyflersnnw knvynaknsw lqpkdasgtf iypftpkeys pyfcesnawq
      541 yywsvaqdip glvaatggan rfeqkldsmf tyaplptdkl pifstgmigq yahgnepshh
      601 vaylynyigk phktqdlvyk irneqyknep nghcgnedcg qmsswyilns lgmypvnaaq
      661 gildlsvpqf skasiqlpnn ktfevkatgl seenryvaav slngqqlkrr fitykelmqg
      721 gileflmtan kdtvntqsye qpnplkiyn
//
LOCUS       WP_010518760             379 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Croceivirga radicis].
ACCESSION   WP_010518760
VERSION     WP_010518760.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..379
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42263
     Region          3..276
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mpkkirlgiv ggggdsligv lhrvashind nyqitgavfn pdfeknkefa eeidvpldri
       61 ytdfdtmvae elklpeseri qvfsiltpnf lhfpmakkll engfhvicek pmttsleeak
      121 ilaethkkag tifalthtyt gypmvrqmre mikagalgki hkvdaryyqg winpiihdke
      181 krnsvwrldp ekagisscmg digvhafnmv eyttgleves llcdfnylye dnkmdvdgtv
      241 lirmgdhvkg virgsqvatg eenglaiaiy gekasfrweq ekpnflymms dteptkiykp
      301 ghaynsefsl dgtklpaghp egifdsmani ylgvarairg esqndgaypt mrdgvrgmsf
      361 iegtvashkn gnvwvnveg
//
LOCUS       WP_010518835             430 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Croceivirga radicis].
ACCESSION   WP_010518835
VERSION     WP_010518835.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..430
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47904
     Region          1..114
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Site            order(24..25,27,51,54..55,58..59,61..62,84,87..88,91..92,
                     95)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          49..78
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          83..107
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <142..401
                     /region_name="RPT1"
                     /note="ATP-dependent 26S proteasome regulatory subunit
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1222"
                     /db_xref="CDD:440835"
ORIGIN      
        1 mlesllealk hspdnvplkl qvaklyleal dylmaeehlt gilalqpkhe eakyllascf
       61 lklgkqaaae iiaeelsqqs tniqylellc ecqlaqdnys eaqntyryit elqpgyqnhk
      121 fdqvlknpvl tneddfteev vsfmskpnit fkdvggmeqv kneidlkiik plqhqevyka
      181 ygkkigggil lygppgcgkt ylakatagqi danfinvgin dildiwlgss eknlheifek
      241 arantpcvif ideidalgan rndmnktagr tvinqflsel dgvdsnndgi liigatnapw
      301 yldpafrrpg rfdrivfvsp pdttsreaif dvqlknkptd sidlkelakk tkefsgadin
      361 aaidlaiedk lqsafvdgip kplttkdilk gikktkpstk dwfssarnya lyandsglyd
      421 diltylnikk
//
LOCUS       WP_010518898             332 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Croceivirga radicis].
ACCESSION   WP_010518898
VERSION     WP_010518898.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..332
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37219
     Region          138..289
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mqqpqnnkyq ingiqqvgig vnnlvetfnw ynkykgfnil vfddvanaql mtkytgnsle
       61 qrrallslnl nggggleiwq ftkrkplsqk spflwgslgi nalilktntk taqsyeqdln
      121 gnwlvleptt dkkntnsgva gvvigvsnme kaltfyrqlf klkitsdkti tgnefhtipg
      181 gneqfrkvel cstnenpggf gtlygkyklv llecltakrt kiyedrywgd lgyihlcfdv
      241 fnlenlksta anvgyhftvd sansfnmgaa agrfaylddp dgtlielvet hkvpickpln
      301 lyynlrgdng nkpvpnrlik alaihkkrkl kk
//
LOCUS       WP_010518911             191 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Croceivirga radicis].
ACCESSION   WP_010518911
VERSION     WP_010518911.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..191
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22092
     Region          13..188
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mqklreffkq sgelseenld lllsscapkt lpkgqvllqt ndwvnsiyfi esgflhyytn
       61 mqdgtrvtlk vvspnyfwtm ldeffnqkqt ldtcvaltdv hyceikrqdy nqlksintti
      121 anfmhsiteq ilsnkvkeen dkskmsveek yldllehnpq mvqvvpvgil asylgtsret
      181 lhrirrklss v
//
LOCUS       WP_010518928             642 aa            linear   BCT 01-JAN-2025
DEFINITION  PAS domain-containing protein [Croceivirga radicis].
ACCESSION   WP_010518928
VERSION     WP_010518928.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12091914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..642
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=73233
     Region          125..624
                     /region_name="KinA"
                     /note="Sporulation sensor histidine kinase A (Stage II
                     sporulation protein SpoIIF/SpoIIJ) [Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5805"
                     /db_xref="CDD:444507"
     Region          <377..624
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mdfnqlgiff lqttlvsgli ltlfrvrktm glgmvyiclg lfqfiqvflp tnfymritgv
       61 lavsfasvvf ttvlftmllv yikedanetk kviyalllsn lvialtllil nfnldsqnyt
      121 npygismies plkfkilllg tlvlladmif aiflyefisk yinklffrif ltmalvlafd
      181 sivfnlitfw grdnlselig tstiakifta tflsflytiy layfekdnka eellkiqdif
      241 qklsykqkfe laskdiikts telqikedry ktltdtapvg vfhttptget tyvnpkwcei
      301 tgisaedaik dgwknyihpd dvdrishcwn eavnkkmsss atyrfirkdg tlrwvlgnav
      361 pelnkkneii gfigtttdit eikkyqeqli klknkaeean rlksaflanv sheirtpmng
      421 ilgftnllkn qqltsddrle yldiiedsgr rmlhimndii nisrieagsv elhketfdll
      481 nlltykldff tpiaqkknle liyeknepdh piimhtdkdk vcsivsnfit naikytdkgs
      541 vtfgyqlqkd nvqlyvkdtg igivpekhqv iferfiqadi edrmaregag lglaisksya
      601 elvngkisme skpgvgsify ltlpydpklt lhnqivnnes kp
//
LOCUS       WP_010518947              97 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Croceivirga radicis].
ACCESSION   WP_010518947
VERSION     WP_010518947.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 97)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..97
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11209
     Region          4..90
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mmemeindns flrqfettvd ghlakieyss qerkvfltkl vipegvtqeg fkenfikavl
       61 hhlqeqnlrv vptsphiagf lrknrqykem lpvgiri
//
LOCUS       WP_010518948             210 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Croceivirga radicis].
ACCESSION   WP_010518948
VERSION     WP_010518948.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..210
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24358
     Region          <31..>105
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          <33..179
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mpgmaaspai fenlkldptv filhylkwhl prpndtlady akmvnesivh dnpvligvsf
       61 ggmlvqemar hrrfkkviii ssikskfemp krmhfarytr ihkllptglv nnvellakya
      121 fgekvnkrla lyeiyldvrd kvyidwaihq ivnwkqtqpp knvihihgel dnvfpinnik
      181 gcitvnkgkh tmiiyrakwf nehlpklile
//
LOCUS       WP_010518982             451 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Croceivirga radicis].
ACCESSION   WP_010518982
VERSION     WP_010518982.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..451
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50116
     Region          1..447
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdtellariq faftiafhyi ypplsiglgl lmvvfeglyl ktgkkayeil trfwlkifai
       61 tfgigvatgi imefefgtnw svysryvgdi fgsalaaegl fafglestfl gillfgwnrv
      121 spkvhfisti gvflgsmfsa vwivvanswq qtpagyhivg eglnaraevt dfwamvfnps
      181 svdriihvwq gaflagaflv lsvhayyllk gryveiskka fkmalavaal vslsqlvsgh
      241 ssadgvaknq paklaamegh ynassaadly llgwvdhesk kvtgigipgg lsflvhqdfe
      301 apisglnafp kdevptqvna vfqfyhimia igmfligltl yacylwwrgt lfkkkwllri
      361 fvlsallpqi anqvgwfaae mgrqpwvvyg hlktsdafsq evssnqilfs lilflvvysi
      421 lfllflysvn kkikhgpyde adnpneflky t
//
LOCUS       WP_010518990             146 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Croceivirga
            radicis].
ACCESSION   WP_010518990
VERSION     WP_010518990.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..146
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16451
     Region          11..142
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mekkvknvfk egaiapdfia naiakhqvkt nigahniflg qvradkidgk ivsaieysay
       61 etmanqkfhe ikeqtflayn itcmhiyhsl gkvavgevcl fvfvsaphrr vvfealeyvv
      121 eaikkevpvf gkelfeddsy qwkvnt
//
LOCUS       WP_010518995             166 aa            linear   BCT 01-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Croceivirga radicis].
ACCESSION   WP_010518995
VERSION     WP_010518995.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..166
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=18642
     Region          27..138
                     /region_name="SnoaL_3"
                     /note="SnoaL-like domain; pfam13474"
                     /db_xref="CDD:433238"
ORIGIN      
        1 mgnklvfial fgllcvtlsa qeqkdkinmv ldswhkaaad adfdayfglm thdgvflgtd
       61 atenwqndaf rafskpyfdk grawsftavd rniyvdgsva wfdevldtqm klcrgsgilk
      121 lvdgdwkiah yvlsilvpne nvdalvkikk qkdslllidf knkikn
//
LOCUS       WP_010519015             129 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Croceivirga radicis].
ACCESSION   WP_010519015
VERSION     WP_010519015.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..129
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14493
     Region          8..124
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 msstanlpti miaedehvny lllemwlkgk chilhatdgn eaieifknhp eialilmdik
       61 mpytdgkeat kairkindti pilaqsafvm dyenqdiles gcnavlnkpi rkeefnalln
      121 kflpnlnln
//
LOCUS       WP_010519002             190 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Croceivirga radicis].
ACCESSION   WP_010519002
VERSION     WP_010519002.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..190
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=21587
     Region          5..155
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mnnffcdity ngddfktykl pkgdyenctf ancnfkegfi dninfiectf qecdltnvnc
       61 tatifnqvtf igckmigidf spcnpmflnl gftncnltla nfnalelpkt nfkdctldqv
      121 dfsetqlkgs niencqlknt vfyntkldsc nfnnstylli dpdqnsikkt kfnidqlpgl
      181 lkkhdivvay
//
LOCUS       WP_010519084              88 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF2061 domain-containing protein
            [Flavobacteriaceae].
ACCESSION   WP_010519084
VERSION     WP_010519084.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..88
                     /product="DUF2061 domain-containing protein"
                     /calculated_mol_wt=9873
     Region          23..86
                     /region_name="COG3205"
                     /note="Uncharacterized membrane protein, DUF2061 family
                     [Function unknown]"
                     /db_xref="CDD:442438"
ORIGIN      
        1 miadqlvvds kkekstyakd knaespkrsi aksiswrivg tidtviiswi vtgtltlafs
       61 iglielvtkm vlyffheriw nsiswgkk
//
LOCUS       WP_010519140             239 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Croceivirga radicis].
ACCESSION   WP_010519140
VERSION     WP_010519140.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..239
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=27066
     Region          38..238
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mrismayiki vvllllvigl ygfasvrnak rpmgniaikf vgeenlylte eavnklliqk
       61 lgplenrakd avvldsieki vqsspmvkta qvyrtvdgkl iskiiqrkpi griegnsrfy
      121 ldsegkrmpl sryhsarvpi itgkitektl edayvileyi sqddflrknv igihikdeda
      181 yllklrveef vvnlgsvenl dekfkkfmaf yvkaakdnsl dtyaevslkf dnqvvctki
//
LOCUS       WP_010519180             187 aa            linear   BCT 01-JAN-2025
DEFINITION  DinB family protein [Croceivirga radicis].
ACCESSION   WP_010519180
VERSION     WP_010519180.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..187
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20641
     Region          48..183
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 mknaivisis mlclfataqn ipaksttial asnetqlvqe tlkgmlyrvq dqveqlasaf
       61 eeeqydwkpa egirsvresi lhvaaanyfl atklgytppa dtdfmtmevn ikgkenvlaa
      121 lkksnefils kiteekaenf gsevdfgfak fnrlagllii lehagehkgq liayarsnnv
      181 tppwsqq
//
LOCUS       WP_010519209             381 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Croceivirga radicis].
ACCESSION   WP_010519209
VERSION     WP_010519209.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..381
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40789
     Region          14..360
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,140,
                     143..144,147,213,216..217,220..222,225,253,257,305..306,
                     310,314,330,333..334,337..338,341)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mkslllilgn rkylapalvf aslnvwfgtw aiyiptvkek lgidkgdlgf alfflslgvf
       61 svfpvasklv nyfgvgratw lgvlsssifa lfpllapnyi llctalfffg aangftdiam
      121 ntlvteveke dqvtimsaah gffslggilv glgsflipii snpflhmlgs vvlvllvnwr
      181 fkkeyqnkka tveptngfsl qvfkpllllg lvgfismase gaivdwsgly lqeitlapty
      241 ligagflafs itmtlgrflg dgisekvgsy kllfigatla iigflsvlta ntylaifgfg
      301 lsglgfsamv pelfriggki kgvqssqgva fiagsgyfgf lsgpvilgyl aetfnlklsf
      361 vvlllsaclv llisiykpkg k
//
LOCUS       WP_010519258             166 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Croceivirga radicis].
ACCESSION   WP_010519258
VERSION     WP_010519258.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..166
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19251
     Region          6..165
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdnvceeqqy ntifktnskt vfnyiyykfg neekandavq eafvklwenc nkvtpdraks
       61 ylftvannly lnvikaekvr lkhadkhrne stnespefll eeqqfkekle naldalpqnq
      121 rttfllnrid gkkyaeiael egvsvkaiek rmhlalkslr dkidgi
//
LOCUS       WP_010519263             141 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Croceivirga radicis].
ACCESSION   WP_010519263
VERSION     WP_010519263.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..141
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16011
     Region          4..141
                     /region_name="COG3565"
                     /note="Predicted dioxygenase of extradiol dioxygenase
                     family [General function prediction only]"
                     /db_xref="CDD:442786"
ORIGIN      
        1 mannltpfhv aipvhnlaec rkfykdtlgf eegrssdqwv dfnffghqvv ihykpksnee
       61 lhtnpvdgka vpvphygvvl dwdtfetfsk kltdkgvefv iapyirfkgl pgeqatmffl
      121 dpagnalefk afkdmkqlfa k
//
LOCUS       WP_010519274             276 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Croceivirga radicis].
ACCESSION   WP_010519274
VERSION     WP_010519274.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..276
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31842
     Region          94..253
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mesiikyfet ipplhrslil vggitffwil egivplfsvn ykkwqhalpn ffftlttili
       61 nmplafllll csdwavnnsf giinwmpamp lwlyvvlgvl fldffgayla hlvehkvkpl
      121 wmvhlvhhsd hnvdtttanr hhplesciry aftlfgvliv gapigvimly qslsvicsqf
      181 nhanislprk ldkaisyliv spdmhkvhhh yilpytdsny gnifsiwdrl lgtymeldrd
      241 kikygvdtfp dekenssikg llrqpfhkyr kpttin
//
LOCUS       WP_010519336             282 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Croceivirga radicis].
ACCESSION   WP_010519336
VERSION     WP_010519336.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..282
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=32009
     Region          15..281
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mgnpnwnrrr fikgaaalsg sgllmglysw qiephwlefv hlkmpinnlp nnlkgkklmq
       61 lsdihvgplv dqkfllname makrerpdyv vytgdfihfe nystfdqlea vmdlapkgtl
      121 gtyailgnhd ygeewlddti atkiieilaa nkitvlrnei aenngltfig lddywgtnfa
      181 pdramenyrp nkptvvlchn pdvcdlnvwn nykgwilsgh thggqckppf lkppilpvqn
      241 pnydagikdl qdgrtlyinr alghlyqirf nvrpeitift ls
//
LOCUS       WP_010519309             227 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division ATP-binding protein FtsE [Croceivirga radicis].
ACCESSION   WP_010519309
VERSION     WP_010519309.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Hung,L.W., Wang,I.X., Nikaido,K., Liu,P.Q., Ames,G.F. and Kim,S.H.
  TITLE     Crystal structure of the ATP-binding subunit of an ABC transporter
  JOURNAL   Nature 396 (6712), 703-707 (1998)
   PUBMED   9872322
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..227
                     /product="cell division ATP-binding protein FtsE"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=25257
     Region          5..227
                     /region_name="FtsE"
                     /note="Cell division ATPase FtsE [Cell cycle control, cell
                     division, chromosome partitioning]; COG2884"
                     /db_xref="CDD:442130"
ORIGIN      
        1 maepilkltd vsifqkdnlv lsnvdlqvkk gefvyiigkt gsgkssfmkt lygdlplskg
       61 egtvvdfnlk tlkendipyl rrklgivfqd fkllsdrnin nnlkfvlkat gwtdtskmdd
      121 kiaevldkvg mktkgfkyph elsggeqqri aiarallndp eliladeptg nldpqtsvev
      181 mkvlqeinnn grtiimathd yalilkyphk tikcdggkvf eviqkav
//
LOCUS       WP_010519370             450 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramate--L-alanine ligase [Croceivirga radicis].
ACCESSION   WP_010519370
VERSION     WP_010519370.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Sangshetti,J.N., Joshi,S.S., Patil,R.H., Moloney,M.G. and
            Shinde,D.B.
  TITLE     Mur Ligase Inhibitors as Anti-bacterials: A Comprehensive Review
  JOURNAL   Curr Pharm Des 23 (21), 3164-3196 (2017)
   PUBMED   28201974
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..450
                     /product="UDP-N-acetylmuramate--L-alanine ligase"
                     /EC_number="6.3.2.8"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008763 - UDP-N-acetylmuramate-L-alanine
                     ligase activity [Evidence IEA]"
                     /GO_process="GO:0007049 - cell cycle [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50367
     Region          1..444
                     /region_name="MurC"
                     /note="UDP-N-acetylmuramate-alanine ligase MurC and
                     related ligases, MurC/Mpl family [Cell
                     wall/membrane/envelope biogenesis]; COG0773"
                     /db_xref="CDD:440536"
ORIGIN      
        1 mkihfiaigg samhnlalal qhkgyqitgs ddiiyepsks rlenkgllpl efgwypekit
       61 esldavilgm hakpdnpell rakdlgitiy sypeflyeqs kdktrvvigg shgkttitsm
      121 ilhvlaynni avdymvgaql dgfdrmvhlt tendfivleg deylsspidr rpkfhlyqpn
      181 iallsgiawd hinvfptyen yveqfkifvd givsggsity ntedtavkev veasentirk
      241 fpyetpeytv adgttylete dgpmpleifg qhnlnnlaga kwicqqmgvd evdfyeaist
      301 fkgaskrlek igenknavaf kdfahspskv mattnalkeq ypnkkvlacl elhtysslns
      361 eflkeykgal qaadeavvfy speavkikql eevseqdiaa aferedlaiy tdpadfkefl
      421 fshsmenmal llmssgnygg ldfkevaklf
//
LOCUS       WP_010519438             151 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter small permease [Croceivirga radicis].
ACCESSION   WP_010519438
VERSION     WP_010519438.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..151
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=16688
     Region          1..151
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mvrnkidqil gkllalimgv mvinvlwqva srylvgepss ftdelarylm iwvgvlgaay
       61 vsgrkmhvai dvlpskaseg tqrkikalvy iliilfaffa mviggcrlvy isyllgqksp
      121 alqiplalvy mviplsglli iyyklndllk n
//
LOCUS       WP_010519351             140 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Croceivirga radicis].
ACCESSION   WP_010519351
VERSION     WP_010519351.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..140
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=16087
     Region          12..135
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 msqerrnlsa ciidddpiyq ftmksilnkq kivkeilvfk dgeqaldffi snidndqdlp
       61 dvifldidmp imdgfqfmer yvelkpkvgk kiiiymvsss vdpkdierak kiseisdyiv
      121 kpvepgklki ilkeisntie
//
LOCUS       WP_010519441             346 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Croceivirga radicis].
ACCESSION   WP_010519441
VERSION     WP_010519441.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..346
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37786
     Region          <1..346
                     /region_name="trifunc_aldol"
                     /note="KHG/KDPG aldolase/sugar kinase fusion protein;
                     NF041633"
                     /db_xref="CDD:469516"
ORIGIN      
        1 mkkivtfgei mlrlappgfl rfsqtnsfdv vygggesnva vslanygldv dfvtrlpknd
       61 igdcalmemr krnvgtdhiv fggdrlgiyf letgavsrgs kvvydrahsa maeikpgmvd
      121 wksvfkdadw fhwtgitpai sqgaadacie avkvakemgv tistdlnyra klwkyggdre
      181 aimteltsyc divlgneeda ekhfgikpeg ldittqgehv kaeaflsvck qmtkkfpnak
      241 kvittlrgsl sashntwagv lydgeklfks reyqithivd rvgggdsfmg gliyglmtwp
      301 nddqkaldfa vaasclkhti kgdanlatie eveklmggda sgrvsr
//
LOCUS       WP_010519476             496 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Croceivirga radicis].
ACCESSION   WP_010519476
VERSION     WP_010519476.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430356
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..496
                     /product="ankyrin repeat domain-containing protein"
                     /calculated_mol_wt=53936
     Region          <37..231
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          91..122
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          124..155
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          145..441
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          159..191
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          193..224
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          264..296
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          298..328
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          331..361
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(332,336..337,340..342,344..345,349,352,361,363,365,
                     409..410,413..415,417..418,422,425,434,436,438,442..443,
                     447..449,451..452,456,459)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          363..434
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          436..469
                     /region_name="Ank"
                     /note="Ankyrin repeat; pfam00023"
                     /db_xref="CDD:459634"
     Region          436..466
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mkklavlsil tlgcftqlla qqnvflnrdf wsnnpsisti deqiaagndi ternpaffdg
       61 ptyailqkvd pktiayiiek egngvdklth dgriylhwaa ysgnqqvvdy llkngadaaa
      121 idahgysvin fsanaglnnt tiydallakg adlkatthng analllssss akdyniiqyf
      181 idkglslnsk dndgngafmy asrsgninll ktlkdkgvay kainnngena lflaaqgtrr
      241 sqndkkvfdy leglglannl insdgqsllh liarnnkdla lfkhfiqagl dseladnngq
      301 tpylnaasgn tlevlqllap kkatnpvnkk gqtalmlave rnsadvvayl ieqggninak
      361 dkdgnglayy llqnynprnv dlyeaklall qkanvdftap qnngntllhl aakennlkll
      421 kqlaafqinv nqknnegnta lhlaamsskn ddilkyliai gadvsattdf eetvfdlase
      481 nemlrknnik ldflkp
//
LOCUS       WP_010519503             218 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Croceivirga radicis].
ACCESSION   WP_010519503
VERSION     WP_010519503.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..218
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=24264
     Region          1..202
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlediqtaip lgillsfmig pvffvlletg atkgfraaia vdlgviladi lfifiayfss
       61 fqllenlsne pglyvfggmi llvygivvyv kketkkkesk klkgsylvli vkgfllnfin
      121 igvlvfwlgv livvgpsmen denrliafft tmiltyflvd vikillakql kkkltpkrir
      181 lvkkglgvvl micgivlitk gflpkekfnv qdsierik
//
LOCUS       WP_010519541             333 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Croceivirga radicis].
ACCESSION   WP_010519541
VERSION     WP_010519541.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..333
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37375
     Region          1..286
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mlqvnnvffa ygenpilkdi sfqlpngshl aligesgsgk stllkaiygk lklgqgevsw
       61 nnqkvlgpdf nlipgenymk yvsqdldlmp fttvsenige hlsvfepeth qariqellev
      121 iqledyahvk vknlsggqqq rvaiakalaq epkillldep fssidqfkkn glkqllfpyl
      181 kekgitvina thdpddilpf swltlvlkdg eildfgptkn vynhpknlya aslfgeanti
      241 plyflnpgyy idrpiivyph elsvtqnsdf mvtveesffk gshflvkafh etnlmvwfih
      301 srsiipgtkv alkgtaktll eriskthakd yhs
//
LOCUS       WP_010519515             540 aa            linear   BCT 01-JAN-2025
DEFINITION  S41 family peptidase [Croceivirga radicis].
ACCESSION   WP_010519515
VERSION     WP_010519515.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..540
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=60474
     Region          36..345
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mgkvkkrflv pvlavtffiv gssfksdffe iakqieiftt lfkelnmnyv detnpgelmd
       61 aaiknmldel dpytkflneq dveayrinna gqysgigalv rsykdklliv epyegypadi
      121 aglkagdeli kigeinvadf ddnasellkg sndsevtvty irqgetkqtt ikrggveida
      181 vpfyemvddk tgyivlskfn rkaseqtkaa iidlkgkgae rlildlrgnp ggllseainv
      241 tnlfvpkgel ivttkskvkk fnqeyktknk aldteiplvv lingrsasas eivsgglqdl
      301 dravivgars fgkglvqrpl kltygtqlkv tisryytpsg rciqaldywn rdqngkairn
      361 ttfnqfktkn grtvedgggv lpdielatqk tndlvraldn nhlifdfatq yyyqnplssl
      421 dqfnlsttdy nafkqfvakn gfsfktksea vleeqlqned sllgaavkek ykellvaidk
      481 skiealdtyk kaiehkleee lipryfyrkg lykyhlknde aiktastlls dsnkyqailk
//
LOCUS       WP_010519549             200 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Croceivirga
            radicis].
ACCESSION   WP_010519549
VERSION     WP_010519549.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..200
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22240
     Region          39..179
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 malvnplnpe hdqetkelaa ffnetlgfcp nsvltmqhrp aiskafinln kavmanegkv
       61 tsalkrmiaw vssnatgcry cqahairaae rygaeqeqle niweyrshpa fseaeraald
      121 fslaasqvpn tvnaeikkrl hehwtageiv eilgvislfg ylnrwndsmg tdieegaves
      181 gkhylgkygw ekgkhdgsly
//
LOCUS       WP_010519552             423 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Croceivirga radicis].
ACCESSION   WP_010519552
VERSION     WP_010519552.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..423
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45837
     Region          16..397
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(26..27,30..31,34,66,128..129,131..133,136,156,
                     159..160,163,237,240..241,244..246,249,273,277,330..331,
                     335,339,355,358..359,362..363,366)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mskkldpyaa lrfrefnifl lvrfamvfaw smqfiviewq vysltkdpla lgiiglmeii
       61 paisialfag hfvdqnekrn llvkcilgft lvslglflis apsvaekydq ktilysiyal
      121 vfigglvraf igptifslia livpkriypn aatwssstwq fasvlgpala gfsiswigvh
      181 wsmcvifgfs vlallflsqi kkkpilnpkl gepvlqslkd glkfvfstka ilgalsldmi
      241 avlfggaval lpifaqdilk vgsegfgilr aapavgasit mlastrfplh knagkkllwa
      301 vfgfglcilv fglsklfwls vlalflsgav dgvsmiirqt ilqlktpdnm rgrvasvnsi
      361 fvgssnelga fesgvtaklf gtvravifgg tmtlltvggm aifspsfrkl dlskdveeqe
      421 aek
//
LOCUS       WP_010519567             202 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Croceivirga radicis].
ACCESSION   WP_010519567
VERSION     WP_010519567.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..202
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22206
     Region          4..197
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mafelpklpy aydalepnid artmeihhtk hhngyttkln gaiegtdleg kdieeiltnl
       61 dmsnaavrnn gggfynhslf wevmspnggg tpsgalaeai daafgsfdaf kekfsaaags
      121 rfgsgwawlc vhkggkvevc stpnqdnplm pdtgcegypi lgldvwehay ylnyqnrrpd
      181 yvsaffnvin wdkvselyea nk
//
LOCUS       WP_010519580             181 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Croceivirga
            radicis].
ACCESSION   WP_010519580
VERSION     WP_010519580.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..181
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19588
     Region          43..176
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mstfsplqrd evsegnqaif dnlekalgfv pnlyatyahs tnalanylnf tnaktslsak
       61 qkevvnlvvs qvnnceycla ahtaigkmng ftdsqiielr sgkasfdskl dalaklaqni
      121 tekrgatdee vvnnflksgw tkenlidaiv lvgdktisny ihsttkvpvd fpaaqpleat
      181 v
//
LOCUS       WP_010519590             161 aa            linear   BCT 01-JAN-2025
DEFINITION  GbsR/MarR family transcriptional regulator [Croceivirga radicis].
ACCESSION   WP_010519590
VERSION     WP_010519590.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 161)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 161)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 161)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..161
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18889
     Region          4..160
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 msreeikkrl iedlgvhfen myqipplaar lyaslilteq egltfedcql rrgaskssis
       61 salnlllkme iisyftkpgd rkryfkvses gtfflnklke rlklfqaeke iiykindyhe
      121 qynpekhrkn qpktsvylnf vtesekllnq sidklksfke d
//
LOCUS       WP_010519627             457 aa            linear   BCT 01-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Croceivirga radicis].
ACCESSION   WP_010519627
VERSION     WP_010519627.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..457
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=52100
     Region          5..432
                     /region_name="ASKHA_NBD_FGGY_NaCK-like"
                     /note="nucleotide-binding domain (NBD) of Novosphingobium
                     aromaticivorans carbohydrate kinase and similar proteins;
                     cd07772"
                     /db_xref="CDD:466792"
ORIGIN      
        1 mlkevtavfd igktnkkffl fdtnfkevyr ryieleqivd edgyptenid alhrwmkavf
       61 heilnakkyd itsinfssyg aswvhlnerg qviaplynyt kelpkdliat fyktygpela
      121 fgqttgttns gmlnagmqly wlkhqkphly kkikwsmhlp qylsymftgi pvseytsigc
      181 htalwdydkq dyhswvyqeg iheklapiva aetsinmkyn qkrlkigvgi hdsssallpy
      241 vrsinskfvl lstgtwsicl npfsngilsk ndvadnciny mringepvka srlflghlyn
      301 tktewlanyf nkpvdyhkkv afdshiidnl ttgnshyfts qqiensdsdq qihipfksye
      361 vayhqlvlel velqvsyikk aigqdvitnl yidggfannl ifvellsral psmkikttda
      421 slgsalgaai aisnvkldgq flhknyalkk hsplitt
//
LOCUS       WP_010519693             415 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Croceivirga radicis].
ACCESSION   WP_010519693
VERSION     WP_010519693.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18643657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..415
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=45779
     Region          58..323
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          223..>415
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          223..251
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(224,227..228,231..232,234,258,261..262,265..266,
                     268..269,292,295..296,299..300,303)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          256..286
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          291..319
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkrkmlvlla mgvslagvaq kdeiktaaka mktgdaagak talmsasgsi sgadeklqaq
       61 yyallgdaha klsefdpaie aykkaisiee asgkkkysae ieqkmsqmsa dmvnsavedn
      121 ankdfksaak klyqvynmrp qdtiylyyaa ssavtagpdn ydqaikyyek lkeinydgsg
      181 vkytavnvat geveeldqnt rdlyikagth kdpkdektes kkaeivknia liyqeqgknd
      241 ealaayedai asnpndvnlv lnkanlyysm gdkdkfkelm aqasemdpdn adllynigvi
      301 nmeqgnleea raaykralei npdytnaqln lstsyvnegn alidemntlg tsradtqryd
      361 elkkqkddlf kkgakileda lkqkpnnegi laqlkniyga lgdnenfmri kqmme
//
LOCUS       WP_010519743             126 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Croceivirga
            radicis].
ACCESSION   WP_010519743
VERSION     WP_010519743.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..126
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=13848
     Region          <70..126
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 msvkakyqpv ldlgeklaik dgnvteeagv lkikgeaatq yeknliwdki keiggespsd
       61 lkanitvsdt svyhrhtvks geslsliakh yygdpmkykq ifeantgilk npdvihpdqe
      121 lvipnl
//
LOCUS       WP_010519764             429 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Croceivirga radicis].
ACCESSION   WP_010519764
VERSION     WP_010519764.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..429
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47905
     Region          9..401
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mnipqssnpr vviigggfag ialakklskq efqvvlldrh nyhtfqplly qvstgglepd
       61 siaypirkvl qgypnfyfrl aevlkvntdv nlvdtnigsl kfdklvvatg tetnyfgnte
      121 leansmamkt ipqslnlrsl ilenfeqall tddlhereal mnfvivgggp tgvelagala
      181 eikkgilpkd ypdldtrraq inivqggdrl lpamsekase kaeafleelg vnvwkklrvs
      241 gydgklattn tdisfrtetl vwaagvkavs lkgldgeafv srskrllvne fhqvkgfdni
      301 yaigdvaqme seafphghpm maqpamqqge nlgnnlvaes kgnslkpfsy rdkgsmatig
      361 rnkavadlpk fkfqgvfawf vwmfvhlyfl igfrnrvvvf inwvynyikf drearliirp
      421 fknhfktke
//
LOCUS       WP_010519771             202 aa            linear   BCT 01-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Croceivirga
            radicis].
ACCESSION   WP_010519771
VERSION     WP_010519771.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..202
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21967
     Region          1..199
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mflqlidvlg tiafaisgvl vamdkkldpf gvliigfvta igggtlrdll igntpvvwmr
       61 danymiiiit svffgvlffn klkylrkslf lfdtigigly tivgiekgme aglipaiciv
      121 lgiitasfgg virdilcnei pvifrkeiya tacilggvay fvldyipftk nyatvggilv
      181 vllirilavr ykislptiyk sn
//
LOCUS       WP_010519772             241 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [Croceivirga radicis].
ACCESSION   WP_010519772
VERSION     WP_010519772.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..241
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=27589
     Region          5..152
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mgnlqinttq nvnlnykivs lgerivafli dgfilylyai lvnligdmig yiykdgwtqr
       61 glvaliflpa mgyslfmhsl fngrtvgkml lkmrvvrfdg tpvhwsnylv rwmlrlvdiw
      121 lfvgsigils ilfterrqrl gdaaagtvvi stknktkvsh tiledvtddy eptftnvtml
      181 tdkdirlike tfliakksnd yktltalrvk vdsildtksn lydlqyidtv lkdynyytqk
      241 i
//
LOCUS       WP_010519846             342 aa            linear   BCT 01-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Croceivirga radicis].
ACCESSION   WP_010519846
VERSION     WP_010519846.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..342
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=38648
     Region          30..108
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(30,42..43,45..46,48..49,52..53,55,62..65,66..68,70)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          97..332
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 meteafgpsq eddlfehhkf vaskgqeplr vdkflmnfie natrnkiqqa akdghiwvng
       61 atvkqnykvk agdvvkvlfe hppyeylltp eaipldivye ddhlmvvnkp agmvvhpghg
      121 nysgtlvnal vyhfeslpnn ssgrpglvhr idkdtsgllv iakteeamth lanqffekts
      181 kreyialvwg nieedegtie ghlarnpknr lqmmvfpdgd qgkeavthfk vlerlgyvtl
      241 vsckletgrt hqirvhmkyi ghtlfndery ggdkvlkgtt ftkykqfven tfkvlprqal
      301 haktlgfvhp vtgkelnfds pipedmvaai ekwrgysqhl ka
//
LOCUS       WP_010519797             109 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator
            [Flavobacteriaceae].
ACCESSION   WP_010519797
VERSION     WP_010519797.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..109
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12296
     Region          7..103
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mnientkaqm rkgvleycil silkdedkya seilgalkda kmlvvegtiy plltrlknag
       61 llnyrweest sgpprkyyal tetgqlflke lngtwdelrn avnlvtnnn
//
LOCUS       WP_010519853             200 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Croceivirga radicis].
ACCESSION   WP_010519853
VERSION     WP_010519853.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 200)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..200
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22853
     Region          67..193
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
ORIGIN      
        1 mykvfvnekp lyltnkrplv qenvydieei nlknvldgff qknsfgaflf dpkgdvlntf
       61 akdvpivlaa ggvvknaknk vlfikrnkkw dlpkgkldkg etieaaaire veeetgisgl
      121 elgdflqity hvfvrkgkyk lkvvywyamy ssfdgklvpq qeegitkvkw kgvqkgkkal
      181 kntyenikll feensiyetl
//
LOCUS       WP_010519563             913 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Croceivirga radicis].
ACCESSION   WP_010519563
VERSION     WP_010519563.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..913
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=105074
     Region          150..858
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 misflqetvl kivaespnlg qsyfilpsrr aglylkkyla qqlekpiisp kiisieefil
       61 evselnettn fdlllklyec yleiepketl adfltwgttl lgdfneidrh lgnaeelfny
      121 itavtriqqw npnqeptdli kgnlkfinrl telypkyqkt llnaqtgyqg liyrtahqki
      181 eafkrtkgve hyffigfnal ntaeseiikc lldsgsakiy wdidahfyed kqheagyfir
      241 shqqtwkflq enpispskly ntkskkitit gtpkniaqak yvgnllkeiy knpekkqspv
      301 alvlsdetll pavlnalpke vpqtnitmgl plaktalnaf ictflrthqt knqkgwyhkd
      361 ilqltsntyf ktvlkpyeit klssllqyik eqnilflpve qiaeqfdees lvhlllnsnn
      421 dnperfvknl levleklrqv yiskentyel qslkrfiqvi nqlnllqtrk syikdlntle
      481 slylelidse qidfkgsptd glqimgmles rnldfetvil vsvnegilpa gksnnsfipf
      541 eikkefglpt ykekdavyay hfyrllqrck nayityntep dvlfgneksr fisqlltdds
      601 lqlelkeila tprissfkke kravektell vdrlkeiaas gfspsslsny iknpynfylq
      661 svlrirdveq veeqiahntf gtiihdslee lylplvntil tkellntlns kvkeivkkqf
      721 lkfytetdlk ngqnlialrv veqyvhkqie fdinriknnk ivvlgleldl rlalahfkdf
      781 pvflrgkidr iesvngdihi ldyktgnvai sevktadfds ittsdtslka fqllcyalmy
      841 hkqngvdqfk agiipiknln lgtilfgikd tpraqknnpi idlelltsfe qqlniligti
      901 ldpsvpfmdl det
//
LOCUS       WP_010519930             203 aa            linear   BCT 01-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Croceivirga radicis].
ACCESSION   WP_010519930
VERSION     WP_010519930.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..203
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22983
     Region          2..193
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mklicigrny tdhiaelnne rpkdpvvfik pdsavlpkeq dfyipefsnd vhyeveilvk
       61 ikkvgkhisp qfahkyydev glgidftard lqsqlkekgl pwekakgfdg savigkwlpk
      121 kefqnlndlk fslhkngdlv qdghtalmlw kideliayvs tffmlkkgdv lftgtpagvg
      181 kvapndyleg fieqekifai nvk
//
LOCUS       WP_010519860             267 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Croceivirga radicis].
ACCESSION   WP_010519860
VERSION     WP_010519860.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..267
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29693
     Region          4..263
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mkellrrslt gvvyvsllla aiflnsdafd flfmvfglgc iyefkrllki rryyvfvafl
       61 glwwlyiyfi ksilpvyall altlltnill lgylfsgkhk vftalqkfli alfyigsgci
      121 fltmipyrle gfekilimgv fviiwvndsf aylvgksigk nklfpsispk ktiegslggl
      181 ifavlagyli srfdasistv ewlilamvlv isgnlgdlle skfkrsagvk dsgailpghg
      241 gildrldslv faapfayatl tifsyvs
//
LOCUS       WP_010519954             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Croceivirga radicis].
ACCESSION   WP_010519954
VERSION     WP_010519954.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12912609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..300
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35177
     Region          8..75
                     /region_name="HTH_MlrA-CarA"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators MlrA and CarA; cd01104"
                     /db_xref="CDD:133379"
     Site            order(9..11,25,42..44)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133379"
     Region          97..>256
                     /region_name="MtbC1"
                     /note="Methanogenic corrinoid protein MtbC1 [Energy
                     production and conversion]; COG5012"
                     /db_xref="CDD:444036"
ORIGIN      
        1 mnnvkksfsi rdmenlsgik ahtiriwekr ynlfeperts tnirtyslrs lqkllnitll
       61 yhngykiski akipeseipv ivreivakns ershstnafk laminfdqsl ffntynslla
      121 ersfreifse vflpllnelg llwqtdtisp ahehfitnli kqkiyintek lqiieptrkd
      181 kvfvlflpen eihelgllyl nyeinlkgyk siylgqtmpi enlqdllkyh nyihfvsyft
      241 vspsqdqidk yiekfettin qvgncklwil gnqtqhldqd nlpesvstfn slerfisrls
//
LOCUS       WP_010519994             433 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Croceivirga radicis].
ACCESSION   WP_010519994
VERSION     WP_010519994.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46614
     Region          7..422
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(21..22,25..26,29,67,117..118,120..122,125,145,
                     148..149,152,247,250..251,254..256,259,287,291,349..350,
                     354,358,374,377..378,381..382,385)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mrfkglrwwv vglvalaaii nyidrqafga lwpdiakelf pemdgdghka iygsistvfi
       61 lsyaagqglf gkifdwigtr lgfalsiavw siatilhava qglysfsifr silglaeagn
      121 wpgaakanae wfptkerafa qgifnsgaai ggivaypiig iladflswks ifivvgllgl
      181 lwllpwlfiv kgtpkkhpwl seeekeyilt gqknqdldgd gnydegynpt tgkllkhkes
      241 wgviiasaai dpiwwlfivw ipiylsevfg lnvkeiafsa wlpyvgamlg awaggllaqn
      301 ritagwsvdk trkmvitlgc limlpcffll kapgtatnav iimavllfgf qvaigniqtl
      361 psdlfsgkiv gtlsgfagma aklgaagltl lvtfittggn ytpafiiggi lalvalgavw
      421 glcpkiaplk prq
//
LOCUS       WP_010520127             151 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Croceivirga radicis].
ACCESSION   WP_010520127
VERSION     WP_010520127.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..151
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17818
     Region          14..142
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mgnnknqeiv ksvftkflee nghrktpery ailqeiyesd dhfdveslyi kmktknyrvs
       61 ratlyntiel lldcklvrkh qfggsqaqye ksyfdrqhdh viltdtgevv efcdpriqsi
      121 kktieevfdi kinnhslyfy gtrnkqenvt d
//
LOCUS       WP_010520148             248 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Croceivirga
            radicis].
ACCESSION   WP_010520148
VERSION     WP_010520148.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..248
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27736
     Region          11..238
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mgsitegikh liiinviffv agisgladtl yeylalwfpl hpnfgvwqlf thmflhsftd
       61 vmhilfnmlg lwmfgspler mwgrnkflff yfsagigagl lhiatnyyff dqgleavlts
      121 gitkqevidv lasgrdspdw yklasqatid kfmgafnspa vgasgavygi lvafafsfpn
      181 aelmmlflpi pikakyfvpl liagdlvfgl snantgiahf ahiggaligf immwywkknq
      241 fnnnrwdr
//
LOCUS       WP_010520167             509 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 3 protein [Croceivirga radicis].
ACCESSION   WP_010520167
VERSION     WP_010520167.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..509
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57274
     Region          5..>372
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mknklslkqk vgqlfmpaaf indseeeiqr leqlianyhi gsicffhsra saatnfegkk
       61 evlynkdsld qlkilinryq kaaktpliig idaewglamr ventpqypya itlgalpeda
      121 lnliretgkn igrdcleagi hwnlapvldv nnnpknpvig yrsfgsdkhk vlqktqafid
      181 gmnetgilns vkhfpghgdt avdshlglpq iektedelln qelfpfyyie kekldavmvg
      241 hlalpkitgd sllpatlskp lidryirekm nfdgiiisda lnmhsiskkf qekgaveyqa
      301 fmagmdvlcf aehvkegier ivkqapeali nekynrfeil kskafaakpq lnyisyqdli
      361 aktatksltr llpdidtssy ldaqthlitm gkelshfenl lvtessilks avekplstki
      421 vlalappsik pvnqfgfttl elerinkllq qknvvlfnfg nplflneidy kkakqvylvy
      481 qdfpqfqeha akqllqqlpl ygslpvnld
//
LOCUS       WP_010520185             165 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Croceivirga radicis].
ACCESSION   WP_010520185
VERSION     WP_010520185.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..165
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18660
     Region          49..152
                     /region_name="cupin_HNL-like"
                     /note="Granulicella tundricola hydroxynitrile lyase
                     (GtHNL) and related proteins, cupin domain; cd02233"
                     /db_xref="CDD:380361"
     Site            order(58..59,90,92,113,115,117..118,137,139,141)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380361"
ORIGIN      
        1 mkttnnnfrk ftmlmlglic yttgvfaqkt dyaissyqte gvkapnthyi gaawlnpllr
       61 adddldynit katfkanstl dwhkhesvqv liivdgvgyy qekgkeavlv kegdvircek
      121 ntehwhsssk hkdvtylaiy ggenptvwte vvsqayydkv aerln
//
LOCUS       WP_010520186             153 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Croceivirga radicis].
ACCESSION   WP_010520186
VERSION     WP_010520186.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..153
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16248
     Region          1..150
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 matfnlking ktqtvdvdga tpmlwvlrdh lqmvgtkfgc giaqcgactv hlgdnavrsc
       61 qlpvsavgeq eittieglse hgdhpvqkaw levdvpqcgy cqagqimtas allkhnpnpt
      121 ddeiasamhg nicrcgtytr ikkavklaae nns
//
LOCUS       WP_010520258             248 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Aquimarina agarivorans].
ACCESSION   WP_010520258
VERSION     WP_010520258.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..248
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26149
     Region          1..247
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvcishv pdttskinft dgdtkfdtng vsfvinpnde fgltramwfk ekqgasvdvv
       61 nvggadtept irkclaigad nairvnadps dsffvaqela svaknggydl iiagresidy
      121 nggvvpgmla alldanfvnt cislevdgts atavreidgg ketikatlpl viggqkglve
      181 esdlripnmr gimmarkkpl tvieptgtas qsqpssfskp epkgsvklvs adnldeligl
      241 lhneakvi
//
LOCUS       WP_010520263             445 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Aquimarina agarivorans].
ACCESSION   WP_010520263
VERSION     WP_010520263.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..445
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50377
     Region          107..442
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkkllittfa svvfyglgqa qkentktvws iqdcmeyaik nnlqiqqqql dlqdadinkn
       61 daknaflpdl ngsasndwnf gfsrningvl seqntrsssy slnsnipiyn grqnynrlqr
      121 aklqkvanqy nidrlkddir iniansylqi llqqenlnvl kaqnditleq ikrtqqlida
      181 gnlpegdvlq lkataaenlq niansensva iaklglkqil qlnfenafei ekieiefkel
      241 lildqdvsqi vgtvlknrne iklaeqnikl aekditiakg affptisgnv nyntgeitiq
      301 dtpttvpffd qlnnnksfgf garidvpifn rfrvknnvgr nkvtmlrsqn qleqakqqlt
      361 qnvyqaylda kasdtsfeaa kvavtaqera feyaknrfev gisnsldftq ariayqnsqt
      421 qllrakydll fkvkllelyy gnaie
//
LOCUS       WP_010520267             233 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Aquimarina agarivorans].
ACCESSION   WP_010520267
VERSION     WP_010520267.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..233
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25675
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mieikdlhks yqmgsnslhv lkginfnvkk gelvsimgss gsgkstllni lgildeadeg
       61 syildntsik nlsekiaaey rnkflgfifq sfnlinykna idnvalplyy qgvgrkernd
      121 kalhylekvg lanwathlpn elsggqkqrv aiaralasdp kvlladeptg aldtktsyev
      181 meliqninde gktillvthe pdiaqmtkri vdlkdgliin dtriepvkak ahv
//
LOCUS       WP_010520239             424 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A [Aquimarina
            agarivorans].
ACCESSION   WP_010520239
VERSION     WP_010520239.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..424
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47048
     Region          1..421
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mtiplaerir pkslqdylsq qhlvgpkgal tfqltkgiip slilwgppgv gkttlaniia
       61 etsdrpfysl sainsgvkdv revidrakkd hglftsknpi lfideihrfs ksqqdsllga
      121 vekgwvtlig attenpsfev ipallsrcqv yslnafnkke leellkrate kdeflskkti
      181 kleetdalir lsggdarkll nifelvvasf ntksivitna tvtqlvqqnp arydktgeqh
      241 ydiisafiks vrgsdpnaav ywlarmiegg edlkfiarrl iilasedigl anptalvman
      301 ncftsatavg ypeariilsq ctiylatspk snasymaink aqqlvkqtgd lpiplhlrna
      361 ptklmkqlgy gedykyahny qgnfvdqefl pneitgtvly dpgnnnkess irtflktiwn
      421 kygy
//
LOCUS       WP_010520273             242 aa            linear   BCT 01-JAN-2025
DEFINITION  SCO family protein [Aquimarina agarivorans].
ACCESSION   WP_010520273
VERSION     WP_010520273.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..242
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27901
     Region          66..242
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mkkysyvgis fimllfgiif vprivdrike tkivsnsrms adnkitnekl syilingekk
       61 qipefalrnq dsliitqhdy kgkvtvvdff fvncpticpk mtsnlvylqn efkqttdfai
      121 asftinpkyd tptrlkkyae shkvtnpnwh fltgdreqiy nlakksfnlf aeqnpnvpgg
      181 fehsgyfalm dkqgfirsry dvhgnpiiyy rgtvsleeki adngeeeqis ilkkdiqkll
      241 ee
//
LOCUS       WP_010520301             419 aa            linear   BCT 01-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Aquimarina agarivorans].
ACCESSION   WP_010520301
VERSION     WP_010520301.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..419
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45184
     Region          <34..228
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mlgdaytapi ahvsvkesvf apspevsney mylhrdhlgs imaitdsaan vkeethygaw
       61 gtikqfkgan dattldessi lgrgytgheh fasiglihmn grmydaklgr flspdnfiqd
      121 pfntqsfnry gyvwnnplkf ndpsgeflit aiiigavvga yiggaqangn wnplkwdwss
      181 gatwagigig avvgaiggev vgagllgvka fgifsvklgv glavpgigtl gltkignels
      241 teytnpqget ynqnigtipg qgsiggrgng negppdnent dstqveaddv iakvkefvrp
      301 tlnsvfrvtq niykpivnqa sviwnegihe gkaynpsenf vykniytlne syewtisksl
      361 ftsgigtpsf aegkeitsdv itvvpspgln ivrnkifnff iksklkkefk egvdrlpnr
//
LOCUS       WP_010520404             340 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Aquimarina
            agarivorans].
ACCESSION   WP_010520404
VERSION     WP_010520404.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..340
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39086
     Region          100..338
                     /region_name="EEP-2"
                     /note="Exonuclease-Endonuclease-Phosphatase (EEP) domain
                     superfamily; uncharacterized family 2; cd09084"
                     /db_xref="CDD:197318"
     Site            order(104,137,208,263,265,307,330..331)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197318"
     Site            order(137,330)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197318"
     Site            order(208,265,331)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197318"
ORIGIN      
        1 mkripfllns ivvvlslgvl lisyipptkl hfvnycsllm pallvvnfgf vlywllqlnk
       61 kvllsalflv vsaksvqrly gfnfgasrsn qekgedtikl mtynsrhfss adehfvfide
      121 fmevykdsfp dilivqetyt skirelkkvy pyttkkikks nvlsnyilsk ypitnqgliq
      181 wkdtqmgrda afadikiknd tirfysihls sykfskkaee lqkrggksil krfsqvfkyq
      241 ekqveiikth iaespfpvvi ggdfnnnafs yvykrlfnss nfqdtfvaag sgfgatydfs
      301 yfptridfif vpesavvhah kivkrkgwsd hfpviseisf
//
LOCUS       WP_010520435             230 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Aquimarina agarivorans].
ACCESSION   WP_010520435
VERSION     WP_010520435.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..230
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25124
     Region          2..228
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mleakklekr ygehialkdl sftvapgeif cllgqngagk tttiniflgl lkptsgeali
       61 nktsvlenpq irtsiayipe ivelynnfsg ienidffsrl agfkytkdel vsflnqanlq
      121 avahnkkiat yskgmrqkvg iaialakkas yilmdeptsg ldpkasvefa nlckklavkg
      181 vgifmtthdi fnavnigsri gilkegslky ttetakitaq elqdlyikti
//
LOCUS       WP_010520544             556 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Aquimarina agarivorans].
ACCESSION   WP_010520544
VERSION     WP_010520544.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 556)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..556
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62070
     Region          1..555
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mkpllkvtnl svafngknvl hnisfslten silgvvgesg sgksvtslai mgllptkiat
       61 itsgsieflg kdiggysydq fktirgnqis mifqepmsal npsmkcgpqv aevlkthtnn
      121 nnqevkekvl alfdkvklln snriynayph elsggqkqri viamaiackp klliadeptt
      181 aldvtvqkei iallkelqkd qqmsilfish dlalvadiad ttmvmyqgkl iehqnttqlf
      241 ntpkatytka liysrpslne rllklptind flnhkpkstl ltskdrairh qklyakepil
      301 evinasktff nksswfskts fkavdnvsfs iyegetlglv gesgcgkstl gnlilqltki
      361 dqgvikyrgi ditalsrrkm relrkeiqli fqdpfaslnp rmtigkaime pmkahklyen
      421 dqqrnkkvle llesvglste hfnryphefs ggqrqrigia rtialqpkli icdesvsald
      481 isvqaqvlnl lnelkerysf tyifishdla vvkymadqll vmnkgrieek gdadaiysnp
      541 qksytkklie aipkgi
//
LOCUS       WP_010520563              91 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Aquimarina agarivorans].
ACCESSION   WP_010520563
VERSION     WP_010520563.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..91
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=10341
     Region          <2..>76
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mlkkiisnyk kgasfselak kyskdkfyak kggdigwikk gymmkeidea ifthkkgdil
       61 sikapewgwt iilitespii neyaellivk k
//
LOCUS       WP_010520576             448 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Aquimarina agarivorans].
ACCESSION   WP_010520576
VERSION     WP_010520576.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..448
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=51623
     Region          3..>65
                     /region_name="DnaJ"
                     /note="DnaJ-class molecular chaperone with C-terminal Zn
                     finger domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0484"
                     /db_xref="CDD:440252"
ORIGIN      
        1 mknlyqtlgl knnasqdeik kayrklaikf hpdknigddf fdelfrevkd aydilsnptt
       61 krtydlkynl finnskikhr kttnpaekaq qkntnennsk kkytkqtnss freiflknlv
      121 klnhltfkqa ltlllltili iilfvcsyln glwgfltits lygftylfvr tikninkidn
      181 tsslliglif apiiviltfg ksldyfgvqn svwfnshnks evvstknvfe pkisnqknks
      241 stvnenpkll kiydwmdedq rkrirrlnki tinasnfkkd lesgkydlss iktkktisky
      301 kgnqlkngas plddcfgkgi ysqdawlkfd nsnksdaivc lvrnydqkti rneyikagak
      361 femskiptgv yyikvyygnd wnpnkknfcg ingafeknvs fsksdraedq iiikntsksy
      421 ttgiitlyav angnmkteri neevffnk
//
LOCUS       WP_010520581             211 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Aquimarina
            agarivorans].
ACCESSION   WP_010520581
VERSION     WP_010520581.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..211
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23410
     Region          24..95
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          121..188
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mkkllitmlf mlgvcltltg qqtmdkfeiq vdglgcpfca yglekkfkef kgikevqiki
       61 etgdfkfayp sekqltmqav vdqvkkagyt pktakiirsn geqenlsvpg nkiadksqli
      121 teslkvkgnc qmcksrieta altiegvnka lwnvdtkile vdfndketsi reiskkiats
      181 ghdtatmeak kevynalpvc csynnpnlks h
//
LOCUS       WP_010520625             506 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpP1/FadL family transporter [Aquimarina agarivorans].
ACCESSION   WP_010520625
VERSION     WP_010520625.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..506
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55762
     Region          <226..506
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mkkflltllg aiifsaistg qttsdifdis nthnlgtary nglsgafgal ggdltavaen
       61 paggavftns ygsatlsqgs sdfnsnyfnt ntptneanfn fnqiggilil kndddsssis
      121 kislgllfnk dndyrreyel ngnsstgnig gyfvgqangf tvdtisvrdg edfesayidi
      181 gesngfgvrg qqaflareaf iitedesddr lyssevsgig nsqkintits grsskisinl
      241 afeidkkiyl ggnlnfhnyd lrkrslisei nnettddvse lffetrsrtf gngfslslga
      301 iakvskqlrv glsyqtptws tlqneldqnl tsflninnne ireidprlvf lypeydlrtp
      361 geiaasfayv fgknglfsaq ysrkdfsnie ygdnafdfdi lnrrikntfq avntikvgge
      421 yrykkwrlrg ginyatspyk ndqiagdtqg fslgtgydwg kwkldiaynr ietdinevpf
      481 endaynnsaq ingkndaisv tlgvnf
//
LOCUS       WP_010520746             386 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Aquimarina agarivorans].
ACCESSION   WP_010520746
VERSION     WP_010520746.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 386)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..386
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41587
     Region          10..277
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mssaqieiql iativaaaca lpgvflvlrk malisdaish silpgivvgf fitqdlaspv
       61 nillaaltgv itvvlvefiq ktglvkedta iglvfpamfs vgvilialna ndvhldidav
      121 llgelafapf drilikgtdl gpkalwvvgl illitlilli tfykeikvst fdqglaaalg
      181 fspvvmhygl msvasvttvg afdavgailv valmiapaat vylltndlkk llvgavgigv
      241 lsaisgywva hwldasiaga ittvlgglfl laylfapnkg lfsvlyrqkq qrkevmlltf
      301 llhiqnhyee eerhvnhlne hinwqevkak svldlasknn miaikngvie ltekgqvfts
      361 kaiqyitdne rseiegmkde lflfrg
//
LOCUS       WP_010520766             287 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Aquimarina agarivorans].
ACCESSION   WP_010520766
VERSION     WP_010520766.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..287
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=32808
     Region          1..146
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mknilvttdf sknaydalfy atrlfkkepc qfyilntfev ktpiftsrly lekgaalyhs
       61 lseksecelk evlhsivrdt edfehqfeii siskplieti aktivskqid lvvmgtkgas
      121 gikeifmgsn tvnvieains spilvvpeni diyplyhiaf atdftnkynl nvlqtlksfc
      181 klddailkvi hvtdtkelsn sqqenkrsld tyfddvkhst isiaknksve khistmvdcl
      241 efdllamiky rhgffekmth eaiikkighh tkrpfliipd elinviy
//
LOCUS       WP_010520832             588 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 36 protein [Aquimarina agarivorans].
ACCESSION   WP_010520832
VERSION     WP_010520832.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 588)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 588)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..588
                     /product="glycoside hydrolase family 36 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=67783
     Region          186..476
                     /region_name="GH36"
                     /note="glycosyl hydrolase family 36 (GH36); cd14791"
                     /db_xref="CDD:269892"
     Site            order(194,225,267,326,330,379,395,398)
                     /site_type="active"
                     /db_xref="CDD:269892"
ORIGIN      
        1 meidsthhid ilntsnafev ttnliesygs iavyelhffs dtvfepeqtt fkwrlpainv
       61 kgvwkptsdf skrimddwel dhlearisvd spvvavfghn dencvtfacs dainttelna
      121 lyreeddcih chisffkekh hqiknykvql iidtttyhfs naldkisqww ssfkqlspvm
      181 erndiatlpv ystwyqfhqd ldierllaes kkavklgfgv lilddgwqtn dsnrgydytg
      241 dwqperipkm rnfvdkvhqi gmklalwyav pfcgkksraf qkfkgmllae dhrwapvfdp
      301 rypevrthli giyvkalmew dldgfkldfi defkvytnti ltkengrdfa svnlavdrlm
      361 tdivqalkti kpnliiefrq kytgpamrky gnmfrafdcp gdsvmnrvri adlrmlcget
      421 avhsdmftyh idalvahkal qvvntlfgvp qlsvllekat vdelamisfy inywtrnkev
      481 llqgkftplk planypiiks etavhsivgi yddyvlpiek nsdridiing klteeiilny
      541 nsihgaysck vydcmgnltk qftiqmnevf kyinvppcgl iicskitt
//
LOCUS       WP_010520848             183 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Aquimarina agarivorans].
ACCESSION   WP_010520848
VERSION     WP_010520848.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..183
                     /product="YceI family protein"
                     /calculated_mol_wt=21092
     Region          <56..176
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mykrlcllll iplwftsfsi kgdkyicrng kvtffsyats enikaendqv lslfepetkk
       61 iavsilmraf qfekslmqeh fndsyiesdi ypkatfegvv lnfdkdlsgt qtkiingdft
      121 lrgiskpiki kaditkksnt yeiigeteln vkdykikvpq ilanriaqtv kisfnfkynh
      181 yek
//
LOCUS       WP_010520881             366 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Aquimarina agarivorans].
ACCESSION   WP_010520881
VERSION     WP_010520881.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..366
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41207
     Region          9..242
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(12,14,144)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(39,143..144)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            142..144
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mlnnktvavv vpcynesqqi kivldsmpsf vdriivvdda ssdntaqtvm qlignnqssi
       61 kltsklkqtl vpnlynradi evrkksieei slftpselln knpdnekviv ikhlenggvg
      121 aaiatgykwc kdhnidctav magdgqmdpd elvsicspvt negidyvkgn rlihksawvi
      181 iprvrflgns vlsiltkias gywgvsdtqs gytaisnnal nsvplydiyk rygmpndllv
      241 klniafctir evkikpiygv geksklnilk vsipillllm rcffkrlkik ylyrsfhplf
      301 llywiaiiig iinsyfayql iinfinpnsk tptdyliifi flfisgfqsl lfamwmdiqd
      361 neklsk
//
LOCUS       WP_010520896             943 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Aquimarina agarivorans].
ACCESSION   WP_010520896
VERSION     WP_010520896.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 943)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 943)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 943)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 943)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 943)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 943)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 943)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..943
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..943
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=110171
     Region          1..939
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mtrqseyile qnlvaqlqel gyqkvvikde qdlinnlksq lekhnncmls ekefkqilnq
       61 lskgnifeka kilrdkiqyv kdngsngyie lvnqiawckn qyqvthqitm egtyknrydv
      121 tilvnglplt qielkrrgle lkeafnqtnr yqrhsyqsgk glfqfiqlfv isngvntkyy
      181 annsikarsf kqtfywadde nkiisqlsdf tkqflepchl skmitkyvvl netkkelmvl
      241 rpyqyyatea ivkrveetnk fgyiwhttgs gktltsfkta qiltnsdkvy kvvfvvdrkd
      301 ldyqtikefn sfsegsidat nnttalvkqf sddtklsvtt iqklntaiqk pkhlekmell
      361 kdkkvvfifd echrsqfgdt hkrikeffvn aqmfgftgtp ifadnavknq lgkrttkdlf
      421 eeclhkyvit dairdrnvlr faieyistfk gkdgvvdiqv dgidkkevme apkrldnite
      481 yiinnhnrkt hnkkftsilc tsnvdtaivy yellrekkeq gkhdlrvati fsyksnedds
      541 davgfipdee ffddfetskn nthtreklds fiadynniys tnystktfys yykdigkrvk
      601 nrqvdvllvv nmfltgfdsk llntiyvdkn lryhgliqay srtnrvlnel kshgnvvcfr
      661 nlkdqtdeai tlfsnkdave eiilkpyedy lesytnsver llkiaptvds vndlisedde
      721 lefikafrei mrlqnvlnsf tqfdfedlpl deqtfedyks kyldlydevk ttnqkekvsi
      781 lndidfeiel irrdeinvay ilsllaklqd akkpdekekq rkaiseimss etqlrskkel
      841 ierfidenlp lvndsenipe afdtfwtiek qtaidnlske enlnvlklqe vvsnylftqk
      901 mplrdeivnl mntrpslker kskaervaek ilefvntfie gmg
//
LOCUS       WP_010520929             246 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Aquimarina agarivorans].
ACCESSION   WP_010520929
VERSION     WP_010520929.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..246
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26466
     Region          1..243
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mnlqdrviii tgassgigea takklaedga svvlmarsed klktlktdie kvggkalvat
       61 gdvtkrkefe avvdsavkhf gkvdglinna glmplsfvkk lktdewekmv dvnikgvlng
      121 vssvlpqlle nkggdiinis smaanryfpg gavycatksa vkmfseglrq elapehginv
      181 tsiepgvvat nltstitded ikdkmsemqk mttlesedia naihytltqp krvnindiyi
      241 lpteqk
//
LOCUS       WP_010520946             312 aa            linear   BCT 01-JAN-2025
DEFINITION  hydrogen peroxide-inducible genes activator [Aquimarina
            agarivorans].
ACCESSION   WP_010520946
VERSION     WP_010520946.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Jo,I., Chung,I.Y., Bae,H.W., Kim,J.S., Song,S., Cho,Y.H. and
            Ha,N.C.
  TITLE     Structural details of the OxyR peroxide-sensing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 112 (20), 6443-6448 (2015)
   PUBMED   25931525
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..312
                     /product="hydrogen peroxide-inducible genes activator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34982
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..291
                     /region_name="PBP2_OxyR"
                     /note="The C-terminal substrate-binding domain of the
                     LysR-type transcriptional regulator OxyR, a member of the
                     type 2 periplasmic binding fold protein superfamily;
                     cd08411"
                     /db_xref="CDD:176103"
     Site            order(103,106..107,110,114,122..126,221,224..225,228,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176103"
ORIGIN      
        1 mtitqlkyvl avaeyqnftk aaknvfvtqp tlsmqiqkle deldiqifdr tkkpiqltev
       61 gkklvvqarn ivnesnrmqd vvdqqkgfvg geftlgiipt imptllpmfl ntyikkfpkv
      121 klkivelpte giiqdildgh ldaaiaatpl nndtikervl yyepfigyvp psnklashek
      181 lapgdldind mllledghcf rdsvlnickt qktydeerfk lasgsfetmi klaneglgmt
      241 llpylnsldv kesdkknlrn fedpsparev sliyhkselk iqiinslkdt isaivkgaia
      301 fqnvqiispl gk
//
LOCUS       WP_010520963             421 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Aquimarina agarivorans].
ACCESSION   WP_010520963
VERSION     WP_010520963.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..421
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44023
     Region          23..418
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mnevqqkald aaissingdm galwitisai lvffmqagft lvevgftrgk nagniimkni
       61 mdlcigsimf wavgyafmyg dtvllggfmr sssadqgyff fhaddwynlf fqtvfcataa
      121 tivsgavagr tkfttylvfs filttiiypi sgswywpfdd dawlntlgfv dfagssvvha
      181 vgggaalvaa klvgprigky vdgkvnvipg hnllfgalgv lilwlgwfgf nggsqlawgg
      241 sdtvaagsvi intniaaamg aiaalfftwi kygkpdismt lngglaglvg itagcgavsa
      301 ggalaiglic giavvlsief idktlriddp vgaisvhgtc gflgtvlvgv faldggllng
      361 ggakllgvqa lgslsyigwa vlttfivlfi lkkvmglrvs ekeeiegldv hehgisvyta
      421 e
//
LOCUS       WP_010521056             472 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Aquimarina agarivorans].
ACCESSION   WP_010521056
VERSION     WP_010521056.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..472
                     /product="TolC family protein"
                     /calculated_mol_wt=54366
     Region          44..245
                     /region_name="OEP"
                     /note="Outer membrane efflux protein; pfam02321"
                     /db_xref="CDD:396757"
     Region          147..471
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkqfffqfsv ifmllcktfc taqkitippt eifsyqefls fvkkhhpvik qanlnlsmge
       61 akllksrggf dpkievdyqn kefkkqeyyd ilsatfkipt wygiefkanf eentgvflnp
      121 qnnvpdngly sagvsvsale gllindrmat lkkakyfleq sraertlltn eliyqatlay
      181 fnwikattee tifenslkna eirfnatkrr vetgdkavid sieakitfqn rglgleaakl
      241 kriksafkvs nflwlndipl elqpnvrpnv peisvinsll qinqpeadsl llenhpkiqs
      301 lnfkieslnv drrlklnkll pkldlnynfi ssspeqidtf nqreykagik fstplflrke
      361 rgdlrlskfk lqdanfelna qtlairnkin iayaeinsld kqfiliedmv inyrtmlaae
      421 erkfflgess lflvnsreqk lidsqlkqne iqvkllntra klfnslglsp ee
//
LOCUS       WP_010521264             269 aa            linear   BCT 01-JAN-2025
DEFINITION  glycogen/starch synthase [Aquimarina agarivorans].
ACCESSION   WP_010521264
VERSION     WP_010521264.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10550881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..269
                     /product="glycogen/starch synthase"
                     /EC_number="2.4.1.21"
                     /GO_function="GO:0004373 - alpha-1,4-glucan
                     glucosyltransferase (UDP-glucose donor) activity [Evidence
                     IEA]"
                     /GO_process="GO:0005978 - glycogen biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30895
     Region          6..235
                     /region_name="Glyco_transf_5"
                     /note="Starch synthase catalytic domain; pfam08323"
                     /db_xref="CDD:400563"
ORIGIN      
        1 mkdkrilyva selmpylpet evssmafesp kmvngkggqt rifmprfgni nerrhqlhev
       61 irlsgmnlvv ndfdmpliik vasipkermq vyfidneeyf krkatvtdkd gklfkdnder
      121 aiffakgvie tvkklnwapd iihvhgwmaa llplylknyy sneplfketk iitsvygngf
      181 egtlnndikk kvlfdeiaee klslleeanf dnlmklsven sdavimgtpt isseiekfid
      241 akkvptlayk ypeefssaye dfylnevls
//
LOCUS       WP_010521113             362 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Aquimarina agarivorans].
ACCESSION   WP_010521113
VERSION     WP_010521113.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..362
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40462
     Region          8..353
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mdsksisngi lravsiilgv alllfflyki ssillyilig aaislmgrpl mlfltrklkm
       61 rnsfavvicl iiflltflsi ftlfvpiiie qtqiigqvdi qklgddltrl anesaayfri
      121 ekfnlvealq qtdiskyfsf kwvpkllnav lggfggfmig lfsvvfiaff alkdskllen
      181 sllvfakned erkfmnafsk ikellsryfv glllqvfilf imysilllif kidnaialal
      241 iaailnlipy lgpvigfglm maltvtgnle mdfstvvfpk miyisigyii iqlidnfvnq
      301 pfifgnsvrs hpleiflail imgvlfgipg liaavpfyta vkviskefls eykivqslts
      361 ei
//
LOCUS       WP_010521268             382 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Aquimarina agarivorans].
ACCESSION   WP_010521268
VERSION     WP_010521268.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..382
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44440
     Region          17..249
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mksllitlal ciffgtisaq tvtknikslh ldtsrevkir lpksykkdpn keyllivtld
       61 gdylfdpmvg nvkyfsywed mpeaivvgik qsktrkedcr ydsntylpey egrkfydfva
      121 telvpfmenn yrlakfkiia ghdytgnfin yfmktdksaf qayinlspef aptmsdrvvd
      181 iltatenkmw yymatatndv kslrediilv ndklstiene nvrykfddfe dashyslval
      241 gipraledif siyrpiskke ykenianlet spydylieky eiiksllgve krirvndfia
      301 istalekked weeleklgkl arnvypahml gnyylgtaye nkgepkkamr ayqngfllee
      361 isflskdiml ekaerikqdf gy
//
LOCUS       WP_010520640             375 aa            linear   BCT 01-JAN-2025
DEFINITION  MraY family glycosyltransferase [Aquimarina agarivorans].
ACCESSION   WP_010520640
VERSION     WP_010520640.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..375
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=42056
     Region          42..301
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            99..100
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            219..222
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133463"
     Site            order(277,291..294)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 mknyialiia isfvalflsi kifpliitlt kaknlmaapc drsshsvktp nlggvgiyiv
       61 ftlclilsgi ifnflqfemr qllalllsit ilffmgvkdd ligvspkrkl lgqivaallv
      121 vlltdvritn lfglfgvetv aylpsvvftv fmyvffinsy nlidgidgla gsiaviaslf
      181 fgvyflsnql ymatmisfvl vacligflsf nfskkrklfm gdsgsmfigl llmfqalyfl
      241 kvdvktyefi wipnkialvt sifcfpiidt irvftirilk gmspmtadrn hihhkildig
      301 fshiqatifl aisnlavigm vyfidgynvn vqlflvfsli llivylflkl nynktiksai
      361 sfstnffnrk sfklk
//
LOCUS       WP_010521336             373 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Aquimarina agarivorans].
ACCESSION   WP_010521336
VERSION     WP_010521336.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..373
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41528
     Region          43..371
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 meqqqrrtfl knltllssas ilpstlmsfe sfknaslnsg sekklnialc glgryakila
       61 dalqaadnck laglimetpe keetwgkkyn vpskniynyd nfdsikdnsa idlvyvvlpn
      121 smhkeftira akarkhvive kpmalnasdc lemiaeckkn kvqlavgyrl hydpyyheak
      181 rlansdslgp irfidsgfgy rikgwskdaw hlkkamaggg plpnigiyci qnnryilgee
      241 pthvtaqfgp iqrpeffdev eesitwqlef pggaitnsas sysyninkiy asgdkghfel
      301 dpahsyapls gksslgamdf psinqqkeqm dgiaayilkn eplpnhitgr egykdmlvid
      361 aiyesaktgk ktk
//
LOCUS       WP_010521474             347 aa            linear   BCT 01-JAN-2025
DEFINITION  YncE family protein [Aquimarina agarivorans].
ACCESSION   WP_010521474
VERSION     WP_010521474.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..347
                     /product="YncE family protein"
                     /calculated_mol_wt=37675
     Region          <72..224
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mkitrillsl itvtslfvsc qsdddnslie pvseeriivs hegasvsgst siisldlktv
       61 nnkfydtvne eelgvfqqsi gfnddkayiv vdnqntitvv dkvsfkkqas iteklktpry
      121 iafangkgyv tnwgdtslat ddfiavidla sntvestiav aegpeqsvik gnklyvshkg
      181 gfginnrvsv idlstsnvke ietlflpdem vlvgddlwvs cegtpvwrpe gesiggliki
      241 dtttdeitss iefplgqhts qmvfengniy ytvsneifef aitettlptt avtegaingm
      301 airdgiiyvv dakdfasggt lntydlneek wgtpvtvgva pakiyfq
//
LOCUS       WP_010521406             290 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Aquimarina agarivorans].
ACCESSION   WP_010521406
VERSION     WP_010521406.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..290
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32602
     Region          <173..288
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 meaptkkkgk iatkllnkyr lvilnentfe eqvsfkltrl nvfvlvmits lllitgtifl
       61 iafsplreyi pgyssselse kanrlayetd sildkvryne kyyesikkvl tgqvsaesfs
      121 kdsvdkdikk elstvnlkps aedielrkev ekkekytvkn ssdleqeylf ippvkgsvts
      181 kfdyklkhya vdiavdkdtp vkaatqgviv fsewtpdtgy villkhtsgl lsvykhnakl
      241 lkkqgdivia geviaiagst gefstgphlh felwekgqal npsdyidfek
//
LOCUS       WP_010521483             260 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Aquimarina agarivorans].
ACCESSION   WP_010521483
VERSION     WP_010521483.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29280
     Region          6..258
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mssnsievkn lkigyiqgkk hevilknisf hltkgnlvsi igangtgkst llrtlahqqp
       61 klsgtveien tllenfsinq wakqvswvht etiipsslsv yelvslgrqp ytnwldklkt
      121 tdsieiekal qltdladlkq kkcntlsdgq lqrvfiarai aqntpiifld eptthldlhh
      181 kvetltllkr lckeynktiv fssheielsl qvcdqvlsis qkkvalhtpk glietnllne
      241 lfqdskvhfd ktlgkflfke
//
LOCUS       WP_010520972             270 aa            linear   BCT 01-JAN-2025
DEFINITION  prohibitin family protein [Aquimarina agarivorans].
ACCESSION   WP_010520972
VERSION     WP_010520972.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Yoshinaka,T., Kosako,H., Yoshizumi,T., Furukawa,R., Hirano,Y.,
            Kuge,O., Tamada,T. and Koshiba,T.
  TITLE     Structural Basis of Mitochondrial Scaffolds by Prohibitin
            Complexes: Insight into a Role of the Coiled-Coil Region
  JOURNAL   iScience 19, 1065-1078 (2019)
   PUBMED   31522117
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..270
                     /product="prohibitin family protein"
                     /GO_component="GO:0005743 - mitochondrial inner membrane
                     [Evidence IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0035632 - mitochondrial prohibitin
                     complex [Evidence IEA]"
                     /calculated_mol_wt=30096
     Region          27..223
                     /region_name="SPFH_prohibitin"
                     /note="Prohibitin family; SPFH (stomatin, prohibitin,
                     flotillin, and HflK/C) superfamily; cd03401"
                     /db_xref="CDD:259799"
ORIGIN      
        1 mdrlpkigip liillvftii fiskstitid sgkagvlykt fangvvtdep plgegfhfia
       61 pwnsvilyev rqqevfekmq vlssngleik leasawykpk ygdlgklhqe kgknylarii
      121 qpairsaars vvgrytpeql ysskrdviqk eifdetkkiv gkqyidleei lvrdvtlppt
      181 ikdaierklk qeqesleyef rltkaakeae rqkidaegka tankilsasl tdkilqekgi
      241 qatielsksp nskvivvgsa kdglplilgk
//
LOCUS       WP_010521484             153 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Aquimarina agarivorans].
ACCESSION   WP_010521484
VERSION     WP_010521484.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17287
     Region          3..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 msdldeidlk llkllqqsgk lttkeiakqv nlsptpvyer ikrleregii knyvalvase
       61 kvgkglivfc ditlkehtke ighqfvqevm svkyvcecyn isgnydfrlk vvvrdmkhyq
      121 dfvlndlgsi nnigsahstf vmgvikhdya vpl
//
LOCUS       WP_010521487             288 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Aquimarina agarivorans].
ACCESSION   WP_010521487
VERSION     WP_010521487.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..288
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=31686
     Region          7..287
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mkkaftikel lkiliqtykn wmandpfqls aavsyyalfs fpalliiviq svgifynkav
       61 ikgkiideva nvlgkdsast iealiknavi eeqsaiaftv gaatllygat gifvslqksl
      121 neiwnvapdp nagflkmikd rlfslslili igfllltslv ltalisviad winanlpdfm
      181 yslihlvnfv islglitvlf gmifkilpdi dikwkhvwlg afvtsllfsv gkfalgvyfg
      241 tmnpesafga agsivlillw vsysslilff gaeftkvyvd yrnkqltn
//
LOCUS       WP_010521500             339 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Aquimarina agarivorans].
ACCESSION   WP_010521500
VERSION     WP_010521500.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13307529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /calculated_mol_wt=39194
     Region          <134..333
                     /region_name="PRK15186"
                     /note="AraC family transcriptional regulator; Provisional"
                     /db_xref="CDD:185108"
     Region          251..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkdtqitqqk katglallde sltgtityig dmsilnisdk igkghvrfyd lheglkvydf
       61 dlkllkdiei pidsicsntl hffyclegtf shqfesidtp vsieqfqtav ahsndgfqsr
      121 ilieknkhlv vniifvnkkd yfekfndesl efgekiknll ndiskqqkyf haggfslkia
      181 eqlkllidie handvsekls qkgryyivla kqieqfynei ndtentsslf kselekiiei
      241 gnfinkqpel phairslcvk fglspaklqe gfkymykrtv sdyirnvrle kavylikttd
      301 fniseivysv gltsrsyfck ifkkkyecsp kefrkrqks
//
LOCUS       WP_010521555             892 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Aquimarina agarivorans].
ACCESSION   WP_010521555
VERSION     WP_010521555.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 892)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 892)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..892
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..892
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=101780
     Region          69..>418
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 melkpyqhtv ikdlekfldy vqkqptpaka ynqywedklg mpytpqldgs fsgmkpykdn
       61 ipnavhiaik vptaggktfi avnalnsink hfnkgnakav vwlvpwsnll qqtvknlsnp
      121 dhpyreklnt lfgnrvevye kdqllqganf nptsvteqln ifvfnfsslr insrkkddrk
      181 vyqengales frntivdkdl vipdtdetal invirslnpi vivdeshnae sdlsvemlnn
      241 lnpslvldlt atpkensnii syvnalalkk enmvklpvvv ynhhkkeevi tsalhlqrkl
      301 eliadeeekq tgkyirpiil fqaqsnikgk nnttfqkike klvalqipee qikiktsgid
      361 elkginlsak dckvryiitv nalkegwdcp nayilaslad kssaveveqi lgrvlrqpya
      421 vkhqnallnm sfvltasakf ndtlenivkg lqeagfskdd yyaeeqpeev ltpnevltqd
      481 lfeqkeskae etpasdedfn vseiqynpne evtlesieqd npllstitqk aeqqgkefdq
      541 kvneleiddt tsiftevmkt tppiykmied ysemanaikl pqffiekkdd lqsglfpeln
      601 eewqllhkna lldgfklsky ntevtfdeis kdiiavdfde vkgtaivkni kkrakdilid
      661 nilstpkesq inqvsgmvvs klgdmtpike qelkkyvnrv fdnltnkqir divendfiyv
      721 krirdkinal ssayakerfk vlidsnkitv rnnfefpdki tplnlstnin kslyeregkm
      781 nnyeqsmile vaaldnivfw hrnfergkgy alngyssnhy pdfilytkkg niilletkgd
      841 drvnedsrsk nilgktwekl agekfkyfmv fqsakventy tahsvievlk gl
//
LOCUS       WP_010521613             121 aa            linear   BCT 01-JAN-2025
DEFINITION  group III truncated hemoglobin [Aquimarina agarivorans].
ACCESSION   WP_010521613
VERSION     WP_010521613.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..121
                     /product="group III truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14098
     Region          3..120
                     /region_name="TrHb3_P"
                     /note="Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 3 (P); cd08916"
                     /db_xref="CDD:381257"
     Site            order(18,31,34..35,42,45..46,49..50,60,62..64,67..68,71,
                     77,81..82,85,109,112..113,116)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381257"
ORIGIN      
        1 mtdiqnradl eflfnsfyei amsdpkigyf ftevvainlq thlpiiidfw eynlfhkgsy
       61 tknlleihkn ihskatmdfs hfdhwlflln ktvdryfcgt isdklktnal siatvmktkv
      121 i
//
LOCUS       WP_010521742             359 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Aquimarina agarivorans].
ACCESSION   WP_010521742
VERSION     WP_010521742.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..359
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41267
     Region          1..286
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mkkilviqnk rigdvliasv iaqnikkvhp danvdflvyd fttgviqnnp yinhiiaine
       61 ketkqlpnlv klaftirkkn ydiifdpyak fqskficlls ganqriglvk pnkklpfkfy
      121 tdvvhlleek snvcgksied rvnmvsslfp iqknkidytp kifltekein ynkldgynqp
      181 fimlgvlgst pqksmpydyv talidfvtdt fqvnvlfnya phqkkealki yetcknksqi
      241 vidiyedtir gfiklmnkcs lligneggsi hiakalnkpt ftifspyvhk ehwasfedgv
      301 lhtsvhliee kphlfgddlg fesmrkiend pvamyreltp elmipklnlf lqrylkqik
//
LOCUS       WP_010521718             227 aa            linear   BCT 01-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Aquimarina
            agarivorans].
ACCESSION   WP_010521718
VERSION     WP_010521718.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..227
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=24225
     Region          21..222
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mlnslvqeva sdevsqektl siidllisgg vagmivigil fvllfvavyi yferlfaiks
       61 askydegfmg rikeyvslgn tdeakslcre tstpvsrlte kgisrigspl edintaiena
      121 grlevyklek nvsilatvag aapmigflgt vigmvlafhq latssgqadm gnlaegiyta
      181 mtttvagliv giiayigynh lvvktdkvvh qmeatavdfl dllnepv
//
LOCUS       WP_010521749             237 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Aquimarina agarivorans].
ACCESSION   WP_010521749
VERSION     WP_010521749.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..237
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27508
     Region          6..>87
                     /region_name="CE4_SF"
                     /note="Catalytic NodB homology domain of the carbohydrate
                     esterase 4 superfamily; cl15692"
                     /db_xref="CDD:472828"
     Region          60..217
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(66..67,128,132,168..170)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 maklpilmyh nvtlnksdak gltifkdtme shfnylkekg ystfhfkdlg epsfvlpkks
       61 viitfddvyk sqwviaypll qkyglkasff vpfkyvngkd dwstgkqeim disqlksfde
      121 svielglhsy ahkaypllnt neleldfeks lnfieensln vsnvlaypyg kfprkgnqnk
      181 efnailrqnn ikyalrignr insfpfknnf eiqrldikae dgltkfkrkl kwgsklf
//
LOCUS       WP_010521780             219 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Aquimarina agarivorans].
ACCESSION   WP_010521780
VERSION     WP_010521780.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..219
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24158
     Region          1..219
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mieaanihkh ygelevlkgv dlhikkgeii sivgasgagk ttllqilgsl dtmdknslsk
       61 ltingveint lkdkalakfr neqlgfifqf hqllpeftal envcipafik gvpkkkaetk
      121 akklldflgl shryhhkpda lsggeqqrva varalindpk viyadepsgn ldsesaenlh
      181 qlffslrdtf gqtfvivthn nkfadmadrk lvmrdgnli
//
LOCUS       WP_010521755             403 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Aquimarina agarivorans].
ACCESSION   WP_010521755
VERSION     WP_010521755.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..403
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=46134
     Region          <82..403
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mrlhrnlvfa vidtlteifn ehkyadkvvt ktlkrdkrwg ardrgfiaet tyeivrwkrl
       61 yaeiadikeh ysrenlfkvf cvwavlrgie lpdwkqftgt parrikgrfd elskdrrfke
      121 sipdwmdtlg tnelgeslwi keinalnkqa pvilrtntlk cetkklrsil aeheivcetv
      181 pnypealqlv eranvfstqa fkdglfevqd assqlvahyl evqpgmrivd tcagaggktl
      241 hiaaltknkg qiiamdiyen klkelkrrar ragahniepr vinstkdikk lankadrvli
      301 dapcsglgil rrnpdakwkl qpefiaaiqq tqqeilqsys rmvkpggklv yatcsilpse
      361 nqhqvekflk seagkefsfv kdqkilahqs gfdgfymalm ekk
//
LOCUS       WP_010521808             169 aa            linear   BCT 01-JAN-2025
DEFINITION  Dps family protein [Aquimarina agarivorans].
ACCESSION   WP_010521808
VERSION     WP_010521808.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..169
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=19577
     Region          1..155
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mnylnmnnek lipvvselni llaeyhmyyq klrnfhwnii gknffdlhek fedlygdart
       61 kideiaeril tlqyhpisky seylqiakiq esdslisdke mveillgdhg tllsqmrkvv
      121 knadeatdeg tidligayir eleksswmln awskstadtl ktmevnepa
//
LOCUS       WP_010521825             321 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Aquimarina agarivorans].
ACCESSION   WP_010521825
VERSION     WP_010521825.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..321
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35166
     Region          1..317
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mlkagvigag hlgkihlrll sesknyelvg fydsdeihaq qivkefgyty fdslsklida
       61 vdvvdivtpt fahfetakka iesgkhvfie kpitntiaea ealislaqkh nvkgqvghve
      121 rfnpaftaik nkinnpmfie thrlaefnpr gtdvpvvldl mihdidails vinsdvksvt
      181 asgvaviset pdianarief engcvanlta srislksmrk trffqkdayi svdffekkce
      241 vvkmkdapes sgefdmilqn aegvkkqiyf enpeiganna ildeldafae aihtnatpiv
      301 sleqataalk valavikdfs a
//
LOCUS       WP_010521863             554 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Aquimarina agarivorans].
ACCESSION   WP_010521863
VERSION     WP_010521863.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..554
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=62757
     Region          <200..>302
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          352..550
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msiktlilii insligfvvl ilsllfynqf skvlndrill qlnsiktlkq iqvenliqse
       61 wndflnvkki dtadldtnfk ipdsilsldg ihdltpyhke kqtsigfiqs tnegsivkii
      121 pyhklkkill ertgmgesge sylvgsdycl rsqsrffpdk npykvkvktk gvidalagnk
      181 grgvfkdyrg vnvysvyspl etsylelvil seidvdevtl plkklryrlf vltlgiliva
      241 vllsllltkm isnpvknmrk nlkimamgny nqsddfkkns ieikemfdal anlkdslrga
      301 vnfsnqignm nlnsnytpks sndqlgksli amrdkllefr tneqksrivt krllldglek
      361 erkrlsrelh dgigphltsl kfyvenniid pmkkiemkti vdstisevrl msnalmpssi
      421 ddfgvgatlt nfvrsienst kisiefedlt khskskitnh qginlfrisq elinnslkhs
      481 eakniritls efndfvslfy fddgigfkle taklgsgiin ikqrveicng tivinseqgr
      541 tttfeiefpi kndl
//
LOCUS       WP_010521875             614 aa            linear   BCT 01-JAN-2025
DEFINITION  T9SS type A sorting domain-containing protein [Aquimarina
            agarivorans].
ACCESSION   WP_010521875
VERSION     WP_010521875.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..614
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=67878
     Region          541..614
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 mkkilliltt fisvnifaqe lsfteernin lnkdynytiv dhtksgftid nennkiivgg
       61 fdglnvdfgn snlisaeeqf tayiakynqn nnllwlksig gstykdpshp lstiyystid
      121 fatdvkvdse dniyvlatid vattetvdld pehphtnsii stnnspgtfi renqniflik
      181 yskngeylwh neiqddfndi alkldidvnd nviftgying fssnfidfdp skthsddkdl
      241 iqselftvgf vvqydnngnf itvngigngi tsditvnalp sgdtyasgsf natisptntg
      301 yslfknspnp tyigslghye lgpenqdifv tkynntgqvl wvntisssse nrvveivtde
      361 nenvfvsgyi ngnsvdfdrn sisssdylsa tvggsafvak ynstdgslnw vklieggnfs
      421 kvrditiqnd kliiggefng dinigsskls tnvtnpfiai idtdgnwega gkiektifas
      481 isdvtiandg tinyfgfeae yinsintlnm qkmflgkvdn fivsptlsld epglkagffs
      541 ispnpasnyl niefrevkse idlkiynsfg qiifsqqysn tkketilins fskgiyiltt
      601 eengilsmvk iikk
//
LOCUS       WP_010521916             444 aa            linear   BCT 01-JAN-2025
DEFINITION  sialidase family protein [Aquimarina agarivorans].
ACCESSION   WP_010521916
VERSION     WP_010521916.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..444
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50006
     Region          58..338
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          99..151
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          163..211
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          226..263
                     /region_name="Sialidase propeller 4"
                     /note="Sialidase propeller 4 [structural motif]"
                     /db_xref="CDD:271234"
     Region          283..336
                     /region_name="Sialidase propeller 5"
                     /note="Sialidase propeller 5 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 minkilcslf vvtffgclpq knlkknkstt sdsftpknik iyeqtdrksl gpcepsicid
       61 ptnsnnivag svldyihtsn dggltwstkk qtsefgiwgd pvivankkge fyyfhlsdpe
      121 gtnwkseqil drivvqnstd kgatwstgtg iglnrpkqqd kqwacinpkn nhlyttwtef
      181 dkynssnpdn ksrilfssse dsgktwstpk nisvhegdck dddlttegav pssdgkniyv
      241 swafdhhiwf tkstnngksw snepikiaaq kagwrfkipv vnrtngfpvi dvdisdskyn
      301 gtiytnwsdq tdsnrtsiyi skstnqgktw stpkiidnki pnthhffnwm kidpatgfiy
      361 iiyyeqnpnn aplinvklav skngaksfkn ytisekpfhp kganffgdyn nidvqngiir
      421 piwtqvengl vsvwtaiiev snlr
//
LOCUS       WP_010521977             436 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Aquimarina agarivorans].
ACCESSION   WP_010521977
VERSION     WP_010521977.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..436
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49767
     Region          <186..427
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mtlelnylra lieyrldiyf npeseisepk ippinkwsie ipddlkklel ntdekavlll
       61 alvphidsgf ldsviqtklq stgdfpqlgg vrgknfrgfl ptgetalflv gginfeerke
      121 cyklfdtdhf fsksqllwld dapnnepkms gklvlsqdyv dlflfgkksk pnfsmkfpaq
      181 vietsmewed lvlseetnqq iqelktwith gntllrdwgm skkmkpgyrv lfhgppgtgk
      241 tltanllgky tgkevykidl smvvskfige teknlanlla kaektenilf fdeadalfgk
      301 rtnvrdahdk yanqevsyll qriegykglv ilssnlksni ddafvrrfqs iihfplpkla
      361 erfliwqkaf pkaiklekdv dmlqlaqkyd lsgaeiiniv qyaclctlgk nnktihlhdi
      421 vngiqreyqk ggrimr
//
LOCUS       WP_010522010             147 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Aquimarina agarivorans].
ACCESSION   WP_010522010
VERSION     WP_010522010.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..147
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16082
     Region          7..135
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mkvtlnrvne kfhfqvkner gymvdldkrk eqggddlgas pmelllmgva gcsgidligi
       61 lqkqrqeies yqmevegdrt pmgeakpftk ihatifikgk vapkkalkaa elsfekycsv
      121 sktleptatv tysvvvngek vttnggk
//
LOCUS       WP_010522031             737 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Aquimarina agarivorans].
ACCESSION   WP_010522031
VERSION     WP_010522031.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..737
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82758
     Region          36..737
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkyiflslat lvgsisayaq ttnqkeitnt kkdslngtil hevvisasre kqkrsevpaa
       61 isvisqkeln evkafgvdqi vndvpgvfvs sskasgneqh ftatrspist ralflyledg
      121 lplrptavfn hnallelnsi sykrvevlkg passiygsea vggsfnfltk dpskeltgsv
      181 qfqlndlgla nggfevskyl seklgfyagt qyternngpl gnsdyekfas tfkfvydfse
      241 kikwtnvydl idyrtdtsgs lsqedydnen fesdqtfter dafairfrst fetdwnsknk
      301 ttasfvyrdn rlaqipsfrv rqnrdrgqlt gtgsgrindn rfnsyvglvq hkikfdqlks
      361 sliigsavdf spqtyveent siivdpetgi nrsftinesd fvldyqadil nyagyvqfei
      421 npikslkits airydrfkyd fnnritensa nrindrqdqf rnfspkfgin ynplknlgiy
      481 gsysngftpp qtstlyrslg denrnlkptt fdnfeigvys spvsglrldl aayslegidt
      541 dvsfrdevtg vivntnaggt isrgieygvs fkihdftlsh ngsyaehkyk nfileetitn
      601 pdqsrtrsnr dvsnsireva pnwlgnskii ytphqikgls lsiihelvgd yntslegqvv
      661 nfnsegsivr stetysghni inglisykfk nveiwgqaln ifddlyavra sfntfrgent
      721 fslgnprafh vgvkynf
//
LOCUS       WP_010522138             199 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Aquimarina agarivorans].
ACCESSION   WP_010522138
VERSION     WP_010522138.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 199)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..199
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23399
     Region          69..193
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
ORIGIN      
        1 mykvfvnnsv iilsteswis dehikvnikk anmtkiinel lmypsikyhl yhkkedklfk
       61 ilhkklpvva agggkvynaq keilfihrng kwdlpkgkae knesisqtal reveeetgie
      121 nlilgdfirk tyhvyrrnnv fklkltywfe mysdfkgell pqedegitkv rwksfkkskk
      181 alentygaik elfpmeyfd
//
LOCUS       WP_010522237             130 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA thioesterase [Aquimarina agarivorans].
ACCESSION   WP_010522237
VERSION     WP_010522237.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..130
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14470
     Region          2..114
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mryhsrnivk pgdlnpygtl fggrllewid eeaglysviq lqssrvvtky mseinfvssa
       61 mpgdiveigl evvkfgnssl vlkcearnkm trqpiitven itmvnldeng iptphgktev
      121 ingsdrhyem
//
LOCUS       WP_010522244             294 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Aquimarina agarivorans].
ACCESSION   WP_010522244
VERSION     WP_010522244.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..294
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33870
     Region          39..101
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <203..287
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkqqisynkp sfehlapdig nsliykrfni enknkqpiwh yhpeielvyv negsgkrqig
       61 shvsyyqngd liciganlph cgftdgfskt rnetviqmlp eylgekffdv semlpiksll
      121 nrakqglvff gatkievgai ienmytkspf erildsllil hkleaskeye ilnaegftlk
      181 aqaqdnsrin ntfnyvqknf knqisieeis dfvnmtppaf crnfkkvtgk tftqfvneyr
      241 lvhatkllte kqesiqgicf ecgfnnfshf nkvfkkytgk tpteyrkdmn ftis
//
LOCUS       WP_010522261              85 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2061 domain-containing protein [Aquimarina agarivorans].
ACCESSION   WP_010522261
VERSION     WP_010522261.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..85
                     /product="DUF2061 domain-containing protein"
                     /calculated_mol_wt=9284
     Region          19..84
                     /region_name="COG3205"
                     /note="Uncharacterized membrane protein, DUF2061 family
                     [Function unknown]"
                     /db_xref="CDD:442438"
ORIGIN      
        1 mitekvagan ttyeqdvsse kpirsvvkai swrvvgtldt lvvsylvlge grlgeasaia
       61 gvdfvtkmil yfahervwnk vkwgk
//
LOCUS       WP_010522279             372 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Aquimarina agarivorans].
ACCESSION   WP_010522279
VERSION     WP_010522279.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..372
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43021
     Region          19..360
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mpkyiykynq wpdftwdekr ignilgkvry fqgkifgqms nlgfnlkeet ylstltldvl
       61 ksseiegefl nfnqvrssia qklgiessgl vhvgrdvegv vemmldatrn ydknltnerl
      121 fgwhaslfpt gysgmskidi gryrkdkmqv vsglmgkekv rfeapnhsei qnemdvllew
      181 inneneidlv iksaivhfwf iiihpfddgn griaraltdl llaksegsaf rfyslsnqil
      241 tekktyytil qkvqhssgdi tewlewflnc lhrslqstes tlqkvlhkan fweyhnetdl
      301 nsrqrkmlnq lldgfdgklk tskwakitkc stdtalrdik dliskgilkq eesggrstny
      361 ewaernnlkn ii
//
LOCUS       WP_010522284             175 aa            linear   BCT 01-JAN-2025
DEFINITION  shikimate kinase [Aquimarina agarivorans].
ACCESSION   WP_010522284
VERSION     WP_010522284.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..175
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19664
     Region          5..175
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 mhkniillgy mgcgkssvgk qlaimnqmny mdlddyieqk egmtineifs tkgevyfrki
       61 egnylneslv nlnnavlslg ggtpcfgtnm dtiiaadqnp svylqtsige lskrlftekd
      121 krpliahtkt vdeltefiak hvfersqyyl ksthkvvtds ktideivkei lelvn
//
LOCUS       WP_010522321             317 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Aquimarina agarivorans].
ACCESSION   WP_010522321
VERSION     WP_010522321.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..317
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36954
     Region          5..>109
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mnpntpffsi iiplfnkely ikktldsvfk qtvqdyeiii vndgstddsl klckeynvdn
       61 mliidqknqg apiarnngit kaagkyiafl daddfwhqnh lqefknsidl yenesifcnn
      121 yeinfsakkn kktsfsnfne nknqivfied yfknslyndi awtsavcvkk stllsgyyfd
      181 seiisghdtd lwirlalryn fvfnktvtai hnkyilnsls ktnhsdsrfk vtqkyliees
      241 khfflkkymd qnrfaialqy klngnskklt ilknqilsnn lnwkqtialq lptsllkyvl
      301 kaksilmrmn iylsifk
//
LOCUS       WP_010522368             143 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Aquimarina agarivorans].
ACCESSION   WP_010522368
VERSION     WP_010522368.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..143
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16339
     Region          1..143
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mkqllivsif ilgfinanaq kwitdldeak kiaaledkki vmvfmgsdwc ppckklnknv
       61 lsskefkaha drnyvmvkvd fpkktpnlls enqtaynlel skqynpkrkl priivmndka
      121 eilgktgykr mnpmayikll ssf
//
LOCUS       WP_010522352             127 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Aquimarina agarivorans].
ACCESSION   WP_010522352
VERSION     WP_010522352.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..127
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=15061
     Region          5..114
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 msaafkknts iyiqiaesic dklllnefke eekipsirdm avklevnpnt vqrsyewlqq
       61 heiiytkrgr gyfvmekatq kvmemkriqf veevlpdvfk nmellqidin qfeekysnyl
      121 nnktnen
//
LOCUS       WP_010522388             251 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Aquimarina agarivorans].
ACCESSION   WP_010522388
VERSION     WP_010522388.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..251
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29776
     Region          6..214
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mfeekkisvi tpsynserfi setiksvlmq syknweliiv ddcssdktie iikefannek
       61 rikffknkan lgaavtrnya ftrvtgeyia fldsddlwhp dklklqlefm kknnynfsft
      121 gykqinendl fikninnlpe kvnyentiks nkigcltvmi kvgffkeism pnlrkrqdfg
      181 lwlkllkecd yayclpeils syrvrrdsvs sdklslikfh welyrniekq svlkslyyls
      241 yhifnkvflr k
//
LOCUS       WP_010522441             276 aa            linear   BCT 01-JAN-2025
DEFINITION  M48 family metallopeptidase [Aquimarina agarivorans].
ACCESSION   WP_010522441
VERSION     WP_010522441.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..276
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29621
     Region          65..263
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(136..137,140,199,203,246)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(136,140,199,246)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mkfknqiila lssvlllgca tnpftgkktl alvsnsqifp mafqqydqfl senkvvkgts
       61 daemikrigq kiskaaerwf nanghpeyln gykweynlvd datvnawcmp ggkivfytgi
      121 lpiaaneagi aaimghevah alanhgqqrm sagqiqqvag vagsiamsgk saaaqqifaq
      181 afgigtqvgv mlpfsrshet eadkiginlm aiagynpeea aklwvrmksn saksgngapp
      241 emlsthpsnd trianltkwa pearseakkf gvttfk
//
LOCUS       WP_010522473              56 aa            linear   BCT 01-JAN-2025
DEFINITION  T9SS type A sorting domain-containing protein [Aquimarina
            agarivorans].
ACCESSION   WP_010522473
VERSION     WP_010522473.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 56)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..56
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..56
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=6164
     Region          <5..56
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 milenisvlg pngevieake lsrkrkridi sklssgkyii kimkkggtlv kqlikk
//
LOCUS       WP_010522480             287 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Aquimarina agarivorans].
ACCESSION   WP_010522480
VERSION     WP_010522480.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..287
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31101
     Region          3..261
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(9,11..14,34,58..60,86..89,109,136..138,151,155,185,
                     187..189)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(110,138,151,155)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(138..140,145,151,183..184,190,209,212,261)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mkknilitgt ssgvglaasi llaknnykvy atmrnlkkst vlkeaiakdn ldieileldv
       61 tkydtiehav nmivekdgki dvllnnagag faktleqtsl dqidwitdvn ykgvvittka
      121 vlpimrkmns ghiinitsig glvgqpfnel ycgakfaveg ftealatyva kpfninfsli
      181 epggiatefm nnaitktvde kgemvtgeya piftkylega ksragsgtas pyqtpeeiaa
      241 iildtinakn pplrvrtsew aenmtalkvk adpdgtklvn qvidyfl
//
LOCUS       WP_010521792             399 aa            linear   BCT 01-JAN-2025
DEFINITION  alanine dehydrogenase [Aquimarina agarivorans].
ACCESSION   WP_010521792
VERSION     WP_010521792.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Usha,V., Jayaraman,R., Toro,J.C., Hoffner,S.E. and Das,K.S.
  TITLE     Glycine and alanine dehydrogenase activities are catalyzed by the
            same protein in Mycobacterium smegmatis: upregulation of both
            activities under microaerophilic adaptation
  JOURNAL   Can J Microbiol 48 (1), 7-13 (2002)
   PUBMED   11888165
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Siranosian,K.J., Ireton,K. and Grossman,A.D.
  TITLE     Alanine dehydrogenase (ald) is required for normal sporulation in
            Bacillus subtilis
  JOURNAL   J Bacteriol 175 (21), 6789-6796 (1993)
   PUBMED   8226620
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..399
                     /product="alanine dehydrogenase"
                     /EC_number="1.4.1.1"
                     /GO_function="GO:0000286 - alanine dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0042853 - L-alanine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43252
     Region          29..399
                     /region_name="Ald"
                     /note="Alanine dehydrogenase (includes sporulation protein
                     SpoVN) [Amino acid transport and metabolism]; COG0686"
                     /db_xref="CDD:440450"
ORIGIN      
        1 messltpfss helipqvekl eienrkgdlf igipkesqpl enrvcltpda vnalvsnghk
       61 ilmeagagkl asfedkeyse agatitqdta kvfgcpiilk veppsldelk mikpqavlls
      121 alqlktldrq yfqtiekkki talafefikd ddgtypairs lseiagtasi liaseimsnv
      181 ndgsglmmgn itgvppvevi ilgagtvgef aaraalglga nikifdssin klrtiqnnig
      241 rpmhtstiqh khllkslkrc dvvigavrgk drspilvsea mtthmkkgav vidvsidmgg
      301 cfetsevtsh kkptftrngv ihycvpnips ryaktssvsi snifspylln igevggleha
      361 irndkglkng vysyhgvltn kavaewfdls yrdinllvf
//
LOCUS       WP_010522481             145 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Aquimarina agarivorans].
ACCESSION   WP_010522481
VERSION     WP_010522481.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..145
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16567
     Region          1..143
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mkklffslfi listasfaqd lkwetdftta kdlakdqnkn ilvyftgsdw capckqlkad
       61 ffhsekfiek adkvvllmvd mpfrqdiitp eqrkknekli kkynpgksfp tligldssgk
      121 llntisayss lrdttghfrf lesil
//
LOCUS       WP_010522493             372 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Aquimarina agarivorans].
ACCESSION   WP_010522493
VERSION     WP_010522493.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10136841
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..372
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43186
     Region          288..339
                     /region_name="NAT_SF"
                     /note="N-Acyltransferase superfamily: Various enzymes that
                     characteristically catalyze the transfer of an acyl group
                     to a substrate; cd04301"
                     /db_xref="CDD:173926"
     Site            order(307..309,319..320)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 mikiievask kqfldfvnfp ntlykdhpcy vpaitkeeln aikkeenpvy nnadaafyla
       61 ykndkivgri aaianwieik elnkpkvrfg wfdfiddinv tkalietvvt ygkkhnlsti
      121 egpvgfsnmd kagmltkgfd elntmitwyn apyysehlkq lgfeeaatwv efkidiptet
      181 rpkvvkvani iqtryklkii kfkknkeilp yvnrmfelln ktydslqtfv piqqyqidhy
      241 kkkylpfvnp dyitcvaneh neviafsiim psfskalqka ggklfpfgfl hilkaqrind
      301 taafyligvd peyqnkgvaa lifkemneif lrngikkvet npelienkai qalwkdyvhk
      361 qhkerktfrk ki
//
LOCUS       WP_010522515             230 aa            linear   BCT 01-JAN-2025
DEFINITION  SCO family protein [Aquimarina agarivorans].
ACCESSION   WP_010522515
VERSION     WP_010522515.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..230
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26653
     Region          74..225
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mlnnhiikil vivlscltsc kektekspik dqtntvkava kvkklpyfnt pdftptwapd
       61 hielkkihki pefsftnqlg ntvtnkdleg kiyianffft tcpnvciqlt nnmrkiqtiy
      121 anddeiklls htvwpsvdtv kvlkeygerq nvnpekwhll tgkkekiyel areayfaddl
      181 yketndpnrf ihtenlllvd knshirgvys gtkpeeikrl qrhinllkke
//
LOCUS       WP_010522524             303 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Aquimarina
            agarivorans].
ACCESSION   WP_010522524
VERSION     WP_010522524.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..303
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=34607
     Region          142..246
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mflaqvksfp rtefwryilg flvialfyfl gqapitfawl fklgltelqn tpqnelyfif
       61 dsnttlflml lmfvitlfgi ilvikkihkq tfktlvtsri ridwkrvlfa fsllaifigv
      121 ttfigykaap qdfewnfnlp kflglfiiav lllpiqtsve elifrgylmq gfaklsnsrl
      181 falaftsiif gamhlanpev relgyitmvf yigtglflgi itlmdegmel algfhaannl
      241 vtallvtsdw svlqtnsvlk disqpsvgle iltpvlvlyp iyllvfakry rwsnwkekli
      301 gkv
//
LOCUS       WP_010522567             251 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Aquimarina agarivorans].
ACCESSION   WP_010522567
VERSION     WP_010522567.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..251
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26816
     Region          6..250
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 melkdlvlil vgvvtgfint vagggsviil pvlilyfglp ptlangtnri gifiqtifsa
       61 wgfkskgvsp fvfgfkksil vgiialigav lgskialeip dalftkilsv vmigvliltl
      121 vkpkppqllk skprlayift liafffigiy ggfiqagtgl llilalsvln nmslvksnal
      181 ktivvfifti gtitvfaind qinykyglll gignaiggws asrwsvkkgd kaiqifmvia
      241 vilmaiklwv f
//
LOCUS       WP_010522606             202 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Aquimarina agarivorans].
ACCESSION   WP_010522606
VERSION     WP_010522606.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..202
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22144
     Region          4..197
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mafelpklpy aydalephid artmeihhsk hhngyttkln gaiegtdleg ktienilsnl
       61 dlenkavrnn gggfynhrlf wtvmsadggg kptgdladai nasfgsfeaf kesfkkaaat
      121 qfgsgwawlc vheggkveic atpnqdnplm pgvgcggtpi lgvdvwehay ylnyqnrrpd
      181 yleaffsvin wsevsalfaq nk
//
LOCUS       WP_010522610             264 aa            linear   BCT 01-JAN-2025
DEFINITION  undecaprenyl-diphosphate phosphatase [Aquimarina agarivorans].
ACCESSION   WP_010522610
VERSION     WP_010522610.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..264
                     /product="undecaprenyl-diphosphate phosphatase"
                     /EC_number="3.6.1.27"
                     /GO_function="GO:0050380 - undecaprenyl-diphosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28090
     Region          1..263
                     /region_name="UppP"
                     /note="Undecaprenyl pyrophosphate phosphatase [Lipid
                     transport and metabolism]; COG1968"
                     /db_xref="CDD:441571"
ORIGIN      
        1 mevfdaiilg iiqglteflp vsssghlelg kailgdttva eeslmftvvl hfataistli
       61 vfrkdiaeii ggllkfkwna etqfvakiml stipaviigl ffedeleqlf ggkvtfvgfm
      121 llitavllrl adkskntdkp vsyvnsmvig isqaiamlpg isrsgatiat svllgndksk
      181 aarfsflmvi plifgkigkd lldgaissqt gnnvalgagf vaalisgyfa ctwmialvkk
      241 sklsyfaiyc livgiiaitv gflh
//
LOCUS       WP_010522710             239 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Aquimarina agarivorans].
ACCESSION   WP_010522710
VERSION     WP_010522710.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..239
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26153
     Region          13..239
                     /region_name="carb_red_sniffer_like_SDR_c"
                     /note="carbonyl reductase sniffer-like, classical (c)
                     SDRs; cd05325"
                     /db_xref="CDD:187586"
     Site            order(17,19..22,42,66..67,93..96,116,141..143,161,165,
                     190..194,196,198..199)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187586"
     Site            order(67,73,110,115,118..120,123,126..127,145..151,159,
                     162..163,166..167,170..171,173..174,177..178,238..239)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187586"
     Site            order(117,143,161,165)
                     /site_type="active"
                     /db_xref="CDD:187586"
ORIGIN      
        1 mkisnrnpks qkvlitganr glgfgflmhy ltqgetviat crnddtlifd klkkdfpnql
       61 yienleltne qsiidfahki kenkvrfdlv innagvsiee nfgnwtlatf etnfkvntig
      121 palliqainp ylnqnakliq lssglgsval ninpegpyda yaaskaalni ltkklaskly
      181 trgiivtain pgwvqtdmgg pdatstidea ieqmtstint ltikdtgtfi sltgeilpw
//
LOCUS       WP_010522713             544 aa            linear   BCT 01-JAN-2025
DEFINITION  S41 family peptidase [Aquimarina agarivorans].
ACCESSION   WP_010522713
VERSION     WP_010522713.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..544
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=61476
     Region          35..391
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mkksfivils tlflglgfls fnrdsdgfel skqveifvtf ykklnqnyvd ktnpaelmni
       61 aikaitdemd pytkfwteqd viaskirssg qytgigagvf ekdkrlfvse pfknfpadks
      121 glkagdeiik iddivvsefe geakellkge agskvvltyk rqgktqitsv nrslvdvaav
      181 pyykllsdnt ayivlqkfnk kasaetiaal kelkargadk vildlrgnpg gllveavnvc
      241 nifipknklv vytesvikss nkvyktkkep idteiplvvl vngrsasase ivsgvmqdmd
      301 rgvvigarsf gkglvqtyrp lvyntklkvt ssryyipskr ciqaldywhk dkngkpkrik
      361 nsdykafktl nskrtvydgg gvspdvevea tkrsglatal ikekaifdfa tdyyhknsyk
      421 slsefkfkds dfqdfknylk sinfeyetkt eksldeamty aikekmdksi nseyqsllkr
      481 idafkqsslk tqekeikgll ideilkryfy regmyeyntl ksdeiitaqa vlkdearynk
      541 ilgk
//
LOCUS       WP_010522717             556 aa            linear   BCT 01-JAN-2025
DEFINITION  S8 family peptidase [Aquimarina agarivorans].
ACCESSION   WP_010522717
VERSION     WP_010522717.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..556
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=61991
     Region          83..517
                     /region_name="Peptidases_S8_Subtilisin_Novo-like"
                     /note="Peptidase S8 family domain in Subtilisin_Novo-like
                     proteins; cd07483"
                     /db_xref="CDD:173809"
     Site            order(91,314,484)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173809"
     Site            order(287,314,318,375..377,404,406..407,484)
                     /site_type="active"
                     /db_xref="CDD:173809"
ORIGIN      
        1 mkrifkiapv tfsaslllts cfstnptiin tpaekvdnlp lkttaitqeq lknwnqsdll
       61 ldtipgmsvd raysdllakr kgktvivavi dsgidinhed lkgkiwvnkk erpnngkddd
      121 kngyvddvng wnflgdvvae nmeftriird ykdkfegktl asisekdkem fqtyeaakte
      181 yaqkvdqnnq rmaqyeplak nlksahtyat kkfatdkytq kdlfawkpta deaiqhrqll
      241 vgmypnveeg kffgdfvtdi eeyveyfker qqthfnlnly prkilnndpd nfetriygnn
      301 kvggpdpkle daehgthvag iiaanrknti gmkgiaenvk impvravpdg deydkdiama
      361 iryavdngak vintsfgkyf sthpdwvrda iryaakkdvl ivnaagnesk dldvttvypn
      421 dqtltgaeis dnfitigaln ydygtrlvad fsnygkqnvd vfapgvkiys tvpnskyefl
      481 qgtsmaapav sgaaavlrsy fpnltakqvk tilmesgnas ktnvvvgsgi gksfqetsks
      541 gkmvnlynai llaqry
//
LOCUS       WP_010522742             129 aa            linear   BCT 01-JAN-2025
DEFINITION  HIT family protein [Aquimarina agarivorans].
ACCESSION   WP_010522742
VERSION     WP_010522742.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..129
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14376
     Region          1..127
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 masiftkiin geipsykite denfyafldi npntkghtlc ipkkevdqlf dldeatykgl
       61 fdfsrkvaka lektvtckrv glsviglevp hvhvhlipln emkdatfshk tsvtdsemqk
      121 landiashl
//
LOCUS       WP_010522820             201 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Aquimarina agarivorans].
ACCESSION   WP_010522820
VERSION     WP_010522820.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..201
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23198
     Region          <1..186
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mynpffkrit dfvlsligfl mlspviiiii mvllfvnkgk pfffqqrpgk ngkpfniikf
       61 ktmtdidskd dqkvhnlsrv tksgafirky sldevlqlvn vlkgdmslvg prpllmeylp
      121 lyndiqskrh nirpgitgwa qvkgrnsisw skkfeydvwy vdnvsflldf eillltvkkv
      181 fikegvnsde nitmevwkgn v
//
LOCUS       WP_010522797             293 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Aquimarina agarivorans].
ACCESSION   WP_010522797
VERSION     WP_010522797.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..293
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31903
     Region          4..217
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mnnkvfvtga tgfqgmsiak slinagdkvi tlsrsldskn qtfegidvit gsleneadvs
       61 kamknankav ftcplvfdla lakkyvenfi kaaeenhiel vvynssfdlp eeetglisld
      121 ikvlisdlfk ksalkvinlv pdiyldnasa pwsvpvivtn kifpypvesg kklpwishsd
      181 lgnftasain kpelagktls iggnlvsgqe iadaiseqlg eqisfvsitp dafqkeltpa
      241 fgelagkeis nlyryietns nkivnknfke tqqllghtnq slsdwaksid wkv
//
LOCUS       WP_010522986             340 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Aquimarina agarivorans].
ACCESSION   WP_010522986
VERSION     WP_010522986.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..340
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37153
     Region          <3..340
                     /region_name="trifunc_aldol"
                     /note="KHG/KDPG aldolase/sugar kinase fusion protein;
                     NF041633"
                     /db_xref="CDD:469516"
ORIGIN      
        1 mhkiitfgei lgrfsppnnl rfsqatsfev iygggefnva aslanygana efvtaipvna
       61 igdcamntir sfgvghkhil rqgkrlglyf lengasgrns avvydrddsa isqikkgdid
      121 wdvvlngatw fhwsgitpal senaaevcle gikaahakgl tistdlnyrk klwnygktpk
      181 evmpellsys nvilgdvdta lfmlgkekld pdytvdleak kvfakvfell pnlqtmamty
      241 rnslnashqi iggllynkge myrarlneit pvvdrvgtgd afmggliysl teytndleka
      301 iafatgacvi khtifgdvnr askeevlnfi ssdgsakvdr
//
LOCUS       WP_010523056             146 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Aquimarina agarivorans].
ACCESSION   WP_010523056
VERSION     WP_010523056.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..146
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16921
     Region          8..138
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mgaysdfake llnkhhlkat ttriklieii ktfktaipyt kiqehfkdsd ritlyrtiqt
       61 llkkeiihka linkeetyya lyendtkdqt hshnhvhfkc tvcnhvscqy lydkisvtlp
      121 nftidtmqiq ltgicnlcts kgnqqn
//
LOCUS       WP_010523182             396 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Aquimarina
            agarivorans].
ACCESSION   WP_010523182
VERSION     WP_010523182.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..396
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43210
     Region          5..396
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(100..102,126,176,208,236,238..239,247)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(103,136,201,245..247,276,279)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            239
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 msnqlserin slapsatlem aakarelraa gkdiiglslg epdfntpdyi kdaaiqavnd
       61 dynsytpvdg ygelkdaiit kfkrdnnlsf eapqivvstg akqalynvaq vclnkgdevi
      121 lpcpywvsys divkladgvp vevttsidnd fkmtpeqlea aitpktkmlw ysspcnpsgs
      181 iyskkelral advlknhpqi vvvsdeiyeh inygvtahas maefedmydr tvtvngvaka
      241 famtgwrigy igapayiara cnklqgqvts ganciaqrav italaepvsr iqymvdkfke
      301 rrklilslln diegfkcnep egafyvypdv taffgktldg kkinnasefa iylleaanva
      361 tvtgdafgng ncirisyaas eaqiieaikr ikeavs
//
LOCUS       WP_010523310             286 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Aquimarina
            agarivorans].
ACCESSION   WP_010523310
VERSION     WP_010523310.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..286
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31649
     Region          22..286
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 miqmmpfsnf slfgyeiske tidklvvstm sylpkivaal lilvlglwvi kfinkvirkf
       61 farkdyditl ekfiadlinw glkvmlfimv itqlgvqsss llailgaagl aiglalqgsl
      121 snfaggvlil lfkpfkvgdf ieaqgqmgtv ksisifttil ntpgnqqaii pngklsndti
      181 knfnaeptrr nfmtigvsyd sdikkakdil ldivtsheft lkepapevvv anlgdssvdl
      241 slrfsaentn ywklnfyvle eakarleand isipfpqrdi hvynqa
//
LOCUS       WP_010523347             176 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Aquimarina
            agarivorans].
ACCESSION   WP_010523347
VERSION     WP_010523347.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..176
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18891
     Region          31..173
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mskliipkkg evstanqaif dnlekavgfv pniyaamahs englgnylqy sggktslsnk
       61 ekevvdlavs qvngcqycla ahtamgkmng fndteikdfr qgtaenskyn alaklaqsia
      121 inrgkatdae vdsfyeagyt kenlvdlvla vgiisttnff hnltdvaidf pvaqei
//
LOCUS       WP_010523324             105 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Aquimarina agarivorans].
ACCESSION   WP_010523324
VERSION     WP_010523324.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..105
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=12057
     Region          3..98
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mrqdidqdew iellendena vildvrtdge ieegyianmk qidflegqnf leevakldks
       61 knyyiycrsg nrsgqacdim eqlgfdttyn leggfmnwtg dived
//
LOCUS       WP_010523336             148 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Aquimarina agarivorans].
ACCESSION   WP_010523336
VERSION     WP_010523336.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..148
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17152
     Region          15..147
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mlditiksfe tltkaelyai lrirsevfvv eqliayqdld qkdqkamhii gridseivay
       61 trifkpndyf kyasigrvlv akkyrrfnyg rdivkasisa ieaqygetti kisaqlylkr
      121 fytelgfesy gdvyledeip htamlkqn
//
LOCUS       WP_010523406             408 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpP1/FadL family transporter [Aquimarina agarivorans].
ACCESSION   WP_010523406
VERSION     WP_010523406.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..408
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44712
     Region          4..407
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mkkllfsial glitlntyag gyrvslqgqr alamghtgvg vvdsaelaff npaglvylen
       61 klnisggvtl isstakyqns ltgetaetdn sistpfnlyi sygindwlsv alaaytpygs
      121 tvewekdwag sdlvnsislq siyinpvisv klneyfsigg gpiyatgnvn fnrnlqrapg
      181 gtanrpniev daegvdnwgw vfstmfrpse hvaigatyrs kidlnaeggd vtytnidlpe
      241 tqfnatlplp aeltfggsvq vskklllaae fnrtywstyk sldldftnpe atdsrntrny
      301 qnsniyriga qydasekfiv ragyyfdetp lqsgfyapet prndshgftt gfsynvtskl
      361 aidasflyly fseidesyds dpndtverfs gtyksnaiia glgltykl
//
LOCUS       WP_010523475             387 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide pyruvyl transferase family protein [Aquimarina
            agarivorans].
ACCESSION   WP_010523475
VERSION     WP_010523475.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10514996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..387
                     /product="polysaccharide pyruvyl transferase family
                     protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44695
     Region          15..316
                     /region_name="PS_pyruv_trans"
                     /note="Polysaccharide pyruvyl transferase; pfam04230"
                     /db_xref="CDD:427804"
ORIGIN      
        1 mskkigivti lsvnnygael qafalqnkln slgyhaeiin ylfyknpdfk atkksksfvk
       61 lgfkqqmker lyphykkiks lpyhkqklkr drkfenfhve htnrtavint idklyaktfd
      121 ydvymvgsdq vwnpnthvnl epyfltfape dklkiayass fgvseippiy eghyqnllen
      181 ldhigvrekq gvsivenlvs kpakwvldpt fllsnkewss fesastikep yllmyiltda
      241 eyitnlarhi akvknlkivr icknafvedk ssdviniida gpkeylglfk kasfvlttsf
      301 hgtcfsvnfn ipffvvlkrn ktnnsrqinl lkeleirnri lyvgeefpqa enfdfnfsks
      361 nllltefvtn sieylktsin tlkngvr
//
LOCUS       WP_010523520             152 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA (cytidine(34)-2'-O)-methyltransferase [Aquimarina
            agarivorans].
ACCESSION   WP_010523520
VERSION     WP_010523520.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..152
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=17047
     Region          1..151
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 minivlihpe ipnntgnigr lcvgtnchlh lvhplgfeit dknlkrsgld ywpelqvtey
       61 knfeawkaqi kdasrvflft snteksflap kykegdwlvf greskglepe ilalynnhvs
      121 ipstgkvrsf nianavsfai gealkqingf qf
//
LOCUS       WP_010523523             291 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Aquimarina agarivorans].
ACCESSION   WP_010523523
VERSION     WP_010523523.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..291
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34261
     Region          116..271
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mlqvfktftt aslntinwvw ncitfsvpwy snyfwglvli sllvwgieil fpwrknqaif
       61 rkdfwldafy mffnffvfai iingfykvie sgfanlgihi nslsvipisn wplglqllvf
      121 fvildffqwf thtllhkyhf lwkfhkvhhs vkemgfaahl ryhwmenily kplktfavml
      181 lggfepeqay ivhfiaiaig hfnhanikit wgplkyvlnn pvmhlyhhay klpkgtygvn
      241 fgislslwdy ifktnyipen sgtieigfkg dhkfpksftd qaaygifkrs k
//
LOCUS       WP_010523561             247 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Nesterenkonia sp. F].
ACCESSION   WP_010523561
VERSION     WP_010523561.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..247
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26576
     Region          17..209
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 msidsalply ddsqlsrvlc vaahpddley gtsaavarwt argvhvsyll ltageagmrs
       61 rdpeeagplr aaeqrracal vgvddllild lpdgtlqadt etrrhisrri revrpdlvvt
      121 qpwelhvpwg lnhadhrtag iatldavrda dnpwvfrell eqehlepwaa telmvvgaep
      181 athlidvgga pleqgiasle aheeylaelg gavdvrsmle sstadvaaas dvdglthalg
      241 atvhrma
//
LOCUS       WP_010523551             119 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase, partial [Nesterenkonia sp. F].
ACCESSION   WP_010523551
VERSION     WP_010523551.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..>119
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
     Region          65..>119
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 mstmpedsvp sehddgadrl tlesgltvrp waegddlall evwgdpenal qhqdrallrp
       61 ssddpwarci vaedhgvpva aatilrsslh pdrlsfyaev addhrrrgia aemlellaa
//
LOCUS       WP_010523563             280 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Nesterenkonia sp. F].
ACCESSION   WP_010523563
VERSION     WP_010523563.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..280
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=31125
     Region          27..242
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mdiehvtasp arrtdppagp tetprtvlwv sahpepeslt gnlrrhglev lrrrghtvle
       61 sdlhaldwdp vvraetldtr patrplqitr qgrsaqlagt qppdvvaeqe klrradalvv
      121 qfplwwygmp ailkgwfdrv fvsgfafgkd patgrrlrfe qgpfrgtral aaitlgdrpa
      181 sigprgksge leellfgllh gtfaytgmda lrpwalpsad ftdegswpda agslagrler
      241 lfdeepipyr eqftgdyted walreeirpg etglsvhlhr
//
LOCUS       WP_010523597             220 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Nesterenkonia sp. F].
ACCESSION   WP_010523597
VERSION     WP_010523597.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..220
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24197
     Region          6..220
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mdrtedaepr getaqraera aavlrariaa geippgaklp evqlcdelev srhtlrsalq
       61 tlgaeglaer rpnvgvfvha ptledlaeiy rvrrvveiga vrqaafdapa leelaalveh
      121 aqqraaaddv aavaeanqrf hrrlvaqags eqlstfmeri larmrlvfhv mrgeptfhve
      181 faagnaelvr llraddrdga erhmesyfdh aeqllgarls
//
LOCUS       WP_010523598             428 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Nesterenkonia sp. F].
ACCESSION   WP_010523598
VERSION     WP_010523598.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10150691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..428
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42853
     Region          38..377
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 msrtdasaag gttqtssrpa sslseapgsp appspsprrl lvgffaasvs lvlifvgagt
       61 piplfptyrl edgltnadla aaaatymvaa afsllvlgrl sdhfgrrpva vvalvlaagg
      121 mgalltvdge aplllgrglq glatgiatsa lgayvidsap rrppwlaavv tsaapmlgip
      181 tgallsgalv dhgpdprhlt ygvvlvglla aglavalspe ttartslrra aaslrpritv
      241 prgagrplla msalilatws vggfyqsfgp sittdhlgst salvaaavfs sftmlnmigg
      301 pltarlrpvl glrlgaaayv lvlagilasl aagaivpfvv lslvagitqg aaqtggmrtl
      361 lpmtspgera glvstiylvn yssaaipsli agrltehlsl vtiglgygvl allavtaalv
      421 lsrsprqg
//
LOCUS       WP_010523637             577 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Nesterenkonia sp. F].
ACCESSION   WP_010523637
VERSION     WP_010523637.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..577
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=62042
     Region          32..546
                     /region_name="YdbT"
                     /note="Uncharacterized membrane protein YdbT, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3428"
                     /db_xref="CDD:442654"
ORIGIN      
        1 msqhpeyper vepaeeqpad espaegeqwf dstwtrvhpl spvvrgwlal vaipfvalts
       61 nwetitdlwe alrsgeltea agrhpmitla viggilllil lifggfalsw wftrykitdd
      121 hvmvksgifv rqhrqaridr vqavdlrqpl larltglael kfevaegdgt aatlafltrs
      181 aaeqmrteim drasgrtaar drsagsageq sddaeqpgdg gqsgdgapdg paapasgsar
      241 atppelpeae drqivqvptg rligsvltgg ltvallvvvl ltglasgvgl tifvlsggdl
      301 addpgarlga slsgislasl palipaaigl lagyyqqfss gfrftatmta aglklrygll
      361 etttqtvppg rvqaiqiqrp llwrpfgwar imvvvagyga gekrsvllpv gtredvlavv
      421 aemfpdlqva dpaalidegl tgidedgaft agpraarwld pivrrrrggt vtpaallard
      481 grlgrrltlv pheriqslsi qqgpvqrlag latlrlhspa gpfqaqltnq rladvhgffe
      541 hesrqaavar rirdreqwmm peelhefekm mrqgsap
//
LOCUS       WP_010523698             217 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Nesterenkonia
            sp. F].
ACCESSION   WP_010523698
VERSION     WP_010523698.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..217
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23563
     Region          15..200
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mrligagtre gfdytvrrtf wtvpnivtvl rfllvpvfiq lalteelvaa fvvlvvlggt
       61 dwidgwiarr fdqhstvgrw ldpladrlsv aivavtlvav diaplwfvls ilvpdavlai
      121 naavlfagsp elavtalgkv rtavlmvgap lvllaraevl agtewtpiae svlaagclmh
      181 ilaavdylrr ahrqarrlra qgidprdrsr wvageqt
//
LOCUS       WP_010523710             297 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Nesterenkonia sp. F].
ACCESSION   WP_010523710
VERSION     WP_010523710.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..297
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30876
     Region          83..287
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 migqkrprpa esaeaaaprt rtpragrdlp aailtgaall ipavlgivfm plllillavv
       61 llamgaweva valetqglrl pkiplflgal tmplaayfgg vealtlalmv tcaaiaviaa
      121 iyrihdagrs imasmfvacw vpflisfavl lidqpmgqwr lavvvllvva ndtfgylvgv
      181 lfgkhpmapt ispkkswegf agsmlgsiav gvlasalifd eplsigavla aavvvvstag
      241 dfsesmvkre lglkdmshvl pghggvmdrl dslvfampta yfvivalspq sagiplg
//
LOCUS       WP_010523724             355 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Nesterenkonia sp. F].
ACCESSION   WP_010523724
VERSION     WP_010523724.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..355
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36365
     Region          1..355
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mqkltvgivg ggfmgrvhsh aaraagaevv gvtssspers aaaagqlgta avddvaelve
       61 qvdvvhvcsp naahaghvra aldagrhvvc ekplaldaae adelaaraea agvvaavpfv
      121 yrfhpmarqa aahvaagelg rlltvrgsyl qdwmldpeag nwrvdpatag rsrafgdvgs
      181 hladllefls gdrivrlaaa ttiahprrgg vdvttedaaa ltvqlrsgav gslmvsqvda
      241 grknaltlel agtetsvvfd qehpdelwig gveasrtvtr dapalaadaa rlnlvpaghp
      301 mgyldaftaf ardvyaavgg etphglpsfa dgaranavid avvasaehgg wvdld
//
LOCUS       WP_010523547             131 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA-binding S4 domain-containing protein [Nesterenkonia sp. F].
ACCESSION   WP_010523547
VERSION     WP_010523547.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Novel predicted RNA-binding domains associated with the translation
            machinery
  JOURNAL   J Mol Evol 48 (3), 291-302 (1999)
   PUBMED   10093218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594118
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..131
                     /product="RNA-binding S4 domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=14079
     Region          57..116
                     /region_name="S4_2"
                     /note="S4 domain; pfam13275"
                     /db_xref="CDD:433078"
     Site            order(65,77..78,80..81,83..84,87..88,90,97..104,106)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
ORIGIN      
        1 mseehqderh dhpqdeavee taaaaageqi daeaddaadd avdedfdeae fievdqipir
       61 desirlgqll kladvvehgg marevldaga vtvddevetr rgrqirpgei vqldgealgl
      121 peaaitpvae e
//
LOCUS       WP_010523744             538 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Nesterenkonia sp. F].
ACCESSION   WP_010523744
VERSION     WP_010523744.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..538
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57578
     Region          9..534
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mpspttlgvt dltvrrpdgv pildgltftl gpgrhglvgd ngagkstlla vlagklapss
       61 ggvhvagetg llpqdpaadp rltvagllgv eqtvtalaai ergsvrpadf davgddwdva
      121 erveamldrv gladlaldrp atslsggelv ltslvglllr rpsvllldep tntldararq
      181 rlvavldefp gvlvvvshdr gllarvdsvg elrggrlgwy ggnlehyeqa vaveqraaeq
      241 aastaraevr rrrrelvdqq tkqarrdrrg rgraenqapi iahaekrraq etagrltavh
      301 rdrleearqf ageaerrvrd gaeiridlpd trvparrevl raeglasahg avpldlmlrg
      361 pervaltgpn gvgktsllrc lageerpvgg tgeilvphqm lpqnptpsdp grsvleavra
      421 aaptadpari rhqlalflfr geevhqpvgt lsggeqrrar larllladpa pqllildept
      481 ddldfagvrh lvqalrahqg allvvshded fleqlaldrr llltregvee rggddaas
//
LOCUS       WP_010523746             292 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Nesterenkonia sp. F].
ACCESSION   WP_010523746
VERSION     WP_010523746.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..292
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31629
     Region          95..291
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mstttngtst vppeterirh ilvsrqdtpq rpgavsaslt ygwrallkik hvpeqlfdvt
       61 ifpimmtvmm tyvfggsiga avsgqeaggd avdayvqwli pgifaqtlvm itmytgltln
      121 rdiskgvfdr frslpvwrpa qlvgallgdq vrytlagvii lvvgfimgfr pagglpgvla
      181 aflmllvfsf clswvwttva llmrteqaam gvsmfimmpl tfvsnifapt esmpgpvraf
      241 aeanpvstlv gcirqfmdgv ydvgsitavl iycavlvvif gpismfvynr ts
//
LOCUS       WP_010523764             312 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Nesterenkonia sp. F].
ACCESSION   WP_010523764
VERSION     WP_010523764.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..312
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33850
     Region          51..309
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mpgetpavyq prdastlgde aprrdpaeen sgrrrrleyp papeplavpv idnhahldfr
       61 dgqvavsvve aldaaasvgv againvgydv dssefsvraa rqdgrlkaav alhpndapel
      121 aavgqyddal ariaelagde evvavgetgl dyfrtgeegr aaqrrsfadh lqlaaerglp
      181 vqihdrdahd dvvavlkdap rlpevvvfhc fsgdaelari csehgwymsf agtvtfknae
      241 plregldvad pelilvetdt pfltphphrg rpnapylipq tmrlmaerrg veldalcrqv
      301 mdntvrayga wl
//
LOCUS       WP_010523770             354 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Nesterenkonia sp. F].
ACCESSION   WP_010523770
VERSION     WP_010523770.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..354
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38019
     Region          11..330
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mmsttttqdn avvldgitkr fgpttvlddl slhisagelv svlgpsgcgk ttamrilagf
       61 ekpttgrvlv sgkdltavap nrrdigmvfq ayslfpnlsv rqnveyglrv rrvrrearrr
      121 taeellemcg lpqladryph qlsggqqqrv alaralavqp svllldepls aldaivrhqi
      181 reeirrlqqq lgittmfvth dqeealaiad rvavlnggvi eqvdeprtiy rrpatefvaq
      241 fvgtvtrlga dpsftrgalp vqgpahgldt lfvrpedltl spaaegtctv vsqtftgert
      301 ivrasgdegp elissvsaae aadlvpgtrv iphvldepal rlpaaasaae rvpa
//
LOCUS       WP_010523829             275 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Nesterenkonia sp. F].
ACCESSION   WP_010523829
VERSION     WP_010523829.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..275
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29935
     Region          8..269
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mehlplnsgp sipqigfgtg gtpdaaerva aalqagyrhl dtaqrygnea gvgagirtsg
       61 vpredlfitt klddfhhapa dvdrtldesl arldldavdl flvhwpmprl evsyvdtwra
      121 mlaaresgra ravgvsnfqq dhleriieat gevpavdqie vhpsfandml rafcrehgim
      181 vtawsplgkg ddladpavva laeqlgrspa qvilrwhler gdviipkssr pegmaanldi
      241 ldwqldeedv aaldaldrge agrrtphpde ielrg
//
LOCUS       WP_010523813             524 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Nesterenkonia sp. F].
ACCESSION   WP_010523813
VERSION     WP_010523813.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..524
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57201
     Region          24..522
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mtenttfdyv vvgggsagaa vaarlsedse vsvalleagp tdadkdvvlr lnrwmelles
       61 gydwdypiep qengnsfmrh arakvlggcs shnsciafwa pkedldewes mgaagwnaea
      121 typiyqrlet ndaegdhhgr tgpvnlmtip phdpcgvsll daceqagipr vqfntgetvv
      181 kganffqvnr kedgtrssss vsylhpildr enlsiltdtw vkeilfdgdr avglsavgga
      241 fgkahtitan reivlsagai dspkllmlsg igpaehlaeh giasrvdsrg vgehlqdhpe
      301 avigwdakkp mieegyqwwe igifadtkeg ngesdkpgrp dlmmhygavp fdmhtlrqgy
      361 ptsentfclt pnithaksrg tvrlqsrdyr dkphvdpryf tdaeghdmrv avegiklare
      421 ivsqpamaew ageelypgkd vvtdeqiady vsrthntvyh pagtvrmgaa dddmspldpe
      481 lrvkgvsslr vadasvmpel ttvnpnittm migercadli katr
//
LOCUS       WP_010523844             378 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Nesterenkonia sp. F].
ACCESSION   WP_010523844
VERSION     WP_010523844.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..378
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39483
     Region          13..349
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(33,35,66,108,235,299,323,325..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(33,35,66,108,110,117,183,186,188,235,242,299,323,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(35,110,183,186,188,326)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mttpvdeqta aqklfsparl gaveldnrlv mapltrirag edgvpteamv syyaqraslg
       61 mivtegtfpv gegrtwigqp gietsaqiag wrkvadavha aggtivmqlm hggrighplv
      121 sttgrvtaps alaapgqirt pegkdehpvp halttdevge tieqfvagar naiaagmdgv
      181 qihgangyll heftapstnt rtdpyggspe nrarlsvdva aavsaaigad rtgirlspqh
      241 niqgaleeda ddalatyral aeglaplgla hvdvlhaepa gelvqairrv sgaplvantg
      301 fsvqttreea itlvaddvae avgvgrsaia npdlarrwel daeenapvpe tfyvggergy
      361 tdyptleeta etaetlqn
//
LOCUS       WP_010523903             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Nesterenkonia sp. F].
ACCESSION   WP_010523903
VERSION     WP_010523903.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..247
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24979
     Region          1..239
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mgtiflfeim gtatlillga gvvanvvlsg tkgngggwll infgwglgvf cgvyvayatg
       61 ahinpavtvg llasgaeeya pgiavnlpnt layfaaelig aflgavaawl aykkhyddet
      121 dpaailgtfs tgpekrslgw ntvtevigty vlvllvlmlg etpaelgpla valvvlaiga
      181 slggptgyai npardlgpri ahailpirhk gssdwsyawv piagpvigai lagasvqvfp
      241 llgagaa
//
LOCUS       WP_010523904             602 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Nesterenkonia sp. F].
ACCESSION   WP_010523904
VERSION     WP_010523904.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..602
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=65037
     Region          47..561
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 mkaeplnpea rtraldefag tmegepldvl vvgggvvgaa aafdaatrgl rvglveaqdl
       61 gqgtssrssk lvhgglrylq mldfklvaea lrerdlllkr taphlvrslp fvfpfstplv
      121 drafigsgvs lydamslrpg ekravpfhkh lsrsrlrrrf agldhdtfvg aleyfdaqvd
      181 darlvmtlar saqglgaava trtavesyih dadaavgagt gespvvgarl rdletgrrld
      241 vraketiiaa gvwteqqqda aeadaglkvl askgihitvp kdrivaedhv gvisqteksv
      301 lflipqedcw aigttdtawh envdvpapns tdidyvleha nailqtdltr ediigtwagl
      361 rpllqpeqkg dgggsakvsr ehtvkriapg ltavaggklt tyrvmaedav dfaaqdrfsh
      421 resltevmpl lggqgygewa graeeiaaer gldvervrrl lrrygsllgd vlapaeeqsd
      481 lleplehapg ylraeiryaa eqegavhled llerrtrivh evrdrglgam devialvagp
      541 lgwdeerqeh errswtsrve allaaeksgs daeaaallad tipatqtawg swgaaestgr
      601 ad
//
LOCUS       WP_010523926             309 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Nesterenkonia sp. F].
ACCESSION   WP_010523926
VERSION     WP_010523926.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..309
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=33201
     Region          35..292
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msqhdqhdqh dggrdagqhd epatprldaa sfttlriteg edrlharldr pevrnaidat
       61 midelhalca hlehapkili lsgspstgpg adddadpgar prrgvfasga digqlrdrrr
      121 edalrgvnst afdrlsklpm pviaaldght lgggaelawa adfrlgtptl rvgqpetglg
      181 iipaagalwr lrdlageala keillagril daeealahgl iseihpsqel ldaadalagr
      241 iaaqdplavr iskqvfampr eahpqvdnla qailfeseak vermqafldr rearkksqhq
      301 drttsgdqs
//
LOCUS       WP_010523935             369 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Nesterenkonia sp. F].
ACCESSION   WP_010523935
VERSION     WP_010523935.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..369
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37673
     Region          9..270
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgepvsrvrp lrigmvgagt isgqylqtva rledlqltav adldaaraea vaaehgaaae
       61 evdglmgrgd vdvvlnltvp qshaevssaa iaagkgvyte kpfaadvaag revlaqgrgs
      121 gavvggapdt vlgtgvqtar aaldagvigt ptsatatlil pgheswhphp dfyyqpgggp
      181 lmdmgpyylt alvtllgpvr evvgaasalr dervigsgpr ageripvatp shvtgalvha
      241 dgvistvvms fdgaatraap ievqgtegal svpdpnrfsg rvalsrdggg whevpvsagy
      301 rhaargygla dlhwagafdg dplrgraqge lglhvlevme gllasaesrr avgmdttver
      361 papvpmdhr
//
LOCUS       WP_010523955             549 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Nesterenkonia sp. F].
ACCESSION   WP_010523955
VERSION     WP_010523955.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..549
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58846
     Region          29..547
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtssprsdsg agprarsatd gaeeldldtt agklaafrrr rdqtlapage aavekqherg
       61 khtareriem lldpdsfvel dalavhrsts fgmekrkplg dglvsgygtv dgrlvavyaq
      121 dftvfggsls qvngekivkv qefaarngcp vigindggga riqegvasla mfadifrnnv
      181 hssgvvpqis limgpaagga ayspalndfv imvdqtshmf itgpdviksv tgedvdmetl
      241 ggarshnett gtasylaade edaleftkel leflplnnla eapvepheer vkieaedeal
      301 ntlvpdsanq pydmravieq tlddghflel qalrapnvli glgrvegrtv gvvanqpsql
      361 agtldidase kaarfvrfcd afnipiltfv dvpgflpgtd qefngiirrg akllyayaea
      421 tvpkitvitr kafggayivm gskklgadvn lawptaqigv mgasgavnil hrrelasvgk
      481 eggdvearra elvdeyekel ltpyqaaelg yidaviepae trwqitqalr atfhkrealp
      541 akkhgnipl
//
LOCUS       WP_010523962             291 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Nesterenkonia sp. F].
ACCESSION   WP_010523962
VERSION     WP_010523962.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..291
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=30419
     Region          36..283
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mtearellav aaeaaaagaa vlaeredvap sgrvlrsdes glgtkssesd lvtdfdrrse
       61 qavravigrr rpqdaitgee ygtstperas girwsidpld gttnfvrgiv yygtsvavqg
      121 pdgdwlagvv hapaldrlww asrgagaftg rasaarpgad dagqtgvdrl tgpqgtraag
      181 llstgfgyda arreqqvsav vellnsfgnl rrlgaaaldi cmvadgtvea yaeygiqehd
      241 waagaliaee agvtmrrpla adgaahpdwc iagdlgvphe qlrpapretr p
//
LOCUS       WP_010523979             311 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Nesterenkonia sp.
            F].
ACCESSION   WP_010523979
VERSION     WP_010523979.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..311
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=32833
     Region          211..291
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mfqpcgiraa psgsaftrdp apttaetrrp sryadrrgsq dspadaapaa pldagtrrll
       61 iielvlvlal slgrsavyav lelaerlsrg plgeqtatvq tsqsrlevfd aayqvldsvf
      121 alapaalalf llhlhhaggs pnpfrrigld lrrpgrdaas glglfgliga gtllvyltgr
      181 slgitaelvp advaahwwtp aalllaalrh glveeiimvg wfldrcrrla phtspwvlvv
      241 lsavirgayh lyqgigpgig nllmglifga lylrtgrvmp lviahvllda vaflafplvl
      301 ratglgavls g
//
LOCUS       WP_010523998             467 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Nesterenkonia sp. F].
ACCESSION   WP_010523998
VERSION     WP_010523998.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..467
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48877
     Region          16..429
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mewmllgvgl llilgtaffv avefslvald qptvqravdr gdpgaralls clrslstqls
       61 tcqlgitvtt lltgyvvepa lgellaspla algvpdaaag pvslivamll atlvsmllge
      121 lvpknlaiae aerlgralag pqlvvtavak plvlllngfs nlvlhrfgle vkeelsgart
      181 peelssmvrr saklgtmdad tatvldrtlr faeqtaadam tprprmaave aeapltelig
      241 marrtgysrf pvlgesvdev rgvthvkkav avprdkregl vaatvmsevt rvpetlslda
      301 llpvlreasl qmavvvdeyg gtagvvtled lieeivgeva dehdriapgv lqsaagdwff
      361 pgllrpdein aqivglavpd gaayetvagf ivdalgrlaa vgdevpvagg tlrvvvvdgr
      421 ridrvrfipd aearraalaa qaeraeragr teladagpah raggggr
//
LOCUS       WP_010524039             311 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Nesterenkonia sp. F].
ACCESSION   WP_010524039
VERSION     WP_010524039.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..311
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30686
     Region          27..242
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mslpplvlal aavvgvllgl lggggtilav plltyvagmp tkeamaastv ivgvtaalsl
       61 aapsrrgtva wrtgalfgaa tmagafggga lgarlpdtll mvlfavlmaa aglamlrrrs
      121 tqrtrptpga vavlgqglgv glltgmvgag ggflivpalv mlgglsmpia vstsllviam
      181 ksltgmagyl ttvsidwptt llvtaamvag sligssiarr vpasalkrsf gvlvlamslv
      241 vltvelpglw glgagflvav agvalgswsn tgsergddde gsrpgspaqd repaqagpra
      301 arlgdqrsgg r
//
LOCUS       WP_010524050             261 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Nesterenkonia sp. F].
ACCESSION   WP_010524050
VERSION     WP_010524050.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..261
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28649
     Region          22..252
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 medprseatt aeagagahrl vdgpspkhvq lsralarmar rdlapgemip serrlmadyg
       61 vsratvrrav dglivdgllr rvpakgtyva pprleshlhl asftqdmrrr glhptttlvs
      121 lerrepspev aeslgiadde pvwemtrvrr adgrpialet gwypvvvfpg ldeqdltgsl
      181 yevfstvygv tiesaeqtvw gevadrpaar hldggeatpl lvfrrvsrad grpveytvsr
      241 yrgdryqvhm slggdssatr g
//
LOCUS       WP_010524065             334 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase, partial [Nesterenkonia sp. F].
ACCESSION   WP_010524065
VERSION     WP_010524065.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         <1..334
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          <229..333
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 aavqarvdel tapepeqess nsssseepss sdsestssaa sgpslsqylp gtrslvnela
       61 ellgkssert fdqlisqeky teggvldhaa iqarvdelta pepepeepss sssdsessss
      121 gssgpslsqy lpgtrglvte laelqdrgvq atferiladd alvgsngvid haalqrkvds
      181 ltqsenstss tgssgsstsg sstaassasd agaaatavsw avdkvttpgv hyvlggegpw
      241 aydcsslvqq afaqggvsvp rtanqqfqgg rsvslsnlqp gdlvfwtsgg rahhvaiyig
      301 ngklaharnp qagvgitdly yayqdpnpva kryf
//
LOCUS       WP_010524117             726 aa            linear   BCT 01-JAN-2025
DEFINITION  BCCT family transporter [Nesterenkonia sp. F].
ACCESSION   WP_010524117
VERSION     WP_010524117.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..726
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79141
     Region          84..596
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 madrqppntr peggrdpaqd paqdpahdaa qspergredr srsrrateat rragqalgri
       61 spysrgdyph dihpalvpgl aideqrrryr vdkvvfliag altvafviwg ivspasvstv
      121 sgaaftwtme nlgwlfnvva iavlvflliv afsrygripl gkdgeeaeys tfawvamlfa
      181 aglgiavlff gpfepmdhyq hpapltaape tpealhrgma qvfyhwgfha wamyalvgga
      241 vayaayrrgr vllmssifrs lfgrrqsegf agqlvdifai iatlfgtaaa lgiaamqigq
      301 gvtiitgvde ltntalvvvi cvltigfvls avsgvsrgir ylssinivlt valvglvfil
      361 gpslfllnll pasimeyfns mfemmgrsas wgqetldyqs aqtvyywaww iswspfvgif
      421 iarisrgrsi rqfilgtili pstlifiayg imggtsiwmy regmegfsdd maaptvffti
      481 venlpaldwl plliivvlai ffitstdsas vvmgmlttrg dqkprawvvv fwglvmtgia
      541 vvmlllgdat alqglqslvi vtavpfaiim llimvawfre lgtdpralrt kygekalrda
      601 vidgvdrygd dftlqvvpta pgfgagsdvd sedamytewy qrtdendepv gydfttgewe
      661 dgwtpeddde whgdvenysp atslatapvp vvsedgtiqd paqaadgpeg pesgresqpg
      721 sepapr
//
LOCUS       WP_010524130             189 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein, partial [Nesterenkonia
            sp. F].
ACCESSION   WP_010524130
VERSION     WP_010524130.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..>189
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
     Region          1..>187
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mfgglhafpl tpmpddvlde paliglierl aaagvdaitv lgstgsyayl taaerarvve
       61 lavahagttp viagvgalrt sqvlrhlada eaagasgvll apmayqplas revlglyrtv
      121 taatdlpvmv ydnpttthve fslelygeia alpgtaaiki ppvplepeqa rqrvaavraa
      181 ipehvevgi
//
LOCUS       WP_010524141             744 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin domain-containing protein [Nesterenkonia sp. F].
ACCESSION   WP_010524141
VERSION     WP_010524141.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442502
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..744
                     /product="thioredoxin domain-containing protein"
                     /calculated_mol_wt=78456
     Region          1..738
                     /region_name="YyaL"
                     /note="Uncharacterized conserved protein YyaL, SSP411
                     family, contains thoiredoxin and six-hairpin
                     glycosidase-like domains [General function prediction
                     only]; COG1331"
                     /db_xref="CDD:440942"
ORIGIN      
        1 mghrlaesss rylrqhadnp vdwhpwgega faearrrdvp vfvsigysac hwchvmaaes
       61 fsdaqiaetl ndgfvaikvd reehpdvdda ymaatqaltg qggwpmsvft dpsgrvfhag
      121 tyfpprrrgq ipsfaevlda vraawtrrrd eveasaaqia aalgdqrrrq aqlatapaee
      181 lgaphpehdg vpgtgilaqa gdvvaqaiqa llaeedtvhg gfspapkfpp spllglllee
      241 aardpespag ppairvmeam grsalhdqie ggfaryatdr awalphfekm ladnaqllgh
      301 yarlsvhpaa teatraeaer vgrgvvdwlh rrmlldsgll assldadtvd asgrhqeggt
      361 ylmsdrdlra aaraaglgdd daarlvaldr gvpadeagta ahvtedtprt vhfdaplsge
      421 drrvweavlp vlrrrraara qpardekava awnamavrsl aeaavcwade dlleragrlg
      481 erlwdvhvdd gtgdvgpgla agdadagpvv rrvshagrad aalgtltdha qmisacftla
      541 svgagdaqrw ldrgrrllat lrrrfvvede egrpalvesa dggamltaal qgpalatpfd
      601 gpepggvaaa adalqqaeal vatadgdglp dedalraadi lhhaptaapr apmvvgsslq
      661 vlrrvavgsp afrilsatae dlaavrraav lhgpaveppa egaigpgrpl rlsvclnave
      721 amvclppest vaaalgrlge rppg
//
LOCUS       WP_010524137             228 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Nesterenkonia sp.
            F].
ACCESSION   WP_010524137
VERSION     WP_010524137.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..228
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23946
     Region          30..216
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mrntpartpe gdggdswgal ardarshllr talpvlipva vmwvmllvrl vtgnwltlsl
       61 slearelsgl igivtmplvh ggvrhlignt vawlllggli alldrrfpli llliwllsga
      121 vlwvigtpwv cqapgsldca ghhigasgvt ygfgtfliay gvltrrivav lvavlvllvh
      181 gvsmlfgmlp ftagtgvswt ahlsgaiagv avaflmtrta raaraara
//
LOCUS       WP_010524167             476 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar porter family MFS transporter [Nesterenkonia sp. F].
ACCESSION   WP_010524167
VERSION     WP_010524167.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..476
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50336
     Region          17..458
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(29,147,150,154,277..278,282..283,286..287,383,
                     387..388,392,415..416,419)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 msinsrsqdl aatsvawvvl vaafggflfg fdtavingav saiqsafgls dwligfavss
       61 allgcmvgaw vggslsdrlg rvgamliaas affvsaigsg lavgpvdlia wrllggvgvg
      121 masviapayi aevaptnlrg rlgslwqlai vvgifaaavs nafvanlagg sdaelwlgmd
      181 awrwmfviea apaliyglla tsipespryl vsrgddrraa qvlrevvgls eesqvrekia
      241 eisrtinhes rqkirdlvvg gkimpilwvg lglaifqqfv ginvifyysn tlwqavglte
      301 dqsfliqvit tsvnilatvi gilivdkvgr rmplavgsag mavglgmmav afsqavtvdg
      361 elelpgawgm ialvsanvfv lffgatwgpf mwvllgemfp nriraialgv saaanwlanf
      421 vistifpama dlslvfaygf yavsavlsli fvikwvpetk greledmseg ayerah
//
LOCUS       WP_010524207             310 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Nesterenkonia sp. F].
ACCESSION   WP_010524207
VERSION     WP_010524207.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 310)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..310
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34617
     Region          40..306
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mairtrhrae paqdpavahd qvrldgspli rvgarpplgr ylaqiwhfrh fiifdshsrv
       61 qtantseslg rvwlvmnpil nglayflifg lllntsrgvp nfigyliigv fmfryittsv
      121 ssgatsiask qsvvqafnfp raciplavnv relfqsvpmf lvmavlvttm gdipledaea
      181 spvvlswkwl vffpalaltl mlttglgmll aravsahtdv khlitfgtri wfyasavffs
      241 vsrfadtpli idlmhlnpaf ctldiirqaw vydewadpmr wvvlggwavg alvigfivfw
      301 qgeetygrdr
//
LOCUS       WP_010524228             401 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Nesterenkonia sp.
            F].
ACCESSION   WP_010524228
VERSION     WP_010524228.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..401
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42235
     Region          5..401
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(104..106,130,180,211,239,241..242,250)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(107,140,204,248..250,279,282)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            242
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mtaptsrvsr rigsiaesat lavdakakam kaagegvvgf gagepdfptp dyiveaavda
       61 arnprfhrys paaglpelre avaektards glpveaqqvl itnggkqavy ntfatlldpg
      121 devlvpapyw ttypeaikla dgvpvevfag peqgyqvtve qleaavtert kvlvfvspsn
      181 ptgavqspqa teeigrwaae kglwvvtdei yehltydgvp ftsiasvdel adqvvvlngv
      241 aktyamtgwr vgwmvgpadv ikaasnlqsh atsnvanvsq maalaaitgp ldsveemkva
      301 fdrrrramve glnaisgfsc ptpqgafyay vdvrgalgre iggttpqtsa elaevileqa
      361 kvavvpgeaf gpggflrlsy algdedlarg lerirellgs a
//
LOCUS       WP_010524239              64 aa            linear   BCT 01-JAN-2025
DEFINITION  YidH family protein, partial [Nesterenkonia sp. F].
ACCESSION   WP_010524239
VERSION     WP_010524239.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..>64
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
     Region          4..>57
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 mtsarrfpqs vyrhgdepda rftlanertf lawirtalal maagvaleal gagmhtglrl
       61 aaal
//
LOCUS       WP_010524278             402 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Nesterenkonia sp. F].
ACCESSION   WP_010524278
VERSION     WP_010524278.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..402
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=44138
     Region          94..352
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 madrehdgap rrhrprrvrv vsptaptpsa rgerprrgrr vlgwslvava tlvvvavavv
       61 gvylqdlrss fdenrnvlem nldddtaart dddvvnllll gsdtrgegqd laeikgedgq
      121 rsdtmmfvhi padrstvyvm sivrdlwvdi pgvgtnrint ainsggyplv vdtveelldt
      181 hidhaaiidf egfkdlteal dgvyvdnpqa fssgqhnpdf ypegtirleg analryvrer
      241 ktfsdgdftr venqrrvvqa iidrflsaet ltnparvsdi vesmvpylwl degldadtva
      301 gyavqlrnlr sddiemftip agepmttsgg aqvitrdeaa mdvlrrslde esmddfvddl
      361 aeseanpfdt aetdsetdpe tgtetesgsg tetgdeagev fp
//
LOCUS       WP_010524306             498 aa            linear   BCT 01-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Nesterenkonia sp.
            F].
ACCESSION   WP_010524306
VERSION     WP_010524306.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..498
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=51069
     Region          1..480
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 msavaeglga ladptvllci lvgalagmlv gafpgitatm svalasaftl tmdpipglav
       61 lltiyvaanf gdrvpailvn tpgtpasist tfdgypmakq gkagialtts afsaafgtfg
      121 gllvlifaai plsrmalnfg paemfalvvf gltmvvgvsg snllkglaaa afglvlstvg
      181 rdpitgaerm tfgvlelsdg lpfiaviigl fgiadvfdqm lthhagtata iknlgrwmpn
      241 rserrrmrkp aligtgigav vgalpaaggd iagitswsas rrlsktpeey grgsveglta
      301 gdsasnatlg psvsttlalg vpgdsvmavv igslviwgfn pgpglfasqp dlvytiagim
      361 alatvltlvl sllrmrgvsk llelpphylw tvvivfclvg tfavnnsvvd vavmlvagvv
      421 glfmrrlgfp aapvvlglil gelaeanlrr aleiggvsei ltspialafl vvavasvtlp
      481 palrrlrrsr rrdrrpvs
//
LOCUS       WP_010524313             228 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Nesterenkonia sp. F].
ACCESSION   WP_010524313
VERSION     WP_010524313.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..228
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23696
     Region          39..>170
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mslvaasalh lgdpalfeqw giwyfavlvv avavtalvpp fpselmvias gtmaseglmg
       61 lplvltttml gcllgdvgvh llfrrqglrv lhrwrwgrrl hrmllrvtlr aggattwigl
      121 lliraipggr ttsmitagml rlsgprtval alvgaatwsa wlvglgyitg tttglppwas
      181 tvtaaaagtl vgalaagvaa rrrrarsrra agrnatsavg tsptdvgs
//
LOCUS       WP_010524396             215 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Nesterenkonia sp. F].
ACCESSION   WP_010524396
VERSION     WP_010524396.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..215
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22568
     Region          8..205
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 msgeqltvgv lgagrvgtav grqavraght vkiatsrpae enrlltevvv pgataadpqd
       61 fadadlviva vplnkyrsid tsvlqgkvvv damnywvgvd gfiaefdgtr stsevvgefl
      121 gdvrlvktln higygeleve akpagaedrr algvasddae akalvsrfvd slgfdvvdag
      181 elaagrafen gseiftgrht aaqmrevler esarv
//
LOCUS       WP_010524366             183 aa            linear   BCT 01-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Nesterenkonia
            sp. F].
ACCESSION   WP_010524366
VERSION     WP_010524366.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10053807
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..183
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19326
     Region          99..>163
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 msdedrlral eqrvqaleda rgtgsaapdd agaaaaeppp epaaeagprd dtfwaleglr
       61 hradpdrgav lwagvvpadg gtwewqmarp adelrspddp qhaadrlaal shpirlslll
      121 evldgttrlt dlaerlglgs tgqlyhhtra ltaagwlrpg erghvavpge rvvpllvilg
      181 asa
//
LOCUS       WP_010524440             382 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Nesterenkonia sp. F].
ACCESSION   WP_010524440
VERSION     WP_010524440.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..382
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41344
     Region          23..342
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msaasstirv gvvgaggiaa gahlptlksh egrvevvgla dvdpdrvarv adewgipgrh
       61 ggidelleae rpdllvlctp psahregvmk glragawvwc ekppmltlae ydevaalere
      121 ggpyasyvfq hrfgsgaqrl krhvqegtlg rplvalcntl wyrphsyydv awrgkweteg
      181 ggpamghgih qmdllleilg dwtevsataa aldrdveted vsaatvrlas galatvvnsv
      241 lsprevsylr fdfqdatvev ehlygydnss wtwtpaphvg eevpadwtpe edvpsshrrq
      301 lgelldamaa gvrprasgdd grrvlefiaa lyqsaetgrp vrraeltrsg tyyagmhdaa
      361 hdyrvadnta gvvptpaeep ar
//
LOCUS       WP_010524489             339 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease, partial [Nesterenkonia sp.
            F].
ACCESSION   WP_010524489
VERSION     WP_010524489.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..>339
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          26..234
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 msattdashr artgrpahar ltpatrtgls iavavslygl sfgalstaag mtfwqtvals
       61 allfsggsqf afigilsggg apaaalgast llsarntlyg vqmkalldpr gvrrlfaaql
      121 tidetaatam sqstdaerrr gfwvtgvacy tgwnlataag allgdvvgep ealgldgavv
      181 aaflallwpr lrgaepwala vvaalvtalt mpalpagapv llaavvaivw glaapptrrr
      241 rpgrgsdrgp grgsdrgagr rcdrggppmt lwlwvlaasa avyatklvgh lipgswlrhp
      301 lvgrisglmt vallaalvtm nsvdgddgvv vdarlgala
//
LOCUS       WP_010524499             532 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Nesterenkonia sp. F].
ACCESSION   WP_010524499
VERSION     WP_010524499.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..532
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58143
     Region          4..527
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 misvsklelr vgarllmddv sfridagdki glvgrngagk ttmtkilagd gmpaeghier
       61 rgsigylpqd prvenmeqla rdrilaargl deviatmrrt eeemtseddv vrdramrrys
      121 tleaeftaag gysaeaeaat icanldlper illqpletls ggqrrrvela rilfsgadtl
      181 lldeptnhld qdsivwlrdf lqqypggfiv ishdvelmer tvnkvlylda nrstvdvynm
      241 gwknylaqre qdearrrrey anaekkatal raqadkmrak atkavaaqnm lkradrmmsg
      301 legerqaeki anirfptpas cgktpltaeg lsksygslei ftgvdlaidr gsrvvvlgyn
      361 gagkttllrm lagvgepdsg vvraghglkl gyfaqehdtl dpqrsvlanm ktaapeltdt
      421 qqrtilgsfl fsgddvekpa dvlsggektr lalatlvasg anvllldept nnldpasree
      481 ilnalhnyeg avvlvshdeg avealaperv vllpdgiedl yteeyedlvt la
//
LOCUS       WP_010524500             252 aa            linear   BCT 01-JAN-2025
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Nesterenkonia sp. F].
ACCESSION   WP_010524500
VERSION     WP_010524500.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..252
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26746
     Region          46..246
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mpvehaarpg qstgepearq sagrrrrtih vdgagldvea adgarrrvla pvhaelteev
       61 iavvgangsg kstllrliag lvepslgevr fsptpprtgf ifadptaqli mpivgediaf
      121 slrgrirnrs argaesrril aslgledreq asvhdlssge rqkvalagvl aaepelvvad
      181 epttlldlra saefrdrlls lgvplvlath dldfaaaadr vlvfdggrlv dddepaaaip
      241 ryrrlalgdr ad
//
LOCUS       WP_010524570             100 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Nesterenkonia sp. F].
ACCESSION   WP_010524570
VERSION     WP_010524570.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..100
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10659
     Region          6..92
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mtfanvgtig vqpghrddvv ailsrhnpql aaagclsyev gvdeeqpdtv fvaelwtsrq
       61 ahddslqles vkeaiaeamp mltgdmgghr fevvgsplrd
//
LOCUS       WP_010524577             500 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Nesterenkonia sp. F].
ACCESSION   WP_010524577
VERSION     WP_010524577.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..500
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=52401
     Region          26..439
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 msdgplvpil llvlaalcal aavvlstaes afmrlsrrea eeiaqkhgss avarilddpv
       61 ahtvalqlwr wlgaaiavll vtlaavrltg gplagglaag gmlvlggigl atlsprrvgr
      121 qhhllvatht arlvrglrtv lgpvprllit tgtrlvpgtg gpdqgffdde elrdavvras
      181 egdviedaea eliqsvfdls etrvravmvp rpdmvsvsat atlgevlsif lrsgysrapv
      241 iegsadavtg miylkdvafl ehrlhagepp aafaerapeg vvaaevqraa rfvpesqrvs
      301 allpelqres thvavvvdey ggtaglvtle dlieeivgdi vdeydveaae veelgdgrrr
      361 lsarmsvddf aelhgldldd eedvdtvggl lakalgqvpi vgseaeiqgv lvradglsgr
      421 rnrvshvlta papsrqeret merpsdagfg adagaedrgg pagppahrgp gptaaaptrp
      481 aptssrstse rfpdralrga
//
LOCUS       WP_010524620             210 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Nesterenkonia sp. F].
ACCESSION   WP_010524620
VERSION     WP_010524620.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..210
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21726
     Region          1..>89
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mslirtlarp mlgagfivhg vdrlrntpea aealeptlee vgslvpqaep vtahpqrttq
       61 vlggvevvag aalavgkfpr laaltlagvh kldsyvefrt akaesadgaa vrtgllknlg
      121 ilgglglavv dldgrpslsw raehlaksak gspfsdkthr iaeqtggdav ktlkayqkaa
      181 akglknaere arqavaavae eakkkteaas
//
LOCUS       WP_010524626             311 aa            linear   BCT 01-JAN-2025
DEFINITION  ACP S-malonyltransferase [Nesterenkonia sp. F].
ACCESSION   WP_010524626
VERSION     WP_010524626.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Marcella,A.M. and Barb,A.W.
  TITLE     Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as
            templates for engineering
  JOURNAL   Appl Microbiol Biotechnol 102 (15), 6333-6341 (2018)
   PUBMED   29858956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..311
                     /product="ACP S-malonyltransferase"
                     /EC_number="2.3.1.39"
                     /GO_function="GO:0004314 - [acyl-carrier-protein]
                     S-malonyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31849
     Region          1..304
                     /region_name="FabD"
                     /note="Malonyl CoA-acyl carrier protein transacylase
                     [Lipid transport and metabolism]; COG0331"
                     /db_xref="CDD:440100"
ORIGIN      
        1 mlaivcpgqg sqtpgflspw ieddsaratl trfsdaagtd llthgtesda etirdtavaq
       61 plivaaslls aralglgagp agasreqlll aghsvgevpa aalagaltee qamrlirvra
      121 sgmaeasaat ptsmaavvgg veqevrqaia dhgltaanan gpgqivaagt qgaiaaleae
      181 ppqrarvipl pvagafhteh madarrrlde avasfetsdp tlpllsnrdg edvadgtevl
      241 rrlvdqvtrp vrwdlcmetm aargitgile llpggtltgl akrglkgvps favktpedld
      301 darafiaeha a
//
LOCUS       WP_010524666             312 aa            linear   BCT 01-JAN-2025
DEFINITION  SURF1 family protein [Nesterenkonia sp. F].
ACCESSION   WP_010524666
VERSION     WP_010524666.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..312
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=33746
     Region          23..273
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mlktalqprw latlalalil atvfvvlsaw qfgrsqiddd atgadpatag ssleealqdp
       61 tpltevirpg epmggpqadr vvslrgefve gtevlidqrl qgdregywav aafavdgapd
      121 gqvipvvrgw vadpddadaa psdeeltvvg rllpteapea eprpdgrvlp slsvaelinr
      181 wdvssysgfv vafsaqpaga adptgesdga evdaaaegsp lesvwvgpqp egpqihwlnv
      241 fygvewtvfa gfafylwgrl vkddherrle eerldrewee qwrreqlarr aeqsgrpagd
      301 agsdgpeeqt hd
//
LOCUS       WP_010524671             298 aa            linear   BCT 01-JAN-2025
DEFINITION  stage II sporulation protein M [Nesterenkonia sp. F].
ACCESSION   WP_010524671
VERSION     WP_010524671.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003460
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..298
                     /product="stage II sporulation protein M"
                     /GO_process="GO:0030435 - sporulation resulting in
                     formation of a cellular spore [Evidence IEA]"
                     /GO_process="GO:0042173 - regulation of sporulation
                     resulting in formation of a cellular spore [Evidence IEA]"
                     /GO_process="GO:1901893 - positive regulation of cell
                     septum assembly [Evidence IEA]"
                     /calculated_mol_wt=31546
     Region          17..277
                     /region_name="SpoIIM"
                     /note="Stage II sporulation protein SpoIIM, component of
                     the engulfment complex [Cell cycle control, cell division,
                     chromosome partitioning]; COG1300"
                     /db_xref="CDD:440911"
ORIGIN      
        1 msccgstsap pptcrwsrpi dpggpvaagl sarlgrarsr ltgggdnllv siarfvmqvl
       61 paafhrvavp tvvigalfll vsgafalwtq hhpqiellms dearaayard dfvdyysdhp
      121 nasfaaqvwt nnawiaaqev algvtgvwvp avllvnaqgl gisagvmfeq geawtfwahi
      181 lphglmelta vfvagaaglr ifwawvapgr rrrltalaee grrlitvaig ltavllvsgv
      241 vegfvtpsdl ptavkillga lvlagywtyt lvlggrarra gitgdlaryd tgvhelta
//
LOCUS       WP_010524704             109 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Nesterenkonia sp. F].
ACCESSION   WP_010524704
VERSION     WP_010524704.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..109
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12249
     Region          2..91
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mifivvkfpv kpehaeewpe ivrefteatr aepgnkwfdw srsledpney vlveafddda
       61 aeahvtsdhf qkataeggpm hqalaatpki isrpiqgedw eamgelqvd
//
LOCUS       WP_010524755             172 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Nesterenkonia sp.
            F].
ACCESSION   WP_010524755
VERSION     WP_010524755.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..172
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=17935
     Region          36..170
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mpessvqdag raeasapltr dgrpqdaaea pagervvhar lsaepldvaa ahaevwasta
       61 gavvdfagiv rdhdggtave rlsytahpda ermlaetara vaedhpgvrl waahrtgplv
      121 igdhalvaaa aaahrqeafa acaalverik aevpiwkeqf fadgtrewvg ig
//
LOCUS       WP_010524777             122 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Nesterenkonia sp. F].
ACCESSION   WP_010524777
VERSION     WP_010524777.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..122
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13547
     Region          21..108
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 msddhttgts dsastsddqe tvrrhgeksr fevhvgeela gfsmykelpd ddqrifyhte
       61 ifdafggrgl astltrsale tsaaegwriv pvcpyvkkwl eshhevddav davrpahlea
      121 lr
//
LOCUS       WP_010524779             253 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Nesterenkonia sp. F].
ACCESSION   WP_010524779
VERSION     WP_010524779.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..253
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=27236
     Region          27..224
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mtstdhdtqt agrrsaaata pdfshlratf fnctlkpspe vshtealvea sarlmrdhgv
       61 sveiirpvdh diapgvqpdm tqhgwqtdew pqlhrtvmas dilvlagpiw lgdnssvmrr
      121 vierlysnsg dlndagqssy ygrvggalft gnedgikhca mnvlyslqhl gctippqada
      181 gwvgeagpgp syadpgsggp endfttrntt fmtynlmhla amlraaggip sygndrrawd
      241 agtgaehvnp eyr
//
LOCUS       WP_010524783             259 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Nesterenkonia sp. F].
ACCESSION   WP_010524783
VERSION     WP_010524783.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..259
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27317
     Region          14..215
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 msishiigeg atmriavaga tgtagvptva larerghhvv evsrsagvdl ltgerlttal
       61 agvdvaidas nprlpdpead lvevyaqats rlieacrsag vehlvylsis aihdpafdef
      121 pyylakraqe qvihdsgfpa tiiattqwhe famnpaavtt gdyevtvqdw liqpiavaav
      181 aealhdaahs rlprrslagp etlrlpeltq rylaargddr pvrtvetamp alaegallap
      241 egaeligpsv egwlagqaq
//
LOCUS       WP_010524891             372 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Nesterenkonia
            sp. F].
ACCESSION   WP_010524891
VERSION     WP_010524891.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..372
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37509
     Region          191..368
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 msaihapvps pvagrpapsr asaadvvltl lvvvsgplll vlgavlmsga etsaarllrp
       61 epstlqvwga aleeqrqalt vgdlqaveel igllcvalgv llgllaalsv aatallqlsr
      121 rvgvrrgtal lellspgfmr ralvvalgaq mavmgtvagv sssvtsqttm ptataaqddq
      181 drdaggetpd aedaeagstt aadselvadr ledspdplfa papsadedeg ssaddaadda
      241 staeadapsd gssdsssega sgrsseesdg tggpttprpa gsqrtaspep gdrltggqvr
      301 taadeadhvv vrsgdtlwsi aaehlgdeas daqiaaewpr wyaanratig ddpsqllpgm
      361 vlelpddaps rs
//
LOCUS       WP_010524896            1613 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Nesterenkonia sp. F].
ACCESSION   WP_010524896
VERSION     WP_010524896.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 1613)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1613
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..1613
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=179700
     Region          1..1611
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 maetvlwtrd dsevetlrsa yfahvasddl rtvsradqrv rveehlrlag rrtdaapeaa
       61 vvvgerrsia mvvtddmphl vdsvtaevsr hglamslvvh pivlttreat agellavrev
      121 ptaqpgmssg dtqtlpdlaa lvddesrrta veswiavdid hpidearage lteglrrvig
      181 dvaashrdqd rmagrargaa gllrendsie esaesadlld wmadgnflfl gyceyvldrd
      241 sadgaqlvpq pdsalgilae rhglealhre payeggpgap dgepvaeter eralvitkan
      301 irstvrrrty mdyvavktfg sdgsvagerr fvglfsqray tqsivnipll rsradqllrr
      361 sgfspeshsg adllqilety prnellqmdi eevedtawqi lqlqerrrik lflrkdlhgr
      421 fmtallympr drfntavrlr vqdelmrhid aesidfnvrl tesvlarlff rmrladdaae
      481 malsveelqa klartirswa egiaqeaaes rsegeaeria arwgeafpdd yrvlyevpda
      541 lvdiaeleql eahpedgprm qfyapggedp admrlklylt epktltetlp vlddfglsil
      601 dersytltcg dgsvfhlydl glgypeglda dsvdigllee ayshvlrgta esdvfsrlvl
      661 rlgldirtvt vlrayakymr qlgsahsydf laetlrqnpe valalvwhfe arfdptpaed
      721 reelmerrrq evldaleqvr tldadrvlst flnlidater tnvhqghvrv alkiapdrvd
      781 sapeprpahe vfvyapdveg vhlrfakvar gglrwsdrqe dfrtevlglv kaqmvknavi
      841 vpsgakggfy pkqlpdqsvg raqwmeagka ayrtfirgll dvtdnqverd gvmeivppre
      901 vvrhdgddpy lvvaadkgta tfsdtaneis qeyghwlgda fasggsvgyd hkemgitarg
      961 awesvkahfs emghdtqsed ftvvgigdma gdvfgngmll sehirlvaaf nhlhifidpd
     1021 pdaaasfaer rrlfaerpsg wdaydeslis agggvfsrta ktipisepmr rrfdlpadve
     1081 qmtppeliaa llkapvdlly nggigtyvka aeeshddvgd rannavrvdg rqlrakvvge
     1141 ggnlgltqag rieaaqqgvr lntdaidnsa gvdcsdhevn ikilvdqlva sghldaaerp
     1201 ellhgmteev aelvletnra qnvvlltdrh rlgdwspsfh rlmgwleesv gldreleglp
     1261 tddqlaarrd aeepltspel avlvawskiq lkgalvessl pddewftatl eeyfpsaltd
     1321 rfasqlprhp lqreiianev andvvdmgga tfvframeet fateeqvvra fvavrelfrl
     1381 gefdaamrel pvsfprdewa htyldmrrll dravrwfvnh aargtsvqed veafaehirp
     1441 lygrleehlr eedrrrvaak reaarsagmp eqladwvgev fesfslldia alsaelavds
     1501 advadvyfav yaefdidall vritdqprrd kwqalargaq rdelyravre vtesvlttte
     1561 pgdaetrlls wreaheakis rveklvdevn qvsrdnvasl tvllrhlrgm iga
//
LOCUS       WP_010524837             288 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Nesterenkonia sp. F].
ACCESSION   WP_010524837
VERSION     WP_010524837.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..288
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29840
     Region          14..272
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 meliveilaa plqfafmqna lavavvaagv cgllscwlvl mgwslmgeav ahsilpgivl
       61 aellgvpmaa gafvfgllav lliggisstp vikrdtsigv vfttlfalgl vlisrvpsqt
      121 hlqhilfgnv lgtsrtdlwq vlvlglataa vlllarrdlt llafdrtyah tvglstagls
      181 alllvllalt tvtslqtlgi ilvvamlvip gatgmltcrt fgrmlmvssg gavfaavsgv
      241 ylsywldlst ggtivlvqst lfglayvfap hkgmlarlar arrtaaaa
//
LOCUS       WP_010524800             867 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK, partial [Nesterenkonia sp. F].
ACCESSION   WP_010524800
VERSION     WP_010524800.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 867)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 867)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..867
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         <1..867
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
     Region          264..763
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
     Region          <744..822
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
ORIGIN      
        1 aglahmahgm pplnaafedm lasggivgyl vtvplaslit vypvwavlga vllagllvlt
       61 dtpvrriper asvakdyvvg erreprapre parsddgasr ptrarrasra pepadepldd
      121 vfdegesapk kagllskllr grdadevpea epasvadtse aeasraaaga fdasavesda
      181 eqdaepavpp gvkrptaqel aiqrarekaq sppssaasga saasadeaap aagrpaapat
      241 taptaavgpg agapssapap saveapapap dmpvrseqle lagdvtytlp dqsllpsgpp
      301 akehteande vvdalnrtfe qfkvdaqvtg fsrgptvtry eveltpgtkv ekvtgldkni
      361 slavasnevr ilspipgksa igieipnkdk evvalgdvmr snaarktehs mvmgvgkdve
      421 ggyvvanlak mphllvagat gagksafvns mitsilmrat pdevrmvmvd pkrveltaye
      481 gvphlvtpii tdpkkaaeal qwvvkemdnr yddlahfgyk hiddfnkavr ngkitlppds
      541 krelrpypyl lvivdeladl mmvaprdved sivritqlar aagihlvlat qrpsvnvvtg
      601 likanvpsrm afstssvtds rvvldsagae kllgqgdalf lpmgnakpmr vqgawvsete
      661 ihsvvehvks qlsaqyredv ipdkpqkqid edigddldll lqatelvvtt qfgstsmlqr
      721 klrvgfakag rlmdlmesrg vvaasegska rdvlvspeel pgvlatirge eppaaapsed
      781 apeayeqdvv ayepasgqpa pqppqeasas pasgpppqgg stvsgmssad liardlaert
      841 aalpeateyh dghdtdaged awqltgr
//
LOCUS       WP_010524938             189 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Nesterenkonia sp. F].
ACCESSION   WP_010524938
VERSION     WP_010524938.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 189)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..189
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20663
     Region          53..180
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mpttsrsalt tafaedldaw hpvdagqddl rrryldllah gdeawrrqpr pehltascfv
       61 fdasfthvll cfhgkgrfwv qlgghieadd gsvadaafre vaeesgleav tpvrripvdl
      121 nihplgsgft rcsahwdvgf aavasrdaev lvseesddva wwpvddlpsg iadqfdqrla
      181 tvlaelgrg
//
LOCUS       WP_010524962             304 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Nesterenkonia sp. F].
ACCESSION   WP_010524962
VERSION     WP_010524962.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..304
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32600
     Region          8..239
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 madprddvlv agasgylgrh lvrtlhrrgf rvravvrdvg raggpgahga paleglvdew
       61 vecdivagpl dglvrpgetv lsalgvtrqk adpwdvdfaa nlallaeaer ssarqfgyvh
      121 vmhaershsq lvrakrafva alrrspvpsa vvnpsgyfsd meellamarr gvalsigdgs
      181 vrlnpihgqd ladflvdqlt stdaedpvrd elghrhrawd vggpevftlr eilqlcfavc
      241 dlparivdvp tgllraglpl lrpaarvhdl aqffldgfsg dgvgertgth rledhlraag
      301 hgng
//
LOCUS       WP_010524971             448 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Nesterenkonia sp. F].
ACCESSION   WP_010524971
VERSION     WP_010524971.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45582
     Region          39..396
                     /region_name="MFS_MdtG_SLC18_like"
                     /note="bacterial MdtG-like and eukaryotic solute carrier
                     18 (SLC18) family of the Major Facilitator Superfamily of
                     transporters; cd17325"
                     /db_xref="CDD:340883"
     Site            order(45..46,49..50,53,85,135..136,138..140,143,163,
                     166..167,170,262,265..266,269..271,274,301,305,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340883"
ORIGIN      
        1 msdrsssdsr apveaagetp grprprhpla dphilvgall pallfslgvg amlpviasfa
       61 vergaslata gaiaamlpvg qiladmpags ltarigdrra mllagllgal gflgaalspg
      121 plplaaavll vgganavfhl arhahltavt ppqhrarvls tlggmnrigq flgpflgaav
      181 llvgelplvf vvaavtalaa satvamtred prtvdddgaa gvgaaqsgra graqsaeasr
      241 aprmlevlrd hrrllmtlgv pvllvgsvrg arqqvlplwg ehlgldpati sllfglaagv
      301 dmllfypagk imdrmgrlwi gvpsmtllgl amalvpltsg esqlaaaavl mglgnglgsg
      361 immtiasdva pergrpqflg awrllqdvgv asgplivsag aalgslaagi wtaaamgpag
      421 aaalrrwlpr wsihatratr rrveqsap
//
LOCUS       WP_010524997             585 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Nesterenkonia sp. F].
ACCESSION   WP_010524997
VERSION     WP_010524997.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 585)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..585
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63200
     Region          3..531
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 msapiiaaea lsfrypgapt dtlrnvdlri ergdfvavvg gngsgkttlc ktfnglvphy
       61 wsgefagrvt vdgqdtftss vaelsqtvgy vyqdfqnqlv rptvrdevsf gpvnfgrpdh
      121 aertaealem vgiehlaekf vwqlsggqsh lvalasvlal rpevivvdep vaeldpaaae
      181 evyrrltaln rdhgltviti ehhaefiaah arsvllmsdg spvwhlptdq alaradelsr
      241 hgipapqivd aaarlglpqv pqsvadaaam lsehrrapyp dpatttatta taprdrpatg
      301 ersvvvaegi rhahrgvrge lrpvlddldl qlhagdrval iggngagktt lmkllagiav
      361 prageilleg istrsrsarr ladqacyldq rpermflkds vradvalfpr grgvddaeql
      421 vdrilrrvrl eqlsdrdgrt lsggqqrrat lgiglamrps lllldeptas ldvasrddvi
      481 tmldelsddi acsvvathdm hlvaewatrv ialehgrvla dmapaelfas peimrrarlv
      541 ppqvvelgla lgmeppplsv aelldacadr teptadrtee apawr
//
LOCUS       WP_010525001             263 aa            linear   BCT 01-JAN-2025
DEFINITION  CGNR zinc finger domain-containing protein [Nesterenkonia sp. F].
ACCESSION   WP_010525001
VERSION     WP_010525001.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..263
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28850
     Region          9..192
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mfhaeinrtl taavnlmnta eglhsakpsp deitsieslr kfvaaqdpel kwpssgldrs
       61 qvdgiielrd tlreiwsaap itggrpveqi nelldgvstk lvrtdetstt peyraapipv
      121 ssqlvdvvta avgdalkfll vndetsrmrt crgddcdavi idltrnrskl fcdfgncanr
      181 ahvrayrarq aalreagkqa lkqsetedkl arpsaaekaa eldeptsesg vaakqfrsam
      241 rdelmdqrdk kggkkkkkkk skk
//
LOCUS       WP_010525126             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Nesterenkonia sp. F].
ACCESSION   WP_010525126
VERSION     WP_010525126.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 308)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..308
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32977
     Region          18..288
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mshllntsgs slggpsrrgv lvgslgaaga laltscglad avgggggddt tismivtesa
       61 pfqepteiak ellaedgwtl ettyvtdiiq pnqvvsqgey danffqhiay lrqfnedngt
      121 dvepafsvyy apsgifsleh dsiedlpega qialavdtan ngrgikllae agaleidesk
      181 pvtelsqrdi tanpknfefi evdqqstpqt lpdvdagfaf arliaeaghd vdetaliled
      241 daevrrpyti vvagqpgfqd tekaralqka fqseevrqwy aeyldgaidf tdeftlstve
      301 dvwadfag
//
LOCUS       WP_010525187             124 aa            linear   BCT 01-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Nesterenkonia sp. F].
ACCESSION   WP_010525187
VERSION     WP_010525187.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..124
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13536
     Region          11..111
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 mtsaddlltt llevehagwr alceqrggah ygtlmtpdgl milvdgsild rdavvasldg
       61 appwddyalt epraldlsrd vaalvyraea rrtgrepfra qmtstyrfld gvprlalyqq
      121 tatp
//
LOCUS       WP_010525251             498 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA repair protein RadA [Nesterenkonia sp. F].
ACCESSION   WP_010525251
VERSION     WP_010525251.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..498
                     /product="DNA repair protein RadA"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140664 - ATP-dependent DNA damage sensor
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=51736
     Region          13..488
                     /region_name="Sms"
                     /note="DNA repair protein RadA/Sms, contains AAA+ ATPase
                     domain [Replication, recombination and repair]; COG1066"
                     /db_xref="CDD:440685"
ORIGIN      
        1 masrsssrsk saptfectec gwqtvkwvgr cpecqawgsv qekgqvtart tastslvepa
       61 raigdvdatv aqhrptgige ldrvlggglv pgavilmage pgvgkstlll qlaaavargs
      121 qpgerpdgge lgaeaggeaa ddgarrpvly ltgeesaaqv kkraertesl adalhlaaes
      181 dlgqalgqie hldpaltimd svqtlssgev egaaggvtqi revtasmiea akrrnmttil
      241 vghvtkdggi agprmlehlv dvvcqfegdr hsrlrllrav knrygptddv gcfdlheagl
      301 tsladpsglf vsalservpg tcititlegr rpltaevqal iaespasqpr ravsgldspr
      361 vsmllavlqr rarlatlsss eayvatvggv ritepaadls ialavasaal ekplpsrfva
      421 fgevglagev rpvpglqrrl qeaqrlgfth aiiprgvgrd agpggpeipe glrvkevgsl
      481 pealnlvldg gpppnaqe
//
LOCUS       WP_010525181             220 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Nesterenkonia sp. F].
ACCESSION   WP_010525181
VERSION     WP_010525181.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 220)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 220)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 220)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..220
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22069
     Region          20..216
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtpllealdw vltadswtgp gglgvrageh llysllavgl salvalpagl lightgrgrg
       61 iavvstgvtr alptlgvitl valaagiglt apmvafivla vpsilagays gveavdpqiv
      121 daaraqgmsp vqvllgvevp lgmrlilggv rlatlqvvat atlaayvgag glgrplflgl
      181 rnydyammlg asivvillav vldalfalgq rllarrpgta
//
LOCUS       WP_010525309             328 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Nesterenkonia sp. F].
ACCESSION   WP_010525309
VERSION     WP_010525309.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 328)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..328
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=37490
     Region          21..150
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          163..320
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mtrvprrrtt tcaddghdae vlaagalcwr lnrgalevll ihrpryddws fpkgkldpge
       61 tlpecavrev qeeiglkvrl gmplpitryd vgkngkvksk evwywaaqvt egkpepdaee
      121 tdevrwvavp qaremlsndt drepldeler lheemrlrts pfivlrhaka kpraswskae
      181 gkrplaatgk rqakaverll tawrprmles spwkrcvetv apyvkrhrhr lkyrdsltek
      241 raqekpqkpr nrtrksleal qpvlmcthrp vlpmvleelr gwirdpvlle alpsedpylr
      301 pgavlvaqqa vdgsgmivai evhdpfdd
//
LOCUS       WP_010525423             497 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Nesterenkonia sp. F].
ACCESSION   WP_010525423
VERSION     WP_010525423.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..497
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=51337
     Region          2..484
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mielsaaeva eavdgrlvgv vdphaatvta adtdsramvp galfiakpge ttdghlfied
       61 alaagavlvl aeretaaadg tphpavived vvaamarlaa dvvrrirehs pttvigitgs
      121 agktttkdll ravleaegpt aapqgsynse vgvpltvfta aletrylvve mgadapgnir
      181 dlaaivepdv gvvlmvgsah agkfggaeki aavkqelvea vgpegtviln dddpqvrama
      241 dvaaapvtwi tadsmdvapr avaaqqvmld ddgrpqltlv fgaelvdpde praveltsgl
      301 igahhvtnll aaaaaaavvg vgsaaiaerl dgrgaasrwr merteradgv tvindaynan
      361 pesmrealrt lamitrsagr rsvavlgaml elgdesiarh aqlgetvvrl disrvlvvge
      421 eayplyrsai aegswgsevr wtataeeaee lladelragd vvlfksshga glrllgdrva
      481 arhgdaldgs gkagttw
//
LOCUS       WP_010525491             306 aa            linear   BCT 01-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Nesterenkonia sp. F].
ACCESSION   WP_010525491
VERSION     WP_010525491.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..306
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32841
     Region          20..297
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mtaldelvrd gaepvkiadg atwsegpcwi petstvrwsd ihgdrilqhd lltgatsvhr
       61 dgveftngrt rradgaivqc shglrrieve rdgvveplve rwsggrfnsp ndvvvasdga
      121 vwftdphygi tvageghpge meyggchvfr vdpetgeaep mitdiaepng lafspdesvl
      181 hvsdtsavrr pvgvgerrvv sydvvreqge qgrirctggr tlfeipagip dgirvdeagr
      241 iwssaadgvh vytdagehlg ripvpevvgn lcfggadgre lfiaattgiy qlpvavrdat
      301 wsrigg
//
LOCUS       WP_010525487             329 aa            linear   BCT 01-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Nesterenkonia sp.
            F].
ACCESSION   WP_010525487
VERSION     WP_010525487.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..329
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=34990
     Region          7..287
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mtstvqsist vtvvgagymg ggiaqslala gytveivdvd veasrrgler llgeaqdfed
       61 qglypagste tiranltagr tleeavadvd fieeavfesp evkkdvlgri sesaredaii
      121 gtntstipvh vlapavkrpe rfftvhysnp apfipgvelv sgeetapeav aavkellers
      181 gkegaevadk pgmvlnrlqy allkeavnvv eegvatpeav dtivrttfgf rlgffgpfai
      241 adqagldvya kcftiveday germatpqml tdnveagrhg vkngkgwtgd fdeetaaelv
      301 ayrnkayakm gdllrelgpa prgtgsdqv
//
LOCUS       WP_010525516             301 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Nesterenkonia sp. F].
ACCESSION   WP_010525516
VERSION     WP_010525516.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..301
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=30767
     Region          2..230
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mgldvggtkt ealaldaagr vvarhrcvtv pgpsgvvdtv gravaalcgp sgevsaesvg
       61 vgipgqievp sgrvrhavnl glrdldlari lerelgvpvr vendvkaaai gacrirgrer
      121 eslvylnlgt gvaagvvvdg vlqrgvggva geighisvdp rgetcpcgqr gcletvaggg
      181 avarrwgggd lpvlemfdaa drgegramrl rrefaagvaa avrlivltld vptvllgggl
      241 vhlgdrlrdv vvdelrrage asdflhslri derlemlpps sgapavgaah lgvgmrradv
      301 g
//
LOCUS       WP_010525525             346 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Nesterenkonia sp. F].
ACCESSION   WP_010525525
VERSION     WP_010525525.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..346
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36375
     Region          3..295
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,90,104,106,139,171,255,258,294)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(225,230,246,255..257,260,282,286)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mtdaiclgea mamvtpppge cladcdalsl siggaeanva lglsslgvst awasrlgdda
       61 fgerirrtlq dggvdgscie hdprrhtgly akdpaaraad rmlyyragsa asamgpdflr
      121 tgrlpglles arlihtsgit palsaecfam teellsrrpg ealvsfdvnw rpalwegrea
      181 adlarladra dvvlvgrdea eaafdvhdeh qlrellpspr llvikdeavg avaleadgar
      241 trvpsltvdv vesvgagdaf aagylaellr ggdqrralrs ghlcaaatlt vptdrgplpa
      301 tetaaaalas seaawravra saeglqlphr plrpdheppr rdgsrs
//
LOCUS       WP_010525527             133 aa            linear   BCT 01-JAN-2025
DEFINITION  RidA family protein [Nesterenkonia sp. F].
ACCESSION   WP_010525527
VERSION     WP_010525527.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..133
                     /product="RidA family protein"
                     /calculated_mol_wt=14645
     Region          1..133
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mtkhiisten apqpahtfsq glrkgpilqi sgqgpmdpet aqyigdgdvr vqtrrtleni
       61 raileagdas medvvmlrvy lkdqqdfaam neayaefiee hvpsgrkpcr ttvfvclphe
      121 vmhveidaqa vva
//
LOCUS       WP_010525533             476 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Nesterenkonia sp. F].
ACCESSION   WP_010525533
VERSION     WP_010525533.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..476
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52244
     Region          5..462
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 meqifdpltm arwqfglttl yhflfvplti gmalmaaimq tawvrtnkvt ylkltrlfgk
       61 iflinfamgv vtgivqefqf gmnwseysrf vgdvfgapla ieglaafffe atfiglwifg
      121 wgriprlahl aciwvvfias tlsayfilaa nafmqnpvgy tmnaergrae ltslwevltn
      181 pvalaafpht ifaaimfaaa vmvavaawhl rrrqhvetmr palktglwan vaafagvgls
      241 gdqlslamvd aqpmkmaaae glyettknas fsiftlgtpd gaselfsiri phllsllsth
      301 tlggevegin dlqdqyvaqf gpgeytpiiw itywafrwmi glgacsalvs lialwftrkk
      361 arplgaraed lkwraliwta plpllaslvg wvftemgrqp wivfgemkta aavsptvagw
      421 qvaislaaft liygvlavve frlilkaaqe gppeiaeddd geggssadda dfamvy
//
LOCUS       WP_010525540             255 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Nesterenkonia sp. F].
ACCESSION   WP_010525540
VERSION     WP_010525540.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27116
     Region          16..236
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mttspettvt rpeaaapavr aerlsktygt gdaavrplre lsleipraqf taimgpsgsg
       61 kstlmhvlag ldspdagrvv vgdveltgld ekrlteqrra higfifqayn lvpamtaeen
      121 illparlgrt rvdretldav vdrlglgdrl ghrpfelsgg qqqrvavara lvtrpsvifa
      181 deptgnldht tgdevlqllr tavdefdqtv imvthdpgaa avadrtvlld dgrvvdaleg
      241 qsaealaaal vevgr
//
LOCUS       WP_010525556             569 aa            linear   BCT 01-JAN-2025
DEFINITION  BCCT family transporter [Nesterenkonia sp. F].
ACCESSION   WP_010525556
VERSION     WP_010525556.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..569
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60016
     Region          60..549
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mpqdhpagph praaehsspd hpdsddpdsa tggaavvdrp rrdtaerfpa epqtpgraln
       61 gvfftavtli vallavagfw permstaada amnwvtssag wslmliplgl iglllvlacs
      121 rfgrirlggd dsrpeyptya wiamllgavm giglitygva epvthlfdpp hglsepgsqq
      181 avvdslrftf ldwgihawav fatfglaigy sthrlgnkgl vspilrplig rhadglvgka
      241 vdvlvilstl fgtttslglg aaqisqglsq vtgleltrtg vqvsvialit vlftasamsg
      301 vgrgirmisq ttmvlaaall afvlvtgpts wlinlflrsl gsyaggfvei slmlpadgdd
      361 lawmqwwtyf mmawwiswga fvgiflaris rgrtirqfvl vvlgvpslif sawftvfggs
      421 amfmdlergt aigeaaaadi ntaffglleq lpltmltsvv avvlvvlyfi tgadsntyvl
      481 svissdgrmh psrpvmgvwg vltgataavl lyagglqalq tavmlsaapf ifvilalavs
      541 lvmllrrdpl iaspgagsts ttsaaadar
//
LOCUS       WP_010525315             659 aa            linear   BCT 01-JAN-2025
DEFINITION  NHL domain-containing thioredoxin family protein [Nesterenkonia sp.
            F].
ACCESSION   WP_010525315
VERSION     WP_010525315.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Kumari,P., Aeschimann,F., Gaidatzis,D., Keusch,J.J., Ghosh,P.,
            Neagu,A., Pachulska-Wieczorek,K., Bujnicki,J.M., Gut,H.,
            Grosshans,H. and Ciosk,R.
  TITLE     Evolutionary plasticity of the NHL domain underlies distinct
            solutions to RNA recognition
  JOURNAL   Nat Commun 9 (1), 1549 (2018)
   PUBMED   29674686
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   7  (residues 1 to 659)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
REFERENCE   8  (residues 1 to 659)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10221804
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..659
                     /product="NHL domain-containing thioredoxin family
                     protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=69652
     Region          20..138
                     /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"
     Region          237..580
                     /region_name="NHL-2_like"
                     /note="NHL repeat domain of NHL repeat-containing protein
                     2 and similar proteins; cd14951"
                     /db_xref="CDD:271321"
     Region          250..299
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          328..368
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          384..430
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          442..491
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          494..529
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          539..580
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
ORIGIN      
        1 mtetirrtdr vraselvgrg wlntggeevt ladlrgkivi ldfwtfccin clhvldemrp
       61 leerfsdvlv tvgvhspkfd headpdalaa averyeiarp vlddpnlttw qaysarawpt
      121 lvvidpegyi aahlageghv agldslveel vaeheakgtl hrgdgpyvpp epvsrtlrfp
      181 gtavpvtrpl gadddaaaag rflvadtghh riveldadle tvvrswgggp eggekghrdg
      241 taaealftep qgvailpaev aaqvgydlvv adtvnhrlrg idvsgdrvlt vagngvqrli
      301 dsdrvaqeqa agvgslgtep levslsspwd vlwseaagtl ivamagthqi fefvpttgel
      361 rvlagtgleg ltdgsadeaw faqtsglaad aagdvwiads etsslrvlrt aedpkaprve
      421 tivgegmfdf gfrdgdpaqa rlqhplgvaa lpdgsvlvad tyngairryr gehlaadgtt
      481 vpaevstvar glkepsdvll dadgstllvv etnahelvrv aipeefltvd egamqshrps
      541 tdvapgeltl tvgfsaptgq klddrfgdpt qlkissspde livsgagsse gltrtlqldp
      601 tvgegvlhit araaacdgap geeipmhaac hlyqqdwgip vnlvegagdt lqldlrgvk
//
LOCUS       WP_010525671             285 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Nesterenkonia sp. F].
ACCESSION   WP_010525671
VERSION     WP_010525671.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..285
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30200
     Region          30..281
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mpefiesapr rldgdddrpt epaggppasl raasltvgyg arpvledlsl avpdgrvtav
       61 vgpngcgkst llktlartlt prsgevlldg tpltrwksrr iarrvamlpq spvvpdgvtv
      121 rglvargrhp yhsalrqwva gddeaiaaam eatgiaefad spvvelsggq rqrgwiamvl
      181 aqdtehvlld eptsfldlah qvevlrlcra ireqgrtvva vlhdldqaar wadhvvvldg
      241 griaaagppe eiitaelvae vfglacqitr dpqsgtpkvv pladg
//
LOCUS       WP_010525731             236 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Nesterenkonia sp. F].
ACCESSION   WP_010525731
VERSION     WP_010525731.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..236
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25335
     Region          31..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mspeqtppte pttepspgrr rgrppspvls rssitsaair ivssrdhral tmaalarelg
       61 vstsalynhv askhdvlvlv qdrlneqidc rafdtepwpe alrvwarsyr dcyiehtali
      121 pimavlpvad apqtlqmyer vtralqadgv pgpeavdmiv gvealvfgaa ydasapadif
      181 dpgdradlap aftaaaaerg pdarraadra felaldalvd glaeglrrre ddaats
//
LOCUS       WP_010525734             509 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Nesterenkonia sp. F].
ACCESSION   WP_010525734
VERSION     WP_010525734.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..509
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53831
     Region          17..481
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtqtgesapa ttgatrdhsk glsagavgvl gavvigvsti apaytlsgav gptasavgeh
       61 lpavlivgfi pmmlvaigyr elnrampdsg ttftwaskaf gpwigwmgsw cllaatilvl
      121 snlagiavdf fylaisqlvg epwiaeltrs vpvnvltcla fmaaaawvsy rgleatkgvq
      181 yvlvsfqvlv lgwysvaafg hvgsgtafda ldpswewfnp fgvesfsafa agialsvfiy
      241 wgwdvvltmn eesrgttttp gkaalvtilv vvglytmvtv atlsyagvst gefglgnpei
      301 qgnvfaalag pvmgpfailm slavlsssas slqstmispa rtmlamghyg alsekyarvs
      361 pkhqtpayat vvsvviasvf yavmrvvsen vlwdtittlg mmvcfyygvt alacvwyfra
      421 earasigafl tkmlapllgg llllifffqt awdsmdpayg sgseiggigl vfilgvlifv
      481 lggaamiyqy iqrpeffrrr fetsehlae
//
LOCUS       WP_010525782             345 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Nesterenkonia sp. F].
ACCESSION   WP_010525782
VERSION     WP_010525782.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..345
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36928
     Region          7..322
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msispqdelr vavvgagrmg sdhvdrlahr tlrarvsavv dvdvdrasaa aagadgaqvf
       61 tgldellaad vadavvlatp gflheeallr lidagipvlc ekpltpdpqs slrvveaeaa
      121 agrqliqvgf mrrfdagyrq lkqlidsgeh gellllhhqh rnpvsppeft demiihdsvv
      181 hefdavryfa geeitevqvr lgrrssraae slhdpqlvtl rtesgllatv eifvnaqlgy
      241 qvhtqasfed gvvsigqgse lqltaggrsg gtvdagfvtr fgeaydrevq dwvdatlrge
      301 iagpdawdgy ataaccaagv asqqdqslqp vrlaerptfy srsaa
//
LOCUS       WP_010525799             275 aa            linear   BCT 01-JAN-2025
DEFINITION  TlyA family RNA methyltransferase [Nesterenkonia sp. F].
ACCESSION   WP_010525799
VERSION     WP_010525799.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..275
                     /product="TlyA family RNA methyltransferase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29187
     Region          5..244
                     /region_name="YqxC"
                     /note="Predicted rRNA methylase YqxC, contains S4 and FtsJ
                     domains [Translation, ribosomal structure and biogenesis];
                     COG1189"
                     /db_xref="CDD:440802"
ORIGIN      
        1 mgsrrldral veeqlvasrs raahlvvegl vrvdgrtvrk aaakvteqar levdddpwvs
       61 raahkllgal tacpsvdprg rrcldagast ggftqvllsr easavvavdv ghdqlapalr
      121 eeprvtaveg lnlrhlrpge lgepfdliva dlsfislrli vpalaaqaal gaelllmvkp
      181 qfevgrerla rtgvvsspql rreavagvva acedaglrlv sahrsplpgq dgnlefflhl
      241 raparsagga avdiadaesa aadrleqidh idyrd
//
LOCUS       WP_010525809             227 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Nesterenkonia sp. F].
ACCESSION   WP_010525809
VERSION     WP_010525809.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..227
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23254
     Region          7..219
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 maesvtrtvs raldllaavc daggtnlaea aratdlssst alrllrtles sgfvrrddag
       61 sfrpglrlvq lgaqalsses lvslaeaplr rlveatgesc ylsvphlqgt eheqciylam
      121 eegthsvrha swvgrsfpmt gsaagaalsg avdeqgytvv gqavesdvta vaapiaippa
      181 adaepqivaa lsvvapsyrm tseavdrigq fvaaeaagil haravaa
//
LOCUS       WP_010525817             168 aa            linear   BCT 01-JAN-2025
DEFINITION  SMC-Scp complex subunit ScpB, partial [Nesterenkonia sp. F].
ACCESSION   WP_010525817
VERSION     WP_010525817.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003627
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     gene            1..>168
                     /gene="scpB"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0051304 - chromosome separation [Evidence
                     IEA]"
     Protein         1..>168
                     /product="SMC-Scp complex subunit ScpB"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0051304 - chromosome separation [Evidence
                     IEA]"
     Region          35..>166
                     /region_name="ScpB"
                     /note="Chromosome segregation and condensation protein
                     ScpB [Transcription]; COG1386"
                     /db_xref="CDD:440996"
ORIGIN      
        1 msdaqetsgp epqadgasre paledaqgtr lvahedhlaa leavlmvaee pvtpaelaea
       61 lalaehqvvv lldelrvead gahggrergf elrevaggyr yysrpryadq vsafvlggqt
      121 srlsqaalet vaiiayrqpv srsqiaavrg vnvdgvvrtl varglvdt
//
LOCUS       WP_010525815             295 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Nesterenkonia sp. F].
ACCESSION   WP_010525815
VERSION     WP_010525815.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..295
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31735
     Region          40..291
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 msnqqptelf tvhgepiigp tgrpkhefpe pppleghgpa rtiamvnqkg gvgkttsain
       61 lgaalaeqgr rvlmvdfdpq aalsaglgtn phelevsvyn vmmerevttq eailsthveg
      121 vdllpanidl saaevqlvne vareqvldra lravrddydv iiidcqpslg lltvnaltaa
      181 hgviiplvae ffalravall vdtiekvqdr lnpdleidgv latmvdprtl hskevisriv
      241 eafgdkvfet vikrtvkfpd atvaaepits yaqkhegaka yrtlvrelvs rggap
//
LOCUS       WP_010525859             253 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Nesterenkonia
            sp. F].
ACCESSION   WP_010525859
VERSION     WP_010525859.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26434
     Region          10..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 matsssldge srrarlleil esegritsse vaetldvsam tlrrdladle aagrlrrvrg
       61 gavapsqprs faersgrraa akrtiaskar qlvpqrgtcs fdasstagvl lagltgagel
      121 tvvtnsgenf eaaagrpgie pvllggtrqe ttrsfvgpla elmasslqca rfftsaaald
      181 avwgsseatp eeaalkrvla dhadttvmla dssklgarav argvgldavd vliteldpdd
      241 arlnpfrelv evr
//
LOCUS       WP_010525864             272 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Nesterenkonia sp. F].
ACCESSION   WP_010525864
VERSION     WP_010525864.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..272
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28653
     Region          11..272
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mpdaaagtpl hiitlvksvp daqlerrfte erhidrsegv lgeldeyple talriketae
       61 ereirvtalt mgptgasaaa kkalqigadd ayvltddala gadisatsta lraaieriqq
      121 vseldaqllv vtgmasddge sgavpaqlae rlgvhllsqa tsvelsegrl vvtrtatveq
      181 qkvsaalpav vsvtdqandp rypnfkaima akkkpltels ltsvgigpta vkpraqvlta
      241 eprpprhggt vitdegdagv qivdflqker vl
//
LOCUS       WP_010525866             390 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Nesterenkonia sp. F].
ACCESSION   WP_010525866
VERSION     WP_010525866.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..390
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42463
     Region          6..390
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mfpgfyeeih eefrevvref varevtphyk ewdaahlmdr avweaaaeng llglavgedh
       61 ggmgltdyrf rmildeelar adalglalal hlhddwvlpa lrrfgtaeqq qtwlprflds
      121 sfiasvafte pgagsdlrgv rtkavrqddg swlltgqktf ignavsgdga lvlartdgsd
      181 vkrrggaasf slflvekqdd sgyqvgsqle kmglkasdta elffsearvp aenliggegr
      241 gleiakeilp qgrlavaaga aavaeaalaq tvdyvrerta fdrpvaefqn trfqlaelqv
      301 eleavqryla atveafdage ldvvgaskak lfigeraksm idaclqlhgg ygyileypva
      361 qaylavrlmt ifggtseilr etigadllrd
//
LOCUS       WP_010525880             285 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Nesterenkonia sp. F].
ACCESSION   WP_010525880
VERSION     WP_010525880.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..285
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=30690
     Region          65..276
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mslllglalg agllliwwsc wprrrpeaar rqrlgrldql laeaghqrvg vsgavtamvs
       61 savivflivl vitravpval cfalfasavp ivvlrwqark rqavlreiwp davdhlrsav
      121 ragmslpeal iqlstsgpvp lrepfaefar dyrsgqnlgt alvglkdrla dpvgdrivia
      181 ltitrevggs dlgrllstlg eflredartr selearqswt vnaaklavaa pwivvlllst
      241 qaeaadayrg legmavlagg lvvsvvcyql mlrigalpke grvll
//
LOCUS       WP_010525872             290 aa            linear   BCT 01-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase, partial [Nesterenkonia
            sp. F].
ACCESSION   WP_010525872
VERSION     WP_010525872.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..>290
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
     Region          2..290
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mivtvtpnps ldrtveldap ltpgavqrav ratsepggkg vnisralvaa gretlavlpg
       61 deadpmiaal aavdvpranl ptgapvrtnv tvtdpqgvtt kinepgaald daqvaalldl
      121 avarsrgaqw vasagslppg aptdlharlv dalrdqlgdd apqvavdssg palaaavavg
      181 pelikpnaee llelaallte drdgdgapad cpqarlteeq leadpsaava lvrrlqshgv
      241 rdtlvtlgar gallvpadpq atvlhadgps ltarstvgag daslaglllg
//
LOCUS       WP_010525913             141 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Nesterenkonia sp. F].
ACCESSION   WP_010525913
VERSION     WP_010525913.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..141
                     /product="VOC family protein"
                     /calculated_mol_wt=15095
     Region          5..134
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(5..10,26,59..60,63,77..81,85,87,91,122,132)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 maigltpylq fpgtareale fyravlggel stmtfaegmg aedetqdlim hsslyvdrgl
       61 hlmasdhdpg qqpggsptla lsssdgdpee darlercwda ltegaeiqep latapwgdrf
      121 gmltdrfgvt wmvnisvasg d
//
LOCUS       WP_010525917             266 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Nesterenkonia sp. F].
ACCESSION   WP_010525917
VERSION     WP_010525917.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..266
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28325
     Region          34..>123
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          94..211
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 maestetglp ravaiawgmq evpqrgpsrg lsherivaaa veiadadglp avtmqavaks
       61 lgfttmslyr yvsskdellr lmqdaaltvp etvrldedwr aalhqwagli rdayrahpwa
      121 lsiprdqtsv lmpntmrtvd valaamrdla lddaeklgti mvisqhaagm velelslnda
      181 gtlaitaega emlgevvtae rhphlralma rghyvplggp srdadggadd agadgavppp
      241 aedvdeeytf gldllldgla araenr
//
LOCUS       WP_010525939             503 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Nesterenkonia sp. F].
ACCESSION   WP_010525939
VERSION     WP_010525939.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..503
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=52336
     Region          284..492
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mmgtgtgggr vgrpriqdta ddlvasvlat agsrvgtpef strrvaeltg lsqtvvsrsf
       61 rrlrrrgags agpagpagsa asaerdvple laalqvafpr irvvfrpaea paaaprrtaa
      121 drratallaa lrvagvgqwa ggsegvgevg dageaggvgg agqgrasagr lvhewspggd
      181 weafleglaa aldcaapsle alpgdllall aarvgrglhg vdwrrgtsrr sgdgaaaqte
      241 qdsdsdepnd epgemlgvpe ypapgprpar drsagrwlph gelsvteqia ialrreimna
      301 gyrpgdrita gplaatlgls aatvrtamrr laddglldsg vggfsvpavt gadvvdlyaa
      361 rlhvgmvllr gvaarprhrm lparlalgav eaaarqgsga dveradlqfq qeladasgle
      421 qsarsfhalt lrvrmfisvl qldytpaaer ivaddrrlla avlegraeda vriwrgkldn
      481 avrhmsalap eafdaelwar lsr
//
LOCUS       WP_010525957             207 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Nesterenkonia sp. F].
ACCESSION   WP_010525957
VERSION     WP_010525957.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22627
     Region          20..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maarrprats grprgadsvq rraeildaae elfadqgyrg vsmsavaraa gisqtglvhy
       61 fatkddllaa vldrrdeqdt aqllttpeqg wrfvetlvgv vrqneeretl vrlytalsge
      121 avtpdhpatr wlrrhhhdvr agiaaaveqa vvdgelvaea padhisrllv aamdglqvqw
      181 lvdessssma edfrqlvdal haqwrag
//
LOCUS       WP_010525986             452 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Nesterenkonia sp. F].
ACCESSION   WP_010525986
VERSION     WP_010525986.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..452
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48068
     Region          5..356
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msnqntrtry vivgtgsrca myvdailgah advaelvava dsnpgraehh rgriaaehga
       61 evgtfdpgel tavvqarsid rviitspdft hadyiveslt agadvvvekp ltidaessar
      121 iartvhetgr dvtvtfnyry sprntalkaa vqegrigtvt sidftwvldt vhgadyfrrw
      181 hrvkensggl lihkashhfd lvnwwlddsp qrvyasgglk fygaenaaar gispaergtr
      241 edsasdpfal dlrtdetlra lylenehhdg yrrdqdvfgg gitiednlal ivdyaggpvl
      301 nyslnahspw egyrvaingt egrlelevve raavlpasgg spvdpsvaed grssavrakg
      361 erlvlqrhwg eaeeieivqg egahgggdrl lladiftgpg edpyhrpagl gdgieaiavg
      421 vcgnaslaag apvqvadvel glgaaataaa as
//
LOCUS       WP_010525990             142 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Nesterenkonia sp. F].
ACCESSION   WP_010525990
VERSION     WP_010525990.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..142
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14558
     Region          1..136
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msapiivgvd gsetarkaae qalelaralg aelkvisays qdrsetiqsg sdkwvvsdad
       61 nalhtaekvv asldadgvtv tpgaefgrpa eallaaaekn daqmivvgnq rirgmgrvlg
      121 siatsvahna dcdvhianty ta
//
LOCUS       WP_010526000             112 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Nesterenkonia sp. F].
ACCESSION   WP_010526000
VERSION     WP_010526000.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..112
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12726
     Region          13..107
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mshadvtfsv hlqelrrgti vlgclrlldr pdygyrlleq lqqhglavdg ntlypllrrl
       61 ekqgfltsew qaadprprkf yrtseageel aealeadwrr ltaavdslte es
//
LOCUS       WP_010525995             388 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Nesterenkonia sp. F].
ACCESSION   WP_010525995
VERSION     WP_010525995.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..388
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42977
     Region          7..385
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mseprvlria mngitgrmgy rqhllrsilp irdqggielp dgskvtvepi lvgrnedkir
       61 elaakhdveh fttdldgiir dpsvdivfda smtslrhqtl saaiaagkhl ftekptaetl
      121 dgavdlaqka saagvtagvv hdklylpgli klrrlvdegf fgrilslrge fgywvfegeh
      181 qeaqrpswny rladggsmtt dmychwnyvl egivgkvksv tsrtathipq rwdekgeryd
      241 adaddaaygi fdletpdgdd vvgqinsswa vrvyrdelve fqidgthgsa vaglqkcvaq
      301 qrahtpkpvw npdlpvtesf rdqwmevpdn atfdngfkaq weefladvva grehrfglls
      361 aargvqlael glqsaaerrt vdipeitl
//
LOCUS       WP_010526035             343 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Thermophagus xiamenensis].
ACCESSION   WP_010526035
VERSION     WP_010526035.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..343
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=37136
     Region          39..336
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mkkhpfsltr vivsstfill mvvscapkek wiknqgavfg tyyhlvyesp ggkdlqaavl
       61 qaldsvnhal stydsasvis rfnqsdkgia vtnhhfktvv eaaqaitkat dgafdmtvap
      121 lvnawgfgfs kkqtitphll dsltslvgmq kvllrgdsli klkpglmida saiakgygvd
      181 iaakvleing canylveigg evyskghnpq skpwrvgidk piddpaasnr qiqtvvnlsg
      241 kalatsgnyr qfyidentgi kyahtidprt gnpvnhslls asviandcmt adayatacmv
      301 mgleksmelf sqhpelegyf iydtpqgmkt ihtpgfekyl adn
//
LOCUS       WP_010526122             287 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF3822 family protein [Thermophagus xiamenensis].
ACCESSION   WP_010526122
VERSION     WP_010526122.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19234307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..287
                     /product="DUF3822 family protein"
                     /calculated_mol_wt=33028
     Region          21..283
                     /region_name="ASKHA_ATPase_BT3980-like"
                     /note="ATPase-like domain of DUF3822 family proteins;
                     cd24013"
                     /db_xref="CDD:466863"
ORIGIN      
        1 mmvpdlsivd etfdanisss yflsiqasld gfsfsildpi rnkyiqfssy alqdhitead
       61 lpkltnkvfe enellnlpfk kvfiliptry stvvpsglfn heeasqwlff thqvpgnykv
      121 vssqmklada wnifaipatl ydiferqfpe piifqqyvpm tesklaisrp gmgkiqfiin
      181 lqkdyfdvvv iennnlklcn sfqikgkndl lyytlfifdq lqlspsktdv qitgyhhnfn
      241 eikqtiekyv khvkfpglps gfqysylfks vpghryynll tlascvs
//
LOCUS       WP_010526141             129 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Thermophagus
            xiamenensis].
ACCESSION   WP_010526141
VERSION     WP_010526141.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..129
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14265
     Region          23..87
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mkrkmlsllt vfligsvamf aqsktekfev kgkcgmcesr iekaansveg vskadwdqes
       61 mmatvvfdks ktsvddiqka itkvghdtgk hkasdeaydk lpgcckyerm ekkdahgkke
      121 hnhdghsch
//
LOCUS       WP_010526067             440 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Thermophagus xiamenensis].
ACCESSION   WP_010526067
VERSION     WP_010526067.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..440
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=50933
     Region          19..427
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 mkqqlkeiil enqqfepgni ierepykipi ksgkiislvg arrsgktfml yqlvnqlrkn
       61 gvipekivfi nfederlnlq aadldlilqa yqelfpevdl rdaffffdei qnvkgwekfv
      121 rriydtkckn lfitgsnsrl lsteiatelr grtvsysiyp fsfsefvrah hgpsnlntts
      181 nragvihlae qfllgggfpe liafdhsfki kvlqeyfnvm iyrdiierys ianpevlkff
      241 ikkifaavtg tlsvnkaynd lksmgykisn kylyeyleyc navfltqsis rfdyseikqa
      301 ksdkkvyvid nglltavdfh issnrgklfe nmvalelikl gyqlfylknk vecdfivqeq
      361 dshsfipiqv afslqqhdtr kreisglina ckklklnhgy iitfdeeesl sfngcsvdvi
      421 pfyktffrte rlltnrplas
//
LOCUS       WP_010526153             291 aa            linear   BCT 01-JAN-2025
DEFINITION  pseudouridine synthase [Thermophagus xiamenensis].
ACCESSION   WP_010526153
VERSION     WP_010526153.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..291
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=33232
     Region          55..278
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 makkgkipgk ytsaarrsrn drfqehrphr ierssskeny tpkgdteftd ripatmrlnr
       61 fisnagicsr readnlikkg eikvngkvvt elgtivsihd vveyhgqkln pekkvyvlln
      121 kpkdtvttah dpqgrktvid ivknacpqri ypvgrldrnt tgvllltndg elakklthps
      181 feakkiyhvf ldkklklddf nilangiele dgpvrpdnis yvdpndhkqi gieihsgknr
      241 ivrrifehlg ykvekldrvy fagltkknlp rgkwrfltqq einflkagfk d
//
LOCUS       WP_010526187             409 aa            linear   BCT 01-JAN-2025
DEFINITION  alanine dehydrogenase [Thermophagus xiamenensis].
ACCESSION   WP_010526187
VERSION     WP_010526187.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Usha,V., Jayaraman,R., Toro,J.C., Hoffner,S.E. and Das,K.S.
  TITLE     Glycine and alanine dehydrogenase activities are catalyzed by the
            same protein in Mycobacterium smegmatis: upregulation of both
            activities under microaerophilic adaptation
  JOURNAL   Can J Microbiol 48 (1), 7-13 (2002)
   PUBMED   11888165
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Siranosian,K.J., Ireton,K. and Grossman,A.D.
  TITLE     Alanine dehydrogenase (ald) is required for normal sporulation in
            Bacillus subtilis
  JOURNAL   J Bacteriol 175 (21), 6789-6796 (1993)
   PUBMED   8226620
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..409
                     /product="alanine dehydrogenase"
                     /EC_number="1.4.1.1"
                     /GO_function="GO:0000286 - alanine dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0042853 - L-alanine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44316
     Region          35..408
                     /region_name="Ald"
                     /note="Alanine dehydrogenase (includes sporulation protein
                     SpoVN) [Amino acid transport and metabolism]; COG0686"
                     /db_xref="CDD:440450"
ORIGIN      
        1 mgdigksasq yfainqtglm pkeelleigk gqksmsfgip rehekgenri pltpqgvell
       61 tangheivie sgagnganyf dhdfseagak ivdnheepfr cdvvlkvapp neeerqlfsp
      121 gqllisllhi fkqdresiqq lmhkkinala yeflkdesnc ypvirsmsei egytaimias
      181 eylskekngk gvllggitgi spaevvviga gtagefavra alglgcqvkv fdnsyrnlre
      241 lernvgqrlf tsvlhpqvls kalksadavi sslryfdpqs rffiseeqia gmkpgsiivd
      301 lsmgnggcfd agcsskshgs avtiqhgvih yrvhniasrv artasialsn ifapvllrla
      361 msggvsqlik qdlgvshgly lykgiltnht lgerfnlpsk digllmaaf
//
LOCUS       WP_010526189             301 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Thermophagus xiamenensis].
ACCESSION   WP_010526189
VERSION     WP_010526189.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..301
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33942
     Region          115..299
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mgvnkrkafv qklrskykla vfneqtyeev lvirlsrlnv ftiigfsvil lvvlviflia
       61 ftglkeyipg ypdptqrlli vrnservdsl imeiekrnkf ienmkmiing evpnenpedt
      121 vatensdaig enlsddtsgw rsidftrsee dsmfralver eekftppqst eqvlnpllen
      181 tfffpplkgm vvnefgnpqr hfgvdivagp garvsavmdg vvifsgwtve tgyviqiqha
      241 nnfismykhn erllkstgdh vkageaiahv gnsgelttgp hlhfelwhng ipldpkeyis
      301 f
//
LOCUS       WP_010526231             234 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Thermophagus xiamenensis].
ACCESSION   WP_010526231
VERSION     WP_010526231.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..234
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25897
     Region          3..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mddtviliee lhkhyhlgnq vvkalngvsl tikkgeyvai mgpsgsgkst lmnligaldt
       61 pssgryilng ndvshmsddk laeirnreig fvfqtfnllq rysalenvvl plvyggvpre
      121 eryrrgkeal vnvgledrml hkpnelsggq rqrvavaral vnnpslilad eptgnldtkt
      181 sidimrlfdq ihaagntivl vtheediaqy aerivrlrdg riesdvmnea riqa
//
LOCUS       WP_010526253             784 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Thermophagus xiamenensis].
ACCESSION   WP_010526253
VERSION     WP_010526253.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..784
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87890
     Region          66..784
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mkfilfvslf iqfsifvnaq tgsirgriim pieeeapini gikgttigti tnangeylle
       61 nlrpgrytlq asyvgykpqe vvvhvvageq tiapaikmer tekeiaevlv vgnhqsdysi
      121 qepsqslrnn vpllkmsqnv qiiseevlad qqltemlesv srntsgaqmi ehwgtfarin
      181 mrgfkipafr ngmnvdlpwg pltedlsive riefvkgpag fmlssgepgg fynvvtkkpa
      241 ltpknnasvm vgsfntlrat idlgghfsgr nnllyrfnam astknshrdh efndrytlnp
      301 siqyhfsdnt titgeyiyqy srlsvvgaay vfapdgmgtl prdftlaepn idptdirehn
      361 lfvtlnhklg nrwqltaqlg yldyklvgss lwpdsvtsdg lvyrglgiwd aisnvksgqa
      421 yiegntftgk ighhilagid mnsktyyadw fqsgplagvn nplniynpvh yvptsqmpvf
      481 drslsirqra yngsypasqt iqsssayfqd eliffsdrlr ltlagrytny rtsvygantd
      541 dqvftpragi sfsfddntsv yglwdqtfip eagtdkegna fkpveaidme agikrkwgng
      601 kwissitffq itkqnvlttd pedvnyqiql geaqsegief dlqgnilpgl nlilnyaytd
      661 veitkdtnpe vvgtklagha rhmtngwlky ssngwlpkgw giglgyqyqv drsswswgad
      721 neamlpdyfr ldgalfwenn aiavrlnvnn lldeylysgg sygnfyywqt epginyrlsi
      781 nyrf
//
LOCUS       WP_010526270             778 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Thermophagus xiamenensis].
ACCESSION   WP_010526270
VERSION     WP_010526270.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..778
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88698
     Region          32..112
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          99..689
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mryyifliaw fymyfpiadv fgnrsfqkkv tvsgyvkdre tgemlvgati vikgtgkgtv
       61 tnvygyfsie iegenqilqf gflgyknlek evgessvitv elepitqelg evkikgegnv
      121 hssrypligl ekmesssirt ipvlmgetdp mkaiqmlpgv satsegssnf tvrggnpdqn
      181 lllmdeaivy naghllgffs vfnndavksi dlykgdfpas eggrlssvld vhtkegnmkk
      241 vkgsagigli ssrlnlegpv vkdkssffvs grrsyldlfl plapdeeihd nklyfydanl
      301 kfnwivnekn riflssyigr dvfsdklaql dygnttftfr wnhvfspslf anftlvrsry
      361 dyflgttend iddlewvsqf ndymlgadfs wyinpsqtfr fgnrtiyhri dpgdvsamde
      421 nsliqsiklp rnnslehgiy ishtsevvpw lvlrlglrys lfqnigkgkl fkfddsynvv
      481 dtiyyssgei fneyhglepr agvsilfssr wsaklsysrt rqyiqlasns tsstpldvwf
      541 psspnvkpqv adqvslglfh ssrnrvfens veffnkwmen tidfkdhpdl ilnetiesev
      601 rqgkawargf eimsrwntir fngwvgytfl kservapdin qgrpylshyd hthdlsafmn
      661 yrissrvsvs gnwvyytgap vtmpvgryev sgesvplyse rngermpdyh rldlsltlrs
      721 kkggkkggew ifsiynvygr knawainfvs deenpykira ektylfsvvp svsykfef
//
LOCUS       WP_010526329             404 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 27 protein [Thermophagus xiamenensis].
ACCESSION   WP_010526329
VERSION     WP_010526329.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Kitaoka,M.
  TITLE     Diversity of phosphorylases in glycoside hydrolase families
  JOURNAL   Appl Microbiol Biotechnol 99 (20), 8377-8390 (2015)
   PUBMED   26293338
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Naumov,D.G.
  TITLE     [Phylogenetic analysis of alpha-galactosidases of the GH27 family]
  JOURNAL   Mol Biol (Mosk) 38 (3), 463-476 (2004)
   PUBMED   15285616
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14423446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..404
                     /product="glycoside hydrolase family 27 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45915
     Region          31..302
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(38,73..74,114,148,150,182,201,205)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          315..400
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
ORIGIN      
        1 mnsktsclgi fiflfgiliq aqkfeklalt ppmgwnswnk fgcevneeli rsiadamves
       61 gmkdagyeyi viddcwqggr dslgfiypds akfpngmkal adyvhskglk lgiysdagtk
      121 tcagypgsrg yeyqdalqya lwgidylkyd wcnteninpi gaystmrdal ykagrpilfs
      181 mcewgtskpw ewakdiahmw rttgdificw dckhdhggwy swgvmkildm qeglrqyagp
      241 ghwndpdmle vgnglsvned rahfsmwaml aapliagndl rnmsketvei ltnqeviavn
      301 qdslgiqgfk ynsidsletw fkplsngewa vcflnrrdqp avikfdwkie nvvdeifgfe
      361 tafnetiyni rnlwdkknig ntkrvfkatv pshdvimlrl tplk
//
LOCUS       WP_010526363             614 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Thermophagus xiamenensis].
ACCESSION   WP_010526363
VERSION     WP_010526363.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..614
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=70406
     Region          12..609
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkrfiysflr aylfwlvffa ffrtlfiivn qsfiedtpit vllasywpgl rmdmsfagyl
       61 mllvivfqlf llplkkdfcy rcfkwvyyil ipifvglllg dinlfrywag hlnkeaisfl
      121 ktpdiifdsi hlgeailffv lcvvfswlwi flfnkvvikt afqskfnqkq iavnwlytll
      181 lgafmivpir gsfsvapint gvayfsgylf annaavnplw nlaysmkrna indggysfmd
      241 dqkaqerfnn lmhqsgkfpk ilntdkpniv villesfsaq aikklggqnv tpnlntlmke
      301 giffsnlysa sfrsdygivg vltgypgipg ysvmqypeks rhlnfipqkl kkagykdlnf
      361 lyggdmtfkn mkslivlagf dsitsiedfp akyrgkkwgv hdqytfekll nllensnnps
      421 fsffftlssh epfdvpmerv inddylnsvy ytdhclgiff dqvkkrglwd ntlfilvadh
      481 gvvgpeklgy tnarryhipm lwtggavavk dtvietvasq vdlaatllnq lnidasdfkf
      541 sknildesvn gfafvhypdg fgfidsnvfq mynknnfsvq vmsgaktked slkakvwmqi
      601 iakdfkerls newk
//
LOCUS       WP_010526471             232 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Thermophagus
            xiamenensis].
ACCESSION   WP_010526471
VERSION     WP_010526471.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..232
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26372
     Region          21..229
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mgqetinept ikdipqlydv ltpeeqqyle ahhttirykk nqiiyqegew ptgllcigkg
       61 kvkiykegil grdqivrmas gpgfigyral fanerhiasa vvfepcvifh iakdvimklm
      121 ksnndlcmni iksfatelgf arfrtvtltq khirgrlaes llllrdiygy eddnctlsiy
      181 lsredlanfs nmtasnairt ltafakekll tvdgriiril deeklerisr lg
//
LOCUS       WP_010526392             586 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Thermophagus xiamenensis].
ACCESSION   WP_010526392
VERSION     WP_010526392.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..586
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=66836
     Region          73..497
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          267..561
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mktfniiqii lviivgvsac ndelnvtnpn nqttydfgds kseleeavia cynrirlegt
       61 farvgytlda vrgdevwnss qqwyleydnl nspgtieigd lwpwrdfyhv vnrtnfvlsk
      121 vdkvdlteds ynkiagqalf lrslayyyla tyyqnvplii dysaysdint myasnntqde
      181 vfdqieedlk kamqmlpsrd eggewaqgra tcgaaagyla ralmfrhkye eayevlkdii
      241 agkyghyelt adygdnfreg peyennsesl fevqfmdygt ggtveewtpi nispeatqgh
      301 aiesnyasqe mgswgdlags pwlynlfkke rctdgrldpr lywtlvtyee eynsytglkt
      361 aaypdgdprc niiyqqeita tplsntsqgg isiakftnar tnlyksitng lhcginlrlm
      421 rysdvllraa eceneingpt qtaidyinqv rrragledlq lsdfptadhl feqianverp
      481 kefgcengrg idlirwgffy dedrlnqlie hgyykrdgta steeltaeta ddssfkyyyk
      541 gheyfpiyqs tlnanpnleg nsanknedng pafrekwtir pvield
//
LOCUS       WP_010526506             361 aa            linear   BCT 01-JAN-2025
DEFINITION  LptF/LptG family permease [Thermophagus xiamenensis].
ACCESSION   WP_010526506
VERSION     WP_010526506.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Owens,T.W., Taylor,R.J., Pahil,K.S., Bertani,B.R., Ruiz,N.,
            Kruse,A.C. and Kahne,D.
  TITLE     Structural basis of unidirectional export of lipopolysaccharide to
            the cell surface
  JOURNAL   Nature 567 (7749), 550-553 (2019)
   PUBMED   30894747
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..361
                     /product="LptF/LptG family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41504
     Region          3..359
                     /region_name="LptF"
                     /note="Lipopolysaccharide export LptBFGC system, permease
                     protein LptF [Cell wall/membrane/envelope biogenesis, Cell
                     motility]; COG0795"
                     /db_xref="CDD:440558"
ORIGIN      
        1 miikkldlyi lkkflgtfff aillilsisi vfdlaekidd fletnaplka iifdyyknfi
       61 pyfanlftpl fvfisvifft skmayqteii ailssgvsfr rlmfpyflga ailtlfsyvm
      121 ggyiippank vridfentyi kkiretgmsn ihmqiepglf iymrrfssfr ergddfslek
      181 iegkklkfki tartvqydst enkwifkdfv rrdfpdsggm vltkgeemdt vvnmkpadfi
      241 eerkffetmt npeldryire qqqrgvgnie pyliekhrri aspfsafilt ligvslasrk
      301 trggmglhig vgialsfsyi lfmtisttfa ingnlspmva twipnfvfaa igaylyfrap
      361 k
//
LOCUS       WP_010526524             542 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Thermophagus xiamenensis].
ACCESSION   WP_010526524
VERSION     WP_010526524.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..542
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60915
     Region          50..494
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkvkkykliv gffslllllg vactddldti pldedelvae ivygselgpy qesiakiyag
       61 laisgnsagd gdpdvagvdg gsqasflrgl wnlqelptde ahcawgdagi pelnnmtwgs
      121 gnvfikgfyy rlyyqinlan eflrqttddk lssrgvdest kavitqyrae arfhralayy
      181 ylldmfrnvp fvteenemgk dapiqksade vfdyiesell dceedmldpi vgydnanygr
      241 ahkaanwall srlylnaeay igepkysesi tyskkvldaq yelesvygnv fkadnhnske
      301 mifpiryegd dtqtwggmtf llsstipsdm qtevnavgaw qgnrarssll etfeqesdke
      361 ldarfsmlel eytenveies pslfkdngip vvkyynvysd gtyppsniay tdfplfrlge
      421 iylnyaeavl rggsggdett alqlindlra raygenssla titssdltld fifeergrel
      481 fyeahrrsdm vrfgkftgss yiwpwkggvq egrsvdsyrd vypipsddmg snlnleqneg
      541 yk
//
LOCUS       WP_010526533             133 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Thermophagus xiamenensis].
ACCESSION   WP_010526533
VERSION     WP_010526533.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..133
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14747
     Region          1..131
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 meylgsclcq gikfkvtgdf esfylchcny crkdtgsaha anlfsstakl ewtkteteir
       61 ifqppeskhv kafcancgsa lpnvqmdgkl ivvpagcldt klekrpdahi ftaskacwdd
      121 alddiksfkr fpe
//
LOCUS       WP_010526577             978 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Thermophagus xiamenensis].
ACCESSION   WP_010526577
VERSION     WP_010526577.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..978
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=109301
     Region          1..528
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          480..976
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mkpladilsl rikgkvftde liralyatda svyremplav vfpqdeedir qlilfarenk
       61 valiprtagt slagqvvgng ivvdvsrtft rilevntaes wvrvqpgvvr delnlylaey
      121 glffgpetst snramiggmv gnnscgansl vygstrdnil evtgflsdgs kvvfkeltvd
      181 efaekslssd dsleaaiyrq ingmlsnpvn qkkieqsfpk ssvhrrntgy aldvlarsap
      241 fksggpninl aqliagsegt lmfiteiklk chslppkekg vlcihfhsve ealkanlaal
      301 rhrptaselm ddfilnctkn npeqnknrff idgdpkallv veftkptkee ieaaahlltd
      361 elkkaglgyh yplvtgtdik rvwslrkaal gvlfttpgda kpvaviedts vaaedlpnyv
      421 tdikkmlqsl nttcvfygha gtgelhlrpl inlktgeghk lfrkiaedta klvkkyrgsl
      481 sgehgdgrlr gefirymvgd eiysffkelk rtwdpnhifn pgkivetppm dtslrynast
      541 etpeietifd fsrergyira aefcngsgdc rkthlsggtm cpsymatrde mhttrarani
      601 lreylrkpyv knrfnhyeiy rvmdlclsck acksecpsgv dvtklkaefl qhyyeangvp
      661 frtrlianis rlnalaslap alynfvvtns fttkvlkhla gfaskrslpl lnsttlsrwy
      721 rkekrmlarp ssskgkvlff ndeftnynda eigrkavlll nklgyeviip phvesgracl
      781 skgllkkarn iaieninqls qwvseevplv glepsalltf rdeyidlvpd emkplarnia
      841 rnallfeefl lrevkkgnvs selfvkehrk illhghchqk slasveptvk mlslpenykv
      901 evipsgccgm agsfgyekeh yevsmkigel vlfptirkke aetlvaapgt scrhqikdgt
      961 gerayhpvei lydalrek
//
LOCUS       WP_010526602             255 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Thermophagus xiamenensis].
ACCESSION   WP_010526602
VERSION     WP_010526602.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28657
     Region          1..237
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mievknvyks fdgvevlknv sarfepgkvn liigrsgsgk tvllksivgl hevdkgeiiy
       61 dgrsftnmse kdrkqirkei gmlfqgsalf dsktveenvr fpldvfsdls vaekkertnf
      121 clkrvnlena nnlypselsg gmqkrvaiar aislnpkylf cdepnsgldp ktaivideli
      181 yeitkeynmt tiinthdmns vmgigekiif isegqkvweg snneilisdn kqlndfiyas
      241 kflkqvregf lkkgi
//
LOCUS       WP_010526621             598 aa            linear   BCT 01-JAN-2025
DEFINITION  V-type ATP synthase subunit A [Thermophagus xiamenensis].
ACCESSION   WP_010526621
VERSION     WP_010526621.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF003220.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK04192
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..598
                     /product="V-type ATP synthase subunit A"
                     /EC_number="7.1.2.2"
                     /calculated_mol_wt=67217
     Region          6..585
                     /region_name="NtpA"
                     /note="Archaeal/vacuolar-type H+-ATPase catalytic subunit
                     A/Vma1 [Energy production and conversion]; COG1155"
                     /db_xref="CDD:440769"
ORIGIN      
        1 mekndkttgt vtgiianlvv vdvngpvgqn eicyilhnqe rlmaevikit ekqayvqvfe
       61 ntrglkpgsk vefeghmlev tlgpgmlsrn ydglqndldk megvflkrge ytdpldrekk
      121 whfiplaseg deviagdwlg eveengmphr imvpfklqgs yivksvakeg dytvddeiav
      181 iestngesis vnmvqkwpvk ipiktykekp rpfklletgv rcidtlnpit eggtgfipgp
      241 fgtgktvlqh aiskqaeadi vimaacgera nevveifkef pelddprtgk kliertiiva
      301 ntsnmpvaar easvytamtl geyyrtmglk vllmadstsr waqalremsn rmeelpgpda
      361 fpmdlsaiis nfysragfvr lnngktgsit figtvspagg nlkepvtent rkaarcfygl
      421 sqdradskry paidpidsys kyleypelqe tlsktlgeqw lsnvlkakdv llrgreaneq
      481 inilgddgvp idfherfwka elidfvilqq dafdqidast plerqkymle kvlsivdaqf
      541 nfnhfeevgn ffkrvinqlk qmnysefkse qfnnfekeld dilnefsiea eetqqata
//
LOCUS       WP_010526664             102 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Thermophagus
            xiamenensis].
ACCESSION   WP_010526664
VERSION     WP_010526664.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..102
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11906
     Region          3..95
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mvklvwtela tkdleeifny iakdsvryas fsvnkiynra qdiiynpyvg rvvpeinnkv
       61 irevisgnyr ivykivnefq vdilrvyhsa rllkadrldk pi
//
LOCUS       WP_010526689             464 aa            linear   BCT 01-JAN-2025
DEFINITION  aminopeptidase P family protein [Thermophagus xiamenensis].
ACCESSION   WP_010526689
VERSION     WP_010526689.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..464
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52015
     Region          7..124
                     /region_name="AMP_N"
                     /note="Aminopeptidase P, N-terminal domain; pfam05195"
                     /db_xref="CDD:461581"
     Region          172..446
                     /region_name="Prolidase"
                     /note="E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase,
                     X-Pro dipeptidase, proline dipeptidase., imidodipeptidase,
                     peptidase D, gamma-peptidase. Catalyses hydrolysis of
                     Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline
                     analogs. No action on Pro-Pro; cd01087"
                     /db_xref="CDD:238520"
     Site            order(231,248,260,343,392,432)
                     /site_type="active"
                     /db_xref="CDD:238520"
ORIGIN      
        1 mfskdiyinr rnklkklvks glilvlgned apmnytdnty hfrqdstfly ffgidlqgla
       61 gvidldnnre ilfgddfsid diiwmgpqps lreqaskvgi sdtrpakelf sfikdalkqk
      121 rkihftppyr frnimkladl lnihhnevkn hasleltkac ielrsikepc eieemerhms
      181 varemhttam kmaspgiqeq kiagvlegis msgggiisfp vicsvrgetl hnhyhgnilk
      241 egdlllvdag sespkhyatd htrttpvsgk ftdlqrqvyq ivldandkvr eatrpevpyr
      301 dihllackvi aaglkdmglm kgdieeavaa gahalfmphg ighmigldvh dmedyndtlv
      361 gydeeikrst qfglsalrmg rrlkpgftit nepgiyfipa lidkwkadkk ftqfinydkv
      421 eamkgfggir leddilvtes garilgqrip itveeveqia gsgv
//
LOCUS       WP_010526690              96 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Thermophagus xiamenensis].
ACCESSION   WP_010526690
VERSION     WP_010526690.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 96)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 96)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..96
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11219
     Region          5..89
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 medkdlilnk narrfelpvk ghmatlyyev yqpsvwqlth tlvpdplkgq gigtylvekv
       61 leycqkhqir iipecsfvia fiqknpewkt llfeqe
//
LOCUS       WP_010526695             429 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Thermophagus xiamenensis].
ACCESSION   WP_010526695
VERSION     WP_010526695.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..429
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=47761
     Region          11..418
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mfeklknkea klsviglgyv glpialefar kmkvigfdik pdriekmkqh idpsneleas
       61 afegcdikft snpedlkeac fhvvavptpi nkhnlpdlnp llsatrtvgk alkkgdyvvf
      121 estvypgcte edcvpvleqe sglkfnvdfk vgysperinp gdkehtltki lkivsgsdpe
      181 aleeisavyg siikagiyka ssikvaeaak iientqrdvn ialmnelsli fnrlnintye
      241 vleaagtkwn flrfspglvg ghcigvdpyy ltykanelgy hskiitggrf indamgpyia
      301 kqvvkklisk ghkingsrvl imgatfkenv sdirnskvad vynelksfsv nvdvtdphas
      361 skelmeeygy glvdkidkky havilavnhd eymkldevyf ksitvddplf vdvkgvfrgk
      421 iremtywsl
//
LOCUS       WP_010526696             338 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Thermophagus xiamenensis].
ACCESSION   WP_010526696
VERSION     WP_010526696.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..338
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38532
     Region          4..258
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mstkktvkfa ivglghigkr hakmiednpe aelsavcdvr speetgwqnp nipyyrdfte
       61 mlkklkecdv vnictpnglh alqaiealkh kkhvvvekpm alskadaeki iykalqvsrh
      121 vfvvmqnrys ppsvwlkevm dkkvlgkiyf vqlncfwnrd dryylnnswh gtadmdggtl
      181 ftqfshfidi lywlfgditd ieakfgdfah qhstafedsg svifrfvngg mgninystav
      241 wdrnlestmt iigekgtikv sgqymneite chikdyqlpd lepvnppndy gpykgsaanh
      301 qyvienvvqt lkeqtyvhtn aleglkvvdi ieriyqkk
//
LOCUS       WP_010526724             226 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Thermophagus xiamenensis].
ACCESSION   WP_010526724
VERSION     WP_010526724.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..226
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25437
     Region          147..225
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mevkkspkad lenkktvfmq iglvvvlslv fiafewttqe tkvneglkie eeeveeeiip
       61 itrqdevkpp ppppppkvtd ilniveddve leeeliiqdt eatedtevdf tdmtteeeee
      121 dapvffivee mpefpggeqa lhkflasnie ypviaqengi qgrvyvkfvv ntdgsitdve
      181 iargvdpsld kealrvvrsm pkwkpgkqrg kavrvsytvp infvlq
//
LOCUS       WP_010526764             403 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Thermophagus xiamenensis].
ACCESSION   WP_010526764
VERSION     WP_010526764.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..403
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42736
     Region          1..399
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mdvllitgii ifagfllgel aakislpkis gyivagilln pkvfglipas fieagtplvn
       61 vslavitfhi ggslsfekik rdgrnyfimt lgesilayls vgllvfvtve ylfhlfdsvy
      121 lslalsvila slaaptdpsa tlavigeyka kgpvsstvlg iaafddiagi vlftlsvafa
      181 kilmgnsdas liytlgqmiv niglaigmgi afgfllnlls rffkretdgg livlilgvlm
      241 lcygtssylr vdellstlam gvtvvnyntq ndkifcvver yteelifvif ftlsglhldv
      301 sllsgnvvlm vvfilaraig kylgivssss mlkvsptvkr ytaggllpqg giviglallv
      361 akesefqqls slimtvvigt aiihelvgpv askfslkkag eik
//
LOCUS       WP_010526830             275 aa            linear   BCT 01-JAN-2025
DEFINITION  ester cyclase [Thermophagus xiamenensis].
ACCESSION   WP_010526830
VERSION     WP_010526830.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..275
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31948
     Region          40..165
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mkqvnqfifg vvmilnqnal sqsnqllmse pmqeisnkki iqclyydvln qrhyqkleei
       61 vskdysnikg etgidgfkkn vvefiqafpd akwtitemia egnkvfvkqk vegthkdffq
      121 nipptnqfit segmgfyvle dgkiimhqvq tnqlaffqql glipttlsli dsnavyfvdr
      181 fimpkssfpr ffekmemnrr fiknlegfis devmlkeeng niivmtvavw ennqaldkak
      241 slvkeeyqri gfnpaeffqr lnitkqretf ksieq
//
LOCUS       WP_010526956             156 aa            linear   BCT 01-JAN-2025
DEFINITION  regulatory protein RecX [Thermophagus xiamenensis].
ACCESSION   WP_010526956
VERSION     WP_010526956.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Ragone,S., Maman,J.D., Furnham,N. and Pellegrini,L.
  TITLE     Structural basis for inhibition of homologous recombination by the
            RecX protein
  JOURNAL   EMBO J 27 (16), 2259-2269 (2008)
   PUBMED   18650935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..156
                     /product="regulatory protein RecX"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /calculated_mol_wt=18368
     Region          2..150
                     /region_name="RecX"
                     /note="SOS response regulatory protein OraA/RecX,
                     interacts with RecA [Posttranslational modification,
                     protein turnover, chaperones]; COG2137"
                     /db_xref="CDD:441740"
ORIGIN      
        1 mdfktalnka sslcsrqeqc cfdirkklqk wnvlpddqek ildllvqekf idesrfatsy
       61 vrdkfrfnnw grekirwqlk qkgisnenid halaqidede ykktlssllk kkkeqlknte
      121 fnkvkaalir navskgfemd iifpiveqll lknqkn
//
LOCUS       WP_010527028             249 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Thermophagus xiamenensis].
ACCESSION   WP_010527028
VERSION     WP_010527028.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..249
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27080
     Region          1..241
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mqekiidvkn lsvsfderqi ledvsfsvnq geiavilges gsgkstilkh mlglfplapg
       61 tvtifgqdia eldediamkf yrklgvfyqn gallnsltva enialpleqh tdlpadiied
      121 lvrtklslvn lnhafhlyps qlsggmlkra aparaiimdp pllfcdepga gldpvslatl
      181 delilnlrdq lgmtvvmvth evtsilrian kvifvnkgri afegsleeaq isdvpelraf
      241 frvgtggkk
//
LOCUS       WP_010526487             584 aa            linear   BCT 01-JAN-2025
DEFINITION  LamG domain-containing protein [Thermophagus xiamenensis].
ACCESSION   WP_010526487
VERSION     WP_010526487.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Hohenester,E.
  TITLE     Structural biology of laminins
  JOURNAL   Essays Biochem 63 (3), 285-295 (2019)
   PUBMED   31092689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Sasaki,T., Fassler,R. and Hohenester,E.
  TITLE     Laminin: the crux of basement membrane assembly
  JOURNAL   J Cell Biol 164 (7), 959-963 (2004)
   PUBMED   15037599
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10597119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..584
                     /product="LamG domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=63693
     Region          186..354
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Region          405..577
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
ORIGIN      
        1 mktlklifas llvlsffnac dqqyiddisk vepgedesap eitvnfppeg yelqtndava
       61 sitfdfevrd dieiasvsle ldgveiasft dfkdyrvfme eytydevttg shvftvkatd
      121 legktsevni nfkksppyvs eyegeifymp fnneyremns lslatvvgnp gfaegilggt
      181 ayqgatdsyl tfpasvlega tavsasfwlk idasadragi lvvsppadnn ndrtkgfrlf
      241 ressndgatq rfklnvgtgd seswfdggta advevntgdw vhlafsiset yaalyingei
      301 vadgafdgid wtgcdvisim sgapnwtewn hlsdvgqmde lrifnkaltq deiktimlkd
      361 easfymdfdg dyqdaisgid atvvgspsfe ygggisgday kgaadsyltf saedlniqsd
      421 efsasfwlni ndaaeragil vmgpedadsp daqndrtsgf rffreatndg atqrfklnvg
      481 ngtadswfdg geaadvtpnt gewvhfafvi gnsearvfin gtevsrgvfd gidwtgcdll
      541 simsgsprfn gwghtsdqsl mdelylfpqa ltedevallm ndgl
//
LOCUS       WP_010527029             353 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Thermophagus xiamenensis].
ACCESSION   WP_010527029
VERSION     WP_010527029.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20324114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..353
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38746
     Region          6..79
                     /region_name="MlaB"
                     /note="Binding protein subunit MlaB of the ABC-type
                     intermembrane phospholipid transporter Mla, contains STAS
                     domain [Cell wall/membrane/envelope biogenesis]; COG3113"
                     /db_xref="CDD:442347"
     Region          99..353
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mlnnkltisn taeflhdldn lfrktketnl tidlaklnei dsagslaihq lpeiaakyhi
       61 sikienadek ikrkmelfrp vavnftnpre kkeglfmvlg ektshfftey visflylvsd
      121 ilywsikdlf srkhrrkgev inqaisigvn alpivmamaf iiglvlalqs sfqlrnfgan
      181 vyivdltvia mmaemgplit aimvagrsgs siaaeiatmk vtaetdalqt mglnpirfvv
      241 ipkiygslit lpfltilacm agiiggavaa nfylditpei ffnrmplvly qkdiltgifk
      301 slcfafiivi tgtffgfkvk egaegvgkst tsavvaaial viiadlvlgi lfy
//
LOCUS       WP_010526809             285 aa            linear   BCT 01-JAN-2025
DEFINITION  GIY-YIG nuclease family protein [Thermophagus xiamenensis].
ACCESSION   WP_010526809
VERSION     WP_010526809.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Dunin-Horkawicz,S., Feder,M. and Bujnicki,J.M.
  TITLE     Phylogenomic analysis of the GIY-YIG nuclease superfamily
  JOURNAL   BMC Genomics 7, 98 (2006)
   PUBMED   16646971
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10179942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..285
                     /product="GIY-YIG nuclease family protein"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32189
     Region          53..130
                     /region_name="GIY-YIG_unchar_2"
                     /note="GIY-YIG domain of uncharacterized hypothetical
                     protein found in bacteria and archaea; cd10447"
                     /db_xref="CDD:198394"
     Site            order(53..55,69..71)
                     /site_type="other"
                     /note="GIY-YIG motif/motif A"
                     /db_xref="CDD:198394"
     Site            order(55,69,71,79,83,112,129)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:198394"
     Site            112
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:198394"
     Region          223..276
                     /region_name="DUF4357"
                     /note="Domain of unknown function (DUF4357); pfam14267"
                     /db_xref="CDD:433823"
ORIGIN      
        1 mknygkkitl flidgvpngr itcelsnwtg kaykipriyl sdsskreelk kpgvyllfgk
       61 deanndkvyi geaeviydrl kqhlsqkdfw netiafiskd enlnkahiky lesrlfgiak
      121 nvkrykieng atptmsaise adkaemeefi enikmltntl ghkvfeeite qlnkkakkif
      181 einaargaka kgiatsagfv vlkgsqials tvpsypkpfe qirnnlinrg tlkrenekli
      241 ltedyefssp staasivmgr nangltewkf kdgttlkdfe srndk
//
LOCUS       WP_010527038             168 aa            linear   BCT 01-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Thermophagus xiamenensis].
ACCESSION   WP_010527038
VERSION     WP_010527038.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..168
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=18156
     Region          2..111
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 minkvilign vgkdpevryf dnnegvanfp lattepgftt rdgrqipert ewhniqvrrg
       61 lvkvaetyik kgtqlyiegk lrtrsyeqng vtkyitevvv dtlkllgrka dnpaaantsa
      121 aasssaptst pasegspfap pqsappmnee gftsgdegls qeeddlpf
//
LOCUS       WP_010527113             506 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Thermophagus xiamenensis].
ACCESSION   WP_010527113
VERSION     WP_010527113.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..506
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57736
     Region          62..457
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkminilikg fgifllliis fscsldkdpl sefsevtigs sdddgdrikf etrsemltqy
       61 egmyelfrsr qehwyldylm itevrsdnay agtvgaevmp fennsldggn svitrdwnry
      121 lediayvnsi ienidlvpdp sfseeeraqw kaeakifram vmldmvrfwg nipvitkeae
      181 ditaenieev yptyfpsqnt peeayqqivd dltsaipdap eagddktilt kavarsllak
      241 ayaekpirdy dkvieycdav iadgfqlvdd ysllfrmnea gtdiearnts esifevqfft
      301 gsgnwvtwmf grnlldwdqn fswakwvtps rdliaafede nddirmgqsi vyydcnwsly
      361 ypsdyypfmy kirsgnnsii klrladimll kaealawkge lnaaadivdq irarvdlpgl
      421 sesvkasqes mieavlnerr lelafeghrl fdlirngklq svmnsvndrd sgrlsqsrpf
      481 tedsellpip qtvldantnl vqnpgy
//
LOCUS       WP_010527123             604 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Thermophagus xiamenensis].
ACCESSION   WP_010527123
VERSION     WP_010527123.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..604
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=69788
     Region          62..>471
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mykkvllfft amwtfgilvq aqwkpvgdki ktawaeevnp knvwaeyprp imerthwknl
       61 nglweyaits kescepknfd gqilvpfave sslsgvqkrv geenilwykr tfsipedwke
      121 krillhfgav dwraevwlnd vkigmheggy tpfsfditpf lkvgeqelvv kvwdptdkgp
      181 qprgkqvsrp ggiwytpvtg iwqtvwlepv gdkyisavrt tpdidhnive vkalvagady
      241 gdvlevqvke ggkviktvra svpnpveikl enpqlwspef pflydlevvl lnkdreldrv
      301 ksyfamrkvs igrdekgimr lqlnnknyfh fgtldqgwwp dglytapcde alrydiqktk
      361 dlgfnmirkh vkveparwyt hcdrigilvw qdmpngdagp gwqnktyfkg senqrsphse
      421 niyrkewkei idylysypsi avwvpfnesw gqfktveiae wtkqydptrl vnpasggnhf
      481 qtgdildlhn ypepdlylyd aqratvlgey ggiglpikgh lwakdrnwgy vqfksskevt
      541 deyvryakkl kelvksgfsa avytqitdve vevnglityd rkvvkveepr irkinqevis
      601 vvsd
//
LOCUS       WP_010526837             962 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Thermophagus xiamenensis].
ACCESSION   WP_010526837
VERSION     WP_010526837.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 962)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 962)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..962
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=111780
     Region          25..959
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 msfflerlae yylqkystdi sdfcfvfpnr ragvffrrhl qnkspkpifs peiltindff
       61 fyfdkrpvsd nislifklyq sykevidpkt tiddfipwge mclsdfddid kyladpnqif
      121 knmadlkale ddfshlnqeq idairtfwss fdpkrlsqlq ksflelwerm pllyehfndr
      181 ldrdreiyeg klyrsvaqki knktigevpf srvifaglna lnncekllln ylktqniadf
      241 fwdypqwilt npakpnekis lfgeheaarf ikqnlqdfpm psdwesptcn gpskiiiaqa
      301 andleqtqia aqflkdisdn qedsdhtkta vvladetlml pvihaipsqw ksinvtlgyp
      361 lkntpaysli dalmtlqrtt rttangktwf yhrhligllr hqyvspllgd krdqlinqli
      421 kankvfiekd qipendfikk tltkvetiea lssyfmeill lvykslkerp dtdfeqefvy
      481 hlyltikrlg eilgklnepi stdtwyrlfr kltdfstipf kgeplnglqi mgiletrvid
      541 fdnliitsmn egtfphtspp nsaipynlrk gfglptidhq dsifayyfyr lihrakkvil
      601 iwsasdanqq tgemsrflhq lyyefhgkvv tqtyvrkagt kalpqimaek nkqvmvqlsa
      661 flhehnrals psalstyvec plrfyykylv gakepedise eldprifgnl fhqtvealyk
      721 pfmgqiised ilkqiaqpdn lrntlkeifs lnvpfikqkq nvfidlqgkn slvfevliry
      781 ltgffqneik kvpfvikgle ysmgmvfktp sgrsvylggn idrleekegt lkvvdyktgk
      841 gtnrindies lfdsskhpen kaifqtllys lmveeqtrra psaiqpsvvw mrklftdsds
      901 nlylqpvrgk kevitldlvk tvfvdslgkl ldelfdphmp fkqtpeeknc nyciykeicl
      961 kg
//
LOCUS       WP_010527128             523 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Thermophagus xiamenensis].
ACCESSION   WP_010527128
VERSION     WP_010527128.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (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   5  (residues 1 to 523)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..523
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60963
     Region          38..475
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkkliiyifs lgllissced ivdvsnpnni evrsfwqnea davsgvnaiy nmfykpgtys
       61 rwiwfrfdla sdegfssspw ielaewtrfi ynnynfwegn gwtyrdcyea ifranqvlyy
      121 vpgiefqdqa skdqvlgqay flralyyynl ailwgsenns lpivlepskp gdtpeghpvs
      181 dvweqvendl qnaiemlppq wddnnlgrat kgaayalrak clmqqhkwde alqdlewlvn
      241 gdgaqyydlv pnykdnfthf nennmesvfe iqysdihkap agdgdfdidp nlglnrgqff
      301 appgigwtdg earpwiveef rkelnldggy dirlkeslfy eqmaedfpgn dkiyrfgmev
      361 wnqdnyrnrv firkygtdyy rdyddyhspv nvrliryadv llmyaecian lpsgnldeav
      421 amvdrvrsra nmpklevnyp eatltkevfl krlqmersle lcfeghrwad lrrwglmenq
      481 egvnelaqrd pdfnnfvvgr hdclpipsse vnnnenldqn pny
//
LOCUS       WP_010527157            1058 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Thermophagus xiamenensis].
ACCESSION   WP_010527157
VERSION     WP_010527157.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..1058
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=116848
     Region          1..1037
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msifktsink pvttalifva vmvvglfslk qlpidqypei dppyisvmts ypganaseve
       61 tnvtrllens lnsvdglknl tsksqdnmsl itlefewgln ldevvndvrs yidmtkdelp
      121 dgagtplifk lstssmpimm yavtakesya gldkllndiv mpqlnrvdgi gnislsgspe
      181 rriyvdidqe kidaygisle dvgtaisnnn instsgtvkm nkeqyqlelr sefvesdein
      241 nivvatyddg rqifvkdlat vrdtikdltl dekidgqdgv rvviskqsga ntvevcekvn
      301 remakikell padvdiriif dssdnikdsi rsleesimya llfvvlvvll flgrwratli
      361 igitipialv vsfiylafvd sslniislss ltvaigmvvd daivvlenit rhiergsspr
      421 eaaiyatnev wvsviattlv iaavfvpltm lgglagimfk elgwivtivv vtstlvaisl
      481 tpmlsskllk srpvkvdefg hlifeeprkn wyqkyvvgal dridawysrv lrfslthkkl
      541 tmgvvlvvff ltllpmflgl igtdfmqqsd hgrltvtvel nrgtrieetl ktarklearf
      601 lelapeikii stsagsrdda sisalfsstn nntismvvvl kdkdqrersi fetaeilrqe
      661 manypeiiey qaqvasgmgg ngpstvdvei yghdfdqtni laekiqriiq ekvegardvt
      721 isrdedrael kinvdkekia rhgldastva tlaynrvtgm tagylkedgd eyaivvrlle
      781 edrnsisdie nlsiptvkgn iklsevadve eywapptier ksrqrivtvs atpfkislge
      841 lavdikaale qvdvpqgiti rlagdyedqq etfadmglll llivllvyiv masqfesmsk
      901 pfiimmsvpf aisgvvlalf vtgisldmig algvimlvgi vvkngivlvd yinlmrdrgy
      961 elneaialsg asrlrpvlmt afttilgmlp malssgtgse awrpmgvvvi ggllvstfvt
     1021 livvpllygi mskhgerdkn eqkrkefffl qiaddedk
//
LOCUS       WP_010527180             239 aa            linear   BCT 01-JAN-2025
DEFINITION  (Fe-S)-binding protein [Thermophagus xiamenensis].
ACCESSION   WP_010527180
VERSION     WP_010527180.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..239
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27139
     Region          <5..238
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mtvdlfipcf idqlypdtaw nvvkilekag vevnynsrqt ccgqptfnsg ywkesrkiaq
       61 kfirdfsndr pivvpsasca gyirnhypkl fkddasmqde vnrvcknvve ltdflvnhlk
      121 kenfeasfhh kvtyhdacsa lreygikdep rrllshvegl efkelpentt ccgfggtfmv
      181 kfvpvstamv eqkvenalst gaeyivstea scllniqsyi rkhdlpikti hiadilarf
//
LOCUS       WP_010527332             768 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Thermophagus xiamenensis].
ACCESSION   WP_010527332
VERSION     WP_010527332.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..768
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=87056
     Region          3..732
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mksylehlne aqrkavvete gpaliiagag sgktrvltyr iahlisqgvp pwsilaltft
       61 nkaareiker ishivgqela akiwmgtfhs ifarilrmea ehinfpgtft iydttdaksl
      121 insilknmkl nkekaykpgt ilgrissakn dllvpaayaq dakrsmadaa anipmmpeiy
      181 eryvrecrka gamdfddlll ytnilfrdhp evlanyqerf ryilvdeyqd tnfsqyliir
      241 klagkhknic vvgddaqsiy sfrgarieni lnfrndypdy klfkleqnyr stqtivnaan
      301 sviekntgqi rkkvfsqnde gakitviqah sdvdegfiva nhinemrlrh ryqfqdfail
      361 yrtnaqsrif eealrkknip ykiygglsfy qrkeikdila ylrlavnphd nealkrviny
      421 pargigkttl dklealanhy nvslwnvltn pglpqagfhs gtvkklnaft nlisgfisqv
      481 pnmsafditn eiasqsgilk elhqdkshes qtrlenleel fnairefsdn keesgenngl
      541 vdflqevsll tdqdtekpdd inkvtlmtih sakglefktv yivgieeglf psamastsea
      601 gleeerrlfy valtraqera tltfarsryk fgeltfarps rflgeidqsy ldisagansf
      661 dpanafssvs erserksfnl krnnvskpqf rfseeklkkq saspsfhfsd hdsssqiqpg
      721 vivehqrfgr gkviqvegee pnikatvdft nagkkqlllk faklkiit
//
LOCUS       WP_010527352             171 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma carbonic anhydrase family protein [Thermophagus xiamenensis].
ACCESSION   WP_010527352
VERSION     WP_010527352.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..171
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18278
     Region          4..171
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 maliksvrgf tpkigknvfl adnatiigdv emgddcsiwf navlrgdvns irignkvniq
       61 dgsvlhtlyq kstieignnv sighnvtihg akiednvlig igatvldhav vgsnsivaan
      121 slvlsgtkie pnsiyagvpa kkvkdiepeq tqeminkian nylmyagwyk d
//
LOCUS       WP_010527473             290 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Thermophagus xiamenensis].
ACCESSION   WP_010527473
VERSION     WP_010527473.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..290
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31648
     Region          4..289
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mglniivlak qvpdtrnvgk damkadgtvn raalpaifnp edlnaleqal rlkekypgtk
       61 vtlltmgpgr aaeiireglf rgadggillt drafagsdtl atsyalscai rkiktydlil
      121 agrqaidgdt aqvgpqvaek lglpqvtyve eilsaekgkl rlkrrlergv etvetpmpvl
      181 ltingsaapc rprnarlvmk ykhartvter qnlsedyidl andrpylnip ewsvndiecd
      241 anslglsgsp tkvkkienvv fqakearhiq aneqeieelv kelianhtig
//
LOCUS       WP_010527440             647 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Thermophagus xiamenensis].
ACCESSION   WP_010527440
VERSION     WP_010527440.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..647
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=74951
     Region          113..539
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          299..623
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 migkiklmte kvlviiiiqf tlgcsedflk pdplsfyepa ktfttragle salamadrhl
       61 rtywsfyssq drslpistey ifselavysm tdngniftdi antltptngi gngdnnrmay
      121 fwdetyngik yantiinfid qvegldddtr keflgrayfh rafryfalvf qfkdvplvtk
      181 ilevpklnyr sttreailem itkdlekave wvpeqsemdl tgmiskgacr qllikcylat
      241 grwedaieqa dilinnsgys lmmepfgnfi spqentwpit rnviwdlhrp enkcipanke
      301 vilgmpnrag tdaeikmrmm rnylplldnr welkspagin airyyapadn nfdpkldyvt
      361 aygrgiahmr ptsyytqslw yidgvedtgd lrhnskvgnw mrmdslkynn radsewygkn
      421 lrlydddgni lcadtircwf dwphykiyvp dpeelvptna nhrggagdwy cyrlaetyll
      481 raeakfylgd iagatadvni irershcdrl ystvtigdim derarelyle ewrhmelsrv
      541 syclalsgka defgktysid nlsndsywwq rvsnyndfyn kgavvwqqgn rpytiaphni
      601 ywpipnwain snrdgilrqn pgydgyddsv pvwdnwedav adeekie
//
LOCUS       WP_010527487             313 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Thermophagus xiamenensis].
ACCESSION   WP_010527487
VERSION     WP_010527487.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..313
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36647
     Region          1..193
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mlisiiipay nvenyieecv hsafsqtwpe kevicidnns tdgtwkklqq lqhqypelii
       61 dkelkagapa arnkglrlsh gqwlqfldad dllmpgkieh qqkqiqqnpk ssfiagacik
      121 rdlkgietkh iprhdhplks lfitqlgits snlwnrtlie qvngwdeslk ssqeadlmfr
      181 llqvndqvif ddepltivre rpsgqisqtn pkekwmryfn krlemvrwid qhrpelyike
      241 kdffmdnlfg llkiignedl naacqlyrqh lkgryrpspn qnhsthpylw lyksfgfrga
      301 eicrkwqnrl lgr
//
LOCUS       WP_010527518             197 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Thermophagus
            xiamenensis].
ACCESSION   WP_010527518
VERSION     WP_010527518.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..197
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22383
     Region          9..177
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mkqltikgek vlnvpnllsl yrllvfpvil ymaltgrest fvvllcislv sdildgniar
       61 ifhlqthfga aldnladivt yamallglfl fkwtdiepha wvlylfltvf visyfvsfvr
      121 fgkipglhly savsagylqg vfffvlfvyg fipwfyylav gwgaiayiek ifvllklddi
      181 kigvkglywl mrdsgkr
//
LOCUS       WP_010527570             248 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Thermophagus
            xiamenensis].
ACCESSION   WP_010527570
VERSION     WP_010527570.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..248
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27428
     Region          3..237
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mdskqplasi knvsvgyggt pvltdvnldi ypldfigvig pngggkttls kvllgilkpy
       61 rgrvlfpsgr inigylpqis ridrsfpitv kevilsgvss rrnwwkslft ktegiaekll
      121 delglegyed raigqlsggq lqrvllarai vnnpqllild epntfvdrnf eaelykiler
      181 lnkrmsivli shdigtissi vktiacvngt lhyhpsnelt eevlhiyncp idlithgelp
      241 hrvlkqhs
//
LOCUS       WP_010527609             440 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Thermophagus xiamenensis].
ACCESSION   WP_010527609
VERSION     WP_010527609.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..440
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=50325
     Region          248..440
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mkpfcsvktk illqttslit ilalwlpacq ntaskktstp ifkgsyqdni kgmveiytyd
       61 hynrplkkgf gffidrdlvv tnfnwlkgsy kakiappgtk dfrdvrgyti ydhnlnilil
      121 kvnrnnpkyl klntnnqppd siytllrpsr kllvrkgktg pfhnrdsisf weapgpmvag
      181 kpafrydhql lgivqqrnin dslkkvilpl kyiktlmsrq ssqpksiwel rtktnktyis
      241 ykkvkgfrik ttmgditirl ynetpkfrdn fiklvsdqfy dsllvhrvlk dfliqmgaad
      301 skyagkddvv gwqgpgynlp thivpslyhk rgavaasklp pernprnrsd gsqfyiisgr
      361 rfthdeldei eqekgfkftp sqretyttig gapyldgdyt vfgevisgmd vvdkiaavkt
      421 ygenrpvddi riktieiikk
//
LOCUS       WP_010527627             451 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Thermophagus xiamenensis].
ACCESSION   WP_010527627
VERSION     WP_010527627.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..451
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50987
     Region          134..451
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrfksllliv ailstnvfaq snadtlsfsl edamsyaskh ayqkisseld iksarkklwe
       61 tiasglpqid fsaqynhsid vpvsllpaei ipedmlppgi gpgdkvpisf staydgsysv
      121 samqmifkgs yfvgleatkv fldltrhqde kteiqirdav akayflvlaa renynafken
      181 leinkgtlke teamfdngfr esmdvsqikl mvreaekqiv etkrneeval avlrfsmgld
      241 edrqliltdk letlsqrlve qqetekwapv ehidykiant naesqrlllk nakaqylpei
      301 safytyqksg ygdswnifke qwykaqfvgi tvsmplfssg mrhaqvqqqk lawdkslneq
      361 qqtlrniqtq sltaltnyys aldqldiake skalaediys ktrvkfsngi vgsfelnqlq
      421 gqfvqaqiny vnailnlmna kidylkaigk l
//
LOCUS       WP_010527678             184 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Thermophagus xiamenensis].
ACCESSION   WP_010527678
VERSION     WP_010527678.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..184
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21232
     Region          5..181
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mqsspseyel vklskegnie afsklidlyr qkvfqtcmgf lhsrddaedl tqdifikvwn
       61 slksfderst fstwlyriav nsainqvrkn klrsfvglsk avndfsnpse nadhrlmrte
      121 vkqeikeaig rlkinqrkaf ilvyyqelsi kevasvmkis pkaaesllfr arknlqkmls
      181 qktn
//
LOCUS       WP_010527680             434 aa            linear   BCT 01-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Thermophagus xiamenensis].
ACCESSION   WP_010527680
VERSION     WP_010527680.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..434
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=47280
     Region          1..431
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 msdlkfetlq lhagqevdpt tnsravpiyq ttsylfndaq haanlfglke fgniytrimn
       61 pttdvfekri aaleggvaav avssgqaaqf iaitnflqag dnfistsnly ggtfnqfkvq
      121 fkrlginvkf vetddpadye akidentkai yvetignprf nipdfeklge iaakhdipli
      181 vdntfgaggy lfrplehgan vvvesatkwi gghgtsiggv ivdggnfnwg ngkfpafsep
      241 segyhglkfw evfgsdgpfg niafsirarv eglrdfgpal spfnaflllq gletlslrve
      301 rtvqnalela qwlenhpqve yvnypglpss pyhelakkyl krgfggvlsf kikgpadtad
      361 kfidnlslvs hlanvgdakt liihpsstth eqlsaeeqka agvepgllrv svgiehiddi
      421 ksdftsafek vsqk
//
LOCUS       WP_010527691             124 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Thermophagus
            xiamenensis].
ACCESSION   WP_010527691
VERSION     WP_010527691.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..124
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14314
     Region          23..123
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mrnyllllfl ifpcltlyaq gnltakqfsl fmdtcknvvv idvrnkeefl eeripgaisc
       61 enkdalfqvt dtidkqqpil vycnmgnrsk salellknkg fkniyqlkkg fvewrrkgyp
      121 ivqn
//
LOCUS       WP_010527701             592 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Thermophagus xiamenensis].
ACCESSION   WP_010527701
VERSION     WP_010527701.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18646610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..592
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=68824
     Region          55..273
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          55..80
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(56..57,60..61,63,87,90..91,94..95,97..98,121,
                     124..125,128..129,132)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          85..115
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <95..559
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          120..147
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          155..179
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(197..198,200,224,227..228,231..232,234..235,258,
                     261..262,265..266,269)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          222..252
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          332..360
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          365..395
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          404..428
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(441,444..445,448..449,451,475,478..479,482..483,
                     485..486,510,513..514,517..518,521)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          441..468
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          473..504
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          509..537
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          544..572
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrylsiislv iifftscsvl skyqagenky sklsdslnvr sisldeseqr kfdyyfyegi
       61 rykalnevnk sfmyfaeafk idstcsacay elsrillann svedaqklmv kavqydpynr
      121 yyilllsriy qnlgngeaav diarrllnnn gnssvediyy vaelevqngf idaaidnlki
      181 ienrlgisep inlriyqlyl qkedfnnaek elykliknnp ynsnyrillg dfylengnfk
      241 kafseynevl kiepvngnvy fslgnyylek gdtlsfkknf fkgfesknvd ftnkfrklls
      301 lvgnndnske lfekeeiktl yrilirvhpy evdvyhsfgn ylmslgekdl ardifqqgle
      361 idasqpllwq dylillsefq dyntlsnkas qaikfypeep vfrllygval fqlkdyraaa
      421 nvllnglele kvksnlplkg qfhaylgdif ysmknvdscf yhyeealkid enniivlnny
      481 syylalegln lekaehmsak tiqlepgnpt yldtyawvlf krkrfneakf iieravenld
      541 epngvilehy gdilyktgdl egaliqwqka lelgehsktl ekkielkkfv de
//
LOCUS       WP_010527704             131 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Thermophagus xiamenensis].
ACCESSION   WP_010527704
VERSION     WP_010527704.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..131
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14981
     Region          3..130
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mnkvvfksei knislverli ddisvkynlh sdiygkllla vvegvnnaiv hgnklekeki
       61 vilkyiitde kiefiirdsg egfdyrnlpd ptkpeniekt hgrgiflmkh lsdelefnek
      121 gnevrivfnl t
//
LOCUS       WP_010527820             306 aa            linear   BCT 01-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Thermophagus
            xiamenensis].
ACCESSION   WP_010527820
VERSION     WP_010527820.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..306
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33756
     Region          41..293
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mkqlttiltt ivlfaqfsea taltplyesf ditpdsvfmd laegpavspn gtlyavnyrh
       61 qgtigfvkpd gshglfvdlp egstgngirl wknetllvad ytghnilqid intksisvla
      121 hnpqmsqpnd iaisskgvvy asdpdwenns griwmtdqsg klkllmqnmg tvngielspd
      181 ekllyvnesn qrniwvfdiq ddgtlankrl likfadygfd gmrcdekgnl yvarfnkgtv
      241 aiispdgkli revvlkgdqp tnvafggkdg ktvyvtvadr gaieafrtef rgralllqdv
      301 whnhkk
//
LOCUS       WP_010527831             275 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Thermophagus
            xiamenensis].
ACCESSION   WP_010527831
VERSION     WP_010527831.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..275
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=30185
     Region          5..275
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 meniknwfsn peqimgfvik yggqlliaii tlivglwiis llmkgmkklf rardmdpglq
       61 sfllsvssia lkimliisvi smlgvkmtsf iavlgaagla igmalsgslq nfaggvmllm
      121 fkpfkvgdyi taqgesgtvs eiqifhtilk tpdnktvilp ngalstgsmv nyskepqrrv
      181 dftfgigydd didkaknlil siiekdsril kepapfigvi nlgdssvdlv vrvwaeasny
      241 wgiffdlqet vkkefdrqgi sipypqtdvh liqsk
//
LOCUS       WP_010527894             251 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Thermophagus
            xiamenensis].
ACCESSION   WP_010527894
VERSION     WP_010527894.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..251
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26744
     Region          3..248
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mdfhqallli lagiaagvin tfagsgslit lpllmfmglp pavangtnri gvvfqnlvat
       61 gnfirqkelq prqewpliip tlfgsllgaa laveikedil nyfiggllvv mffvillkpt
      121 twikgkagkm ktskskwins lifffigiyg gfiqagvglf llsglvlgag ydlvranavk
      181 vlmvlaftlv amvvflsagq iawsyglcla agnalgawfa skyankigak niryillavv
      241 lfsglkvlgl f
//
LOCUS       WP_010527901             501 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Thermophagus xiamenensis].
ACCESSION   WP_010527901
VERSION     WP_010527901.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..501
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55527
     Region          2..501
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mdtsskrhpq glwvlfftem werfsyygmr allvlyltss ivnggfayae nhaleiygif
       61 tglvyltpil ggiiadrfig qrksvfiggi vmalgqaala yseyiavpeg geaiqtlref
      121 wlfiglglli lgngffkpni stmvgrlyad gdprkdsaft ifymginlga flapfiagyl
      181 gesvgwawgf gsvsvgmvlg viwfwieqsk lgtigfgpkr kftgeverln ardwgevwiw
      241 vlaivgfiyl fvktwwimpe vvtdwiirvv algaisviay miiknttgkt ewsrigailv
      301 fcffniffws gfeqaggtfn lfardmtdcm igsfeinasw fqsvnaaliv glapvfsmlw
      361 iwlgkynpnt pvkfglgltl lslgfvvmyt admkaspenl vsplwlvsvy llhtmgelcl
      421 spiglsmisk lsppkitslm mglwfgstal anylagalks iletympgmn lflflvitsg
      481 saallmylis pwlkklmrgv d
//
LOCUS       WP_010527234             541 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Thermophagus xiamenensis].
ACCESSION   WP_010527234
VERSION     WP_010527234.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..541
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62008
     Region          50..501
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkrkylifts fiflgalifv mpactklene nfsefiaddf spsesdliri tsaaygdwrk
       61 vlllwdgywr aqevsadevv iparpngwvd ggvhkrifmh swlpsdpivs etwyrcytgi
      121 nncnrvifql kslleeedav saiselralr asyyyvlcdm ygnvpivtkf dvpdgylpeq
      181 ssrkevynfv vkeleesipy ltdennaety grfnvwaart llakmylnae vysgtpqwdk
      241 claqcdsiiq sgkfalepdq knvfitenqn sneiifgisi denyttdwna fdihmqtlqp
      301 anqatynmth tpwggmcavp qfidtfdped krlinnfiyg qqfsssgdsl yctmgeltge
      361 playinevps idrseeihgy rfgkfeiamg asnilnndfp lfryadvlmm kaecllrtgy
      421 edeaaqivte irrrafpsas ekavvtgeel lqgsvydygl rdenyttyeg gnniiygrfl
      481 delgwefnqe grrrqdmirf giftekswfs hspngdfril ypiplsamet nsnlvqnpgy
      541 k
//
LOCUS       WP_010527986            1051 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Thermophagus
            xiamenensis].
ACCESSION   WP_010527986
VERSION     WP_010527986.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1051)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1051)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1051)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1051)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..1051
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=121572
     Region          62..1044
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mnqssdngii vfiqsrkiiv qdnfgakslq fkrlvnkkyk qknqgnpnik gikvqtimat
       61 gtkeihfeeh ienylvnevk eyhvispqey nkelcvipse iiafikdtqp ekykalkeqy
      121 ganvdkqivn niarnlnknk tlhvfhnkvk drgqslnmvy fkpannktpe hgewykknrl
      181 aivrqlqysn knnhkidivl fingipvvtm elknaltgqt hhnaikqymk drnpkgeafl
      241 efkrclvhfa vgtekvfmtt qlkgdstvfl pfnqglensn angfatsylw edvlrkdsll
      301 dliqnfisiq tdketyydek tktlkqktst kllfprfhqr rvvlrmleav rkdgvggkyl
      361 gqhsagsgks nsitwlayrl sgfyqnytdn kalfdstivv tdrrvlnsqi qenirqldnt
      421 pgvvayidek ksardlkqai ldgkriivtt lqkfpvisdt itklpnknya viideahssq
      481 tgeaaghlrk slslevaeel esknkdldei iadeikskgi qknisffaft atpkpktiel
      541 fgtvqedgsk apfdiysmeq aikegfildv lknytsfkry fkivkrneip dkeyekkktv
      601 qllssyvdlq dhaiekkari miehfvtqtq neiqgkaram lvtrsrlhav rfkrkfddim
      661 remklpynal vafsgtvrdd etgedytevs mnnlqgkisi pealklpkyr ilivadkfqt
      721 gfdepllhtm fvdkklggts tvqtlsrlnr ttkgkdstmv ldfvndpemv ledfqrfygk
      781 nymkeehqtd pntlydvqnk idsynllykn eidafaniff rkgdnyeelq pilnevcrry
      841 eeeldedkqt gfkgdaksfv klyrflrgii sftdveleky yvfltalikk lpyikssmpl
      901 dvlgevelhs ykiqhqyttd lklvsgdgem kgmtpgggnr kpeeeydllt niikvlndtf
      961 gldlteedrv dfekmkeniy sneelmsffn pnntkeniqe kfneeidsel lnfintklef
     1021 ynklsedrvn tmfkqlwfnd lydkkvrgia i
//
LOCUS       WP_010528008             245 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Thermophagus xiamenensis].
ACCESSION   WP_010528008
VERSION     WP_010528008.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..245
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27426
     Region          11..245
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mkdintsafa ievvdlvkkf gnftandhlt fnvrrgeifg flgangagkt taikilcglm
       61 aptsgqvvva gynvmthpel vkqnigymsq kfslyedlti fenirlygai ygltaneirq
      121 rsdtilrklg llkdrsrlik tlslgwkqkl afsvamvhhp kivfldepts gvdpvtrrqf
      181 weliyeaaad gitifvtthy ldeaeycdrv tvmvdghika ldtpaklkkq fnvdtmnevf
      241 lnltr
//
LOCUS       WP_010528017             381 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Thermophagus xiamenensis].
ACCESSION   WP_010528017
VERSION     WP_010528017.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..381
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42563
     Region          5..379
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 milttekhen yrkqirafae eviqpeaerl dreerfspel tkkmgeaglf gitlpkkygg
       61 qeldtlsyii aveelarvda sqaatvaahn slgidpiyvy gseeqknkwl pklttgehlw
      121 gfglteetag sdalgtktka vrekdywvln gtkrfitnss neltlgvtiq amttdkngke
      181 klsailvekd rpgfysermt gkmmwrasdt griklenckv pysnllgkeg mgarymlktl
      241 dggrlsiaam gvglargafe halqhaqtry qfgqpiskfq sisfkladmd mkielarntl
      301 ykacllkdqg ksftreaaia klyasemare iadeavqifg gsglfkdnpv erfyrdqrll
      361 qigegtseil ryviarqlgi k
//
LOCUS       WP_010528067             258 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Thermophagus
            xiamenensis].
ACCESSION   WP_010528067
VERSION     WP_010528067.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..258
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27722
     Region          1..258
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mnefilavii mviaflmtmt grgggnfyvl tlvisgvgin lsasigqfil mcsslmaail
       61 fskqkmnhwq ltlilgvmlf fsslaggyfg nyfnerflki tfavvmflaa mlmlrkpsrk
      121 lksdrkwvim fksgdqvfhv nflitvpvvl fagfvsgmvg vsggsflvpl mlltmnvpmh
      181 vavgsttvlv slsaaagfmg hwgagvfdwh laiplaiggv iggyagakma ikskpknlky
      241 lfvgtqilas vlmivnal
//
LOCUS       WP_010528056             448 aa            linear   BCT 01-JAN-2025
DEFINITION  fasciclin domain-containing protein [Thermophagus xiamenensis].
ACCESSION   WP_010528056
VERSION     WP_010528056.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Clout,N.J., Tisi,D. and Hohenester,E.
  TITLE     Novel fold revealed by the structure of a FAS1 domain pair from the
            insect cell adhesion molecule fasciclin I
  JOURNAL   Structure 11 (2), 197-203 (2003)
   PUBMED   12575939
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..448
                     /product="fasciclin domain-containing protein"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=48180
     Region          1..176
                     /region_name="FAS1"
                     /note="Uncaracterized surface protein containing fasciclin
                     (FAS1) repeats [General function prediction only];
                     COG2335"
                     /db_xref="CDD:441906"
     Region          <183..314
                     /region_name="FAS1"
                     /note="Uncaracterized surface protein containing fasciclin
                     (FAS1) repeats [General function prediction only];
                     COG2335"
                     /db_xref="CDD:441906"
     Region          317..448
                     /region_name="FAS1"
                     /note="Uncaracterized surface protein containing fasciclin
                     (FAS1) repeats [General function prediction only];
                     COG2335"
                     /db_xref="CDD:441906"
ORIGIN      
        1 mkkmkfslli vlsgifilas cdknddnnte eipdesntiv dvasadenfs vlidaleltd
       61 lkdaladena eytvfaptnd afsdlltelg ydeledlpnd dlkeillyhv lagkaeanev
      121 engyystlad gpqdgytlsm yinmddemin srasitatdi madngvihvv dkvilplsls
      181 ghaaansafs vleevvekag lsetlnnssl sftvfapvdd afnqlftnlg ftlddlsled
      241 lqpillyhvv tgflpsadie sgyvttlsqi geqfvslqvs lgdniilngn snviiedvva
      301 tngiihaide vlippevvdl aldnsdfsyl vealvkvdlv ealrdegpft vfapvnsafe
      361 dlfetlgvng lndiddetle nvllahvvsg yflssdlsng slstlnseks ltinvdngiv
      421 idgdinvlla dikgtngvvh vidkvivp
//
LOCUS       WP_010528068             130 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Thermophagus
            xiamenensis].
ACCESSION   WP_010528068
VERSION     WP_010528068.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..130
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14585
     Region          24..120
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mnelekvike mdfrhfgtgq hnmdaetflt sdntvlldir tkeevdtlkl plshfcpvie
       61 ipthevpdri eeipkdktig vfcsagvrav iifvylrskg fnnvkiipgg ysglieaikp
      121 gklykklnne
//
LOCUS       WP_010528140             324 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Thermophagus xiamenensis].
ACCESSION   WP_010528140
VERSION     WP_010528140.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..324
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36735
     Region          2..320
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mkhisilipr gdysvvnimg crqmlaaash rhkmqsgkdl fcidlvgfee adrpkpgrae
       61 vaptkqwqdi artdlilipa vhqapnvviq nntsliafvs eqyqkgatva slcigaylla
      121 atglmngksc sthwqhaael kalfpevrvk eeriitdeqr litsggayaf tnlilyvvek
      181 fggrelalfl aktfmididr trqsvysqfi gakqhadevv lqvqdfienh faekftiaql
      241 aekfhlvrrt lerrfksatg fsivkytqkv rvekakrqle kgrksvtevm ydcgyndpks
      301 frevfkknvg itpleysrkf eqvw
//
LOCUS       WP_010528122             456 aa            linear   BCT 01-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Thermophagus xiamenensis].
ACCESSION   WP_010528122
VERSION     WP_010528122.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..456
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=52050
     Region          4..435
                     /region_name="ASKHA_NBD_FGGY_NaCK-like"
                     /note="nucleotide-binding domain (NBD) of Novosphingobium
                     aromaticivorans carbohydrate kinase and similar proteins;
                     cd07772"
                     /db_xref="CDD:466792"
ORIGIN      
        1 mekviavfdv gktnkklllf npklelvyqd eqkippvldd dgfecddidf ieewvktsld
       61 rllrggkfnv lgvnfstyga sllfldnkgq ritplynylk pipeivqnqw yqdnggkdef
      121 crktaspple amlnsgvqil wlkrfkdhlf kkvnhilhfp qylsfiltqk vvadytsigc
      181 htglwdfdtm tyhpwllkeg iflpqpinns ekfqidfggn klwvgigihd ssaslapyll
      241 akvepfills tgtwcinmnp fnhhpltleq lkndclsyls idkkpvkssr fflghihdln
      301 vnrlcehfnv gndyfkrvva ndqliksfmk dgknsssaff rfgvpdnfvd dqidlnafns
      361 feeayhrlmf dltrmnvrsi nlildktngi knifisggfa kneifvklia affpemnvyt
      421 snidnasalg aamviadifg eqpipeinln lkqvtf
//
LOCUS       WP_010528165             412 aa            linear   BCT 01-JAN-2025
DEFINITION  FecR family protein [Thermophagus xiamenensis].
ACCESSION   WP_010528165
VERSION     WP_010528165.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..412
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=46994
     Region          <189..406
                     /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"
ORIGIN      
        1 mkltkftgls ideliedssf lsiiselddt ewekevancs kedqvvleea rnlvrlfcak
       61 esvplmpssi krqlwnrivs dsrkelvfga vrygirqyik vaammlvils igvygywhlk
      121 dkeatyqfst geawiysdep vlflskgeki kldgekkeie vlekenavri ggdsivknvv
      181 pkdenseyvl mnevtvpfgr qtklvlsdgs kvwlnagsrl afaqefrrnn rtvflegegy
      241 fevaknknkp ffvktesvii rvlgtkfnis ayttddkvet allegsvkvi plksifnrev
      301 tikpgdraiy vksgkkmqvk rednieqfis wkdgwyqfsn eniinvlakl eriynvkfiy
      361 naedvshtfp isgklsmyns idsvltnltv vagieykmln dsifvysrns te
//
LOCUS       WP_010528159             783 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Thermophagus xiamenensis].
ACCESSION   WP_010528159
VERSION     WP_010528159.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..783
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87464
     Region          32..118
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          105..728
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mklikyffls ltlltasiti qaqqkwrsda niighvvdqd gnhipfanvs ivnttigtat
       61 detghyrlin lpvghhqvka qflgykpqiv evelkgnetk eikfqlqedv lgveevvvta
      121 drnetnrres stivntltpk lfataqvstl seglnfcpgl rmetncqncg fsqvrmngme
      181 gpysqilins rpifsglagv yglelipsnm ierievirgg gsalygsnai agtinlilkd
      241 pinnsyefgt gnsisgigvd gagdpaqdyt vnfnasvvsn dnktglaiyg fyrdrepfda
      301 nddsfselte lknttiggrv fhrfgtrdkl tadffnikes rrggnkfdmp ehmadiaesv
      361 dhnittgala ydrffrdadk lsvyasgqhv vrdsyygaeq sladygntkd fsytvgaqyn
      421 whflnsdlll giedvgawlk dkklgypdle dpnftvedgp yienrivadq etntlgmfaq
      481 yefdinklnv svgarfdhys ieddaensst sgdvlsprit lkydiveslq arvsysqgyr
      541 apqifdedlh ietsgakkii henaddlkqe tshsymvsld fnrqlgnsym gvlvegfytq
      601 lddafanefg epdedgvviy trvnaeggat vkginieanl vpsdkwefkg gftiqrseye
      661 evhelnetrf frtpdyygyf tidwdptkkl cvsstgnytg smlvpynesv lresdpffdf
      721 gmkvrytipi ngaklqfyag mknifnsfqd dfdtgidrdp ayiygpalpr tlyfgiklgn
      781 mlk
//
LOCUS       WP_010528177             655 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Thermophagus xiamenensis].
ACCESSION   WP_010528177
VERSION     WP_010528177.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..655
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76097
     Region          17..604
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkhskegney fillfrfgli mllyticrla fyffnsdlfe nlsfqtfkri lygglrfdls
       61 avlyinslyl llylipfkik frigyqnflk wlfivtnaig laanvsdiiy yrftlkrtta
      121 svfkifshee nllllwgrfl vdywyatllw lvligvmvwg ysrfkprpmg frnrwqysmv
      181 gilflaiigg ltiggmrggf rhstrpinis naaqyverpe eipivlntpf ailrtfdkst
      241 fqevkyfsse eldsifspvh ypkrsasfnq hiiqekrpni vliilesfgr ehigalnknl
      301 edgnykgytp fldsliaqsw afnrayangr ksidalpsiv asvpslvqpy ivseyannri
      361 ngmahllkki gyetafyhga pngsmgflaf tkmagydqyl gknefnndge fdgiwgiwde
      421 pffqffaqdm nrlnepfftt ifslsshhpf kvpekyegvf pegplplhkc mgytdmalrr
      481 ffesaakapw fkntlfiita dhctipfhee yktpvesfai pilfykpdei eprmdnslaq
      541 qtdilptvms fidypypfva fgndlwsakn nkrfvinyfn esfqflyeny alyfdgknvt
      601 giydlehdpl qkhnligqvd kpsaekllka viqqyisrmi ndrlawnveg nkhdh
//
LOCUS       WP_010528178              90 aa            linear   BCT 01-JAN-2025
DEFINITION  HU family DNA-binding protein [Thermophagus xiamenensis].
ACCESSION   WP_010528178
VERSION     WP_010528178.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..90
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9343
     Region          1..90
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mnkaqlieai agesgltkad akkaldgfik vtgealkkgd rialvgfgsf svsersartg
       61 rnpqtgkeiq ipakkvvkfk agselndavn
//
LOCUS       WP_010528183             754 aa            linear   BCT 01-JAN-2025
DEFINITION  inorganic phosphate transporter [Thermophagus xiamenensis].
ACCESSION   WP_010528183
VERSION     WP_010528183.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..754
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=83950
     Region          1..281
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 metiylvivg vlfllaisdl vvgvsndavn flnsaigari asfkvilsia algvfvgasf
       61 sggmmevark gifnpqfflf eeimivflav mltdiiildl fntfglptst tvsivfellg
      121 aaigvaviks fknpemvvad yinsakalai isgillsvai sftvgvitqf itrlifsfnf
      181 knrlkylggl wggiaitait yflivkgvkn atfisdsiri wvtenagivi syslifwtli
      241 lqvlywlfnf nilkftvltg tfalamafag ndlvnfigvp laglesfkif kasgaptatl
      301 lmdslageih tqayllvlag limvitlwts kkakkvvqts idlgrqtege erfgssffar
      361 sivrgsiavs nsinqfiptg irnfinrqfd sskyeeerqk lgkeapsfda lrasvnlvva
      421 siliayatsm klplsttyvt fmvamgtsla drawgresav yritgvvsvi ggwfltafsa
      481 atiafmmati mmfggnyaii alillaafmv yrtqvitkkq ekeikrfqem eiedvngeis
      541 slkvlekcql niseiindll klysntlsyf eaedrkhlke cvkevdslnk rtkklkaniy
      601 ntvrklqeds vdsglfyvqv idylretvhs ltfivkpcfe hldnnhkvfs edqfeeinil
      661 egkirsllik synminksdf tllpelaeeq sniievikgm rkkqlkrikk ekagtkisml
      721 ylsvlhetqn mllhlinllk aqrdfvkaik ekke
//
LOCUS       WP_010528210             320 aa            linear   BCT 01-JAN-2025
DEFINITION  L-histidine N(alpha)-methyltransferase [Thermophagus xiamenensis].
ACCESSION   WP_010528210
VERSION     WP_010528210.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..320
                     /product="L-histidine N(alpha)-methyltransferase"
                     /EC_number="2.1.1.44"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=37126
     Region          8..319
                     /region_name="COG4301"
                     /note="Uncharacterized protein, contains predicted
                     SAM-dependent methyltransferase domain [General function
                     prediction only]"
                     /db_xref="CDD:443442"
ORIGIN      
        1 mepklllsql aadtlsglsa ypkylhskyl ydhrgskifq dimampeyyl tdceleifns
       61 hkasiieafg hhnrmfnmie lgsgdglktk illrqmvkkh infqyisidi sakankelkt
      121 rlnadfpnlk vetktgdfff tlknqngfna lpkitlflgs nignfsdnet heflmdiasf
      181 sqkgdkvlig fdlkkspqvi mkayndphgh trrfnlnlle rlnrelnanf nidnfeqhts
      241 ydpasgevns flvskipqtv higelersfq fhqwetifme rsrkydipti nemaarygfk
      301 vmhhftdkrr yfvdslwvke
//
LOCUS       WP_010528212              94 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF427 domain-containing protein [Thermophagus xiamenensis].
ACCESSION   WP_010528212
VERSION     WP_010528212.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..94
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=10414
     Region          1..92
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 mkaiwngkii aesndivnve gnayfpmesv npkylkksnt htqcpwkgta syftimvdgk
       61 enpdaawyyp spsglaqsik grlafwkgvq itkd
//
LOCUS       WP_010528289             476 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Thermophagus
            xiamenensis].
ACCESSION   WP_010528289
VERSION     WP_010528289.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..476
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=51871
     Region          3..463
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mfkrlplhwk iiiglvlgiv wavlssfwgw tqftehwiap wgrifinllk liavplvlfs
       61 imggivslgn pkdlgrlggk tlllylitts iavtvglllv nfvapgktld snvrlenrlg
      121 yelwllnqgq tpndgrwlss dstysdllkt iasrqglees eevrtrlata qkaetegplv
      181 flenmvpgnl fvslsdnrnm lqviffgiff giailfidnk krgvltgaid aisevflkmv
      241 dlimkaapyf vfalmagmvn qmagdnpshv felfkgltwy vlvviaglli mafviypafm
      301 glfvkglsfk dflkgispaq mlafttsssa atlpvtiecl eenlkvdkri ssfvlpigat
      361 vnmdgtslyq avavvflaqm hmvdlsfgqq ltvvitavla sigaaaipga gvimlmvvls
      421 svglnpawig iilpvdrild mlrtvvnvtg datvcslvdk ttnfdqhfik pdsics
//
LOCUS       WP_010528349             150 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Thermophagus xiamenensis].
ACCESSION   WP_010528349
VERSION     WP_010528349.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..150
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16521
     Region          1..148
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslidkisee iknamkaknk lklealrsik kelleartaa nsggeiseee eikilqrmvk
       61 qrkdsaniys aqgradlydn emaeaeiiaq flpeqlspea leeelkkiie evgaesmkdm
      121 gkvmgaatkk lagkadgkdi sdtvkrlltq
//
LOCUS       WP_010528335             380 aa            linear   BCT 01-JAN-2025
DEFINITION  AAA family ATPase [Thermophagus xiamenensis].
ACCESSION   WP_010528335
VERSION     WP_010528335.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 380)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..380
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43070
     Region          3..357
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 miisriklin wknfkeidvp lsgrtfivgp nasgksnlld vfrflrdiak aggglqnavl
       61 drggiskirc lsarkhpeve veielseygs kevlwkyaig ikqevrgyrl pilvyekvwk
      121 knklilnrpd khdendkerl yqthleqina nkefreiarf lesivyqhll pqllkhpqsf
      181 tgpdlpgdpf gksflerisk vnrntrnawl rkiesalkia vpqfkqfefk eengrphlea
      241 vydhwrpsag kqredqfsdg tlrligllws lqegdsllll eepelslnga ivskipaliy
      301 klqkpkkrqv litshspdll sdkgisldei lvlmpstegt tvqpasslps fkkmleggmt
      361 paqailpstk pkdisqlalf
//
LOCUS       WP_010528352             245 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Thermophagus xiamenensis].
ACCESSION   WP_010528352
VERSION     WP_010528352.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..245
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=28640
     Region          <57..242
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mllrqiknsl lwgllvlyfp vmlgfvenhq nkvvcsevev nildslkyrf vrtneiknai
       61 iakfdqvlgv pinelklnki eafvekhpav ancevyntie gklkidllqh nplfrvfend
      121 rsyyidedgn emplfdhyaa rvmvvsgnle gqmdhliyla rrfredsfwl aqieqvyikk
      181 ngdyvlvprv gdhlilfgpp erideklrnl kalykyglsp rewneyhvin lkykgqilcs
      241 knrni
//
LOCUS       WP_010528386             183 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Thermophagus xiamenensis].
ACCESSION   WP_010528386
VERSION     WP_010528386.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..183
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21552
     Region          3..181
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mhpddkeilq laqdsdrqne alvllmkkyk erlywhirkm viihedaddl lqntfmkawk
       61 nlrnfrgdas lytwlykiat netlnyinkk kesllnedad memmlgnmle tdalfsgdei
      121 qkrlqkclla lpekqrlvfn mkyfddmtye qisqilgtsv galkasyfha vrkieafikn
      181 evf
//
LOCUS       WP_010528450             190 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Thermophagus xiamenensis].
ACCESSION   WP_010528450
VERSION     WP_010528450.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..190
                     /product="YceI family protein"
                     /calculated_mol_wt=21185
     Region          1..190
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mtkiklisay llallvlpyi vngqeinltg dnntlkvtgt stlhdwemem kkfdvsarfe
       61 qtensnflls ntkftanakd llssksmmnn kahealkakk hpsisftqdk pievnknqqn
      121 yfvpgqltia gktnsvtipv hlswneknel kvtgdielkm tdfdmeppsv mfgsintddl
      181 vkvsfsislk
//
LOCUS       WP_010528467             428 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Thermophagus xiamenensis].
ACCESSION   WP_010528467
VERSION     WP_010528467.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..428
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48653
     Region          44..331
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mskqyqsrre flkklaitgs vatlaaspwi kafsdntpig knpsdkvrla vigtgsrgkq
       61 lmrylfrian annieicalc dvyqphldka inmcqkenik vksynnyqdl itkekpdgvi
      121 iatplhqhah itidclkhgi hvfcekamar tlddtkamyd ahketgkilq ighqrlfnpv
      181 ylegmkrihn gelgtigqir aywhrnnnwr rkvpdntvem erfinwrlyk eysaglltel
      241 lshqiqvanw alqktpvsvm gtgsivfwkd grevednval iytydngvqf iydsmisnkk
      301 ygleeqvmgh kgtiefevnr yytetpppap gilqllndie sgffekvnig gaswipetav
      361 kyqgepiied tdfydsalql egfaqyirkg kapekmiieg ynasiwtlla eiaidtgkkv
      421 alpekyri
//
LOCUS       WP_010528500             213 aa            linear   BCT 01-JAN-2025
DEFINITION  FecR family protein, partial [Thermophagus xiamenensis].
ACCESSION   WP_010528500
VERSION     WP_010528500.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..>213
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
     Region          73..>198
                     /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"
ORIGIN      
        1 mnqeqeqlfd eylngcggdl pteknfvklf cgeaneislk krmrkdwdal skanikkdls
       61 pilhkihyii nlehekkllp kggikkvlfw yskiaailll piiglmigwl ligysdhlqp
      121 svvevvvplg ariktqlpdg ttawlnsgst lsytipfkqr kvtlegegff nvrkdsihpf
      181 vvkgkqgavr vlgtrfnidm wpdeevmegv lgg
//
LOCUS       WP_010528502             372 aa            linear   BCT 01-JAN-2025
DEFINITION  formylglycine-generating enzyme family protein [Thermophagus
            xiamenensis].
ACCESSION   WP_010528502
VERSION     WP_010528502.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..372
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=41475
     Region          64..371
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mkklvyvsll lilcfsgcht nnqssesesd lccmpttsqe srflaspqtl geaennssnq
       61 slgdmvlipg gefemgaken qfakpdefpv hkvyvdsflm drhpvtnaqf refveatgyv
      121 ttaerrpdwq eikkqlppgt pkppdsllvp aslvfkspdh evslsdyiaw wewvpganwr
      181 hplgpgssie glddhpvvhv swydamayat wagkrlptea eweyaarggn ndyiypwgne
      241 pvsaqranfw qgnfpyknvv edgfqrtapv gsfpangygl ydmagnvwew tadwyhpdyy
      301 aflaqqvial npqgpetsfd pmepgvpkkv irggsflcnd sycagyrssa rmksspdsga
      361 lhlgfrcvkd id
//
LOCUS       WP_010528531             834 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Thermophagus xiamenensis].
ACCESSION   WP_010528531
VERSION     WP_010528531.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 834)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   6  (residues 1 to 834)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   7  (residues 1 to 834)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..834
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90183
     Region          86..143
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          198..830
                     /region_name="P-type_ATPase_HM_ZosA_PfeT-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     Bacillus subtilis ZosA/PfeT which transports copper, and
                     perhaps zinc under oxidative stress, and perhaps ferrous
                     iron; cd07551"
                     /db_xref="CDD:319849"
     Site            order(480,482,793..794,815,819)
                     /site_type="other"
                     /note="putative HM ion binding site [ion binding]"
                     /db_xref="CDD:319849"
     Site            order(524..526,591,607..609,640,681..683,703,706,709,728,
                     731)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319849"
ORIGIN      
        1 mkklqikipl ilpevpddkd rcvqkliqrl edkeglekvh vadetdngvp qlcfhynpel
       61 itidqiqkla krtgasiidk yghrlieveg irhtrharki eealnrldgv lqsavsasgm
      121 iglefetaki ndekiltvlr kegldilste veveryikkt heaekgeeqk eeadkehehe
      181 egedhehshg gifgknteli fsiicgallg igfglsyvea vpswvslaly igayffggyf
      241 takeaiqtva kggfeidflm lvaaigaail gewaegalll flfsmghale hyamnkarks
      301 iaaladlapk talvkrngkt eevgieelsi gdiivvkpns kisadgvvvs gsssvnqapi
      361 tgesvpvdke pvdnpdkdws qekdikdenr afsgtingnn tleikvikva kdstlsrlvk
      421 lvneaqtqks ptqrltdkfe kyfvpsvlvl vvllnfaflv idepfsvsfy ramavlvaas
      481 pcalaiatps avlsgvaraa kggvlikggr pledlgvlta lafdktgtlt egkpkltkvv
      541 algdvkedel lkiaiavesl sdhplakavv rdgkerlkga dvpdakdlea vlgkgikatl
      601 gndkvyignl dlfeslddnk pekeieekvk slesdgnttm lirqndhyig iialmdtprk
      661 eakntleqlk klgikrmiml tgdnqkvada vakeigltda wgsllpeekv eaikelkeke
      721 skvamvgdgv ndapamanst vgiamgaags dvaletadia lmadkletlp faiglsrkak
      781 giikqnlwvs lgivallipa tvfgfanigv avlihegstl vvvfnalrll aykk
//
LOCUS       WP_010528557             188 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Thermophagus
            xiamenensis].
ACCESSION   WP_010528557
VERSION     WP_010528557.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21565
     Region          3..>102
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mertktknki faealelfin kgfsasvnei ilktgiakgt fyyyfntkee livelykklm
       61 feieaecvte yggesardys knifgaivkw filnpdkfny ilifetspfi kkivgrvpet
      121 lkapventmk kvnmgmlkay ppemitffdf sftraaanyf lshsdplsaf ksdfnmvfdl
      181 ywdgvsgk
//
LOCUS       WP_010528640             336 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Thermophagus xiamenensis].
ACCESSION   WP_010528640
VERSION     WP_010528640.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..336
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39329
     Region          1..183
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mlvsiiipny nkapfieati ksvqsqtypd weaivvddgs tdgsteiiqt lasqdprirf
       61 fqrtkapkgg svcrnigigk algeyimffd sddlmspncl kvridsikqf pdihfgifpv
      121 gtfhhhigdn knvwntkngn hlikflrhdl pwnimsplwk tefikkhlkg fdesfprlqd
      181 vefhtralmv pnvkyqifnk tspecyyrid pnrsrknyfq mletmwpgvk myiqkfipll
      241 ddkkylkqlr gtffafltql nyfratkkit pkqyqlfltv indfmnetts lfptkiiklt
      301 niynifyqkg awkikgfnfa fkqliiqhns ysffss
//
LOCUS       WP_010528643             139 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Thermophagus xiamenensis].
ACCESSION   WP_010528643
VERSION     WP_010528643.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..139
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16011
     Region          19..138
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 maqgkkgtsn ksgktpkvtg vggiffycen leetlkwyse nlgieindwg fssfesrdin
       61 hpeqkntlqw kpfkkgddyi lpskkdfmin yrvqnieelv eklkkngvtv ldtiktydyg
      121 kfvhildkeg nkielwepi
//
LOCUS       WP_010528653             115 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Thermophagus
            xiamenensis].
ACCESSION   WP_010528653
VERSION     WP_010528653.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..115
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12799
     Region          23..87
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mkrimlsflt llliapmamf aqsktekfev kgqcgmcekr iekaaksveg vtsadwnlet
       61 kmlvvtfddt ktqldniqka iakaghdngk hkapdevydk lpgcckydrs dvkke
//
LOCUS       WP_010528756             248 aa            linear   BCT 01-JAN-2025
DEFINITION  uroporphyrinogen-III synthase [Thermophagus xiamenensis].
ACCESSION   WP_010528756
VERSION     WP_010528756.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schubert,H.L., Raux,E., Matthews,M.A., Phillips,J.D., Wilson,K.S.,
            Hill,C.P. and Warren,M.J.
  TITLE     Structural diversity in metal ion chelation and the structure of
            uroporphyrinogen III synthase
  JOURNAL   Biochem Soc Trans 30 (4), 595-600 (2002)
   PUBMED   12196144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..248
                     /product="uroporphyrinogen-III synthase"
                     /EC_number="4.2.1.75"
                     /GO_function="GO:0004852 - uroporphyrinogen-III synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006780 - uroporphyrinogen III
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0033014 - tetrapyrrole biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28473
     Region          1..224
                     /region_name="HemD"
                     /note="Uroporphyrinogen-III synthase [Coenzyme transport
                     and metabolism]; COG1587"
                     /db_xref="CDD:441195"
ORIGIN      
        1 mkikkilvsq pkpstpkspy felseknnvk idfrpfiqie gvsakefrqq kinilehtav
       61 iftsrtaidh ffriceetrv tvpddmkyfc iseatafylq kyivyrkrki fhstgkfpdl
      121 vevikkhkqe kflvplsdih kqeipdlltk akvkftkail yrtvssdlsd lkeidydvlv
      181 ffspsgiksl lqnfpnfkqn dtliasfgpa takavkeagl rldiqapmpq apsmtaalem
      241 yikkynkk
//
LOCUS       WP_010528776             223 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Thermophagus xiamenensis].
ACCESSION   WP_010528776
VERSION     WP_010528776.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..223
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25475
     Region          <35..219
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mryinfhthy ppadtkpeia ivscvapepl qqcppgiwls ygihpwyilh snmtnliekv
       61 ktlahnqqvi aigeagldkl rgpamdiqrq ifcqqidise ttqkpliihs vkanneilsl
      121 rkkrkplqpw iihgfnglpq emeqlikedf ylsfgprify sdskaanslk aipsdrffle
      181 tdhtnksisa lylraaeirg istqeleeii ennfrrlfgn iie
//
LOCUS       WP_010528784             141 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA thioesterase [Thermophagus xiamenensis].
ACCESSION   WP_010528784
VERSION     WP_010528784.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..141
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15829
     Region          11..>124
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mrkgniqvyg naetrlckmv fpgtlnanet lfggeimkwm detaficatr atrqkmftas
       61 vekvefiapv kensivemva nvktagpvkl evevqlfsep lyaddktlaa kalfimvaln
      121 ernkvtrlsf hhltnlfkkk r
//
LOCUS       WP_010528822             395 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu [Thermophagus xiamenensis].
ACCESSION   WP_010528822
VERSION     WP_010528822.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     gene            1..395
                     /gene="tuf"
     Protein         1..395
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43400
     Region          1..395
                     /region_name="TufA"
                     /note="Translation elongation factor EF-Tu, a GTPase
                     [Translation, ribosomal structure and biogenesis];
                     COG0050"
                     /db_xref="CDD:439820"
ORIGIN      
        1 maketfqrtk phvnigtigh vdhgkttlta aitkvlakqg lsevkdfdai dnapeekerg
       61 itintshvey qtekrhyahv dcpghadyvk nmvtgaaqmd gailvvagtd gpmpqtrehi
      121 llarqvnvpk ivvflnkvdm vddeellelv emevrdllnf yefdgdntpi ikgsalgale
      181 gdekweakil elmnavdewi plpprdnekp flmpiedifs itgrgtvatg rietgvihtg
      241 demeiiglga egkktvctgv emfrkildeg qagdnvglll rgidkkevkr gmvlakpgsi
      301 tphtkfkaev yvlkkeeggr htpfhnkyrp qfylrtldvt geitlpegte mvmpgdnvti
      361 svsliypval nvglrfaire ggrtvgagqv teiie
//
LOCUS       WP_010528871             445 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Thermophagus xiamenensis].
ACCESSION   WP_010528871
VERSION     WP_010528871.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..445
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50588
     Region          28..438
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrnktliilt llslvtigis gqeprkwslr ecieyakenn isvrkqelnt qyqsnlyqqk
       61 rlnklpslng sagyqlsfgr vpdettyqyv dqttqfsrfs lgtsvplfqa ftlrneikqt
      121 eanwkmsqse qeaaindlal nitayylqvl fdkellkvaq qqyevaqqqi ettrqlveag
      181 rvsesnllei ksqaakealn vtqmennlkl sllnlaqald lentdnfdiv spdiadleqr
      241 tltppsilfn tavdimprik ayqynlessq yglkaakgal ypslyldagw stnisktess
      301 vnfdfgqrfk dnatqyiglt lripifnsls arynvknakl giqsanldll qekqnlrkei
      361 qqayadaeaa fqkylaaqta vnayeeslry tekkyalglv spvdysvara dyikaqsdyl
      421 qakyeyvlrt kildfykgee ltldy
//
LOCUS       WP_010528887             664 aa            linear   BCT 01-JAN-2025
DEFINITION  PAS domain-containing protein [Thermophagus xiamenensis].
ACCESSION   WP_010528887
VERSION     WP_010528887.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..664
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76352
     Region          <29..>166
                     /region_name="KinA"
                     /note="Sporulation sensor histidine kinase A (Stage II
                     sporulation protein SpoIIF/SpoIIJ) [Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5805"
                     /db_xref="CDD:444507"
     Region          154..656
                     /region_name="KinE"
                     /note="Sporulation sensor histidine kinase E [Cell cycle
                     control, cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5809"
                     /db_xref="CDD:444511"
     Region          413..652
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mwrsvnilqk ianffinkta kfrqivtlak llsnkerlqi linatpdiic fkdstgkwle
       61 anvstkklfr lkgnefflks deqlkkmvpe ladvfeqcis tdqeawekkq rveteevipl
      121 pdgtlrvfdv iktpvfdetg arkgivvlgr ditnrkktee klreseerfr tvathandii
      181 fewepctdvl kwygkydtlv genntpqtld efltfvhped kerivsfwkk efkqkkewkd
      241 efrifsskgk liyyrasgim lfkngnpdka lgtfadvtle kqlidnlres vevaqynqar
      301 itsllsvmpd lififdrkgi ikdyhansin slivppeafl drpvdavlpp dladltreki
      361 kevmlhknve tyeyelkggd lcgvfesrmv ymdkdrvlti vrdithsrev eneliraker
      421 aersdrlksa flanmsheir tpmnaiigfs ellrnphlsq nekdsyidii vnsgqqllsi
      481 innvlevskl etgqvrlfpe kinlnrlmsd lmrffsieaq sksielncri pqkehylvsd
      541 ggkitqvfnn lignalkftp qggqitfgye hvnnmfqffv vdngvgiepk nhkliferfe
      601 qvcneprsar kgaglglsis kslvtlmggn iwvesepghg asffftipid qskqtkeset
      661 kffd
//
LOCUS       WP_010528913             470 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Thermophagus xiamenensis].
ACCESSION   WP_010528913
VERSION     WP_010528913.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..470
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52587
     Region          49..452
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mnicwynlgi qikteiskmg riinailllg llftiplysq neegakgwtl ekcieyalen
       61 nisvqsaria ieaeeanlle tkssrlpsls asstlsgnns rafdntggef skgvqvgvnt
      121 evpiyqggii nnnikageie lekarldvae aqndivlsvt qawlnilyar enylyyqdvv
      181 etskvnlery kalfdagtis rkdlaeiesq yasdrysmvt akneldirit dlktmlnlsy
      241 didfsplfpd rvdvpndevp sldtivvevl tkrpevknsn lstevaridl anakagylpt
      301 inlnasasss ysdnydgslg sqfndrftqy vglslsvpif srnqnkanva rskvmvyqae
      361 lnaretqnnl lqtveqvfve lkgqqeryqa alekvnaaki syeyqqeqfq lgmsnaidlr
      421 qskndllnan aeliqarysv llyhkildfy rgypigteny dtametntse
//
LOCUS       WP_010528916             406 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Thermophagus xiamenensis].
ACCESSION   WP_010528916
VERSION     WP_010528916.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..406
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44094
     Region          5..406
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mnifnlakia lkamfrnkmr tfltmlgiii gvtsvitmla igqgskqsiq eqissmganm
       61 vmirpgseer ggvridpssm ktldmkdiet ikkyaehisa ispvvktsgq aiagsnnwpt
      121 miqgvntefl dirkmevdeg vmfsdyhikr askvcllgqt vveelfpdke svigetvrfg
      181 kipfkvigvl gekgensfgq dqddiilapy ttvqkrvmai thiqdiyasa tseadseaae
      241 eeiaealrls helgeddedd ftvrsqqeli stfsstseml tillgaiagi sllvggigim
      301 nimfvsvter treiglrmai ggrgidilsq flmeaiivsv gggllgiflg lavsygignf
      361 lnwpilvteq sillsfavca vvgiffgwyp arkaasldpi dalrye
//
LOCUS       WP_010529023             149 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Lentibacillus jeotgali].
ACCESSION   WP_010529023
VERSION     WP_010529023.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..149
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=17132
     Region          54..149
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mayliprnta iklitkygtn cpfeiarqkg itiyfeslgg sfgyyacykr iqsihindsi
       61 nealqkfvca helghsilhk nentpflkrn tffstnkiel eankfavell ipdefiyefr
      121 dtrvtikeva qkfgvpeevc hlkkidhid
//
LOCUS       WP_010529077             375 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Lentibacillus jeotgali].
ACCESSION   WP_010529077
VERSION     WP_010529077.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..375
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39805
     Region          <69..>134
                     /region_name="LytD"
                     /note="Beta- N-acetylglucosaminidase [Carbohydrate
                     transport and metabolism]; COG4193"
                     /db_xref="CDD:443347"
     Region          <239..369
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mkhiwgavka igkkkaigwm vglaaaniip iliglvlmai mfaiigalgg svdeqqsnkn
       61 hpsagyvcsa tgeinqekwt svfqnkersg alkghgedii qlseekdldp vlfasialhe
      121 tawgksnaiq qknnpgglmn pdgsglfsfp tlkdglesms qtlynrikvd glvtieqlgs
      181 vyapvgaand pnnlnehwvp ttkeiaqklg gltmncepsn qpdmevigdk switshtkri
      241 tsgfgnrscg gcssfhagid vasgditgtp itafadgeiv iseangtthk sssnnmgtgy
      301 gwyvevkhdd glrtryahmm ekgkrvgtnv eagevigkvg stgastgahl hfevivngek
      361 vdpmpyvkpf ltgqq
//
LOCUS       WP_010529264             128 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Lentibacillus jeotgali].
ACCESSION   WP_010529264
VERSION     WP_010529264.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..128
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14685
     Region          1..113
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mnvnfnkrdp vymqvirhfk eriatgvfep gqeipsrrel agrlkinpnt aqraykemee
       61 agliyternl psritkdeai lksvrgelie eavdsfvhsi rsidvpveev lelvkekykn
      121 dgeevqdd
//
LOCUS       WP_010529210             197 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Lentibacillus jeotgali].
ACCESSION   WP_010529210
VERSION     WP_010529210.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..197
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22200
     Region          6..186
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mtkigfvrhg vtqwnkegra qgtsdiplde eglgqarlla erlefgewdv vyssdllrak
       61 qtaeilnakl gtqlyldsrl rerncglaeg tteeervqrw gpgwreldmq fesydsiisr
      121 gdalideise khmdqnvliv shgafikvvl nalipdsnmd eslkntslts likceggwdc
      181 nlynwtehil kgdslkm
//
LOCUS       WP_010529349             325 aa            linear   BCT 01-JAN-2025
DEFINITION  ring-cleaving dioxygenase [Lentibacillus jeotgali].
ACCESSION   WP_010529349
VERSION     WP_010529349.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10327061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..325
                     /product="ring-cleaving dioxygenase"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36192
     Region          5..129
                     /region_name="VOC"
                     /note="vicinal oxygen chelate (VOC) family; cl14632"
                     /db_xref="CDD:472697"
     Region          156..319
                     /region_name="PcpA_C_like"
                     /note="C-terminal domain of Sphingobium chlorophenolicum
                     2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and
                     similar proteins; cd08347"
                     /db_xref="CDD:319935"
ORIGIN      
        1 melkgihhvs aitanaanny rfytdvlgmr lvkktinqdd psvyhlfyad eignpgtdlt
       61 ffeipragnt ypgkssisat slrvpnddal kywekrlteh dvdhdgiteq gerrvihfrd
      121 penqrltlis detnsgvkgg kvwehssvpa dkgiiglgpv kltvedpapt vkvltevltf
      181 reissypspv ngqddirifs tgkggtgaei hlevrndlak erpgrgsvhh vafrvenede
      241 lakwkdriva eripnsglvd rfyfkslyfr epngilfela tdgpgfatde dtdhlgesla
      301 lpplfegqre eieanlnpld ttrsr
//
LOCUS       WP_010529283             201 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphoribosylanthranilate isomerase [Lentibacillus jeotgali].
ACCESSION   WP_010529283
VERSION     WP_010529283.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..201
                     /product="phosphoribosylanthranilate isomerase"
                     /EC_number="5.3.1.24"
                     /GO_function="GO:0004640 - phosphoribosylanthranilate
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21294
     Region          1..198
                     /region_name="TrpF"
                     /note="Phosphoribosylanthranilate isomerase [Amino acid
                     transport and metabolism]; COG0135"
                     /db_xref="CDD:439905"
ORIGIN      
        1 myvkicgmtt veaakeaaya gadfigfvfa pskrqltpek aaaiskemps svkkvgvfvn
       61 etknaiieta etagldviql hgdesasfae slpfpvikaf rmgkhdtsei rsypchyyli
      121 dspkgpnrgg ngttfdwtrl adagldprkt ilagglnpvn vqsaisiakp agvdvssgve
      181 tdgakdlkki nqfinnakmk g
//
LOCUS       WP_010529354             183 aa            linear   BCT 01-JAN-2025
DEFINITION  cysteine hydrolase family protein [Lentibacillus jeotgali].
ACCESSION   WP_010529354
VERSION     WP_010529354.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..183
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19843
     Region          5..183
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mgkralinvd ytvdfvadeg kltcgkpgqa iednivsitk dfiaaddfvv faidahetgd
       61 nfhpetalfp phniigtqgq elygslasvy aenkdkssvh yfdktrysaf agtdleiklr
      121 ergideihlv gvctdicvlh tavdaynkgf sivvhqdava sfnaaghewa lghfketlga
      181 klv
//
LOCUS       WP_010529362             148 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Lentibacillus jeotgali].
ACCESSION   WP_010529362
VERSION     WP_010529362.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..148
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17502
     Region          14..146
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mdwyiksfqe ltnedlyail klrvdifvve qecaypeldd ydqqgihyfl kdnneivsnv
       61 rilprntife epsigrvava esyrgrgyas emmqkavelv shqwdesiik ieaqehlkyf
      121 yselgfrqvs epylddgirh vdmiwkrn
//
LOCUS       WP_010529377             306 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lentibacillus jeotgali].
ACCESSION   WP_010529377
VERSION     WP_010529377.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..306
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33796
     Region          7..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtktamelid vkktignkdi irglsfeirk gevfgfigpn gagktttirm mvglmglsgg
       61 dvrilgnsin sdyksairev gaivenpemy pfmtgkqnlm hyarmmprvt keriqeviel
      121 vglekpikek agkyslgmrq rlgiaqallh kpsvlildep tngldpagir eirryirkla
      181 eeenvaviis shllseieqm cdriglikng emiaiqdvna ataettdvgi emeaapvnqa
      241 aeilhnehgi natvvndrls lhveretipk ivqtlvnydi qiyqvvttks tledkffdli
      301 gentig
//
LOCUS       WP_010529376             319 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Lentibacillus jeotgali].
ACCESSION   WP_010529376
VERSION     WP_010529376.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 319)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..319
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36301
     Region          <113..316
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mgnffqllvn eqlklyirks twimyilial lvlglafinh namensrtye asqddnwrqt
       61 lqdenaemqk emeqkemmqg aytgqieknn yylendiqpr sydtwqfvme nkfllslvsl
      121 ltiiiaagiv anefkwgtik lllirpitrt kilaskyvsv llfalltllf vlifswivga
      181 lffgvnglnp hivlnqsdgy ayvsiigeii egyglqlitl vmmatfafmi stifrqsala
      241 iglaiflmls gnaivgffsh ydwakyilfa ntnmnqying spmfdgmslg fsiavlavyy
      301 vvflviswvf ftkrdiagh
//
LOCUS       WP_010529378             188 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Lentibacillus jeotgali].
ACCESSION   WP_010529378
VERSION     WP_010529378.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..188
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22286
     Region          5..177
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mreqdaelfy rvqnkdedal eqlydryekl lfsfsyrmtn nkflaeeavq dvftkiwsrq
       61 rhfdeekgkf sswlltvtrn acidllrkkk epayeleerd alhaqeptpe etvewqerge
      121 eirgavrqlt eeqqeiielf yfkrmsqtni aktchiplgt vkgrvrlalk hlkeilaskn
      181 ergvrddg
//
LOCUS       WP_010529385             390 aa            linear   BCT 01-JAN-2025
DEFINITION  CapA family protein [Lentibacillus jeotgali].
ACCESSION   WP_010529385
VERSION     WP_010529385.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..390
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=43842
     Region          55..344
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mkqgqlnwiv llliicvlls actgeeqetp kvanyheasd rvqaiktqkp dtghkeitis
       61 aigdmlihsr vyedartddg gfnfmpmleq vkpylndsti tfanqetmig gedlglstyp
      121 afnspyavgt alnkvgvdvv slannhtmdr geeaiknaie hwekidmmyt gayksegdsn
      181 kmrvyetdeg isvaflayty gtngipipng kdhlvnlidk evmskrigea kqqadavils
      241 lhygtqyerm ptaeqkdlaq faanegvdvi lghhphvlqp idwvegkngh ktlvayslgn
      301 flsgqdefyr riggifrfsi ekamengett vkvkepkflp tfvnyenwan fevvpmyqlt
      361 ddeftnakgh yqeikkhmsr wlpelefiee
//
LOCUS       WP_010529404             252 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Lentibacillus
            jeotgali].
ACCESSION   WP_010529404
VERSION     WP_010529404.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..252
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28384
     Region          14..198
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mfirnersik efmqlypvva wliiiqlvlw lltgflhtpl gnlirdwgmg infaisqgqy
       61 wrlitsiflh aglmhvlfns falvlfgpal eqmlgkvkfi taylgaglig nlatfllgpa
      121 lyshvgasga iyglfgiyaf mvafrkhlid psssqiitii lviglimtfv rsginiyahv
      181 fgfiggfala plilnnvrpy spwlrrqyvd dgsvqfdpnr wqkkkrnkki fknglwiflg
      241 ilvvlglfsr if
//
LOCUS       WP_010529435             154 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Lentibacillus jeotgali].
ACCESSION   WP_010529435
VERSION     WP_010529435.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..154
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=18603
     Region          64..154
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 megcyinthl edyiqnlykf lrinrpeqlt idniakrlnl niyygkfslr fgndlviqks
       61 trqrewqlfg hevghylrhc gnhltlhclf ldmqewqanh fayhfcvptf mlqkienltv
      121 ydimnlfnve hdfavrrlem yqnklykegm nhvl
//
LOCUS       WP_010529465             375 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Lentibacillus jeotgali].
ACCESSION   WP_010529465
VERSION     WP_010529465.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..375
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39726
     Region          <80..>134
                     /region_name="LytD"
                     /note="Beta- N-acetylglucosaminidase [Carbohydrate
                     transport and metabolism]; COG4193"
                     /db_xref="CDD:443347"
     Region          <240..369
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mkhiwgaika igkkkaigwi iglaaaniip iliglilmti mfaiigalgg svdeqqsnqn
       61 npsagyvcsa tgevnqkkwd difqnqkrsg alkghgddii qlseekgldp vlfasialhe
      121 tawgksnaiq qknnpgglmn pdgsglflfs tlkeglesms qtlynrikvd gmvtieqlgs
      181 vyapvgaend pnnlnehwvp ttkeiaqklg gltmnceasa qpdmeligdk awisshtkni
      241 tsgfgnrscg gcssfhagid vasggirgap itafadgeiv iskangttfq ssssnmgtgy
      301 gwyveikhed glrtryahmi ergkpvgtkv eagdvigkvg stgastgahl hfeviingek
      361 vdpmpyvkpf ltgeq
//
LOCUS       WP_010529507              96 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF378 domain-containing protein [Lentibacillus jeotgali].
ACCESSION   WP_010529507
VERSION     WP_010529507.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..96
                     /product="DUF378 domain-containing protein"
                     /calculated_mol_wt=10469
     Region          1..69
                     /region_name="YuzA"
                     /note="Uncharacterized membrane protein YuzA, DUF378
                     family [Function unknown]; COG2155"
                     /db_xref="CDD:441758"
ORIGIN      
        1 mrtiqrialv lviigalnwg liglfqwdlv atlfggqeaa lsrvvytlvg vgalfclpll
       61 fdpvdegehg negvresgnm nyatefseen epfrdk
//
LOCUS       WP_010529508             196 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Lentibacillus
            jeotgali].
ACCESSION   WP_010529508
VERSION     WP_010529508.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22837
     Region          14..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkksrteked lewtrdrilk vaqqlfmekg fravttreia akckitqpal yyhfpdkqsl
       61 yiamlesfvm niqskieais aetiserlea mlevlsrehp asimtmvhdi fvefkeenrr
      121 hiyllwkety ldpfikifee mkedgllrdt ispeeaarfc lltmgqtmst lkyqseslag
      181 qytllvdlil hgtkks
//
LOCUS       WP_010529514             198 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Lentibacillus
            jeotgali].
ACCESSION   WP_010529514
VERSION     WP_010529514.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23689
     Region          6..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 makkedrrir ksrqlikeaf idlmhekgfr gisvydiadk adinrgtfyl hyqdkfdlfe
       61 kyvdellnel iatieisnqe ketlnkqkmr erqpyveffk hfqehacfye amfkyqgdty
      121 fynrfidifk nhfcqeikkl rihddwlkvd kaflihsmvy ahlgsinywi engmsdsaet
      181 mgeqlntllc aiarvghd
//
LOCUS       WP_010529565             531 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lentibacillus jeotgali].
ACCESSION   WP_010529565
VERSION     WP_010529565.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 531)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..531
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59923
     Region          9..515
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mkvlkgyqkp iievhnfsfs yeevdeqrlf dgldfklnqn evtllmgpsg sgksslalcl
       61 nglypeaveg tssgdifflg eniqeyekge ltqeigivfq dpesqfcmit vedelaftle
      121 nrkipasdir griesvlrav gmkgfnqhki hefsggqkqk ialaavllle pkllildept
      181 anldpvssle figlvegiqr eqqisvliie hqaeewlrli drilvmgsdg lllasnvper
      241 lfieerqlle regiflpgky snrpafrerw hwdvqsdekv lsarglsfsr gkqdvlkkvn
      301 mdirggefva vagengagks tllqllagll epgegeicmf drplrkwqen dlrkrmgfvf
      361 qnpehqfitd tvyeeltfgm klngyaeeem kntaeglmeq fyltehrhsn pfalsggqkr
      421 rlsvatvlde tpdvllfdep tfgqdaattv elmdyvmglk akgkaiifvt hdmnildtad
      481 rvdvleqgkv afsgppdslw qerkllsear lllparlrqk qregeiydli h
//
LOCUS       WP_010529552             219 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lentibacillus jeotgali].
ACCESSION   WP_010529552
VERSION     WP_010529552.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..219
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23946
     Region          3..217
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtlvmenvsk vykdgpkefk aldhaslevk sgefiaiigp sgsgkstmls iagallapts
       61 gkvlldgedv aelsaqkitr qrlrkigfvf qaanlipylk vedqlqvinv iaknkgesks
      121 sellkhfgld hrtanypsel sggerqrvai aralindpkl iladeptasl dskrgrevve
      181 mladeiknre kagimvthde rvldmcdrvv kirdgrlkk
//
LOCUS       WP_010529573             214 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Lentibacillus jeotgali].
ACCESSION   WP_010529573
VERSION     WP_010529573.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 214)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 214)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 214)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..214
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22826
     Region          1..208
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mmeffaehgn elviktwehf yislaamllg vivavplgvl lsrvpkladr lisfvgilqt
       61 ipslailaff ipivgigkip ailalffysl lpilrntyig vrdvdqgvve agkgmgmsnw
      121 qsvlkmelpl slpvimagir lstvyligwa alaafigggg lgdfifdgln lyqpslilag
      181 tipatilavi adrslalles kltpeglkds yeaa
//
LOCUS       WP_010529631             187 aa            linear   BCT 01-JAN-2025
DEFINITION  GbsR/MarR family transcriptional regulator [Lentibacillus
            jeotgali].
ACCESSION   WP_010529631
VERSION     WP_010529631.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 187)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 187)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 187)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..187
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21221
     Region          8..170
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 meanddiqki eesrdilisa iaqtmviygv tpsvgriygv lyfadkplnl ddikdqvams
       61 kgsvstglrd lldtemvikv wkkgdrkdhy iaekdffknf fafftkmlrq erniisrane
      121 qvegtlkdia vngdseeake maqgdlqdie qtmtyfdwtl rlanamesre ifnhfpkykg
      181 gdsagqd
//
LOCUS       WP_010529674             709 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Lentibacillus
            jeotgali].
ACCESSION   WP_010529674
VERSION     WP_010529674.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 709)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..709
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79245
     Region          1..>46
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          77..704
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mqcqncgirp asinvamqin nermnmhlcn qcfreiqgsm mngdngqgqq gdfankffqg
       61 ngqqgqgftg tttqqgagnn glldqlgknv tnaaraglvd piigrdnevk rtietlnrrn
      121 knnpvligea gvgktaiaeg lalkitegkv paklmdkeiy lldvaslvan tsmrgqfeer
      181 mkqlvqelqe rqnvilfvde ihllvgagta essqmdagni lkpalargel qligattlne
      241 yrqiekdaal errfqpimvq epsledavki ldgikdryek fhevrysdea irafvtlsqr
      301 yiqdrflpdk aidlmdevgs rlnldnaekd sdsiqsrlde ivrekeaaae kedyeeaahl
      361 ryqeiqlqkq ldkakdeeqv tdvdisdiql iveektgipv tklqtdeqek mrdlgknlge
      421 kvigqdeavq kvakavrrsr aglkskyrpi gsflfvgptg vgkteltkal aeelfgsrds
      481 lirldmseym ekhatskiig sppgyvghee agqltekvrr npysilllde iekahpdvqn
      541 mflqimedgq ltdshgrtvs fkdtviimts nagtgekqin vgfnrdehes vqtlenlsdy
      601 fkpeflnrfd siitfnelae esllqivdlm laeleetiee sdisisvtde akhelvqlgy
      661 dprfgarplr rviqdkiedq ltdlvleees ieavnvdvkd geivvgkte
//
LOCUS       WP_010529737             261 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Lentibacillus jeotgali].
ACCESSION   WP_010529737
VERSION     WP_010529737.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..261
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29499
     Region          3..257
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mlktimfdld dtliwdeksi deafkaacrl aaqksdadpn lletkireha qslfasydty
       61 eftemigisp feglwgefdd egesfrqlne iapiyrkesw akalkeagvd dpqlglelae
      121 afqeerrknq yvfeetfdvl nklrgdyqll mltngspdlq qtklnitpei kpyfdhivis
      181 gafgkgkpdp sifdhalsll saekdevlmv gdnpnsdilg asragvqsvw inhqkyeigd
      241 nnptfeitrl eellevlakl d
//
LOCUS       WP_010529792             321 aa            linear   BCT 01-JAN-2025
DEFINITION  S8 family peptidase [Lentibacillus jeotgali].
ACCESSION   WP_010529792
VERSION     WP_010529792.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..321
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34368
     Region          44..283
                     /region_name="Peptidases_S8_Subtilisin_subset"
                     /note="Peptidase S8 family domain in Subtilisin proteins;
                     cd07477"
                     /db_xref="CDD:173803"
     Site            order(49,84,127,152,181,248)
                     /site_type="active"
                     /db_xref="CDD:173803"
     Site            order(49,84,248)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173803"
ORIGIN      
        1 makmhlipyq veeiedtake iprgiqmiqa pdvweqaneg dgnviaiidt gcdtnhpdlk
       61 gqvvdgknft sdgeetdysd gnghgthvag taaaaakeeg iagvapnakl lvvkvldeng
      121 sgdyqwiidg inyatdwegp ngekvraism slggpqdlpe lyeavkrain sgipvvcaag
      181 nqgddrhdtd etafpgayne viqvgainyd rdiapfsntn deidivapgv dilstytdqk
      241 yarlsgtsma tphvsgalal visiaetqfd rklteaelya qlvrrtvplg ypksaegngl
      301 valdilnrfe nlfqtfntaf k
//
LOCUS       WP_010529803             156 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [Lentibacillus jeotgali].
ACCESSION   WP_010529803
VERSION     WP_010529803.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..156
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18154
     Region          7..153
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 msenqetyea qtteavnhry agfwmrfway ladliivfsi ngillspfkf mndgngidig
       61 lwtaggiiga ivlylyfllm tkffrktlgk mifglrvvre draplewsdl ifrevigrfi
      121 hrvfwftnll ylfvafgtqk qgihdmfgnt rvvfdr
//
LOCUS       WP_010529813             229 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Lentibacillus jeotgali].
ACCESSION   WP_010529813
VERSION     WP_010529813.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..229
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25964
     Region          5..216
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mepilerlsp qeydilidas neihipknsf vfregtsaeh iyfliqgkvr vykkiesnke
       61 ltiftrgmyd gigeigvfgg vnysnsakal qdsvlyvidr ktieeilsqn grislhftrw
      121 iaesleaska kirdyiafgs egavasvfvr fsnmygvvtp dgvritepvm iqdiskhiai
      181 sretvsrivn kwkeqdivdn enkffliknm aylknllmcd hcsvencvl
//
LOCUS       WP_010529823             396 aa            linear   BCT 01-JAN-2025
DEFINITION  NupC/NupG family nucleoside CNT transporter [Lentibacillus
            jeotgali].
ACCESSION   WP_010529823
VERSION     WP_010529823.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..396
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42122
     Region          15..396
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mdillgilai iivlglaylm sndkkninyk glgimllaql iiawfmlyts vgrtviewis
       61 agfnkliefg tagvnfvvgg iqiaeggsvf ffnvllliif fatllsvlty lrilppiiky
      121 lggllskitg lprvesfnav nsiffgqsea llaiktqfhh ldnnrlyivs asamgsvsas
      181 ivgaylqilp peyvlaalpl nmfsalilss viapvnipee edkvdvqevs hdksifeams
      241 ngaldggkia livaamliaf iaslelvnwl iqlvfagvtl qeilgyiiap igilmgispa
      301 evieaggvmg tkivtnefva mlefeqmlgs msektigivt vfltsfanfs sigiiagtvq
      361 gidskkavqv sgfgmkllig atlasilsat maglfl
//
LOCUS       WP_010529828             271 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Lentibacillus jeotgali].
ACCESSION   WP_010529828
VERSION     WP_010529828.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..271
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=30228
     Region          110..>264
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mdndqrnrds idddlyeeld eeelyelveq erekalarar enknrkprpp fpkwvfwlia
       61 aamllnvisl iprtfsipai dflissaqls tqddiqayke svvvieteds rgtgfsisad
      121 gtiitnhhvv edeesvtvay peeglfsgdv vasypsvdla vldvsgeqmp hleladkatf
      181 epgdeqvyfi gnpirfsgia nkgrvldrle lsgwekpvvm meapvyrgss gspvinqngk
      241 vigivfatlh hdthgrvglf ipieyyhnqh g
//
LOCUS       WP_010529843             399 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Lentibacillus jeotgali].
ACCESSION   WP_010529843
VERSION     WP_010529843.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..399
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42992
     Region          14..392
                     /region_name="MFS_YfmO_like"
                     /note="Bacillus subtilis multidrug efflux protein YfmO and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17474"
                     /db_xref="CDD:341027"
     Site            order(24..25,28..29,32,64,119..120,122..124,127,148,
                     151..152,155,229,232..233,236..238,241,269,273,324..325,
                     329,333,349,352..353,356..357,360)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341027"
ORIGIN      
        1 mkqqlteqek rwavislasi plimtlgnsm lipilpvmeq elgisklqss yiitsysvia
       61 iflipvagfl sdrfgrkkvi ipaliitgag glvaglasqm manpflvila grilqgigss
      121 gafpivlplv gdmfkddkea sttlgiiets ntvgkvlspi lgaalaaliw yipfysipvf
      181 caasvllvaf miknkggeen qtkfkeylgl akdilkehgr wlfavfiiga ilmfilfgfl
      241 fylssileeq ydyegiwkgi llavpllals iasfitgrki kdnlnvmkwv tfigiiltga
      301 svavipftdh pfyllaiflv cgtgigmalp cldalitesl eksvrgvits iysamrfigv
      361 aagppviaim mkgniswias llaafaliag flgyrnikp
//
LOCUS       WP_010529867             157 aa            linear   BCT 01-JAN-2025
DEFINITION  GbsR/MarR family transcriptional regulator [Lentibacillus
            jeotgali].
ACCESSION   WP_010529867
VERSION     WP_010529867.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 157)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 157)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 157)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 157)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..157
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18239
     Region          4..155
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mrkstlehat ydvilefakt iemfgasple arlfvylylq dqpktldemg ealgksktsm
       61 stsirslsda klvtlvwkkg vrkdlyeann qlfkrfmsny vnkwldassh qknalrdiqq
      121 nledydteqs reivdnlnki idfheqiess frklqhn
//
LOCUS       WP_010529958             141 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Lentibacillus jeotgali].
ACCESSION   WP_010529958
VERSION     WP_010529958.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..141
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16168
     Region          9..140
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 miiktvetse ekqlaydvrt nvfvheqnvp peveidefde qaihligykn dvpiaacrvr
       61 fldhygkler icvlkdqrgk sygselihtm edvirkegye kaklnaqtha idfyqrlgyd
      121 vvsgefmdag iphvtmkkil k
//
LOCUS       WP_010529976             284 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Lentibacillus jeotgali].
ACCESSION   WP_010529976
VERSION     WP_010529976.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12134272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..284
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33003
     Region          <26..122
                     /region_name="Acetyltransf_3"
                     /note="Acetyltransferase (GNAT) domain; pfam13302"
                     /db_xref="CDD:379112"
ORIGIN      
        1 msktirmldi nddphyeamd tgiefdyvgr ifdrlttgnn rlyglflddq lvsvggysiy
       61 adsyamlgrl rsdrrfmgng fstevvsyvl qealnvegih wigantqehn isaqrvleki
      121 glspyitlhg altkatsale sgaapwqpvi dlqrkkdwvn qlyiqtraif pyecyypfps
      181 sadllqdqdl qqwsfyenea ktrflitkyd qkkhhylhav ypwhditsqp glwetiardy
      241 rkllqhtdde tyiwmdltke eartlpadhq felpspwily gkek
//
LOCUS       WP_010529989             317 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Lentibacillus jeotgali].
ACCESSION   WP_010529989
VERSION     WP_010529989.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..317
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34867
     Region          2..294
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(33..34,37,89,103,105,134,167,254,257,293)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(224,229,244,254..256,259,281,285)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mdvvtlgetm vlftpehagp mrysdrfssr vagaesnvai glarlgvqsg wmsrlgndef
       61 gkkirsfirg egvdtsrvif detadtglff keklangewr vkyyrrdsaa srlkpedlde
      121 syiagakylh vtgitpalsd scyetvlsai eyakrhdvkv vfdpnlrrkl wpehkarkvl
      181 velvrkadiv lpgieeaefl fgigspeela rqfneqgast vimklgeega yylthdtery
      241 vegfrvtevv dpvgagdgfs agvlsglldg lnledsvqrg naigamavla agdieglpek
      301 drlidfmhnr gqgdver
//
LOCUS       WP_010530041             242 aa            linear   BCT 01-JAN-2025
DEFINITION  M48 family metallopeptidase [Lentibacillus jeotgali].
ACCESSION   WP_010530041
VERSION     WP_010530041.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..242
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28495
     Region          1..239
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mpsiqygkti iyynhyiqsr kdvkisidlv ngvevfapkt itnvkltqim qrkaewitnk
       61 leelneants vqtkefvsge klpylgrhyr lkvlkepvqn adiqmkqgrf fatvphnwsh
      121 kktqrtlerk liewyrqygi kkieeraghy qamlgvspns islriqhkrw gtctpngdiy
      181 lnwriimapv riidyvivhe lthlivpkhn dkfwrlvktt lphykeskew lrvhgvelhc
      241 ig
//
LOCUS       WP_010530050             292 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Lentibacillus
            jeotgali].
ACCESSION   WP_010530050
VERSION     WP_010530050.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..292
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32270
     Region          3..281
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mekfegvyis lvtpmtkdyk vdykrlseic ewligkgvdg lipagplgey atlsneerrk
       61 vvetvikask rrvsvivgtg asatrdvidw akhaksnead gilalppvny kplenevith
      121 feaisevgip iiafnnprdf gvdlspdlla kisesenivg vkefsgdirr vqeilektnl
      181 evfvgvddla megalcgasg wtsgvsnalp eegiklfqla kerrfeeasi lyrdlvklfh
      241 ydanpqliqs ikymmelagq pvgptrpprl altnkaykei ehhfnkaint ea
//
LOCUS       WP_010530058             439 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Lentibacillus jeotgali].
ACCESSION   WP_010530058
VERSION     WP_010530058.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..439
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46197
     Region          22..439
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mlditfigii cillllifia igvpvgisfi tsglistfli ldgaraiall vgsahssiaa
       61 pswvaiplfi llgalavqsg latkafrsad avasgipgsv giatclatag fgaisgasia
      121 atsifgkmal pemrklgynk sfssgiiasa gtfasmipps mmfiiyalft qtsvaglffa
      181 giipgllsav iysiyiyirc kndpammkrq kaqpeltvkq rfsamgeswp iilvavallg
      241 giytgiftpt esaavgcili vvigfiqghf rkfdafsgal rdsanttsmv flinigalfy
      301 akvlalsqmp anltsyfvnl dvppiviiii isliffllgm imvpigiyal ilpivapivs
      361 glgydliwfg vialklteig avtppvglnv yalkgvvsrd ititdifkgv tpfviidifv
      421 livliafpil slwlpnllf
//
LOCUS       WP_010530081             324 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Lentibacillus jeotgali].
ACCESSION   WP_010530081
VERSION     WP_010530081.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..324
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33991
     Region          2..317
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mkllvigear dgelrnvtfe avvaakqids naeivgvlcg sddlnksgqe viyhgadrvv
       61 tvthdnlesy tsegysqavm aviedespdg ivmghtaigk dltpklaakl gtglisdatd
      121 iendgdkavf irpiysgkaf ekkmitsglt fatirpnnip alerdasrsc dvsskeveik
      181 dintvikdvi rkasegvdls eaniivaggr gvksadgfep lyeladvlga avgasrgacd
      241 aeycdyslqi gqtgkvvtpd lyiavgisga iqhlagmsns kvivainkdp eanifnvady
      301 givgdvfevv pkltkgltnl nvga
//
LOCUS       WP_010530116             226 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Lentibacillus jeotgali].
ACCESSION   WP_010530116
VERSION     WP_010530116.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..226
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26334
     Region          2..217
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 maklsmkeyv yqtlkyaiye qklvpgqkmv ehdissslsi srtpirqaft qlqeegflti
       61 lpnkgaqvin ptieeiteaf thrknlella tsnimqaist nnihrlselv klekesyqqk
      121 dllgytevnk efhytllkgc rnrflknhtl kminqthiyl alydhffhid ekenirssne
      181 hqmlitlike keieafsqll akhistatee yksrvsrfhq asdlfn
//
LOCUS       WP_010530129             260 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Lentibacillus
            jeotgali].
ACCESSION   WP_010530129
VERSION     WP_010530129.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..260
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28228
     Region          7..254
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msqegnvrik keggmfwltl nrpgarnald tamlseigqa ideaerddti kvvmvkgege
       61 ksfasgadik qlydkqplea llpgmqalyd kieslnkati alvdgyalgg gcelamacdi
      121 riaskkakfg lpelnlgiip gaggtqrmar migkgrtldm iltgkmidgr eaeriglvny
      181 fvqeeeslid kaktvageil kkgpvaiqia kmavhkgydm degtamwlek lsqavvfgte
      241 dkkegtkafi ekrkakfqnr
//
LOCUS       WP_010530130             386 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Lentibacillus jeotgali].
ACCESSION   WP_010530130
VERSION     WP_010530130.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..386
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42678
     Region          1..380
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfnlpeeie flrenvrkfv kdevepvamd ieenneipek iikqskemgl fslsipeeyg
       61 glgldmvgks aifeelgkth ngfttligah ngigsagive lgneeqkqky lpkmatgewi
      121 gafaltepta gsnaanlktt aekkgdkyii ngskhyitna vdanvftvma vtdsskgakg
      181 itsfivekdf pgftlgnvee kmglrgshsa elffedmevp tenvlgeegq gyvnalkila
      241 ngraglaarn lgscdklleh clsyanereq fgkplleiqt vqnmladisl qietlrslty
      301 rvawmtdqkq rvvkeaaiak lygsevynni adlavqihgg igymkdypie ryyrdaritk
      361 iyegtseiqr niisgelire lkrkeg
//
LOCUS       WP_010530134             304 aa            linear   BCT 01-JAN-2025
DEFINITION  ketopantoate reductase family protein [Lentibacillus jeotgali].
ACCESSION   WP_010530134
VERSION     WP_010530134.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..304
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33179
     Region          1..304
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkigvagaga vgsffgallh kgghdvifla rgkqleklse qglsiqgesg nlhiggefte
       61 dpyglaqsdl ilfcvksndt eqmakqllpi lkegsavltv qngvdneekl qrifganrll
      121 saatyvqvfm eapgqvrqrg rvklvigeve srasgkakmm teeirsagid akyssniler
      181 kwkkllwnit fnplsamvev kvgeildssp lrktaenicr ealataaatg mivdqekafs
      241 tifsnaelar shqtsmlqdr qqgkemeves mcgyvvrkaq klgvatptle tiyhlltfmn
      301 eknq
//
LOCUS       WP_010530142             134 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Lentibacillus jeotgali].
ACCESSION   WP_010530142
VERSION     WP_010530142.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..134
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14917
     Region          1..133
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mdkliedvrn sfesspffsh vgfeiiefee gnvilklpir kqllnandsl hggvhatmld
       61 lvlgmairsm trtrcttisl ninylnpste geiiyatgni lkqgyrmvva egeikdendn
      121 ilakgmgnyk lird
//
LOCUS       WP_010530170             231 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Lentibacillus jeotgali].
ACCESSION   WP_010530170
VERSION     WP_010530170.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..231
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26967
     Region          <80..214
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 mttkyqrlfk neqeeshfwp sftdlltiil lcfilifiam miikslqiee mkrtidqlmg
       61 vrselvndlq defsdsamgi evdeetgaii fnteilfeyn kselkpesfq fldefvpkyl
      121 dillqngyed yiaeiiiegh tdrdggylyn lelsqerahs vaayilsddf pykniqqhlk
      181 ekltvngrsy tdfrtddagn ysadasrrve fkfrlkdeei lektreilge s
//
LOCUS       WP_010530140             257 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Lentibacillus jeotgali].
ACCESSION   WP_010530140
VERSION     WP_010530140.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..257
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28213
     Region          1..256
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mnifvllkkt fdteekikin dgqieedgae yiinpydeya veesiiqrde hggevtvvti
       61 gddesekqlr talamgadka vlintdedle dgdqsttvki lesffddkea dlifagnvai
      121 dessgqvgpr laealdiscv ttitslkidg dtasiekdve gdvemvesal pllvtcqqgl
      181 neprypslpg imkakkkple eleiddldle eeelepktvt idiflppekg agkvlegevd
      241 dqvrelvtll kdekkvl
//
LOCUS       WP_010530196             469 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Lentibacillus jeotgali].
ACCESSION   WP_010530196
VERSION     WP_010530196.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..469
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50635
     Region          19..457
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,144,
                     147..148,151,275,278..279,282..284,287,315,319,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 mentetfnwk kyvplfavll sgafitilnq tllgtalppi mqdlnlsest vqwlqsvfml
       61 vngimipvta flidkfttrk lfltamglfa tgtlvaaisp nftflmaarv lqasgagimm
      121 plmqtilflt fpvhrrgtam glfglviafa paigpslsgf lvdqfpwrsv fyvilpiavl
      181 diiaayfllr nvteqknpsl dilsvilsti gfggllygfs tagnagwlsl qvilsivigi
      241 vslylfitrq lklkepllef rvfkhgtftl atglgmvvfa amigtniilp lymqnmigfs
      301 alksglvllp gaiimgfsnp itgylfdkfg gkwlarggll llalttfaft nlsmdtsfty
      361 latmngirmi siamvmmpmt tlalnqlpdq liphgtamnn tfrqvagsig tailvtimst
      421 aaipdetvsg lihgvnvsfi aagiaailgf ilsfklkedv kpgdrlskh
//
LOCUS       WP_010530204             157 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Lentibacillus jeotgali].
ACCESSION   WP_010530204
VERSION     WP_010530204.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..157
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17404
     Region          5..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtsnldehdk ailrelqeda sisnlnlskk iglspsacla rtknlaetgv ikkfttivde
       61 kklgievtai alinlsplnr etihsfledi nkypqvqecy tltgshdyml kiitkdmesy
      121 rnfiidslmq npavsgvdts mvmstekrtv svpidev
//
LOCUS       WP_010530207             151 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Lentibacillus jeotgali].
ACCESSION   WP_010530207
VERSION     WP_010530207.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..151
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16941
     Region          17..139
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mgkridelqi hekhyvqire qvkndpyaqa lgiqltklea gfaeavldvq shmvnayrtv
       61 hgaviyalad hafsaacnay grtslglstt iqfiesakpg dkivarttei krnyrtgfyr
      121 tdiyhgqnli atmdavsyrk gqffieldeq e
//
LOCUS       WP_010530278             449 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Lentibacillus jeotgali].
ACCESSION   WP_010530278
VERSION     WP_010530278.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Kaatz,G.W., DeMarco,C.E. and Seo,S.M.
  TITLE     MepR, a repressor of the Staphylococcus aureus MATE family
            multidrug efflux pump MepA, is a substrate-responsive regulatory
            protein
  JOURNAL   Antimicrob Agents Chemother 50 (4), 1276-1281 (2006)
   PUBMED   16569840
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..449
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48649
     Region          12..434
                     /region_name="MATE_MepA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Streptococcus
                     aureus MepA; cd13143"
                     /db_xref="CDD:240548"
ORIGIN      
        1 mslaeqkllt qsvtksffhy llptlvgmml msanividgi fvgngigsva lasvniavpv
       61 wsiiisisll igigggtlys iatgerdtdr aqrvftlsml lvtivimiig ltgyiasepl
      121 arlfganadt lsyamdymqi iflwapviaw entlsifvrn dggpqlamag livsallnii
      181 lnywmifilg mevagaalas viataaglli ytihffkkda glkfiltkwk kddmlmvskl
      241 gfpnflseag tglfvigyni alsyyagttg laafsvinyl htfvflafig igtsiqpmis
      301 fyygakkyes ikntvkvaei tglvlgisfl aigwfgaggl vsifgvetea irqlaikgit
      361 lfftgylfmg infiymtyyq siayvvpsig itlfrgfill vaaliilpll fdttgvwlal
      421 paaegltatf lvlfarrgvm nrqwrsqgy
//
LOCUS       WP_010530296             126 aa            linear   BCT 01-JAN-2025
DEFINITION  RidA family protein [Lentibacillus jeotgali].
ACCESSION   WP_010530296
VERSION     WP_010530296.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..126
                     /product="RidA family protein"
                     /calculated_mol_wt=13880
     Region          1..125
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mtrktyeakn aivsgpysha vdagefvyfs gqtaknapta admsgdiqaq trqcfanlfd
       61 vletsgltsd dvvkvnvylt smkhfatmne vyetqfrepy partcvavle lpleaeveie
      121 miarrt
//
LOCUS       WP_010530298             553 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Lentibacillus jeotgali].
ACCESSION   WP_010530298
VERSION     WP_010530298.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..553
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=63358
     Region          6..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          249..543
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mktlndlfil dgmkecvvla ghrgltrnve svnisdtpdv iqflyknhll lttgygfynd
       61 tnqfcelire mhdlncsgii ikvnrffyki peeaklladd lafpiidlpt nrtlgdlsrh
      121 ilnylndhea eqlyyalhvq qefsdmmvkg ynlnslvehl ghflvrpvll lnhrgemiar
      181 shdfrmdsmk laeteivaai reetapyqdg ttfnipslkq qtvttfpvkt krqqpsmlvi
      241 infqtlpyps sqmaveqagn visstlikeq aieensrllk nnffadliek rvqaeeeims
      301 rtafygllpd kesicvlcsv dsegdnyetl qlyekkigel hnsiydqled eiingnmqat
      361 lftkekffvm ilqfnqytea eirmvteftk qaqnhvqgey svsfgisnpv esvteipnay
      421 qeaaeaidng yddnmtgfin fyktreikel lntlprkdik alyenalksl aypktkedqe
      481 lvktieiyld cqceisdtar klyihrntvk yriskaeell dcsfrnpads lrvrvaltig
      541 sileeeaqtp spq
//
LOCUS       WP_010530317             288 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Lentibacillus
            jeotgali].
ACCESSION   WP_010530317
VERSION     WP_010530317.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..288
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33315
     Region          3..>129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtqrheelld aaiqlfqksg ihavsvadit eacgiskgaf ykhfdskenm ilellkryyd
       61 emfreadrft eefnqsplmi lkrkitiele ksieyrsffl alltefppye kgpipefldr
      121 iqqthqqwhk qalldafgsk skkymddltl vlegilhsyl mqiiwkgpal pldrlgdfia
      181 ecikaivend eaispllpvy snadseasil eiigndlhtl rtemntdrar ysqkdlqtid
      241 llieeltqek preflvdall aqlhrrtylk tgitkimtsw evwkgdlt
//
LOCUS       WP_010530335             404 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Lentibacillus jeotgali].
ACCESSION   WP_010530335
VERSION     WP_010530335.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..404
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=44563
     Region          3..396
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mskpkivvlg agyagmmttk rlmqklspee aelvlvnkhn yhyqttwlhe vaagtrnqnq
       61 armmisdvin ptrvnliyde vvevkkdenr vvlknseity dylvislgfe tntfgikgme
      121 knafsitdid ssrmirehie yqfakystak npkdedlail vggggftgie fagelvekvp
      181 elckkydidr skvriinvea mprvlpgfdd dlvayakesl aeggvefreg akiseckkns
      241 fvigdgddae eikagtivwt ggvtgssils ksgfditkgk vtvdgdmrap deenifilgd
      301 cawvmneeeg kpfpptaqaa mqhadtcsdn lkallrnepl skfvfddkgt vaslgskdam
      361 gtvfndnkly gkpavsmkkv idnrylfllg gpklilkkgk lrml
//
LOCUS       WP_010530383             278 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Lentibacillus
            jeotgali].
ACCESSION   WP_010530383
VERSION     WP_010530383.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..278
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30252
     Region          3..278
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 meifgisidl agllgsvvpv vlqiglmila fiilvpigkk vigktlnkag snqklspsrv
       61 ktleklllnv fsyvmffvlv lmifgaldip lgpilagagi iglaigfgaq glvsdivtgf
      121 fillerqlei ddyvttagyd giveeiglrt tkirsfdgtl nyvpnryieg vanhtrgnmr
      181 alvdisiryn dnldqaiavl eevcaefked erfkegpdai gvqgfgtsdi vlrvvgqten
      241 glqweceram rrqikeafdh agietpfpqq vavhsnqd
//
LOCUS       WP_010530449             456 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Lentibacillus jeotgali].
ACCESSION   WP_010530449
VERSION     WP_010530449.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..456
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50006
     Region          22..456
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mlfttkwltt vfsdykgaav deveivevtt dsrrklkksl fiplagenfd ghhymkdafd
       61 qgaaaalwdk hkalpeslpa dfpvffvndt ltamqelaka yrkkvnpvvi gvtgsngktt
      121 tkdiiasvvg ssykthhteg nlnnqvglpl tilsmpldte alvvemgmnh fgeietltki
      181 aqpnyavitn igeshieflg sregiarakl eiikgttkdg yllidgdepl lrqvhqrehv
      241 ikcgyhtnnd vtirninitr qstqfelsdg gsytipllgs hhalnasfai tigrllniat
      301 dnvkqaltgl eltsmrfelm ngkngssiin daynasptsm kasinavkhl dgfhqkvlvl
      361 gdvfelgqns kplhrsvads idesmsavlt fgedadeiss avykqhpaid srhftskeal
      421 mnalneyise gtlilfkasr gmqfesfikq vidpsh
//
LOCUS       WP_010530744             509 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Lentibacillus jeotgali].
ACCESSION   WP_010530744
VERSION     WP_010530744.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..509
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56223
     Region          5..507
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 msstedfkhr vetikqggqe kyhrkneekg klfvrkrlel lfdedidied affanymdgd
       61 lpsdgvvtgi grvngqdvcv mandstvkag swgkrtveki vriqetaakl eipmlylvds
      121 agaritdqve mfpgrrgagr ifhnqiklsg rvpqvcllfg psaaggayip afcdivvmvd
      181 gnasmylgsp rmaekvigek vsleemggan mhcsvsgvgd vlvkseeeai tytrnyldyf
      241 panfrhqpag aepkdvkafe ksitelipen qnspfnmhdf ieriidensf cevkkkfape
      301 litglsring ksvgiianqp rmkggvlfpd sadkgakfiq lcdafnipll flmdipgfmi
      361 gtkveqagii rhgakmlamm seatvpkisv vvrkaygagl yamagpafep daclalptaq
      421 iavmgpeaav navyankiae lpeeerpqfi kekqeeykdn idiyrlasem vidaivdped
      481 lrhdlikryk iyeaknttft drkhgvypv
//
LOCUS       WP_010530683             241 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Lentibacillus jeotgali].
ACCESSION   WP_010530683
VERSION     WP_010530683.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..241
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27723
     Region          5..240
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mslkmdsrhl ylqvidqikr diengkyktk qklpsefqls kelgvsratl realrileee
       61 nivtrrhgvg tfvnpkpifs sgieqlnsvt ymieqsgktp gsqflsteil eptedeqvkf
      121 epkkistlak iervrtadnl pvvfcidklp eglipldrvh qtdsifklie essgkeiaya
      181 vtyiepvgyh driyeilkcd pdqsllllkq mhytnedepv lysanffrsd vfsfhvlrkr
      241 m
//
LOCUS       WP_010530871             391 aa            linear   BCT 01-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Lentibacillus
            jeotgali].
ACCESSION   WP_010530871
VERSION     WP_010530871.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..391
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43215
     Region          1..380
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mkkfvlltsi ifsilfmpft vfgeengqdd tdqelnlapd aqsgvlmerd tgkllfdkna
       61 heklppasmt kvmtlllime sldkgkidkn etirvseraa smggsqifle tgeemsvnnl
      121 lkgiavasan dasvalaeri agsekafveq mnkkakalgl entqfqnstg lpaenhysta
      181 hdmavmakel lkyesvteyt siyedylrkg eenefwlvnt nklvksypgv dglktgytne
      241 akycltatae kndmrmiavv mgadttkern stitgmldya fnhfetknly ekgqtittle
      301 llkaedtsid vttsesisti hrkgendknv ktsvnlesdl dlpidkgdqv gelivksnge
      361 tlsktplivd ydvkkasylt llkrtaqnmv k
//
LOCUS       WP_010530783             360 aa            linear   BCT 01-JAN-2025
DEFINITION  type III polyketide synthase [Lentibacillus jeotgali].
ACCESSION   WP_010530783
VERSION     WP_010530783.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..360
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40147
     Region          2..358
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 miasigtgip pnertqpevk slvreifkqh dskliqrlqp vfdhaqidkr qfavetkwfk
       61 eahtfqekns lyhelaikhs leavdsclsn rkflkepipf eavdmiifvs stgiatpsld
      121 tymmakrpfr edtsrmplwg lgcaggaigl srafdwirah peknvllvcc elcsltfqkd
      181 dynksnivgt alfgdgagaa lvmgnkspyl pyskqskpri ietssatkkn shsvmgwdit
      241 nrglevvfsk sipalvrsfw skhislflnn vnidhvhsyi ahpggrkvle amteilqipq
      301 ekikhscnvl rdhgnmssat ilyvlnewmq egiapgsksv lsalgpgfss ellllewhes
//
LOCUS       WP_010531283             300 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Lentibacillus
            jeotgali].
ACCESSION   WP_010531283
VERSION     WP_010531283.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..300
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33412
     Region          4..288
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mdfvsdwlvd lwavvtgtsl wmdigkallk aiailvialv ivrvgnkvig rvfesrsrgp
       61 lriterrevt ikkliqnsmk ytvyfiafim ilddafgfdi gallagagva glaigfgaqn
      121 lvrdvisgff iifedqfsvg dyiftagveg fveeigmrtt kieswtgeqh vlpngnvtqv
      181 tnysihngla ivdvnvpyen dvaaaeeiig dviktlpdqy eeivkvpeif gvevldtshf
      241 vlrviaetlp syqwkgarni rkeikevlyk egiqipaprl imysrnqepe slqidperem
//
LOCUS       WP_010531310             124 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Lentibacillus jeotgali].
ACCESSION   WP_010531310
VERSION     WP_010531310.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..124
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13746
     Region          13..>88
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mqtmhmpkwi syavgyvfla sgtlklvssd fkatfmnlgl pspetmlllv alteiacsaf
       61 ilarlyvrha aapliliilg alyltklpil mnqgflqfaf darldivmli llillwqhkp
      121 akql
//
LOCUS       WP_010530752             214 aa            linear   BCT 01-JAN-2025
DEFINITION  RlpA-like double-psi beta-barrel domain-containing protein
            [Lentibacillus jeotgali].
ACCESSION   WP_010530752
VERSION     WP_010530752.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Castillo,R.M., Mizuguchi,K., Dhanaraj,V., Albert,A., Blundell,T.L.
            and Murzin,A.G.
  TITLE     A six-stranded double-psi beta barrel is shared by several protein
            superfamilies
  JOURNAL   Structure 7 (2), 227-236 (1999)
   PUBMED   10368289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15349727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..214
                     /product="RlpA-like double-psi beta-barrel
                     domain-containing protein"
                     /calculated_mol_wt=24330
     Region          43..131
                     /region_name="DPBB_RlpA_EXP_N-like"
                     /note="double-psi beta-barrel fold of RlpA, N-terminal
                     domain of expansins, and similar domains; cd22191"
                     /db_xref="CDD:439247"
     Region          141..213
                     /region_name="DUF3889"
                     /note="Protein of unknown function (DUF3889); pfam13028"
                     /db_xref="CDD:404048"
ORIGIN      
        1 mysktnpyft nlypyayhpy daaqqlhyqd vmypdfrqqf vsgqatwteg ggltkcgipw
       61 sdnlymtaav genspyqcgq tlhisypvtg rsilveivdq vpgypdnrln vhrrvfetlg
      121 anpqqgvidi qiapvsqveq qqwgryllei tqtaysgyni teynfvnktq espsrtrety
      181 eyslqsvqet itvrasvvyn pgnnrvisld ikev
//
LOCUS       WP_010531005             202 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Lentibacillus jeotgali].
ACCESSION   WP_010531005
VERSION     WP_010531005.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..202
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22627
     Region          5..198
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 matfelpelp yaydalepti dketmnihht khhntyvtkl ntalegkadl qnksledlvg
       61 nldavpedir tavrnngggh anhslfwkvm spngggepsg eladkinskf gsfdkfkeef
      121 eaaakgrfgs gwawlvvnng eleitdtpnq dtplmegktp ilgldvweha yylkyqnkrp
      181 eyvaafwnvv nwdqveknyn ea
//
LOCUS       WP_010531550             271 aa            linear   BCT 01-JAN-2025
DEFINITION  (Fe-S)-binding protein, partial [Lentibacillus jeotgali].
ACCESSION   WP_010531550
VERSION     WP_010531550.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         <1..271
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
     Region          <6..262
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 wreqnedayi ptvkelkked kdfeylfwvs smgsfdnrsq kialafaklm nqagisfail
       61 gnkeqnsgdt arrigneflf qeiaeknike fekhdvkkiv tidphaynif kneypdfgfe
      121 aevyhhtqml ydlvmngklk pqreinqklt yhdscylgry ngvydpprei lksipgldlv
      181 emdrsrengm ccgaggglmw tedttgnrin varteqamet estmissacp fcltmlsdgt
      241 kakeveedis tmdvaeilal svlvddeqkt a
//
LOCUS       WP_010531610             287 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Lentibacillus
            jeotgali].
ACCESSION   WP_010531610
VERSION     WP_010531610.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..287
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32803
     Region          3..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnakkiklie agmklfaekg yhmtsveaia dgagvskgaf ylhfeskkdf imtaihyyhe
       61 eiagriehvk senlpprdsf akqidvvtty iyeykdflmm hfyqnisige ntdafikemn
      121 aqnfhwlrqn vitiygdqve pydpdiiiql eglinvyfkw iiidgisikr nqlgayivrr
      181 mddivsglle rneaplvtaa dipdvyreeg svvevlntmk akietldlag ekadelrevl
      241 kiiqseagke qpqkvviqgl lvhfqrmpef ateckdiarl lhmdlld
//
LOCUS       WP_010531628             258 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Lentibacillus jeotgali].
ACCESSION   WP_010531628
VERSION     WP_010531628.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..258
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29804
     Region          3..258
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mktylqeilr rkdllfylvk sglkaehrns ylgyfwwlld pllnvmvyyf lvviilqrgg
       61 enypvflvig lvvwrwissa vnssaksilr yssiinqvyl pksifplsft isqmfnflfg
      121 liviamflai ygimpdwhiv ylpvlvvitm iflmavgfil ayvtvfvrdi dniltyvtrl
      181 ffyaspiiwr ggrlppeysi fvdlnpvaii vtayrdilmr qitpdfmslg iitaisivav
      241 vitlyhyskn ehkiikal
//
LOCUS       WP_010531654             437 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Lentibacillus jeotgali].
ACCESSION   WP_010531654
VERSION     WP_010531654.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..437
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=48387
     Region          13..423
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mslferlttn eekiaviglg yvglplavel akkfdvvgfd inkakldkyl tgidvtqevg
       61 dealqnttmt ftsdeadlrd ckfhivsvpt pintdktpnl npviaasetv grnltkgsiv
      121 vyestvypgt teevcvpile eqsgltfgdd fkvgysperi npgdkvnklt sitkivsgsd
      181 ddalkeisgv ygaiieagvh eaesikvaea akviensqrd iniafmnels ivfnkmnint
      241 navleaagtk wnflkftpgl vgghcigvdp yyftykaeql gyhsqiilsg rkinddmgry
      301 igsniikkmi nakqeisgar vgilgitfke dipdvrnskv idiieelkdy gvevvvhdpv
      361 adkdavydef gielvekeql ndldcvvfav shnefkeryd ldmmdtlyrt dnkvlvdvks
      421 iydrkeceak gyhywsl
//
LOCUS       WP_010531543             443 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Lentibacillus jeotgali].
ACCESSION   WP_010531543
VERSION     WP_010531543.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..443
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52623
     Region          11..412
                     /region_name="YdhJ"
                     /note="HD superfamily phosphohydrolase [General function
                     prediction only]; COG1078"
                     /db_xref="CDD:440696"
ORIGIN      
        1 mpykdeqlhe ekvfkdpvhr yvhvqdrviw dliaapefqr lrrikqlgts yltfhgaehs
       61 rfnhslgvye ivrriignfe drddwndder llclcaallh dlghgpfshs fekvfkldhe
      121 hftqqiilgd trihtilelv epgfsqkvad vidktyedkl vvslissqid adrmdylqrd
      181 ayftgvsygh fdmerilrvm rpiedqvvik ssgmhavedy imsryqmywq vyfhpvtrsa
      241 evilskilhr akylfennyt fklkpfhfvs ffnenvglad ylkldesivf yyfqlwqeed
      301 deilrdlcer fmnrrlfkyi efnpnqqmne wmelyklfqk aginpdyyle vdsssdlpyd
      361 fyrpgeeder lpinlltqdg slkelsrnsd ivesisgkkr tdhklyfpad ilrglsnddp
      421 vkkrimelld feqhlegege nad
//
LOCUS       WP_010531337             183 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Lentibacillus
            jeotgali].
ACCESSION   WP_010531337
VERSION     WP_010531337.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..183
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21363
     Region          6..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          84..179
                     /region_name="TetR_C_8"
                     /note="Transcriptional regulator C-terminal region;
                     pfam14278"
                     /db_xref="CDD:464123"
ORIGIN      
        1 mnekldrrkk ytrmvlkdsl itllktkqis aitvkeicge adinrstfys hyhdqfdlle
       61 qieeeliadl ntyldqynfe qeaealkmte klleyviskr dicqtllsgs gdqsferrvm
      121 dvtrtfliks winnnevdpd iseyagtfvi sgsiyvikhw landmdkspk qiaelinsfr
      181 fre
//
LOCUS       WP_010531681             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Lentibacillus
            jeotgali].
ACCESSION   WP_010531681
VERSION     WP_010531681.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..279
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30765
     Region          15..265
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 maknqlngik psitmeqhkh sftksekkiy hyiqsnsqqv lyhsltelse asgvaeatvl
       61 rffrklgfkg fqdfkflfaq evtvnddddh detyadkikd nmlqaignsh eiidydelqk
      121 cvdaidassd vvlfgvgssa iaaldmqnrl mrigkhvsav tdphfqfmra ssmdkdtvvi
      181 avsltgstkd ivdsveiakq qnatvialtn yikspltqya dhvllssake spldsgslva
      241 kvsqlflidl ictgltikny enaekvkmgi skntagkly
//
LOCUS       WP_010531711             183 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Lentibacillus jeotgali].
ACCESSION   WP_010531711
VERSION     WP_010531711.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..183
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20293
     Region          1..161
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mklvgisgtl agdktskavy dvleaaklmd tsvktelidl rdyelsfadg splayfeddt
       61 wpvadkimsa dclvfgtpiy qasiagvlkn lldhfpeyaf knkvtgivat glsekhflvt
      121 eyqlkpvlsy fkglvptenv fvqndcfdle sgeiidklia krlrnlaeei lflqgsiner
      181 mer
//
LOCUS       WP_010531772             275 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Lentibacillus jeotgali].
ACCESSION   WP_010531772
VERSION     WP_010531772.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..275
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31074
     Region          4..260
                     /region_name="HAD_YbiV-Like"
                     /note="Escherichia coli YbiV sugar
                     phosphatase/phosphotransferase and related proteins;
                     belongs to the haloacid dehalogenase-like superfamily;
                     cd07518"
                     /db_xref="CDD:319820"
     Site            order(9..13,44..46,67,148,150,184,192,214..216,218..219)
                     /site_type="active"
                     /db_xref="CDD:319820"
ORIGIN      
        1 mtvkliavdm dgtflniqkk ydyerflkqy lklkeqgvqf vvasgnqyyq lksffgdiqd
       61 eisyisenga lvvnqgqevs saeipkkdvn limdvlvmyn klsivlcgke sayvlesvsd
      121 dffetmnkyy irlkrvqsfe liddqilkfa lfcpeeetnp lrdllhskig kiitpvssgh
      181 gsidlivpgf hkasgiqflq qkwdikddet mafgdggndi emlkhvkygf amenasdevk
      241 nianyiapsn eesgvleiid qyflnqgpfg snlnh
//
LOCUS       WP_010531805             365 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF917 domain-containing protein [Lentibacillus jeotgali].
ACCESSION   WP_010531805
VERSION     WP_010531805.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..365
                     /product="DUF917 domain-containing protein"
                     /calculated_mol_wt=39197
     Region          1..357
                     /region_name="COG3535"
                     /note="Uncharacterized conserved protein, DUF917 family
                     [Function unknown]"
                     /db_xref="CDD:442756"
ORIGIN      
        1 mkligkeeie niaigaallg tggggdpfvg kmmalqaiee qgpvklldit eiededvivp
       61 sammgaptvl vekipsgdea iqafhslekv lnkkikatmp ieaggvnsll pialaastgl
      121 pivdgdgmgr afpelqmvtf ylngvsttpm vladekgnst vlntvngewa ekiarsatmv
      181 mggsimnaiy pmtgrqvkds siyrtltlee kigqtikeaq lnkknpieev lqllggmtlf
      241 sgkvtdierk tdggfvhgta tveglnqykg dngylefqne nlliktdhdv lcmtpdlicv
      301 ldtetalpit teglrygara tvigipadek wrtekgieva gpryfgydyd ftpvetlner
      361 qggkq
//
LOCUS       WP_010531827             186 aa            linear   BCT 01-JAN-2025
DEFINITION  Uma2 family endonuclease [Lentibacillus jeotgali].
ACCESSION   WP_010531827
VERSION     WP_010531827.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..186
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21192
     Region          10..185
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mgllheryst yeefeklree tdemleyidg liymspspsi khqeissylh gelynalkgk
       61 dcsvfsaptd vlfdtthdeg kkkvvpdlfv acnpdnftes eyvgapefii eilspssrsh
      121 dmvtklnlym nngvkeywiv dpiknhimiy vkdhnnevqf dliniggvat srtitsfain
      181 lnilfk
//
LOCUS       WP_010531836             264 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Lentibacillus
            jeotgali].
ACCESSION   WP_010531836
VERSION     WP_010531836.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..264
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28922
     Region          3..254
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mkmfvserrn kimehlyekk rltvkglale igvseatlrt dlnkmeeegm lirthggail
       61 ndgtesdtsf sarekknkqe kiqiakegfk fieekqcill dasstalela rylknqairl
      121 tvvtsglnta lelkenpdlt viliggvvtn rsssiegtlg lnildyvnvd imftsgngfs
      181 vengltdfnl yevslkkqlv kkagkiiamv daskidksss avfaapeeis tlitdksvsq
      241 efseglkqkn ieliasklps easl
//
LOCUS       WP_010531921             370 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Lentibacillus jeotgali].
ACCESSION   WP_010531921
VERSION     WP_010531921.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..370
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40208
     Region          3..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrtdllivgg gpaglnaayk aasyglktii vdkwfslggq lrqqtqsydh lpqhfaklrg
       61 ykladflidr lkpldvtile khtligaysd gsvgvtnekd ilpidaknvl ittgameepd
      121 ifpgwtlpgv mtagaaqili nrervlpgkq alilgsnefa levaaqlhdc giaikgiven
      181 rsellcqnek liarisnaei pivlngvies aigkgkveea yvnhngnnal ydvdlicvak
      241 gitpilepfe vmncdliyre rlggwlpeyy gnfettnpsi yvagnaagit nmggilltge
      301 iaaisavesl naastvqike ekeylwnely rieynsvlea rldvinelhn ekdaqlpplv
      361 dslngrling
//
LOCUS       WP_010531948             488 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Lentibacillus jeotgali].
ACCESSION   WP_010531948
VERSION     WP_010531948.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..488
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53533
     Region          11..487
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(68,70,74,77,81,114,117..118,127..134,139,142,145,
                     238,242,245,248,250,423,425..426,428..429,432,435..436,
                     438,440..443,452,456,458,472,479..484,486..487)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(154..157,165,180,183,213,230..233,236,254..256,288,
                     388,390,416)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(157,254,285,288)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mtqpqtkseq lknyiggkwi eaksdktesv inpatgevia evpissnedv dhavevahea
       61 fqdwkelavp krarilfkyq qllvdhwdel aelitiengk nlkeakgevq rgienvefaa
      121 gapnlmmgdq lssiasgles gvyrypigvv ggitpfnfpm mvpcwmfpma iatgntfimk
      181 psertpllan rlaelleeag lpegvfnivh gahdvvngll dhdkvaaisf vgsqpvaehv
      241 ykrgtdnlkr vqalsgaknh tivlndanmd nastqilnaa fgsagercma asvvaveesv
      301 adefidqlik kaneinigng ldedvflgpv ireqhkertl gyietgeneg aklirdgred
      361 gnaqekgyfv gptifdnvtt emkiwqeeif apvlsivrvk dldeaidvtn qspfangscl
      421 ftrdggsvrq frenidagml ginigvpapm affpfsgwkd sfygdlhang kdsvefytrk
      481 kvmttrwv
//
LOCUS       WP_010531955             120 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Lentibacillus jeotgali].
ACCESSION   WP_010531955
VERSION     WP_010531955.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..120
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13240
     Region          <1..107
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mlaydeggav eevinkglea htensitnpd elrsrlaavr edgyaistee fregiksvaa
       61 tirdhtgkvi saitvvgplq rmtnnktphi kkkvmaagke asermgyder yfkqlgrlhr
//
LOCUS       WP_010531974             170 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter small permease [Lentibacillus jeotgali].
ACCESSION   WP_010531974
VERSION     WP_010531974.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..170
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19106
     Region          1..162
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mkilrwldeh leeyilials cftvaviflq vfmrfilsds lswseeiary afiwmiyigv
       61 sygvkkqkhl gvdafamlfe ktgkivigii anicflifav vitvygveiv tkitresaal
      121 qlpmgwvyaa pavgmfltvi rlvqnlikqf qaigntkans ddyqeqggii
//
LOCUS       WP_010531976             528 aa            linear   BCT 01-JAN-2025
DEFINITION  amidohydrolase [Lentibacillus jeotgali].
ACCESSION   WP_010531976
VERSION     WP_010531976.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..528
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58951
     Region          4..527
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mrklyingnf ytfdkmrpit qavvvengrf idmgstddml lrwenhgset inlygkavtp
       61 glidshmhls itaehflnld ltdvtskyem lnkiqsyakt lqqgewllgr gwdenlftdg
      121 giptideldn vspanplyip rvcshaflvn skaleashyh psmsvpeggt ivldeqtkkp
      181 sglllesasq litehipeks ydqlksalrk tmqfailkgl tsvhtndpqf lggfnqtyql
      241 ydellnqeql glrtnllidy dflgglrtng myagfgndtl qigaiklfad galgrrtall
      301 sepysdapgt ygeamynqet lykmvqdarr lsmpvavhti gdqalenvld ildqfpavsy
      361 rdriihvqil redlikrlan psriadiqpr fvpsdfpwvk erlgekraal syawktlqqa
      421 gvicaggsda pvepvdplmg ihaaitrktp genhegwnph eklsmgeafr lftemgaypt
      481 neenkkgtis rgkladmtvy shdpfkmehp dellgtnvem tiiggdvr
//
LOCUS       WP_010532034             349 aa            linear   BCT 01-JAN-2025
DEFINITION  dipeptidase [Lentibacillus jeotgali].
ACCESSION   WP_010532034
VERSION     WP_010532034.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..349
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38322
     Region          1..349
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mtnfpifdgh ndtllrlhms dnppsffees saghidlpra kkggfaggff avytpnedye
       61 aepkehmtdd gydvplppki sheralsftn alaaklfkle feakgqlkvv rstdelkycl
      121 ehdimatifh iegaeaidsn fdalhvlhqa glrslgivws rpnvygegvp frypsspdtg
      181 dgltdngral vrecnklgim idnthlnekg fwdvaaltda plvathsnah alspiarnlt
      241 dkqlsaiaes nglaginfav nmlredgglg tdisldeivr hvayiaekfg vehvalgsdf
      301 dgttvpdslg dvtglpklie rlkvhgfhds elqkitygnw mrvlrdtwk
//
LOCUS       WP_010532042             226 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Lentibacillus jeotgali].
ACCESSION   WP_010532042
VERSION     WP_010532042.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..226
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26243
     Region          3..215
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mqpnnsaimq kplseliadh lkqniwneki qfgerllete laehydvsrs tirealkile
       61 seelvvsqar kgtyvadftd kdagemielr tlleshafmq amprlksedt kklegivgqm
      121 kakadeedwn dlfdldmqfh syvvglcgnt riikiydslq vqirtflmhl dryyssthaf
      181 yhehrqllea lvsndvhtln grvrehieyv etkllgqnnd ikyeev
//
LOCUS       WP_010532045             127 aa            linear   BCT 01-JAN-2025
DEFINITION  RidA family protein [Lentibacillus jeotgali].
ACCESSION   WP_010532045
VERSION     WP_010532045.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..127
                     /product="RidA family protein"
                     /calculated_mol_wt=13479
     Region          1..126
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mkevietlna pkpsgpysqg vkteslifvs gqdgvkpdgd lvgtsiaaqt aasldninni
       61 laekdaglsd lvyvtchlsn lneetvrefn kayesyfedv dvkparitig sqlletdvem
      121 taiasvs
//
LOCUS       WP_010532065             377 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerate kinase [Lentibacillus jeotgali].
ACCESSION   WP_010532065
VERSION     WP_010532065.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..377
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39680
     Region          2..366
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mnivvapdsf kgsltsiqas eimkravtav dnnasvtlkp madggegtle sllaaadgkr
       61 vhirctgslg eniettyaiv esntaiieca niagvvqvpe drrhpdvttt fgigevmlda
      121 ldkgctsfvi glggsatndg glgmlkalgm kaweqngket gqfgrdlqhi tdisfaeidp
      181 rlekatikva cdvdnplcge rgatyvygpq kglsdselkq ydnalnqlgd tvestlnkgf
      241 kniagagaag glgfallaig ghlvsgakll aevinieeai qeaglvltge gqsdeqtlyg
      301 kapgyiasla qrnqvpavlv sgsldgdldm lrehfagcfs ivnkpmslke cmekadklly
      361 eqtkqviyla shflvrk
//
LOCUS       WP_010532140             183 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerol-3-phosphate responsive antiterminator [Lentibacillus
            jeotgali].
ACCESSION   WP_010532140
VERSION     WP_010532140.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..183
                     /product="glycerol-3-phosphate responsive antiterminator"
                     /calculated_mol_wt=20199
     Region          7..179
                     /region_name="GlpP"
                     /note="Glycerol-3-phosphate responsive antiterminator
                     (mRNA-binding) [Transcription]; COG1954"
                     /db_xref="CDD:441557"
ORIGIN      
        1 mevprgivpa irqmkdfeka lessyntivf letrlaqlks lvkyskrsdk qvllhfdliq
       61 glkadeygme flirdinpdg iistrgniik lakkhkllai qrmflldsma vehnlklidr
      121 fkpdciellp glipdvieqi ndetgipvia gglirssaea ssaldagava vstsntelwg
      181 vnk
//
LOCUS       WP_010532141             276 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Lentibacillus jeotgali].
ACCESSION   WP_010532141
VERSION     WP_010532141.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..276
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29078
     Region          1..234
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mpeflaelig tmiliilggg vvggvvlkks kaegtgwvli tigwglgvtm gvyavgqftd
       61 ahinpavtlg faaagefpwa kvpmyisaqv igafigaviv ffnylphwke tedkiakrdv
      121 fsttpairsp fsnlvsemig tfvllfglmf iganeftegl nplivglliv aigmslggtt
      181 gyainpardl gpriahallp ipqkggsdwg yawipvagpi lggiygavfy namflgefsv
      241 lfwvlsgvva iifigaanse lkkgntvade venriv
//
LOCUS       WP_010532158             344 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Lentibacillus jeotgali].
ACCESSION   WP_010532158
VERSION     WP_010532158.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..344
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38178
     Region          32..338
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mheliemqkk lypdllevmq erymllqnie llqpigrral aenthlterr vrgevdllss
       61 qnlinmssig mqltkegklv idqlassmhd imgmdvlekq lketlqldni mivsgnsdeh
      121 dwvkqemgkt cvsylkkhlp snqtvtvtgg ttmaavadmm tpfkdnrdcl fvparggige
      181 keegqantia akmarqaegr yrllyvpdpl setsyktmie epavievlkl iqgssfilhg
      241 igdaitmaqr rktsseiire lreekavsea fgyyfdadgn ivhqvrtigl hmddltensq
      301 tvvtvaggks kaqaiasyfk qgksdllitd eaaaeailgd rtsl
//
LOCUS       WP_010532169             307 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Lentibacillus jeotgali].
ACCESSION   WP_010532169
VERSION     WP_010532169.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..307
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35130
     Region          26..284
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mektywltrp dnvelhlkrw ipaekepeai iqiahgmieh igrynhfvsf mtenniavyg
       61 ndhrghgktg ekqglfgyfa deggfekvsd dmravtkrik qeypdtpifl lghsmgsfla
      121 rhyiqeksnl idgiilsgtg yypriiteig mriaaalppk eqsrlmntlv fstynkrikn
      181 nttnfdwlag dqktiqsyid dpycgfipta gffkdlmngl stihhqnnnr hirsdlpmli
      241 isgtedpvgd ytkgvwktae lynkagldhv mtmladnerh ellnglnrhe iytllldwvv
      301 rltrkns
//
LOCUS       WP_010532197             251 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Lentibacillus jeotgali].
ACCESSION   WP_010532197
VERSION     WP_010532197.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..251
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28004
     Region          1..250
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 meepvvsmks ityayerknv lndinfeipr gvfmgvlgpn gggkttlikl ilgllkpdng
       61 nirlfgqpie nfkdwgkigf vsqkansfnk gfpatvyevv smgltakigy lklftskhkk
      121 kvlqtidqvg msdyayenvg slsggqqqrv fiarslvsdp ellildeptv gvdqenvrkf
      181 ydllhqlnde hnitlllvth dtrtmtehat divcvnktlh fhgnpseykt lsnqdlsqfy
      241 ghpvnivahd h
//
LOCUS       WP_010532209             273 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Lentibacillus jeotgali].
ACCESSION   WP_010532209
VERSION     WP_010532209.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 273)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..273
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29677
     Region          19..268
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkglafvsl llvvllaacg gsgsgdntei kvgasstpha qileeakpil eekgitltie
       61 eyqdyvlpne dlsngeidan yfqhipylkg qiedigydft hlggihiepm giyskdfnsi
      121 devaegtevl msrsvadhgr vlglleregl iklaedvetv nattddiven pknltfsydy
      181 daatlpnlye teentlvain tnyaiganln psedalileg nespyvnvva vkkenkdnet
      241 lntlvdvlhs eeiqsfikee fngavvpvdg kse
//
LOCUS       WP_010532254             319 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Lentibacillus jeotgali].
ACCESSION   WP_010532254
VERSION     WP_010532254.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..319
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36639
     Region          <188..313
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mlnkaiflls lfffavvlnp vhaeeeeqdl hekrmvlykk teavtqipwy yiaaidqyer
       61 nsseedkddq lvsisipdel wygignssmi kneniiqffq gkgkdgsgdn kadpenpedv
      121 lytmasille ygpshdevki alwnyyqrdl tvqtimntak vfkkhnrikl tdrefpvdts
      181 ynysynnnwg drrgfggvri hegsdifady gtpvksttyg vvemkgwnly ggwrlgirdi
      241 nnvyhyyahm sgynddievg qvvepgdllg kvgstgygpp gtsgkfpphl hyglyqddgy
      301 sewsfdpypy lrkwermse
//
LOCUS       WP_010532146             553 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Lentibacillus
            jeotgali].
ACCESSION   WP_010532146
VERSION     WP_010532146.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..553
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61750
     Region          37..548
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 msvfsshkrd aifqqieqkq ldvlvigggi tgagisldaa trgmdtavve mqdfaagtss
       61 rstklvhggl rylkqfevkv vaevgrerev vyengphvtt pewmmlpfyk ggtfgpfttn
      121 iglrvydlla gvkkserrkm lnaeetleke plvkqdnlkg sgyyveyktd darltievmk
      181 kaiekgvnai nyakvvdlly dagkvagavv edqitgrkhh vfakkivnag gpwvddlrem
      241 dgskqgktlh ltkgvhlvfp krrfplqqai yfdapdgrmi faiprnkkty vgttdtsyeg
      301 diahphmted drdylldain yifpslnmtk ddvdssyagl rpliaeeged dpdeisrkde
      361 ifvsdsglis maggkltgyr kmaedavdev vkqlkeeygi lysesetehl pisggevggs
      421 kgfqqfkerk iaeaadlgia eetaiflvqk yganvnqife lfqgekaqae kagiepivfa
      481 elryaldnem aykpvdffvr rtgalffdid fvtaykdnvi nymaeilhws deqkrlytee
      541 ldqlldeavt pvk
//
LOCUS       WP_010532288             406 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Lentibacillus jeotgali].
ACCESSION   WP_010532288
VERSION     WP_010532288.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..406
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=45199
     Region          3..386
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mekpdivilg agyggimtav klqkmlnmnk stitlvnkyd yhyqttwlhe naagtlhhdr
       61 tripikdvvn takvnfvtdi vvsikpdkrk vklqngelyy dilviglgfe tatfgipglk
      121 dnafmienin sarlirdhle ynfamyqyed gknqgrlniv vggggftgve flgelanrip
      181 elckeydvnk sivriiniev estvlpgfdp qlseyamssl esrgvefitg atlkeckhdr
      241 iifekdgkes tiptytmvwa agvranaile esgfehhqgk ievrpdmrap dyddvfaigd
      301 calimdrktn tpypptaqia vqqaetvahn ikalvkgtdd ldefqpdllg tvaslgnsda
      361 igdvfnnrkl fglkavilkk iidnryllkl gglgllmrkg kfnify
//
LOCUS       WP_010532291             157 aa            linear   BCT 01-JAN-2025
DEFINITION  divergent PAP2 family protein [Lentibacillus jeotgali].
ACCESSION   WP_010532291
VERSION     WP_010532291.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..157
                     /product="divergent PAP2 family protein"
                     /calculated_mol_wt=17222
     Region          1..157
                     /region_name="YuiD"
                     /note="Acid phosphatase family membrane protein YuiD
                     [General function prediction only]; COG1963"
                     /db_xref="CDD:441566"
ORIGIN      
        1 mdffanfplw aalsaivfaq vikipirlia trefkpglaf stggmpsshs aavaalttav
       61 givegadsvm faisavfsvi imfdasgvrr qageqaivin qlvedfqyfm egakdwnrke
      121 lyqkrkelke llghqpievf fgglsgiaia fflyqyy
//
LOCUS       WP_010532315             276 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lentibacillus jeotgali].
ACCESSION   WP_010532315
VERSION     WP_010532315.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..276
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30311
     Region          4..256
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mqtlsakdlt lgygddiiid dlnitipkge itvligsngc gkstllrsla rllkpkgggv
       61 vldgeniakm gtkdvakels ilpqgpatpd glsvmelvkq grhpyrgflk qwskedenav
      121 hnaldatnml eykdrpvdsl sggqrqrawi amtlaqetdt illdepttyl dmthqidvld
      181 llfdlnekdg rtvvmvlhdl nlacryahhi vaikdkdifa qgrpeeivtc klvhevfqmk
      241 cdvtfdpmfg tpmciphgrg rcifadkagl qqtaan
//
LOCUS       WP_010532347             104 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Lentibacillus jeotgali].
ACCESSION   WP_010532347
VERSION     WP_010532347.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..104
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11920
     Region          11..101
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(28,31)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkrlesekql ndviknenvv avfsadwcpd crviepelpe iekaysnftf vevdrdqfid
       61 vcqeydvfgi psfiafknge eagrfvskdr ktkdeitafm ddls
//
LOCUS       WP_010532359            1034 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Lentibacillus
            jeotgali].
ACCESSION   WP_010532359
VERSION     WP_010532359.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..1034
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=112721
     Region          38..756
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
     Region          <862..>940
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
ORIGIN      
        1 mdfkqlsqky rdkiksfwrs fnshhyvkka ksvwgtgkiq kssrigydvv wsiilffivi
       61 aviggffagg vgagyfaslv kdepvrayen mqediynyeq tsslyfagdn yigdirsdiy
      121 reevsldnvs dalinaviat edqyfsehkg ivpkaivral vqqvtnsstq sggstltqql
      181 vknqiltnev syerkakeil iamrlerffe kdeilesyln ivsygrdasg gniagiqtaa
      241 qgifgidase vnlpqaayla glpqspsyyt pfknsgglkd kealqpginr mqsvlermye
      301 sdyiskeqye kamnydittd ftkesqspve kypyltyete krasniimkh maeqdgysme
      361 elnnndalke eysiladral rkngyqihtt idkethdkfr kitqnyeyyg pdwtgyvedp
      421 etgeqvkdtq kvqtggilie nssgriisfv ggrdynpenq fnyatqaers ngstmkpilt
      481 yapafekgvi qpgtpiadvp ktfaggytpg nygggyhglv sarkalynsy niptvevysr
      541 fneqdpvsef lepmgitsig ekeyanlsls igatstgvtv eenvnafstl gnngkfadgy
      601 miekitdqdg nviyehkpdp vkvfspetsf ltidimrdvl dkgtgtylns qlkysgvdwa
      661 gktgtsqnyk dawfvgvnpn vsmgvwlgyk egksiqcpsc slsysqrtqk lwaelvnaas
      721 dinpdlvapd ksferpdgiv srsycatsgk lpsdlceeag lvktdlfnsk yvpteednsl
      781 irggsyvmvd gnavaagakt pnefvegngl tfnpeflkrk gydqlgdlsi lfprtnrdaw
      841 ekiglpqsgv sssgiendgn spdapgsvsa sdktlswsss dssdvvgyri fraskpngsf
      901 sqvgstagts ftassnnavy hvkavdyfgq vssasntatv gspggsddss esngnnidsd
      961 ndsgnnnngd gsngenngeg ssddgtggdd ngsgsddnng dsdksesgds sgesgsdsds
     1021 dteesnnsnn ennn
//
LOCUS       WP_010532422             167 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Lentibacillus jeotgali].
ACCESSION   WP_010532422
VERSION     WP_010532422.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..167
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18682
     Region          2..139
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          72..>139
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mnisvikpqt khaaaiaeic atgwkqtveg klseeyqkrn vefwynherv lndinggayt
       61 haaliesdia gvigggmtss dtseifllyv detfryqgig krllesltre qinqgatgqw
      121 vsvqeenqlg ipfyeargfm yqekrltpte tgevqvsiry arslldt
//
LOCUS       WP_010532472             166 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Lentibacillus jeotgali].
ACCESSION   WP_010532472
VERSION     WP_010532472.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..166
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=19268
     Region          53..154
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mnyittpled hvanmyykig isepdssiee iarrlgivll yrkkpsfsme gvitlnpfts
       61 kevrkitfah elyhtlyhvg tqidmphlfr qlqewqatnf ayhfcvptfm lqklklpayr
      121 seaitfiaet fcvtnqfake rltiyekqii gtlfherlss skelpg
//
LOCUS       WP_010532456             321 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Lentibacillus jeotgali].
ACCESSION   WP_010532456
VERSION     WP_010532456.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..321
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33766
     Region          2..319
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mkllvigear dgelrnvtfe avaaakkids daeivgvlcg sddlnesgqe viyhgadrvv
       61 tvthdnlesy tsegysqavm aviedespdg ivmghtaigk dltpklaakl gtglisdatd
      121 iendgdkavf trpiysgkaf ekkvmtsglt fatirpnnip alerdasrsg dvtskevdvk
      181 dintvikdvi rkasegvdls eanvivaggr gvksaegfep lyeladilgg avgasrgacd
      241 aeycdyslqi gqtgkvvtpd lyiavgisga iqhlagmsns kvivainkdp eanifnvady
      301 givgdifevi pklteelkqt v
//
LOCUS       WP_010532565             110 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Brachybacterium squillarum].
ACCESSION   WP_010532565
VERSION     WP_010532565.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..110
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11762
     Region          24..97
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mepspapaas rhgtvrlhgv lrcadaeear tvtrhlpqhl tltraepgcl slrvepsaep
       61 lvwevaeefa dagafrahqq rvaasawgra tadiareytv dglpeegeeg
//
LOCUS       WP_010532587             471 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Brachybacterium squillarum].
ACCESSION   WP_010532587
VERSION     WP_010532587.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..471
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50212
     Region          37..466
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mdprnpstap ihpalhptrs tvsrfrqviq hfatptparl altaftglia lftallslpa
       61 asadgertal vdalftavsa vcvtglvsvd tgehwsdlgl viiavaiklg glgmltvfsl
      121 lslsvmrkmn laqklltate trteklaevg nvvrtvvits sifevatfil ltpymivtdh
      181 ppgrsvflga fyaisafnna gfipeaegva qyagdpffli pvgiavlvgs lgfpvilvmv
      241 kkwkhpvrws vhvkltlvtt gmlfglawvg llamewanpd tlgehgigrk lltswftaim
      301 prsggfstld iglmtgesrl lmdalmfigg gsgstaggir vttfallmls iwaevrgnpd
      361 vevfgrrips etirqaigvl vmavsvvmig tflmlrmtaf tldqslfevl safgtvglst
      421 gitgtlptda klviialmyi grlgpmtvaa slalrsrtrm iryplerpiv g
//
LOCUS       WP_010532628             457 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Brachybacterium squillarum].
ACCESSION   WP_010532628
VERSION     WP_010532628.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..457
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49112
     Region          3..>157
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mpktlniavi gvgtqaqavh lpvlrrrwdr favtalvdhs errrresaev wgvpeqqrya
       61 svahlvaavr akeialdgvl lstdglhved lltlirrgip vlvepplgfs aaevariadl
      121 ermtgrrlvm maypqqydes vqrvpdlvar kdvrmlehev lmpasqplfg aahvttasyd
      181 lpsekraerr salqsavkeg sgpsatqrdr dlyvkglltg vahqlavlea tygpiselea
      241 vrhwptgvvp gsielwgqle gggrvrlvwh ylpfapeyse hlrvlsarkr lhvelfapsh
      301 gdrrtavslr ekksgvvqet tsaaghgaae smwegfhafv vkgrepisga aselaqvell
      361 rrvlaavvea dgrdidapve aeedaaaeqs dgttvepehg atapagapat tgapatadtp
      421 tptntadpae dsaptgtedp aapapepgvl dlprers
//
LOCUS       WP_010532187             327 aa            linear   BCT 01-JAN-2025
DEFINITION  sodium:calcium antiporter [Lentibacillus jeotgali].
ACCESSION   WP_010532187
VERSION     WP_010532187.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..327
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=34475
     Region          17..293
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mvfvwfflaa avtvytamkl seyadvisek tamggmmvgt illagatslp evttsfsavl
       61 idnidiavgn mlgsnvfnvf iiaafdlyyr khklfdlass nhkytaflgl llmilvsval
      121 vlridytllg igadsllila ayivglivis ktpspsvsee kakettdekk svsvkhaiig
      181 fiiaaifilg agtllsvtgd qiavvtglgs sfigsfliaa ttslpeavsv fsalrlknvn
      241 lavgailgsn sfnmiilais dvvyqggsil adasgshlvs afggsllivm viwaflrqrs
      301 tslaayslps vitvigyfvv qylifnr
//
LOCUS       WP_010532649             296 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Brachybacterium squillarum].
ACCESSION   WP_010532649
VERSION     WP_010532649.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..296
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31008
     Region          3..215
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mariavlggt gflgrhaisr lltdghqvra ivrsprgadl padveivpgd vtvpgtlpaa
       61 lagteavlla lnggstpara vrveeqglah vaaaagaagv grmllltgmf sqpafashpw
      121 eqakvrgasl lldgpvpatv frvgfvnetl arfvrggrpv ligrqphpir piaaddimaa
      181 asrafdlpst adrtydvagi qaitlreata ayataisgre vsprevrvmp lslmravnrl
      241 alkgemtrpl gilssmdrhg dvtdtsawfr digapptsfp dwiarqrpgt tertss
//
LOCUS       WP_010532667             321 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Brachybacterium
            squillarum].
ACCESSION   WP_010532667
VERSION     WP_010532667.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..321
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34369
     Region          41..96
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(42,67)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(49..50,61,64,68..69)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          118..283
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mstsstapdp rqgiraeisd flrtrrdalt pqaagiiags rrrvpglrre elamlagmsv
       61 dyyarmergd lagvspevld alaralqlde aetdhlhdla eaaqprprrp rhapsstvrp
      121 alqqfldaaa apmwardrrm dvlatnalgr alyaplledv aargntarfl flspasrvff
      181 pdwersadgv vatlrsyagr tprdtgltdl igeliarsee fsarwsahqv rhhrtgtkri
      241 rhpqvgelel syegmelsae egwtlfgysa epgspslerl allaslavsp sgssgssaps
      301 gpsgpaagps sggaasgrgr r
//
LOCUS       WP_010532717             836 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Brachybacterium squillarum].
ACCESSION   WP_010532717
VERSION     WP_010532717.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 836)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..836
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..836
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=88558
     Region          4..829
                     /region_name="YprA"
                     /note="ATP-dependent helicase YprA, contains C-terminal
                     metal-binding DUF1998 domain [Replication, recombination
                     and repair]; COG1205"
                     /db_xref="CDD:440818"
ORIGIN      
        1 mqegraeell ralgepltrr gclthverrp aregrrgsfp awtdprlreh laargitapw
       61 thqqqaaela qagqdvvlat atasgkslay llpllsavgt reldptarra talylsptka
      121 laadqltnit amadgagird arvavydgdt pseqrrwirr hgsvvltnpd mlhfgilpgh
      181 eqwasffral ryvvidechs yrgvfgshva lvmrrlrria ahyraeptfi lasattahpe
      241 lsasrligrd vqavtedgsp ragltvglwe pgtrgavvdg rpeqaghdsr taadgtestg
      301 diagsggtad iggtgstgga agsgreemlr rsataeagal ladlvaedvq tlvfarsrrg
      361 aelvsgtarr mlsqraeeeh sgaladlagr vaayrggyla aerrrleddl rsgelralas
      421 tnalelgidi agldavvvag wpgtraslwq qmgragrrga ggagggalal fvaredpldt
      481 yvvhhpetvl gaeveaavfd panpyvmtph lcaaaselai kdgeegifgp tarellgtla
      541 argvlrarpg gwywtlsqsa hdltdlrgsg gepvrivesg sgtllgtvda asadtqvhdg
      601 avylhqgrsy vvdhldteqa vamvhredpl htthpqstss irirqtdsev pwaggvrlcf
      661 gtvdvtdqvt gyqvrdvftq avlaqhsldl pprtlttkav wwvvprertd aaeipgeelp
      721 galhaaehaa ismlpllatc drwdiggvst aqhedtgept ifvydgapgg agfaergcqd
      781 aaawlratad midecpcavg cpacvvspkc gngneplskv warvllgelt pepata
//
LOCUS       WP_010532732             225 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Brachybacterium
            squillarum].
ACCESSION   WP_010532732
VERSION     WP_010532732.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..225
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24576
     Region          12..224
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mdenivrssp lfaaldedgk qavlasmkqe dyhrsaivfr egdpgdrlfi igqgkvkvgh
       61 asgdgrenll avlgpgetlg elslfdpapr natatvvaet tlysltqqdl yrvlaqrpev
      121 arhllaslar rlrktnesla dlvfadvpgr vaknvldlaq rfgrqtddgv mvahgltqee
      181 laqlvgasre tvnkaladfa srgwirlear avlivdverl rrrar
//
LOCUS       WP_010532764             278 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Brachybacterium squillarum].
ACCESSION   WP_010532764
VERSION     WP_010532764.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 278)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..278
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31151
     Region          19..278
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 msgpvrnrag ssrgtlqvvr eliatrsilw vlvkrdlklr yagsmlgwvw tvlepllmag
       61 iywfvftqif trsvgqdpyi ifllagllpw fwftngltqg teallsqrrl lastslprqi
      121 wvlrsvgakg ceflfsvpvf liflifyrpt fdgelwlipv gialelvllt glglllspim
      181 vlvrdlkpii rlvtramfya spviysyhdi vaanlpdvlv tlyslnpvtg imecyragff
      241 adqtqyaail iaagiavvtl vggwfsfmrl eprvlkei
//
LOCUS       WP_010532824             238 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brachybacterium squillarum].
ACCESSION   WP_010532824
VERSION     WP_010532824.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..238
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25535
     Region          1..228
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mielqnvtlt fpdgdnrita vddvtlrgdn gtvtgitgps gsgkssilav aatlirpdsg
       61 gvlignesdl idaaqlskre atelrrerig ivfqqsnllp altgreqlqv mgrlgggtnr
      121 nrrgridsrv eelldavglt ehadkrphql sggqrqrvai arglvhepev llvdeptsal
      181 dqergaeimq liarltherd tatvlvthdl vhrdaldnlv tvidgrittp vsghalth
//
LOCUS       WP_010532826             398 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Brachybacterium squillarum].
ACCESSION   WP_010532826
VERSION     WP_010532826.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..398
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41800
     Region          135..392
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mphstlapvf tglrfglhal liglagfavv rafvvfspva pwtlvvgvaf vavylagawa
       61 arsgraagss grrfavvwva altllwavlt wlspegaylv fplfflhlhv lpgsggvaai
      121 vittafsila lglhlgfsvg gvigplvgag valliglayr alrreaeere rlltelihtr
      181 qqlaetereq galaerarla reihdtvaqg lssiqmllra aerdtpepga aylelareta
      241 adslsetrqm ireltparld dglaaalrrl gqeqtdrasl pvevaaedld lpmgtqtall
      301 riaqgavsna irhadatria velaceddav slvvcdngqg fdvssavads headsfglqa
      361 mrerveqldg alaitsapgd gtsvtarlpl ptgsgafs
//
LOCUS       WP_010532889             191 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Brachybacterium
            squillarum].
ACCESSION   WP_010532889
VERSION     WP_010532889.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..191
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20753
     Region          3..187
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mtreivytgf vtadgvldsp ggtveghpyg gwvmdtpfdp eafalkgdei aetgalllgr
       61 nsyqafapiw rdsedhaayr dlpkfvvstt ldeadltagl getrilrsla dvaalkdteg
      121 raifihgsae larelaaagl idryhllqfp vlrgagkhlf preqpisgql rlreseaypn
      181 gvvkliyevv r
//
LOCUS       WP_010532886             371 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Brachybacterium squillarum].
ACCESSION   WP_010532886
VERSION     WP_010532886.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 371)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..371
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39438
     Region          15..188
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 matmngalrl rprgtwlvas lelrqrlrsr gwiialavwt vvllglgflv laptlyfagw
       61 dhlagtarvv lslqiilvlf allvvvpals agsingdrna gtlailqasl lssaeivmgk
      121 llagwltgla flvlalpstl itavlaqtsp wyflrmvami aliaacltal glglssitvr
      181 qlssvvlayv vvfgvtvvlp vafgaaatfv sqerqvtvye sqpppgwtgd dwtsepdqst
      241 wtceplestq tvlrtdlvlp llwanpvvml aetapsvnlr dtatadfgdl dalsgmklll
      301 qyaaapahps hfvscdpgqe gypedlatmp qrpvgwigvm lwllvgggsl alairrlaap
      361 irrlgrgtri a
//
LOCUS       WP_010532897             473 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Brachybacterium
            squillarum].
ACCESSION   WP_010532897
VERSION     WP_010532897.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..473
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=49086
     Region          23..443
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mttsapsspt asrsrnplra iaripfgwqv liglalgvvl glvasamgpg sgedganwlv
       61 taldtigttf vtllkalvpp liflaivtsi anlrqvtnaa rlawktllwf aitsliavsi
      121 gialgaltnp gertgidssa aeasetqggw mdfltglvps nflgitgstg ddgsvslsfn
      181 alqilvisia vgiavlsvge kaepflrftg saleivqkll wwvirlapig tvgllgnava
      241 sygwdaigql gvfvadvyig mllvllvvyp illkvnglgv gsffrgvwpa tslgfvsrss
      301 lgtmpmtqtv termgvprhy asfavplgat tkmdgcaaiy palaaifvan fygvplgvtd
      361 yllivlvsvl gsaatagmtg atvmltltls tlglplegvg lllaidpild mgrtalnvtg
      421 qalvpvivsa reklldrday daarrtsfae iqaeqareae atteeerkvp ata
//
LOCUS       WP_010532936             186 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase [Brachybacterium squillarum].
ACCESSION   WP_010532936
VERSION     WP_010532936.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..186
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19585
     Region          7..185
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(11,28,33,66,120,126,139)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(13,20,50..52,73,121..124)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 msgavpeial iwaqarggvi gadgampwhl pedlrhfsaa tagspvvmgr rtwesfpprf
       61 rplpgrtnvv itrdatvaea gavharslde alrlaaaele prpgdaapsp taapaavwvi
      121 ggggvyreal pradrlvvte idlevagdtt apavpeefvl taadpaegwh taasglryri
      181 ltyrrr
//
LOCUS       WP_010532991             318 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Brachybacterium
            squillarum].
ACCESSION   WP_010532991
VERSION     WP_010532991.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..318
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34214
     Region          13..305
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mlettmdlql lhraasayyl ddlrqaevae rlgvsrptvs klltearrig mvrfevldlp
       61 aedlpaledr lrellgiaqv riapgdqier gcrglgellt qelrvlqlrr gdvlmvssgr
      121 ttyavsgmds lpalpgviva ptvgglqepd rayqtnetag rlasrtgaea ryifapalps
      181 pslweslqad psfreitglw eraramiigi gapyrgresl tsvvprqepa ldaaagdicl
      241 hfyddrgrpi eypgsdrllr pslellhrip hilalaagte kvpsilagan aglftslitd
      301 aptaravlae geaaaava
//
LOCUS       WP_010533006             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Brachybacterium squillarum].
ACCESSION   WP_010533006
VERSION     WP_010533006.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 228)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 228)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..228
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23661
     Region          1..183
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mswvsanldt iaeqllahia qalpaivlaf vlalpiakla nargwlrggl tgtagllyai
       61 pslplfivlp lmlgtsirsp vnivvaltiy glalmvpsas ealravsret lqaataqgya
      121 pwarfwrvel plagpalvag lrvvvvstvs lvtvggvlgv pslgmlfidg fqrnitaeil
      181 tgivltaala llldalvvlg grlalpwasg raprrrtapr dtgqeaar
//
LOCUS       WP_010533009             278 aa            linear   BCT 01-JAN-2025
DEFINITION  class II glutamine amidotransferase [Brachybacterium squillarum].
ACCESSION   WP_010533009
VERSION     WP_010533009.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Zalkin,H. and Smith,J.L.
  TITLE     Enzymes utilizing glutamine as an amide donor
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 72, 87-144 (1998)
   PUBMED   9559052
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Zalkin,H.
  TITLE     The amidotransferases
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 66, 203-309 (1993)
   PUBMED   8430515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000620
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..278
                     /product="class II glutamine amidotransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006541 - glutamine metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29619
     Region          2..259
                     /region_name="YafJ"
                     /note="Predicted glutamine amidotransferase YafJ [General
                     function prediction only]; COG0121"
                     /db_xref="CDD:439891"
ORIGIN      
        1 mcrllgvvsr ssrslpqavp aelplftals erhkdgwgva wygdapgart plvlratdta
       61 lasnsygeav eaahgevmtv hlrrasvgla lelrnthpfv hgevsfshng qfdlseelre
      121 rilarggrrp egttdselff slvtawaaed aargagdldg lsgvawarav qraaaeltgw
      181 tlelfgrvpe slncllttpd alvafaahdp aqaptdqppe vyelryrved vrvlvsstgy
      241 pqegfatlaq ggaiavargt levtqlaply apeavapr
//
LOCUS       WP_010533050             403 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Brachybacterium squillarum].
ACCESSION   WP_010533050
VERSION     WP_010533050.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..403
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42051
     Region          10..403
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mtgliasvve afgelrvhkg rimlslfgva vsvftltgvl gaggmlssal eqsietfggr
       61 etvlsvtqis ggedatpadr detvlqetdr lgieqrsryl mlsgrfqtsa gvqtssmyav
      121 dpayadmyrl rpeqgrwfad sdahrlapav vishdlweqa grpavgtgti tlydgdsves
      181 aqalvvgvlp asytaatgee nvmftpassa delpgvddaa ltsteyrlwv ppeqadavte
      241 rlqdtladtp vgtfdtysmg ysmedtgfgm lrnavvavav avlllgalgl vnislvtvry
      301 rvreigirrs ygatggrifl gvlmesvvat avagvvgvag avalvrapft qdafrsmglv
      361 dvpafplsav liglgaaiav gilagalpal iatriavida irt
//
LOCUS       WP_010533121             251 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Brachybacterium squillarum].
ACCESSION   WP_010533121
VERSION     WP_010533121.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..251
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27068
     Region          18..248
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 msvsrdvaap leitvdrssa tplylqlaga ieeavrsgvl ppgsrlenel alaqrlglsr
       61 ptvrqgiqel vdkgmlvrkr gvgtqvvqap vhrqvaltsl yddlrtagka prteiveyri
      121 grpgpeavdr lqlgpgeqvl dllrvryadg eplavmrnmv periapsrea laatglyasl
      181 rergiatvla qerigatvad eehaellgee lgaalltmer tafandgsvv evgrhvyras
      241 rysfevtlvd s
//
LOCUS       WP_010533129             397 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Brachybacterium squillarum].
ACCESSION   WP_010533129
VERSION     WP_010533129.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..397
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40920
     Region          5..290
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msaaplsvav igagmagrth anawrqagtv yelglppvrl atiadahlpf aedaaahygy
       61 ekavgdwrev aedpsidvvs ivvgnalhre iaeamadagk hvlcekplag tledaaamaa
      121 lqeahpelvl atgytfrrna giamlaklaa egdlgtpshl dahywadyga dpntpiawry
      181 kgpmgsgalg dvgshmvdsa elvmgpiaev sgaqlvttit erpvmtgavs ggrgvtadad
      241 apreavendd vatftarfas gaagtfscsr vafglpndkt ltvlgtggsa rwelhrggei
      301 qladasspag rgglrqvlvn pefpyyangs smafagvglt qveqftyqah aflqqvagit
      361 egalppcasf adgyrqmril aavaesaarh gaavaid
//
LOCUS       WP_010533131             498 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Brachybacterium squillarum].
ACCESSION   WP_010533131
VERSION     WP_010533131.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..498
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=52565
     Region          7..481
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(61,63,67,70,74,107,110..111,120..127,132,135,138,
                     231,235,238,241,243,417,419..420,422..423,426,429..430,
                     432,434..437,446,450,452,466,473..478,480..481)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(147..150,158,173,176,206,223..226,229,247..249,281,
                     382,384,410)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(150,247,278,281)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mtydithwid greepgtgst qpilnpatga qvgtvqlgda dtvdravqva aaaqkewagv
       61 slskrtqily rmrqlvldav deiaaaitre hgktlpdakg eiargletle fatsitqdlk
      121 ggfsenvssg vdahtmrqpl gvvagitpfn fpamvpfwmh piaiatgnaf ilkpserdps
      181 asniiarlyq eaglpdgvfq vvhggkatvd alctnpgiaa vsfvgstpia qhvhatasaa
      241 gkrvqalgga nnhavvmpda niefaasqia sgafgsager cmavpvavtv gdvherflea
      301 iaaeaeklvv gpgedsatdm ppvitadard rvvrmtdeae qaggriivdg rglvvagfeg
      361 gnfvgptvit dldrthstyt devfgpllvv mhadnfdeal elvnsspfgn gtaiftdsgh
      421 yarryqeevq vgmiginvpi ptpvgyysfg gwkdslfgeh hahgpeavgf ytrqkavttr
      481 wpaqnetves smsfpthd
//
LOCUS       WP_010533151             230 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Brachybacterium squillarum].
ACCESSION   WP_010533151
VERSION     WP_010533151.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..230
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25934
     Region          2..227
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mairrqvlrd eveqlilqrl lenrwepgsr lsidglardl evsptpvrea mvalersglv
       61 eyvalrgyvv apmldaahmi elldarnvve saalgrsftq weglladlei aharhgevld
      121 aieavetvdy plmhehfrad wafhqvffeh aanrylhtmv enlgththrm rqtwtgaglf
      181 dgrqahsehg eilemvrrhh hdgalkales hldgvlsrsl pavateetrg
//
LOCUS       WP_010533158             114 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Brachybacterium squillarum].
ACCESSION   WP_010533158
VERSION     WP_010533158.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..114
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=12114
     Region          3..113
                     /region_name="Usp"
                     /note="Universal stress protein family; pfam00582"
                     /db_xref="CDD:425765"
ORIGIN      
        1 msvlvagtat pagqaayrya ieearrrgeg ivyfqlegeh tpspeldgip etvehpdgrt
       61 hspagdlidr aerddisalv igvrhrtava klflgssaqq iileankpvi cvka
//
LOCUS       WP_010533165             519 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 32 protein [Brachybacterium squillarum].
ACCESSION   WP_010533165
VERSION     WP_010533165.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..519
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57898
     Region          33..516
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mdpftrrhll rttslgglal agasalplaa caedpslrar fhmtpphgwl cdpqrpivrd
       61 gvhhlyylhs einsgdggwd rattedlvhf thhgdaiplr pdfpvwsgcl vvdehddagy
      121 gagtvlaypt qptdgirkyq eqylyvshdg gatftrreep vipnedgrea vtgeevlnae
      181 wfrdpkihwd aateewvcvi grkkyaafyt stdlvhwrlr rnfdylvepd dldlggiecp
      241 dlfeitaddg tshwvlgasm dawgvglpmt yaywtgrwdg eqfladdltp qwldwgwdwy
      301 aavtwpkped pertryaiaw mnnwkyanrd vptdasdgyn gqnsivreih lqresdgrya
      361 llsrpvpqla atasevveip dqvvagwwdl pwsgrayele ldlawdsaan lgvslgrsad
      421 gsrhtnvgvh dgklyvdrgp sdlegfsfge ftqaeapidp aarhvhlrif vdtqsvevfa
      481 nsghtvlsqq vhflpadtgi alhgdggpvt ashitvrvh
//
LOCUS       WP_010533192             653 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Brachybacterium
            squillarum].
ACCESSION   WP_010533192
VERSION     WP_010533192.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Maindola,P., Raina,R., Goyal,P., Atmakuri,K., Ojha,A., Gupta,S.,
            Christie,P.J., Iyer,L.M., Aravind,L. and Arockiasamy,A.
  TITLE     Multiple enzymatic activities of ParB/Srx superfamily mediate
            sexual conflict among conjugative plasmids
  JOURNAL   Nat Commun 5, 5322 (2014)
   PUBMED   25358815
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 653)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19896137
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..653
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=66568
     Region          <128..338
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          <232..>332
                     /region_name="PRK14959"
                     /note="DNA polymerase III subunits gamma and tau;
                     Provisional"
                     /db_xref="CDD:184923"
     Region          379..642
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mtqkrglgrg lgalipgaga apqqapaapa eeapaaapsp aeaaplaeta gaaevgqaaa
       61 aasspseapv peapvsaapa setpsveetp alrtrtqptp epeqgsaaae rpvdmffsge
      121 qagsreerar aergsardla gdmakaaaer rgrgtsvrst akgssastet asagrgastg
      181 kksgatgsgg kkspggaaas sarssssrst gsatakkkts ktsassasak rgatkggask
      241 ggaatrsstt sapgtgavse taaqptsprt aaesspvvdv eevpltpara esspvttvea
      301 qatapagtpe sapaepvesa esspapaeps epmettpvpa saaeaaptta aadeepvvaq
      361 dlspigttpa ggdllpvpga efaeipihei renprnprtl fdedeldela aslrqvgvlq
      421 pvvvrsiavt engesfelvm gerrwraatr aglpsipaii rqtsdddllr dallenlhrs
      481 qlnpleeaaa yqqlledfgc tqdelgerig rsrpqitntl rllrlpplvq rrlasgalsa
      541 gharallsld npalmeelaq rivaeglsvr averlvaagg aaqpaartar rstydphvvd
      601 ltsrlsnrle tqvridvgkr kgritleftn ledlerlven igldpaevlg sed
//
LOCUS       WP_010533218             471 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Brachybacterium squillarum].
ACCESSION   WP_010533218
VERSION     WP_010533218.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..471
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50303
     Region          17..444
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mdligpllsl aaslvlilac ggfvaaefsl itanrndvea aakagdkraq gvlegmrtls
       61 tqlsgaqlgi tvtnlaigfl aepaiaaivg pplqdlglss vaartvsval alvlatgltm
      121 ifgelvpknl aiaqplrtak avvgfqrlfs kilmwpirlf ngnanavvra mgiepqeelg
      181 sarsaeelsa lvkrsadega laaetanlvq rtlafgdrra hdamvprgrm dvldvddsva
      241 dllhlsretg hsrfpvltee neiagvahir hglavpfakr adtrvdtvmg aatfvpdtvp
      301 lddlmdtlrq gglqmavvvd efgdhaglit ledlveeivg evrdehdeee ddtpeadgsw
      361 efdarirpde aserlgvtvp ehedydtlgg lvtmelgrla elgdeivvdt dpepgedpar
      421 lrievleidg lrietihvtv eaapdededg edesarddsa rendtdkeea r
//
LOCUS       WP_010533219             346 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Brachybacterium squillarum].
ACCESSION   WP_010533219
VERSION     WP_010533219.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..346
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36576
     Region          1..>340
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 msdgmgialt lvllalnaff vgaefslisa rrsviepkal egnraakvti rameqvslmm
       61 agaqlgitvc slalgaisep aiahllevpf eaigvpsalq hpiafvials lvtylhvvfg
      121 emvpkniala gpermamilg pilmgivtvl rpvlwtfnai gngvlrllgv epkdevtsaf
      181 tqdevaamvs esreggmled ndealllgal tfdqrsvanl viplaevttl pegvtptqae
      241 taamegfsrf pvqaadgrlt gyihikdvle teedardlpi dperirplpa iradqplrqa
      301 ltsmqtsaah lgaatdadgt vigivtledm leelvgqird dsraaa
//
LOCUS       WP_010533266             356 aa            linear   BCT 01-JAN-2025
DEFINITION  LLM class flavin-dependent oxidoreductase [Brachybacterium
            squillarum].
ACCESSION   WP_010533266
VERSION     WP_010533266.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..356
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37970
     Region          37..341
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mrafgflsfg hyggrpeqgg lsarqmlhda ldisvgadel gvngayfrvh hfatqsaspm
       61 pllsavaart qrievgtgvi dmryenplym aeeaaaldli adgrvalgvs rgspepaerg
      121 weafgytgst dprgadiare kfpqflaair gepmaraaaq pygapvspga glhiepqspg
      181 ldtriwwgag sresaedvgr qglnlmsstl lteatgasfa dlqaeqidry reafrdaght
      241 raprvsvsrs vfpviteqdr rlfglrpgdg adqigiidgh rstfgrtfvg epdqlieelr
      301 adaavqsadt lmltipsqag velnlhiles fathvapalg wrpntegpvq gdpisa
//
LOCUS       WP_010533267             146 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Brachybacterium squillarum].
ACCESSION   WP_010533267
VERSION     WP_010533267.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..146
                     /product="VOC family protein"
                     /calculated_mol_wt=15036
     Region          7..135
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(7..11,27,63..64,67,87..92,94,98,128)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 matpqntpyi sfpgnageaf ayyrdtfgge levmtydefp dlsgfpfapp pgavahgvlt
       61 gglltlaggd siaspgqelp plgsdvysfl igldsveeak aliekvtstg grlampfela
      121 pwgdhygqvt dpfgvlfaiv vagahg
//
LOCUS       WP_010533275             219 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brachybacterium
            squillarum].
ACCESSION   WP_010533275
VERSION     WP_010533275.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23212
     Region          34..205
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 msmpseeptv aaaeggaraa prrrrhdper rdrivaacld viaehgvagt shrrvaaaad
       61 vplgsmtyhf agmdelleaa frrfaegaaa slerrtaaaq gleealaafa snidedvfgt
      121 drdlvlslel htlaarrpaf reitsawmdr traclepfvd dtaatlldam negltihral
      181 hdreprpgla qeaiarlaap attpgcgseq aggpeptpa
//
LOCUS       WP_010533272             238 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerophosphodiester phosphodiesterase [Brachybacterium
            squillarum].
ACCESSION   WP_010533272
VERSION     WP_010533272.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..238
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24230
     Region          4..236
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mtsprpsvvg hrgapvhape ntlagfrrae qdgaawlecd vhlsrdgqvv vmhdesidrt
       61 aaadsarrtg alaaltaael aevrleagep vpllpellav tgvplfievk apaaatavgk
      121 llaalptssp aaastvisfh pealaqvvrd apgtpvsllv eqideaavaa atelgasgig
      181 pgidglclaa gravhaaglr lnpwtvntae qlavalacea dtittddpaw lharlddr
//
LOCUS       WP_010533308             333 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Brachybacterium squillarum].
ACCESSION   WP_010533308
VERSION     WP_010533308.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..333
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35116
     Region          24..333
                     /region_name="CeuB"
                     /note="ABC-type enterochelin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4606"
                     /db_xref="CDD:443656"
ORIGIN      
        1 mtgsttatta pgtprrgrer lfdrwlllgi lgvalllaas lftgvydifg addgaemfai
       61 triprtialv laggamamsg limqlmtqnr fveptttgtt ewaglglilv mivapsstll
      121 trmvvavvfa fvgtlvffaf lrrvtlrssl ivpiigimlg avvssistfv alqfdalqll
      181 gvwfagsfts virgqyevlw vvalvglavf lvadrltvag lgediatnvg vnyqrvllmg
      241 tglvavatgv vtvvvgnlpf lglivpnivs lirgddlrsn lpwvcllgia vvtvcdligr
      301 liimpfevpv slilgivgav vfialllrtr qaa
//
LOCUS       WP_010533274              69 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Brachybacterium
            squillarum].
ACCESSION   WP_010533274
VERSION     WP_010533274.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..69
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7630
     Region          1..64
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mrneikalrt errwsqaelg talgvsrqtv iaiengrydp slplafklaa vfgapieelf
       61 hpdpeqeqp
//
LOCUS       WP_010533311             279 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Brachybacterium squillarum].
ACCESSION   WP_010533311
VERSION     WP_010533311.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..279
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29826
     Region          11..274
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mtpvaplpln dgrtipqlgy gvfkvdaaka advtgqalta gyrhvdtaki ygneegvgea
       61 vrasglpreq vyvttklwnd ahahddavaa legslerlgl eyvdlylvhw avpsqgqyle
      121 awktlielrd rglatsigvs nypaeqlrei ieatgeapav hqielhpyfq qralrelhse
      181 hgivteawgp lgqgksdlle ndaitsiata rgvspaqvvl awhiahgiva lpksvtpsri
      241 venleaaeie ltaeevaaid aldrpdgrgg adpatfgqs
//
LOCUS       WP_010533313             483 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Brachybacterium squillarum].
ACCESSION   WP_010533313
VERSION     WP_010533313.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..483
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51159
     Region          20..475
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msestgtspa pgaasdsdgq npggelkqai tpkllllfiv gdilgtgvya ltgrvagevg
       61 gagwlpiila favamvtals ylemvtkypr aggaghyihk afgmhfltfm vtfavlssgi
      121 tsastssvfl aenvlaafgl tesmgadaar listiiavcf vvliacvnmy gvsesvkfnv
      181 vltlieltgl alvilvgfwa igrgeadfsq vilfetpedk glfmavigat alaffsmvgf
      241 edsvnmaeev vdpvrnfpra litglsitgv vyvlvsvtav aivpigdlqt attplltvve
      301 vgapnlpige ifpfisifav antvlinmmm asrllygmsr qgvlpgflry vlpgrqtpwa
      361 givfstalav gliltvrfvl neetigalgs ttallllavf glvniavlvl rkdtvrtkhy
      421 rtptvlpyig afttlflvgp waqetrnyvi agallgiglv lyicswiynr airsrrtrfh
      481 dld
//
LOCUS       WP_010533314             137 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Brachybacterium squillarum].
ACCESSION   WP_010533314
VERSION     WP_010533314.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..137
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14592
     Region          1..126
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mptvllayvp sasseaaltf avedalrrda alvvlasdag adprkargvt dprplaerla
       61 etgleldlrt vprrddpadd ildaidemhp dlvvlgirrr tpigkfllgs tsqrvvmest
      121 apvtlvkpas frapsrp
//
LOCUS       WP_010533338             405 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Brachybacterium squillarum].
ACCESSION   WP_010533338
VERSION     WP_010533338.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..405
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42479
     Region          169..401
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtrsggradp rrdldpgpla ptatralsva yavgglgvas iyvplipgql pyfhlpwtma
       61 alavtyllpl gvllaapvap vgalrrvlav agvlgtltlw tlplglrtpl vsldppwvil
      121 avtssavama iaghgrtawa lsvlnglait ldrvlagppg lgptalrdga wsvvlssviv
      181 glvmltqqai rtvdaatata raelreaahr qvarddrrws rqflhdevls vlnladredp
      241 alrdvarrra rsalitlnla spasppttgd gpgvparell arvretvadi dpgttmeael
      301 hdhlvvpaav rtavlaalge alrnslrhag pgtsrrlrvr adrdelrlal eddgrgfdpa
      361 rvgadrlgma esvlagmrrl pgggaevrsa pdrgttvtlt wtpeg
//
LOCUS       WP_010533376             437 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Brachybacterium squillarum].
ACCESSION   WP_010533376
VERSION     WP_010533376.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..437
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=46468
     Region          3..433
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mdpsvlvnia lvllfviigg vfagtemaiv nlresqidql eesgergaat arlvrdpnlf
       61 lsavqigvtv agffssayga stiapslapv lerlglssga agtaalivmt liiaylslvl
      121 gelvpkrlam qnamaltkvv gpplnvfgrl mrpviwllsv stnlvvrllg gdphanreav
      181 sseeiramvr dsdaleeaes rvladvfdas ertvsevmrp rhqvdfldga mtvgearrli
      241 rssghsrypv tgedlddvlg fvhvrdllha eddavttlaa ivrpiehvpg tvavlsalnw
      301 mraqaqqiav videyggtdg ivtledllee lvgeiydefd qagatvtgeq aaviegeidg
      361 glilqefeat tgielpdtgg yetvggfvma rlgriaevgd evqvegghlt vtamderrva
      421 tvhlsrdpaa edeaqed
//
LOCUS       WP_010533417            1144 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Brachybacterium
            squillarum].
ACCESSION   WP_010533417
VERSION     WP_010533417.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..1144
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=119328
     Region          3..1026
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msrlarlsln nrafialvci avsiigafam ttmrqelips vslpqvqvvt sspgssseqi
       61 qerisgpieq avsglenves ttstsqagts mvtlemsygt dvartsnqvd aalnqiedql
      121 pedaepqvvs ggtsdlpavv lsvssdleps eladrldaav vedleridgv ssvavigape
      181 eivritpded elaarglses distaldeng lsvpggsvtd gdksldvvvg qsmdsiedle
      241 tmvlmpseea qeqaqsagqt letttladva tverttedat sisrtdgres lvlmvtatad
      301 gnvvdisedv davledtlad vggdaesavv fdqapfiees ivalaeegll glvmaigvil
      361 lflrrvrpti vtaisiptsl liafigmlvt gytlnmltla altisigrvv ddsivvieni
      421 trhlsygkar mraildavge vagaitastl atvvvflpia lvsgmsgelf rpfaltvaia
      481 mlssllvslt ivpvlaywfl rrpkdapsah deegaaaare aaeakeersi lhriyapilh
      541 ltldtlprrl atlavslvvl vgtvflvpll tinflgdtgq nlasitqtlp agtsledssd
      601 kaaegeealm dldgvetvqt tiggsqfsfs saeneisysi ttdteadqea ltdemvsvla
      661 dipdsgevea advtsatgst svdiqitgpt aearqeandl llaeldplpa gveevtsdle
      721 gdqptavvtv dreaaaergf teeavvglva qqlypgaigt itledteldi vveqgdsvdt
      781 lqqlrdlela pevsltdvas vdeelsrpsi ttqdglqtvt vslapegedv gavttaanea
      841 ieavdlpegv satvggtsad idetfgqlgi amlaaillvy vllvwifksl vqplvllvsi
      901 pfaatgalgl lvitgvalgl psmigllmlv givvtnaivl idlvnqyrrq gmgldealhl
      961 gaakrlrpil mtaaatifal lpmafgitgn ggfiaqplav vvigglisst lltlvivpvl
     1021 yritegpger rrlrreerev aekaaadraa aerrarhrse aaeetsvpte aaamssspvp
     1081 saesssasqv gpedtaarga dvapaedstp aastgpaaag hgarkpslke rgglvgilrr
     1141 rrrr
//
LOCUS       WP_010533466             281 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Brachybacterium squillarum].
ACCESSION   WP_010533466
VERSION     WP_010533466.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..281
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29336
     Region          7..281
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mstftrrttl aatgagvaal alsacgaggt egpqeedgvt tirigaspap hgeilafvqe
       61 nlaadaglal eiteytdyqi pnqaladgdl danfyqtpaf ladqeeekgy effgfegvhv
      121 epmgvysesi tsldeladgd tiaiandptn rgrglavlaa ndvivldpev aenahtpadv
      181 tenplnleft eleaaqiars lgdfaagvvn gnyaleagla psedaiviea gednpnanmm
      241 vvrdadqene alvaldgllh sdevrtfied tytdgsvipa f
//
LOCUS       WP_010533478             234 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Brachybacterium squillarum].
ACCESSION   WP_010533478
VERSION     WP_010533478.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..234
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24511
     Region          4..215
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 msrralvvap hpddevlgag atiarladag wevtvvaaca dlpplypsei apqveaeara
       61 ahavlgvads rfldlpsvev srgsvaalng plqrvmdele pqlalipfpd rhvdhrvvfd
      121 asmvvtrpig sgaalqmvam yetvsetfwn apgaepafvp swtvdatdtl erkveafgcf
      181 asqlqadpga rslhalrala gfrgsqvgla haesfqivra tglegllsrg gigt
//
LOCUS       WP_010533486              79 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl carrier protein [Brachybacterium squillarum].
ACCESSION   WP_010533486
VERSION     WP_010533486.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Moretto,L., Heylen,R., Holroyd,N., Vance,S. and Broadhurst,R.W.
  TITLE     Modular type I polyketide synthase acyl carrier protein domains
            share a common N-terminally extended fold
  JOURNAL   Sci Rep 9 (1), 2325 (2019)
   PUBMED   30787330
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10655536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..79
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=8737
     Region          3..77
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 mnddqildll irqvaaelgt dpdqvepdas fmrlgvssvq alkivnrlrq elgrdinpva
       61 lfefttieqm seyladess
//
LOCUS       WP_010533494              76 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl carrier protein [Brachybacterium squillarum].
ACCESSION   WP_010533494
VERSION     WP_010533494.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..76
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=8213
     Region          7..73
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mdsdsyldvl adfaetprer itmeaeladi gldslsllei imrletatga sldvdqgvtt
       61 vqelfdhvre rageas
//
LOCUS       WP_010533556             173 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brachybacterium squillarum].
ACCESSION   WP_010533556
VERSION     WP_010533556.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 173)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..173
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18180
     Region          2..>172
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 milqatalth rygprevlre vdlavapgev valvgpngsg kstalrllhr alvpqtgtve
       61 legrdlagls arerarsiav msqeaepels vsvadavllg riphrgglgt pthedeavaa
      121 avlervgalh larqematls ggerqrvlla ralaqqprll lldeptnhld iga
//
LOCUS       WP_010533513             307 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Brachybacterium
            squillarum].
ACCESSION   WP_010533513
VERSION     WP_010533513.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..307
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=31442
     Region          1..252
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mrtlvllalv gfaaqlvdgs lgmaygvtst tlllaigtnp aaasatvhla eigttvasgv
       61 shwtfrnvdw gvvakigvpg aigafagatf lswlsteiat pvmavlllal glyvlirftv
      121 rglrtdrlgq plrkrflapl gllagfmdat ggggwgpvgt pailasgrle prkvigsidt
      181 seffvavaas lgflvglgga gvdyrwalal llgglvaapi aawlvrllpp rvlgsavggl
      241 ivltnartlv nletlgldpl lrsavlglvv lawiaavvhs vrrhrgerdl paasaraeqe
      301 vtaapts
//
LOCUS       WP_010533594             250 aa            linear   BCT 01-JAN-2025
DEFINITION  urease accessory protein UreF [Brachybacterium squillarum].
ACCESSION   WP_010533594
VERSION     WP_010533594.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..250
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25227
     Region          2..249
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mallladsrl pvgahvtsng leaalregla pdrigdylas rmqtvtavea gvaviarhlv
       61 ltaapeelpg rvaslrahwa artpsraqre iavvlgdgla rlaavlwpti ldaatvtaap
      121 gaggdapvgp ggddpggaar aadrraparg lpralvlgli aaavgidapa lvrlvaydda
      181 qtviaaqlkl epsdprfgaa qvlaacaald pevgalaalt dpaqlpssga pltehwaeaq
      241 atlprrlfra
//
LOCUS       WP_010533622             249 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Brachybacterium squillarum].
ACCESSION   WP_010533622
VERSION     WP_010533622.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..249
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26405
     Region          6..117
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
     Region          135..243
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mrldnigida adphavgefw eaalgatrlt tepdllesrl vidgdasldi cvvkvaeadq
       61 eplrlhldll ggtpgnpggq aeaatrlral gahdldigqg evpwtvladp ggtpfcvmea
      121 raayvgtgpi aalpldvadp drdaefwawl tgwqdapgia prtlrhpsgr gpllefcpep
      181 apkpagpaak nrihldvrle egddveeihe qildlggrvr ehdwgplpwr vyldpsgnef
      241 cvlggggva
//
LOCUS       WP_010533669             215 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Brachybacterium squillarum].
ACCESSION   WP_010533669
VERSION     WP_010533669.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..215
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=22626
     Region          2..215
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtatttgptl aerayrelra rlllldiapg dpiseaalaa eigvgrtplr eavkrleadh
       61 lvvtyprrgt faasvdladl aelteiraav fplvarraaa srggaaatel aeargqvaaa
      121 dgaegprall emdlavhali draaaspfle etlarldglv trmwclmldr lppmgdhiae
      181 htalidailg gdeehaaala vehvrhfdaa vrgvl
//
LOCUS       WP_010533713              89 aa            linear   BCT 01-JAN-2025
DEFINITION  HPr family phosphocarrier protein [Brachybacterium squillarum].
ACCESSION   WP_010533713
VERSION     WP_010533713.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..89
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=9024
     Region          1..89
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 maertvsias ksglharpat ifskaaaeqp aqvtiekvgg spvqassmlm lmtlgagngd
       61 evtlraegeg aeesvnalae llekdldae
//
LOCUS       WP_010533681             437 aa            linear   BCT 01-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Brachybacterium
            squillarum].
ACCESSION   WP_010533681
VERSION     WP_010533681.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..437
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45303
     Region          10..407
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mfrwtlhgvg rsvapdaiva peerlawplt igigaqhvva mfgatflvpl ltgfppsttl
       61 lfsgigtllf lvitqnkvps ylgssfafia pitaataads mgaalggvmv tgallallgl
      121 lvsrigtawi galmppvvmg sivaligfnl aptayenfqq savtatitlf avvlctalfr
      181 gllgrvsvll gvllgygvav argevdfssv reaawfglpe fhhptvelgl lpmflpvvlv
      241 llaenvghvt svglmtrrnl dhmvgrtlas dglatmlsag fggsptttyg enigvmsatr
      301 vystaaywva gvvaillsls pkvgaaifti pagvlggvtf vlygligivg vrmwvdgkvd
      361 fskpknqfta gvalvvgian vtwtfdgiql tgialgtlaa liiyhlmtli gratgtdavh
      421 qepvartgei pavrpeh
//
LOCUS       WP_010533724             157 aa            linear   BCT 01-JAN-2025
DEFINITION  peroxiredoxin [Brachybacterium squillarum].
ACCESSION   WP_010533724
VERSION     WP_010533724.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..157
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16854
     Region          11..149
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(46,49,124)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mpdpvklavg daapafdlpt agggqvslee lrgapaliwf ypaantslct kpacdlrdnh
       61 qmfldagyrv igispdpvae ldrfaaeqdl pytlacdesh rvmeaygawg tknmygklve
      121 gtirssfaid aegvltfvky rvgtpkhial lqeklgl
//
LOCUS       WP_010533741             379 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Brachybacterium squillarum].
ACCESSION   WP_010533741
VERSION     WP_010533741.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..379
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=38731
     Region          81..373
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mptsspvaap sspsaaevyr dllhhgprar tdlaaglgls gptitrltre mldggllrel
       61 ppvpqakgrp qqplevaedh arflgvkita dsvhaavvtv rgepleersv plsrpapelv
      121 eattaelcre llaahprvag vgvgigaqvd gagtvvsssm lgwsqpvalg prleaalgvp
      181 vtlgndfhal leglawsgps rglrsfavvt igagvgvgsv qdgqvhrgrr hlagvtgslp
      241 titrdgrglp lrdlastahv leaarargld ldpagglapl laagaagder alavaadvah
      301 gvavagaglv gvldpealvl ggegvgllrl dpgfedtlrs rlsrvmrdvd lrllpddfdd
      361 wargagvlav rrfidaadg
//
LOCUS       WP_010533748             197 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brachybacterium
            squillarum].
ACCESSION   WP_010533748
VERSION     WP_010533748.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20735
     Region          10..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgrlprfeta avvssarelf wregyegasv salqqatgln sssiyhafgs krglfdaaie
       61 dylasvvrpg larlraeqvd peaivdylat vrelvldpag htlpdgcllv ntacsgiard
      121 pevaavvsay rselaesfgr giaarfpeas aadrehltrt cvaslvaala ltrvdgeaaa
      181 gflesalall rrphpia
//
LOCUS       WP_010533757             730 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Brachybacterium squillarum].
ACCESSION   WP_010533757
VERSION     WP_010533757.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..730
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=76631
     Region          24..288
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(24,47..48,77,82,87..90,102)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(31..32,34..37,39,51,53,85,101..104,108,110,147,149,
                     151..152,154,178..179,182,199..202)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(31..32,34..37,39,51,53,85,101..104,108,149,151..152,
                     154,178..179)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(35,108,110,147,149,151,182,199..202)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(178..186,195..202)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <336..524
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mdstsrprvp radprlvala qdsgyriger igaggmgivy rasdadhqdv aikllrhdia
       61 ddprarqrla revaaqrsvr nenivrilda elesseafvv tefvpgptle daviergglh
      121 peavreigtt lgetlrvihe agvihrdlkp snvllrgaea adldgfdpeg nrldpviidf
      181 giavaaeesr ltstglvmgt aayldpevvr tnstaaagdw wawaavlafa atgrppfgtg
      241 radlvflrae rgeidvegvp teldawlrda lqadpaarpd peelierlag ldleryddag
      301 etqaldtqgr taafpagaaa gaaagavaga aaagattpla saaaatdedd laatqamapi
      361 ldedddagpp taamdpvgee rpraldaera aapdpdrtqa lppiredegr tqalppirdd
      421 adrtqalpat pvpdptealp avgpattpmp vvrapmpqrq qptaglsgpp pqqqgyppqg
      481 ypqqgrppqg ygpqgyapqq rpvapppgqq mtphpgypgq qpgqagpwpa aaaapkrtll
      541 vwagnvllia lgalapyval tallllgala rtwershrav enrrfkgatg sgprvqvgfa
      601 apfrflwglv etalqallpl ilglvvgiav daiawlglnq alpdgvafgt amavtvlvtw
      661 vglgspttrh gahrvmdaaa pdrtwtavlg vllllmigav iatilarqgm vdyfpfaggf
      721 rledvavwrl
//
LOCUS       WP_010533756              73 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Brachybacterium
            squillarum].
ACCESSION   WP_010533756
VERSION     WP_010533756.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 73)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 73)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 73)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..73
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7282
     Region          1..>40
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 msttavaveg ltcghcvgav teevsalpgv tevrvdlvag gtstlhveae relareelag
       61 aldeagdyrl asa
//
LOCUS       WP_010533776             538 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Brachybacterium squillarum].
ACCESSION   WP_010533776
VERSION     WP_010533776.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..538
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55456
     Region          3..401
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mttpdfarlg vpaslieala pqgittptpi qaatlpdsla gtdvlgrgrt gsgktyafll
       61 plvarllenp rrrqarrprs lvlaptrela tqideslqpl vratglrstv vfggvgqnpq
      121 vqalaggvdv liacpgrlld lmgqkhadls aieitvvdea dhmadmgflp mlrrildatp
      181 kggqrmlfsa tldggvqtvv dryltkpvth sadpatspvg tmehhvlevd sgdrfdvlrd
      241 laaapgrtim ftrtkygakn larklrnqgv savelhgnls qnartrnlea fsdgtastlv
      301 ctdiaargih vdevglvvha dppvehkayl hrsgrtarag esgtvitvqt pdqkkdvldl
      361 mrkanirptr hqhvtvdspv ltqlapgerq isevaveaps aegqaqggrs gggrgqggrg
      421 qngqggrggr sgggrgrsgg sgrgrdgqgs gearggqdrs grggeqgrsg gqgrggsgrs
      481 ggqgrsgrgg eqgrsggqgr sgarggnrgs gssgvystss gegrsgggla afsagrgr
//
LOCUS       WP_010533809             394 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdopterin molybdotransferase MoeA [Brachybacterium squillarum].
ACCESSION   WP_010533809
VERSION     WP_010533809.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..394
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.10.1.1"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061599 - molybdopterin
                     molybdotransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=40469
     Region          12..385
                     /region_name="MoeA"
                     /note="Molybdopterin Mo-transferase (molybdopterin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG0303"
                     /db_xref="CDD:440072"
ORIGIN      
        1 mrperpdpwa wrarlldhla vaprretval aaargrllat pllapdplpa hpvaamdgfa
       61 vrhadlgcep levaaelpar pgvpaplppg taarimtgap ipagadtvvp vedsdarptg
      121 paprrvrlre tprgrhvrta geevsrgqvl aeagdrvgag llglaatlgi ttlpvwarpr
      181 ltvvatgdel sgeevpgavr esngamlrav leaegaavrt lrsgddpdql hrvldgaarg
      241 adlvvttggi sqgavdvvka algprgtgts rfvhlalrpg gpqgagtlpg psgttvpvvh
      301 lpgtpvgalv gaqlfvrpll pgadarprrv dltgtlpeir pgtttalpgr lrlgadgrea
      361 veilegsrla pygraemvvl legqergsal airl
//
LOCUS       WP_010533821             152 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Brachybacterium
            squillarum].
ACCESSION   WP_010533821
VERSION     WP_010533821.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..152
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=15738
     Region          37..150
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mstsesdeqv paarvrhaev tlapvdaatm aaavadprcg alvtfdgvvr dhdegrgvtr
       61 leytahpgag eeiaavaaev aarhpevlla lahrhgplai getalacava aphrkaafaa
      121 cddlvdtvka rlpiwkhqhf tdgsdewvga lg
//
LOCUS       WP_010533840             290 aa            linear   BCT 01-JAN-2025
DEFINITION  SURF1 family protein [Brachybacterium squillarum].
ACCESSION   WP_010533840
VERSION     WP_010533840.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..290
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=30451
     Region          3..250
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mlrvalrprf lgllalmvla tvvcgllatw qwerahrals edtsvaeelg pvqdviglad
       61 pvtnelvggi vtasgsfdae rqilvggrhi dgtdavivvt alevttsege qailpvargw
      121 vpaeqvtgad geldpalapa ppsgeveisg rleaseaatd gifegvasei atpllvnawg
      181 dpmyagyvaq tsaaeglspm pvaesafqrg ldwqnigyaa qwivfgvffl ylwgrtvrta
      241 hldelaaqre elerslasag ehpdqrpdpg vpadaaptqe dadagtptpr
//
LOCUS       WP_010533844             615 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Brachybacterium squillarum].
ACCESSION   WP_010533844
VERSION     WP_010533844.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..615
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=64134
     Region          33..428
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(40..41,44..45,48,79,129..130,132..134,137,157,
                     160..161,164,289,292..293,296..298,301,329,333,386..387,
                     391,395,411,414..415,418..419,422)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mtasttraph paaaepasfa gldrqgtlvf vglmlgmfva slsqtivgpa mprivaelgg
       61 vehyswiata amlvsavavp ivgklsdlyg rrwfylggla vfmlgsilag laqgfwflvf
      121 aravqglgmg tlmplsqtii gdiipprqrg kyqglmgavf svtsvigpli ggtvtdnlgw
      181 rwlfyltlpi gvaafafiwr flnlprgeqq gridfagilt ltpglvigll aitwggnsya
      241 wsspvilgmf avaavflavf vvieirveep llplhllgrp ivalsvlasf aiavamfgai
      301 iyipvyaqgv lgvsatnsga iliplsvami ltsilvgmli trtgkykpfl laggavlvag
      361 ylllarmqyg dsqwhltlam vviglglgls vqvytlivqn avgqrelgia taavqffrni
      421 gstvgtallg tvmtaqmata ierqlqqlpa dqlaaldssg geldasglqa avldpaalaq
      481 lpeflvepir mgmgeamhvv fltavpfval alllslfikq vplrdtlapa edatatgtdi
      541 agtagtgtdq daepdtaapt paeqrrerel vgtstgplhs vmgaagsmsg thtgqfpavd
      601 dsedepegsg rgvar
//
LOCUS       WP_010533943             261 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Brachybacterium squillarum].
ACCESSION   WP_010533943
VERSION     WP_010533943.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..261
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27086
     Region          14..248
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mtasqpapss apltavvtga ssgigratav rlvaegwrvl avarradrla elaaetgcev
       61 lavdvtdeas vdglaarcre lfggtlnavv hvaggalgve svaeadldkw qgmfsmnvlg
      121 slrvtrallp dlrrsgrgdv lfvtsvaate vypggsgyha akagehmlgr tlrlelngep
      181 vrvievapgm vrteefslvr lgdpeaadav ydgvdqplta edcadvisya lnaphhvnld
      241 lvivrplaqa aahkvarhqg l
//
LOCUS       WP_010533878             181 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator, partial [Brachybacterium
            squillarum].
ACCESSION   WP_010533878
VERSION     WP_010533878.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         <1..181
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <2..146
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 prhdplarig rravarmvda agesghlavl hgrdalylve erarrrpslv tergvrlpah
       61 ltasgramla alppaqlrsl ypartpferr teaptitsrp elvaacarir eegvawedge
      121 vtpgfvsvaa pardaagwpi agvaltweag twgageqeae vreerartvr evaaevaraa
      181 g
//
LOCUS       WP_010533976             332 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine recombinase XerC [Brachybacterium squillarum].
ACCESSION   WP_010533976
VERSION     WP_010533976.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..332
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=35710
     Region          12..332
                     /region_name="xerC"
                     /note="site-specific tyrosine recombinase XerC; Reviewed;
                     PRK00236"
                     /db_xref="CDD:234698"
     Site            order(180,278,281..282,313)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 mseerdrpre daalldafvd hlrlergrse htlrayrrea adllthlraa erievtevdv
       61 aalrswlsar aetgaaaptl arsaaaartf vtwlattgri phdvggrlra prrgrhlptv
      121 lstaqagdll dahrqpppad tadpsaatap gtkesadpqa qavrlrdaav lellyssglr
      181 vselvaldrd gidraeatvr vlgkgakerv vpvgrpavaa lddweqqgrp vlaavagaap
      241 gdalflgvrg rrlgdravrd ivdrwardag iarhvsphtl rhsaathlve ggadlrsvqd
      301 flghsslatt qiythvsaer lrrtveqahp ra
//
LOCUS       WP_010534007             433 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Brachybacterium squillarum].
ACCESSION   WP_010534007
VERSION     WP_010534007.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..433
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=45277
     Region          66..362
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 msttepsqmp dppagtwadp lgragsragq vlllaavaag tvwllqqvtv vviavlvali
       61 laaavspmvh wltskgwpdl latlasflai vavaggaitg vvlairsewd slvssalgaw
      121 delrdwiast slpidtgvid davqqatefv tsadfasstl agvsaatevl tglvlivvll
      181 ffflkdgsam wnftlrwfrg esraklaesi draaatlggy vrgtatvalv davligigla
      241 llgvplavpl avivflgafi pvvgatvagt laaavslvtn gpftaliviv iviavnqieg
      301 nllqpvvmgr alslhplivl laltigtivg gifgailavp ytamawtliq vwtdryqagd
      361 dpvlgedpls arerpsrqas ekqrewyrkl rrddrqgapl gaveqeqdat aegdddrdge
      421 qaspgyylrg edn
//
LOCUS       WP_010534022             261 aa            linear   BCT 01-JAN-2025
DEFINITION  regulatory protein RecX [Brachybacterium squillarum].
ACCESSION   WP_010534022
VERSION     WP_010534022.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Ragone,S., Maman,J.D., Furnham,N. and Pellegrini,L.
  TITLE     Structural basis for inhibition of homologous recombination by the
            RecX protein
  JOURNAL   EMBO J 27 (16), 2259-2269 (2008)
   PUBMED   18650935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..261
                     /product="regulatory protein RecX"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /calculated_mol_wt=28875
     Region          80..249
                     /region_name="RecX"
                     /note="SOS response regulatory protein OraA/RecX,
                     interacts with RecA [Posttranslational modification,
                     protein turnover, chaperones]; COG2137"
                     /db_xref="CDD:441740"
ORIGIN      
        1 mtptarpgrg geepagppaa paahpeqgdg pgdlrvpadd edaalredla rrtrriletp
       61 rpapdperaa qekavlhesr ylmrllagrr rsegelrtrl rerevpadva heamarlqra
      121 dllddaafaa ewvrqrrglr alsdealrre lrgkqvdpal ieqalaqplh dttglaavag
      181 eeeldaaere eaeaercral vrsrlrerdr aelradrdgs arqrvtrrld alltrkgypg
      241 dlavrviaae vraareepaa r
//
LOCUS       WP_010534070             396 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Brachybacterium squillarum].
ACCESSION   WP_010534070
VERSION     WP_010534070.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..396
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42458
     Region          10..390
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msiehelfpe dllatfrdra pghdrdntfp eqdladlraa gylgllapad lggrgaslle
       61 agrvqrrlaq aapatalamn mhlvvtgaal hahrlgvqaa rtilaeaaqg tlfafgisea
      121 gneamlfdss tvaeddgagg hrlsgtkift slapvwdrlv vhgrvdrgee epelvfgtle
      181 rseqvevknd wdthgmrgtq srttrlhgah lpaervitrt pigpnrdpfp mgifgvfell
      241 lasvyigiae ravtvgceia rtrrsvtrgl vhaddpdirr rlaeaaigid gsvlqieavl
      301 adldalgtge tgpgltdhga rwflqfsgvk hrsteaaiaa vdqvlrasgg ahffrrsele
      361 rlsrdvragl yhpsdaesvq asyarallge igedrg
//
LOCUS       WP_010534106             594 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Brachybacterium squillarum].
ACCESSION   WP_010534106
VERSION     WP_010534106.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..594
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63598
     Region          45..416
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msetipteea asasaaveqs sgdtlttaga eapaepakqp vvsetfadfd vrediveals
       61 skgiihpfpi qsmtlpvalk grdiigqakt gtgktlgfgi pllqstvapg ednptgrvig
      121 kpqalvvlpt relavqvaed lqdasakrpv riltvyggra yepqiealek gvdvvvgtpg
      181 rlidlmrqky ldlsqvrtav ldeademldl gflediekll ravpekrqtm lfsatmpgpi
      241 lalarrfmtq pthirahdpg dvsrtkadik qvvyrahqld kievlarvlq srgrgltivf
      301 mrtkrqadrv aedlqkrgfa aaplhgdlgq gareqalraf rngkvdvlva tdvaargidv
      361 ddvthvinwn spdddktylh rtgrtgragk kgtavtfvdw edlarwalia rqlglestea
      421 vetystsphl yadldipegt kgtlpkaqrt ragleaeeve dlggpegprd rgsrggdrgg
      481 rsgdrggrgg rggersgggg rgprreerad seagsdagee rprrnrsrtr trrvngevvd
      541 geqgsgpaqq sgtseqggeg eapkrrrrsr ggrgrrrsgq geggtgpaad ssge
//
LOCUS       WP_010534117             131 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Brachybacterium squillarum].
ACCESSION   WP_010534117
VERSION     WP_010534117.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 131)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..131
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14191
     Region          42..129
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mssgtpvdae tgpgepeeaa plsaedaewv aelgrswvev ykksattlvl lrivrdhgpv
       61 aageaaerft easgwsiser glyrtlrrla qsgllttaqv evprtgakrq dfrltpagri
      121 ylrrieaeli t
//
LOCUS       WP_010534098             217 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Brachybacterium squillarum].
ACCESSION   WP_010534098
VERSION     WP_010534098.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..217
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22694
     Region          45..217
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 masgkvaswa hgeefvdeat lfpetgvlar arergnelga tpvlpgagal mrvlaaavqa
       61 rsaveigtgs gvgslyllag mhpegvltti dpevenqraa resfteakir parvrtiags
      121 prdvvgrltd haydlvsfpa hadhapella hatrllrpgg vlviphalfh drvadptard
      181 aatravrell reveqsedli taltgsgdgv laavlrg
//
LOCUS       WP_010534138             339 aa            linear   BCT 01-JAN-2025
DEFINITION  Fpg/Nei family DNA glycosylase [Brachybacterium squillarum].
ACCESSION   WP_010534138
VERSION     WP_010534138.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..339
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=37310
     Region          2..318
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpeghtvhrl aaairtgfgg ervitsspqg rfpeadalag wtladaeaag khlllaftpg
       61 pdveagapvt ryvhvhlgly gswtfageeg fasapaigap rlrvgereda lggaepwrei
      121 vpretvrlri vgprgladlt gptaceelda agrqavldrl gpdplredae perfvrrvlr
      181 srtaigtllm dqsvvagign iyraellfra rldptvpgrd lsegmvrglw edlvpliryg
      241 artgrivttq pehrqieari versrgtrqn gdedptvvpr eesfyvyhrq tlpcrlcrtt
      301 vrsgemagrt vfwcprcqtr rvrragwtre hpaeawava
//
LOCUS       WP_010534146             660 aa            linear   BCT 01-JAN-2025
DEFINITION  M13 family metallopeptidase [Brachybacterium squillarum].
ACCESSION   WP_010534146
VERSION     WP_010534146.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..660
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72225
     Region          2..660
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mttadarpsg ldlshrddav rpqddlfghv ngawlrehvi padrssdgaf halrdrseeq
       61 vreiveeaaa saepsrigtl yamfmdtaai eqaglrplep mlgeiaelad lpaivramaa
      121 pdagtaalls yvwtddhdst ryqvrlhqgg lglpdesyyr edaygeirea ytahlanlar
      181 laelpgragl agdtpealae avmgletrla achvdvvrlr dreksdnpmd avqraelapa
      241 fpwdafiegt gapaaafevt gvgqpefvsa maemlaaedl avlrswmavh avaayapyls
      301 salveedfaf sgtvlsgaee lrerwkrgvg fvegvvgfev greyvarhfp pehkermqel
      361 vaalleayrv sitgldwmtp atrtralakl ekftpkvgyp dkwreyedle ivegdlvatv
      421 rasrrfeaaf eyakvggpid etewhmtpqt vnayynpgan eivfpaailq ppffdaeadd
      481 avnyggigav ighevghgfd dqgskydgdg nlvswwseed raafdertas litqystlsp
      541 reledthtvn galtigenig dlgglsiavk aylatrseee aaaeidgftg lqrvflswat
      601 vwrgknrpqe airrlatdph spaefrcntt lghvdafhea favtegdgmf lapdqrvriw
//
LOCUS       WP_010534246             360 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brachybacterium squillarum].
ACCESSION   WP_010534246
VERSION     WP_010534246.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39187
     Region          1..358
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matvtfdnas riypgqerpa vdnlnieiad geflvlvgps gcgkstslrm lagleeidag
       61 riligdrdvt dvppkdrdia mvfqnyalyp hmtvadnmgf alkiagtpka eirkrveeaa
      121 kildleqyld rkpkalsggq rqrvamgrai vrspqvflmd eplsnldakl rvstrtqias
      181 lqrrlgvttv yvthdqteam tmgdrvavln ggvlqqidsp rrmydhpnnv fvagfigspa
      241 mnlleekltd qgvqfggavl pvdrstltdt nensvtvgvr pedlelvtdg eglavevdvv
      301 eelgadayvy grlagddsgk eiiarvdgrr ppakgetvyf rpkqghlhlf dvksgqrlgd
//
LOCUS       WP_010534250             466 aa            linear   BCT 01-JAN-2025
DEFINITION  D-alanyl-D-alanine
            carboxypeptidase/D-alanyl-D-alanine-endopeptidase [Brachybacterium
            squillarum].
ACCESSION   WP_010534250
VERSION     WP_010534250.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Kishida,H., Unzai,S., Roper,D.I., Lloyd,A., Park,S.Y. and Tame,J.R.
  TITLE     Crystal structure of penicillin binding protein 4 (dacB) from
            Escherichia coli, both in the native form and covalently linked to
            various antibiotics
  JOURNAL   Biochemistry 45 (3), 783-792 (2006)
   PUBMED   16411754
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..466
                     /product="D-alanyl-D-alanine
                     carboxypeptidase/D-alanyl-D-alanine-endopeptidase"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47542
     Region          76..464
                     /region_name="DacB"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG2027"
                     /db_xref="CDD:441630"
ORIGIN      
        1 mvperiwrnt aialciavpa sfyllgdlad afpgvltvrs eqsepgagpa aeaedwervt
       61 tpapqghvap evdeeaaadv atrmdahagl pvvegnlays vvdadsgeqi aardaetari
      121 pastlkllta aavlrvrdad evlttsavvs dgtitlvgeg dmtltedklt slaedaatla
      181 aeqdtdtval avdttaltgg enpawgdngi dggwvtptaa maleegwldg eqygaksadp
      241 vgdvaerfre lleeqgltve gdvasaeapt gaaaaevtsa plgeivrhtl lisdnttael
      301 lahlvaqarg edttpeaaaa aveaeirela aelgvpeedl eafeiadgsg lsrdnrvppt
      361 vlasvlgeva sgdvaeleqi lydvpiaals gtladrfdae dtsqaaglvr gktgylggaa
      421 tlagittlpd grtvgysiiv hgfegseaad araavdevaa elvsgs
//
LOCUS       WP_010534271             266 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Brachybacterium squillarum].
ACCESSION   WP_010534271
VERSION     WP_010534271.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..266
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=29240
     Region          28..181
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mdtlrelldw alhfsgqlee wvllvadaww vylvvlgfaa fdgffptvps estivtlssl
       61 wsssgqpyiw liclaawmga wagdnmgfwi gkkvgwerfr flregkgrra veaadrglqr
      121 rallflmtar yipfgrtavn lvagavgyph arfwprslls tfvwavysca igavagawfe
      181 dnhllaitva lvaavvlalv verlisalhr vldlraerrg evptdrtslp geepsatyae
      241 geavsspasp sevstkdasi aegehr
//
LOCUS       WP_010534306             214 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brachybacterium
            squillarum].
ACCESSION   WP_010534306
VERSION     WP_010534306.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..214
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23960
     Region          13..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          <159..208
                     /region_name="TetR_C_32"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam19344"
                     /db_xref="CDD:437176"
ORIGIN      
        1 mamqeaprar tprmtgrerr eqlvtigrtl faekgydats veeiasragv skpivyehfg
       61 gkeglyavvv drevstllas lesslrdqra hprvlmeraa maflsyideh edgfrilvrd
      121 spvsqtggtf sslltdvarr veeilaaqlr qhrypttdap myaqmlvgmv sytgqwwlet
      181 rqpskeevaa gmvnlswfgl saierrpqlr aras
//
LOCUS       WP_010534427             367 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Brachybacterium
            squillarum].
ACCESSION   WP_010534427
VERSION     WP_010534427.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..367
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41216
     Region          23..334
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mstspsspss rpspgtpatg qvthdqrgsy vtqgkafdrd mtyipdritr dgrdgwpvep
       61 gryrlaaara cpwanralis rrllgledai slamagpthd qrswrfdldp ggvdpvlgie
      121 rlqqayfary pdyprgitvp avvdvpsgqv vtndfqrmtl dfatewtahh regapdlype
      181 gqreeidaln rwmlhrvnng vyktgfagtq edyereyrsl waaldeleer lgrsrylmgs
      241 riteadvrlf ptlirfdavy hghfkanrqp lftmpnlwgy trdlfttpgf gdtidlqqik
      301 ehyyvvqtdi nptqvvplgp dpsglisphd rdrfdtdtwg pegsappppr adervdpart
      361 plppaaa
//
LOCUS       WP_010534422             425 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Brachybacterium squillarum].
ACCESSION   WP_010534422
VERSION     WP_010534422.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..425
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43313
     Region          5..416
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mstpnsspal arrlgtgdav miglgsmiga gifaafapaa aaagsgllig lalaaliayc
       61 natssaqlaa qyptsggtyv ygrerlgawp gfvagwgfvi gktascaama mtfaayavpe
      121 swqrpaavaa vlalaaintr gvtrtaaatr vivtvvllvl amvvlaglts gapaldgvvs
      181 lrmgdggwma ggwygvlqsa gllffafagy ariatmgeev reprrtipra iltalglala
      241 vyvliavall vtvgaagvaa sptplaevlr vrgwewgvpl vrigaaaaal gallaliagi
      301 grtslamarq gdlprwlatv hprhqvphra eialalvvsa lvltvdlrea igfssvgvll
      361 yylianlaal tqeapdrlya kgwqvlgaig cvvlvatlpp vsiaaaavmf algvgyrllr
      421 lrrar
//
LOCUS       WP_010534559             281 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Brachybacterium
            squillarum].
ACCESSION   WP_010534559
VERSION     WP_010534559.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13293421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..281
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31080
     Region          58..258
                     /region_name="PRK08317"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:181382"
     Region          60..149
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 maeqphrsat edelaswrei laeqptgwdf sdlegirhpe tpwsyetivr nlvvtahrvl
       61 dlgtgggell atladvlpeg tvategwapn vplardrlar lgievvqhhc eegarlpfed
      121 dsvdlilcrh esfdaadvar vlaprgaflt qqvggddlqe ipaafgiepr ypentlmdaq
      181 nalvragltv eradvvhdry efadmttllr flrrvpwmap egldadrhre glerlaaefe
      241 dgpftatatr fvilarkpge vdegrtdfss lptddlevpq v
//
LOCUS       WP_010534654             462 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A [Brachybacterium
            squillarum].
ACCESSION   WP_010534654
VERSION     WP_010534654.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..462
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=49244
     Region          19..462
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msgeddlftl ggdapaprtl sdrnrdhrap lavrmrprsl eeivgqhaal epgsplrrlv
       61 aaddartapa svilwgppgt gkttlayvva qsgdrefvev savlagvkdi revvdaarsr
      121 lrttgretvl fvdevhrfsk sqqdallpsv enrwvtliaa ttenpyfsvi spllsrsimv
      181 tlesldradl dalvdralts pqgldgavtl tpeareallr lgggdarkil tsleaaaaaa
      241 lmtgggeger eitaevlaqa vnraalrydr agdqhydvts afiksmrgsd vdaalhylar
      301 mieagedprf iarrvviaas eevgmadpta lqvavaamqa vqmlgmpegr iplaqavvhi
      361 atapksnasy taldaaiadv ragragdvpa dlkdahyaga salghgqgyr yahdaphgvv
      421 aqqyppdelv gtdyyhptgh gaeertrqrv qalrrivrdq qg
//
LOCUS       WP_010534699             207 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Brachybacterium squillarum].
ACCESSION   WP_010534699
VERSION     WP_010534699.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..207
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21248
     Region          17..201
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 meqflavala halallipgv dfvlivrtal ergaaraslv clgialahaa iialaftgva
       61 lvqrpvvldv lqlaggvfll wmawriarap shreltlhnp sapsrprsaa saigagaava
      121 alnpknllfy lalsaalgsa ttavrlgygv wmvavvlggd llialvlgrg rgtttlrral
      181 pwinrlaala laivgaamil rlllaaa
//
LOCUS       WP_010534725             357 aa            linear   BCT 01-JAN-2025
DEFINITION  LLM class flavin-dependent oxidoreductase [Brachybacterium
            squillarum].
ACCESSION   WP_010534725
VERSION     WP_010534725.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..357
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37600
     Region          46..352
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 msdtpasapg lgigmiaqie hgrvraegds rrsdalaegi elftaaealg ydvgyvrtrh
       61 lqdtlaspll flaalgqrvt rmqlgtavip lrfenparla edlatcdlll ggrlraglss
      121 gyssrdtmya gaygtvrggv gdhvdrvlsr llslvdgevv shadahiegv dagtplqirp
      181 qvpglrsrls ygaaspqraa sigsrgmglq latmalddgs grsfetlqld alhayreasr
      241 aaghgegtvm vsrqmlpvat eeeieryvsl iprersatpg ttgeyrgrei ggqgavygpv
      301 iiddpsvvaq ylmadavvre adeltlvlpf gasldeqrgv lttfaeqvvp hlvaggl
//
LOCUS       WP_010534775             490 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar porter family MFS transporter [Brachybacterium squillarum].
ACCESSION   WP_010534775
VERSION     WP_010534775.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..490
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51771
     Region          25..463
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(36,154,157,161,282..283,287..288,291..292,388,
                     392..393,397,420..421,424)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 mssphsgpgq aeapapglnr kvigisvaaa vggflfgfdt svingavgam sdafelgvfl
       61 kgfsvssall gcavgawfag glanrlgrvp vmvlaaalff isaigsglav gvadlivwrv
      121 igglgvgaas viapayiaev apakyrgrlg slqqmaivlg ifaallsnal lagvagssae
      181 tlwlgiaawr wmfmieaipa liyglmalrl pespryligk geldkasrvl ydftgeldvn
      241 lkiqqiqtsl ererkesmrd llgdrfglkp ivwigillsl fqqlvginvi fyysttlwqs
      301 vgfdesqall tstigsvtni vatiiaillv drvgrrimll vgsagmfvsl gmmalafsfa
      361 egvgdsvsls qpwsgialvf anafvmffgv twgplvwvll geifpnrira salavaaaaq
      421 wmanftisvs fpslsaigls fayglyaafa lisfifvftq vpetkgrele dmdslelgrk
      481 rrdrgastar
//
LOCUS       WP_010534781             512 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Brachybacterium squillarum].
ACCESSION   WP_010534781
VERSION     WP_010534781.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..512
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53536
     Region          29..512
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mntphdpetp ssestggpgg aaladapvdh npsgktffgh prplanlfsv emwerfsfyg
       61 mqgilaiymy fsatqgglgi detvaagivg ayggsvyifs ilgalvsdrl lgpektlfgs
      121 asmimaghia lavlpgvpgl vvglllvgig sgglkstaat lvgslyevnd pkrdagfsiy
      181 ymgvniggll gplltglfqq lwgfhlgfgl aalgmaiglv qyaltrsglp aavhrvpdpl
      241 prrlypvwgg ialavivlvi vlvatgvvhp gnlasimvgl aligaivifa llltsskvdt
      301 dersrvvafi plfigtaaff alfqqqftvv tlysdsrldr elslpflgdw tmpipwvqsf
      361 npffiivlap vfaalwtklg prqpgtpvkf algillmgsa fllflpmasv asvpvlwial
      421 illvatlgel slspvglsla tklapraypv mmmalfnlsi algtamsgal arfysaenev
      481 ayfgglgavt iaiglimlai snpvgkamrg vr
//
LOCUS       WP_010534857             196 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmD family RNA methyltransferase [Brachybacterium squillarum].
ACCESSION   WP_010534857
VERSION     WP_010534857.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002368
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..196
                     /product="RsmD family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0031167 - rRNA methylation [Evidence IEA]"
                     /calculated_mol_wt=20270
     Region          3..190
                     /region_name="RsmD"
                     /note="16S rRNA G966 N2-methylase RsmD [Translation,
                     ribosomal structure and biogenesis]; COG0742"
                     /db_xref="CDD:440505"
ORIGIN      
        1 mpriiagtlg grpvpgtvak gtrptsdrvr ealfsrltgw dalagarvld lyagtgalaf
       61 ealsrgaasa llvethapta rslratakel glaercevra gkaetvaaql asdhpapaah
      121 pflpadlvfl dppyvvdtsv ledllatlap alaaealvvi erssrsrpia wpegwgddgt
      181 ktygetvlqy ggplap
//
LOCUS       WP_010534861             343 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Brachybacterium squillarum].
ACCESSION   WP_010534861
VERSION     WP_010534861.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..343
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36255
     Region          10..246
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mssalplpgv ehlrdlveah pawwdgapga gdpspvtggi eltelgrges yiaylarrga
       61 aelvlrvphk dpaeldgdpa aelatlarvt aglgaapiav htpeatpgas isvttrvpgr
      121 mlpaaawddp allrrlaqrl avlhvhgdta glevperidp vaaaedgrrw wqehepasae
      181 alieplwpsf larleqtlpa fdgadrvllh gdpaasnllv deagevrfvd wewaqvgdaa
      241 rdlafiggpv aaepwyavlt parvraqaed yltareaeha aaglaapdld leallvrrea
      301 hllqevvfta ahlhrvgesg gergvqaaat sramaaqlrd hlg
//
LOCUS       WP_010534807             174 aa            linear   BCT 01-JAN-2025
DEFINITION  Dps family protein [Brachybacterium squillarum].
ACCESSION   WP_010534807
VERSION     WP_010534807.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..174
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=18593
     Region          30..172
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mnetvtvpqp agaartrpen aeggflagda laknlqsvlv dltalslvgk qahwnivgpn
       61 frdlhlnlde vvdiaressd dvaermralh atpdgrpavv aeqsslpafp agevlttdai
      121 dlmtraveat vatmrevhde vdeadptsad ilhgviekle qqawflsaen rrpa
//
LOCUS       WP_010534876             165 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Brachybacterium squillarum].
ACCESSION   WP_010534876
VERSION     WP_010534876.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..165
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17547
     Region          21..163
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mtdptstqts tpaptthlpd yarvvvglgq dersrhvvdr aaqitraadg mlfvvvafdp
       61 lprrdqarla sdvpdsrfwq vatleaaeal leetlarled tgvrtqgvlv eyepahalel
      121 valenqaglv vvgnsgvstm lgrmfgspav qvlrrascdv lvvag
//
LOCUS       WP_010534977             213 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Brachybacterium squillarum].
ACCESSION   WP_010534977
VERSION     WP_010534977.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..213
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=23285
     Region          1..206
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mtqapaprtl vflgdsitdc grredpdelg ygyvrliaey faahepgarv inrgiggdkv
       61 advaarfeqd vlaldpqvvt ifvgvndvwh gftrgetvtd edfergyryv ldqlsatrpg
      121 lpvllvipfv vdvdqekagy hgeldrkvai irdlakefga avvdletmle eawrvghtpa
      181 siaedgvhpt iaghrliadt wldafatidr tkg
//
LOCUS       WP_010534982             209 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Brachybacterium squillarum].
ACCESSION   WP_010534982
VERSION     WP_010534982.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..209
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22781
     Region          5..193
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 maeytlpdld ydygalapsi sgqimelhhs khhatyvkga ntaleklaaa reagdfgtvn
       61 qlskdlafnl gghtnhsifw qnlspeggdk ptgelaaaid eyfgsfdafr ahftaaalgi
      121 qgsgwavlay epaggnlvie qfydqqngip vatiplfqld mwehafyldy qnvkadyvka
      181 iwdivnwadv qkrfenarsn asgivvptv
//
LOCUS       WP_010534999             255 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Brachybacterium squillarum].
ACCESSION   WP_010534999
VERSION     WP_010534999.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..255
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26653
     Region          7..251
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtvvtavqsv draarvlehl avhgeasige lgralgvhas tasrlvaala ehhlvertda
       61 gpvrlgvgvl rlaaatrgrl dlaeqsrevc eelaaelget invavyrdga avnvhqsrgp
      121 stiamhswvg eaaalhatat gkmllahqde aeqervlglv reaftprtvt avaaleaelr
      181 rargagwvaa veeyepglva vavpireedg avaaamsaag payrlpaegl davarrlerg
      241 aseisarmgw rtdqp
//
LOCUS       WP_010534994             100 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Brachybacterium squillarum].
ACCESSION   WP_010534994
VERSION     WP_010534994.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..100
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10434
     Region          7..92
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 msvtkgllvr lealpgkede vqkflgigrg lveeepatia wfairlgpss fgifdvfpdd
       61 agrdahlsga vaaalgeqtg klfseptiek ldvlgsklpa
//
LOCUS       WP_010535109             235 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Brachybacterium squillarum].
ACCESSION   WP_010535109
VERSION     WP_010535109.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..235
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25471
     Region          21..191
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(23,25,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(50,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mtqpaplgag aapaadrtwf vvplfnegev vgdvirslre ryplvvcvdd gsaddsaria
       61 eeagaavvrh pynmgqgaal ktgidfalrd pamaqivtfd sdgqhqvdda aamialreae
      121 dvdlvlgsrf ldartrpgwa krlvlrgavw ysnltsgvkl tdahnglrvi grgacekisi
      181 eqnrmahase iveeigrhgl svreypvhil ytdysrskgq smlnsvnivi dmlfr
//
LOCUS       WP_010535068             835 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Brachybacterium squillarum].
ACCESSION   WP_010535068
VERSION     WP_010535068.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 835)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..835
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84482
     Region          12..820
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 marttpirlt plrrhlaavi tialscafva vmvvagtllt qalssqatqt yagtdlvitt
       61 gideedlaag qplpapevag atdvrpqiqg fvamsgpdgd relfldaval aedptlvegt
      121 lpssadevvl dataaeqlda avgdtvtvga dlsmagerte yevvgiapga egsvfgatar
      181 vmispenaas llgpfegtds gtwfadvaag edpaavaaaa arddltvrts eevideevqe
      241 ltgssivllm vlgvfvvial ftsavviant favtvaqrtr slallrtlga traqvrrvvl
      301 resmlvgllg agigvlaghl lvqavlaaaa gigwleglam vpisllsvll pilagvlitl
      361 laslapmraa trvapletlr paeaavrgrg pgargvigiv lfalgvallv ggtalslagq
      421 gavgiltgma ggvlsfsgll lglrlltapl vrgigsllgr lgglparvar tnvgrnprrs
      481 aatigallig ttlmtmmavg artaevslts eldsrrpidl visaeampad aseqvaavpg
      541 vaaalptera evevgardtm ttyavtpetm reishrpeaa dqladgvvli gaeragifgl
      601 tggetitvdg adgtpvqlev vidanlqmfl vtpatledla gddtapvvla dhadpgtaar
      661 egidagalyl dvsavtaqeg weeptiqagg mereaygqil dvllgitlgl lavavlvalv
      721 gvantlslsv vertrenall ralgttrrqm ramlgwegvl lalvgavlgi vlgavygmlg
      781 itailgadfp vtislpwgrl givlgtaila galasvipgr aaartapaaa lagge
//
LOCUS       WP_010535208             619 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 3 protein [Brachybacterium squillarum].
ACCESSION   WP_010535208
VERSION     WP_010535208.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..619
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66376
     Region          50..564
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mptsdgslpv lataedgtry rdlngngrmd pyedprlgpe ertedllgrl slaeaagllf
       61 htvietgpgg allegpgqia ksgteqvvlg khlshfnvhg lesaeaaatw snrlqqlaer
      121 tphgvpvtis tdprhgatqn agaswetgff slwpeplglg aigdeelver wadtvrreya
      181 avgiraglhp vadlateprw arqreclgqd aawvsravrr alrglagdgs gpavastikh
      241 fpgagpqkdg edahfpygrd qvypggrfae hlapfeaava egtdaimpyy grplglsidg
      301 edieevgfgf nrqvltgllr erlgydgviv sdwelvndnh vgeqvlpara wgvehlspae
      361 rmarileaga dqfggeecte llldlvaegt vseervresa rrllrvkfrl glfddpyvde
      421 qaapaavgre adrraghaaq atsvvvlhdd ggrlaalaag agerriyveg lhaeaaarlg
      481 tvverpedad lallrigapf qprddlflea wfhqgdlaft pglahrlari rahcplvldv
      541 dldraavltd iapvtdtltg tfgvsdlawv daltgtippr grlpiemprs mqavrdaped
      601 vpggtadply prghgltad
//
LOCUS       WP_010535232             253 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator
            [Brachybacterium squillarum].
ACCESSION   WP_010535232
VERSION     WP_010535232.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26256
     Region          1..253
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 myapqrhrqi ldalehdgrv avsdlaeqfg vatetirrdl deldrrglll rvhggavarr
       61 ttvlepdlda rrstntaikd riaaaaaell ptdpaaavql dagtttlalv phlrgrtgsv
      121 vthaldvaqa alaldgpavh llpgrlrpgt gaavgaatve aihrlrpela vlacngfdae
      181 alytpdpseg avksaivqra arrvlvadss kastthlvav aamsdidtlv tddglppsmr
      241 saladagidv vla
//
LOCUS       WP_010535249             198 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Brachybacterium
            squillarum].
ACCESSION   WP_010535249
VERSION     WP_010535249.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..198
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21694
     Region          52..187
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msiraltelp aaprrarvpl gptgplestl gaiarrlygg kvpdplraaf hhrrvlagwl
       61 glesaamtwk rlpprlhala vlavsqeigc swcidfgewe frhrgidpra vreidrwtts
      121 daysdldrav lryavaasat psaatdamve dlrpalddrq ivelaalval enyrsrfnag
      181 lglrsqgyrd dcavpevv
//
LOCUS       WP_010535256             272 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Brachybacterium
            squillarum].
ACCESSION   WP_010535256
VERSION     WP_010535256.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..272
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26025
     Region          38..245
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mtllgivvvv lavlvglslg llggggailt lpllttvagl gpreavggsl lvvgssallg
       61 vllrrrgggi rwraalvlgg ggvigaqlgq vfgrqvppav lmvvfglvml vsaahmirgr
      121 rprgpadega gsppgshdaa prvswvrtal lglgvgvltg fvgagggfll vpalvlglgl
      181 pmpvavgtsl vviaansvsg lagylaaggs vgpmvlgvta aallgtvlgt rlagrvpaaa
      241 lrrgfgvlvl vvglgvlgge llgavppvga ag
//
LOCUS       WP_010535269             216 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Brachybacterium squillarum].
ACCESSION   WP_010535269
VERSION     WP_010535269.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..216
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22688
     Region          27..>205
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mppsspstsa patvepladl rvphhpledv lgvltgtfla slglylleta gavtggtagl
       61 alllthatsl pfavlfllvn apffglaiwk kgwsftlrta lcvaivsgfs vlherwlhia
      121 qihpleavig gnllvgvgll ivfrhgaslg gfnilalilq eraglragyv qmaldvtvil
      181 lgllvipwpw vllsalggvv lnlvlalnhr pgryra
//
LOCUS       WP_010535286             431 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA recombination protein RmuC [Brachybacterium squillarum].
ACCESSION   WP_010535286
VERSION     WP_010535286.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..431
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46448
     Region          74..362
                     /region_name="RmuC"
                     /note="RmuC family; pfam02646"
                     /db_xref="CDD:460637"
ORIGIN      
        1 mdaltvilil ltglllgaal gatggvlvmr erhrtqlsrq ggqaessral mdlagerfer
       61 dtsrreatdq ardaqlqrtl apisaslgqv eqalarteql rarsegmlrq hlgdlaertd
      121 rldqgthalt aalrsptarg rwgevqlrri veaagmlehv dfteqlagsr adgekgqrpd
      181 lvvhlsgdrr vvldakapmd ayldateetd peraaarrra hakalrghvd tiagkaywkg
      241 lgdspeftvl fvpsdgvlaa alesdpglle hafakevvia spatlmallr tvahtwrtda
      301 lnrdaravle agrelhhrlg tfgghlgkvg rsldssvaay neavgslqsr vmvsarrfed
      361 lgltgtplpe peqltrrart lratepdead prqvgpdeve qaltepveqe iadlaagdaa
      421 argeqegrha g
//
LOCUS       WP_010535132             295 aa            linear   BCT 01-JAN-2025
DEFINITION  biotin--[acetyl-CoA-carboxylase] ligase [Brachybacterium
            squillarum].
ACCESSION   WP_010535132
VERSION     WP_010535132.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Chapman-Smith,A. and Cronan,J.E. Jr.
  TITLE     The enzymatic biotinylation of proteins: a post-translational
            modification of exceptional specificity
  JOURNAL   Trends Biochem Sci 24 (9), 359-363 (1999)
   PUBMED   10470036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..295
                     /product="biotin--[acetyl-CoA-carboxylase] ligase"
                     /EC_number="6.3.4.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009374 - biotin binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=30123
     Region          24..286
                     /region_name="BirA2"
                     /note="Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme
                     transport and metabolism]; COG0340"
                     /db_xref="CDD:440109"
ORIGIN      
        1 metdrsrdpl aatttpaprg pvpplrelpr vgstqdeaaa rlsggvgapf avlaaeqtag
       61 rgrlgrpfss paegslaltl awrtplppta rswfpfavgv aavdavrsvt gatgvglkwp
      121 ndlvtaegrk lggilaearg adavllgigl nllgpvrgpd gapvpvatwl ygpdgllpgp
      181 sptgaataal rralaeemlt gltgeltale anggrarasg lrdrytmtcl tvgrpvrvhp
      241 lgatgaedps awdglargvd eagrllvedt rghrhavdvg dvrhlrspea arngs
//
LOCUS       WP_010535324             384 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Brachybacterium
            squillarum].
ACCESSION   WP_010535324
VERSION     WP_010535324.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..384
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=40388
     Region          <235..383
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 msgalapdqt erailqhase dgmgcpcdlm vledatgalt aealdiaaeh edarvlswta
       61 sarraaalhe rfsdhplrar lllpegpepw plqeaaasmd arttlarlpr slgeledrar
      121 rlgvaaltag rddltliagg rvkhmtrsqn evlarvfmev apgrgvgksr alrgagvrpg
      181 lalpepaagq advrvrgesa riplrgigga fggakpdags llllgaldaa lvdgevpevs
      241 aavdlgcgtg lltqwlaral paaqvlgsdd dadavastra glqaaglddp arirlswdda
      301 lsrepegsad lvllnppfha gtaidptlvq glldaaarvl rpggelwtvh nshlryrpev
      361 errigpvrer ardrrftvls arra
//
LOCUS       WP_010535383             497 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Bacteroides].
ACCESSION   WP_010535383
VERSION     WP_010535383.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..497
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55604
     Region          40..448
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkrihiyilt amvllnsscs adwldlntts svetgqaivt lddaqialng iyrlasghsy
       61 ygdnywyygd craadvqari tkgdgkrvsp yyeynvlasd nlnivlpwnt vykvirqtnn
      121 liqkiesgsi qssdtkelnr iksealvmrg lslfnltrlf gmpytndkga slgvpietsp
      181 sdpthkpsrn tvaqcyeqvv sdmsnalsgl tqetsngyin ywaaqallsr vylnmgeyqk
      241 aydaatdvin nnggryqlys yeeypnvwgq dfqseslfel yitlsepsgg tggegapmvy
      301 aneatidwnn lilsedflnl lnedpkdvrh cltkesvien ntglptaarh ekvylakfpg
      361 ktgddpktnn iciirlsevy lnaaeaglkk gtnleeaqsy lndiisrrtt dtsqqvstet
      421 ftldrilker rkelvgegei fydylrngla ierkgswhle tlkafnaqki eatdlrialp
      481 ipqseidanp niqqnpr
//
LOCUS       WP_010535399             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Bacteroides].
ACCESSION   WP_010535399
VERSION     WP_010535399.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..190
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22048
     Region          21..186
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnpfnvkdnt tidtgkleki fleegickkl kkndylirqn eknsqigfvs sgifrlshid
       61 gnanewivgy sfkddfvcdy pslmsktnst vniqastace vylltsdrln qfwetdmdtq
      121 rlgrqiaenm faeiyqrllg fycdtpeqry qtlmkrcpdl qkhlslkeia qflgitsetl
      181 srirrkqlfk
//
LOCUS       WP_010535504             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Bacteroides].
ACCESSION   WP_010535504
VERSION     WP_010535504.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..267
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=29430
     Region          119..213
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mrtaiklill nlliaqiiap ilvmipcviy lvattgnldk dalitmlmip aqlagqlmmg
       61 vylwkagyis tkkttwspvs ssylffsalt vltcgfvvsa ltelmdwipn imeqsfdilq
      121 sgwggilaia iigpvleell frgaitkall qqysptkail lsallfgvfh inpaqilpaf
      181 ligilfawty yktaslipci lmhvlnnsls vflsikypea enmsdlmnts tylmvifaav
      241 lilagviwgm rrttipypwk eetnitd
//
LOCUS       WP_010535549             216 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Bacteroides].
ACCESSION   WP_010535549
VERSION     WP_010535549.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25209
     Region          8..>103
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mmehgrdasq kaelreriim tateaftlkg ikcitmddia aalgiskrtl yevfadkesl
       61 lkecilhkqa erdkylqaiy eqsnnvlevi lavfqksiei fhqtnkrffe dikkypkvya
      121 mmkdrsesds ektmsffksg veqgifrsdv nfeivnllvr eqfdvllntd icneypfiev
      181 yesimftyir gistekgarv leefiseyrk nrveqq
//
LOCUS       WP_010535585             227 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Bacteroides].
ACCESSION   WP_010535585
VERSION     WP_010535585.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..227
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25212
     Region          148..226
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 meakkskkaa ienqrgswll mglvvalafm fvsfewtqhd vrvaalssdd esifvtelvp
       61 itfpeeklep ppppetkvtd lfeivddtee vtdnvsvvpd nvnepykvvw vppvvetaev
      121 eedvihvsve impefpggsa ellkylsthi kyptmsqemg sqgrvivqfv vdkdgsitsp
      181 tvvrgvdayl dkeairvisg mpkwkpgvqn gkkvrvkytv pvvfrlq
//
LOCUS       WP_010535751             339 aa            linear   BCT 01-JAN-2025
DEFINITION  FecR family protein [Bacteroides faecis].
ACCESSION   WP_010535751
VERSION     WP_010535751.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides faecis
  ORGANISM  Bacteroides faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Bacteroides faecis"
                     /db_xref="taxon:674529"
     Protein         1..339
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=38749
     Region          90..331
                     /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"
ORIGIN      
        1 minnklnide iiiryldgta tdsdkeqllt wlkesdknlh sysefrdvwf asqsnssvhs
       61 dmekalkrle krikgkesek kinivspynf yktarvaaff allfiigitf yhigrnvtkk
      121 dililnhlit dsgskrrfvl pdstivwlns nskleypttf sessreisle geayfevshd
      181 vnkpfhvhag dmdievlgth fsvenypdkk gveavlaegr ikvtgseipv plvlepgeli
      241 rydksnkqtv vkkvdaenyi swiqneltfd nakladivmn lkkwysidie cdssigqnls
      301 msftlhkged ldeilkamtl iipvryywkd nvlnivsvk
//
LOCUS       WP_010535671             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhomboid family intramembrane serine protease
            [Bacteroides].
ACCESSION   WP_010535671
VERSION     WP_010535671.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..224
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=25180
     Region          1..218
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mptvtknlii invlvffgtl vaqrygidlt nylglhffla sdfnpaqlit ymfmhggfsh
       61 iffnmfavfm fgtvlertwg pkrflfyyiv cgigagliqe gvqyikyvvd yshysqvdig
      121 tgiipmgdfl nmlttvgasg avyaillafg mlfpnnqlfi fplpfpikak yfvigyalie
      181 lyagfannpg dnvahfahlg gmifgfilim ywrkksrnng tyys
//
LOCUS       WP_010535791             734 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha-galactosidase [Bacteroides].
ACCESSION   WP_010535791
VERSION     WP_010535791.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16044983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..734
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=84009
     Region          45..274
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          279..628
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Site            order(323,354,401,469,473,519,538,541)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          642..730
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mkkivyvlll cllfpakklq awndkvlist prssillntw gegqqlqfay fgdrinedqi
       61 nqvfdswngl srpvypvfgt sayessalqv vhadsnltld livdkvetfd eenakltviy
      121 lkdrvypfyv tlnyrafkti diietwaeys hnekkavilk rfdsghfmir rgnvwlsslp
      181 ghwgaetqit tepltsgmkv iknmdgvrng lgehsevmfs ldgkpqensg rvigailcwg
      241 grtkiridsd dtygshvhhv fagmneease ykleprekft tpklaltysc eglggasrnf
      301 hrwarmgmvh ncdkprdill nswegvylni keqemdqmmk dfaamggelf vmddgwfgnk
      361 yrrvqdnssl gdwvvdtqkl phgikgltdi akkygikfgi wiepeftntk seliekhpdw
      421 vlrptnrelm cgrggtqivl dlcnpkvqdf vfnvvdells knpeiayikw dangevmnyg
      481 ssylpkdkqs hiyidyhrgl invlerirak ypdvvmqacg sgggrasygv mpyfnefwvs
      541 dntdalqrlf iqwgtsyfyp siamaqhvsa spnhqtgriv plkfrfdiam tgrlgmeiqp
      601 knmnadekef skkaidtykg irpviqngdq yrlispyekr gvasmmyvae nkeravffaf
      661 kmehyvnqql phvrlvgldk nkkykireln laaddklcyl nnrvfsgdll mnagfaldln
      721 keydswvlel ievk
//
LOCUS       WP_010535800             344 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Bacteroides].
ACCESSION   WP_010535800
VERSION     WP_010535800.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..344
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=39014
     Region          80..322
                     /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"
ORIGIN      
        1 mpdkninidt dvilrylekt aspeeirqlr ewialseena nyfqeirniw evttpavdpe
       61 kidtskalak vknrihttpq apmkrtrlit ycrriaaill lpaiiavval lmkkdhqapl
      121 iafnevtapy gtvstltlpd sskvwlnags tlkyptafts nvrevemsge ayfevhadkk
      181 hpfivstgdl kvtatgtafn vcnfakakee vitlvtgkvn vshennirhl lpgqqlnyqk
      241 asksmevtdi dtyqyiswkd gilafrddpl ktifdrleqv yrvrfilkdp sinqftyrat
      301 fkgetldeil dymgmsipit frttetkqeg ndsvsvrtie vykn
//
LOCUS       WP_010535842             426 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF3575 domain-containing protein [Bacteroides].
ACCESSION   WP_010535842
VERSION     WP_010535842.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10572683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..426
                     /product="DUF3575 domain-containing protein"
                     /calculated_mol_wt=48956
     Region          259..421
                     /region_name="DUF3575"
                     /note="Protein of unknown function (DUF3575); pfam12099"
                     /db_xref="CDD:432330"
ORIGIN      
        1 mkygiyilai fmafsaslks gyamvssftv tqdttrqvvv yfdredttvd lsyknnnqyi
       61 nvldsllgnk eniryitavn vitfvspdgd svyntvlsar rnnsvreflq qrypavdmkk
      121 iqlfsggedw sefrkvveed sdfpereevm mlmdyhrndi gkrkqllrkl nkgmayqyml
      181 rnvlpqlrrs vitivreipe idresfepvs sasglfvseq eealpnhrpd kpvgeskkkq
      241 vyevtiseag gpaknetila vknnllydla lapnieveip mgrrwslnte ykcpwwlnsk
      301 hnfcyqllsg gvegrcwlgd rrkhkrltgh fvglyaeggi ydfqlqsdgy qgkyygaagv
      361 vygyarqlar hfsiefslgi gyltteykky tpyegdiiwa nsgrynfigp tkakvslvwl
      421 itkrrr
//
LOCUS       WP_010535906             735 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GH92 family glycosyl hydrolase [Bacteroides].
ACCESSION   WP_010535906
VERSION     WP_010535906.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..735
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=83201
     Region          1..735
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mkklllsvca fsltlatlqa geitkyvnpf igtgtidggl sgnnypgats pfgmiqlspd
       61 tseapnwgda sgydynrsti fgfshtrlsg tgasdlidvt lmptssgrts stfthdeeka
      121 spgyyqvmlk deninveltt tqrngihryq ypagkdaevi ldmdhsadkg swgrriinaq
      181 irilndhave gyriitgwak lrkiyfymef sspiltstlr dggrvhenta vvngtnlhgc
      241 frfgklngkp ltckvalssv smenarqnme qeaphwdfdr ymaaadadwe kqlgkieikg
      301 tevqkeifyt alyhtmiqpn imsdvngeym aadytarkvg dnethyttfs lwdtfrashp
      361 lytlleperv tdfvksmirq yeyygylpiw qlwgqdnycm ignhsipvit dailkgipgi
      421 dvekayeavy nssvtshpns pfevwekygf mpeniqtqsv sitleqafdd wcvaqlaekl
      481 nkdadyerfh krseyyrnlf hpktkffqsk ndkgewiepf dpyqyggngg hpftegnawq
      541 yfwyvphniq almeltggtk afeqkldtff tsnykseqmn hnasgfvgqy ahgnepshhv
      601 aylynfagqp wktqkyvshi lntlynntss gyagnddcgq msawyvfsam gfypvnpadg
      661 ryiigsplld ectlklagnk dfhirtirks pediyiqsvt lngkkhkdff ithqdimngg
      721 tmvfkmgkkp sgwgk
//
LOCUS       WP_010535939             196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Bacteroides].
ACCESSION   WP_010535939
VERSION     WP_010535939.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..196
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23231
     Region          11..194
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtlfssfkrd etdeqlmerf vfrdnekafe elycryaprf kgffirmlsa dgaladdflq
       61 elflriyear gsyqhgkqfs twafsmaynl ckneyrhrdi vdeyrlqqsy tneedscssp
      121 efeavhdrqv fdrqlkkala gltdeqraay tlryeeelpv qeiaqvlccp egtvksrlyy
      181 tlkvlqrsls dynpqk
//
LOCUS       WP_010535915             667 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Bacteroides].
ACCESSION   WP_010535915
VERSION     WP_010535915.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..667
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=75959
     Region          102..600
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          359..665
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mnrmktkisq iiskgllfaf ivllgscnyl dvdqyfddtl kfdsvftqkr yfeaylwgaa
       61 gqlpdesrif gheyapgita gddiftvmss difrgsafal gyvnpdnlrg mnvwsdmykv
      121 irkanlmlar mdecqdmtal drrnytgyih flrgyayyhi lmtcgpailv gdeifesnld
      181 gpayntyrat ydetveyics eletaaaylp lkasiaqfer ptkgaayali arlrlhaasp
      241 lfngtstarl yfgnwkrtyd kayyinqnys eekwalaaaa ckrvidmnvy elftvskdqn
      301 tpqlpagvpt enfpngaggi dpfksyshmf tgdepfknnn eviwgrisee vkgytqqsfp
      361 qymggyngmg ltqkmidayr medgktieea mavgeykegp ndftsgprdf sdyhlngniw
      421 qmyanremrf yacvgfngcy wpatsttdgs yrlqtvkycm dgnagkyagt vgsdnytptg
      481 yvikkyissy dawrgnsser yekgfpiiry aeillsyaea lnqlttthai tlptgesysl
      541 srdvdemaka fnqvryragl pgltqaqles ptemfeqikr ermveflgeg rrfydvrrwg
      601 iyedvdsepi mglniaanef ggfyqrtvvd eknyrdrvvh rkllflpisk selrkvelld
      661 qnpgynn
//
LOCUS       WP_010535973             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: uroporphyrinogen-III synthase [Bacteroides].
ACCESSION   WP_010535973
VERSION     WP_010535973.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schubert,H.L., Raux,E., Matthews,M.A., Phillips,J.D., Wilson,K.S.,
            Hill,C.P. and Warren,M.J.
  TITLE     Structural diversity in metal ion chelation and the structure of
            uroporphyrinogen III synthase
  JOURNAL   Biochem Soc Trans 30 (4), 595-600 (2002)
   PUBMED   12196144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..248
                     /product="uroporphyrinogen-III synthase"
                     /EC_number="4.2.1.75"
                     /GO_function="GO:0004852 - uroporphyrinogen-III synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006780 - uroporphyrinogen III
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0033014 - tetrapyrrole biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28320
     Region          1..225
                     /region_name="HemD"
                     /note="Uroporphyrinogen-III synthase [Coenzyme transport
                     and metabolism]; COG1587"
                     /db_xref="CDD:441195"
ORIGIN      
        1 mkikkvlvsq pkpasekspy ydiaekygvk idfrpfikve slsakefrqq kvsildhtav
       61 iftsrhaidh ffnlctelrv aipetmkyfc vteavalyiq kyvqyrkrki ffgatgkied
      121 lvpsivkhkt ekylvpmsdv hnddvknlld knhiqhteav myrtvsndft sdeefdydml
      181 vffspagvts lkknfpdfdq keirigtfgs ttaqavrdag lrldleaptv qapsmtaald
      241 mfikennk
//
LOCUS       WP_010535966             551 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Bacteroides].
ACCESSION   WP_010535966
VERSION     WP_010535966.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18797862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..551
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=64206
     Region          39..179
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          112..364
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          112..140
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(113,116..117,120..121,123,151,154..155,158..159,
                     161..162,185,189,193,196..197,200)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          145..179
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          184..216
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          228..256
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          262..288
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 madtqiyylf krvalrfsif igllllflfs ctsqkenqll lhadslmaeh pdsalifles
       61 ipfpqklsra dralyalllt qaryknyitl dddslikvav dyygkkkslr aaqahyywga
      121 ayrdmgnvpf aveeylkaie lmpekddfla miydnlaecy leedlydvam eaykkayqil
      181 hkdkehayyp lrgmahvflv qnqldsalcy fqkaydcvlv tqdssqlpil yndfaivykq
      241 kkeyvraney iskvismlks deldkvyrhk geimfalnqp dsaryyfdwn kdvydiygra
      301 arynglyqve kklgnweaav qnadaymvly dsiqelsdkq qldelmdnhq laeqkqfllh
      361 rgrlimgsli aififlvftg gllflwidrs rkkhyillqq elvqnrvdtm llrenkiaks
      421 eeerintlse lrdqqlqicf smfqstesyk klqgmenakp keliklrafk peinatirkt
      481 fidvmsnlge ccpaltnddl fycilsllgc skaiimelmd assdalksrk srikskmylk
      541 lfdsifisdn q
//
LOCUS       WP_010536040             488 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 125 protein [Bacteroides].
ACCESSION   WP_010536040
VERSION     WP_010536040.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..488
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55553
     Region          43..486
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 mknmrlctit aalligggym nafnlvcskd ntmiispasv aekyksqrpa lkerlfisea
       61 veteivrvkk lltnsklawm fencfpntle ttvhyrtidg kpdtfvytgd ihamwlrdsg
      121 aqvwpyvqla fkdpklkkml egvirrqfkc inidpyanaf ndgakggdwm tdltdmkpel
      181 herkweidsl cypirlayqy wketgdasif dnewiqaiin ilktfkeqqr kegvgpykfq
      241 rkteraldtl nndglgapvn ptglivssfr psddattlqf lvpsnffavt slrkaaeilk
      301 tvnqqtelav qctelaqeve talkqyatyn hpkygtiyaf evdgfgnhll mddanvpsll
      361 ampylgdidv ndpiyqntrr fvwsednpyf fkgkagegig gphigydmiw pmsimmkaft
      421 sqddqeikec ikmlidtdan tgfmhesfhk dnpkkftraw fawqntlfge lilklvnggk
      481 lellnsiq
//
LOCUS       WP_010536127             141 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GtrA family protein [Bacteroides].
ACCESSION   WP_010536127
VERSION     WP_010536127.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..141
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16025
     Region          16..135
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 meiiksvfhs kskryqfiry ctvgslaagi hygvyfvlqe yelvnlniay tigyatsfic
       61 nffmtsyftf rsnpslkkal gfggshlvny lihmglfnlf lsldvnqeia plfvlavavp
      121 vnfvmlrfvf khkkeqvann l
//
LOCUS       WP_010536148             403 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aminotransferase class V-fold PLP-dependent enzyme
            [Bacteroides].
ACCESSION   WP_010536148
VERSION     WP_010536148.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 403)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..403
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=44716
     Region          2..402
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mniekiredf pilsrtvygk plvyfdngat tqkprlvids ivdeyysvna nvhrgvhyls
       61 qqatelheas retvrrfina agtneviftr gttesinllv ssfgdefmqe gdevivsvme
      121 hhsnivpwql laarkgiaik vipmndkgel lldeyeklfs ertkivsvvq vsnvlgtvnp
      181 vkemiataha hgvpfivdaa qsiphmkvdv qdldadflvf sahkiygptg vgvlygkeew
      241 ldrlppyqgg gemiqhvsfe kttfnelpfk feagtpdyig ttglakaldy vngigldria
      301 ahehelttya lkrlkeiphm rifgeaadrg avisflvgdi hhfdlgtlld rlgiavrtgh
      361 hcaqplmqrl giegtvrasf amyntkaevd alvagiervs rmf
//
LOCUS       WP_010536200             281 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FAD:protein FMN transferase [Bacteroides].
ACCESSION   WP_010536200
VERSION     WP_010536200.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..281
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=31008
     Region          25..265
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mqhtiqhiyk thdndgllya wfssmhtrvd iilscqksek elmsavnhiy dtlcqlerta
       61 nyydpssela lvnqaasttp vvisqslfsm ialcieyhkk tigcfditih senynqdtih
      121 sihlspeass iffhqagtai nlsgflkgya ldrikeivnt hrignalisi gnssilalgn
      181 hpsgmgwkvg frnqtnsvqs dkdqsillnn eclttsgnds cerkhiispw sgqplegvrq
      241 vavvtndgtt gevlstslfv anqeqrkvlt aeflpsiiid l
//
LOCUS       WP_010536209             705 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Bacteroides].
ACCESSION   WP_010536209
VERSION     WP_010536209.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 705)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 705)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..705
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=81377
     Region          78..>345
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          352..701
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mikkiymlll tvlgmgaiss csdylnseky fkdrltlekt feskdhveew layafsfikn
       61 enyevttkgp sensfcfsdd myygdrdkti datknelsyn mfklgeyden tynvgawgac
      121 ykgifqasvf ihnvdrcqem adweildykg qarfvrayyy wlllrrygpv pimpdegvdy
      181 tqsydqiatp rssyeevaqy isdemlqatk elqydrrtdn yaigrptrga alavrayali
      241 faaspfangn ndeyaqqlvd degrrllsse yseekwakaa aacrdvidld vyelnivnks
      301 tsdngpserp tvtppadgef skqpwpkgwt nidplrsyrt ifdgtilpan nkeliftrga
      361 tnidmlvlhq mpkddggwnc hgmtqkmlda yymnngsnep gmnsmyqgva nyqgivdtre
      421 rrtgftdlqd lkdnkypelg wkydpkkgdn dqaktgmnvs lqyvereprf yasvayngct
      481 wyylsqtesk padvnqqvwy yfgssdgyrn dgfylrtgig ikkfvhpndy pgnyvakaet
      541 airyadilll yaealneltg tynipswnea ttytisrdke qmergihpvr iraglpdypd
      601 efylqsgvdd mrkalkrerm ielmgegkry fdirrwkdap ieeslqiygc nvfvgeakrd
      661 efhsaipvyn lpstfseklw lwpikhselk rnsrltqnpg wtmyd
//
LOCUS       WP_010536211             390 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Bacteroides].
ACCESSION   WP_010536211
VERSION     WP_010536211.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..390
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=45434
     Region          21..333
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 metlyrayrt llnntstdfv rylhdqiewd srliailgar gigkttmllq hikqydnide
       61 tlfvtaddly fsehrifdla mefyqhggkk lyideihkyy gwsreikniy dlipgiqvvy
      121 tgssildlet geadlsrrkl eyrmtglsfr eylaisrgyr lpvysledil knkvdfpynl
      181 erplqlfkey lqqgyypffk ekgyyirlrs ilnqalendi pifakmnitt aqklkrllyi
      241 iaqsvpfkpn ftklaalldi nrntiselif ylekagiinq lrcdtegirl lgkvdkvyln
      301 ntnlayalsd smpdignire tvffslmrat qpittsscsd fsigkytfei ggkgksqkqi
      361 qniensyivk ddiefgmqni iplwmfgfty
//
LOCUS       WP_010536319             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Bacteroides].
ACCESSION   WP_010536319
VERSION     WP_010536319.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..218
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23618
     Region          1..218
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 miklegitks fgslqvlkgi dleinkgeiv sivgpsgagk ttllqimgtl depdagtvai
       61 dgtvvsrmke kelsafrnkn igfvfqfhql lpeftalenv mipafiagvs skeatdrame
      121 ilafmglter ashkpnelsg gekqrvavar alinhpavil adepsgsldt hnkedlhqlf
      181 fdlrdrlgqt fvivthdegl akitdrtvhm vdgtikkd
//
LOCUS       WP_010536215             685 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Bacteroides].
ACCESSION   WP_010536215
VERSION     WP_010536215.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 685)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 685)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 685)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..685
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=79191
     Region          66..>230
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          342..681
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkkkyillsa ilgiglglss cadqldadry fkdrmslkdv fssrdyteew lanafehltg
       61 snadvsskgh tmycfaddmy fgdrddkykk wkngeydenw eqgpwgscye girqasifil
      121 nidqnmkfte eeradlkaqa rfvrayyywl llrkygpipl lpeegldytk eyeelaiprn
      181 tydecadyia semkiaardl pskrgannva rptrgaalaa rakvllyaas pinnprpgdt
      241 ekftdlvdrn grnliaqeyn eekwakaaaa aldvmklegg tryelyhksa seqvgtgylp
      301 tlppyddgnf vnkswpdgyk didpyesyrs lfngnvnasd npeliftrgq nqsteginvm
      361 vrhqlpraan gwnthgltqk qcdayymkdg kncpgkdsey idypayakri dpnpraegfv
      421 tdenkdqype lgnnrvgvsm qyvgreprfy asvayngstw yllnepndan kdkqifyyrg
      481 ggngytntmf wlrtgigvmk fvhpddtnrd ekeeyirkka epairyaeil liyaealnel
      541 tgnyniaswd eetqytiqrn idemkkgiqp iriragipdy trseyedqdl freklkrerq
      601 ielmgeghry ydirrwkdae veeslpiygc ntlmtekwrd vfhvpvaips lptnfsrkmy
      661 fwpishselk rnkmltqnpg wtynd
//
LOCUS       WP_010536327             513 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TldD/PmbA family protein [Bacteroides].
ACCESSION   WP_010536327
VERSION     WP_010536327.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..513
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55497
     Region          54..511
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mdrrnflktg giallgsltt gsamalatpg alggegadkk atvalamnhf gvseadlkkv
       61 laaalekggd yadlffehti tnsirlmdga vnnsysnidy gvgvrvligd qsgyayveni
      121 tledmlkaar taariasank gnkplnltek vlkknyytva spweevslkd kmpylqklnd
      181 qifaldkrvh kvqasqsdtt shiffcnseg vmfydyrpmv tlgavcimee ngrtengyaa
      241 rayrrgfdfl sdevvdviar eavdqtsllf kaikpkggem pvvmgaggsg illheaight
      301 feadfnrknv sifadqlnkk vcsehinvvd dgtipfnrgs vnfddegaeg qktylikdgv
      361 ltsylhdris akhygveptg ngrresfrnm piprmratym eagnvnesdi issvkkgifv
      421 dnftngqvqi gagdftffvk sgymiedgkl tqpikdinii gngpkaladi tmvatnakid
      481 ngtwtcgkdg qscpvtcgmp salvskltvg gen
//
LOCUS       WP_010536373             130 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Bacteroides].
ACCESSION   WP_010536373
VERSION     WP_010536373.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..130
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14488
     Region          25..130
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mfkmnqlvvg lflflsslfs cqqkgdfktv nvdefdsfiq deevqrldvr tlaeyseghi
       61 artininvmd dsfasmadsl lqkskpvaly crsgkrskka aailsekgyk vielgkgfna
      121 wqaagkeieh
//
LOCUS       WP_010536405             373 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aspartate aminotransferase family protein
            [Bacteroides].
ACCESSION   WP_010536405
VERSION     WP_010536405.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..373
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40915
     Region          3..373
                     /region_name="ArgD"
                     /note="Acetylornithine/succinyldiaminopimelate/putrescine
                     aminotransferase [Amino acid transport and metabolism];
                     COG4992"
                     /db_xref="CDD:444016"
ORIGIN      
        1 mklfdvyply ninivkgqgc kvwdengtey ldlygghavi sighahphyv emisnqvatl
       61 gfysnsvink lqqqvaerlg kisgyedysl flinsgaean enalklasfy ngrtkvvsfs
      121 kafhgrtsla veatnnpsii apinnnghvt ylplndieam kqelakgdvc aviiegiqgv
      181 ggikipttef mqelrnacte tgtilildei qsgygrsgkf fahqynhiqp diitvakgig
      241 ngfpmagvli spmfkpvygq lgttfggnhl acsaalavmd vieqdhlven aakvgnylle
      301 elkkfpqike vrgrglmigl efeepikelr srliydehvf tgasgtnvlr llpplclsme
      361 eadeflarfk rvl
//
LOCUS       WP_010536388             160 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: regulatory protein RecX [Bacteroides].
ACCESSION   WP_010536388
VERSION     WP_010536388.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Ragone,S., Maman,J.D., Furnham,N. and Pellegrini,L.
  TITLE     Structural basis for inhibition of homologous recombination by the
            RecX protein
  JOURNAL   EMBO J 27 (16), 2259-2269 (2008)
   PUBMED   18650935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..160
                     /product="regulatory protein RecX"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /calculated_mol_wt=18775
     Region          6..156
                     /region_name="RecX"
                     /note="SOS response regulatory protein OraA/RecX,
                     interacts with RecA [Posttranslational modification,
                     protein turnover, chaperones]; COG2137"
                     /db_xref="CDD:441740"
ORIGIN      
        1 msaqltdeea lnrvasycsa aehcraevne klqrwgiaye tiarilerle tekyidderf
       61 crafvndkfr fakwgkmkia qglymkkips dvawrhlnei ddeeylsilr dllaskrksi
      121 hakddyelng klmrfamsrg felkdirrci elpeeegqfs
//
LOCUS       WP_010536416             196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Bacteroides].
ACCESSION   WP_010536416
VERSION     WP_010536416.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22602
     Region          5..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtvsktkakl vdvarqlfak mgventtmnd ialaskkgrr tlytyfkskd eiylavvese
       61 ldilsdmmkr vaerdmspdk kmlemiytrl davkevvyrn gtlrayffrd iwrvekvrkk
      121 fdakeiqlfk avllegqakg vfhiddvemt adlihycvkg ievpyirghi gahldeetrn
      181 kyvsnivfga lhrtei
//
LOCUS       WP_010536472            1061 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Bacteroides].
ACCESSION   WP_010536472
VERSION     WP_010536472.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1061
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=116190
     Region          1..1034
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnlkffidrp vlsavisvvi mllgaiglas lpieqypeia pptiqvytqy pganaetvqk
       61 avivpleeai ngveglnyit stasnsgdvt iniyfkqktd pdmaavnvqn rvskalgllp
      121 aevtkigvtt ekqqnaelkt falyapedky drqflnnylk inveprikrv sgvgnvmqlg
      181 snysmriwlk pdkmaqyklv psdisavlan qnieaatgqf genhdnahqy tmkyrgrlsq
      241 pdefenlvvr slpngevlrl kevadielgd eaynynvtln ghpaamsiiy qtsgsnasqt
      301 ineidrvlee lsaglpagme fvtlndtnrf lyasihevve tlliaillvv fvvylflqdl
      361 rstfiptvai fvsiigtfav lqaigfsinl ltlfalvlai gtvvddaivv veavqakfde
      421 gcrssykaai eamgnvasai ltstlifmav fipvsmiggt sgefykqfgl tmaiavgisa
      481 inaftlspal calllrpykd efgreknnfa arfrrrfnkm fetftggylk gvnrfvkrrw
      541 avwsiltvsv malvllmhgt ktglvpqedt gtvlisinlk pgssmeenkk mldkfgkrls
      601 eipaiqyhad vsgysfdgag psmgmvfvsl rpwderksee asaygvlysi yelatefpgm
      661 emfamtppmi pgygmssgfe lylqdklagd vhefkkvada fiaalserpe igqvyssfkt
      721 dypqywvdid aakceqagit sgevlqtlga yysgeyisdf nrfskiyrvm mqgtpdsrit
      781 peslnhvfar ttngkmipls qfvkltktsg psdlsrfnly nslpisgmaa egystgealk
      841 aiketaaeil sanysyelgg lsreeekttg ssaiifaicl vliylilcal yesifvplai
      901 ilsvpcgllg cfifaqafgl enniymqtgi imligllakt aillteyaaq crkggaslke
      961 aavvsakirf rpilmtaltm ifgliplmfs ngagaygnfs lsstavggml igtlallflv
     1021 pplfmvfqni qekvfseksa ynsteeavqt epdklkkgyd l
//
LOCUS       WP_010536479             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Bacteroides].
ACCESSION   WP_010536479
VERSION     WP_010536479.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28743
     Region          1..237
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 midvrglyks fedktvlsdi nasfengktn liigqsgsgk tvlmkcivgl ltpekgevly
       61 dgrnlvlmgk kekkmlrkem gmifqsaalf dsmsvldnvm fplnmfsndt lrdrtkramf
      121 clervnltea kdkfpgeisg gmqkrvaiar aialnpqylf cdepnsgldp ktslviddli
      181 hditqeynmt tiinthdmns vlgigekviy iyeghkeweg tkddiftstn erlnnfifas
      241 dllrkvkdve vqsmeg
//
LOCUS       WP_010536234             487 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 125 protein [Bacteroides].
ACCESSION   WP_010536234
VERSION     WP_010536234.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..487
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55369
     Region          41..485
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 mkkqvkyisa gmlagmllcg gqmqaantms emyvcvtdai qkdnrpevsk rlfrsnavek
       61 eilrvqkllk neklawmftn cfpntidttv hfrkgedgkp dtfvytgdih amwlrdsgaq
      121 vwpyvqlans dpelkemlag vilrqfkcin idpyanafnd gavednhwms dltdmkpelh
      181 erkweidslc yplrlayhyw kttgdasifs eewiqaitnv lktfkeqqrk dgvgpykfqr
      241 kteraldtln ndglgapvkp vglivscfrp sddattlqyl vpsnffavss lrkaaeilek
      301 vnkkttlake ckdlaqevet alkkyavynh pkygkiyafe vdgfgnhflm ddanvpslla
      361 mpylgdvnvn dpiyqntrkf vwsednpyff kgkagegigg phigynmvwp msimmkafts
      421 kddaeiktci kmlmdtdagt gfmhesfhkd dpknftrawf awqntlfgel ilklvnegkv
      481 dllnsik
//
LOCUS       WP_010536512             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fumarylacetoacetate hydrolase family protein
            [Bacteroides].
ACCESSION   WP_010536512
VERSION     WP_010536512.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..204
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22936
     Region          2..195
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkiiavgmny alhnqelght sinkepvifm kpdsailkdg kpffipdfsn evhyetelvv
       61 rinrlgknis prfahryyda ltvgidftar dlqrkfreag npwelckgfd ssaaigtfvp
      121 verykdiqnl nfnlmidgke vqrgctadml fkvddiiayv sqfvtlkigd llftgtpagv
      181 gpvsigqhlq gylegeklld fyir
//
LOCUS       WP_010536526             121 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Bacteroides].
ACCESSION   WP_010536526
VERSION     WP_010536526.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..121
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14224
     Region          1..121
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mekltiqeee vmiyiwelqd cfvkdivsky pqpappyttv asivknlerk gyvkskhign
       61 tyqytpaire neykrhfmsg vvrnyfensy kemvsffakd qkistddlkd iieliekgke
      121 k
//
LOCUS       WP_010536531             484 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Bacteroides].
ACCESSION   WP_010536531
VERSION     WP_010536531.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..484
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53396
     Region          <24..140
                     /region_name="tolC"
                     /note="outer membrane channel protein; Reviewed; cl30340"
                     /db_xref="CDD:357216"
     Region          154..483
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkklflltil lsltfivkaq sflsldscra lalannkdll isnekinaah yqhkaaftny
       61 lpsfsatgty mrnqkefsll nndqkaalsg lgtnlagplq qaagiiaqlh peiasqipal
      121 gasltsafne agsslvdalr tdtrnvyaga itltqplymg gkiraynkit kyaeelaqqq
      181 hqggmqevim stdqaywqvi slvnkkklae gylkllqqld sdvekmiaeg vatkadglsv
      241 rvkvneaemt ltkvedglsl armllcqlcg idlsspitla denmedipll tpethfdmst
      301 ayanrpeirs lelatqiykq kinvtraehl psialmgnym vtnpsvfnsf enkfkgmwnv
      361 gvmvqipiwh wgegiyktka akaeariaqy qlqdarekie lqvnqsafkv keaskklvma
      421 tknmekaden lryatlgfke gviatsnvle aqtawlsaqs ekidaqidvk lteiylkksl
      481 gtlk
//
LOCUS       WP_010536581             779 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Bacteroides faecis].
ACCESSION   WP_010536581
VERSION     WP_010536581.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides faecis
  ORGANISM  Bacteroides faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Bacteroides faecis"
                     /db_xref="taxon:674529"
     Protein         1..779
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=87986
     Region          4..777
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mnkmkkkvlm mtmaaatlsa vaqqpvdyvn piigtngmgh tfpgactpfg wvqlspdtdt
       61 iphningayq knayeycagy qyrdktivgf shthlsgtgh sdlgdillmp avgdlklnpg
      121 radhpeegyr srfshateka tpgyyevmld dygikaqmta tqrvgvhkyt fpkgkdghli
      181 ldlvhgiyny dgkvlwanlr vendtlltgy ritngwartn ytyfaislsq pikdygykdk
      241 qkvlyngfwr rfnmeknfpe itgrkivayf nfdtaedpel vvkvalsavs tegavknlra
      301 evsgksfeql aeaartdwnn eldhfevegt pdqkamfyts lyhtminpsv ymdvdgsyrg
      361 ldhnihqakg ftnytifslw dtyraehpfl nlvkpernad mvesmikheq qsvhgmlpvw
      421 slmgnenwcm sgyhavsvla daitkgvfsn adealaamvs tstvpyyegv adymklgyip
      481 ldksgtaass tleyayddwt iyqtalnagn kelaetyrkr alnyrniydt sigfarprys
      541 dgtfkkefdv lqtygegfie gnswnfsfhv phdvfgmmdl mggektfvqk ldelfsmhlp
      601 ekyyehnedi teeclvggyv hgnepshhvp ylyawtsqpw ktqywlreil nkmyknding
      661 lggnddcgqm sawylfsvmg fypvcpgtdq yvlgapylpy vklklpngkt leikapgvsd
      721 kkryvqslkl ngvsydkmyi thadilkggv lefkmasspn krrglsaedk pysltngin
//
LOCUS       WP_010536583             779 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Bacteroides faecis].
ACCESSION   WP_010536583
VERSION     WP_010536583.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides faecis
  ORGANISM  Bacteroides faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Bacteroides faecis"
                     /db_xref="taxon:674529"
     Protein         1..779
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=88704
     Region          10..765
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mvnkvgrkrl flvwsclvsi lpgmaqtekl tdyvnpfvgt dgygnvypga qipfggiqms
       61 pdtdsrfyda asgykynhlt lmgfslthls gtgipdlgdf lfipgtgemk lepgthedpd
      121 kgyrsryshd kewaspnyya veladygvka emtsgvrsgm frftypesds afimidmnht
      181 lwqscewsnl rmindstitg yklvkgwgpe rhvyltatfs kkltglrfmq dkkpviynts
      241 rfrssyeawg knlmaclsfd tkageevivk tavsavstdg arnnmkeldg ltfnelkakg
      301 ealwekelgk ytltadrktk etfytsayha alhpfifqds dgqfrgldkn iekaegftny
      361 tvfslwdtyr alhpwfnlvq qevnadians mlahydksve kmlpvwsfyg netwcmigyh
      421 avsvladmiv kevkgfdyer ayeamkttam npnydclpey ramgyvpfdk eaesvsktle
      481 yayddyciaq aarklgkedd yhyflnrals yqtlidpetk ymrgrdskgd wrtpftpvay
      541 qgpgsvhgwg ditegftmqy twyvpqdvqg yineagkelf rkrldelftv elpddipgah
      601 diqgrigayw hgnepchhva ylynylkepw kcqkwirtiv drfygntpda lsgnddcgqm
      661 sawymfncig fypiapssni ynigspcaea itvrmsngkn iemtadhwsp enlyvkelyv
      721 ngkkydksyl tyddirdgvk lrfvmsskpn ykravsdeav apsisspgkt vkyshvigq
//
LOCUS       WP_010536577             654 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Bacteroides].
ACCESSION   WP_010536577
VERSION     WP_010536577.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 654)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 654)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..654
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=74789
     Region          48..>233
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          316..651
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mknifkigtl alclavglss cndffdaipg eqydledtft nrskteqfln nvynyvpdet
       61 lersarntms giwttgslec klswdgnngs ewasgatyag sswinfwyie yykgisrast
      121 fimnvdrcle asaaqrkqwk aqaralrafy yfmifrsygp fvilgeepip ldistaellk
      181 erntvdecvd fmakefddaa nelpdrydgs nlgridraac kafkakmlly aasplfncnp
      241 dyaaivnpes gkqlfpqdks qekakweaar daykeffdey gntfslytek tadgkidfye
      301 syrkvtsgvl ygtenkeqif irladhdyra yettpyhkgy ddnngalrgg lgfgvpqemv
      361 dlyfmkdgrr ivddtnykey egvpsneylg wssdytdevv psrtyfksnl nqtlkqwanr
      421 eprfytnitf hgstwlktdt prgeittelt yngnsgyana nwdapytgyg mrkmaskegr
      481 sganrhcatl lrladmylgy aetlsacdqr neaikyvnki raragipgyg avgttddngf
      541 acipyedtrd gvdkrihrer lvelmfewnh ffdvrrwkva dmavgddwiy pkyhrggegg
      601 pihgmafrsd apaffekvvv etrtflpkhy lfpipdedvr rnpkmvqnlg wtte
//
LOCUS       WP_010536599             177 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RsmD family RNA methyltransferase [Bacteroides].
ACCESSION   WP_010536599
VERSION     WP_010536599.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002368
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..177
                     /product="RsmD family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0031167 - rRNA methylation [Evidence IEA]"
                     /calculated_mol_wt=20342
     Region          1..177
                     /region_name="RsmD"
                     /note="16S rRNA G966 N2-methylase RsmD [Translation,
                     ribosomal structure and biogenesis]; COG0742"
                     /db_xref="CDD:440505"
ORIGIN      
        1 mrvisgiykr rrfdvprtfk arpttdfake nlfnvlnnyi dfeegvtald lfagtgsisi
       61 elvsrgcdrv isvekdpahh sfickimkev qtdkclpirg dvfkfinsgr eqfdfifadp
      121 pyalkelesi pelifknnll kegglfvleh gkqnnfeenp hfierrvygs vnfslfr
//
LOCUS       WP_010536487             586 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase family protein [Bacteroides faecis].
ACCESSION   WP_010536487
VERSION     WP_010536487.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides faecis
  ORGANISM  Bacteroides faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Putnam,A.A. and Jankowsky,E.
  TITLE     DEAD-box helicases as integrators of RNA, nucleotide and protein
            binding
  JOURNAL   Biochim Biophys Acta 1829 (8), 884-893 (2013)
   PUBMED   23416748
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12212200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Bacteroides faecis"
                     /db_xref="taxon:674529"
     Protein         1..586
                     /product="DEAD/DEAH box helicase family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68013
     Region          <50..194
                     /region_name="DEXDc"
                     /note="DEAD-like helicases superfamily; smart00487"
                     /db_xref="CDD:214692"
ORIGIN      
        1 mkqeiinggn arylgelerf kdgipfgivn ktktdvggty vaancssnyi ivcpfkdlvd
       61 siaadknnry evfkcyggvr eyqfrkyikn nttykiavty dslpkligwl sgtegwkvlv
      121 deyhliledm dfrydaingl meeiqkfrhy sflsatpidl dfeidflkql phykvqwngv
      181 tkitpirykv tqltkglarf iqifldegis lpdingnvsk veelyifins vtsikqiadt
      241 lklnpddvki ccadrirnnk llgeyqiesv sshnkkinff tkkcfqgcnl ftnngliiva
      301 sdayrtqtlv disttmeqia gririndeyq nifrnvivhl fstnknvmsd eefemlmqdk
      361 ekeadkllsg wskldkeerq tyikrmnldt elvsiingkm vynnlkkqsf iykqalrkty
      421 kdgisirdsf mqsekfeltn qnkwkdfnik lakamtvsye qllkdyldsp sesyeqeype
      481 fplikrylke semntlrwnr ekmlkavedk kqvdkvflai yqpgfisnkd lksklkdefg
      541 rlgiklspka tlienctlyn vekasrkidg ktvsgyelgk miftfe
//
LOCUS       WP_010536644             443 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [Bacteroides].
ACCESSION   WP_010536644
VERSION     WP_010536644.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..443
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49959
     Region          105..425
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mkevidtvsv alangetenv gnavmqevnr tlvsagvdev wadkidnliv llfiigiall
       61 anlicrkiil rvvaklvkqt katwddivfn hkvmvnvsrm vapiliyiai piafpehads
      121 dlldflrrlc liyiiavflr fisalftavy qvysereqyr dkplkgllqt aqvilffiga
      181 iiiisilinq spmvlltglg asaailmlvf kdsimgfvsg iqlsannmlk vgdwitmpky
      241 gadgtvievt lntvkvrnfd ntittippyl lisdsfqnwq gmqesggrrv krsinidmts
      301 vrfctpemle kyrkiqlltd yveetervve eynkehdidn svlvngrrqt nlgvfraylt
      361 nylrslptvn qemtcmvrql qptetgiple lyffsankvw vayegiqadv fdhvlaiipe
      421 fglrvfqnps gedlrrigvk ieh
//
LOCUS       WP_010536645             298 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Bacteroides].
ACCESSION   WP_010536645
VERSION     WP_010536645.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 298)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..298
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34698
     Region          21..102
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <137..295
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mntpipnqii reitplsdkd cfyiaerykt eftypihnhs efelnfteka agvrrvvgds
       61 sevigdydlv litgkdlehv weqnecrske ireitiqfss dlffksfink nqfdsirrml
      121 dkaqkglcfp msailkiypm ldtlasekqg fyavikfmti lyelslfeee artlssssfa
      181 kidvhsdsrr vqkvqeyinl hyqeeirlgq lagmvgmtdv sfsrffklrt gknlsdyiid
      241 irlgfasrll vdstmsiaei cyecgfnnls nfnrifkkkk dcspkefren yrkkkkli
//
LOCUS       WP_010536685             460 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SGNH/GDSL hydrolase family protein [Bacteroides].
ACCESSION   WP_010536685
VERSION     WP_010536685.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..460
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=52947
     Region          29..233
                     /region_name="SGNH_hydrolase_like_2"
                     /note="SGNH_hydrolase subfamily. SGNH hydrolases are a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site...; cd01834"
                     /db_xref="CDD:238872"
     Site            order(38,71,100,214,217)
                     /site_type="active"
                     /db_xref="CDD:238872"
     Site            order(38,214,217)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238872"
     Site            order(38,71,100)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238872"
ORIGIN      
        1 mkkflvlvaa vcmayttafa qtvkpfkegd ravflgnsit dggryhsfiw lyymtrfpnm
       61 pirifnggig gdtaydmnkr ldgdifsknp tvlmvtfgmn dsgyyeyngd nakefgeqky
      121 qesiknfqqm ekrfkelpht rivmtgtspy detaqikdnt vfkkknetik riieyqresa
      181 arngweftdw napmvainqe lqqkdpsftl cgndrihpdn dghmvmaylf lkaqgfagkd
      241 vanmeinank kqavkaegct isnikkigkd isfdylaeal pypldtiarg wgskksqaev
      301 ikevpfmeem ntellkvtgl kgqykllidn qeigtwdaad lakginlaae sktpqyqqal
      361 aimhlneyrw elertfreya wcqfgffqqk gllfangrka ievmdenvek nmwlkgrrdl
      421 yskmmfkeir dareqemdvl vskiyeinkp vvrkivlrki
//
LOCUS       WP_010536713             525 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 28 protein [Bacteroides].
ACCESSION   WP_010536713
VERSION     WP_010536713.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Abbott,D.W. and Boraston,A.B.
  TITLE     The structural basis for exopolygalacturonase activity in a family
            28 glycoside hydrolase
  JOURNAL   J Mol Biol 368 (5), 1215-1222 (2007)
   PUBMED   17397864
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..525
                     /product="glycoside hydrolase family 28 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57436
     Region          50..477
                     /region_name="Pgu1"
                     /note="Polygalacturonase [Carbohydrate transport and
                     metabolism]; COG5434"
                     /db_xref="CDD:444185"
ORIGIN      
        1 mntllkkdlr vmmtgilmfi sclaysnpgn gtkekedvyk nlpfsmpevs kpsfpdyevn
       61 irdfgalsdg vtlnteainn aiktvsskgg gkviipeglw ltgpvvllsn vnlyteknal
      121 ivfssdtsly piieasfegl dtkrcqspis amnaeniait gsgvfdgagd rwrpvkkdkm
      181 terqwknlvs sggkvdengk vwypdagalk asvlmtgqns gqkeitdeew iymkswlrpv
      241 mlsivkskri llegvtfkns pgwcihplsc esltlndvkv fnpwysqngd aldvescknv
      301 lvtncffdag ddaiclksgk dedgrrrgep cenviiknnt vlhghggfvi gsemsggvrn
      361 vyvsgcsfvg tdvglrfkst rgrggvveni fidninmidi pndaltmdly yavndspetp
      421 ipdvneetpv frniyisnvl crgagravyf nglpemplkn iliknmtvtn akkgivinqa
      481 sqvnmenikv edseipaiqi enatgviing keykkdsgkm llsgn
//
LOCUS       WP_010536737             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide deacetylase family protein
            [Bacteroides].
ACCESSION   WP_010536737
VERSION     WP_010536737.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..322
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37184
     Region          35..>145
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(43..44,104,108,144..145)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mkkfslfils llfctgymsg adwnvyvary kqdkacaisy tfddglaehy tlvapqlekr
       61 gfrgtfwicg sninkdnrni tdttrmtwpq lkemsdkghe isnhgwahkn farfpieeik
      121 edilkndsai fantgvmprt fcypnnnkka egrriavqnr vgtrthqrsi gskstlqdle
      181 kwmntlietn dwgvgmthgl tygydafrnp qrlwdhwdqv kareneiwvg tfrevasyir
      241 ereetkldvv nkkntllitp elkldqklfv epltmvitgk dikkvtvkqg krklpvqvtg
      301 dkvlfdfdpy gdvikvtlks rk
//
LOCUS       WP_010536762             528 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Bacteroides].
ACCESSION   WP_010536762
VERSION     WP_010536762.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..528
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=60176
     Region          40..465
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          270..523
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkklliyivi agttlltssc ndwldvlpkn eqvspeywkt keqveevlaq gyhnmrltvp
       61 tliywgelrg asiyaysgks kqelqnfqlt sssneckwas fysilnvans iikyapevkr
      121 qdetyhesvm nsnmaeayfm rawtyftlvr nfkevplive pymtdeyavd vpksseeaii
      181 aqikldieda lstgaakemy ddedwtgmsk grvtvwalya lmadvclwse dydgcvryad
      241 mlinstspfr pafvedpeqw ysiffpgnsn gsifelnfdq srnqspddda tastypspsn
      301 iyswtqstva alqfsnamck rlfdeqtdtw vtsntvrgyg ntfilssgtv ignsntegyl
      361 pfkfriggkd glsttrsykd anwilyrmad vllmkaeali wkggeanfaq alelinkirt
      421 ranvttlsvq tnavsqenml gyllqerdle faaegkrwyd llrfgrsqnf kykdqfinmi
      481 iennstvsas wirsvlkntd awylpinqge idtnpmliqn pyydvtan
//
LOCUS       WP_010536820             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Bacteroides].
ACCESSION   WP_010536820
VERSION     WP_010536820.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..193
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21331
     Region          18..193
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mkksiiiila vvailviwav svynglvtmd envtgqwanv etqyqrradl ipnlvntvkg
       61 yasheketle gvvearskat qikvdadglt peklaeyqka qgavtsalgk llaisesypd
      121 lkanqnflel qaqlegtenr invarknfnd aaqsyntnir rfpknifagm fgfdkkayfe
      181 aeegtekapk vef
//
LOCUS       WP_010536862             582 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S41 family peptidase [Bacteroides].
ACCESSION   WP_010536862
VERSION     WP_010536862.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..582
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=64777
     Region          45..358
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mstrnssrft piiiaisvva giligtfyak hfagnrlgii ngssnklnal lrivddqyvd
       61 tvnmtdlvek ampqilaeld phstyipaqn leevnseleg sfsgigiqft iqndtihvna
      121 viqggpsekv glmagdrivn vddslfvgkk lnnelamrtl kgpkgsqvkl gvkrvgepkl
      181 ldftitrgdi pqntvdaaym lnddigyvkv skfgrtshve llnalaqlnh kkckgliidl
      241 rgntggymea airmvneflp egklivytqg rkyprseefa ngtgscqkmp lvvlidegsa
      301 saseiftgai qdndrgtvvg rrsfgkglvq qpidfsdgsa irltiaryyt psgrciqrpy
      361 esgkdrnyel dlynryehge ffsrdsikqn eneryltslg rtvyggggim pdvfvpqdtt
      421 gvtsylssvi nrgltlqftf qytdnnrkkl sqyeteeell nylrhqglve qfirfadtkg
      481 vkrrniliqk sykrleaniy gniiynmlgl eaylkyfnks datvqqgiel lekgeafpka
      541 pveteeevtk ekkdgkkkrt aqaygitedp trifdfaeaa is
//
LOCUS       WP_010536881             277 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Bacteroides faecis].
ACCESSION   WP_010536881
VERSION     WP_010536881.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides faecis
  ORGANISM  Bacteroides faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Bacteroides faecis"
                     /db_xref="taxon:674529"
     Protein         1..277
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32504
     Region          1..193
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mpeitvlmpv rngekyikna idsvlnqtlt dfefliiddg stdrtvkiiq dyaderihlv
       61 krkhqfiqnl neglqlasga yiarmdaddi mhterlriql krmkknpdit vcgtwakifs
      121 dkgnerkish lgygiihepv lellkynmll hpsvmikkef llnhhikyqn ypcvedyklw
      181 fdiaksggil fvepqellmf rrsdtqvtvt kkeemslgsi rlrkeillyl lsvynnktln
      241 sllsdfenle knkwmsnedi frffvnlfnr iqrdtmv
//
LOCUS       WP_010536896             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Bacteroides].
ACCESSION   WP_010536896
VERSION     WP_010536896.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..220
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25216
     Region          14..219
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 metmfdtllq lplfqglche dftsildkvk lhfikhkage tiiksgnpct qlcfllkgel
       61 sivtnakdni ytviekteap yliepqslfg mntnyassyv ahtevhtvci skafvlsdlf
      121 kydifrlnym nivsnraqnl ysrlwdeptl dlkgkiirff llhcekpqge kvfkvkmddl
      181 arclddtrln isktlnelqd sglielhrke ilipdaqkll
//
LOCUS       WP_010536913             170 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Bacteroides].
ACCESSION   WP_010536913
VERSION     WP_010536913.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..170
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=19232
     Region          <59..169
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkvkfklili ltglifilss crtsaprldy qalarasill gvdinmednh klylesaewi
       61 gvpyrgggds krgtdcsglt yqiyrkvyrm qvprnsedlr kestkvakrn lregdlvffs
      121 ssrskkkvah vgiylkngkf ihastskgvi vsrlsedyyt rhwisggrir
//
LOCUS       WP_010536942             183 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Bacteroides].
ACCESSION   WP_010536942
VERSION     WP_010536942.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..183
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21520
     Region          5..181
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtpynerevl kllqeestqr kgfelivaqy seqlywqirr mvlshedand llqntfikaw
       61 tnidyfraea klstwlyria lnecltflnr qrattmvaid dpeavvvqkl esdpyysgdq
      121 vqmllqkall tlpekqrmvf nlkyyqemky edmseifgts vgalkasyhh avkkiekfle
      181 evd
//
LOCUS       WP_010537016             600 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YncE family protein [Bacteroides].
ACCESSION   WP_010537016
VERSION     WP_010537016.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..600
                     /product="YncE family protein"
                     /calculated_mol_wt=66206
     Region          4..171
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <110..293
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <244..>369
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          395..580
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mkkilipvsi iavllctaak dadqtvispd rlfladngks lfvtnragse likmsadgke
       61 meqkvefssp vnamtqdpdg nlwvvcdgny gmmyqldgkk lsiqsktksg atpsdilynp
      121 lsqslwvaqr fnnelweidp atrkvkakit vgrepvamas fagdscllia nnmpempsta
      181 yplaaqldiv dvsskkvasr imlpngstdv ksiavdknra yayvthliar yqlptnqldr
      241 gwmatntlsi idlkarkllt svlldtpqkg aanpwsvivt pddkqiivaa agsqelvrid
      301 rialherlak akqgvmvtps vkswnnipnd agflygirdf iptqgkgprs vvatgnkiyt
      361 anyytselvs mdmngknlnk qvlgaplaft kvgkgdmyfh daticfqnwq scatchpnda
      421 rmdglnwdll ndgmgnpknt ktlllshqtp pcmatgirkn aevavrsgvk yilfmegnde
      481 iyesideylk slkplpspyl vngklsgkak kgkkifeenc aschsgeyyt dqkqykvdwt
      541 tgpdkglsmd vpalnecwrt apylydgrsy smkdmlkihg phkpvtekel eeleeyvlsl
//
LOCUS       WP_010537027             461 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: lactate utilization protein B [Bacteroides].
ACCESSION   WP_010537027
VERSION     WP_010537027.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..461
                     /product="lactate utilization protein B"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51784
     Region          1..449
                     /region_name="LutB"
                     /note="L-lactate utilization protein LutB, contains a
                     ferredoxin-type domain [Energy production and conversion];
                     COG1139"
                     /db_xref="CDD:440754"
ORIGIN      
        1 mstkhskaae kflqdskmaa whnetlwmvr akrdkmskev peweelrnka celklysssh
       61 leelllefek natangaivh wakdadeyca ivyeilnehn vhhfiksksm laeecglnpf
      121 lmergidvve sdlgerilql mhlepshivl paihikreqv gelfekemgt ekgnfdptyl
      181 thaarknlrh lflnaeaamt ganfavastg divvctnegn admgtsypkl niaafgmeki
      241 vpdlealgvf trllarsatg qpvttytshy rrpreggeyh iiivdngrst llskpghikt
      301 lncircgacm ntcpvyrrsg gysytyfipg piginlgmah dpekyydnls acslcmscsd
      361 vcpvkvdlae qiyrwrqdld algkantgkk imsggmkflm erpalfnaal waapivnglp
      421 rfmkyndldd wgkgrelpef agesfnemwk knkvqgkees k
//
LOCUS       WP_010536721             261 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Cof-type HAD-IIB family hydrolase [Bacteroides].
ACCESSION   WP_010536721
VERSION     WP_010536721.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Lu,Z., Dunaway-Mariano,D. and Allen,K.N.
  TITLE     The catalytic scaffold of the haloalkanoic acid dehalogenase enzyme
            superfamily acts as a mold for the trigonal bipyramidal transition
            state
  JOURNAL   Proc Natl Acad Sci U S A 105 (15), 5687-5692 (2008)
   PUBMED   18398008
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..261
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28807
     Region          3..259
                     /region_name="HAD_HPP"
                     /note="phosphatase, similar to Bacteroides
                     thetaiotaomicron VPI-5482 BT4131 hexose phosphate
                     phosphatase; belongs to the haloacid dehalogenase-like
                     superfamily; cd07517"
                     /db_xref="CDD:319819"
     Site            order(8..12,43..45,188,210..211,214..215)
                     /site_type="active"
                     /db_xref="CDD:319819"
ORIGIN      
        1 mtkalffdid gtlvsfethr ipsstieale aahakglkif iatgrpkaii nnlselqdrn
       61 lidgyitmng aycfvgeevi yksaipqeev kamaafcekk gvpcifveeh nisvcqpnem
      121 vkkifydflh vnviptvsfe easnkeviqm tpfiteeeek evlpsiptce igrwypafad
      181 vtakgdtkqk gideiiryfg irleetmsfg dggndismlr haaigvamgq akedvkaaad
      241 yvtvpidedg iskamkhfgi i
//
LOCUS       WP_010537032             170 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Bacteroides].
ACCESSION   WP_010537032
VERSION     WP_010537032.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..170
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20127
     Region          1..168
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mksgdseyfg elynryiplt yglclkylqd edraqeavmq mfedllpkis nyeikvfrpw
       61 lyrvaknhcl qllrkenkei pldytinime sdeflhllse eessedqlka lhhcleklpe
      121 eqrtsitrff leemsyadiv eqtgftlnnv ksyiqngkrn lkicikkqtl
//
LOCUS       WP_010537038             437 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleobase:cation symporter-2 family protein
            [Bacteroides].
ACCESSION   WP_010537038
VERSION     WP_010537038.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..437
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45894
     Region          22..432
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mktdliygve drppfkdalf aalqhllaif vaiitpplii agalkldvek tsflvsmslf
       61 asgvstfiqc rrigpigarl lciqgtsfsf igpiiatglv gglplifgsc iaaapiemvv
      121 srtfkylrni itplvsgivv lliglslikv givscgggys amddgsfgsw enlsiaalvl
      181 lsvlffnrck nkylrmssiv fglclgygla falgkvnmsa lnvemlmsfn ipqpfkygvd
      241 fnissfiaig lvylitaiea tgdvtansmi sglpiegdsy lkrvsggvma dgfnsllagv
      301 fnsfpnsifa qnngiiqltg vasryvgyyi agmlvllglf pivgavfslm pdpvlggatl
      361 lmfgtvaaag irivssqeig rketlvlavs lslglgvelm pdvlkqapea irsifssgit
      421 tggltaiian ivirvkn
//
LOCUS       WP_010537052             364 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Bacteroides].
ACCESSION   WP_010537052
VERSION     WP_010537052.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..364
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40080
     Region          <160..346
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 mkirnlllls lltvsstmaf aqeqrikeeg ktvfkphwsm qvqagaahtv geadftdlis
       61 paaavnvgyk fapafgarlg vsgwqakagw vtpsqtyqyk ylqgnldlma dlstlfcgfn
      121 pkrvfngyif ggvglnhafd ndeanaldtr sheleylwqd kqnlvagrfg lgcdlrlndr
      181 lainiegnan alsdkfnskk agncdwqfnv lvglniklgk sykktapvyy epepvveqpk
      241 pqpvvekpqp kpepavvvep mkqniffaln sakiqndqls kidamvayme kypnskvait
      301 gyadketgnp rinlalsekr aknvadalka kgiaasrivt dfkgdtvqpy rvpeenrvsi
      361 ciae
//
LOCUS       WP_010537065              90 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Bacteroides].
ACCESSION   WP_010537065
VERSION     WP_010537065.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 90)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 90)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..90
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10094
     Region          3..85
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mdyeithqpe qklfktevdg rtafveyrll gdyldiihti vpkpiegrgi aaalvkaayd
       61 falangmkpk atcsyavrwl erhpemnadn
//
LOCUS       WP_010537258             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: saccharopine dehydrogenase family protein
            [Bacteroides].
ACCESSION   WP_010537258
VERSION     WP_010537258.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..397
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44954
     Region          <3..>39
                     /region_name="hemA"
                     /note="glutamyl-tRNA reductase; Reviewed; PRK00045"
                     /db_xref="CDD:234592"
     Region          29..389
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mgrvliigag gvgtvvahkv aqnadvftdi miasrtkekc dnivkaignp niktakvdad
       61 nvdelvalfn dfkpemvinv alpyqdltim eaclkagvny ldtanyepkd eahfeyswqw
      121 ayhdrfkeag ltailgcgfd pgvsgiytay aakhyfdeiq yldivdcnag nhhkafatnf
      181 npeinireit qngryyengq wvttgpleih kdltypnigp rdsyllyhee leslvkhfpt
      241 ikrarfwmtf gqeylthlrv iqnigmarid evdyngtkiv plqflkavlp npqdlgenye
      301 getsigcrir gikdgkerty yvynncshqe ayketgmqgv syttgvpami gammffkgew
      361 krpgvnnvee fnpdpfmeql nkqglpwhev fdkdlel
//
LOCUS       WP_010537317             609 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TrkH family potassium uptake protein [Bacteroides].
ACCESSION   WP_010537317
VERSION     WP_010537317.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..609
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=67416
     Region          155..603
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mkiyhkflly qnkllkpyir iilglvealt ylaslllivg vvyehgfpls pgeveqiqvl
       61 ykavwiifli dvtlhisley rntkkqyrrl awilsgllyl tlvpvifhrp eeegailqvw
      121 eflhgkfyhl vlllifslln lsnglvrllg rrtnpslila vsflaiilig tgllmlprct
      181 vngitwvdsl ftatsavcvt glvpvdvstt fttsglvvii lliqigglgv mtltsffamf
      241 fmgntsiynq lvvrdmvssn slgsllstll yilgftlvie gigmisiwfs ihgtlgmnle
      301 eelafaafhs isafcnagfs tlsgnlgnpm vmtnhnwlfi svslliifgg igfpilvnfk
      361 divlyhlrrf wkfvrtrkle rhkvqhlynl ntkivlimtf lllltgtlav aafewnasfa
      421 gmpvadkwtq affnatcprt agfssvdlas lsvqtllvyl flmwvgggsq staggvkvna
      481 favvvlnlva vlrgservev fgrelshdsi rrsnatvvms lgvlflfifi lsilepeasl
      541 laltfecvsa lstvgsslnl tpqlcdaskl lvsllmfigr vglitlmlgi vkqkkntkyr
      601 ypsdniiin
//
LOCUS       WP_010537341             278 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Bacteroides].
ACCESSION   WP_010537341
VERSION     WP_010537341.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..278
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32094
     Region          1..>86
                     /region_name="DUF1425"
                     /note="Putative periplasmic lipoprotein; cl12345"
                     /db_xref="CDD:472303"
     Region          200..277
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mkainlclfc llligcankp kqekvpqtli nntvgindtl glslhpefpi ystkqkqvtf
       61 ilhnnsgtdi gfggyysyty edekgiwrdv pmqlvvfdee iilwqgnkyy ynaelfrhtp
      121 gryrffltvr ryskeytlmt efqlqdnmie lfkrhpysql ndtllpseee avyppiynvi
      181 dqmpefpggi dkllqfindn mkyptkaqte giqgrvavqf ivdengyiie pnivrsveps
      241 ldnealrlik mlpqwkpgtl kgkavkvkyt vpvafklk
//
LOCUS       WP_010537378            1035 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Bacteroides].
ACCESSION   WP_010537378
VERSION     WP_010537378.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1035
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114781
     Region          10..1028
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mkkelmlsii qkrwvmlclf vvmcifgyys wkqlsieayp diadvtsqvv tqvpglaaee
       61 veqqitiple rainglpgmh vmrskstfgl smitivfkdg tedywsrqrv qerlnevelp
      121 ygatpgldpl tspvgevyry ivesdqhslr eltdlqnwvi iprikevsgv advtnfggit
      181 tqfqveidps kleqynlslk qvieaiennn anvggsvlnr gdlgyvvrgi glignlddlg
      241 hivvsttsgv pvflndigsl kygnlerkgv lgytdrtrdy seslegivll lkhenpskvl
      301 eavhtavdel nnetlpegvk ihtfldrtdl vdttlstvsh tllmgmglvv lvlilflgnw
      361 rgallvsiti pvslliafil mhltdipanl lslgaidfgi ivdgaivmle tilkkrednp
      421 eqyleeksia qrakevgrpi lfstiviita ylplfaferv erklftpmaf tmsyamvgal
      481 lvalllipgl ayaiyrkprk iyknkwldkl kdeytcivtg iletpskvim ssslvlvggi
      541 vlsavvgkdf lpeldegsiw lqvnlppgis veksrelsdt lrartmkyse vtymmvqagr
      601 nddgtdpftp shfevsigik pygewpkgkt kkdlinelee eykslsgfkv gfsqpmidgv
      661 mdkiagahse lvvkvygedf retrriaeei trvlgtvkga vdldidqepp lpqlqismnr
      721 daiaryglnv sdvadlieva iggkaiaqly qddrqyditc kykeearntp ekiaglmlts
      781 stgakiplsq vadvrlslge stitremnrr hltvklnlrg rdlasflnea qatinenvhy
      841 dknkytvkwg gafenqkray trlsviiplt lvgmfillya tfgkfrqagl vlsivplalf
      901 ggmlalnvrg mtlnvssavg fiamfglsiq ngiimvsqin glrikgmelr ksviegalqr
      961 frpilmtsvt tilglfpasl atgigsdvqr platvivygl mfstlvsmfl lpafyylven
     1021 nvlnkkknde keytl
//
LOCUS       WP_010537400             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hydrogen peroxide-inducible genes activator
            [Bacteroides].
ACCESSION   WP_010537400
VERSION     WP_010537400.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Jo,I., Chung,I.Y., Bae,H.W., Kim,J.S., Song,S., Cho,Y.H. and
            Ha,N.C.
  TITLE     Structural details of the OxyR peroxide-sensing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 112 (20), 6443-6448 (2015)
   PUBMED   25931525
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..308
                     /product="hydrogen peroxide-inducible genes activator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35319
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..290
                     /region_name="PBP2_OxyR"
                     /note="The C-terminal substrate-binding domain of the
                     LysR-type transcriptional regulator OxyR, a member of the
                     type 2 periplasmic binding fold protein superfamily;
                     cd08411"
                     /db_xref="CDD:176103"
     Site            order(103,106..107,110,114,122..126,220,223..224,227,
                     230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176103"
ORIGIN      
        1 mtiqqleyil avdqfrhfar aaeycrvtqp tlsamiqkle eelgvklfdr tvqpvcptai
       61 gekiidqarv ilaqtaqvke iiseekqsla gvfrlgvlpt iapyllprff pqlmekhpel
      121 dirvtemktq diqqalhage ldaaiiaskl edtflkeetl fyetffgyvs ckeplfkhem
      181 irtsditger lwlldeghcf rdqlvrfcqm etvkvnqmay hlgsmetfmr mvesgkgitf
      241 ipelavsqlt eeqkklvrpf aiprptrqiv latsrdfirh sllnvlkeei laaipkemqs
      301 lqsiqyll
//
LOCUS       WP_010537451             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [Bacteroides].
ACCESSION   WP_010537451
VERSION     WP_010537451.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..429
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48509
     Region          13..429
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mefliilfll vlngifamye ialvssskar letlagkgnk sargvlkqle epekflstiq
       61 igitligivs gayggvaiad dlvpffslip gaeayarnla mittvviity lsliigelvp
      121 ksialsnper yatlfspimi lltkvsypfv wllsistrll nriigvknee rpmtqeeikm
      181 ilhqsseqgv idkeetemlr dvfrfsdkra nelmthrrdl vifhpddtkd kvmktieeeh
      241 yskyllvder kdeiigvvsv kdiilmvgnk kefnlreiar pplfipesly ankilelfkk
      301 nknkfgvvvn eygstegiit lhdltesifg dileedemee edivrrqdgs mlveasmnik
      361 dfmeemgils yedlededft tlgglamfll ggipkagdif tyknlqfevv dmdrgrvdkl
      421 lvikrdeea
//
LOCUS       WP_010537478             328 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Bacteroides].
ACCESSION   WP_010537478
VERSION     WP_010537478.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..328
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=37850
     Region          106..326
                     /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"
ORIGIN      
        1 mmkdtktekn klrrylddmy ireeasqlle smrdadhkdi ldelsaevwe esvsqqpvtd
       61 lerekykkea rqllkhiehk krtwfrrvmt iaasvaavia ivtgsisyfr ymseqqitfa
      121 eistsfgekk rvelpdgtil vlnscsqvry pdsfqgdirk velegegyfr vahnedmpfi
      181 vqtkrldvrv lgtrfdvksy stdeivsvsv esgkvqvdlp eammrltake qvlintvsse
      241 yskkkeergv avwikgslrf nstpirdvak elervyncqi tfasgqefdn litgehdnks
      301 lesvlksief isdinykkeg rnillykk
//
LOCUS       WP_010537444             571 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Bacteroides].
ACCESSION   WP_010537444
VERSION     WP_010537444.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..571
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=65024
     Region          21..205
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          274..569
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkytlkaili lilgclthsc ldldpkaqia dgnywnsvtd yklfanqfys wtrdfsnsvy
       61 daphsdkrsd livdkggtnv ysngtnsipa sdnnytdnyn rirranillq kaetydnptd
      121 iaqyvgeakf fraycyfell qlygdaiitk tpldvtdpel kasrndrsev adliiqdlkd
      181 aagllsatsa vesgrvgseg awaflsrval yegtwqkfrg ntvrgkelld iaanaakevi
      241 nskkfslyap vilgdsaqky mfiledvksn paglqkssnt eyifsrrhde tlnpinknit
      301 keclanaqmi shkfaalylc qdglpidksp nmfmgydkie seylnrdnrm iytlckpygy
      361 fwsnensrvn wtgdaadras asikglipts gsgynnqkwa teravntnye gydypiirya
      421 evllnyaeav ferdetisde dlnislnlvr nrintqmpkl tnsfaqtygl dmrteirrer
      481 tvelfnegfr iddlkrwkta etempqnilg ikwtgteyqt rwpnasyskn sdgfliiesg
      541 rkwedkhyly plptdqlqln pnlkqnpgwg e
//
LOCUS       WP_010537513             584 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Bacteroides].
ACCESSION   WP_010537513
VERSION     WP_010537513.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18640651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..584
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=67835
     Region          106..359
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          152..175
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(191..192,195..196,198,227,230..231,234..235,
                     237..238,261,267..268,271..272,275)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          191..215
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          225..255
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          260..287
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          299..325
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <461..581
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mktplsiria ffffisilav schrdsdvlq mtfskvekcm dlcpdsalni lkgipdpekl
       61 rgesqatyal lmtqtmdkny mkfssdslit ialnyyaitq nkpimyaktl fyhgrvmlel
      121 dkeeealksf laakdiyern qnlkmlalia eeigminrkq dlyddaltnf realttykql
      181 kdslsvisas lniarvylfk sewdscslyy nnaleiavqk nylseitilh elgilyrsmq
      241 nlpeaeryfl aayeketdee kkymeclslg ylymqmgqte narkylkmsa nsskaytqis
      301 aydclyflek didnfeeaiv yheladsitn smeelnsrel iaslqkkyen eklqndnlqm
      361 kvrytnfilw gtiaflsvva cmcyyyyknr nnkkkiaeie lqirdneeei eryrqeiedi
      421 qiskdqvvke nlmleenrtk vgelngkivl ltmqnkilse hlkerggeln vgissgpfih
      481 afrlllaike gtlrgklsne erqklfslfd liywnyvsrl ldraptltkh dleiccflkf
      541 gltheelsci fhttsdsvtr aksrlkgrlg istqddldaf lkef
//
LOCUS       WP_010537568             498 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Bacteroides].
ACCESSION   WP_010537568
VERSION     WP_010537568.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..498
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57677
     Region          153..475
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mqsdlllfkr vlltivtftg ialtsqgqip ltidkameia qenspslrrs ymnlerykqn
       61 llaqkaslks rfslnlnpvd ynknrrfdnr lsqwytnetf ntsgtfqvdq pilwtdgtis
      121 linrfgwqdn ssiiegdkts nrafsndlyl qltqpiftyn krkmelkqie ydyenanisy
      181 alqqlnteks itdqfysvym aqsnleisre elvnaqqsyd iiknkveadl aakdelfqae
      241 lnlatarssv desqvnlena kdklkqtlgm rldedilvfa eveikpiqvn ldqaishglg
      301 srlelrqrei eskelefdmi ktkalnefkg dvsisfglig dnshlnkvyn nptqnprvsi
      361 sfavpifdwg ekkarikaqk maqrinelef qedkvdieln irqvwrnlen lrtqikiaeq
      421 nvqnaqltyd lnqtryregd itgmemsqfq tqlsnkkity tqalinyrie llnlkilsly
      481 dfdkniplvp mkdiidkk
//
LOCUS       WP_010537682             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide biosynthesis/export family protein
            [Bacteroides].
ACCESSION   WP_010537682
VERSION     WP_010537682.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12035721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..264
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /calculated_mol_wt=29171
     Region          41..140
                     /region_name="Poly_export"
                     /note="Polysaccharide biosynthesis/export protein;
                     pfam02563"
                     /db_xref="CDD:426836"
     Region          <92..232
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mngmkqliyy vlaaflltac qsykkvpylq daevvlystq daqlydakim pkdlltivvs
       61 ctspelavpf nltvatqnnm alnyattqpv lqqylvdndg ninfpvlgel hvggltkkat
      121 eqmiveklkp yitespivtv rmvnykisvi gevarpgtft isnekvnvle alamagdmtv
      181 yglrddvkli renangkqei ipldlnkaet ilspyyylqq ndiiyvtpnk akarnsdigt
      241 stslwfsats ilvsiasllf nilk
//
LOCUS       WP_010537724             511 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Bacteroides faecis].
ACCESSION   WP_010537724
VERSION     WP_010537724.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides faecis
  ORGANISM  Bacteroides faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Bacteroides faecis"
                     /db_xref="taxon:674529"
     Protein         1..511
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=57131
     Region          9..397
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mteyssnnkr ivkntlllyi rmmftmaval ftsrvvlnal gisdfgiynv vggfiamftv
       61 lsgsfsnait rfitfelgkk dsqrlnavfc tgvniqlims vviviaaeii glwflnyhms
      121 ipddrlnaah wvlqcaigaf vlnlisvpfn aeiiaheemg ayavisivna vlqliiayml
      181 ylspldklkt ysvlylvvaf iiriiygiyc rrkfeectyh llldkdlfse mgkfagwnfl
      241 gssafmlntq gvnmlmniyf gvaanaargi avqvdsavks fansfttain pqitksysag
      301 eldymyqlvc rgakfsaflf lfiavpivle tptilkiwlk tvpeytivfv rlivfssfvd
      361 sllgnsfwta imatgkikgy qiviaivgvm vfpfswlcfe fgcgpestyi vyiiiycial
      421 lvrlyfmkvl lymplsyffr dvlgrvagvm lltfiiplpl llvldggwir lsvvclcsll
      481 vtstvvytig ltqnekvtvt sklkkivqrf s
//
LOCUS       WP_010537761             194 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Bacteroides].
ACCESSION   WP_010537761
VERSION     WP_010537761.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..194
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22450
     Region          17..191
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mdtllretvn avvnsrfpem siegrrqies ilireefpkg vialnegeva helvfvgkgm
       61 lrqyyykngk dvtehfsyeg civmciesll kqvptrliie tlepaiiylc pydkmlqlak
      121 qnweinmfyr kileyslivs qtkadswrfe sarerynlll ethpeiikra pladiasyll
      181 mtpetlsrvr sgvl
//
LOCUS       WP_010537780             406 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Bacteroides].
ACCESSION   WP_010537780
VERSION     WP_010537780.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..406
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43994
     Region          5..406
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mngtnlfkia lralannklr afltmlgiii gvasvitmla igqgskrsiq qqisemgsnm
       61 imihpgadrr ggvrqdpsam qtlkltdyea lrdetnflsa ispnvsssgq liagnnnyps
      121 svsgvgleyl eirqlsvetg dmfteadiqs sakvcvigkt ivdnlfpdgg dpigkiirfn
      181 kipfrvvgvl kakgynsmgq dqdnivlapy ttvmkrllav tylqgvfasa ltedmteyat
      241 deiteilrrn hklkasdedd ftirtqqels tmlnsttdlm ttllaciagi slvvggigim
      301 nimyvsvter treiglrmsv gargvdilsq flieailisi tggligvvig cgaswivksv
      361 ahwpifiqpw svflsfavct vtgvffgwyp akkaadldpi eairye
//
LOCUS       WP_010537781             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Bacteroides].
ACCESSION   WP_010537781
VERSION     WP_010537781.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..247
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27045
     Region          1..227
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mkkvielqni krdfqvgeet vhalrgvsft inegeyvtim gtsgsgkstl lntlgcldtp
       61 tsgeylldgi svrtmskpqr avlrnrkigf vfqsynllpk ttavenvelp lmynssvsaa
      121 errrraieal qavglgdrle hksnqmsggq mqrvaiaral vnnpavilad eatgnldtrt
      181 sfeilvlfqk lhaegrtiif vthnpeiaqy ssrnirlrdg hviedtvnsh ilsaaealaa
      241 lpksded
//
LOCUS       WP_010537783             465 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Bacteroides].
ACCESSION   WP_010537783
VERSION     WP_010537783.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..465
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51470
     Region          45..460
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mnminvrrlt viaflgagll pgisaqessv qdnvrsevnl paqwdlqsci dyalqqniti
       61 rknrvnaest qidvktakaa lfpslsfsts qnmvnrpyqe ssktvsgsev iettsktsyn
      121 gnyglnaswt iyngskrlnt ikqerlnnqv anldvetsen siqesiaqiy iqilyaaesv
      181 kvnentlqvs iaqrdrgqel lnagsiaksd faqleaqvst dryqlvtaqa tlqdyklqlk
      241 qlleldgene mniylpvlsd envllplpak kdvymsaltl rpeieaskin veaselgidi
      301 akagylptis lsagigtnht sgsdftfgeq vkngwnnsig vsvsvpifnn rqtksavqka
      361 klqretslls lldeqktlyk tieglwldan saqqryaaan eklkstqisy dliseqfdlg
      421 mkntvellte knnllqaqqe qlqakymail ntqllkfyqg dklal
//
LOCUS       WP_010537806             372 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endonuclease/exonuclease/phosphatase family protein
            [Bacteroides].
ACCESSION   WP_010537806
VERSION     WP_010537806.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..372
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42256
     Region          118..370
                     /region_name="EEP-2"
                     /note="Exonuclease-Endonuclease-Phosphatase (EEP) domain
                     superfamily; uncharacterized family 2; cd09084"
                     /db_xref="CDD:197318"
     Site            order(122,154,231,297,299,340,362..363)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197318"
     Site            order(154,362)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197318"
     Site            order(231,299,363)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197318"
ORIGIN      
        1 mkafyrllyy lsilltsila gftlagafag daspdsftlm pfiglilpvl llanvvsaiy
       61 wtvrwrcwvf ipfiailgnw gyptrvlqsp lfdsasqpnt eslslkkner gtesaltiat
      121 ynvnsfnheh tgfsckgiaa ymkelgvdif cfqefginhe fgidslrtvl sewpyyyvps
      181 spagesllql avfsrypike kqlvtypnsn ncslwcdidi ngqtirlfnn hlqttevsrn
      241 krklekelra ddtdraeraa ltlagglhen fkkravqakq inqlisdspy ptlvcgdfns
      301 lpssyvyqtv kgekmndgfq tcghgymytf ryfkhllrid yilhssefqg vdyfspdley
      361 sdhnpvvmrm rl
//
LOCUS       WP_010537882             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Bacteroides].
ACCESSION   WP_010537882
VERSION     WP_010537882.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..265
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29054
     Region          183..264
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mkrgkqtcki lkdirrqiae andiefitse cqyqgdclgt cpkceaevry leqqlerkrm
       61 agkaitilgi saglvamapm tscssspnkg snqetisdsa ntsvmfgevc ptpiedtipm
      121 verdtvnkqe lpelpqeqgl ieitpisgdi itvkdsladv levaavmpef pggaqelmkf
      181 itkninypke iaqgelgaqg rvivqfivdk egniiqpkvv rgvdpyldke alrivglmpk
      241 wkpgelddgt kvavrftipv mfrlq
//
LOCUS       WP_010537975             470 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Bacteroides].
ACCESSION   WP_010537975
VERSION     WP_010537975.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..470
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52672
     Region          136..460
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkknkilfvl walcfsviqt naqtplsfee slhllnqgnq slkiadkgie iakaerdkln
       61 afwyptlqst gafvhmseki evkqplsqft dpakdfvhsi ipddqmisai ldkigantlv
      121 fpltprnltt vdlsaewvlf sggkrfratn igrtmvdlar enraqtaanq qnllaesyyg
      181 lrlaqqvvav reetyrglqk hyenalklea agmidkagrl faqvnmdeak rsleaarkee
      241 tvvqsalkal lnkkdtdeni vptsplfmnd slppkmlfdm svnsgnymln qlqlqehiak
      301 qevriaqsgy lpnialfgkq tlyshgiqsn llprtmvgig ftwnlfdgld rekkirqskl
      361 tqqtltlgkm karddlavgv dklytqleka qdnvkalnat ielseelvri rkksftegma
      421 tstevidaet mlatvkvarl aayyeydval mnllslcgtp eqfvnyqpkp
//
LOCUS       WP_010538174             338 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [Bacteroides].
ACCESSION   WP_010538174
VERSION     WP_010538174.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142950
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..338
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=37649
     Region          1..252
                     /region_name="SDR_a1"
                     /note="atypical (a) SDRs, subgroup 1; cd05265"
                     /db_xref="CDD:187575"
     Site            order(7,9..10,12,31..33,58..60,94..96,122,126,149..152)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187575"
     Site            order(76,96,122,126)
                     /site_type="active"
                     /db_xref="CDD:187575"
ORIGIN      
        1 mkalfiggtg tisadvvela qqrgweitll nrgsrklpeg mrsiiadihd eeavakavtd
       61 esydvvaqfi aytaedverd irlfrdktkq yifissasay qkpladyrit estplvnpyw
      121 qysrhkiaae evlmaayrtt gfpvtivrps htyngtkppv slhgnngnwq ilkrildgkp
      181 viipgdgssl wtlthsrdfa kgyvglmanp haignafhit tdesmtwnqi yqtiadalek
      241 plnalhvasd flarhgenyd frgellgdka atvvfdnski krlvpdfict tsmadglrqa
      301 vqymlshpet qtpdpefdsw cdriadamca adrafesk
//
LOCUS       WP_010538213             394 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: uracil-xanthine permease family protein
            [Bacteroides].
ACCESSION   WP_010538213
VERSION     WP_010538213.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..394
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41119
     Region          6..393
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mdsnnltplr kgvvgvqflf vafgatvlvp llvgldpsta lftagigtli fhavtrgkvp
       61 iflgssfafi apiikately glagtlsgml gvalvyfams alvkwqgvrv verlfppvvi
      121 gpviiligls lagtgvemak enwvlallsl vtavvvsmka kgllklipif cgiivgylaa
      181 wlfydldlsg vrdaawiglp qfvfpkfswe pilfmipvai apviehigdv yvvntvtgkd
      241 fvkdpglhrt llgdglaclf aglvggppvt tysevtgams ltkitnpqvi riaaisailf
      301 svigkisall ksipsavlgg imlllfgtia cagignlvnn cidlsrtrni iivsltltvg
      361 iggavltwgd fslsgiglaa lvgvllnlil pkdd
//
LOCUS       WP_010538259             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Bacteroidales].
ACCESSION   WP_010538259
VERSION     WP_010538259.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..253
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28484
     Region          7..223
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mskeifvafa tqkggigkst vtalaasylh nvkgynvavv dcddpqhsih glrehemgli
       61 dsstyfkala cdhfrrikkn sytivksnav nalddaermi atedvkpdvv ffdmpgtlrs
      121 ngviktlsqm dyiftplsad rfvvestlkf vtmfrdrlmt tgqaktkglh lfwtmvdgre
      181 rndlygiyee viaemgfpvl strlpdskkf rrdlseerks vfrstifpmd tallkgsgir
      241 efseeisdii rpq
//
LOCUS       WP_010538314             409 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA recombination protein RmuC [Bacteroides].
ACCESSION   WP_010538314
VERSION     WP_010538314.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..409
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46337
     Region          78..409
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 melillivia alavisivls lvkgnnhaqa eqlqtalrqq mqenreelnr sirelrmemt
       61 qtlnqnmqql qdvlhknmmt sgelqrqkfd tmarqqevli kstekrlddm rlmveeklqk
      121 tlnerigqsf eivrsqlenv qkglgemksl aqdvgglkkv lsnvkmrgtf gevqlgalle
      181 qmmspeqyda nvktkksgte fvefaiklpg kddanstvyl pidakfpkdi yeqyydafea
      241 gdtsliessg kqlevtikkm akdihdkyvd ppfttdfaim flpfesiyae virrtslvet
      301 lqkeykivvt gpttlgailn slqmgfrtla iqkrtgevwt vlgavktefs kfggllekvq
      361 knlqsagdql eevmgkrtra ierklrqveq lpheesqkil piaddgdde
//
LOCUS       WP_010538356             372 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide pyruvyl transferase family protein
            [Bacteroides].
ACCESSION   WP_010538356
VERSION     WP_010538356.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10514996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..372
                     /product="polysaccharide pyruvyl transferase family
                     protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43491
     Region          13..300
                     /region_name="PS_pyruv_trans"
                     /note="Polysaccharide pyruvyl transferase; pfam04230"
                     /db_xref="CDD:427804"
ORIGIN      
        1 mkiniltfqf aknygailqa halssyiknd lheeceiiqy wpersdaswn myyrgfepkv
       61 ilrnifvffn ikfkrefrak nqvmqkaise llpltkeryt resilkhppt anayicgsdq
      121 vwnfvkcfdd ptyffdftks mknvkrigya psiadpwpks rweefkgyls hmdiisvrek
      181 sdvpvvekls gkpvthvvdp vflktreywd nlsqdmnike hyifcyflgt ndlavnlvnk
      241 vkqltgfkiv hlnlnardrf nsdynlravs pqqfiglikn asyvctnsfh csafsiifrk
      301 nyfvapkgfa narmeslqem fglnnrmftq elidgmtieq mtvdyskade kfapfkeksl
      361 qylnnalyge pn
//
LOCUS       WP_010538316             122 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Bacteroides].
ACCESSION   WP_010538316
VERSION     WP_010538316.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..122
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14224
     Region          1..121
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mkrlttkeee imcifwehgp mfvrellsfy depkphyntv stlvrgleek gfvgykaygn
       61 tyqyyalise keykssalke vvsqyynnsy invvssfiee egmsvdelka lieyieqgkk
      121 kn
//
LOCUS       WP_010538382             169 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Bacteroides].
ACCESSION   WP_010538382
VERSION     WP_010538382.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..169
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19394
     Region          22..169
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; cl46601"
                     /db_xref="CDD:480941"
ORIGIN      
        1 mkklevkdlk enffeaigke wmlvtagtke kfntmtaswg gigwlwnkpv afvfirpery
       61 tyefieksdy ltlsflgean kkvhaicgsk sgrdmdkvka tglkpvfteq gnvffeqarl
      121 ileckklyad nikpdcfldk esiekwygga hggfhkmyiv eieniwegd
//
LOCUS       WP_010538385             108 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Bacteroides].
ACCESSION   WP_010538385
VERSION     WP_010538385.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..108
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12428
     Region          7..104
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mnvdnvksqm rkgmleycim lllhkepaya sdiiqklkea qlivvegtly plltrlkndd
       61 llsyewvest qgpprkyykl tekgeaflge lelswkelne tvnhiasr
//
LOCUS       WP_010538403             371 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Bacteroides].
ACCESSION   WP_010538403
VERSION     WP_010538403.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..371
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41799
     Region          175..369
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mikfliekef kqllrnsflp rlilvfpcmi mllmpwavnm eikniqlniv dndhsvisqr
       61 lvnkiaasty frltevpasy adglrnielg tadivmeipr hlekdwmnkg eahiliaans
      121 vngtkgglgs sylatiinny atelraerpd avsasgsaps icidtqglfn pnlnyklymi
      181 palmgmlltl icgflpalnv vsekevgtie qinvtpvpkf tfilakllpy witgfivltl
      241 cfllswllyg itpvghfivi yflailfvfv msgfglvisn ysatmqqsmf vmfffmlilm
      301 lmsglftpvs smpewaqvit yfnplkyfme amrmvylkgs sllellpeig vlflfalvfn
      361 swavfsyrkn q
//
LOCUS       WP_010538424             486 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ammonium transporter [Bacteroides].
ACCESSION   WP_010538424
VERSION     WP_010538424.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..486
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51387
     Region          71..486
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mdtiykkhss vklwiataml ifsclttsvf aqktvvtdtv tavtetitei atdpvkvatt
       61 seeaaisasd tigelalgln tvwmllaaml vffmqpgfal veagftrvkn tanilmknfv
      121 dfmfgsllyw figfglmfga ggfigmphff nlsfldsdlp kegflvfqtv fcataativs
      181 gamaertkfs mylvytifis vliypisghw twgggwlmng eegsfmmnlf gttfhdfags
      241 tvvhsvggwi alvgaailgp rigkygkdgr skaipghnlt vaalgvfilw fgwfgfnpgs
      301 qlaasteada iaishvfltt nlaacaggff alvvswmkyg kpslsltlng vlaglvgita
      361 gcdavsptga vvigaicgvv milavdfidk vlkiddpvga ssvhgvcgfl gtiltglfst
      421 seglfyghga gflgaqifga lvvgawaasm gftifkvldk vhglrvparv eeegldiyeh
      481 gesayn
//
LOCUS       WP_010538398             234 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SGNH/GDSL hydrolase family protein [Bacteroides].
ACCESSION   WP_010538398
VERSION     WP_010538398.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10139723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..234
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=26213
     Region          52..230
                     /region_name="SGNH_hydrolase_like_4"
                     /note="Members of the SGNH-hydrolase superfamily, a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site closely...; cd04501"
                     /db_xref="CDD:239945"
     Site            order(60,85,114,210,213)
                     /site_type="active"
                     /db_xref="CDD:239945"
     Site            order(60,210,213)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239945"
     Site            order(60,85,114)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:239945"
ORIGIN      
        1 mekkklgqwm llavvclsfs vgeiyaqkhe fadfkryake natlaqpvkk ekrvvfmgns
       61 itegwvrthp dffktngyig rgisgqtsyq fllrfredvi nlapalvvin agtndvaent
      121 gpynedytfg niasmaelak ankikvilts vlpaaefpwr reikdapqki qslnarieay
      181 akankipfvn yyqpmvvgen kalnpqytkd gvhptgegye vmetlikqai ekal
//
LOCUS       WP_010538559             212 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Bacteroides].
ACCESSION   WP_010538559
VERSION     WP_010538559.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..212
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23661
     Region          4..212
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mesvafiqwc lehlnywtit llmtiessfi pfpseviipp aaykaavnde lniylvvlfa
       61 tigadigali nyylakwlgr piiykfansr ighmclidea kvqhaesyfd khgalstfig
      121 rlipavrqli sipaglarmk mhtfllytti gaglwntila vigyylstvp gieseeqlia
      181 kvteysheig ycfiaigifi vgflvykgmk kk
//
LOCUS       WP_010538642             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Bacteroides].
ACCESSION   WP_010538642
VERSION     WP_010538642.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..182
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=21069
     Region          15..169
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 meaylkklcf eyqveekevk ellarmemvy ldkgetiasa tmpeqslyii vsgilhtftt
       61 rqgedktvrf lsegdailcy ntskhsiktl trcvayyise deieelcats itfanlmrql
      121 meyqfylkee mnvntrklti rerylsllte ipdilyrvpl kyityylgad vtslgylags
      181 hk
//
LOCUS       WP_010538645             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Bacteroides].
ACCESSION   WP_010538645
VERSION     WP_010538645.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..187
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=21767
     Region          13..187
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mdihdiidni yklpdvskea llsdasevvy pkgfhlfwan rkstkfylmk kgmlhaythk
       61 sdkkvtfwfg kegdaifplq tlydnqagye nielledsal yelsvdklhn lyledihian
      121 wgrkfaerec ikseklfisr qfktsleryq elisdypdil qrvplgiias ylgisqvnls
      181 rirakir
//
LOCUS       WP_010538664             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Bacteroides].
ACCESSION   WP_010538664
VERSION     WP_010538664.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23945
     Region          8..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtttnnnedv ekkiveaake lfiengfaet smsdiaakvg inrpvlhyyf rtkdkmfqav
       61 fgniilsfip rihdiiiqqd ksvsesigei vdayykvfte npclplfmvr emhrdmdhls
      121 ttikelrleq ylhkimdvlq eemnggrlkt vplpfvfytf ysaltvpflt knlsasffle
      181 kedtfedilv qwkpyivrqm eallvvg
//
LOCUS       WP_010538682              91 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [Bacteroides].
ACCESSION   WP_010538682
VERSION     WP_010538682.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..91
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10391
     Region          2..91
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mirlnvfvrv netnrekaie aakeltacsl keegciaydt fesstrrdvf micetwqnae
       61 vlaaheksah faqyvgiiqe laemklekfe f
//
LOCUS       WP_010538696             377 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycerate kinase [Bacteroides].
ACCESSION   WP_010538696
VERSION     WP_010538696.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..377
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39813
     Region          3..374
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mkkvvvamds fkgclsstea ekaaeegvkq vcpdcevvcf piadggegml dvlveatega
       61 yqkviasdpl mrpietgygv sgdkriafie maavnglpll saternpmlt ttygtgelil
      121 haiehgyref iigiggsatn daglgmlqal gfrfydqdge ilgkggqild qivaidfssv
      181 hpalkdarft iacdvrnpfs gpegaayvfa rqkgaddami eklnagmkrf srlihsttgr
      241 eitevagaga agglggafla flnaelkpgi elllrtlkfd ekikdadlii tgegrvdrqs
      301 vmgkvpfgil eeankqgipv ivvagsiadt evlnkagfrg ifsivpspms levamkpeta
      361 knnisrtvaq iislatl
//
LOCUS       WP_010537828             466 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: C1 family peptidase [Bacteroides].
ACCESSION   WP_010537828
VERSION     WP_010537828.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Nagler,D.K. and Menard,R.
  TITLE     Family C1 cysteine proteases: biological diversity or redundancy?
  JOURNAL   Biol Chem 384 (6), 837-843 (2003)
   PUBMED   12887050
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of cysteine peptidases
  JOURNAL   Methods Enzymol 244, 461-486 (1994)
   PUBMED   7845226
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..466
                     /product="C1 family peptidase"
                     /EC_number="3.4.22.-"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52899
     Region          27..462
                     /region_name="Peptidase_C1B"
                     /note="Peptidase C1B subfamily (MEROPS database
                     nomenclature); composed of eukaryotic bleomycin hydrolases
                     (BH) and bacterial aminopeptidases C (pepC). The proteins
                     of this subfamily contain a large insert relative to the
                     C1A peptidase (papain) subfamily. BH is...; cd00585"
                     /db_xref="CDD:238328"
     Site            order(64,71,73..75,184..185,249,251,253,259,402)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238328"
     Site            order(86,92,385,407)
                     /site_type="active"
                     /db_xref="CDD:238328"
     Site            462
                     /site_type="active"
                     /note="G bulge [active]"
                     /db_xref="CDD:238328"
ORIGIN      
        1 mnkrilsvfv ccalyysaqa qdakggisad mmqqikqsyq gtstdkairn aisnndirkl
       61 alnqdnmkgm dthfsvkvns kgitdqkssg rcwlftglnv mrakaidkyn lgsfefsqty
      121 pfffdqleka nlflqgiidt sdkpmndkmv ewlfrnplsd ggtftgvadi vskyglvpkd
      181 vmpetnssen tvrmaslial klreqglqlr dmasknakpa amekakteml stiyrmlvln
      241 lgvppteftw tqynakgepv etatytplsf lkkygdekli dnyvmlmndp sreyykcyei
      301 dydrhrydgk nwtyvnlpie dikemaiasl kdstmmyysc dvgkflnsdr glldvknydy
      361 dslmgttfgm dkkqriqsfa sssshamtlm avdldkngkp akwmvenswg agagyqghli
      421 mtdewfneyt frlvvetkyv tpkalevlkq kpirlpawdp mfagee
//
LOCUS       WP_010538727             414 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Bacteroides].
ACCESSION   WP_010538727
VERSION     WP_010538727.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..414
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46317
     Region          27..>192
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          149..414
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mslslfiarr iyresdggkq vsrpavliam agiaiglavm iiavavvigf ksevrnkvig
       61 fgshiqianl davnsyethp iavgdsmmta lssypevshv qrystkpgmi ktddafqgmv
      121 lkgvgpefdp gfmqeylveg eipvfsdsvs snqvliskal atkmklklgd kiytyyiqdn
      181 irarrltiag iyqtnfseyd nlflltdlyl vnrlngwqpe qvsgvelqvh nydkledity
      241 eiavdtdnqr defggiyyvr nieqlnpqif ewlnlldlnv wvilflmigv agftmisgll
      301 iiiiertnmi gilkalgadn ftirktflwf avfligkgml wgnviglafc fiqsqfgifk
      361 ldpenyyvdt vsvsfniwff llinagtlla svlmligpsf litkinpass mrye
//
LOCUS       WP_010538776             417 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Bacteroides].
ACCESSION   WP_010538776
VERSION     WP_010538776.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 417)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..417
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47908
     Region          <84..417
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mqllkqiwne rrsngwlwae llivfvvlwy ivdwtyatar tyyeplgydi tntyylelsl
       61 knnksdsyip kgqketttgq diieltnrlr rlpeveavsi svnarpyigs nsgirfrldt
      121 lvrsplkrpv tpeffqvfry qsadgqgyrp lvqaikngns vigeniwpdd ykgdrtllgk
      181 evinvddstn vykiaavstk vryndfwsny gdrymavpft etelaenndd lypvnvevcl
      241 rvkpntaagf serlmelsdt qlsvgnlfil kvhdyeaire iynrsnvnqm qtrfwmmgfl
      301 lvnillgivg tfwfrtqhrr gelglriavg strmgiwhrl nkeglllltl aavpaavlcy
      361 nigylelteg giewsilrfl iafcatcflm almiligiwf parqairvqp aealree
//
LOCUS       WP_010538731             622 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Bacteroides].
ACCESSION   WP_010538731
VERSION     WP_010538731.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..622
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72109
     Region          8..524
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          553..619
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mavpylqvdn ltksfgdlvl fenisfgiae gqrvgliakn gsgkttllni isgkeghdsg
       61 sivfrrdlrv dyleqdpqyp eeltvleacf hhgnstveli keyercmete ghpgledlla
      121 rmdqekawey eqkakqilsq lkirnfdqkv kqlsggqlkr valanalite pdllildept
      181 nhldldmtew leeylrrtnl sllmvthdry fldrvcseii eidnqqlyqy kgnysyylek
      241 reerieaksv eierannlyr teldwmrrmp qarghkaryr edafyelekv akqrqrndnv
      301 klevkasyig skifeadhls ksfgdlkild dfsyifsrye kmgivgnngt gkstfikilm
      361 glvkpdggti digetvrfgy ysqdglqfde qmkvidvvqd iaevielgng kkltasqflq
      421 hflftpetqh syvcklsgge rrrlylctvl mrnpnflvld eptndldiit lnvleeylqs
      481 fkgcvivvsh dryfmdkvvd hllvfngqgd irdfpgnysd yrdwkeakaq kekeaekpqe
      541 ektarvrlnd krkmsfkekr efeqlekeia qleaekaqie ellcsgtlsv deltdkskrl
      601 pevnelidek tmrwlelsei eg
//
LOCUS       WP_010538781             463 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Bacteroides].
ACCESSION   WP_010538781
VERSION     WP_010538781.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..463
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=51845
     Region          23..403
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mslniakdsk krvvivgggf gglklanklk ksgfqvvlid knnyhqfppl iyqvasagme
       61 ptsisfpfrk ifqhrkdfyf rmaevraifp eknliqtsig kaeydylvla agtttnffgn
      121 khieeeampm knvseamglr nallanlera vtcsnkqeqq ellnvvvvgg gatgvevagv
      181 lsemkkfvlp ndypdmpssl mhiylieagp rllagmseds sshaeqflre mgvnillnkr
      241 vtdyrnhkvt ledgseiatr tfiwvsgvtg vsfgnmnaaa igrggrikvd afnrvegtdn
      301 ifaigdlcil sgdedypngh pqlaqvaiqq gellaknlir lekgkemkpf hyrnlgsmat
      361 vgrnravaef skvkmqgwfa wvmwlvvhlr silgvrnkvv vllnwvwnyf tydqsmrmiv
      421 yarkakeird retieatthw gkeliqepqp vkqepqsaep kke
//
LOCUS       WP_010538830             441 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpP1/FadL family transporter [Bacteroides].
ACCESSION   WP_010538830
VERSION     WP_010538830.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..441
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47499
     Region          5..441
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mrkisligfv mlivsiptfa gglltntnqh vsflrmlarg asididgvys npaglaflpg
       61 dglylslngq sayqtrnist tfplfpeegn rryykgtasa pfipsfqgay kkgdwtisgs
      121 favvggggka sfddglgmfd smimgnisqa sggqitpsmy sinsamdgsq fiygvqlgls
      181 ykindwlsvf aggrmnyfsg gyegfltatv nsnipnlggt elaaieldcd qtgwgitpil
      241 gadvklgkwn iglkyefltn lnlenktrka evrasgvvmp dnelnplasf kdgvntpsdi
      301 palltaavgy eilptlrasv eyhhffdkaa gmaggkekal khgtheflvg aewdvtkqlt
      361 lsggfqrtdy gladdfqsdi sfscdsyslg fgaaikmtkh ltmnvayfwt nysdydkita
      421 tgsttysrtn kvfglgvdyk f
//
LOCUS       WP_010538903             419 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphoglycerate kinase [Bacteroides].
ACCESSION   WP_010538903
VERSION     WP_010538903.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..419
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=44865
     Region          3..419
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mqtidkfnfa gkkafvrvdf nvpldenfni tddtrmraal ptlkkiladg gsiiigshlg
       61 rpkgvadkfs lkhiikhlse llgvevqfan dcmgeeaavk aaalqpgevl llenlrfyae
      121 eegkprglae datdeekaaa kkavkesqke ftkklasyad cyvndafgta hrahastali
      181 akyfdtnnkm fgylmekevk avdkvlndik rpftaimggs kvsskieiie nllnkvdnli
      241 iaggmtytft kamggkigis iceddkldla ldlikkakek gvnlvlavda kiadafsnda
      301 ntqfcavdei pdgwegldig pkteeifanv ikesktilwn gptgvfefen fthgsravge
      361 aiveatknga fslvgggdsv acvnkfglas gvsyvstggg alleaiegkv lpgiaaine
//
LOCUS       WP_010538969             392 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Bacteroides].
ACCESSION   WP_010538969
VERSION     WP_010538969.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..392
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=45750
     Region          19..>326
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 mesfyrthay lvehtnapvr rdlmdeidws drligikgtr gvgkttfllq yakekfgtdr
       61 sclfinmnnf yfsghslvdf anefqkrggk vllidqvfkh pewsrelrmc ydrfpslkiv
      121 ftgssvmrlk eenlelrdia ksynlrgfsf reflnlqtgm kfraysleei lstheqiakg
      181 vlskvrpldy fqdylhhgfy pfflekrnfs enllktmnmm vevdillikq ielkylskik
      241 kllyllavdg pkapnvsqla sdiqtsrati mnyikylada rlinlvypkg eefpkkpski
      301 mmhnsnlmys iypvkveeqd vldtffvntl wkdhkvhkgd knvsfmvdev mpfkicaega
      361 kiknnpdvty alqkaeigrg nqiplwmfgf ly
//
LOCUS       WP_010539000             340 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide deacetylase family protein
            [Bacteroides].
ACCESSION   WP_010539000
VERSION     WP_010539000.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..340
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38257
     Region          46..>170
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(48..49,114,118,156..158)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 myriclglll iiagfyvkat epvhdglvkl risnfkddka gavsytfddg lrnqyliaap
       61 imeklqipgt ffiipgqvsa tlqeaeakkp gawggvtwde irtlvakgfe ignhgynhkn
      121 lvtqvkepee leneiensad iirretgifp vsfcypynsf neqvgkiver rhmvarifqq
      181 gigardttak ninqwmdkli srrewgvami hgltdgfdpl rpdvfeshlt yakkhekdlw
      241 idtfgnigsy ikqrdattik eieigtnsvs ftldcklskk qvkvpltlvi ltenkvteak
      301 atqgreslpv tisnkqimid cvpdsgrvtv ewkfsdvyid
//
LOCUS       WP_010539016             948 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Bacteroides].
ACCESSION   WP_010539016
VERSION     WP_010539016.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..948
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=106743
     Region          24..111
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          94..848
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkklyiltvl illtgfgtaf aqtlkghiyd antneplvga avtyklhgnq gvvsdingay
       61 eiklpeggvd lvfsyvgyed vlmpivigrr dvitkdvymk estklleevv vsagrfeqkl
      121 snvtvsmdlv kasdiarqap tditstlrtl pgvdivdkqp smrggsgwty gvgarsqilv
      181 dgmstlnpkt geinwntvpl enieqvevik gassvlygss alngiinirt arpgltpktr
      241 fsayvgvygd aendeyqwsd ksfwkdgkys vkpilrgsll sgirnpiyeg fdlshsrrig
      301 hfdvsgsinl ftdegyrqqg ynkrfrmggn ltyhqpdmgm kilnyglnvd fltnqygdff
      361 iwrsptevyk pspftnmgre ennfhidpfi nyvnpengts hkikgrfyhs adnivrpssg
      421 asitdilgnm gtnaqtiqni aggdysslyp alvgigsgli ngnledamng vftslgnifp
      481 nattadycdl iswvmdnglp gdlgsiqngq lpsdlipwls nvmnpsrnds ktktdksyny
      541 yldyqfnkkw dggaqittgm tyehvrydss imdevyksdn vaaffqydqr fwdrlsvsag
      601 vraeyyrvdn hyreaetkil gtkvpfrpvf raglnyqlad ysfirasigq gyrnpsinek
      661 ylrkdiggvg iypnldikpe kgynaelgfk qgykignfqg fvdvagfyte ykdmvefqfg
      721 lfnnadysmi nsisdairml mdgkgfgiga qfhnvskaqi ygmeistngv ynfnkntklf
      781 ynlgyvytep rdadykerne ledtysdalq mkeksntgky lkyrpkhtfk atvdfqwkri
      841 nlganvawks kilavdylml derekqqkdl mdyvrtilfg qsrgetlasy wkkhntdyat
      901 vdlrfgvkat kevafqfmvn nllnkeysyr pmavaaprtf vlkmdvtf
//
LOCUS       WP_010539018             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit beta/FixA
            family protein [Bacteroides].
ACCESSION   WP_010539018
VERSION     WP_010539018.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..290
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30927
     Region          4..289
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mslkivvlak qvpdtrnvgk damkadgtin raalpaifnp edlnaleqal rlkdahpgst
       61 vtiltmgpgr aadiireglf rgadngyllt drafagadtl atsyalatai rkigecdiii
      121 ggrqaidgdt aqvgpqvaek lgltqityae eilevgdgki kvkrhidggv etvegplpiv
      181 itvngsaapc rprnaklvqk ykhaktvtek qqgnldytdl ydkrdylnlt ewsvadvngd
      241 laqcglsgsp tkvkaiqniv fqakesktis gsdrdveeli vellanhtig
//
LOCUS       WP_010539125             426 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: O-acetylhomoserine
            aminocarboxypropyltransferase/cysteine synthase family protein
            [Bacteroides].
ACCESSION   WP_010539125
VERSION     WP_010539125.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..426
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46496
     Region          3..426
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 makqfkpetl cvqagwtpkk geprvlpiyq sttfkydtse qmarlfdled sgyfytrlqn
       61 ptndavaaki aaleggvaam ltssgqaanf yaifnicqag dhfvcssaiy ggtfnlfgvt
      121 mkklgidvtf vtpdaseeei saafkpntka lfgetvsnps levldiekfa riahnhgvpl
      181 ivdntfptpi ncrpfewgad ivvhsttkym dghatsiggc ivdsgnfdwd ahadkfpglc
      241 tpdesyhglt ytkafgkgay itkataqlmr dlgsiqspqn afllnlglet lhlrmpqhcr
      301 naqkvaefls knekvawvny cglpdnkyya laqkympngs cgvisfglkg grdvsikfmd
      361 slefiaivth vadarscvlh pashthrqlt deqlleagvr pdlirlsvgi enaediiadi
      421 eqalna
//
LOCUS       WP_010539258             351 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metallophosphoesterase [Bacteroides].
ACCESSION   WP_010539258
VERSION     WP_010539258.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..351
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=38894
     Region          108..348
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mkktnilfiv fvlflfvsck skknvvstlp rpvlnvdsvr pdssaiidgl ftpdhsqlad
       61 lkvstkqqkk tvkketvseq eernlvlrgt kitsstvsas saysgidrvv eydfthrdvp
      121 eafegfriaf isdlhyksll kekglnnlvr llndqkpdvl lmggdyqegc eyveplfaal
      181 arvktpmgtf gvmgnndyer chdeiirtmk hygmrplehe vdtlrkdgqq iivagvcnpf
      241 dlkqngvspt lalspndfvi llvhtpdyve dvsvantdia laghthggqv rvfgyapiqn
      301 shygtrfltg laynstkmpl ivtngigtsq mpvrigapae iimitlhrlk e
//
LOCUS       WP_010539281             164 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase [Bacteroides].
ACCESSION   WP_010539281
VERSION     WP_010539281.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..164
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18274
     Region          3..163
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(7,24,29,60,98,104,117)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(9,16,46..48,67,99..102)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mskvsiiaav drrmaigfqn kllfwlpndl krfkalttgn tiimgrktfe slpkgalpnr
       61 rnivlssrpe tvcpgaevfp sleaalqsck edehiyiigg asvyrqalpf adelcltein
      121 dlapeadaff pevspaqwhe ksreahpvde khlcpyafvd yvkq
//
LOCUS       WP_010539263             750 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: inorganic phosphate transporter [Bacteroides].
ACCESSION   WP_010539263
VERSION     WP_010539263.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..750
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=83279
     Region          1..>210
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 metiylciii flfvlavfdl ivgvsndavn flnsavgaka asfktilfia gigifigasl
       61 sngmmdiarh giyqpehfyf aeimcillav mltdvvlldv fnsmgmptst tvslvfellg
      121 gtfalslikv nndatlamgd lintdkalsv imaifvsvai afffgmlvqw lariiftfny
      181 tknikysigl fggiaatsii yfmlikglkd ssfmtpenkq wiqdntllli gsffvfftil
      241 mqvlhwfkvn vfkvvvlmgt falalafagn dlvnfigvpl agyssfidyt tngtgtspds
      301 flmtsllgpa ktpwyfliga gtimvfalct skkahavikt svdlsrqdeg eenfgstpma
      361 rtlvrfsmal angtsrimpe gakqwinsrf rkneaiiadg aafdlvrasv nlvlagllia
      421 lgtslklpls ttyvtfmvam gtsladrawg rdsavyritg vlsviggwfi tagaafticf
      481 fvalvlhygg nisiialigi aifilirsqv mykkrkakeq gnetlkqlmq tsdseealql
      541 mrkhtreela kvleyaetnf eltvtsfihe nlrglrramg stkfekqlik qmkrtgtvam
      601 crldnntvle kglyyyqgnd faselvysis rlcepclehi dnnfnpldai qkgefsdvae
      661 dityliqqcr kklenndyqn meeeirrand lngqlsqlkr kelqriqsqa gsirvsmvyl
      721 tmvqeaqnvv tyiinlmkvs rkfqmetemp
//
LOCUS       WP_010539342             642 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Bacteroides].
ACCESSION   WP_010539342
VERSION     WP_010539342.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..642
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=73664
     Region          40..581
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          321..642
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkykhlftst llavlitscn yldivpdnia tlemafntra naekylatcy nfvpaaanld
       61 hnsglicgge mwylkpeshy yknitsfnia rgmqnsndpl lnywdggqgg ynifrgihec
      121 nifidnidrv pdmrmeeknk wkaevmtlka yyiyylmlhy gpipllkeni sveadldmmq
      181 leretindiv tyttdlldea mnipsgltfn vtsprtelgr itlpiakaik akllilaasp
      241 lfngntmyae fvnsegipff dqeykkekwe aaaaacldai ntaheagasl ykfdeklnyt
      301 pspalqqelt lrntitgrfn seiiwalgsn atdgiqnlcq ahltnyslgn rmgrscsqla
      361 psleiveqfy tangvpmded kdyeyenryk ltttpeddpi hftpnyttik lhlnrearfy
      421 ayigfdggkw fsieccndne tssypikskk gdiagvsdel ysptgyftkk lvsyqnvnts
      481 atninyvysf piirlsdlyl lyaealneln etpttdvyyy vqqvrnkagl deggslvntw
      541 rnhsnrpdkp ttqrgmreii qkermielaf eghryhdvrr wklgstylnt qikgwsvleq
      601 dpeyfynarv lftrkfmprd ylwpiktnsi nrnpklvqnp qw
//
LOCUS       WP_010539354            1046 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Bacteroides].
ACCESSION   WP_010539354
VERSION     WP_010539354.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1046
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=116759
     Region          4..1043
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 midiskwafe nkkliyflia vlivggayss yemskledpe vtvkvamvvt typgasahqv
       61 elevtdvlek nirtmgnidn vesysyndls liqvelkttv keadveqcwd llrrkvanaq
      121 aelpegaatp lvkddfgnvy gmfyaltgdg lqdrelsdya elikrevsel dgvervdlyg
      181 kreecinisl lqdrmanlgv kpaevlatln gqnkttytgy ydngdnrirv tvsdkfktve
      241 digrmliqgh dddqlrlsdi ariekdyenp trnelfydrq ramgiliaas sgsdiikigk
      301 rveqkldelk aerlptgvec hkvfyqperv sgslgtfiln liesviivvv ilmitmgfks
      361 gviigislvv tvfgsflfly fvdgtmqrvs lasfvlamgm lvdnaiviid gilvdlkagk
      421 srmeamtaig rqtampllga tliaiiaflp ifmspdtagv ytrdlfivla vslllswvla
      481 lvhvplmanr ilhpevskea sttgkrvyeg kiyavlrsll rfslahrwsf vfamvalvvl
      541 safsyrfmkq gffpdmvydq lymeyklpeg tnytrvtrdl eeieaylktr pevthvtasv
      601 ggtpgrynlv rnianpslay geliidftsp dalvdnmpei qqylssrypd ayvklnrynl
      661 mfkkypieaq ftgpdpvvlh qladsarsim escpdvylit tdwepqipvl tieydqptar
      721 aiglsrndvs lsllsatsgi pigsfhegih rdniylrcld eqgrpiedld ntqifsslps
      781 lnglltqemm mklktgtlsk delvetlmgt tplkqiskri dvqwedpvvp ryngqrsqrv
      841 qcspvpgiet ekarqsiaaq ieqiplpdgy klqwqgerna stksmqylfk nfpfaiilmi
      901 silimlfkdy rkpiiifcci plvfvgvvav mlltgktfnf vaivgtlgli gmiikngivl
      961 mdeitlqisq gvepvtalid saqsrlrpvm maslttilgm ipllpdamfg slaasimggl
     1021 lfgtlitllf ipilyalffh ikktdk
//
LOCUS       WP_010539372             194 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Bacteroides faecis].
ACCESSION   WP_010539372
VERSION     WP_010539372.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides faecis
  ORGANISM  Bacteroides faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Bacteroides faecis"
                     /db_xref="taxon:674529"
     Protein         1..194
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22418
     Region          19..188
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 medfnlqyaq hpslgllkdf llehgtykil kkkelfsmqg kinskgayik sgafrytcvd
       61 dkgdehivgy afphefvgsl dtwinptqps pvtiealcds eiyyvtypia kqffntnmet
      121 lyircilaer sysviykrll dsyckkteel yldlvnrcsn iqnyitlkei asflqvtpet
      181 ishirkkill nrks
//
LOCUS       WP_010539373             240 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Bacteroides faecis].
ACCESSION   WP_010539373
VERSION     WP_010539373.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides faecis
  ORGANISM  Bacteroides faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Bacteroides faecis"
                     /db_xref="taxon:674529"
     Protein         1..240
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26425
     Region          1..232
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 menkglaiit gasqgigavi akglahdgfq vvliarnikk lekvrdeilq shtqenhepi
       61 ilpmditdni kvdseirkin esfgkidilv naaamfmdgs lseaideyrk imeinviaqy
      121 gilktitnim kkqasgyifn ivsraakygf pnggiygstk faflglaesl yrelaplgir
      181 vtslcpgwvn tdmakqagtp fmddemvqpd dilntiryll nlspnvcikd ivfemkksii
//
LOCUS       WP_010539460             312 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacteroides faecis].
ACCESSION   WP_010539460
VERSION     WP_010539460.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides faecis
  ORGANISM  Bacteroides faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Bacteroides faecis"
                     /db_xref="taxon:674529"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34885
     Region          6..222
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mdepivrveh lshrysvqwa irdinleikk kgvfgllgsn gagksttmni mcgvlnqteg
       61 evfvngislr enpveakkfi gflpqkpply adftvdeylv ycaqlrhmds ksiraavdca
      121 kekcgimhys krlisnlsgg yqqrvgiaqa ivhnplfvvl deptngldpn qiveirhlik
      181 eiavdravml sthilsevqa tcdeikmieh gnvvfsgtir dfnnymapst lvtilenppq
      241 ieelekipgi lkvekltatr frchfdgndh gmtrritemg vekgwrpsei ilerdsldtv
      301 faqlsgkgik id
//
LOCUS       WP_010539426             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter permease [Bacteroides].
ACCESSION   WP_010539426
VERSION     WP_010539426.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 269)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..269
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29405
     Region          6..262
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mdllqytffq hallgsllas iacgiigtyi vtrrlvfisg githasfggi glglfagisp
       61 ilsaavfsvl safgvewlsr rkdmredsai avfwtlgmal gimfsflspg fapdlsaylf
      121 gniltinqad lwmlgilafi ltgffylfir pivsiafdre farsqkipve vfeyvlmmfi
      181 altivaclrm vgivlaisll tipqmtanlf tysfkkiiwl sigigflgcl gglfisyhwk
      241 vpsgasiiff siliyavcki gkscckkqs
//
LOCUS       WP_010539494             564 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Bacteroides].
ACCESSION   WP_010539494
VERSION     WP_010539494.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..564
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=65036
     Region          86..499
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          274..563
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mktknlllgl alsalalqsc nvldidptdt ysestayasi knldlyvksf ygvfysnadi
       61 nvganlamdd gvsdlikysw fnvaegsvnk lfyydnmmsp dgnyrsnwdg myeqirrfne
      121 yfydvhsgfa dkldsdqlai rtaevrfmra fayqelvlrh ggvilrined rvddhnqraq
      181 arsseddcwt fildeyekaa qmlpeewtgs eagrltkgaa ygmkaraaly akrwqdavna
      241 aleveklekk gvyqllsgts kdsymqifnt vnnkelilpv yfqqktkqhm fnhffcppyd
      301 tekaglqpgt lgaaatptde yasafdikvg qewksfdwth lneysegpwg nrdprfyasi
      361 lynganwtgr qlelyvggkd gymdfstsas qdyvrtsttg yifrkfmdes dninyvdies
      421 tsywiemrya eiililseay arldkfkeay dylnkirtrv glpilaqqst wdnyledlsk
      481 ervcelgleg hrwydlvrwd iaqkvlngqr lhgikiektg ssflytrvec dtqdrkfpkk
      541 ynifpipsse lrnnimceqt pswk
//
LOCUS       WP_010539687             221 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Dietzia alimentaria].
ACCESSION   WP_010539687
VERSION     WP_010539687.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..221
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24171
     Region          11..204
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 miplfaavre vavlgahcdd iaigmggtls elcstirglr vralvltgag tpredeeraa
       61 laallpgadl eitvldfrdg rlpaswdrvk dsvaafaras dpdivfaphr ndahqdhrll
      121 aevtptefrd hlilgyeilk wetdtpspsv flpfspetaq rkqqvllahy psqhhhdwfg
      181 dgesfvalsr lrgvqcraph aeafvlekat isftkestcv s
//
LOCUS       WP_010539714             481 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Dietzia alimentaria].
ACCESSION   WP_010539714
VERSION     WP_010539714.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..481
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=51409
     Region          70..452
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mtrpttdprg qavphrprrg kelvlliaaa vivsfslllv qlaqeqelsl sllwitlafl
       61 gltggahlvi rwlapfadpv llpgvallng lglvliyrld lasaaravan gtdppgmdvt
      121 rqllwtligl tvmagvlyvl rdhrvlsryg ytmgfaglvl latpavlpsr fseingaknw
      181 iilpgftiqp gefakilliv ffasilvekr elfttagkrv lgvdlprard lgpiivawfl
      241 slgvlvfntd lgmclllfat vltmlyvate rvswlligvv lvaiggvlay alfghvrvrf
      301 qiwqdpfayf dtggyqssqa lfglasggma gtglgngrpd qvpfantdfi astigeelgl
      361 iglaavlmvy ailvlrgirv gltirdsfgk lvavglaftm aiqlfvvvgg vstlipltgl
      421 tlpfmayggs sllanyalia illrlsndar rplptprqap aladaatgmm rtprlrarks
      481 g
//
LOCUS       WP_010539747             427 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Dietzia alimentaria].
ACCESSION   WP_010539747
VERSION     WP_010539747.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..427
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46171
     Region          2..427
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 myewsetdlm ireavrsfid keirpnleal esgeippypi irklfaefgi dsmaresvek
       61 mlareragas dgsgrgreda ggegsgggaf agqdsmmavv iselarvcmg lvsalgvslg
      121 lgattimsrg tlgqkerwlp givsmekvas waitepdsgs dafggmrtyv rrdgddyiln
      181 gqktfitngp yadvmivyak ldeggsggag kaseedkrsr kvltfvldkg mdgltqgapl
      241 qkmglhsspt gelffndvrl grdrllgese egrggdgres arssftaert gvaimalgii
      301 eecrrlcidy arertlwgqe igrfqliqlk larmevarin vqnmvfhsie raragapltl
      361 aeasamklys seaatdvamd avqlfggngy maeyrveqla rdakslmiya gsneiqvthi
      421 akgllar
//
LOCUS       WP_010539767             187 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase [Dietzia
            alimentaria].
ACCESSION   WP_010539767
VERSION     WP_010539767.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..187
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20162
     Region          23..187
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 middtrdaft dralvtesvd vlyraadtpi gelllaatpr glayvafeve drqevlqmla
       61 arlgsrvqaa paesaildda aaqlldylag drrhfdmpld trlatgfrge vqqhlaeidy
      121 grtttykqla aelrrpgavr avgtacatnp lplvwpchri lrsdgglggy rgglavkqrl
      181 lamesaa
//
LOCUS       WP_010539775             316 aa            linear   BCT 01-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Dietzia alimentaria].
ACCESSION   WP_010539775
VERSION     WP_010539775.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..316
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32032
     Region          58..304
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 msnrvrsata laavvsftvl gafagppala adlspgslsp lptcdgpapr itpfgdaaap
       61 vlgwrenlvf dgrgrmwvsg mlanevvayd pggrrvasvp idspgglalt pegevvvvtg
      121 atptathski fafdpdsarp aprlvttlap gknglavdaa gnmyttglfa ptitkvradg
      181 tvddawsata avggtngivi rdrtayvtvt asvdtvvyei plsnpiaarp hvltrlpala
      241 rglddlavtd dalylagltg geilrvdrwt aapcvlvggi pgptsvrvae gfggygpgdl
      301 fvtsvdgsir hvaigt
//
LOCUS       WP_010539840              72 aa            linear   BCT 01-JAN-2025
DEFINITION  ferredoxin [Dietzia alimentaria].
ACCESSION   WP_010539840
VERSION     WP_010539840.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..72
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=7964
     Region          1..65
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mdihvtddce gygrcaelap evftvpdepd fqttvirpti deeseeelas raiaaiqrcp
       61 vralrtnldv qf
//
LOCUS       WP_010539852             373 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerate kinase [Dietzia alimentaria].
ACCESSION   WP_010539852
VERSION     WP_010539852.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..373
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37282
     Region          3..372
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mtivvacgaf kgsltaveac hhaaegarra hpdvdvlerp vadggggsle vmvasgartv
       61 avtvsgptge mvetsfaaid pdtafvemad acgllrlpgg elrpleassr gvgevllaal
      121 rsgrgnihlg iggsastdgg tgmlsalgvr fldaagnelp dgggalseld rvdldgldpa
      181 vrasrilvac dvdnpllgpl gaarvygpqk gataeqvddl eagltrlvev lrtqglnvdp
      241 dapgsgaagg vgfaarellg asldpgfevl gtltgledvv saaelvvtge grlddqtmhg
      301 ktpmgvaalc rthavpvvav cgrldleadr vaaagfaaaa altekepdla rsmanagpll
      361 edvaaevisr ilp
//
LOCUS       WP_010539912             517 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Dietzia alimentaria].
ACCESSION   WP_010539912
VERSION     WP_010539912.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..517
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55264
     Region          5..514
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtakttaekl aelrvkteea qdpgseraka rrdaagltpp rvridellda gsfvemgqla
       61 kapgdatnpf gdgvvtgrgt idgrpvavya hdntvfggsv geafgkkvca imdfaikvgc
      121 piigindsgg arvqdavtsl ayyseisrrq ypasghvpqi simlgkcagg avyapvttdf
      181 vvavqdqaym fitgpdvikk itgeeismed lgsalvqakn gnvnhvavse heafmyvrnl
      241 lsylpssaae kaplinpgle peptesdlql dsiipdsdna aydmhdvlir mfddgefmet
      301 sgqfapnmit gfarvdgesv gvvanqplhl sgaldidase kasrfmsicd aysipivylv
      361 dtpgylpgvq qeklgiihrg akmgfavvaa svpkvtfvvr kayggayavm gsknlggdln
      421 fawptariav mgaegavdll qrrqieeagp eegpklrkql idmynefiat pytaaergyi
      481 daviepsqtr lvlrgalnql rdkvrnelpr khpiapm
//
LOCUS       WP_010540008             193 aa            linear   BCT 01-JAN-2025
DEFINITION  GbsR/MarR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010540008
VERSION     WP_010540008.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..193
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21528
     Region          7..155
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mdrrspvqra verfgqglel dgiprmparv fafmmiggqe syssrdlarg levsaaaisg
       61 avrylvdarl vireraprgr gdlfrlmdgd vwaeifasrl plidqvnasi ddavailddl
      121 pqsdkapgla klhetreffe fvrndmprml vrwaehkans hseapeetna plpflapded
      181 gattlerrea trr
//
LOCUS       WP_010540023             216 aa            linear   BCT 01-JAN-2025
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme [Dietzia
            alimentaria].
ACCESSION   WP_010540023
VERSION     WP_010540023.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..216
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23452
     Region          12..192
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mrtrrratwq ivhaerrllv adlaalrdeq weqpslcpgw dvhdilahlv dtartgrvsf
       61 vrdlvaarmg fdlanengva rrkrenpqdt laafadattl trtppaalat rvveaivhge
      121 dirrplgiag rypdaaisqa ltyqlrtpvs fgggreradg lrlvdlrtgs twgngedvta
      181 daldllltvs grsvdrstls gpgasrllta qtdhds
//
LOCUS       WP_010540026             302 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010540026
VERSION     WP_010540026.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32115
     Region          8..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          102..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,223..228,
                     234..235,237..238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mttewpdlsa lelllaider gslgaasrel giaqpnasrs lrrlekqlgl tlidrrargs
       61 qltaegtvia hwassvltes rhllhaaqgl haenestial casmtvaehl lpgwlgrlrs
      121 hhpglgvrle vqnsatvcqr vfdkgcdlgf ieapevpgnl hsavvardel vvvvtpdhpw
      181 aarsaplrat dltstplvvr eagsgtrttl dtaltevgrv qpllelgssa avrsavlgga
      241 gpavlstlav aehltkgdlt ripvedldlr rslhavwrge rvvtgaagdl mriahdelvr
      301 sr
//
LOCUS       WP_010540045             531 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Dietzia alimentaria].
ACCESSION   WP_010540045
VERSION     WP_010540045.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 531)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..531
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56201
     Region          59..530
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mklavttlaa laltltacgg ggdtattasd redaqapaea grcteekagg titmgefvml
       61 psfapgqgny gvrgaaesaa vfdrlmrwdp qaqefapkla eslesaednt kwtlklrddv
      121 rfsngdplta ddvaftiglh knpatrsvvm tdamqvkdtk vvdpqtveft ldepwsgfpi
      181 llagaagevi pqkayeaasp eewarnpiga gafvmdsytp nqevvlkpnp dyyggpvcps
      241 lrfinipgsq gtfdafqtge lqaaflrnak fvsmakdadv agfeevsssg svvnmnsgng
      301 gydgiltder arqavayald rdlynqrvtg gkgqatssll aessrfydgq eglefdldka
      361 rtmvdelkae tgwdgsltll igdspevves gvvikamlds agfdvtiqna pisqvtarqf
      421 tgdyeivmgg latsdadpva afasgmtpgg atnltgvddp elteaitelk aadeleaqke
      481 afgklqevyn rvmpftvvan aemfvaiaes vkgveptmss tmlfdgayie k
//
LOCUS       WP_010539807             274 aa            linear   BCT 01-JAN-2025
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme [Dietzia
            alimentaria].
ACCESSION   WP_010539807
VERSION     WP_010539807.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..274
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28633
     Region          35..247
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 migrltrdrm ldaleaqvgl iryalvgdgs gpevdlatpv pscpdwtvhd lvahigtanw
       61 wgganvrdan pdarargmra vmesappate gaaalagwya dlavdaleiy tdgdpddpaw
      121 tfagpgragy wmrrqlhetv ihrwdlekal qgssgttpls edvavdtvde fctsmrplma
      181 llsgelpatl rvramlqape glasgaepvg aldpgsdlew vlpgadgape avvtgppetl
      241 alllwgrvda dapglevtgd raaldavlea glta
//
LOCUS       WP_010540047             412 aa            linear   BCT 01-JAN-2025
DEFINITION  8-amino-7-oxononanoate synthase [Dietzia alimentaria].
ACCESSION   WP_010540047
VERSION     WP_010540047.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..412
                     /product="8-amino-7-oxononanoate synthase"
                     /EC_number="2.3.1.47"
                     /GO_function="GO:0008710 - 8-amino-7-oxononanoate synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_process="GO:0009102 - biotin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42227
     Region          22..389
                     /region_name="PRK05958"
                     /note="8-amino-7-oxononanoate synthase; Reviewed"
                     /db_xref="CDD:235655"
     Site            order(117..118,121,184,213,216,245,248)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:99742"
     Site            248
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99742"
ORIGIN      
        1 mpdhppttpg rscegqirst sldwldaaaa drharhlhrv lrprgpgddv idlasndylg
       61 lgthpevvhg aieatrrfga gatgsrlvtg ttadhqales elaaftghps alvfssgyta
      121 nlgavvalsg rgslivsdgg shaslvdacr lsrarvvvve rgdtiaveqa lagrsearal
      181 vvtdsvysad gdlaplaamh aaceqhgavl ladeahglgv rgvgghglvh elgltrhenv
      241 vvtatlskal gaqggvvlas qrvrdhlidt artfvfdtgl apasvgasra alavlrrepd
      301 rarrvlevae rlasvtgaqr pssavvsvil gdaerafsas qrcaelglrv gcfrppsvpa
      361 gtarlrltar adlsdaelat acevltqvlg ehgrghhvad stlagaaaga pa
//
LOCUS       WP_010540052             177 aa            linear   BCT 01-JAN-2025
DEFINITION  CAP domain-containing protein [Dietzia alimentaria].
ACCESSION   WP_010540052
VERSION     WP_010540052.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..177
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=19335
     Region          44..175
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
ORIGIN      
        1 mcstlarhaf aavaavatta alatpvagaq sfsfeittap rcdsaspaev eelvteihee
       61 tnrereaagq npvkrldsld diaqtwssqm anenrmyhnp nirdqvstty pgqwrsygen
      121 vlqnwcgktg kdlvtqwmns lphrlnlinp ahthlgvgva vadnkklfat qnfvslr
//
LOCUS       WP_010540079             234 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010540079
VERSION     WP_010540079.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..234
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25795
     Region          21..233
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtidrrtdqs addvltragi fqgvepaavs alrsdltree yskgdviire geqgdslyiv
       61 tsgkvklsrk spdgrenlls ilgpsdmfge lsifdpgprt ssavcvtdvt vqamdrsalk
      121 rwiaerpeis dqllrvlarr lrrtnnnlad liftdvpgrv akallqlaqr fgtqeggnir
      181 vthdltqeei aqlvgasret vnkalaefah rgwlrlegks viisdterla rrar
//
LOCUS       WP_010540046             266 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent dethiobiotin synthetase BioD [Dietzia alimentaria].
ACCESSION   WP_010540046
VERSION     WP_010540046.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Schneider,G. and Lindqvist,Y.
  TITLE     Structural enzymology of biotin biosynthesis
  JOURNAL   FEBS Lett 495 (1-2), 7-11 (2001)
   PUBMED   11322938
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Schneider,G. and Lindqvist,Y.
  TITLE     Structure of ATP-dependent carboxylase, dethiobiotin synthase
  JOURNAL   Methods Enzymol 279, 376-385 (1997)
   PUBMED   9211290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     gene            1..266
                     /gene="bioD"
     Protein         1..266
                     /product="ATP-dependent dethiobiotin synthetase BioD"
                     /EC_number="6.3.3.3"
                     /GO_function="GO:0004141 - dethiobiotin synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0009102 - biotin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26438
     Region          15..224
                     /region_name="BioD"
                     /note="Dethiobiotin synthetase [Coenzyme transport and
                     metabolism]; COG0132"
                     /db_xref="CDD:439902"
ORIGIN      
        1 msaeagsgaa daapvivtgt gtdvgktiat aamaalgrsa gldvgickpv qtglwpgepg
       61 dvheaarlag vgrvlevrrl tdplapetaa rlagvpqsta gelldpirsw lgavgapspt
      121 gphsggparl dlieaaggll vrlgtgltvl dlaaaldapl vvvaraglgt lsdteltvra
      181 iesaglrcag ivigawphep glaencnled lprltgvpvl grvpcgaggl spiefarrap
      241 gwfrpdvlad lragdlgtpg vtmspr
//
LOCUS       WP_010540145             442 aa            linear   BCT 01-JAN-2025
DEFINITION  amidase [Dietzia alimentaria].
ACCESSION   WP_010540145
VERSION     WP_010540145.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..442
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45535
     Region          6..439
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mttdpltaie taekvragai rasatldaav ervadldptl raftsllhae sraaadavda
       61 mgqeqrerlp lagvplaiks tvtpdnpava pllaagavpm gmtaapqlct wgmtdseahg
      121 itrnpldvsr spggssggsa aavasgmvpl avgddgmgsl ripaaacgla tikpgpgvvg
      181 tslsggnwgg maesgplart vadvalalsv magrpelagi dhvpggtrig lsvaspirlg
      241 rdlvrihepw kraareaaai lrgddlvvvd tplpspkdpv lylarwtsav araaedenlp
      301 lsamerrtrh hallgrtvfr nggadggdtr wnrgvaalra dveramdsag vdvwltpala
      361 dvppeatewh rrswgrslwa smryspftpl anvlgwpams vpcgathspl grvlptsvql
      421 vgrpgseatl lglaavierg gr
//
LOCUS       WP_010540187             239 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010540187
VERSION     WP_010540187.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..239
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25544
     Region          11..229
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtssdpavdl dpvirestpa liaralrrav sdgtfppgaq mgeaalarsl evsrgplrea
       61 mqrltqegll vshrnrglfv adltpeaved mylmrttiet aaldrvldlg lgqetarald
      121 aavdamaala deprstamve adldfhhalv eaarsprlsr vhetvlvets mclhamsgty
      181 sdagsrlteh raiadavrag epvvaknllv ehmrdghdrv rsggahsdag vtarsrlvr
//
LOCUS       WP_010540131             285 aa            linear   BCT 01-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Dietzia alimentaria].
ACCESSION   WP_010540131
VERSION     WP_010540131.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..285
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30859
     Region          15..238
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 maeltrvhas apmatitdal leqgavlvee llepdllfrf naeldqhlte sahgaergfv
       61 negvaaffgn rtehlaglaa ksqvfateil thpiyravcd evllpncaay qlnlghvlnr
      121 gpggtpqmlh rdeevwsqlp sprpniqlas vvalrdfted ngatrvvpgs hlwdrdrqpt
      181 eaeivpavmk agsgiiylgs tihaagantt adqwrrgmhi syclgwlrte enqylsiple
      241 qarqlpresl ellgfgvhda iadgggyvgt vdladpvelf aagkl
//
LOCUS       WP_010540162             884 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Dietzia
            alimentaria].
ACCESSION   WP_010540162
VERSION     WP_010540162.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 884)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 884)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 884)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..884
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..884
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=96594
     Region          1..809
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mferftdrar rvvvlaqeea rmlnhnyigt ehillglihe gegvaakale slgisleavr
       61 sqveeiigqg qqapsghipf tprakkvlel slrealqlgh nyigtehill gliregegva
      121 aqvlvklgad ltrvrqqviq llsgyqgkea eatgapagag gresgtpsss tvldqfgrnl
      181 tqaamegkld pvvgrakeve rimqvlsrrt knnpvligep gvgktavveg laqaivnnev
      241 petlkdkqly sldlgslvag sryrgdfeer lkkvlkeinq rgdiilfide ihtlvgagaa
      301 egaidaasil kpklargelq tigattldey rkhiekdaal errfqpvqvp epgvelsiei
      361 lkglrdryea hhrvtitdaa laaaaqladr yindrflpdk aidlideaga rmrikrmtap
      421 pdlrefdeki aearrekesa idaqdfekaa glrdtekkli aerserekqw ragdmdvaav
      481 vdeeqiaevl gnwtgipvfk lteeettrll rmeeelskri igqdeaikav srairrtrag
      541 lkdpkrpsgs fifagpsgvg ktelskalan flfgeddali qidmgefhdr ftasrlfgap
      601 pgyvgyeegg qltekvrrkp fsvvlfdeie kahteiyntl lqvledgrlt dgqgrmvdfk
      661 ntvliftsnl gtrdiskavg mgfqssdnte dayermkqkv ndelkkhfrp eflnrideiv
      721 vfhqltqeqi vqmvdlmvsr vgvalkakdm tievtdrakq llakrgfdpv lgarplrrti
      781 qreiedtlse kilfgevaag elvsvdvegw dgesdktena kftfsgaprp dgdkserege
      841 eitasvaptg eagpgdslpp ssggfgggst ggpagsggaa pats
//
LOCUS       WP_010540217             253 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010540217
VERSION     WP_010540217.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..253
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26923
     Region          4..208
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mteppaspvd rafdvlrvta agngltlsei sretrlakst tlrllvsler ngavtrigqr
       61 yrlgplvhel dpipaspaye rirrvltpfl ahlfeatrat vhlatmhrde vvylnklhgp
      121 rpipspsrig gglpayctgv gkamlafdee aasrvalgpm vawtdttvts aaelamelad
      181 irrrrraldr aeltpglycv aapvfdddeg gggetravaa lsasasdesa larleplvar
      241 vaaaagrala edr
//
LOCUS       WP_010540230             381 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Dietzia alimentaria].
ACCESSION   WP_010540230
VERSION     WP_010540230.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..381
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39156
     Region          15..372
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtapttpass pgvdteeqsa lrqsvaslla kksdseavra amnsadgydp alwstlveqi
       61 gaaalsipek hdgagatwve thlvceelgr gltpspmlgs avlaaqavla sgdadaaarl
      121 lpgiaageqi alcwagldgw avpgvraegt tltgtahhvl gadtastllv vavagetval
      181 ydvpadaagv tvtrvpvmdp trtlsrvefd gvtataigtr dsflsrlraa awaaisaeqv
      241 gaaravldat vqytqerkqf grvigsfqal khrmadmyvk aetarslsys aaalvaeaqa
      301 lgdgpeadaa ayaaeieaaa akvycsealq witgesiqlh ggvgitweyd shlyfkrahg
      361 taqllgqphe ilsalevaag l
//
LOCUS       WP_010540388              89 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Dietzia alimentaria].
ACCESSION   WP_010540388
VERSION     WP_010540388.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..89
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9813
     Region          3..73
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 martgarpyr rnrarilagn pvctecgqpi dtsitdqydp gyptadhkvp ysrggtdald
       61 nlapmhrgcn lakhskphsn lirrsrdwv
//
LOCUS       WP_010540477             701 aa            linear   BCT 01-JAN-2025
DEFINITION  M3 family metallopeptidase [Dietzia alimentaria].
ACCESSION   WP_010540477
VERSION     WP_010540477.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..701
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=76888
     Region          8..688
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 mtppssetsp hplldesplp yglpdfaaid dadlepairt aiddhaaeia avvdnpeppt
       61 ventvialer sgqaldrvls tfygllgpda tparrdvdrv vspllaahhs avmtdpglya
      121 rvdalhsale agsldvadet arlvrrhhrd flragaaldd eararltaid trlaelttlf
      181 genllastse lavsvtdeae ldglpdsmrs tlaataadag regwliplgl ptvqpisawl
      241 dheglrrrvm easlrrgstp dhdngpivle ivrlraeras llgltchadh vlavetagtp
      301 daargllldv vdaavtnarn eakdllgged relnpadwaw eserlrserf rvddatvrpf
      361 felervlrdg vmhaasslyg lrfvdrpdlt gflpdvrvie vfddvrserd agiglllldy
      421 yarptkrgga wmssfrdqsr lldsrpvvvn vmnlarpaag eptlltmdev ttmfhefgha
      481 lhgllsdvey pvfsgtsvpr dfvefpsqvn emwarrpevl enyarhvesg esidedlver
      541 mreerfgegq atveylaaal ldlawhslsl eearavtdvd efestvlaea gldvpgiepr
      601 yrsryfqhif aggysaayys yfwaevldad aaewfaergg lerssgdamr revlsrggsi
      661 efleayrrmr gsepspaall rrrgldssvv ggreaaaaar t
//
LOCUS       WP_010540550             325 aa            linear   BCT 01-JAN-2025
DEFINITION  carbohydrate kinase family protein [Dietzia alimentaria].
ACCESSION   WP_010540550
VERSION     WP_010540550.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..325
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34386
     Region          2..294
                     /region_name="ribokinase_group_A"
                     /note="Ribokinase-like subgroup A. Found in bacteria and
                     archaea, this subgroup is part of the ribokinase/pfkB
                     superfamily. Its oligomerization state is unknown at this
                     time; cd01942"
                     /db_xref="CDD:238917"
     Site            order(52,254,257)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238917"
     Site            order(195,223,252,255..256,259,281,284)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238917"
ORIGIN      
        1 mpvvitgsia sdhlmnfsgr fseqllpdql ahvslsflvd slqirrggvg gnisfalgvl
       61 grepylvgaa gedfaeyrdw lechgvdcsa vhissalhta rfvcttdsem aqlasfypga
      121 mgeaatisla rlverigrpe ivligandpt amnshtaecr elgldfaadp sqqlafldgd
      181 asaalvegar ylftneyeyq lllnktgwta deldskvgtr ittrggkgvv ivekgaepie
      241 vgvvpsdnll dptgvgdafr agflsgvldg lslersaqfg aliathvlet tgtqewtidp
      301 vaarrrlaat ygdeaaeels allpa
//
LOCUS       WP_010540619             731 aa            linear   BCT 01-JAN-2025
DEFINITION  acyltransferase family protein [Dietzia alimentaria].
ACCESSION   WP_010540619
VERSION     WP_010540619.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..731
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=78641
     Region          28..396
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          496..709
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 matpsppepa ergrgttwlq tvtvwrkpgk mayrhdidgl rglaiglvvv fhiwmgrvsg
       61 gvdvfltlsg ffflgsllrg adnpatslnp lphlqrlirr lypalvvtia atvlgtvlik
      121 pptqwsaife qtvasllyyq nwelastasd yaaadatisp lqhlwsmsvq gqfyvvllav
      181 ilgftalwrl iirrgspkwp lvvivaasta asvwwsilgq aanqqlnyyd taarmwelli
      241 gglvaillag ivlpwplrwi atvaglflvv stgfffdgaa yfpgpmawyp iggalliilg
      301 gnlppgerat pakdpvswll sakafrrlgd isyslylwhw pllilwlssd reaeitvtsg
      361 ltiiaisivl alitekyver pirmasrarg nktpaaiard mrdsgpkrsv leqrrfvgat
      421 alvvvaavas lgtvgwwsat agsrssvpyi dsltdpdhpg araylegipt pdapyvpsli
      481 qvandlpast ldgcisdfes sevemcvygd tasprtialv ggshaehwis gldevgrhyg
      541 frvvtvlkmg cpltldatvs ddgeiypsct ewtpralaal aglapdfvft tatrpvgvvg
      601 pdfaprqyvd lwraldqqgi gviavrdtpw lnngrgpira gdclgdggtp aecgmprels
      661 ispvnpasla gagidslrll dltdglcnpv ncpvvvgnvi vyhdshhlsg swvrsasgel
      721 arqmgpatgw w
//
LOCUS       WP_010540586             500 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase [Dietzia
            alimentaria].
ACCESSION   WP_010540586
VERSION     WP_010540586.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..500
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=51142
     Region          2..496
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 midltlgeia givggrlvgg epstavtgsv efdsrrlgpg glflalpger vdghdfvara
       61 idagaaaalv arevdgvdga qivvpavdrr etnamalaad tdgsgaavlt algalarasv
      121 drlvadhglv vvgvtgssgk tstkdligav lsakgtvvap pgsfnneigh pwtalradet
      181 tdflvlelsa rapgnitela aiapprvgvv lnvgtahlge fgsrdviaat kgelvealpp
      241 ramggvavln adddrvsama prtsaevvtv ghdgsadvra edvrlddevr atfrlitpqg
      301 dadvalrvhg ehqvgnalsa aavglacgme veqiaaalgt aeaaserrmd vrvtadgvtv
      361 indsynanpd smraalksla vmarsggrpr rtwavlgemg elgddsvieh dlvgrflvrl
      421 dvsqlvvvgi grpqramfqg aiqegswgse adhvgsaeea maildervep gdivlvkasa
      481 avglwsvaeh llaargeeks
//
LOCUS       WP_010540648             229 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L family deacetylase [Dietzia alimentaria].
ACCESSION   WP_010540648
VERSION     WP_010540648.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..229
                     /product="PIG-L family deacetylase"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0000225 -
                     N-acetylglucosaminylphosphatidylinositol deacetylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006506 - GPI anchor biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24633
     Region          14..139
                     /region_name="PIG-L"
                     /note="GlcNAc-PI de-N-acetylase; pfam02585"
                     /db_xref="CDD:426852"
ORIGIN      
        1 mssstalpfw dhvlavvahp ddesfglgat isafvasgat vdvlcltrge astlqgiegd
       61 lsrirehelr sagdalgvrs vdlrslpdgg lhdlpepvld aevrqsvaat rpdgiitfdt
      121 tgisghpdhl aathaairva dsdelpvlaw tlpdeicgtl adegftgfrg rpmsevdvil
      181 tvdrtaqraa vdrhpsqavp gsvlwrrlel qgdtehlrwl rrpyeqrrp
//
LOCUS       WP_010540653             266 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Dietzia alimentaria].
ACCESSION   WP_010540653
VERSION     WP_010540653.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..266
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=29690
     Region          81..208
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(86,88,142..143,146)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            88
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(141,189..190,192..193,197)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(147,152..153,185,188..189,192..193,196,199)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(170..172,185..186,189..190,193,197,200,204)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(170,190,193,197,200,204)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(198,204..205)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          224..261
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
ORIGIN      
        1 madrigtlln rsgdggeevl ivsrgsvrtr frrrdelgwn frvestdsen vvernpkrkp
       61 rtdpkpkpkp arrvsrprgq rvayvrvsaa dqnearqlea vgecdrvyie kqsarsradr
      121 vklaeciryl rdgdelvvas mdrlarslvd lkqivgeita kgasvefvhe ratyaagaqd
      181 pradlmlsll gafaeferai irerqaegia iakkkgkykg rkrvlteeqi dkargrieag
      241 egpsaiardl gvgrstlyra lqrhat
//
LOCUS       WP_010540677             214 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010540677
VERSION     WP_010540677.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..214
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23626
     Region          19..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mirnsgngga pspdaedvrl ievaasifae rgikgtstdd iahaagvtrv tlyrrlgpkd
       61 eihraiyahe aqrlmktvns rytpfeslew dpvrhvenll vgtvfdirqs ellrrlievd
      121 kveamavlag qsdtvlggit eimadfvrrt waadvhtrpm dpeeaetlsr evggvvgrfl
      181 hslvvmpdgp plvdseeeir alarrvlvpm ilqr
//
LOCUS       WP_010540678             432 aa            linear   BCT 01-JAN-2025
DEFINITION  SPFH domain-containing protein [Dietzia alimentaria].
ACCESSION   WP_010540678
VERSION     WP_010540678.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..432
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=46323
     Region          3..306
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mggliflavi viliasvvvs svklipqaea avierlgryq rtvsgqlali ipfidrvrak
       61 vdlrervvtf ppqsmitedn ltlsidtviy fqvtdpksav yeinnyiiav eqlatttlrn
      121 vvggltleqt ltsrdminkq lrgvldsetg rwglrvarve lrsidpplsi qdsmekqmra
      181 drekratilt aegqreaait taqgakqaai ldaegnkqas ilnaeadrqs rmlraqgera
      241 arylvaegqa aaiarvnaav kaskptpeml ayqyvqnlpe makgdaatmw mipsqfgdsl
      301 enfakavakk dddgvfryep sevdanadlp aapdewfdts tdpeiarsva aaeaaargta
      361 taydepgskp kpkpgvfdmv peseggiapd spasppgaqq qetpaidgpq ggspggfeqg
      421 gypiegggqh hr
//
LOCUS       WP_010540694             131 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010540694
VERSION     WP_010540694.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..131
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14415
     Region          12..115
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(12..14,28,45..47)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(59,62,66..67,76,99,103,109,113)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 msepnggeqt ikigevaert glsirslrhw devglvspsv hspggfrlyt gadverilli
       61 rrmkplgfsl ermgefcral daraasddaa sdppaadvit evraeaterl erlrrhlaya
      121 eefveiverl g
//
LOCUS       WP_010540705             218 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Dietzia alimentaria].
ACCESSION   WP_010540705
VERSION     WP_010540705.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..218
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=24009
     Region          29..214
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mqnaqidqta agtaaadtvt adtgavlced glrrppwaar dpllreyydt ewgipvrdea
       61 glferlvleg fqsglswvti lrkrpafrea fagfspdava afeeqdiarl maderivrnr
      121 rkinaaiana ravialredg glaeliwsyr pehtpaprtm ddvpsrspes ealakelkrr
      181 gfsfvgpvtv falmeaigvv dthlvnshrr gtsgvwqh
//
LOCUS       WP_010540761             255 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Dietzia alimentaria].
ACCESSION   WP_010540761
VERSION     WP_010540761.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27319
     Region          20..236
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mttqsepdqq pdaaapaaia tdlvmtygeg etevraldrv satfqrgrft aimgpsgsgk
       61 stlmhcmagl drptagsvri gdteivglpd kqltalrrdr igfvfqsfnl vptltaeeni
      121 tlpqdiaghr idrdwfdevi grlgigdrls hrpselsggq qqrvacaral vgrpdilfgd
      181 eptgnldsts saevlsilrs aaddfgqtvv ivthdpraat yadrvlllad grlvrelehp
      241 tadeilaamg aleeq
//
LOCUS       WP_010540870              98 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Dietzia alimentaria].
ACCESSION   WP_010540870
VERSION     WP_010540870.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 98)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 98)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..98
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11208
     Region          7..92
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 maagtslklv hntdrdrfel wdddeflglv gyemdgdvfi llhtvieehy gqqgiarllv
       61 slvltrmrld gskirpvcsy vrrfltrfpe yqllvaah
//
LOCUS       WP_010540523             243 aa            linear   BCT 01-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Dietzia alimentaria].
ACCESSION   WP_010540523
VERSION     WP_010540523.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Rigden,D.J.
  TITLE     Ab initio modeling led annotation suggests nucleic acid binding
            function for many DUFs
  JOURNAL   OMICS 15 (7-8), 431-438 (2011)
   PUBMED   21348639
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446337
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..243
                     /product="zinc ribbon domain-containing protein"
                     /calculated_mol_wt=26341
     Region          3..241
                     /region_name="DR0291"
                     /note="Predicted nucleic acid-binding protein DR0291,
                     contains C4-type Zn-ribbon domain [General function
                     prediction only]; COG1579"
                     /db_xref="CDD:441187"
ORIGIN      
        1 mkadptlqrr lvdladldlr laglshrrsa lpeqatvddl eaqrrgaves aararihved
       61 ldraiaklrs dldavrrrra ndadmlatgg iserqasele yelrslvrre galegelael
      121 eerleavnad vrhsgalitd ldarlgmart vrdtalaele davtettger arsaedipad
      181 lldlyvrsae ssgvgaailn ggrcsacamd ldrrtisvfr sapkdevltc pecgvivvrt
      241 dns
//
LOCUS       WP_010540892             158 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Dietzia alimentaria].
ACCESSION   WP_010540892
VERSION     WP_010540892.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167397
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..158
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17096
     Region          11..>117
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cd07812"
                     /db_xref="CDD:176854"
ORIGIN      
        1 mttepataga iessieidap parvwevise vrnatqwssq avkvialggr ttkgtralni
       61 nrrgplfwpt tsrvvefepg rrfgnqisen gtvwvfelea lpgartklte rrevpaglst
      121 vskvltdklf ggqtsftaem gegvslslqr iktlierg
//
LOCUS       WP_010540919             201 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Dietzia alimentaria].
ACCESSION   WP_010540919
VERSION     WP_010540919.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..201
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21698
     Region          2..162
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkliyyvav svdgfiadps ggfddflveg dhmpwiiehy petipghlrg pvglaqtphr
       61 vfdtvimgrt thqvavdggl asgyphlrqy vvthrpgdlp aeegltasde dpvtlvrrlk
      121 sedsplhiwl cgggtlagqv vdeidefqlk vnpvmlgagi plvaratges ggsgvalpra
      181 ltrrtrrdfe sgvsyveygr n
//
LOCUS       WP_010540988             180 aa            linear   BCT 01-JAN-2025
DEFINITION  Dps family protein [Dietzia alimentaria].
ACCESSION   WP_010540988
VERSION     WP_010540988.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..180
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=19217
     Region          4..158
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mtkftvpgls vedstplakt lqkrltacnd lhltlkhvhw nvvgpnfiav hemldpqvel
       61 vrgfadvlae riatlggspv gtmganadhr swddyslgrd talahlgald kvydgmisdh
      121 rkaitmagkv dpvtedilig qtaelekfqw fvrahlenss gslptaddss ekgaagsata
//
LOCUS       WP_010541024             207 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010541024
VERSION     WP_010541024.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22046
     Region          19..138
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meresrtseq ataarptgrd evrsavlrea rrlfsergpr vplreiadaa gvnpglihrh
       61 igrkdallta vmqdavrfga arlehaddag aavrgmllga sshpeisrll awlavdpesa
      121 fppmvdpsqr paaalrrmes pppagdvell laftavyawp vlretlldal dipagsrddi
      181 deqladllgr vvtgasarsn sdptgpa
//
LOCUS       WP_010541038             803 aa            linear   BCT 01-JAN-2025
DEFINITION  arylsulfatase [Dietzia alimentaria].
ACCESSION   WP_010541038
VERSION     WP_010541038.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..803
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=87474
     Region          61..570
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(71..72,109,167,169,262,370..371,431)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(71..72,109,167,169,262,371,431)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 mqvtngdhqn epgsahhnsg ahfdrhvlpa rrlagrtpae mdrrhqqdaf pgaeqvrape
       61 gapnillvml ddvgfgtssa fggpcrtpti erlardgagy trfhttalcs ptraatltgr
      121 nhhsvgmgvi sematrapgy tgvrpdsaat varvlrgngy atgafgkmhq tppwettaag
      181 pfdrwpteeg fdtfygflga eadhfvpvly dgrrqvdppr tpeqgyhlte dlvdraiqwt
      241 delgsvapdq pwfcylpfga vhaplhvpea yrdrysgefd dgwdelrtrt ltrqkelgvv
      301 pedtelgpwa pglphwdeld ddderraaar lmelyagfle htddqvgrmi dhlqatgalq
      361 ntlvlymvgd ngasteggrl gafnylagln gipattaeil enwdslggpg syphfpsswa
      421 lalntpyqwa kqvashyggt rnglvahwpg riaepgrlrq qwhhcvditp tileaagipm
      481 phtvdgvaqk plegvgmtyt ftepdapdrh ttqyfeifgn rgiydhgwta vtvqrapwlm
      541 atggvdltpl sestwelydt ssdwsqsrdl aaehpeiler lklkfvaeaa rydvlpldds
      601 tvgrqsgren rpphpmsgrs sitlyphmdg lnekagpklf nrgfllsasl dvtgpgpceg
      661 vlmslggrfg glalylldgv pvfeynffgr ahgravgvdq lqvgthtvel efgydggiaa
      721 gadlrlfvdg tqvgsgriav tapamfsmne tldigrsrgs avstayegaf pvrgavlhhv
      781 rvdlqrgdel pkaqrdgial ath
//
LOCUS       WP_010541050             312 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010541050
VERSION     WP_010541050.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..312
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33093
     Region          7..290
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mrheptsrvl aviealatdg pplplteiar kvdasrstlh avltgmqaeg waervdggwr
       61 agprlrqvga slaaevdlvr aarqpledlv dstgiaavvf eirdgmaevv dsvgagmrta
      121 srevmpvghv vplrapfare laarfpmaeq rhwfaesagl ttaarerlef vlpqiarrgw
      181 sierltparr ellrmadsle asgvgslvrd rvselfvels eidvtdselt tvadlavasv
      241 aapilradgr avgsvavapg rrmtgravvr aveavtgcad avsarlasrp gfgrasdlpa
      301 hlvhpahasr aq
//
LOCUS       WP_010541057             354 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Dietzia alimentaria].
ACCESSION   WP_010541057
VERSION     WP_010541057.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..354
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=37163
     Region          32..312
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 msdrditdkp apgtdpdagk pespstlkgg awkiglkraa gefsrdsctd laagltyfav
       61 lslfpallav vsllgvfgqg aatvdavmel legaapeetl aairgpidsl vntpaaglal
      121 vtglagalws asgyvgafar amnrvygvee grpfwklkps mlvltavlvl licvaglllv
      181 vsgpiaawvg dliglgdtav mvwgiakwpv lilvvvvila vlygfapnvk qpkfrwvsvg
      241 aivallvwgv ataafvtyvs nfgsynatyg slagvivfll wlwitnnafl fgaevdaeie
      301 rarelqaglp aeeviqlppr dttasdkaed klqqtlddaa dvrrdaqaeq arnr
//
LOCUS       WP_010541063             188 aa            linear   BCT 01-JAN-2025
DEFINITION  YdcF family protein [Dietzia alimentaria].
ACCESSION   WP_010541063
VERSION     WP_010541063.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..188
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=20091
     Region          30..169
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mrvrgvrvlr gmtmavaaav vvsalaltaw gvfllqprgd dpvradavvm lagaddgrhl
       61 yardlveagy adtllvsnpg gnsevvarrl ctglsrpada evvcfspdpr ttwgearava
      121 aiadargwer vlvvtnkpht lragtwmrsa tgldvrmtpi etvdwamlpv hlvweaagwv
      181 kggvnshw
//
LOCUS       WP_010541074             251 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Dietzia alimentaria].
ACCESSION   WP_010541074
VERSION     WP_010541074.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..251
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26748
     Region          1..229
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtpppeiair ahglrktysh grvevraldg vtvaidkgrw tavmgpsgsg kstlmhclag
       61 ldtpdrgsvt igstevtrls dagrtrlrrt rvgfvfqsfn lvpvlsvren ivlpvrmafr
      121 rpdrtrfddl vgelgigdll rrrphelsgg qqqrvaiara llprpdvvfa deptgnldse
      181 sgeavlkllg acaretgqtv vmvthdanaa ahtdtalvla dgriadevss ptaeavdaam
      241 rslsgrrsat a
//
LOCUS       WP_010541093             390 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Dietzia alimentaria].
ACCESSION   WP_010541093
VERSION     WP_010541093.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..390
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40370
     Region          26..389
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mpdrptrvlp taaaeepvla aelactivdr rvdldlpvpt grrlalvgpn gagkstalsl
       61 laghlrpdsg evrleggvvs sarthlpahr rrvvaleqsp glfphltala nvaygprarg
      121 vgksdslara rteldavgcg dladrrphql sggqaqrval aralavdpel vlldeplaal
      181 dvevapamrr llaerlasrt vvmvthdpld lwalandvav isgggviqag tvedvlarpg
      241 sefvarlagv slvegevvdp dqlrtpagda viglrsegtd agwrpgargv atidpravav
      301 yarpdssdpa tpgtlpadrt ptasprnswq arvvgltpsg altrvttelr dgqrvdaeit
      361 srsaaalala pgagvtlvvk atqislypra
//
LOCUS       WP_010541146             508 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase [Dietzia
            alimentaria].
ACCESSION   WP_010541146
VERSION     WP_010541146.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..508
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54107
     Region          7..492
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(64,66,70,73,77,110,113..114,123..130,135,138,141,
                     234,238,241,244,246,428,430..431,433..434,437,440..441,
                     443,445..448,457,461,463,477,484..489,491..492)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(150..153,161,176,179,209,226..229,232,250..252,284,
                     393,395,421)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(153,250,281,284)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 msdlrqiehy ingkrvaatg grthevlnps tgkaqavvpl astaevddvi akaavaqkgw
       61 aalnpqkrar vlmrfvdlvn qnmdelaell aiehgkttpd argdvqrgle viefsigaph
      121 llkgeftena gtgvdvysmr qplgvvagit pfnfpamipl wkagpalacg nafvlkpser
      181 dpsvpvrlae lfteaglpdg vfqvvhgdke svdailnndt ikavgfvgst piaqyiyena
      241 artgkraqcf ggaknhaiim pdadldqvad allgagfgsa gercmaisva vpvgegtaea
      301 lleklipkvk alkvghshdp qsdygplvtp eskarvldyi dqgekagadi lidgrgvgay
      361 tgefngedis egyyvgptlm dnvttdmsvy tdeifgpvlt ivraadfeda lrlpndheyg
      421 ngvaiftrdg daarefvsrv evgmvginvp ipvpiayhtf ggwkksgfgd lnqhgpegik
      481 fyskvktvtq rwpsgikdga efviptmd
//
LOCUS       WP_010541150             478 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Dietzia alimentaria].
ACCESSION   WP_010541150
VERSION     WP_010541150.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..478
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50343
     Region          29..451
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(41..42,45..46,49,88,155..156,158..160,163,183,
                     186..187,190,283,286..287,290..292,295,323,327,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtttnlpagd sapqspnlpp vqqktslakv aaassigtti ewydffiygt aaalvfptlf
       61 fpgqdpatat lssfatfava ffarpvgagv fghfgdrigr kralvwtlmi mgvatvfigl
      121 lpgyetgafg afengigima pillvacrff qgfavggewa gatlltaeya pvgkrgmmgm
      181 wpqlgvafaf flssgtfllf sliagdgada nspfmqygwr ipfllsavlv lvglwirisi
      241 eetpvfkqdq araetgvvvk ktlpfadavr yqwreiliag galtslfslf ymgtsfltny
      301 atknldhsrp fvlgmgmvaa lvfggaiais amysdrigrk kvigtsvala mvwalfvfpi
      361 ldtgspiafa vvllvtlvif giaygpagal lpelfqaryr ytgaglgynl agilggalpp
      421 laaaamvaag ntlgvgimls llsamsmlcv vamsessknv mhadaqited rvlatevp
//
LOCUS       WP_010541228             175 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase [Dietzia alimentaria].
ACCESSION   WP_010541228
VERSION     WP_010541228.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..175
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18909
     Region          3..155
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(6,23,28,61,97,103,116)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(8,15,45..47,68,98..101)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 msvrmvwaqa rggvigdgsd mpwyipedla ffkkatlgsp vlmgratwds lperfrplpg
       61 rrnivctrna awsaegaela gsvsealala gadavvmggg qiyaaaldya declvteida
      121 dapggvlapd lrgnrtrgaw vlaevgewit dprsrvegyd devrhrhtvw rrrls
//
LOCUS       WP_010541235             516 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Dietzia alimentaria].
ACCESSION   WP_010541235
VERSION     WP_010541235.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..516
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56363
     Region          1..495
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdaldfarwq fgittvyhfi fvpltlglap lvaimqtmwv atgkdhwlrl trffgklfli
       61 nfaigvatgi vqefqfgmnw seysrfvgdv fgaplalegl vafflestfl glwifgwtkl
      121 prlvhlaciw lvaiavnasg ffivaansfm qhpvgafyda esgrarlddi galftnstlm
      181 wgfphviagg lltaatfvtg iggwwmvrnm rraadlrasl paigseldeg stspdgsvle
      241 dasaledear svfrpatrlg llamviagla lvytgdgqak lmfdqqpmkm asaeslchte
      301 tdpnfsilti gthnncdgiq rlievpyvlp flaegridgv tlqgveelqe qyqeqfgpgn
      361 yapnlfvtyw sframigfaa gsaalalagl wltrkgrvpd qkwfgwlali aiptpflans
      421 agwiftemgr qpwvvhpnpt gvdlirltvd qgvsnhpiat vvtslvsftl lyaalavvwf
      481 wlmrthamag plpgdsqvag ldgaddeqpd slnfay
//
LOCUS       WP_010541250             198 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010541250
VERSION     WP_010541250.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21228
     Region          14..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdvgsgtgal tpraqakaqr rieilvaaar lmarrgfhav rlddigaevg isgpgmyryf
       61 askedvlaem lldisrrlvd ggraavnrgg gpaevldall gvhvdfvate pdlisvqfrd
      121 lgslpagprh evrtlqreya emwvdalvrl rpeltstgar ahihavfgll nssprlpama
      181 evelrrvlta masaalrs
//
LOCUS       WP_010541265             213 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010541265
VERSION     WP_010541265.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22679
     Region          33..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mseeiptray rstlraeqaa ntrtrvvaaa aacftergyg gtslgdiadr agvstetvka
       61 ngpkrallls afeqafagae gdqllaesda arelvatsds dellpalagl igaanartsv
      121 lwseylaaan adpviaeals allqrrrldy rsaidllasr givgpiddvd eaaaalsflw
      181 speshqqlvl qggwsfrrye rwlveaarrq fav
//
LOCUS       WP_010541272             590 aa            linear   BCT 01-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Dietzia
            alimentaria].
ACCESSION   WP_010541272
VERSION     WP_010541272.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..590
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=63999
     Region          28..577
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mvqftdpmhs aervaeyrsr gwwddrtlyg efrarvaerg dalalvdpln realvgsppr
       61 rltwnevdde vtylaarlle hgvragdvvg iqlpnsvela eamlatwaig vvasplamqy
      121 rqhelttmgg kagfrviltc arfqdrspaa daigaraala pqppvltlga aceagevada
      181 hlvpgpastk drarvedyra ehphdpnhcv tlcwtsgteg qpkgvprady ewvsigdgtt
      241 tgpavhaesv llnpfpminm ggisgmflpw lftgcllvqh hpfdaptffr qiatervtyt
      301 lappallwml lhnedlqskv dlsslthlgs gsaplqpamv rgwqeqfgls vinnfgsneg
      361 valislpedf pdpadrarff prfgapgvqw haflsdrvsv qvvdmetgee itepgvpgel
      421 rvdgptvfag yldgenvasp fdeqgrlrsg dvfeiagenn efllyvdrnk dliirggmni
      481 apvaleamia ehpavaevav igdpdevmge rvaavvalrd gcsltldelv sflrdrkigs
      541 yqlperlevr pelprnavgk llkrdlrrra aavepgpsta ptaalsgepv
//
LOCUS       WP_010541288             247 aa            linear   BCT 01-JAN-2025
DEFINITION  ZIP family metal transporter [Dietzia alimentaria].
ACCESSION   WP_010541288
VERSION     WP_010541288.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..247
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24162
     Region          41..246
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mpewlgagga gllagsallv gsaiawlvav parvvavvma fgsgvlisal sfdlvleaad
       61 qggllatsgg ffagalvyvg lnillsrrga rhrkrsgdqq sgdsgsggai algalidgvp
      121 esmvlglsfl tgggisipml aavfisnvpe glsstagmkr agrspgfvfg vwggiavasg
      181 laalagylll dgappellaa vnalaagail amisdtmipe afenasvyag liatlgflaa
      241 fslhaia
//
LOCUS       WP_010541322             498 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein [Dietzia
            alimentaria].
ACCESSION   WP_010541322
VERSION     WP_010541322.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..498
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54068
     Region          36..>258
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          357..416
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(381,383..385,387,403..404,408..409,412,416)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mldttttssv lteplrgvde plgsldadal seiarsatls qnlagatrle aafhlverir
       61 rldealresd salrsafarl apadqardhl vaamsltnwh agrlvaaglq ihtrlrllrd
      121 avgrglvpeq laidtacrla tvpdqivgrv esdvvgmlcr alnggsrpsr taldsavdqs
      181 verhdqnaan davdearaqr svrfrpaang mmnmwahlpv edaerlrrri dnaaraages
      241 ghgrprsqlr adalcslgdp ttddvgdpis vesngngsvg trwasdspih isvidgrvqg
      301 lpnrvefvrg ayssfdwlce qllnggdttv rfelidpqpg vldtpdaals yripaalaer
      361 irlrdgtcrh pgcavdardc dldhilafdh lnpalggptv ewnlaclcrr hhrektfghs
      421 ayrpgplgel iittdtgheh rttptgplar sreqildhqw dlhigrliae dghitnppga
      481 hrarqgpppd drerprgv
//
LOCUS       WP_010541325             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MOSC domain-containing protein [Dietzia alimentaria].
ACCESSION   WP_010541325
VERSION     WP_010541325.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..218
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23295
     Region          26..174
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mtsafavrav cvvdqlltvp grvgvsgidk rpvdgpvqvr eyglhgdvqa drkhhggvwk
       61 avyllsdsdv eqwepefggp ippgyfgenl rvtgvdtsql qigtilevgs lrmeitapri
      121 pcqtfahrvg kpkwvrrfte ggrpgayarv laagpveagd virvvavpth gvtigrvfag
      181 vddddvgrll deyavadlap slvrkldpat dvrpvdad
//
LOCUS       WP_010541333             199 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010541333
VERSION     WP_010541333.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..199
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21431
     Region          16..61
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          81..194
                     /region_name="TetR_C_24"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17932"
                     /db_xref="CDD:465574"
ORIGIN      
        1 mkdwrefgpd gltpplraal dvfarhgyhg asirsiaeaa glsvpglyhh yrskqallaa
       61 ivdstmaeml thtavaaeda gdspaqrfan vveclarfhm arrdhafvas temrsmdpdv
      121 rahhisqrda qqtmlqdais agvksgdfac rhprdaarai aslcvsiasw yrpdgplssd
      181 evvarhlefa rgmvgaaqg
//
LOCUS       WP_010541402             214 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Dietzia alimentaria].
ACCESSION   WP_010541402
VERSION     WP_010541402.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..214
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23254
     Region          63..206
                     /region_name="YdbS"
                     /note="Uncharacterized membrane protein YdbS, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3402"
                     /db_xref="CDD:442629"
ORIGIN      
        1 msdpvatlrt ngdplvsapa tdvggahalr aprvavddgp gpdagdallt snrvlitapr
       61 hriekrtpfl fvvegiwswm vlaglqvawf fwgdnvmgfw nwvalavtvp fafmgivvap
      121 ywrylvarwd vsdtavcsrk gwwttqfria plarlqtvyt trtlferwfg latvnastas
      181 aqgtveirgl nladaealaq hliaianlds adgt
//
LOCUS       WP_010541437             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Dietzia alimentaria].
ACCESSION   WP_010541437
VERSION     WP_010541437.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42284
     Region          33..398
                     /region_name="MFS_MdtG_SLC18_like"
                     /note="bacterial MdtG-like and eukaryotic solute carrier
                     18 (SLC18) family of the Major Facilitator Superfamily of
                     transporters; cd17325"
                     /db_xref="CDD:340883"
     Site            order(35..36,39,71,121..122,124..126,129,149,152..153,156,
                     230,233..234,237..239,242,270,274,323..324,328,332,349,
                     352..353,356..357,360)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340883"
ORIGIN      
        1 mtgpstggqr saprtrlpad vwvlvaaafa vaigyglvap vlpqfargfd vsvtaasvvv
       61 safaffrlvf aptggflvdr lgerkvymtg llivavstla tglaqsywql lvfrglgglg
      121 stmftisama lltrlsppga rgrimglyat afligniggp vlggllaefg mrvpffvysg
      181 sllvatavva vflrggrrrl addetpeqep lpvkealrda ryraalvssf vngwasfgvr
      241 vaivplfaaa nfdagpgiag talasfavgt asvitvagwl sdhygrrplv iggllisggs
      301 tfvmgwcdtv pllvaasvva gigagilnps qqasvadvig sdrgggkvla tfqmasdsga
      361 ilgpvvvglv vdalgyrtgf avsgalllta vvpwlfaret rettdravtv ge
//
LOCUS       WP_010541443             882 aa            linear   BCT 01-JAN-2025
DEFINITION  AAA family ATPase [Dietzia alimentaria].
ACCESSION   WP_010541443
VERSION     WP_010541443.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 882)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 882)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 882)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 882)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 882)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 882)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 882)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18409402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..882
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..882
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=95738
     Region          2..>157
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
     Region          <104..>407
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          314..873
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
ORIGIN      
        1 milhrlmied frgvvreeve vpalgvlvie gpnesgktsl mdslemlleh kassgraeik
       61 aaspvgrdvp vvveaeftid germsyrkef vrgkrtslef lssarpalsg ddaheyvrel
      121 ldrrvdrslw kalriaqdep igqvdaakgm dslrraldaa aggedptgdd sliervteer
      181 nryltakkge ptgdlarsqv wvteaatqla aararhaeld aavedhaaqa svhearrvsl
      241 aaieaevarl eeagraaael sractaaese vdravathda rqrehrereg lvesarreea
      301 keaelraaaa taserlspae ararttrsal eeaeervtra rrrldavras qerarrradl
      361 atletrlqtl rkvgdeldkk eaalldvkvp ddavdrlraa eealreavir ssasaprvel
      421 sgegsvrvgg edvdvgehws rdivedtvfe mgtvsltvvp agdtdavrre eqaarahfas
      481 lmetlgvesl aeadqrarrt eglraeidal rrrrgdllag dttedlinrr dllaaeeqdd
      541 psapeeside dvdedsvgsd dpeaadpvae tasaeqelar craedrsata evgalrtela
      601 trlaladeaa arlqecrhtl etargitpds elaeaesqaq alaettreea rvargdldaa
      661 lavaprelld narasltalv veeresaeav aaalgrvnai gdqgrfdevs vaerelemae
      721 renttlwrra raadllhrtl varrsealka yqapfhqavv elgslvygrd fdvrlgedlt
      781 ilsrrtgdvt vdyeslsgga reqlavivri acarlvgegg vpvflddtmg ytdptrrmtm
      841 gaviaaaaat sqvivltcdr arfagiggar thvmgrsgqs ak
//
LOCUS       WP_010541469             399 aa            linear   BCT 01-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Dietzia alimentaria].
ACCESSION   WP_010541469
VERSION     WP_010541469.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 399)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..399
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40390
     Region          5..396
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtadptrtvi vagartpfgr lqgglsslsa aelggiairg alerggvpae avdqvimgqv
       61 lsagtgqmpa rqasiaaglp kkidalsink mclsgltaia ladqairsgy sdvvvaggqe
      121 smsqaphllp ksrsgykygs ievldhmayd glhdvptdqp mgaltetrna elgitreaqd
      181 efaatshqra atawsegkfa devipvtvkg rkgdtvvdsd egvradstpe smsklrpafa
      241 kdgtitagss sqisdgasav ivtsaaraea egwpvlaeiv gygtvagpds tlqhqpadav
      301 ldacrradvs vdeidlfein eafasvglha tkalgvdpak vnvnggaiav ghpigvsgnr
      361 vvltlalela rrggglgaas lcggggqgda liirvpaag
//
LOCUS       WP_010541478             261 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Dietzia alimentaria].
ACCESSION   WP_010541478
VERSION     WP_010541478.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..261
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27495
     Region          3..261
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mtnivvlikq vpdtyserkl sdgdftldre aadavldein ekaveqalqi keanggevtv
       61 lcagpdratd airkalsmga dkavhlndea lhgsdviqts walanvlgti egtelvicgn
      121 eatdgrmgav pailaeylgl pqvthmrtie vadgvikger etdeglfeie atipcvvsvg
      181 ekineprfps fkgimaakkk pvevltladt nveagqvgkd naastvtsss pkpprsagek
      241 vtdegeggnd vakylvsqkl i
//
LOCUS       WP_010541580             134 aa            linear   BCT 01-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Dietzia alimentaria].
ACCESSION   WP_010541580
VERSION     WP_010541580.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..134
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14067
     Region          5..131
                     /region_name="DUF4439"
                     /note="Domain of unknown function (DUF4439); pfam14530"
                     /db_xref="CDD:434020"
ORIGIN      
        1 mttpvglaae daavygyglv lsradgsira avrrelaahr arrdgaeelw pgsppapvgy
       61 ltgpdtptsp vllairiesd cceawraqva taetaemrry avealtaaai qlarwrtlvp
      121 gapfealpgf ppda
//
LOCUS       WP_010541630             441 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Dietzia alimentaria].
ACCESSION   WP_010541630
VERSION     WP_010541630.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..441
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=45873
     Region          12..435
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mtqerttdwt grvlrvrveg paqggefvar hegrvvfcrg aitgelvdvv vdddpgrafc
       61 rgtvsaviep sphrveprcp aaaagagccd wshiapeaar gyagriiaeq aariggidda
      121 ggvvpvespa gddattgwrt varwvtdneg tpgvrrarsr dlvtepcvqp dsrilravld
      181 advgpgrevl gvigddggih vahraadsrg pggrgrrsra saatrararh aragnwqtvt
      241 gehvvlrrva gyewrlpvea fwqahrsaag hyadlvraav aaapgpatdp vvwdlyggag
      301 lfsaavldvl psarvtives assslravtt alseetgirs vrsrvesfle tpadtdggsa
      361 dpdivildpp rggagiavme hlssrvgtri vhvgcdpasl ardvgvlvsr gwslaslsgv
      421 asfpgthhie giavldapgg i
//
LOCUS       WP_010541678             183 aa            linear   BCT 01-JAN-2025
DEFINITION  shikimate kinase [Dietzia alimentaria].
ACCESSION   WP_010541678
VERSION     WP_010541678.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..183
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19419
     Region          10..171
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 msgpvrpvav lvgppgagkt tigrklarrl gvpfldadhm ieesegrtip eifagdgeag
       61 freieerivg ealgsfpgvl slgggavlsa etrrrlrnhr vvhltlgvae gvrrsqgsgr
      121 pllaggdvta ryqalltera plyrkvawtt vtterrssgk vvtdivdrle sgdphlrssv
      181 grp
//
LOCUS       WP_010541735             268 aa            linear   BCT 01-JAN-2025
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme [Dietzia
            alimentaria].
ACCESSION   WP_010541735
VERSION     WP_010541735.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..268
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28764
     Region          15..199
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mteknrivda lvgvwrdird vtvgftdeqw aapspcpgws ahdvvahivg teemlrgtps
       61 peasgerpah vrneigavne vwvehlrsls paellarfde vtaaraealr amseeefhae
      121 swtpegpgty agfmrirvfd cwvheqdlrs vagaeggyds daaelavafm vaklgfvvgk
      181 ragapqqstv tfeltgplar tasvlvdgra rvldspaenp tatlklptsq fvclyagrva
      241 gaavadrvei tgdeelgrrv rdslgvtv
//
LOCUS       WP_010541763             343 aa            linear   BCT 01-JAN-2025
DEFINITION  YncE family protein [Dietzia alimentaria].
ACCESSION   WP_010541763
VERSION     WP_010541763.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..343
                     /product="YncE family protein"
                     /calculated_mol_wt=34648
     Region          155..>334
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mplrylcssv lpavlvtaav gltacspass dledsnrieq gnaspaespq vsdpregevi
       61 ttpgsvrall avgdrviaqv dgppsleigd vegtrwtpek svplpedagv atvgtdgtvl
      121 vphgdgvvlv apggevreld glgavtaaaq tadgrvltgt segdvvvrda dgveqhrigg
      181 ltsvdrisva rdgsvtvlsr pdtviasidl sdevagpllr agsgagmlde fgersvvasd
      241 tvgstlllfs tspvrlhqqf pvasapwava edasrgvvwv tstgtntvqa ydlgdgigvr
      301 raevntvrqp dslavtdsgt vvvgsadgag lhlispalte pss
//
LOCUS       WP_010541919             306 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Dietzia alimentaria].
ACCESSION   WP_010541919
VERSION     WP_010541919.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..306
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=33383
     Region          20..295
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mqqataarpi araipptfdt tdlliegfla rfssestrta yagdlalwrd wcdeqgldvl
       61 tverghvemf arwletargn spasvhrrlv clrsfyrtma adgrilvspa eyarlprvrr
      121 drtqythitr gelstllvaa ddigpaagal vslmgvlglr vseacaldvd cadrherghr
      181 iltatgkgat vtgipvpvpv grridaarge rhlgplilrr dgsrmtrrsa arvvaaaakr
      241 agidkhisph dlraaaitca ldsgiplrdv qtmarhadpr tteiydrgrr didrhgayil
      301 asylaa
//
LOCUS       WP_010541870             316 aa            linear   BCT 01-JAN-2025
DEFINITION  site-specific tyrosine recombinase XerD [Dietzia alimentaria].
ACCESSION   WP_010541870
VERSION     WP_010541870.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Spiers,A.J. and Sherratt,D.J.
  TITLE     C-terminal interactions between the XerC and XerD site-specific
            recombinases
  JOURNAL   Mol Microbiol 32 (5), 1031-1042 (1999)
   PUBMED   10361305
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Cornet,F., Hallet,B. and Sherratt,D.J.
  TITLE     Xer recombination in Escherichia coli. Site-specific DNA
            topoisomerase activity of the XerC and XerD recombinases
  JOURNAL   J Biol Chem 272 (35), 21927-21931 (1997)
   PUBMED   9268326
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..316
                     /product="site-specific tyrosine recombinase XerD"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007049 - cell cycle [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=33517
     Region          8..315
                     /region_name="xerD"
                     /note="tyrosine recombinase; PRK00283"
                     /db_xref="CDD:234713"
     Site            order(163,261,264..265,296)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 mgseggaavq irgyldhlav ekgasphtla ayrreldryr rhlaevgvdd lgsvteahve
       61 afrarlsttd pdrgnrilap ssvaralaav rglhrfaard gvaavdaaas vtpprparrl
      121 pravpvdqmi sviesagdta tdtdparlrd ramlellyat garaaelvgl dvddlegldh
      181 peggtvilrg kggkerlvpv grpacdavga ylvrgrpala ikggpalfln trggrisrqt
      241 lwntvtvaag ragvdaeisp hsfrhsfath lldggadirv vqellghasv tttqvytlvt
      301 vdtlrevwae chprar
//
LOCUS       WP_010541947             702 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Dietzia alimentaria].
ACCESSION   WP_010541947
VERSION     WP_010541947.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..702
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=74119
     Region          7..700
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mtdslpsvse llataveslg gsersgqvam aeavsnalst gehlavqagt gtgkslaylv
       61 pslrhavetg gtvvvstati alqnqlvdrd lprlsaalrp elgvspshai lkgrgnylcl
      121 hrvssgpvde adpdevmaee lfdlpigges tsgripresa prdtgpnswl greiarlhdw
      181 aqdtetgdrd dlpkgvsdaa wrqvsvtsre clgqlcpefs ecfaelarqe agradvvvtn
      241 hallaidamt dvsvlpehda vvideahels drvtgvttae ltgaaviqaa rraaklidqq
      301 tvdrmvaage gfaallelcp egrwdlmpeg adlglaavrh taencrtavp gpkpgeaagd
      361 pqgasdrqkt laaldeiada adrmlssfek gvterveivw msveerrgri lrvaplsvag
      421 llrtrlfaes tviltsatlt tggkfdglaa twglppassa rpdsstaval eppsdddmst
      481 lrwtgldags pfdyrrngil yvakhlpspg regpspqaee elvdlitaag grtlglfssm
      541 rgakaaaell rgtldtpvlc qgedstanlv aqfaadeett lvgtlslwqg vdvpgrslsl
      601 vvidripfpr pddpllsarq ravaarggng flsvagnhaa lllaqgvgrl lrrtedrgvv
      661 avldsrlvta ryggylrasl ppfwqttdrd vvlgalerlr dt
//
LOCUS       WP_010542037             594 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Dietzia alimentaria].
ACCESSION   WP_010542037
VERSION     WP_010542037.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..594
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=64304
     Region          43..546
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 mptirsrsvl gperraqawr rlsedtfdvv ivgggvvgtg saldaatrgl nvavveardf
       61 aagtssrssk mfhgglryle qldfglvaea lherelsmtr laphlvtplk flfpltrrfw
      121 erpymaagfv lydvmggaks vppqkhysra gahriapglr egavvggiry wdtlvddarh
      181 tltlartaah hgavvanstq vigylrdgdr vtgvrvrdae tgletdvraa vvlnaagvwt
      241 dhlqkmlgee ggftvraskg vhivvdrdkv dseaalilrt eksvlfvipw geywiigttd
      301 tdwqldlahp aatgadidyi lghvnsvlte pigredvrgv yaglrpllsg gadttaklsr
      361 ehavmtvapg avvvaggkyt tyrvmaadav daavaelger aagvpsstte ripllgadgy
      421 pgmvnradri adhyevreeq vlhllgrygt ltedvlelaa grpdlletlg gadgylrvev
      481 vyaavaeaal hledvlvrrt rismeyqhgg vdcarevadl maeildwdad rvarevelfe
      541 rridaekasq vtesddeadg flrrvpdvrq flaeaafdpa raqpvvdssa argh
//
LOCUS       WP_010542045             376 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Dietzia alimentaria].
ACCESSION   WP_010542045
VERSION     WP_010542045.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..376
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37450
     Region          177..373
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 miadalayag pikqildlls teefvpaeaq nlmkpvsdgl evaqqvgapl erllseswds
       61 laslgaaqsi aevgrtvgal sesaveiarv tsvaadivvr gtievigivq qfitraaalg
      121 ptllsppgqi allglatehl argiqvaerv qlelqaptae mnaiasgipp aprmpgmlsa
      181 dsstggsain astvaysgsg pgafsgdggs tggleagagv gaeagqsstp gpvasgdags
      241 gvigsgvevv lpdgsvatap nenaagavrn alsqqgvpyv wggttpgqgl dcsgltqway
      301 rdagveiprl aqeqgvgvqv sqqdlaagdl lvwdghvamy igngqiveag dpvavsglrt
      361 dnigmsfygf yrptgg
//
LOCUS       WP_010542055             466 aa            linear   BCT 01-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Dietzia
            alimentaria].
ACCESSION   WP_010542055
VERSION     WP_010542055.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..466
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46890
     Region          107..394
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mtsirrrpvq raaglvaaal valaplatag satgvepeag ipvtdpppva vlpsttsssy
       61 fdtprdltgc pyrttppapv desevplpgg sapapppvpd aapggdalag cevaapdgfe
      121 vpgdvtasaw lisdldtgev vaakdphgry rpasiiktll asvaldsldr eqvievsdsd
      181 legaegslvg igpggkysvh rlmcgllmss gndaavvlah rlggieqtlg amnnhaaelg
      241 asstyiatvn gldgpgmmtt aydmslifrd amtrpefaei vatestgfpg ypagegagpp
      301 dpeaapadia ptvradgvtv npgfvlgndn qllynypgai ggktgftdda rhtfigaaer
      361 dgrrlavvll dgtrvpsapw qqaaglldag faaggadpvg mldsgqhdal ddatehlasg
      421 plgssgksds tshdgsllgr ygpwlalgaa gvavlagavl tlrsrn
//
LOCUS       WP_010542148             390 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Dietzia alimentaria].
ACCESSION   WP_010542148
VERSION     WP_010542148.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..390
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41186
     Region          135..384
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mleesaftrg aqlrlglhvl ivvlalivll ravllseasa gligaltalf vvvyivgass
       61 lrapaarfaw faslcavwva mafigadaay vsfglillfm tevpllpavs vvavitgvnv
      121 ligvytsgqw ggamvgsllg avvgivvglg frvlfheter rqqliedlhr traelaeter
      181 sagklaerer laseihdtva qglssihmll raaeaenlpp gaankivmar rtalaglada
      241 rrlvaalsps dlegnslada lgrvceraaa gtvdvrlrvd gqpvslqmpl esalvrlvqg
      301 avsnvvrhad anhavvtlsy gadavhldvv ddgqgfdatl lddpsahnfg lnamrnrveq
      361 ldgqwfiese pghtavsvtf plaqqgeeyr
//
LOCUS       WP_010542184             288 aa            linear   BCT 01-JAN-2025
DEFINITION  siderophore-interacting protein [Dietzia alimentaria].
ACCESSION   WP_010542184
VERSION     WP_010542184.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..288
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=30728
     Region          21..288
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mqlaqlkdki vfgaarlwyr ntmadvaerd gqaqfeatva rvrelnpvmr ritlaapeft
       61 ryslvgpdey fgllmpgadg qlhmpdanrv nvraaiaemp qeaqpglrwy tirelrcsqg
      121 eidvdivthg dtgpgsvwat tvdvgdrvgf rsggalytty darrqllvad etavpallai
      181 leergrrglh glgegvtahv eapsaaalag tglpaeitvh ergdaapgta vlaaltadas
      241 atsdvdyawv cgesglatsl rrhlvqevgm dkkavtfsgy wkvgaarg
//
LOCUS       WP_010542206             184 aa            linear   BCT 01-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Dietzia alimentaria].
ACCESSION   WP_010542206
VERSION     WP_010542206.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..184
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=18760
     Region          14..183
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mtaptinpva pvakalrial lvggviaiaf giavlvwpvk tavaitavla vyailagivy
       61 aavgivsttq gtgsrvghvl lgllfivaga yafaslqesa lflglfvtim igvmwivegf
      121 talftlnapg nkaitilfai vsvlagfall stpvwgagfl wwllgisllv lgvlnvvrgf
      181 svka
//
LOCUS       WP_010542248             324 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Dietzia alimentaria].
ACCESSION   WP_010542248
VERSION     WP_010542248.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..324
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32990
     Region          1..288
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 migtvevgli ygvmalgvfl tfrvlnfpdl tvdgsfttga ataammitsg wnpvlatlag
       61 fvtgflagti tgllhtkgki dgllagiltm ialwsvnlri mdganvpllr qdtvftpled
      121 agllgtwggv gvlllavvll glvvvwfltt dlglsiratg dngpmiasfg vstdftktlt
      181 lslsngfvgm cgallaqyrg fadvsmgigl ilvglasvii gqailgqrkl vlatfavilg
      241 allyqliifa alrvglnpnd mkavtallvv valllprwkg agsrfgrkpt tavaaneraa
      301 agagttvdag pgsadaaatg akea
//
LOCUS       WP_010542213             223 aa            linear   BCT 01-JAN-2025
DEFINITION  potassium channel family protein [Dietzia alimentaria].
ACCESSION   WP_010542213
VERSION     WP_010542213.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..223
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23448
     Region          <131..186
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 maaavaflaa yamtvlvrpt gaagivtdvv mwgtwllfal dfvvrvvlae nrlrwlvahw
       61 yevavivlpm lrplrllrlv tllgflqrsa gtvvrgqvti yaagwttvll vvsslamlda
      121 ergapgasid sygealwwsa vtvttvgygd fspvtpvgra iavglmiagi allgvvtatl
      181 aswiadrvge qsgahhaatk aqvaelseei aalrrqlsgg qap
//
LOCUS       WP_010542255             223 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010542255
VERSION     WP_010542255.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..223
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23823
     Region          22..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msatitaavm apgaeqmasl rerkkadtri rlsvaavell vtegaegatv aaiaeragvs
       61 artfhnyfah redafvhflq eqvaewvrqv erapadlnpi aalhriirel yrrssddida
      121 aenllvageq iglmlsaear tcvaeellep lyeavgrrsp qmsavrvrvl vdlslaagas
      181 vvrhhprgag hdstghhape qgaaesylde afgllengsg gls
//
LOCUS       WP_010542257             266 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Dietzia alimentaria].
ACCESSION   WP_010542257
VERSION     WP_010542257.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..266
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28670
     Region          10..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 msttprasya lacsdlrvtr drtdilhgid ltveagswvs lvgpngsgkt tllfalagli
       61 paeghlevdg laprragrrr vartvammpq rpvvpegvta relihlgrtp hiarfgteta
      121 rdheivdrvi drlglqdlas riattlsgge lqrvvlarsl aqeprvllld eptsaldigh
      181 qqqvldlvds mrresgltvl aamhdltsaa hygerlvlld rgrvvsegpp eevltverva
      241 qvygarvevl srrdgpavlp lrepga
//
LOCUS       WP_010542274             229 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010542274
VERSION     WP_010542274.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..229
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24450
     Region          17..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdvgtdrgrr wkgkdaderq aerrdkllda gltllaesgp gavtmrgvcr gaglteryfy
       61 esfpsreaml vdlltsvvdd aervlteava sagddpgrii alaaqnftrf vagdqrrgsi
      121 mfvhslspel ypaarehvgr itsvmadare mllavagqdq dnagtaadtg psgstaatve
      181 larrwdplal fgatafvyqd wlgaqpqaga ddvaeyvavl vwrfllsgg
//
LOCUS       WP_010542278             215 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Dietzia alimentaria].
ACCESSION   WP_010542278
VERSION     WP_010542278.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23758
     Region          10..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdpdyqrapr lrpedrreqi lgcairlfge rpysevsvge iadaagvrrp lvnhyfggkr
       61 plyievirrf lfvpefdsaa legytsvper idavvsqwlh qaerhrglwl rvvvgedvag
      121 mgdvrdvlre adevaatrli kavapdldss ssstlhamtv afgamfksgs rqwlvdgtld
      181 rdqlrallva tmstilslvd sdyraateag psstr
//
LOCUS       WP_010542309             123 aa            linear   BCT 01-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Dietzia alimentaria].
ACCESSION   WP_010542309
VERSION     WP_010542309.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..123
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11561
     Region          1..>59
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mptysyrcrd cdvafdiqqs fdedtltacp qcegslrklf ntvgvvfkgs gfyrtdsrst
       61 sgagsasssg ssssasggsg sggsgsgssg sgsseasgsg sssgsgassg sgsssgssss
      121 sss
//
LOCUS       WP_010542320             132 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Dietzia alimentaria].
ACCESSION   WP_010542320
VERSION     WP_010542320.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..132
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13264
     Region          1..131
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 metlsdaail larvgigvvf aahgwqkfft lglsrvgeqf asygvpqphi taaivagvel
       61 iagialiagi ltplagillg vdmagalyfv hatngpfvtq ngwelvvalg vgalliaavg
      121 agrfsvdrvl gg
//
LOCUS       WP_010542428             270 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Dietzia alimentaria].
ACCESSION   WP_010542428
VERSION     WP_010542428.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..270
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28104
     Region          13..120
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
     Region          144..267
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mkqsqhngpe prlgisftes gdgtlswhqp igdqfvdpsg rfatgglavl vdsglgaenh
       61 rrrasgmwtv ttelridmls rpgagstalg vrtdhlgndg hclttrgevh dddgevvaag
      121 lvktvgiaga idaegydeep pwpaalepgt laevlcvsld srddgpggtr aveavvapep
      181 alanplgnlh ggvfaavadi agaavfpher evssssldvr yirqiplvsp vtvraevlhd
      241 grswgiaqat trdqrgllca vasvtvygrr
//
LOCUS       WP_010542344             424 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Dietzia alimentaria].
ACCESSION   WP_010542344
VERSION     WP_010542344.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42465
     Region          12..399
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mtdagpatav gndrrvgpmw vlaltlgvva vfaswfgplq illpaqtdsi agpggreall
       61 avivgggaav smvanpawgf vsdrcrerlg srmpvvfagt aigvagqlvl ltadsgpaml
      121 agwilvqlgf ngpfavlaal ivdhvpdrqr glvgslfgvg qiagviagtv vaesvgggpa
      181 gylvlavvtp lllgavvlas rrvparvddr gadsgdtvli agdqaiaarg lrlaafrpsr
      241 dfawawllrf lmnltnaill iylyffldgv lettdpggav llvtvitlvl aaacaaiagt
      301 isdrygrrrv favagaaata cglaglamss slpavlaaat vlglgwglfi avdmaivtss
      361 lttsdsagtl lgvanvansl pqvvapaiaa plvtsaagyp glygvgaaia vaaalctlpl
      421 rsvr
//
LOCUS       WP_010542432             107 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Dietzia alimentaria].
ACCESSION   WP_010542432
VERSION     WP_010542432.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..107
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12036
     Region          2..89
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 milinvrfdv kpefadtwle itrgfteatr aepgnlffdw yrspespnty llceafregd
       61 apgdhvdsah fteftgsaaq ylertpriin ttaegdewgt mgeitvk
//
LOCUS       WP_010542437             582 aa            linear   BCT 01-JAN-2025
DEFINITION  BCCT family transporter [Dietzia alimentaria].
ACCESSION   WP_010542437
VERSION     WP_010542437.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..582
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62011
     Region          1..525
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mserimralr lktdpgiflt tvgivvafvv vtffagdwvg svfgaasgwi mtdlgwfyif
       61 gvtaflgfli wiamsrfghv rlgaddempe hstatwfgml faagigtilm fwgvaepish
      121 fatpprggve pgstdaarqa igftlyhfgl htwtifalpa lafayfiykr kmpprvssif
      181 apllgdkifg pigrtidvva lvgtvfgvat svglgtlqin aglnelfgia msatvqvlii
      241 avvttiacvs vaaglekgik rlsnfniala igllifvlvt gptlfllkgt veslgiylts
      301 lpelalwnnv fpasddlasw qntwtvfywa wtitwspfvg ifiariskgr tirqfvfgvl
      361 glpvafsvlw fgifgmasfh ielygsggla qavvedgdip galfaflsny paatfisgva
      421 vllvvifftt svdsaamvvd miasgkdddv qvspphqrii wgvlmgavga tllaftgegg
      481 ltalqevitv iglpffvmgf immyslvrgi sndlgerpat vtrqwhrays psalaenega
      541 pspepvhpln ripetdedgg daegagdtag adttdespgg ea
//
LOCUS       WP_010542442             547 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Dietzia alimentaria].
ACCESSION   WP_010542442
VERSION     WP_010542442.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..547
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=56261
     Region          53..544
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 mttpdlptag sdgpstalsa arrardlaal rdrtepvdli vigggitgag ialdaasrgl
       61 dtvlleahdl afgtsrwssk lahgglryla tgnvgiarrs avergiller taphlvrpla
      121 qvvpvfrnts pveailpglg fvagtvlsrl agtgadrlpg srvlgpaave ryvpgvrrag
      181 lrfghlnwdc qlvddarlvt avartaagyg arvitrarvl sasgtqvtvr defaggagge
      241 gggaagrndd ddeftltara vvsatgvwag ettdevrvrp srgthlvlda aalgnpvgal
      301 tvpvpgetnr fcfaipaefg rlhvgltdvd apgpvpdvpe atedevdfll gvvnraldta
      361 ltrddvlgtf aglrplvdfg dsdngetadl srehavltsp sglititggk lteyrlmaeq
      421 avdlvaerag idagpcltad lplvgapgha dvprpaagtg grlpasllgr fgqeastvvs
      481 qslldrpldp vadgldvtra efsyavtheg altvddvldr rsrvglvptd raaaeptare
      541 alaaggl
//
LOCUS       WP_010542449             142 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Dietzia alimentaria].
ACCESSION   WP_010542449
VERSION     WP_010542449.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..142
                     /product="VOC family protein"
                     /calculated_mol_wt=14920
     Region          6..136
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(6..10,26,62..63,66,83..88,90,94,124,134)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 malsssiyis fpgnaaeafp yyadlfggdl dvatydampa meglpftppp gsvahgvmta
       61 pgltisggdn mgehlpqlas dvysflltfd tvdeahdflg kvtetggeia mpfelapwge
      121 mygqvhdkfg irwavnvpgt ps
//
LOCUS       WP_010542461             522 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Dietzia
            alimentaria].
ACCESSION   WP_010542461
VERSION     WP_010542461.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..522
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=55638
     Region          122..512
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mrfdlarlrr pdlgsvllgs ekqstrvrtl rvrillvltl igsnvvgvav sgalilfvlp
       61 gprllsrefl vptwvvvpvy vslatilgav wvyrvfrrrv rwfrdgreps dcervrtlrl
      121 paritviqal lwllgaavvt paygtvdaea vptvgftvvf agmvvcgaaf lfadfsmrpv
      181 aalalsagna prarflgamt rlqvawavgs gvpiagliiv siyalagram tverlavial
      241 slgaasllag fllvtlatgs vlgpvrsvrw amedvtagsl arrvvvydgt elgelqrgfn
      301 tmaaglqere rlrdlfgrhv grdvaeaael hepelggrds rvgvvfvdli gstemavrse
      361 asevvgvlnr ffavvvetve eydgvvdsfl gdaalvvfge prsmvdpata svacarvlge
      421 rlpvrvpdcr agigasfgdv vagyvgsddr feytvigdav neaarlcela kgrsslvlas
      481 giavgaanea ecerwesvgs evvrgrdept elcvpkpvdh qv
//
LOCUS       WP_010542472             446 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Dietzia alimentaria].
ACCESSION   WP_010542472
VERSION     WP_010542472.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46916
     Region          21..416
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,270,273..274,277..279,282,309,313,362..363,
                     367,371,387,390..391,394..395,398)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mttrterldg lpftrkhgkl lwgsglgwal damdvglisf vmaalavhws ltptelswtg
       61 sigfvgmaig aalgglladk igrrqvfaat lliyglatga aalstglaml ivlrfivglg
      121 lgaelpvast lvsefaprki rgrvvvileg fwalgwllaa ligyfvipls ddgwrwalav
      181 gllpaayalv vrfglpesvr fleskgrlde aemvvrefea sagieppaae tasrqpvdtm
      241 aatqaapaqs resiwsprlr rrtgalwivw fginfsyyga fiwlpsllvs qgfdlvksfg
      301 ytliitlaql pgyavaawli eiwgrrltla vflvgsavsa glfglagspa tiiaagmals
      361 ffnlgawgal yaigpelypt atrgsgtgaa aafgriasii apllvpllla rggsamvfgv
      421 faaafvvaav aaftlperkg valeet
//
LOCUS       WP_010542537             149 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Dietzia alimentaria].
ACCESSION   WP_010542537
VERSION     WP_010542537.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..149
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15250
     Region          4..146
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msaytkvvvg tdgsessyla vdraaelaad asaglviaca yvpadprsvn qaadmmgdda
       61 yqirgdnpae divrgardra qsagatdiev rtvkgapves likladevha dllvvgnkgl
      121 nsltgrllgs vpadaarrat cdvlivhtt
//
LOCUS       WP_010542596             107 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF1476 domain-containing protein [Sphingomonas elodea].
ACCESSION   WP_010542596
VERSION     WP_010542596.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..107
                     /product="DUF1476 domain-containing protein"
                     /calculated_mol_wt=12060
     Region          1..106
                     /region_name="COG5467"
                     /note="Uncharacterized conserved protein, DUF1476 domain
                     [Function unknown]"
                     /db_xref="CDD:444218"
ORIGIN      
        1 mttfddreha feekfarded mafritarrn kllgqwaaak mgltpeetda yakavvqadf
       61 eeagdedvir kllgdllaan veiddatvrr aleeqtvear rqlmesk
//
LOCUS       WP_010542694             729 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Sphingomonas elodea].
ACCESSION   WP_010542694
VERSION     WP_010542694.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..729
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77633
     Region          11..728
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mdkpdernrl damaqgiigr pldrpdgsak tsgvapyaae yvvpdcaegv lvlstisrge
       61 vveiesapvl ampgvlavia dprmitrsaq ggagkspvre iqkvdyygqp valvvaetfe
      121 qardaatrlr iayraddpar vplaqedgha shesygepvq rgnldaamrd aahavdvtyt
      181 teghasaame phasiaewdg ntltahsslq mlkynqkela dalglkpeqv rliapyvggg
      241 fgsklgisae laaaavaaie larpvqvvms rqqvfqcvmr rsetrqrirl aadaegrlsg
      301 fgheawvsnl pgekfaepvt qaseflyrge hrtlridlar ihrmtagsvr apgeavgmqc
      361 leaamdelai tsgidpvalr lrnipeehps qglpyssrrl aeclkvgadr fgwdgtdrrp
      421 cqrregewwi gtgmatacrv hnlneaqakv tlssdgtavv esdmtdigtg tyailgqiag
      481 emlglppekv lvqlgdtryp pgsgsggswg aastgsavfv aceaireqla eqlgieetdl
      541 tlkdgeaiag nrripftqll tadisetghf knggidekfa iamygaffve vgvnaytget
      601 rvrrmtgafg lgralnekta tsqclggmvw gigsalteel vfdprdghlv nhdlaeyhvp
      661 vnldvpalev vlvderdaag splqakgvge lgicgaagai anavhhacgv rvrsfpitpd
      721 klledlpda
//
LOCUS       WP_010542703             260 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Sphingomonas elodea].
ACCESSION   WP_010542703
VERSION     WP_010542703.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..260
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27829
     Region          1..253
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mititianqk ggvgktttai nvgtalaatg krvllidfdp qgnastglgi shgarerssy
       61 dllvtdanle dvavptnvpg ldvvpatqdl sgaeielief darthrldaa irrhsagrwd
      121 vilvdcppsl glltvnamva ahallvplqc effaleglsq llntverirt rfnpglsilg
      181 valtmydrrn rltdqvsddv ravlgrvvfd tviprnvrls eapshgvpal iydhrcagse
      241 ayialarevi drlpklqkaa
//
LOCUS       WP_010542708             159 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Sphingomonas elodea].
ACCESSION   WP_010542708
VERSION     WP_010542708.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..159
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16872
     Region          6..153
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 myardhalia tpigpirieg ddwqleriti gsegtktpgg taavraaaeq ieqwfagerr
       61 tfalslaaas tprgttlrdg liaipfgqti sygalstllg ssaraigqlc arnpfplvvp
      121 chrvlntggr lgaysagqgp mtkswlldhe rrltgeyll
//
LOCUS       WP_010542721             155 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Sphingomonas elodea].
ACCESSION   WP_010542721
VERSION     WP_010542721.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..155
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16721
     Region          13..143
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtppepaptg aeahfrales lyaaapinql fpsvleipea giarirfdvd aryfhaagat
       61 hgtsyfkmld daafyaansl vtdrflltta fnllltrplp egpviaegrw vsgqrrvfvg
      121 earlidange eaargtgtfm rsriplatlp gyrta
//
LOCUS       WP_010542729             715 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Sphingomonas elodea].
ACCESSION   WP_010542729
VERSION     WP_010542729.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..715
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=77302
     Region          14..622
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 magkskiaaa pwwrrgsfwk kfflwsligg valaliafia lviavysaka tlpsydqmks
       61 spngqmirvh avdgtvlvsl gpsygewiky dqipqvmkda iiatedrrfe shwgvdpvgv
      121 lrilwvakrl hdegrrlqgg stitqqvart iflsnkysvg rkireailal alerkfskqe
      181 ilelylnkvy fgggaygida asrkffghpa tnlslgeaai vaglvkapsh ysptadaeaa
      241 vdratvvlkv madagkisea qanatdphtv qlapepkqns vryftdwalp qletlidete
      301 apldvwttld lnmqrsadaa iranapdgaq galvsierdg avramvggkd yvssiynrat
      361 qaqrqpgssf klfvylaale aghkpddivv depvtidgws prndsrrnsg pitirtafay
      421 svntiaaklg qevgfttvad makrfgitta intqpamvlg tsnvrlidmt rafasvgnng
      481 vavtpygitr vtangkviyq hevdtshvlv anyvaaqmid lmqtavatgt graaqigrpv
      541 agktgtttsn kdgwfigfss glttgvwmgr ddakvvpglq ggraparafh dfmiqavanr
      601 pveqfetqlt ppdnmlepda daygepdngm mvdedgnpia qppqvpaepq egeimdgtap
      661 aqpggrpapv qqqgerldrd winrmtgrpa gqpqqpgrqp qrqpaqqnqr pndey
//
LOCUS       WP_010542754             309 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Sphingomonas elodea].
ACCESSION   WP_010542754
VERSION     WP_010542754.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..309
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31349
     Region          2..309
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mktlvwvehd nqsvkdatls tftaaaklge vhllvagkgv sgvaeaaaqi agvgkvhvad
       61 daayahflae nvaplivqlm gdhdavlfpa tttgknvapr vaaaldvmqi sdilsvegad
      121 tftrpiyagn aiatvqtsdk klvltvrgta fdkaaatggs gtveavavag dtglstfvga
      181 eiaaserpel tsakvivsgg ralgsqeqfh alidpladkl gaavgasraa vdagyapndy
      241 qvgqtgkiva pqvyvavgis gaiqhlagmk dsktivaink dedapifqva diglvgdlft
      301 vvpeltekl
//
LOCUS       WP_010542755             249 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Sphingomonas elodea].
ACCESSION   WP_010542755
VERSION     WP_010542755.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26537
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkvlvpvkrv ldynvkprvk adgtgvdlan vkmsmnpfde iaieeavrlk ekgaateivv
       61 vtigvakaet dvlltaramg adrgiliqtd etveplavak llakvaeeeq pgliilgkqa
      121 idddsnqtgq mlaallgwaq gtfaskveia gdrvhvtrei dggletvdlk lpaivttdlr
      181 lnepryatlp nimkaktkpv akktvaeygv ditprlttlk vvepakrqag ikvgsvdelv
      241 eklkgmgva
//
LOCUS       WP_010542770             371 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Sphingomonas elodea].
ACCESSION   WP_010542770
VERSION     WP_010542770.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39990
     Region          4..343
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,231,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,179,182,184,231,238,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,179,182,184,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            184
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mpslfdpiqi gaihaanrvw mspltrgrst rghvptpima dyyrqrasag liiseatgis
       61 qqglgwayap giwsdaqvea wkpitaavhe aggrivsqlw hmgrlvhsdf lggeppvsas
      121 attapgevrt ypaedsgeik rpytqarplr tdeipgilad yeraarnair agfdgvqiha
      181 angylidqfl rdnanfreda yggsienrir llrevsqrvv dtigadrtgv rlspngevqg
      241 vndsnpaplf eaaaaalddi gvaflemrep rpggsrgepd qppihpvmrk vfsgvlalns
      301 dydaesaqaa ldageadaia fgrtflanpd lprrlreglp lnpqreelfy vggaegytdy
      361 ptadelalqs a
//
LOCUS       WP_010543000             157 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Sphingomonas elodea].
ACCESSION   WP_010543000
VERSION     WP_010543000.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..157
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16879
     Region          1..139
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdridtailk llaadarapv sqvasavgls qsactrriqa leanglirgy garldhrrlg
       61 frvtalvdit lgtqkeedla qfesavgrid gvvecalvsg gqdyrlkvlc rdlddyerlh
      121 reqlgrlpgv vtinssfvlr dvstrgeada lfgaara
//
LOCUS       WP_010543029             131 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Sphingomonas elodea].
ACCESSION   WP_010543029
VERSION     WP_010543029.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..131
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=13959
     Region          13..126
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mahahahigp elletridag rhplladepp gnggrdagpa pydlllaalg actamtlrmy
       61 adrkgwrida ldvdlrllgt pdvrrirrtl titgpdaaar arlaeiaert pvtltlkqgi
      121 aietqlaeqt a
//
LOCUS       WP_010543074             379 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Sphingomonas elodea].
ACCESSION   WP_010543074
VERSION     WP_010543074.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..379
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41605
     Region          5..378
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mrspsvtarl adgvasipaa qwdacagadn pflshaflsi leasgsataq tgwqplpivv
       61 dgpdgtpaai apayakshsq geyvfdhswa daweraggry ypklqvavpf tpvpgprlll
      121 rdpdlapsli aaieavvdqh rlssghatfv eaaqvplfes agwlirtgtq fhwhnhgyas
      181 fddflgalas rkrkairker aaavegltir hltgaeitea hwdafwdfyq dtgsrkwgrp
      241 yltrpffsml gealgdkvll mlaerdgrai agalnliggd alygrywgct edvpflhfel
      301 cyyqaidaai qrglprveag aqgehklarg yvpvttysah ylpdpgfrra vadflvreqq
      361 avereqeyle eltpfrkae
//
LOCUS       WP_010543082             221 aa            linear   BCT 01-JAN-2025
DEFINITION  YoaK family protein [Sphingomonas elodea].
ACCESSION   WP_010543082
VERSION     WP_010543082.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..221
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23086
     Region          20..214
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mqrtesplia laillaalag fvdalaftsl ggffasfmsg nstrlgvglg sgstrdaama
       61 aslvmsfvag vilstiiara rahrhqpavm atvtlllala amvamlmpgp ivllllaaam
      121 gaengvfhrd gevtigltym tgslvklgqk lagalmgdtd rfgwlrylal wlgfvsgvvi
      181 gaesqfrwgw nalwlaplfa avltlllasm trprpnltpv r
//
LOCUS       WP_010543113             615 aa            linear   BCT 01-JAN-2025
DEFINITION  CocE/NonD family hydrolase [Sphingomonas elodea].
ACCESSION   WP_010543113
VERSION     WP_010543113.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..615
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=69055
     Region          26..615
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mrhwlvsval aalaaplvga appqltptat eapfvfeeam ipmrdgvklh tvilrprdar
       61 gplpilfqrs pygspdaapp rvpnswaplv rdgyifvfqd mrgrfksegg pftlstevkt
      121 gkgavdeatd aydsidwlvk nvkpnngkvg mwgvsypgft aaialakphp alkatspqaa
      181 widywknddl hrwgamrlty asdwvnslqa dktndgiply drydtydwfl hagspdeiek
      241 tyfkgrvpry remiehpdyd ehwkkqvwsn algkttvptl nvagywdqed pwgswkiwek
      301 qrandpnkla lmvagpwahg twhspanslg ripfgvdsgv qfieqieapf faywlhgtgt
      361 rpdfalksfq sgswqwktyq typlanaqat nlylhadgsl sftapaageg crdyvsdpar
      421 pvpfrprpms atyatpdwrw weaedqrfvd drpdvlsyvs aplendltvt gevtaklmas
      481 tsgtdsdfvv klidvfpeny ekaptapgay akglngyelp iameirrgry lksfeqatpl
      541 vpdqvtawdf plrdhdhvfk kghrimvqvq sswfpvidrn pqtfvpniyk akpedyrkat
      601 qrvcagsavt lpvvk
//
LOCUS       WP_010543083             215 aa            linear   BCT 01-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Sphingomonas
            elodea].
ACCESSION   WP_010543083
VERSION     WP_010543083.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..215
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22016
     Region          11..207
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mnasvafqig pilpwldlfg iavfaatgal aatrhqqtiv tatffalitg vgggtvrdll
       61 igapvfwvhd atvaalclgm saivwitpqr wwsdrtfawl dalglaayaa fgaakalgyg
      121 ippvpaavmg vvtacvggii rdvlagqpsi lmrpelyvta aaltasvyvv lsllgwppya
      181 aglvaaaagf alraaaivwk lglpayradq gkpga
//
LOCUS       WP_010543158             280 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Sphingomonas
            elodea].
ACCESSION   WP_010543158
VERSION     WP_010543158.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..280
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31519
     Region          29..276
                     /region_name="EEP-1"
                     /note="Exonuclease-Endonuclease-Phosphatase domain;
                     uncharacterized family 1; cd09083"
                     /db_xref="CDD:197317"
     Site            order(34,70,160,196,198,242,268..269)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197317"
     Site            order(70,268)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197317"
     Site            order(160,198,269)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197317"
ORIGIN      
        1 mmrfwrwmaa iaamlacapa laqggpaltv mslnirypsp ddganlwekr raltiatira
       61 adpdligtqe lfqrqgddiv kalpryrwfg idrrgghade hmgvfyrhdr lklieqgqfw
      121 lsdtpevpgs iswghpfprm vtwatfetkd grrfrfynth fpyrdeddda rtrgarllad
      181 riaagpaalp vivtgdfntt ddkpahavlt ktlsdawlar pdhrgpgftf hgftgkgdsr
      241 idwiltrgvk veriatvdth qgpvypsdhy pvvarvqlar
//
LOCUS       WP_010543116             254 aa            linear   BCT 01-JAN-2025
DEFINITION  DsbA family protein [Sphingomonas elodea].
ACCESSION   WP_010543116
VERSION     WP_010543116.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16062126
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..254
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26148
     Region          36..69
                     /region_name="ScsC_N"
                     /note="Copper resistance protein ScsC N-terminal domain;
                     pfam18312"
                     /db_xref="CDD:465704"
     Region          98..240
                     /region_name="DsbA_Com1_like"
                     /note="DsbA family, Com1-like subfamily; composed of
                     proteins similar to Com1, a 27-kDa outer
                     membrane-associated immunoreactive protein originally
                     found in both acute and chronic disease strains of the
                     pathogenic bacteria Coxiella burnetti. It contains a
                     CXXC...; cd03023"
                     /db_xref="CDD:239321"
     Site            order(114,117)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239321"
ORIGIN      
        1 mnrpnlffgg allvaallgg laalalqall pgiggdkaqv erivqtylle npailrdmme
       61 rlqqqetaaa qkaqegaqaa vpavlpaltt pfgsawagnp dgdvtiavfm dyacgycras
      121 lpalaeliak dpnvrvvyre ypvlgeasvv aarfalaaaq qgkfrpfhda lfasggpsna
      181 sigaalakag ldpaatekla aspaiakeie anhqlgakla mngtpawvvg kqilygardy
      241 saladavaaa rktk
//
LOCUS       WP_010543187             488 aa            linear   BCT 01-JAN-2025
DEFINITION  GspE/PulE family protein [Sphingomonas elodea].
ACCESSION   WP_010543187
VERSION     WP_010543187.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..488
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=52617
     Region          8..486
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mivdlptlpy sfarrhgvll rtsgegiecv hradapldgl levqrlapga rfvrlegaaf
       61 dtalgeaygg aggaaadidl gdmdlaalad saasvddlld trddapvirl inallmeavk
      121 egasdvhvet qekrlvirfr vdgvlrdmie ppralapllv srikvmakld iaerrvpqdg
      181 rvtlrigghd vdarvstipt qhgervvlrl lekgslkldl sglgmsardq avfgrllerp
      241 hgillvtgpt gsgktttlyt alarlndrkr nvmtvedpie yelpgvaqtq vnprtdmtfa
      301 rglrailrqd pdvimvgeir dqetaqvavr samtghfvls tlhtnsavgs vtrlidmgve
      361 ryllapmvvg lcaqrlvrrl cphcrradva seadslllgg alpvgaplwr avgcdqchde
      421 gyrgraglye vvavddvfqk lihdgaseae ierhargdnp sllddgvakl qvgvttveev
      481 arvvrdea
//
LOCUS       WP_010543233              78 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF2312 domain-containing protein [Sphingomonas].
ACCESSION   WP_010543233
VERSION     WP_010543233.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..78
                     /product="DUF2312 domain-containing protein"
                     /calculated_mol_wt=9017
     Region          2..78
                     /region_name="COG3750"
                     /note="Uncharacterized conserved protein, UPF0335 family
                     [Function unknown]"
                     /db_xref="CDD:442964"
ORIGIN      
        1 msdnisaeql rllierverl eeekkgiadd ikdvyaeaks tgfdvktmrt ivrlrkmekh
       61 hreeaemlle tykqalgi
//
LOCUS       WP_010543229             292 aa            linear   BCT 01-JAN-2025
DEFINITION  prohibitin family protein [Sphingomonas elodea].
ACCESSION   WP_010543229
VERSION     WP_010543229.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Yoshinaka,T., Kosako,H., Yoshizumi,T., Furukawa,R., Hirano,Y.,
            Kuge,O., Tamada,T. and Koshiba,T.
  TITLE     Structural Basis of Mitochondrial Scaffolds by Prohibitin
            Complexes: Insight into a Role of the Coiled-Coil Region
  JOURNAL   iScience 19, 1065-1078 (2019)
   PUBMED   31522117
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..292
                     /product="prohibitin family protein"
                     /GO_component="GO:0005743 - mitochondrial inner membrane
                     [Evidence IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0035632 - mitochondrial prohibitin
                     complex [Evidence IEA]"
                     /calculated_mol_wt=31601
     Region          39..249
                     /region_name="SPFH_prohibitin"
                     /note="Prohibitin family; SPFH (stomatin, prohibitin,
                     flotillin, and HflK/C) superfamily; cd03401"
                     /db_xref="CDD:259799"
ORIGIN      
        1 mayepgnfgg gfrlgrlfgr swlwitaava igifglgsca rvepgqvgir vnniaggvrp
       61 eslpvgwyla lpgthiyqyp vftrtytwta skteqspide aftfqdkngl slradvgvsy
      121 hvdpsrasil fqryrtdmdq iiagplrnai rnaiveraaq lgveeiygth kaeliatatr
      181 rvqaffapvg lqveqvywag nvvvpeavln qinakianeq qalaakanve takadaeari
      241 akaagdakai qveaeairtn peivklrave kwngqlptym ggdgpmtflg vk
//
LOCUS       WP_010543289             207 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Sphingomonas elodea].
ACCESSION   WP_010543289
VERSION     WP_010543289.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..207
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22868
     Region          4..194
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mafelpelpy akdalaphms aetfdfhhgk hhkayvdncn klvadipela gakltdviay
       61 akdkgnkglf nnssqiwnhs ffwqcltpny aaptgklaem itrdfgsqea lveklkaesv
      121 ghfasgwgwl vldgdtlkvt sfhdgdspva hgvkplftid vwehayyidy rnarpsfvdt
      181 iltklanwdf vaqnldgega aradqqg
//
LOCUS       WP_010543342             243 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Sphingomonas elodea].
ACCESSION   WP_010543342
VERSION     WP_010543342.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..243
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=26022
     Region          4..237
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
     Region          10..68
                     /region_name="DZR_2"
                     /note="Double zinc ribbon domain; pfam18912"
                     /db_xref="CDD:465906"
ORIGIN      
        1 mdprapflrl ldlalpprcp gcgdiveadh rfcaicwdsl hfvgppwcag chlpfeydrg
       61 egarcgscia dppphdgvra avaygdvarr lalklkyggr laaaetmara mvrlvpeegd
      121 llvpvplhrw rlwsrgfnqa lliargvsrg tgmpvevdll rrvkgtpklq glgrrsraka
      181 vagafalapg aearlegrvv vlvddvhtsg atgdacarll krggaakvil lcwarvlade
      241 tld
//
LOCUS       WP_010543356             625 aa            linear   BCT 01-JAN-2025
DEFINITION  M1 family metallopeptidase [Sphingomonas elodea].
ACCESSION   WP_010543356
VERSION     WP_010543356.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Evnouchidou,I., Koumantou,D., Nugue,M. and Saveanu,L.
  TITLE     M1-aminopeptidase family - beyond antigen-trimming activities
  JOURNAL   Curr Opin Immunol 83, 102337 (2023)
   PUBMED   37216842
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Peer,W.A.
  TITLE     The role of multifunctional M1 metallopeptidases in cell cycle
            progression
  JOURNAL   Ann Bot 107 (7), 1171-1181 (2011)
   PUBMED   21258033
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..625
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=66991
     Region          39..470
                     /region_name="M1_LTA4H"
                     /note="Peptidase M1 family including Leukotriene A4
                     hydrolase catalytic domain; cd09599"
                     /db_xref="CDD:341062"
     Site            order(158,160..161,292..296,317,320..321,324,339,343,350,
                     399,404)
                     /site_type="active"
                     /db_xref="CDD:341062"
     Region          510..621
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
ORIGIN      
        1 mrilalalaa stmlaspala qqtapapilt tpeakdawty arpevarvth valdlradfa
       61 srtlsgtatl dvlaapgake ialdedglai arvtdaagkp lpftvgaakp dlgapltiql
      121 ngarkivihy atapvasalq wlapaltagk kkpylfsqgq pinnrswipt qdspgirqtw
      181 satltvpadl vavasgdrid gargvpagkg whkfrfrmdk pvppyliafa vgdlafqpvg
      241 pragvwteps mlaaaakeva dvekmidaaq alygpyrwgr ydmlvlppsf pyggmenptl
      301 tfltptiitg dksnvdvvah elahswsgnl vtnatwsdsw lnegfttyfe nrimeavygk
      361 eraatdadle wdglqkdiad aggteapttr lhgepgatfg qldyfkgstf lrtiertvgr
      421 arwdvylrgy fdrhafqpqt tagfladlra nlvqgdagle anlqldrway avglptnavh
      481 vqsatlkavd aqlaavnagg pvsavqpqgw atqqwlrfln gldrqqtrar lkeldetlgl
      541 sasnnayvrs awgelaianr ydpavpgigk lvgsvgrgll iypiykdlma qgdwgkpiar
      601 rfyeaskagy hptvaagvak ivgae
//
LOCUS       WP_010543444             223 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sphingomonas elodea].
ACCESSION   WP_010543444
VERSION     WP_010543444.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 223)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..223
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23749
     Region          1..221
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mltltdlrks frttevetra ldavslevga gefvaimgps gcgkstllni lgfldapsgg
       61 syrllgeeva grserertrl rrahigfvfq sfnlvdeltv eenvaiglly rsgataakrk
      121 igealeqvgi ahrarhrpqq lsggqqqrva iaralvaepk liladeptgn ldsangeqvm
      181 gllkgavaag ttvvmvthsp lhaaeaqrti rmldgrvvse tll
//
LOCUS       WP_010543452             453 aa            linear   BCT 01-JAN-2025
DEFINITION  B12-binding domain-containing radical SAM protein [Sphingomonas
            elodea].
ACCESSION   WP_010543452
VERSION     WP_010543452.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..453
                     /product="B12-binding domain-containing radical SAM
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=50995
     Region          20..380
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 mkvkmilpal teakspfwrp ikyslfpplg latlaaflsp ddevelvddh verlttddap
       61 dlvviqvyit nayrayalad eyrakgcyva lgglhvtalp deaaphadsv figpgeqtfp
      121 qflddfragc prpryrsatg rtihglppvr rdlikreryl vpnsivvtrg cpqhcdfcyk
      181 daffaggrsf ytqrvdeala eidrlpgrhl yflddhllgd rrfaeglfeg mrgmnrlfqg
      241 aatvdsvlrg dlieraaeag lrslfvgfet fspenlrasn kkqnlakdya evarrlsnlg
      301 imingsfvfg mdedgpdvfs rtvdwavrhg ittstfhiqt pypgtrlyqq lavagritsr
      361 dwdhydtrhv vyrparlspe alkagydray rdfygwsniv raaaahdntk hrakhlfyaa
      421 gwkkfeplwd lcikarqlga mtplleavls rvt
//
LOCUS       WP_010543482             281 aa            linear   BCT 01-JAN-2025
DEFINITION  S1/P1 nuclease [Sphingomonas elodea].
ACCESSION   WP_010543482
VERSION     WP_010543482.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Romier,C., Dominguez,R., Lahm,A., Dahl,O. and Suck,D.
  TITLE     Recognition of single-stranded DNA by nuclease P1: high resolution
            crystal structures of complexes with substrate analogs
  JOURNAL   Proteins 32 (4), 414-424 (1998)
   PUBMED   9726413
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Rushizky,G.W.
  TITLE     S1 nuclease of Aspergillus oryzae
  JOURNAL   Gene Amplif Anal 2, 205-215 (1981)
   PUBMED   6101052
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181127
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..281
                     /product="S1/P1 nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006308 - DNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=30575
     Region          24..280
                     /region_name="S1-P1_nuclease"
                     /note="S1/P1 nucleases and related enzymes; cd11010"
                     /db_xref="CDD:211382"
     Site            order(28,75,91..92,94,143,147,153,180,184)
                     /site_type="active"
                     /db_xref="CDD:211382"
ORIGIN      
        1 msrillllaa llgfgaaspa sayweyghet vgaiayrnvt pqvrakidal lrrqnlletp
       61 tcpagtieqa avwadcvktl gprfsyaysw hyqnidickp fdlkppcrdg ncvsaqierd
      121 vkllkdpkvp vrervmalaf lvhfvgdlhq plhagdhsdl ggnqvktnyg aftsgklnlh
      181 svwdgylaer aisqppspvr vytpaeraam wggsvadwsr eswqvardtv ypsaagegvc
      241 tagahpahld eatleklvpv arrqvvrggl rlaklldeal g
//
LOCUS       WP_010543535             440 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Sphingomonas elodea].
ACCESSION   WP_010543535
VERSION     WP_010543535.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..440
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=46258
     Region          38..419
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mgkrltwfil aalllgglig wglnlgyggt dagkatleri aygldiptqm flhlikmiia
       61 plvvstlvvg iahmggggai grvglkaffw fvcaslvslt lglllvnllq pgtglhlalp
      121 panassgvdr tafdaakfft hivptsaida masndilqlv ifslffgvgm aavgdkakpl
      181 lrglealvsv mltvtgyvml fapvavfcav artlatkglg vvgdlaffmg sfylglaalw
      241 avllgasfla igprtgllfr ylrdpillgf stasseaayp rtldaldrfg vppriasfvl
      301 plgysfnldg smmymtfasi fiaqaygihl dwatmiqmll ilmvtskgia gvpraslvvi
      361 tgtlahfnip eagvllilav dhfldmgrta tnvvgnavaa avvarwegkl depdeaepdv
      421 rplpaggphd pdkfedyags
//
LOCUS       WP_010543607             185 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Sphingomonas elodea].
ACCESSION   WP_010543607
VERSION     WP_010543607.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..185
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19761
     Region          5..149
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 martrqqkee srqaivrtaa klfrekgfdr vtvaevmega glthggfprh faskddlvta
       61 aladvfesna repllpsgdl aafvrgyldp ahrdapgsgc vfaalgpema rapaatrrll
      121 teaidqqita faaqvpgedv evrrraaiva wsaaigalll srisdsqlls deilaagrrv
      181 adrle
//
LOCUS       WP_010543690             433 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Sphingomonas elodea].
ACCESSION   WP_010543690
VERSION     WP_010543690.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..433
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=46324
     Region          7..430
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 msapfpwidv aiifvliain gifsmselai vsarparlea larmgnrgak tamelaqdpg
       61 kflstvqigi tligiiagay sgaslgepvg kriealglsa elahtlgltl viglttfgsl
      121 vigelvpkqf alrspepiaa amalpmrwls wstapvvwll dsstglvfrl lrlnresenr
      181 vtaeelhliv aeasksgvie ehersiisgv vrladrpvre vmtprtqvdw ldvnldgagi
      241 reellatpht rlpvaegsid avigvvqard iaaalfrgep ldlrklmrka pvlpdqvdam
      301 daltalrqad vpmglvhdey ghfegivtpa nllaaiagef asdaepgdnp nivvredgsl
      361 lvagatpadq laerlgidlp edrdyatvag lalavfkhlp vegevfieqg wrfeivdldg
      421 rkidkllvsr eaa
//
LOCUS       WP_010543701             364 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Sphingomonas elodea].
ACCESSION   WP_010543701
VERSION     WP_010543701.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..364
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=38489
     Region          14..364
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mtnpldaqpd errenaaepa lperlarait lagpiplsqf mgaanahyyg trdplgargd
       61 fttapeisqm fgeliglwla dlwdragrpp aaryvefgpg rgtlasdalr amgkagfapp
      121 vdfletspvl raaqkervpq aewhidlvgl pddapllvva neffdalpir qlvhtaqgwr
      181 erlvacqdtl flpvtgdrgf dpvippalrd aapgailets pasvsllral aqrllaqgga
      241 alildygyeg paigdtlqav rghafanpfd apgeadltah vdfgtlkeaa eaegltvhgp
      301 vtqgdflkal giddrarala raapergdai aadrnrlvgd dqmgslfkvl aitapgwpvp
      361 agfa
//
LOCUS       WP_010543724             357 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Sphingomonas elodea].
ACCESSION   WP_010543724
VERSION     WP_010543724.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..357
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38632
     Region          18..348
                     /region_name="BcsL"
                     /note="Acetyltransferase involved in cellulose
                     biosynthesis, CelD/BcsL family [Cell motility]; COG5653"
                     /db_xref="CDD:444374"
ORIGIN      
        1 malpasrsdp afrvtctagl ataldrvaeq apeshrflrr gwyaaalqay ggagrtlvve
       61 aervpvaalp miakgpnwlg laeipgcywp frsfplaqga splaadalld rlarivralr
      121 igpvydddaa lawlkagavr rgwtllerrl agswlldmaa lsargewprg stlrknryfe
      181 kqlrsegtvd wdfagpdfad ladierrswi atrtdgsdak ftetghgafw raaardpvla
      241 amfsaavlri dgramafsfd lvtgtrihai ansydpavak hspgrvlqyr nlvralergv
      301 aqvdwgagds gykqtmgavp gpairdwilv rpgvegwaar llrrgwgrsg qaaggqa
//
LOCUS       WP_010543746             303 aa            linear   BCT 01-JAN-2025
DEFINITION  XdhC family protein [Sphingomonas elodea].
ACCESSION   WP_010543746
VERSION     WP_010543746.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..303
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30970
     Region          5..303
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 madndsvlaa aeawrgarma latvvttwgs aprprgshll vhedgrfegs vsggcvetdi
       61 lqtaaeviag apavvkdygv adaaawevgl pcggqiavlv qpvaangfpp vlfdairaar
      121 aegrplevgt dlatgqstig gggfvnrydp prrllivgav qiaqalagla relgiattvi
      181 dprgrfltee rfpgvalddr wpdeavtalr pdqatavvtl shdpkiddaa liaalahpsg
      241 yvaalgsrrs hsarlerlsa agvspsdlar iegpaglsig aigpseials iaaamvktfh
      301 aha
//
LOCUS       WP_010543800             681 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Sphingomonas elodea].
ACCESSION   WP_010543800
VERSION     WP_010543800.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..681
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=72756
     Region          10..676
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtgrwgidaa lfslksyaag mltiylalsi gldrpywafl tayivaqpla gavlskalfr
       61 vigtvvgaga avlmvpalin apellvlais gwlglcvfvs lldrtprsym fvlagysavl
      121 ivlpsvdapg tiftvaslrv qeitlgilcg slvhgvifpr svaaflltrv stilqdaerw
      181 shdalalepv agvdaerrrl avditelhql sihlpyetar taprvrtvra lqdqlsllmp
      241 lgaavddrtv rlqahgglpp evaalltdtq awlktldrdr eeraadaaal earcaalepa
      301 vregsswhdl lllsllsrla aligahrdcr elaeqlatld rrpvsprvae llegrrgrel
      361 hvdkvgalrg aigafltlav gsaiwiasgw sdgstavmla gvflalfaaa pdpllplrtf
      421 fwgtliatil gaiygyaimp rldgfgqlaa amappllilg ammhspkwmg ialptllglg
      481 spllisaryt safasfvnga iaqlmgvafa ivmarllqsa gidqairrtl ragwadiaer
      541 snlmtppdvr gwinrmldri allaprlals grspgqplyd alrdlrtgva igelravrld
      601 maperaaplt dvlrdvgdyy rrlepeaekp edpgllahid aalhavagda daavrragtl
      661 glvslrrnlf pdadplpeaa l
//
LOCUS       WP_010543008             190 aa            linear   BCT 01-JAN-2025
DEFINITION  TMEM165/GDT1 family protein [Sphingomonas elodea].
ACCESSION   WP_010543008
VERSION     WP_010543008.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..190
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19999
     Region          1..190
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 mealltstav valaeigdkt qllaillatr fkkpvpiicg ifaatianhf laalvgaeva
       61 glldspwfry aiavsfvamg lwtlipdkld edeaprparf gaflttaiaf flvemgdktq
      121 vatvalgarf havlpvtagt tlgmmlanvp avflgkavie rvplttvhri aamlfvaigl
      181 wlaaqtagwl
//
LOCUS       WP_010543875             499 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Sphingomonas elodea].
ACCESSION   WP_010543875
VERSION     WP_010543875.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..499
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53499
     Region          1..428
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mlfkdlglse tvlaalsakg yneatpiqaq sipallegrd llgiaqtgtg ktaafmlpsi
       61 drlvasgkra qprgcrmlvl aptrelaaqi adnakhyasg tglriatvfg gtsvhknktd
      121 largvdilva tpgrlvdlld qcymillgie ilvldeadqm ldlgfihalr rivkelpakr
      181 qslffsatmp ktirelasqf ihnpvevkvt pvattaerve qfvtyvnqte kqalltmqlr
      241 nleidralif trtkhgadrv vrllagngia anaihgnksq pqreralgef rsgkvklmva
      301 tdiaargidv sgvshvfnfe lpnvpeqyvh rigrtaraga dgiaisycad derpylkdie
      361 rltrqkltvq plpenfmaea dkikstrspm pasrdeqngr ngramqhaqg rrgdgqparg
      421 grggprsdap rggeqrraeg gprsdqprrq dgaghagaga gagrgpgapk rkfnarpags
      481 sqgrpggnrg qgggagrar
//
LOCUS       WP_010543845             227 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sphingomonas elodea].
ACCESSION   WP_010543845
VERSION     WP_010543845.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..227
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24517
     Region          3..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msepvlqtrd lrrsfeqggv ridvlrgvdl dvmpgeival lgpsgsgkst llqavglleg
       61 gfegsirivg eeaaklsasg rtevrrdrlg fvyqfhhllp dfdatenvvl pqlirgaerp
      121 aaqaratell ttlglghrlt hrpnqlsgge qqrvavaral anrpplvlad eptgnldeat
      181 snrvfdefln lvrgegsaal vathnerlaa rmdrvvrlhe grleeta
//
LOCUS       WP_010543931             610 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Sphingomonas elodea].
ACCESSION   WP_010543931
VERSION     WP_010543931.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..610
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=67583
     Region          85..>582
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mgfawlgiss awaqpvlvaa dlrqqqsldg pwhwsidpyr dglagfhgep pnqrtnraad
       61 vipaevmqak prtffeydmq qspvaslpgs wighspemrl yqglvwyqrd ftaaapkpgn
      121 rvflrigaae yrsyvylngk plgehrggyt pfafevtkll rpgrnqvtig vdsvrtandv
      181 pppvtdwety ggitrsvtlv tvpdtyvdda fvrltpdgtr iavsvklegp aaagtavrfr
      241 ipglgavldg ktdgegkwda tlpvpralvr wspenpklyd iaidagadhf adrmgfrtia
      301 vkgadillng kpiflrgism heeelgadpv ramtpaaara llgeikyglh gnfvrlahyp
      361 hsesttrmad emgllvwsev plywlvnwnn pdtladarri qaenirrdrn rasvvlwsva
      421 netptndarn aflrtmiadv raldssrlvt aallsgregk simkiddpla ndldvmaint
      481 yngwysddal edlasqewrg pankplifse fgadaragyh dpvasphkfs eeyqadyyra
      541 tlamaakvpf lrgmspwilk dfrsprrqhp iyqqgwnrkg lisetgqhkl afdvlagdya
      601 kreaadaakk
//
LOCUS       WP_010543943             269 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Sphingomonas elodea].
ACCESSION   WP_010543943
VERSION     WP_010543943.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..269
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28725
     Region          1..269
                     /region_name="COG4798"
                     /note="Predicted methyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443826"
ORIGIN      
        1 mrqtlvgiav ittiaavasv aaqqpsslrq aiegavaaps rtaantardk yrhptetlaf
       61 fgvkpgdtvv eiwpsggwyt eilapltrgk gtlyaavpsg nargiealka kdaalygpir
      121 vvsfpaaagq akvpdgtadv vltfrnvhnw rmggkdgkdy speafkqmya mlkkggtlgi
      181 edhrlpesas deretksgyl kvstvrrlae aagfkfvgas evnankadta dwpdgvwtlp
      241 ptyalkdqdr akyaaigesd rmtlkfrkp
//
LOCUS       WP_010543954             624 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Sphingomonas elodea].
ACCESSION   WP_010543954
VERSION     WP_010543954.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..624
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67540
     Region          4..514
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          559..617
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mlnltditvr lggrtiidga taklpprgri gligrngagk stlvkviasq lepdggsvdm
       61 prgaklgyia qeapggsatp fetvlaadve raalleeset shdpdrigei herliaidah
      121 aapsraaril vglgfdeemq hralesfsgg wrmrvalasl lfsqpdllll depsnhldle
      181 avlwledflk sypatillvs herdflnnvv dhilhlergk ltlypggyda ferqraerqa
      241 qlaaarakqq aereklqdyi arnsarasta kqaqsrqkal armqpiaelv ddpslsfdfp
      301 npdelrppli tldmasvgyg dkpilqrlnl ridpddrial lgrngngktt larllaaqlt
      361 pmdgginssg kmkvgyftqy qveeldrddt plqhmtrnma gaspgavraq lgrfgfsgdk
      421 attnvgklsg gerarlalal itrdaphlli ldeptnhldv darealiqal ngytgtvvvv
      481 shdrhmlemt adrlvlvdqg tarefdgsld dyiafvlskd ssgggkggas kadrkearra
      541 aaearekgta lrkaakaaet elarlqaqls alekamfdpa naeaaltklt mtdlmkrrae
      601 vatkieaaev awmeaseale sips
//
LOCUS       WP_010544042             131 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Sphingomonas].
ACCESSION   WP_010544042
VERSION     WP_010544042.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..131
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14338
     Region          8..130
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 midqqggppd rqpairvttm padtnpygdi fggwlmsqmd maaglfasry srgravtvav
       61 egmkfhspva vgdevsvyae lvkvgrtsmt ieiqawrrgr hveesclvtq aqfvfvavde
      121 nkrprpveqi a
//
LOCUS       WP_010542744              92 aa            linear   BCT 01-JAN-2025
DEFINITION  FeoA family protein [Sphingomonas elodea].
ACCESSION   WP_010542744
VERSION     WP_010542744.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Gomez-Garzon,C., Barrick,J.E. and Payne,S.M.
  TITLE     Disentangling the Evolutionary History of Feo, the Major Ferrous
            Iron Transport System in Bacteria
  JOURNAL   mBio 13 (1), e0351221 (2022)
   PUBMED   35012344
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Lau,C.K., Krewulak,K.D. and Vogel,H.J.
  TITLE     Bacterial ferrous iron transport: the Feo system
  JOURNAL   FEMS Microbiol Rev 40 (2), 273-298 (2016)
   PUBMED   26684538
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Su,Y.C., Chin,K.H., Hung,H.C., Shen,G.H., Wang,A.H. and Chou,S.H.
  TITLE     Structure of Stenotrophomonas maltophilia FeoA complexed with zinc:
            a unique prokaryotic SH3-domain protein that possibly acts as a
            bacterial ferrous iron-transport activating factor
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 6), 636-642
            (2010)
   PUBMED   20516589
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Kammler,M., Schon,C. and Hantke,K.
  TITLE     Characterization of the ferrous iron uptake system of Escherichia
            coli
  JOURNAL   J Bacteriol 175 (19), 6212-6219 (1993)
   PUBMED   8407793
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10512799
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..92
                     /product="FeoA family protein"
                     /GO_function="GO:0046914 - transition metal ion binding
                     [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=9780
     Region          11..87
                     /region_name="FeoA"
                     /note="FeoA domain; pfam04023"
                     /db_xref="CDD:461133"
ORIGIN      
        1 mnasaaipvp vrlaqlhrha pgtvagvdwd qlaepearrl relgldegve vellhrsglf
       61 ggplacrigr mtvalrrhva aaihvtplar qa
//
LOCUS       WP_010544053             273 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Sphingomonas elodea].
ACCESSION   WP_010544053
VERSION     WP_010544053.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..273
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29254
     Region          13..263
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpkrtgapsq rkgsysapal dkafliiell annpqgllas emaaalgrsl gelfrivvvm
       61 eeagylqkse ltdrytatyk fldvayratp arklvvtaqp emqalaatig qschlvvaka
      121 geglviaree npgtrsfalr igatidlids csghvllafa seeravrmre rasalrdtpi
      181 deatlathlr taradgyclr qspitrgvtd iscpvlgfdg ellaaltvpy levvdgsqlm
      241 sveqslqeli rtarriseal gwrpaaaaet tpa
//
LOCUS       WP_010544050             653 aa            linear   BCT 01-JAN-2025
DEFINITION  beta-galactosidase [Sphingomonas elodea].
ACCESSION   WP_010544050
VERSION     WP_010544050.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 653)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 653)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 653)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..653
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=72603
     Region          1..613
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
     Region          607..652
                     /region_name="Glyco_hydro_42C"
                     /note="Beta-galactosidase C-terminal domain; pfam08533"
                     /db_xref="CDD:400716"
ORIGIN      
        1 mlgvcyypeh wsralwaeda rrmkalglry vrigefawsr lepepgtydf awldeaietl
       61 aaaglevvlg tptatppkwl idrypeilpv dpetgrtrgf gsrrhydfss dvylreseri
      121 vtalaerygs hpgvvgwqtd nelcchlttl saspvardaf rlwckarygt iealntawgn
      181 vfwsmeyrsf deielpvgav tetspahrma wrrfssdqva ryhdaqvail rrlsqgkfit
      241 hnfipmnetg vdnhrlardl dfaaydnypl grtdlwmada paeefrrymr tghpdfgaff
      301 fdqtrglapg afwimeqqpg pvnwamhnpr papgmvrlwt leafahgagv vsyfrwrqap
      361 faqeqmhagl lrpdssaaaa wpeveavvrd lallgleerp rgrarvalvv dveaqwlgdi
      421 erqgdsydyt rillgyyqaf rrlgvdvdfi apdgdpadyr livvpslaia radtaahlar
      481 ggavvlygar sgaktedftl petlapgalq avlpiqvqsv etlrpgcegs iawngrvyps
      541 ggwreelgld asvetlgrfe dggaalvrkd kalylatlsd atlltdllea lcaevgvatv
      601 rlsedlricr rgglvfafny aetaamapap qdatfvlggh tiaprdvaiw sek
//
LOCUS       WP_010544068             217 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Sphingomonas elodea].
ACCESSION   WP_010544068
VERSION     WP_010544068.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..217
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22131
     Region          68..217
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mriaimglal cvvaapaaaq galetpaggv rlelvagwdr pvlrlqsagg gtvdagevtg
       61 gqtgisygge igydvatssa tfvggyagls gstaaactap ssiarycvha grnltlglra
      121 gvmshgvafy aqggwsngqi kdertsalfp alngkgsdtl dgfhvglglq arlpgrayak
      181 ieyqftnyng fefnldgspi kldfdrhqis gglgvrf
//
LOCUS       WP_010544150             218 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sphingomonas elodea].
ACCESSION   WP_010544150
VERSION     WP_010544150.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..218
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24281
     Region          1..217
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mitvsdvskv yptrhgsvlv ldgvnfdvkp gekvaflgrn gagkstlvrl isgaeaptsg
       61 tirremtvsw plafggafqs altgldnmrf icrlygldwk ervayveefs elgaylkepv
      121 rsysagmrar lafavsmvve fdcflideii avgdarfhek crielfekra draliivshd
      181 apyirdhcsr vgvlnkgrlt mfddidegyv fyksiqhv
//
LOCUS       WP_010544160             225 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Sphingomonas elodea].
ACCESSION   WP_010544160
VERSION     WP_010544160.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142575
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..225
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23473
     Region          2..222
                     /region_name="SDR_c"
                     /note="classical (c) SDRs; cd05233"
                     /db_xref="CDD:212491"
     Site            order(6,8..11,30..32,43..45,71..73,94,121..123,136,140,
                     166..169,171..172)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:212491"
     Site            order(95,123,136,140)
                     /site_type="active"
                     /db_xref="CDD:212491"
ORIGIN      
        1 miivtggsrg lgrsicerll skgqevlala rsvedvpyaa lacdvsdyaq vkavakhlrq
       61 nnmkvsgvvn aagiaamnla vttppdttar vvqvnllgti yccqvfaplm mrqkggcfin
      121 fstiavalgl kgeavyaask agvegfsraf aremadfnir vnciapgpid tallrgitsd
      181 qigkivsqqi lpwqfgpdav sdvvellldd rsgslsgqvf gigga
//
LOCUS       WP_010544212             863 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Sphingomonas elodea].
ACCESSION   WP_010544212
VERSION     WP_010544212.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 863)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 863)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..863
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..863
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94909
     Region          1..>406
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 melkayqrra ldalrtfldk asirdhaqay aaacavgepg aygagyrpla glpdvpyccl
       61 rlptgggktl lashavgvar dtylgrrypv vlwlvtstti aeqtlgalkk vghpyrqale
      121 atfggavrvy giderrqlrp qdmadaatvi vstvqafrvr naedrnvyld deelephfat
      181 lpagadvarh aegprrgkpi asfanlmklh rplvivdeah nftstlsget fgrlapaavv
      241 eftatpvrsn vivsataael kaadmiklpi hlshhgswqa aiahavdnra wlegiaakdg
      301 ggirpialyq aqparegaea tvdvvkrhli edcripenri avatgdqrel dgidlfdpac
      361 tiehvitvda lkegwdcsfa yvfcsltsir srgaveqllg rvlrmpfatr rsseelnray
      421 ahvserdffl aaeglkdrli dmgfdertal eaiveqpesf ewnenqplft plelpvlrvq
      481 drpdqsswtq emlsatriad dgaggvaitf drdapdqvlr dvaaaittpe vapmtaveaf
      541 iarrvetlsp aeqgevltlp qlaierdgql eivfpetlvd vggwdlrqvd tslpgfaltd
      601 rpdtfemdie gdhvvysrid aaaelaldda tdwdvaalsr wldrttrqrd vaqpifleyc
      661 rrvvegvver iplpqlvrgk yalrraivar vaqlrreagv rgvqllmtdi apvlalgeng
      721 fsfskagydp rtpyagpwrp rkhlfsqvgd lkhggeewma avqiddhaav hrwvrnvdrt
      781 pwsyalptst dmfypdfvae ladgrklive ykgadrtdna dsrekkniga rlqevsggsv
      841 vflwaeldrg gtvarqidaa vat
//
LOCUS       WP_010544236             152 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Sphingomonas elodea].
ACCESSION   WP_010544236
VERSION     WP_010544236.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..152
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16506
     Region          13..151
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 msahhhhehh gadltraart rleeageqwt amrervfeal agfdkpasay diaeavskae
       61 grrvaansvy rildlfvgsn larrvesana yvanahpecl hdciflvcds cgqtthiddd
      121 aitknvrsaa khagfspvrp vievrgkcgn cd
//
LOCUS       WP_010544252             291 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Sphingomonas elodea].
ACCESSION   WP_010544252
VERSION     WP_010544252.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31436
     Region          8..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..283
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,219,236,264)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     213..217,224..225,228)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mfdpdydlfl dildarsisa aarrrgmstp alskrlarle qrlgarllqr ttrrlmltpa
       61 gqelldtlap mrsvlaaaes riagrhslvr gplrvtapts fgrmhvvptl paflaahaev
      121 slaidlsdef vdlldgrhdl airisgeigp glvghrlgts rrllcaapty ldvagepqtl
      181 adlarhrlla tdrqlpwqlq gpegpvvqtg qsfvrtnsse vvrelaiggc gialrslwdv
      241 aqvlaqgalr rvlpdytgse evgvfavhap dpparvrafv shlqatvaqr l
//
LOCUS       WP_010544287             388 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Sphingomonas elodea].
ACCESSION   WP_010544287
VERSION     WP_010544287.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..388
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42269
     Region          96..365
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mlistnanst hfqrqvasfv gdtpewiseh wlsiliatgi aigivlllht lrswgmrlcr
       61 nsegggtnwy tilgrtvart gnffilmtai rlvvnyaqtp vlldktitfl ftvaaafqaa
      121 iwvrevifgl iehrtrgdsp seslasavgi irllisialf aialvmvlsn vgvnvtglia
      181 glgvggiaig laaqgifgdl iaalsilfdr pfrvgdnikf dqtsgtvegi glkstrvrsf
      241 dgemhiisnr qlldkelqnl tdrtrirlpf kigvayetpp eklerlpeif raiveangat
      301 avrngftgfg assidyelia eihtgswdvg hptrdrilvg ivrklaeegi sipyptqtsy
      361 taapdgriim pypdvqpvvr mdkeeger
//
LOCUS       WP_010544330             141 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Sphingomonas elodea].
ACCESSION   WP_010544330
VERSION     WP_010544330.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..141
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14834
     Region          12..137
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mttrtatary tgfgktgkgq ltspsgvlea tpysfntrfg dekgtnpeel iaaahagcft
       61 malsfalaqa gfsdgtletr aavkleqdgd sfrisrsdlt lraevpgigr eqfealakga
      121 eancpvskll kaeialdwel a
//
LOCUS       WP_010544331             143 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Sphingomonas elodea].
ACCESSION   WP_010544331
VERSION     WP_010544331.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..143
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14961
     Region          1..141
                     /region_name="CFF1"
                     /note="Predicted sugar epimerase, cupin superfamily
                     [General function prediction only]; COG3542"
                     /db_xref="CDD:442763"
ORIGIN      
        1 mdeaqaiieq lglaphpegg wyretwrapt vaggrspgta ilflleagqr shwhrvdade
       61 lwlwhagspl alrigdaegg aveavrlggd vlggerpqal vpaghwqate aaqgwglvsc
      121 tvvpgfdfag felappgwsp pga
//
LOCUS       WP_010544356             222 aa            linear   BCT 01-JAN-2025
DEFINITION  spermidine synthase [Sphingomonas elodea].
ACCESSION   WP_010544356
VERSION     WP_010544356.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..222
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24204
     Region          <63..191
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mtprelldta dvpggeplrl frrgddhmiv lernelmnsr msgseealav mtlerlgkre
       61 arlliggygm gftlraalgv ldntakvtva elvpkivdwa rgpmaaltng clddprvkiv
      121 fddvgrviad gqnaydaill dvdngpdglt rvgndslysm rgldlarqal rpggilavws
      181 aapdpafarr mrdsgflvee vavrarqngk gprhviwfgr rr
//
LOCUS       WP_010544389             572 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Sphingomonas elodea].
ACCESSION   WP_010544389
VERSION     WP_010544389.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..572
                     /product="DEAD/DEAH box helicase"
                     /calculated_mol_wt=62496
     Region          5..387
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          458..532
                     /region_name="RRM_DbpA"
                     /note="RNA recognition motif (RRM) found in the DbpA
                     subfamily of prokaryotic DEAD-box rRNA helicases; cd12252"
                     /db_xref="CDD:409698"
     Site            order(465,470..473,475..477,479..480,486,489..492,523,527,
                     530)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409698"
ORIGIN      
        1 msisnlptrl aealeqrgys tltpvqsavl edqaagrdli vsaqtgsgkt vafglamape
       61 llageemlpp agaplaliia ptrelalqvs reliwlyspa gariatcvgg mdaskerrtl
      121 nhgahivvgt pgrlrdhler galdlsslrv avldeademl dmgfreelea ildatpegrr
      181 tllfsatmpr pivalakryq rnafqittks ddrghgdisy qavtvapadi ehvvinllrl
      241 heaetailfc atrdnvrhlh aslmergfaa valsgehsqs ernhalqalr drrarvcvat
      301 dvaargidlp tltlvvhvel prdaetlqhr sgrtgragkk gtavlivpyp rrrrveqmlh
      361 garipavwid aptpeqiraa drerliaall qpietdeedv alaerllaek tpaeiaaalv
      421 rahrsqlpep eelieatpea rraaqqerhr pgfddtvwfr mdigrrqnad prwilplicr
      481 rghitrnevg airiaaneth fqipsqlaak faaavdkfar tagddddgir ierateapqp
      541 garadgptrr gppnrsnang kpggfrkgpp rr
//
LOCUS       WP_010544400             146 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Sphingomonas elodea].
ACCESSION   WP_010544400
VERSION     WP_010544400.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 146)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..146
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16356
     Region          8..141
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 msdriarpaa rillldgqgr vllfrfdpgd rppfwctpgg avdpgeryed aarrelweet
       61 giradpgpev aqrivefvti egvpvwader yflvrteaaa ietsghtale qrvmrgwrwf
      121 trqeiaahae pifpedllem laalga
//
LOCUS       WP_010544412             319 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Sphingomonas elodea].
ACCESSION   WP_010544412
VERSION     WP_010544412.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..319
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33382
     Region          86..312
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mpqripttia rvrhglalga vvlagvatpp alaqndkmap iatpaqpgai elgtgplpga
       61 kaaeswhsqy gsvftrnvtv atltpflpdp vkangtaviv apgggftsls mqnegwdvak
      121 altahgvaaf vlkyrlnqtp qelagyeaam karfaggagg ppraadpkam magiatqvtd
      181 araafalvrk qaaewhvqpe rigmvgfsag amltlatald gqdakpafig tiygplsnfq
      241 vpadapplfv alaaddplfg nngfglidsw raakrpvefh lfeqgghgfg mypkkttstg
      301 wfdefvrwmt mhdwikpaa
//
LOCUS       WP_010544426             324 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Sphingomonas elodea].
ACCESSION   WP_010544426
VERSION     WP_010544426.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..324
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33846
     Region          81..319
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 maeplsrrtl legiaatgal yalparaada ardevlplwp giapgapatl ptpkydqrsk
       61 dptfedrwqt gigqpsltvr raaqpngsav mlipgggygf lavdnegeeq arwlnaigit
      121 afilryript egwanratvp ladaqrglrl iraaaarygl dparvlalgf sagghlagsl
      181 atrhdervya pvdaadrlsa rpdlaglvyp vvslaapfth ggsrdnlfgp gadpkalaaa
      241 svenrvtagt ppiflthasd dglvpiansl alyqallaag rpaelhafdq gghgfgvrla
      301 ktipasawpt lfaafarrhg vlka
//
LOCUS       WP_010544460             247 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Sphingomonas elodea].
ACCESSION   WP_010544460
VERSION     WP_010544460.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..247
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26557
     Region          6..241
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 milrsdettd vdipgsgamr ihwfrpaveg tfpglvlyse iyqvtapirr laamlagngy
       61 vvavpevyhe yepagtvlay dpagtdrgna lkftkpvaaf dadaaatlta laahpacngr
      121 lgsfgvclgg hlayraaldp rvsaaacfyp tdihsgtlge gkaddslarm adlnaemlfv
      181 wgrqdphipf agreairagl eahgiayewh elnaqhaflr degprydpal flhsmaitla
      241 fyrrtlg
//
LOCUS       WP_010544524             203 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Sphingomonas elodea].
ACCESSION   WP_010544524
VERSION     WP_010544524.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21686
     Region          12..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mktaactvak grprefdvde altaalrifw skgyegaslt dlteamgitr pslyaafgnk
       61 ealfckaldl yereklcyig raleaptarg vaeallrgal erqrdtsdpk gcmgvinsva
      121 cgveaesire evlkrgesak raivarfera rtegdlpgta dpegltayii aliqgialqg
      181 gsgatcadle rlvqtslamw par
//
LOCUS       WP_010544592             508 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Sphingomonas elodea].
ACCESSION   WP_010544592
VERSION     WP_010544592.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..508
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55226
     Region          1..506
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 msstieeler rraaarlggg qkridaqhak gkltarerle vlldqgsfee ldmyvehnct
       61 dfgmegqvip gdgvvtgsgt ingrlvfvfs qdftvfggsl serhaqkick imdmamkvga
      121 pviglndsgg ariqegvasl ggyaevfqrn vlasgvvpql slimgpcagg avyspamtdf
      181 ifmvkdssym fvtgpdvvkt vtneivtqee lggavthttk sgvadvafen dieallaard
      241 fvdflpasnr eapperasdd pwdridesld tlippnanqp ydmhelirkt ldegeffelq
      301 pahagnilig fgriegrtvg vvanqpmvla gcldinaskk aarfvrfcda feipivtfvd
      361 vpgflpgvgq ehsgiikhga kllfayaeat vpkitvitrk ayggaydvma skhlrgdlny
      421 awptaeiavm gakgaveiif rgrtpeeiae rtaeyerrfa npfvaaskgf vdevimphst
      481 rrrialglrk lrnkqlenpw kkhdnipl
//
LOCUS       WP_010544630             303 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Sphingomonas elodea].
ACCESSION   WP_010544630
VERSION     WP_010544630.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13300132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32324
     Region          12..>128
                     /region_name="PRK11242"
                     /note="DNA-binding transcriptional regulator CynR;
                     Provisional"
                     /db_xref="CDD:183051"
     Region          94..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,147,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mklpdfeawa vfasvvehrs fsgaalalgv skatvskait rleerlgtal fhrtsrrltl
       61 tdsgqqlaeh aqriledgqs aeeaafesas apsgvvrlaa pltfgarhls gliaefmalh
      121 pqikveltls dafidivgeg idvalriael pdsslrarrl gpvtihvvaa pgyferegrp
      181 qhpadlarha cfvytntatp gvwrfkkagg eeaavrvdgp lrtdngeaml palraglgia
      241 rlpgflvdae laagrleavl adwvagsvgl hlvtppgsrr pvrvealidf lterlrtlcv
      301 raa
//
LOCUS       WP_010544643             145 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Sphingomonas
            elodea].
ACCESSION   WP_010544643
VERSION     WP_010544643.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..145
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=15311
     Region          1..138
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mirvsvdpap ialgvevaal eeggaggvat ftgvvrtddg vealelehyp gmteaalcal
       61 aeaavarwnl lgvsivhrvg rmtagerivf vgtaaahrre aldscaylid rlktdapfwk
      121 rewlaggtrw vepragdeea aavws
//
LOCUS       WP_010544672             499 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Sphingomonas elodea].
ACCESSION   WP_010544672
VERSION     WP_010544672.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..499
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=52720
     Region          17..481
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(60,62,66,69,73,106,109..110,119..126,131,134,137,
                     230,234,237,240,242,417,419..420,422..423,426,429..430,
                     432,434..437,446,450,452,466,473..478,480..481)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(146..149,157,172,175,205,222..225,228,246..248,280,
                     382,384,410)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(149,246,277,280)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mrvidhviag aagagatrha dvfdpnsgav qarvplgtaa dldravaaaq aaqpgwaatn
       61 pqrrarvmfr fkelveanmd alahmlsaeh gkviadskgd iqrglevief acgiphalkg
      121 eytqgagpgi dvysmrmplg igagitpfnf pamipmwmfg vaiacgnafl lkpserdpsv
      181 pvrlaelmle agapqgilqv vqgdkemvda ildhpaigav sfvgssdiah yvyqrgvaag
      241 krvqamggak nhgivmpdad ldqvvadlsg aafgsagerc malpvvvpvg dktadalrek
      301 lipairslrv gistdaeaqy gpvvnaahka rvenwiqtgv degaelvidg rgfslqgheq
      361 gffigpslfd rvtpgmksyq eeifgpvlqi vrapdfetal rlpsehqygn gvaiftrngh
      421 aarefaarvn vgmvginvpi pvpvayhsfg gwkrsafgdv nqhgmegvrf wtkvktvtqr
      481 wpdggvgdaa nafviptmg
//
LOCUS       WP_010544677             257 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Sphingomonas elodea].
ACCESSION   WP_010544677
VERSION     WP_010544677.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..257
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26802
     Region          7..257
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mfagitlaem lpyvavgfaa qlvdgalgma fgvisstllv svlgiapata sagvhlvetm
       61 ttgvsglshv lhrnvnwrlf arllvpgmig gvlgayvltt ldasvtrpfv maylsaigly
      121 llfrairfpp nqrepkivep lglaggflda aggggwgpvv tsnllvqgaq prttigtvnt
      181 teffltltis atflfhigsq gftpefwhpv lglliggvia apfgamfakr mpvrlllslv
      241 gvvltatsaf slyralm
//
LOCUS       WP_010544702             597 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Sphingomonas elodea].
ACCESSION   WP_010544702
VERSION     WP_010544702.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..597
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=67190
     Region          1..594
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mttldlwpig ncqvsalidr tgrfvwgcvp rvdgdplfsa lvggeepegg ywdialdgvv
       61 sveqrylrna pilvsrhtdv agnaievtdf cprfqrlgrv yrpvafariv kpvagsprir
      121 vklrpacgwg kscktriggs nhlrylvepm tlrltttapv gmvdeerlfr vekplhfflg
      181 pdesfsgdva etvddmllns iaewqhwvrg lniplewqdv virsaitlkl cqheetgaiv
      241 aalttsipeh agsqrnwdyr ycwirdayyt vqalnrlgal dvletylgyl rnivddakae
      301 prgghiqply gvlgeatlee reapdlagyr gmgpvrvgnq ayeqvqhday gqivlsnvqa
      361 ffdqrlyria giedfealer vgerawqyhd spdaglwelr trqsvhtysv amcwaacdrl
      421 anaahvlgle errafwqsra dtirttvfdk awraetqrfs atfsgddlda sllqllemrf
      481 lapddprfad tlkaveaglr rgstmlrydt eddfglpeta fnfctfwlie alhitgrtde
      541 aralfeemlt rrtaagllse didpvtgelw gnypqtyslv gmincavlls kpwssir
//
LOCUS       WP_010544492             464 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramate--L-alanine ligase [Sphingomonas elodea].
ACCESSION   WP_010544492
VERSION     WP_010544492.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Sangshetti,J.N., Joshi,S.S., Patil,R.H., Moloney,M.G. and
            Shinde,D.B.
  TITLE     Mur Ligase Inhibitors as Anti-bacterials: A Comprehensive Review
  JOURNAL   Curr Pharm Des 23 (21), 3164-3196 (2017)
   PUBMED   28201974
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..464
                     /product="UDP-N-acetylmuramate--L-alanine ligase"
                     /EC_number="6.3.2.8"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008763 - UDP-N-acetylmuramate-L-alanine
                     ligase activity [Evidence IEA]"
                     /GO_process="GO:0007049 - cell cycle [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=47817
     Region          1..448
                     /region_name="MurC"
                     /note="UDP-N-acetylmuramate-alanine ligase MurC and
                     related ligases, MurC/Mpl family [Cell
                     wall/membrane/envelope biogenesis]; COG0773"
                     /db_xref="CDD:440536"
ORIGIN      
        1 mqhgkatffv giggsgmmpl amilagrgar vsgsdrsldg grlaskfdwl rsrgvdlfpq
       61 dgsgvqsaeq vvvasaaiep tvpdmvraae lgcarmsrae llaslfnasa lpigvagtsg
      121 kstvtgmigw ilhacgrdpt vmngavmknf agpdapfasa lvgagdafvs evdesdgsia
      181 nywpriavln nvsldhksle elrllfgafa gkaattvvnv gdaesaalaa gldrgrtltf
      241 avegeadlma rnlapeafai gfdlvtgeta rgvrlqvpgr hnvanalaai gaataagvsl
      301 adacaavegf tglrrrfelv gtaggvsvid dfghnpdkia atldtlhafp grllllfqph
      361 gygplkvmrr elvamfatkl gaedllvlpd pvyhggtvar evtsadivtd vaatgaqalh
      421 fpgreaaaah lvaqarpgdr ivvmgarddt lsqlaeemvt rlak
//
LOCUS       WP_010544339             280 aa            linear   BCT 01-JAN-2025
DEFINITION  class I mannose-6-phosphate isomerase [Sphingomonas elodea].
ACCESSION   WP_010544339
VERSION     WP_010544339.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Sagurthi,S.R., Gowda,G., Savithri,H.S. and Murthy,M.R.
  TITLE     Structures of mannose-6-phosphate isomerase from Salmonella
            typhimurium bound to metal atoms and substrate: implications for
            catalytic mechanism
  JOURNAL   Acta Crystallogr D Biol Crystallogr 65 (Pt 7), 724-732 (2009)
   PUBMED   19564693
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Jensen,S.O. and Reeves,P.R.
  TITLE     Domain organisation in phosphomannose isomerases (types I and II)
  JOURNAL   Biochim Biophys Acta 1382 (1), 5-7 (1998)
   PUBMED   9507048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..280
                     /product="class I mannose-6-phosphate isomerase"
                     /EC_number="5.3.1.8"
                     /GO_function="GO:0004476 - mannose-6-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009298 - GDP-mannose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30362
     Region          11..178
                     /region_name="cupin_PMI_type_I_N_bac"
                     /note="Phosphomannose isomerase in bacteria and archaea,
                     N-terminal cupin domain; cd07010"
                     /db_xref="CDD:380413"
     Site            order(15,36,38,52,61,63,65,80,82,84,140,142,150,152,156,
                     160)
                     /site_type="active"
                     /db_xref="CDD:380413"
ORIGIN      
        1 mpatllathr vekpwgrhtl ypgfadpapd gepvgevwfq tpgnstpdll ikylftsekl
       61 svqvhpndeq aqavglprgk decwiildaq pestialgtk qpytrealra galdgsiedm
      121 ldwkpvkagd ffysasgtvh aigagitlie vqqnsettyr lydygrprel hldegiavse
      181 pvpfvphpmp gavapdrtil vegpkfvler wegghrrfdl pegttgwlip vkgegvvdgv
      241 afkagecltl eghvelqaev gsdllfaypg darvpsmdaa
//
LOCUS       WP_010544809             322 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Sphingomonas elodea].
ACCESSION   WP_010544809
VERSION     WP_010544809.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..322
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34700
     Region          27..315
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mdeptrasis pqspegrrlg vggkvprrla elgvtermle iakrvaigtf negftyagnl
       61 aylslvtlfp ffivatalas lvgrtgtgvh aleaflqtvp pdvakllrdp vievlqtrst
      121 ggllwfgalv glwttagfie tirgivrqay gvsldkpfwr yrlgaigmiv aavlmvmlaf
      181 afqviltgve qflyrilpwa teaqrfasag kavpafalfg alyvlffalt psryrsrryp
      241 kwpgalcttt wwltvtgvlp wvlsamggyg atygslagvm vsliffflvg lglvvgaeln
      301 aalaevpdpg legeqgqeiq kt
//
LOCUS       WP_010544823             755 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Sphingomonas elodea].
ACCESSION   WP_010544823
VERSION     WP_010544823.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 755)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..755
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81387
     Region          48..736
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mttsallrvl llgsaalttp salaaaahsd tpavqgaqpd etapqdsgei vvtaqrrtea
       61 akdvpvavta iggekldvln ssgldirfls artpslqies sfgrtfprfy irglgntdfd
      121 pnaaqpvsvv ydnvalenpm lksfpafdla rvevlrgpqg tlfgrntpag vvklesqrpt
      181 dqyeargsvs watyntvnad lalnaplggg fslrvsglvq hrdnwvvnds tsaqsvanrk
      241 legytdragr vqlaytngdf nallnvhgrd legtprvfra glfqqgsnnf sagfdpkrvk
      301 ldgytsqwle qwgsnlqldy hfdgigtlys itayerakvq stgdvdggdt ytfpalglnn
      361 alfpsntggi tspkefsqel rfatdqfgaf rgqaglyyfd qnldyseygy plgggaqnqn
      421 ighvnineny gvfasgeyka tdaltlragi ryshdrkndv itgfgplttg ltlpvqtkvk
      481 geavtwdasa tyaltpdvnv yarfatgylg paiqnrvtfg svpttagkqf tksaeagvkg
      541 slpaqglnya ltgywfrtdd lqltavggas nstrllsadh vngygveaef syrpvrgldl
      601 tasgsynftq irdpglavav cgslctvtdp trvvngttva lidgnrlpqa prfvlnatar
      661 ygvplangge vyaytdwayr seinyflyea kefrgrslle gglrigyrap qgyevaafar
      721 nilnqiraqs aidfnnltgm inepriigge irfhf
//
LOCUS       WP_010544837             206 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Sphingomonas elodea].
ACCESSION   WP_010544837
VERSION     WP_010544837.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..206
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21987
     Region          61..206
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mrtklfiatl iassalaapa laqsqapdqt fagshvevit gwdrvndkss ydasrdgvty
       61 ggnigydiqr gstvfgvege vtgssisdrt snvlnagdrl rvkagrdlyv ggrlgfvagp
      121 rtliyakagy tnaqfitdyd spattpavsl rqrdnydgwr lgagaefklt dkvfakaeyr
      181 ysnygsqagg vdperhqiit gvgvrf
//
LOCUS       WP_010544893             396 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphoglycerate kinase [Sphingomonas elodea].
ACCESSION   WP_010544893
VERSION     WP_010544893.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..396
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41290
     Region          7..394
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 martfktldd mgditgkrvl vredlnvpma dgkvtddtrl raaiqtvael adkgakvlvl
       61 ahfgrpkgvp saefslaqvv kpfeqvlgrp vryidwegda asvatlndgd iallentrff
      121 ggeekndpav vdrfaalgdl yvndafsaah rahastegla hklpafagrq meaeldaldk
      181 algnpehpva avvggakvst kldvlkhlva rvdhliiggg mantflaarg vdvgkslceh
      241 dltgtaeeil daadaagctv hlpydvvvak efranppvrt vnvhevaade mildvgpaat
      301 ealadvlktc ktlvwngpmg afeippfdaa tvslartaaa ltkegslvsv agggdtvaal
      361 nqagvagefs fvstaggafl ewmegkelpg vaalar
//
LOCUS       WP_010544906             582 aa            linear   BCT 01-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Sphingomonas
            elodea].
ACCESSION   WP_010544906
VERSION     WP_010544906.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..582
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=63194
     Region          54..582
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtlepivplp adwpkaplta vdalltapga kfemetveir giptrvwkns ppnaailarl
       61 argygdrpft vyqdervsye anyratchla swmqaqgvak gdrvalamrn lpewptiffa
      121 avsigailvp lnawwtgael eygmkdsgak llfvdgerhe rlkqcyaalp dlervvvsra
      181 ctplesevva lesivgpctg waalpdiafp evaiapdddv tlfytsgttg npkgavgthr
      241 nlmtniltsg ysvaramlrr gempppappy kvgllviplf hvtacsaglm aliaaggtvv
      301 fmrrwepvea meiiqrekvn qtggvptiaw qllehperas ydlssldtis yggapsapel
      361 vkriyeefga lpgngwgmte tmatvthhtg edyiarptsa gppvpvaelk imdvdgtrel
      421 pvgevgelwa kgpmivkgyw nkpeataetf regwvrtgdl arldeegfly ivdrakdiii
      481 rggeniysse vedvlyahpa vtdaaligvp hralgeepva vvhlapgtsa teaelqafvr
      541 eriaafkvpv airfseetlp rnangkilkk dlkalfvrdq va
//
LOCUS       WP_010544902             413 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Sphingomonas elodea].
ACCESSION   WP_010544902
VERSION     WP_010544902.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..413
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=44504
     Region          51..378
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mdqrtgrigd ehgggggipd pllgadlpee mdaepqtpsl rrdrlmaalv liagmglvla
       61 lpfalqagar fflpvtaslv iaialvpmle wlerhrlpap iaaflcvllf ltaanvalas
      121 ivvpawqwir rlpesipkiq hnleplirfy snlerfvnkt lnnfasapvr qpvvqaaqpp
      181 tslmdlftts apsaliemff ailviyffls gwtrlrrrai tsrssfggam atarviqdvv
      241 ddtsaylgti tlinftlgli vagalwlmgm ptplmwgglv allnyipyig pviaalllav
      301 gglmsyadig tamvppaimi aahlveanvv tplivghrlt inpimilisl sfwgwvwgtt
      361 gallavplli iiqtvlnaag kpdiagflfe qgtlvrdpsd irsrrranld qsg
//
LOCUS       WP_010544957             464 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Sphingomonas elodea].
ACCESSION   WP_010544957
VERSION     WP_010544957.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..464
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46943
     Region          18..441
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,143,
                     146..147,150,271,274..275,278..280,283,311,315,367..368,
                     372,376,392,395..396,399..400,403)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mqtdglplpr rltaiaavsf gtalvvidga iatvalptia rdlhvdssaa vavvtvyqlv
       61 lvmlllpfsg lgnrvglkrl yqmgqivftv atilcffaks lpfllivraa qaagaaaals
      121 vssalvrqiy pakqlgrglg vnsvvvsvss aiaptlgglv lgvgpwpwvf asavpfavas
      181 lllgrslpdi prskapfdvl gavlcaamfg lvigglesav hgdspvvsaa vviagiaigv
      241 ifvrreqgea epilpvdlla rpvlalstig aftafvatmt lllalpfrlq hgygfapsev
      301 gaaiapwplt tmfvaplags lsdrypagal ggigmgiaia glvalaflph dpsffdiawr
      361 msltgagfgm flspnarlii gsapveraaa agglisttrm vgqttgatlv aallamgvga
      421 gmtpalvasg laliagicsl arlrpairnp gkveadqaqp aqmg
//
LOCUS       WP_010544974             189 aa            linear   BCT 01-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Sphingomonas
            elodea].
ACCESSION   WP_010544974
VERSION     WP_010544974.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..189
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=20303
     Region          1..139
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mrrlwhdrgg atliefaill pvlmallmgl mdisyqayvq avlegavqka grdstieaad
       61 tatidarvvt svrrvagnat vtpsrrsyas fglikaesyt dnngnnryda gdcftdvngn
      121 gqwdadpgiv gqgsasdvtv ykvtvtygrl flmagligws nqvvlsastr fknqpynaqs
      181 vptqqvlck
//
LOCUS       WP_010545037             492 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Sphingomonas elodea].
ACCESSION   WP_010545037
VERSION     WP_010545037.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..492
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50974
     Region          <333..454
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mffrddhgsg laggggglar aipavvpari gkrlatldlv pdlgadigsp twfrgaatca
       61 alcaatwmls pgfdrpitgm tpapltgeae qaqqaqaiap iakgsgtgvh vassklvrpl
      121 tdtperpiie hearlgsgtm lrsvlqrsgv geadagivas lvsgamplgq iqrntvlemt
      181 lgrrvdtsqp rpleklafra afdrrieiar tgaalaiksi piaidrtplr vqgligssly
      241 rsaraagapa kavetflrtl strvsvsklg sackfdlilg qaraatgevq ygqlmyagvt
      301 gcangvqlap wesdgktewf dasgtggktg mmtmpvngrf ssafgmrmhp ilgfnrmhkg
      361 idiaapygsp vyaavdgvvr vaggsagygn lvridhgggf gtgyahlskv mvrpgqsvrk
      421 gqqigrsgns glstgphlhf ettrngqavn pravsftsvr rltggalgaf raklhglmav
      481 pvghgvqkda ae
//
LOCUS       WP_010545012             817 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 3 protein [Sphingomonas elodea].
ACCESSION   WP_010545012
VERSION     WP_010545012.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14303124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..817
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85196
     Region          61..>452
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          424..637
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          664..805
                     /region_name="Exop_C"
                     /note="Galactose-binding domain-like; pfam18559"
                     /db_xref="CDD:436577"
ORIGIN      
        1 mpaslkllla ttilaatpai aqqaptalss iahpekwpaa ksqglidpat ekfvsdlmak
       61 mtleekvgqm iqadigsitp edlaiyplgs ilaggssppi gapdrsprgp wlataqafqk
      121 aalarkvght pipimfgida vhgnnnviga tlfphnvglg amrdpalmek igrataeeta
      181 svgidwafgp tlavpqderw grayegysee pevvrsyaga mirglqgapg tkdrlqkgyv
      241 aasakhflgd ggtfggqdqg dtrvseeeli rihnagypga inagtmtvma sfsswngtkm
      301 hgntslltdv lkrkmgfdgf ivgdwnghaq vpgctptdca atfnagldma mapdswkgly
      361 estiahakag tipmaridda vrrilrvkvq mglfnaarpy eskpeligap ahraiareav
      421 akslvllkns gvlpvkasan vlvagpgads maqqsggwtl swqgdgnpns mfpngetifa
      481 giqaavkagg gsatlsadgs fttkpdvaiv vfgeepyaem rgdvrtlefq pgdkqalall
      541 kklkaagvpv vsvflsgrpl wvnpelnasd afvaawlpgs egagvadvli gdkagkprrd
      601 ftgtlsfswp ktagqftlnr gepgydplfa fgyglsyakp gtvgalsevs gvdaslanis
      661 tffakgvtpa pfsfasdski trktidgpat qegaqqltwp tgpatlrigg gdldlsretn
      721 gdlslrlvyr vdaaptgpvk lsmeggkntg tidatslftg ksgwqtvnil lkcyqkngvd
      781 vtkvnapvvl qasgpftlsl aeakivsdpa nsvcpgq
//
LOCUS       WP_010545048             227 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Sphingomonas elodea].
ACCESSION   WP_010545048
VERSION     WP_010545048.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..227
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23897
     Region          21..226
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtiqavgaan didladrfar lfacseavag dlvaaastrr hgsgttlihq gavcgrvmvl
       61 ldgaaraamv tldgrvlqvg eyrpgdifgg vdpgreqaae ilaiaptlia sfatadfyal
      121 aerharigvv laramvrqfg altqlvsarl tlsatgrvha ellrmaragd grwirpspvl
      181 sdlalrvqta retvsravsa lerrgivcrh edgleivapa rlealiv
//
LOCUS       WP_010545062             420 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Sphingomonas elodea].
ACCESSION   WP_010545062
VERSION     WP_010545062.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..420
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46013
     Region          45..305
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtddafalsr rsfldrilla sagagmsaaa pwaamaaddv vkgprvrigv igtgdrgrtl
       61 iqnlnktrnc avaalcdtfe phlararayv pantptftdh rkmldarqid avviatpldl
      121 hapqtmdald agypvfceka martiadcsa mvtrarkrgk vlqighqrlf nptylnalkr
      181 aqageigpit qiraswhrnr swrrqvppgg tereinwrly rdrsaglmte lathqlqvan
      241 wflgglptrv mgsgsicfwk dgrdvydqva liydypdgrk liytsmlnna rygceeqiqg
      301 skgtiepelg riyqevqpga vpalarmrad vqagrkttvp iggatwfpel pvttpgesig
      361 wgeydetmlq fegfgeavrs grevpgllaq ayhasiasll geqaidqgqa lawptdlvtf
//
LOCUS       WP_010545070             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Sphingomonas elodea].
ACCESSION   WP_010545070
VERSION     WP_010545070.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33293
     Region          8..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..293
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(113..114,116..117,120,124,126..132,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrldrfdlnl lvafhtlmee rsvtraaerl hltqpamsaa lrrlresfnd pllvangkqm
       61 vpsphaeela prvaeivgna qalissstlf dpqtsrrhfr iaasdyvtti avqpllaela
      121 qqapgircsv ipphpgiteq mergqvdcii speqfqgqgh ptellfeeeh vvlgwsenpl
      181 fakpitqedy daaghvvvel sntpafaeqf vrargdtrri evtvssftlv pwllpdthri
      241 alvharlarl figklplama pppfplprmr emiqfnrara tdrglvwlre glrrhagn
//
LOCUS       WP_010545084             157 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Sphingomonas elodea].
ACCESSION   WP_010545084
VERSION     WP_010545084.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..157
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16885
     Region          <11..142
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mrirprsspn leaeypepnl iplaaearar tiwfdeladt vmmaegsail gnrfvkprvm
       61 qspcdhdaad qaehqqlppi ldylertipd sgflvedrlt ladiavaspl atlgcigvcv
      121 dsaryprtaa yidaihardh aqvkamggpv akapata
//
LOCUS       WP_010545135             545 aa            linear   BCT 01-JAN-2025
DEFINITION  ribonuclease J [Sphingomonas elodea].
ACCESSION   WP_010545135
VERSION     WP_010545135.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..545
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=58475
     Region          2..545
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mtprnellfl alggsgeigm nvnlygcdgk wlmvdcgitf gdasypgidv ilpdlqfied
       61 rvddllgivl thghedhiga lpylaadlgv plyatpftag lihgklaeeg iddrvelnvv
      121 keegpfdigp ftitytplah sipegnavli etpygkvfht gdwklddaps lggsataeel
      181 taigdtgvla lvcdstnvfn peasgseaev rkgldeviag akgrvlvttf asnaarlqtl
      241 gevardtgre lcvagrsldr iirvakatgy lrdfpelidf dkamtlpasr vlivatggqg
      301 epraalnria egshvlklhq gdlvvfssrq ipgneiaigk imntladkgv diitdrqafv
      361 hvsghpgrpe laamykwirp eiivpvhgei rhmheqarfa lsegvpkavk qqngeiirla
      421 pngpakigha pvgrlvldgd vilpadgttm gerrrialyg qmsvavaidr kgkllgapqi
      481 rvqgvpveed rddlidaaad aaveavkkdw rdreklresl rlavrrvavr ftgkkpvvdv
      541 lliea
//
LOCUS       WP_010545192             164 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Sphingomonas elodea].
ACCESSION   WP_010545192
VERSION     WP_010545192.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..164
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=17489
     Region          6..133
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mstpdtandr kivtfslakq ifgidmsali eirewdeptp lpnvpsfikg vtnlrgnvip
       61 vvglaerlgw epsvlharsc ilvvnimgkq agflvdevnd ivginvgeiq papavetale
      121 esviaglvri atrakdgtrd engsmvllld lnalsltkhl dlaa
//
LOCUS       WP_010545252             687 aa            linear   BCT 01-JAN-2025
DEFINITION  M13 family metallopeptidase [Sphingomonas elodea].
ACCESSION   WP_010545252
VERSION     WP_010545252.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..687
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75955
     Region          29..687
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mqlkhvllas tlsiaaiaap alsrnpqqaa apsteatryg swgfdiagmd rsvkpgddwy
       61 rfvngswmdr tkipddrssf gafavlrdls emrlrtlieg yqptdtahpd rrkaailyrg
      121 fldeaaierl dakpllqrlq plkaaktkae larlmgasig gfgasffgvg vsddakqpdv
      181 yalylrqsgl glgdrdlyld akfapqvary rqyvaqllgm agwpdaaaaa dkvvametri
      241 aqahwtraqs rdrdktynpv tvaalkaqap gfawdpfwqa agltkasrvi vaqnsavpki
      301 aqvfadtdla tlkaweafri addispmlsk rfadaqfdfr skfmngqpke rerwkravsf
      361 teraigegvg rdyvalyfpp eskakmdvlv gnlrvalagr iknlawmspa tkeqalaklq
      421 gftvkvgypt kwrdyskldv rpgdlvgnae ragrfewdyr rnrlggpvdk aewgmtpqtv
      481 nayynsvkne ivfpaailqp pffdpkadda vnyggiggvi gheishgfdd qgrksdgngv
      541 lrdwwtpeda tkfeaqavrl gaqyeaysfe glpglhingr asmgenigdl ggvlialday
      601 haslggkpap vldgftgdqr fflgwgqvwr tlfrnealrq qlvsdphspg qiravnplrn
      661 vdawyaawni dpsqkqyvap edrvriw
//
LOCUS       WP_010545289             367 aa            linear   BCT 01-JAN-2025
DEFINITION  lactonase family protein [Sphingomonas elodea].
ACCESSION   WP_010545289
VERSION     WP_010545289.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..367
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37968
     Region          30..365
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mtnashilsr rtligagmgi aacpstllar tsaatgliag tyangggpgl vrlvagpqgw
       61 raatplpair nvsfgvrsat tglrylldeq tegrlgiyda rfnrladlst lgadpchaal
      121 spdgrrlava nyssgcvalf aldragrplg egtriqhegs gpnrdrqagp hahwvgftar
      181 gsqlhsvdlg adavflhrlg aggaidtsia yrteagagpr hlarhprlpv aylvtelant
      241 vtvlrahpdg rftalatlst lpkgfagasa aahiavnaag trlyisnrgh dsiavfaiqr
      301 dggltllqha gcgghwprlf llreaggell vanqrsgnia rlplardgrl gtpsrglamp
      361 gvvfvsa
//
LOCUS       WP_010545331             288 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Sphingomonas elodea].
ACCESSION   WP_010545331
VERSION     WP_010545331.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..288
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30031
     Region          48..288
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mpiaprwqaa etialwpagp pggsfrpapr aadlpesfrt giarpdlrlf rpearngral
       61 lvlpgggygf vsvrnegldi advfcplgyt vfvltyrlpg egwtdradvp lqdaqramrl
      121 iraradaegf dsdaiavlgf sagghlaasl ltegpaplyp pvdaadaaaa qplaagllyp
      181 vvamagaaah agsraallgd apaptlvarr spaarigadt ppmflvhaid daavpfensl
      241 llaramaeaa rpfelhlfqe gghgfgtgpr naaaggwpgl fdrwlrrl
//
LOCUS       WP_010545338            1046 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Sphingomonas elodea].
ACCESSION   WP_010545338
VERSION     WP_010545338.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..1046
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=111750
     Region          1..1024
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mnrwlhwvth hrlavaavsa ivaavglwsy fslqidaipd itgvqvqint pvaalapeei
       61 erlvtlpier amggqpgldq trsltktgls qvtllykdgt dplkarqlvt erlnavrdql
      121 pagstpqlap ittglgeiyy ytlewrqppq gmsaerqlme lyeaqeytvr pmlravpgva
      181 dvnsngglee qyvvqpdpak ltahgvtaae laqavagnve nagggivarg aerfavrtda
      241 rvmsaeeiga ipvkfaggvl piqvrdlatv vtshgprqga atqngretvl gtammlvgqn
      301 srqvalriea alpeiqdalp kgmvidrqys radlvdrtia tvernlgega llvalvllvv
      361 mgnwraaliv alviplaflv tvtgmhaigv sgnlmslgal dfglivdgai vvvenglrll
      421 aarrqekggd lspeerraiv aeaarsvarp tffgiaiial vyvpvlslgg vegklfqpma
      481 qavmlaivag lawtftivpm lsawllrapa thaepgeekg liglanrayt pvlsaalahp
      541 lllvigaaal lgatflafrt lgaqftpqld egaitamvyr pvgmslersl aieqatevai
      601 rkafpqitht fsrigtseva tdpmppeqnd lyifyapekd wpegegkprt kaaliagiek
      661 vaqqvyadqh fefaqpiemr fnemlegvra dvavkiygdd ydvleraaaq akailekqpg
      721 tegvafetsg rpktivveld haallrlgig tqevnkaisd avagaevgfi phnaarhaiv
      781 irmaeglran rqailalplr vgpfgmvpls rvarlretqm vepilhddgn rraalmvnls
      841 tsdlagyvdk araelgrqik lpqgyriefg gqyhqleaaq rrlaivvpla lllifalvya
      901 algslreaai vytgipfait ggvlalwlrg mpfsitaaig fialsgiaml nglvlidhin
      961 glrdgregea lpidtavrqg ardrlrpvls talvasigfl pmaiasgaga evqrplatvv
     1021 iggivtstll tlvllpslyr wilsra
//
LOCUS       WP_010545382             448 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Sphingomonas elodea].
ACCESSION   WP_010545382
VERSION     WP_010545382.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..448
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=48547
     Region          22..434
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mtfewpahgl tlqariesrt atigvigmgy vglplavafg eagcsvlgfd ldpekvvaln
       61 qgesyikhip gdriaplvae qritatadld rlgevdvlli cvptpltrhl epdlkyveht
      121 traiarslrk gqlvilestt ypgttrevmq pileeeglva grdfflaysp eredpgnptf
      181 sttkipkvvg addpasagla malyrhivpq aiqvssaata eavkitenvf ravnialvne
      241 lkliftamdi dvwevidaak skpfgfmpfy pgpglgghci pidpfyltwk areynqhtrf
      301 ielagqinad mpqhvirvla dtldarfgrg lrgarvlvlg vaykknvddi respslrlme
      361 mieargatad fhdphvaqin gtrehptlnf rhgiawdeat iagydavlia tdhdavdyaa
      421 laasaklvid trnacgkagv tganiara
//
LOCUS       WP_010545426             235 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Sphingomonas elodea].
ACCESSION   WP_010545426
VERSION     WP_010545426.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..235
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26183
     Region          4..217
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msefialtpk erealdaleq rqrhvrrgai lqrenepcge lfilrkglmm syvllddgsr
       61 qilrflfpgd mlgissaiyh eapetlcals dtvvcpfdra alsdimqahp rlsamilvys
      121 qiervaltdr laalgrtsak arvaallldl rnrlratdks idreytlglt qeeigdatgl
      181 tavhvnrmlr qleeegmiar eggrvtlldr aglagaanyv nryegldlrw lpppr
//
LOCUS       WP_010545527             482 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Sphingomonas elodea].
ACCESSION   WP_010545527
VERSION     WP_010545527.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12135424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..482
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52018
     Region          24..464
                     /region_name="MFS_2"
                     /note="MFS/sugar transport protein; pfam13347"
                     /db_xref="CDD:433134"
ORIGIN      
        1 magspaetpl vppprrvatp tmlaygfgaa aygvkdfcfi tflllfynqv vglpsaevgf
       61 vimcalllda fvdpaigmls drtrsrwgrr hpwmyaaaap ialgwlllwn ppawshagll
      121 gwlfctavlv rtavsafevp sqaltpelss gyeertrima yrylfgwggg mamlvlsyaw
      181 flaegpgrph gqfdragypa falggavlmv vailvsalgt hreirhlppv rverqplrrs
      241 laelfetlrn paflmlmgag lcyftaqgis fsmsnylyah vwrfdstafe llggtlflgv
      301 llafvlaprl arrlgkpgaa tlalvlavll ltapyllrlg gafpapgspw llpllfaift
      361 vnatfavsst mlgasmladv vehsevttgr rsegvffagf ffvqkcssgl gifltglils
      421 ltgfpdgaap gtvptlvvdr ftllfccvyl slagtaaffy rrfpfgkaeh aarlaqlgar
      481 ad
//
LOCUS       WP_010545682             490 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Sphingomonas elodea].
ACCESSION   WP_010545682
VERSION     WP_010545682.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..490
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=51392
     Region          23..469
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mriparafpl gvatllltaa aapgarttvt ggavrgsvaa dgaqvfrgip yaappldrlr
       61 wrapqpvrpw rgeraaiega paclqndygw nrgdathase dcltldvrtp gltgkrpvmv
      121 wihggsnrag sargtvesri tqqgvvlvai qyrlgifgfl ahrgaaaeak ghagnyglmd
      181 qiaalrwvra niaafggdpg nvtifgesag sqdvslllaa paarglfara ilqsgtpgfg
      241 mpfrplgqal algdqaerla gvrgiaglra asaatllatd rklhdpviar pdsvwnddmv
      301 wlrtqidgav lprspralll aaprrpvllg tsiaefgpae galdlsralr lgfgahadaa
      361 aalyrapddr rggpllalst dliftcpteq latllagrgw pvwryrfdla rdggrsshgs
      421 elpflfdgla iggqpallqq lwtrfattga qaaawprytp ayplgvtfds agmtpgplav
      481 pascrfrsal
//
LOCUS       WP_010545718             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: elongation factor Tu [Sphingomonas].
ACCESSION   WP_010545718
VERSION     WP_010545718.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     gene            1..397
                     /gene="tuf"
     Protein         1..397
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=42847
     Region          1..395
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makakfdrsk phlnigtigh vdhgktslta aitkilaenv agnaavdfan idkapeerer
       61 gitistahve yetnsrhyah vdcpghadyv knmitgaaqm dgailvvaat dgpmpqtkeh
      121 illarqvgvp tmvvflnkcd lvddeeilel vemeireels krefdgdnip iirgsataal
      181 ngtddklgkd ailalmaavd esipeperpl dkpfmmpied vfsisgrgtv vtgrvetgii
      241 kvgeeveivg ihdtrkttvt gvemfrklld qgqagdnvga llrgvardev ergqvlakpg
      301 sikphtefks evyvlskdeg grhtpffany rpqfyfrttd vtgtvelpeg temvmpgdni
      361 algvkliapi amdvgqrfti reggrtvgag vvasidk
//
LOCUS       WP_010545772             551 aa            linear   BCT 01-JAN-2025
DEFINITION  arylsulfatase [Sphingomonas elodea].
ACCESSION   WP_010545772
VERSION     WP_010545772.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..551
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59387
     Region          34..516
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(41..42,79,141,143,233,340..341,395)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(41..42,79,141,143,233,341,395)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 mrlrltalll lllpspavva qdkphpappp krpniliiva ddlgysdlga fggeihtpnl
       61 dalaehglrl tgfhaaptcs ptrsmllsgt dnhlaglgnm aelvapnqig kpgyqgylpd
      121 dvvtlaerlr dlgyatamsg kwhlgtrpqd dptrhgfdqa ftllqgganh fgidatatpl
      181 pgqatyreng vtlpnlpkdf yssdayaakl igflgktdpa kpffayltft aphwplqalp
      241 ediakyrgry dagfevlqae rlkrqqalgl vpagvkphpf vlpdgrdwah lsptekreqa
      301 rlmevyaamv drldqnvgkv iahlkatgqy dntiilflad ngaegidlat trlptmaarl
      361 kaadnrldnl gaassytayg pgwaqaattp sflykgftse ggtrvaafls ypgwkrqggi
      421 shaygtvmdv vptlveaagg hwrgssyggr tvqpvrgssw lpylrgqska vhgpkeivgt
      481 elfgrrairq gdwkiidlgd gwklynlaed pgetrdraad qparlktlva awdayakgag
      541 vvmqstpatf p
//
LOCUS       WP_010545829             461 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Sphingomonas elodea].
ACCESSION   WP_010545829
VERSION     WP_010545829.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..461
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50263
     Region          139..444
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mirqllafca lafavpaaaq gpltldqvlr ssaqnapqii ealakqrqae gkalsaegaf
       61 divfdvdaqt rpfgyydgsv veakasrald nnggglyagy rvsrgkfpvy edkaytnqlg
      121 efkvgavfsl lrdrvtderr tklrladqdv diarleremv aigvqrrams ayqawavagl
      181 rlkayrdlla lserrrsqla rqvqlgarpq ilitendqnl arrrsmvaqa eqklaeasna
      241 lsffwrdang vplvpvveql petlpelaia prkagpilrp dlktvlvrid qsltrlnlae
      301 ndlkprldar aelgkdlgai gpggpsrtpa eamvgvkfsv plerrsakgr iaearaeidg
      361 lrtrqrmlee qiaievkgia igiegadrva dlaaqeadla gkmavaeqrr fdmgasdffl
      421 inqreesatd arlraldary qalvaradla aatadravlg l
//
LOCUS       WP_010545872             399 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Sphingomonas
            elodea].
ACCESSION   WP_010545872
VERSION     WP_010545872.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..399
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42719
     Region          1..399
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(98..100,124,174,206,235,237..238,246)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(101,134,199,244..246,275,278)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            238
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mqtsaalqri qpsatlamts rvfelkrqgv dviglgagep dfdtpdfvke aaieairsgk
       61 tkytnvdgtp elkeaviqkf krdngldyta qqvtinvggk htlfnaivat veagdevivp
      121 apywvsypdv iqfaggtpvf iaagaeqqyk itpaqleaai tsrtkwviln spsnptgaay
      181 saaelkalge vierhphvwv faddmyehil ydgfefatia qvcpslyert ltvngcskay
      241 amtgwrigfa ggpaplikai aklqsqstsn pcsiaqaaav aaltgdqgfl kdraaafqtr
      301 rdlvvgmlnd iegmtcptpe gafyvypefs aligkttpkg kviatdedmi gyflddarva
      361 avhgaafgls pamrisyats eallreactr iqtacaelr
//
LOCUS       WP_010545875             426 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Sphingomonas elodea].
ACCESSION   WP_010545875
VERSION     WP_010545875.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..426
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=44680
     Region          7..426
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 marpntrrap erepdapgvp arraalklld avlrrglale qaldsaaqgl apndrglaha
       61 iaaealrrlp dldalidsat rqrlpddaka rfalrialvq aialgtpgha aistvlplvd
      121 ggprklvhgv fgtlmrghat lpdvpvlpdp valrwqaqwg davvqaacea iatpppldls
      181 lktdggtveg atglaprhar ldpgtsvpdl pgfaegdwwv qdlaasipar ligagtgtvl
      241 dlcaapggkt lqlaaagwqv tavdvaenrl arlrenlert glsarivtad llswspaapa
      301 davlldapcs atgifrrhpd vlhrvrpsli aemaelqakl ldraaawvkp ggtlvfatcs
      361 lepregeahl apflaahpef elvpatadel pagiapredg svrvlpgmla dqggldgffi
      421 arfrrr
//
LOCUS       WP_010545947             594 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Sphingomonas elodea].
ACCESSION   WP_010545947
VERSION     WP_010545947.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..594
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=65534
     Region          2..559
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mttqptsdfh vkanllatdd seyggnfsvt gpisetlgyv fsasysnwgg nvrnvidgrd
       61 vngretlstr aklkwkaspd vvftlsgnym ngnttvgrpf irmtpgavlr rqpgltadmt
      121 lpgitvdprn qkvanndrag tkywgwgtml rtdinigkmn vlgltsydkf rmddyidhdd
      181 taasgtygrn iqvgafksrl ftqeirllsp gtdafryalg vyyanvgfqr pflrgpvfst
      241 anwfatsgsr qiaafgqidw efvknltatv ggraqnervk ysfldknlav paswagrasd
      301 nattyrlglq yqatrdvmlf gsyatgykgq tydlttgfns nradagpirp erskdkefgv
      361 rtqffgrrmt fnvtyfdtdy tdlqaqsiet ladgtsnyrl tnvgglntkg lefetaarit
      421 hdlsvngsat yldatytsfp vaqcyplqta algcvagsps yqnltgtrai qspewkanat
      481 veyapaltek lngvlqgswq ytsslhyvar dpetfqkafs ifnvsvgvrd akrrweatlf
      541 vnnlfdkqyf qslvntsanf nvssaagsan aiatqgvlpr dfrryagirf gmny
//
LOCUS       WP_010546070             254 aa            linear   BCT 01-JAN-2025
DEFINITION  (Fe-S)-binding protein [Sphingomonas elodea].
ACCESSION   WP_010546070
VERSION     WP_010546070.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..254
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26284
     Region          <1..242
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 msqdppsrva lfvtclvdam rprvgfaalr aladagcdvv vppaqtccgq palnsgdrat
       61 atdfarrnva mlegfeaiiv psgscagtir chypelladd pawgpraeav aaktweilaw
      121 ldargwrpeg valpatatyh dscsglrelg ikaqprrllg avdgldlvpl ageetccgfg
      181 gtfcvkypai snaiadekaa aieasgagll lagdlgclmn magklhrrga evrafhtiev
      241 lagmadgpai geaq
//
LOCUS       WP_010546088             544 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Sphingomonas elodea].
ACCESSION   WP_010546088
VERSION     WP_010546088.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..544
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59003
     Region          6..544
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mtdtfetfdy iiagagsagc vladrlsadg qarvllieag gdnetelinm prafmkmfgn
       61 ptyfwhfpit eqegrpsget wsygrglggs sstngtwylr gepadydgwa amgfgewrws
      121 eiqrcfqame syrgagadas rgrdgplqit qlpfrspain aaieagtqig lkkvtdinap
      181 gsvrigytqa tvsrrgrras syqaflkpam rrpnlsvlld tlverveitn gratgvrvrt
      241 aggarsiaat revilsagal qspkllqlsg igpaevlera gvpvvqalpq vgrnladhlm
      301 ftmswrlhkd pganrefsgw rltshvlryy ltrtgmmayt spevtallsi dsspdwpdaq
      361 fgvgpyslrt teemkadpgr galedkpgis vngialrpks rgtvairsad vadpvdvhan
      421 wwgdpadkaf lvkmvrlarr ymrqpalkgf vgeervpger fqsdediarq lewlaspglh
      481 stgtcrmgtp etgvvdgrlr vhgiqglrva dcsvmplqpa gntngpamvi gwraaelile
      541 dhag
//
LOCUS       WP_010546145             204 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Sphingomonas elodea].
ACCESSION   WP_010546145
VERSION     WP_010546145.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..204
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22265
     Region          4..199
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mtrtiyivdd ddavraslhs llsvrpdliv rgyrsgdafl eqeeeldpgv vlldfhmpgs
       61 sgldvltkld rtpkfvaivl tgqgnvglav qamkagaldf iekpyeaefl lkvidqafsk
      121 leedseaaar tataeskiak lspretdvlk gliegrsnki iayeldispr tveiyranlm
      181 eklevrslse alriafaagl fpkg
//
LOCUS       WP_010546151             276 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Sphingomonas elodea].
ACCESSION   WP_010546151
VERSION     WP_010546151.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..276
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30411
     Region          30..130
                     /region_name="Methyltransf_24"
                     /note="Methyltransferase domain; pfam13578"
                     /db_xref="CDD:433324"
ORIGIN      
        1 msnllihsmt efwdiilgtl haagarnlae vgaefggtsq hlaayarvtg gtltsidpep
       61 kqefldwvgq tpevrhiplp sleampqlae vdawvidgdh nyytvlnelr iaarlaqrdg
      121 rpllaflhdv swptgrrdmy yapdrippeh rhahspdrgc tlgqsellpp ghgfrgegff
      181 sfalheggpr ngvltavedf ldegraagmq lafanvpavf glgilfdaaa pwaeavanvv
      241 fpwhnnplla sleqnrlrny laviewqdre rdrlsa
//
LOCUS       WP_010546196             308 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Sphingomonas elodea].
ACCESSION   WP_010546196
VERSION     WP_010546196.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..308
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33091
     Region          2..260
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mserirlglv gigkiardqh lpalagddrf dlvatasrna hvdgvpahtd iesliagghd
       61 ltavslctpp egrydqaria idaglnvmle kppaatltei adlakraqak gvtlfttwhs
      121 reaagvepaq awlkgkqita ariswredir rwhpgqewil aaggfgvfdp ginalsivtk
      181 ilpdallldq awmevpegra splraklhmr sggaavtadf dflqtgpqtw dievdtdagt
      241 lrlamggsil qlpgeeahka pdreyarlya rfaelvaage sdvdvrplql vadaflvger
      301 tigetfaf
//
LOCUS       WP_010546210             479 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein, partial [Sphingomonas elodea].
ACCESSION   WP_010546210
VERSION     WP_010546210.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..>479
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
     Region          49..479
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mrltikakla gafgfllllt atlgglgiln masinaqste iaknwmpsin lvnqintats
       61 dlriaqlthv atldqpgmqk vdddirkila dirdkrdrye klissdeers iynqfsgkyq
      121 tyldrsnvfl nlsrenknae anasiaqsrp lyddfssdln klvalnvkgg ndasaaadat
      181 ygsaraafvg llvaaivtga gaalwiarsv tqglsragta vgavaigdls qdvtvttnde
      241 ikdlvetvnt mvanlrvsaa ladriadgdl tvnhkpasdk dvlgnalvrm verlrgvvad
      301 attaasnvss gsqelsssse qvsqgateqa aaaeqasaam eemaanikqn adnatqteki
      361 arqsakdaet sgvavdravg amrtiaekig ivqeiarqtd llalnaavea aragehgrgf
      421 avvasevrkl aersqsaaae issvssetvk aaaeagdmlg rlvpdirrta elvseisaa
//
LOCUS       WP_010546235             244 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Sphingomonas elodea].
ACCESSION   WP_010546235
VERSION     WP_010546235.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..244
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26415
     Region          19..216
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mlnhpphvga apisrlgafa slsederral rlaseiphrl aasrdlfhag qrtggslivl
       61 dgwlgrvklf sdgrrqilsf llpgdviqep rtfqpvavst italcdtilc papaaedegl
      121 reayavsaal deanlmrqia rlgrmsayer ihdwlfemhe rlmlagragp dsfampltqe
      181 tladalglts vhvnrtlqsm rrdnvlewrg gvirlkhkga saratgqrga igtahvpagt
      241 aplr
//
LOCUS       WP_010546359             136 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF1636 domain-containing protein [Sphingomonas elodea].
ACCESSION   WP_010546359
VERSION     WP_010546359.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..136
                     /product="DUF1636 domain-containing protein"
                     /calculated_mol_wt=14377
     Region          11..129
                     /region_name="DUF1636"
                     /note="Protein of unknown function (DUF1636); pfam07845"
                     /db_xref="CDD:429694"
ORIGIN      
        1 mltpvpegpa ivvcntcrls aearedgegr rggallaaal tqqrdtdpry agiaiqempc
       61 lfactehctv hlrapgkvgy vlgrftpdte aadailayaa hyaesehgrv pfgqwpqgvk
      121 ghfivrvppa gqvveg
//
LOCUS       WP_010546370             157 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Sphingomonas elodea].
ACCESSION   WP_010546370
VERSION     WP_010546370.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..157
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16558
     Region          1..151
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mtrftvnnqp vqydmdpqtp llwalrdasn ltgtkygcgt gdcgactvdi dgaarlacre
       61 tigaiegtfv ttieglsadr shpvqqafla anlvqcgyci pgmvmaaail irtnrnpsee
      121 dvrqgipnic rcgiyprlva aiqdaariar gdpadag
//
LOCUS       WP_010549165             302 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [Brachybacterium].
ACCESSION   WP_010549165
VERSION     WP_010549165.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..302
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30769
     Region          14..297
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mriddasstl spararlgvi glgsmgepma ghllaahgtl avhsrtrkas lleagatwtd
       61 tprelaeqvd ailvmlpdlp qltpmlegpd sllaagtell lmigstsspr gvreladrlv
      121 getggrvrlv dvpvsggeag aragtlsima ggesadvera rtlldpcgtv rhlgplgage
      181 vakacnqmiv gatmmaisea tvlaersgia padlfevleg gyagstllad krdklvtgdy
      241 spggiaaymt kdlgfaadva edtgtspall galrgaydel vaaglgeedl svarrfvaer
      301 ga
//
LOCUS       WP_010549176             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Brachybacterium].
ACCESSION   WP_010549176
VERSION     WP_010549176.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19425591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..243
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26460
     Region          120..>195
                     /region_name="N-Acyltransferase superfamily: Various
                     enyzmes that characteristicly catalyze the transfer of an
                     acyl group to a substrate"
                     /note="NAT (N-Acyltransferase) is a large superfamily of
                     enzymes that mostly catalyze the transfer of an acyl group
                     to a substrate and are implicated in a variety of
                     functions, from bacterial antibiotic resistance to
                     circadian rhythms in mammals. Members...; cl17182"
                     /db_xref="CDD:473072"
     Region          159..243
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mpldeqphvg sadapsgaeh pvldnpawss ltgahrelai gnehvlrype dvspfvgvrd
       61 wehpdvwdai ldvfghdavv svshadpllp agwapefqip gvqlvqtdrl aprpepeave
      121 lgaadtdeml aliaqtrpgp fearthemgr yvgirrdgql iamagerlhp egwteisava
      181 vhpehrrqgl asrlvldvah yiqrrgdral lhasaantaa iagyeklgft lrrrltfgal
      241 rtp
//
LOCUS       WP_010549187             271 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010549187
VERSION     WP_010549187.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..271
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29247
     Region          30..268
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mnerttppda dvagqdptrp egaprtgepl isvrgvdklf gdfqalkgid ldihrgevva
       61 ligasgsgks tlcrclnrle titageitid gerlpeegre ltrlradvgm vfqsfnlfph
      121 lkavdnvtlg prkvrgvpka eadrqamell ervgladkan slptalsggq qqrvaiaral
      181 amkpkallfd eptsaldpev inevldvmae lakagmtmlv vthemgfarh vcdrvvymda
      241 geiveegepe qfftaprsdr akaflskila h
//
LOCUS       WP_010549198             181 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010549198
VERSION     WP_010549198.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..181
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19194
     Region          <59..134
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 msspetpqhl paapdllegp veragehefa htlhegagdl rirhhfagss qlpvalqtwt
       61 lapgayegmh ahaepaleem ylvlsgrari rqegethllg pgdalrapag iehdlacegd
      121 eplqvlvawg ptghfdmsgf gsyrkalaar daesasrdep stdtvsrgea pgddsadrir
      181 g
//
LOCUS       WP_010549236             164 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Brachybacterium paraconglomeratum].
ACCESSION   WP_010549236
VERSION     WP_010549236.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..164
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=17551
     Region          5..155
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkipyetavq rhgptvlrvc cavlgpgpda edawaetfla altswpdlae dtnleawlvr
       61 vahrkaidvt rrrarhavpt ddlpeqasrr anpgrddgvw tavaalperq rlavayhylg
      121 glphaetaal iggsaeavrr asadgiralr rsfaagddte gaar
//
LOCUS       WP_010549237             209 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Brachybacterium paraconglomeratum].
ACCESSION   WP_010549237
VERSION     WP_010549237.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..209
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22499
     Region          46..207
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtdtpslpeh lttserealf plpdpalagl rarlvqqadd aglvevayrt ldtplgplll
       61 aataqglvrv aferedfdav laalasrvsp rvleaprrld eaaaeleeyf tgtrrrfdlp
      121 ldralstgfr ekvqrvlpri dygstrsyke iaelvgspra vravgtacat nplpivvpch
      181 rvlrtdgalg gyvggldakt alltlerta
//
LOCUS       WP_010549245             489 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010549245
VERSION     WP_010549245.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..489
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50830
     Region          56..>284
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msspatgthp aagtdrargt dratgadrat gsvpaagsas ataaaapvgt staaapvria
       61 ligtrgfgrv hlenlerlre vgraeligvv dlheppaamq giwhrdlasl laahadappe
      121 vvviatpidt hlplalqale agahvylekp pvpaladhav leraaeaagr vvqigfqarg
      181 gagvdelrel vaagelgeid tvrvhgawsr drayyrrspw agrrrldgrr vadgvatnpl
      241 ahgvhaglvv agidrledia avttelrrah ddieaddtaf vridpvrgaa dadlgedtps
      301 hadptcedtg asrprpavvc altttapvqg apwievvgtg gaarlsyted llrrtapdgt
      361 vtetrhertd lvenllahvr dpevpllcpl aatapfsavl eaiqtapdpa piapahvtwl
      421 gegeaarpvv dgieealtaa letgapfsrs gatwahedai atwrpetatt tttgsradgr
      481 dahdeetrs
//
LOCUS       WP_010549332             189 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010549332
VERSION     WP_010549332.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..189
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21061
     Region          2..175
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrelvyyvav sldgyiagpd hqfdaflieg dhmegineef adtiptdiaa hlgidqsggr
       61 fdtvlmgant havglpdmps pyrhlqqivf thrplepaen lrvtdedpva vvrelkqqdg
      121 gdiwlcgggr latqlhgeid rlllkrqpfl fgdgiplfap geyapeqfeh vrtrtyetgv
      181 sftefarrr
//
LOCUS       WP_010549338             286 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010549338
VERSION     WP_010549338.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..286
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=29125
     Region          124..227
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mstppavaqp vlapapslrr vlaflgaala vstalslpfa tgalppeavg lavplaqlsp
       61 llaallvrrr gapwwralal avpswralgv aaiaaiaafv avplarvlig lgagappsad
      121 alplssvlla vptvlvmqsl faigeeagwr gwlhgelrpl gfwpmsllig amwavwhapi
      181 vlalglapre aitylgtiva vapllsalre vsgtawaavl ghgllnsarv aieqnvlgpl
      241 epgtawlldl sswalwlaaa avvlhlggrr rattpgavsg aglpvr
//
LOCUS       WP_010549345             454 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 125 protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010549345
VERSION     WP_010549345.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..454
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50244
     Region          32..438
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 marlpdtlld avqarvlegl adlgasdalv geiaqrvvay lrntsettvs veedgttfvi
       61 tgdipamwlr dsaaqltpll rlvvagvgad edraelvall agllrrhwqy leidpyanaf
      121 nrapdsshwd adeterdnpw awerkfelds lsygpdlawr lwratgdtsw aderflpasr
      181 ailstvraeq hheersayff rrsgvpvqdt laregrgslt tpnglvwagf rpsddacelg
      241 ynipgnhfla lalerlaell eqvadapaea deareraeqi raalvehgti egptgervwa
      301 yeidgrgdhr flddanvpsl lalpylgcva qddplylatr aavlsrsnpc yyeglylegv
      361 gsphtpkdhv wpialavegl tsaergeklr llelmirtdg gtrmmhegvh vddptvftre
      421 wfswsnsmfc elaldlagve rdragthega ters
//
LOCUS       WP_010549349             344 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010549349
VERSION     WP_010549349.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..344
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35812
     Region          33..253
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtqstppggp ppplppldha spqrapgpeg pgivaeqvsr afgsvqavad lsftaprgav
       61 talvgpngcg kstlmlmlas llapdsgrvl vggvdpaeds savraqvgwm pdqfgawdsl
      121 rvaevlevmg rayflptaql rgrvdellel ldlvplaqqp ahvlsrgqkq rlglaralvh
      181 dpqvlvldep asgldpasrr rllqvvrsra adgatvlvss hilgeleema dhvvfmdggr
      241 avdasslrdl aarprpwris slhhqalvea ldqlqvrhgg vlagdcttsg haeavvelpd
      301 dataarllad ltaagariig fgpttgrlea aylasdaaqr egal
//
LOCUS       WP_010549366             215 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010549366
VERSION     WP_010549366.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22944
     Region          37..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdnddpgtad dpgtadepgt addpgtadep aaqpapqrdk ertraailda aasmivehgs
       61 gvslagiarr agvskgalth hfphrlelek alvrrsneqf wadvhalvdl senrpgkllr
      121 ayvraltapd sraaeifsps slltvlgdrp gmeelvdeda arwrealsad gfdpaqalvv
      181 rlaseglamn mgtpyateqe relaharlle laepr
//
LOCUS       WP_010549406             479 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010549406
VERSION     WP_010549406.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..479
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=51320
     Region          21..411
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mslpfltrrp tvpakdgasw phvvivgggf aganavlglr darvrvtlid rnvyktfqpl
       61 lyqvatagln pgdvtmflrg lslkvpnmry rqgevvgvdp erkvvtlneg qrgdqelsyd
      121 ylvlangatt tyfgtpgaee hampmytraq slairdrvfs elerssreag vthdklhvci
      181 vgggptgvei agaladfrmq eldilypemd pgtlqltvlq rgdellkefs dkyrqyaade
      241 lrdrgvvlrl ghgvkevgyd hvilddgsil esditiwaag vaipeavsrw glpqdsrgri
      301 avddhlqvkg mpgvyaagdv aaqdealpql aqpaiqtgsa vaksiaadvk gkqrptftyt
      361 nlgtmatigr haaiaeipvl gglsgslgwa awlgvhitkm lghrnqrava mnlvslyggt
      421 rgthqpnpvv gevdslraar ifeeqaphrl fglnagaren raaaedapga advaapsqd
//
LOCUS       WP_010549408             457 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Brachybacterium paraconglomeratum].
ACCESSION   WP_010549408
VERSION     WP_010549408.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..457
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45168
     Region          1..448
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mssgaspavl srrlglrdav viglasmiga gafvslgaaq dlagslapaa vlvaavvalc
       61 natstaqlaa qhpaaggtyh ygrerlgpww gflagwcfvi gktascaama lvvaaylvpe
      121 pfqrpvaall vvvltavnlv gitrtavlar vlvtvalaal vltgvrllag ivaggptgga
      181 gdgagagtwe vpgplsgqaa glwdggiaav agageggalg ivlavaqaaa lmffafagya
      241 rvatlgeevv aprhtiprai llalaavgal ylvlsvilvl vgpapgaqgw gpapfraald
      301 avgaggvwav vvtigavaaa sgallalvag isrtvlamar erdlppvlah vsprfsvpqr
      361 aeavagiavv llvllasdvl vaiaassfgv llyyavanla altqtgqwrl fpkamqwlgl
      421 vgcvllvaal pgrtivaglv lvavglayrg lvlavrr
//
LOCUS       WP_010549514             470 aa            linear   BCT 01-JAN-2025
DEFINITION  beta-N-acetylhexosaminidase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010549514
VERSION     WP_010549514.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..470
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52071
     Region          2..469
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mpdpialvpl prsvvwsegm wettdpwegl svglsedlpa teyalsispq gaalsagsea
       61 aladgrntfa qivtgadgsi pcvtiadspk hawrgmhldv srhflpveei etlldgmalh
      121 rlnvlhlhlt ddqgwrveik gyprltevga wreqtlvghm sgdeeswtfd gvrhggsysq
      181 eelkglveya rrrgimivpe idlpghmqaa vaaypelgnf peqqvgvrev wgisdhvlgv
      241 sdqvfdflrd vltqvagifp apyvhiggde cptgewerss qararmnewg ltrvseiqgr
      301 fttfasevla eqgkraiawd evlethlpdd tvimnwrgpa gvgeatsrgf qtivatsdll
      361 yfdhyqadpa deplaiggrt tledvytgrl lpkktsadqe rlvmglqaql wteylpdaga
      421 vqymafprlc afaerawgsp eqswdefqer lrahlprlda fgiryrpldd
//
LOCUS       WP_010549548             246 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010549548
VERSION     WP_010549548.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..246
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=27006
     Region          3..202
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mnivdwavst mdalgplgvf lliflenifp pipsevilpl agvtsagpnq sfwlmllasi
       61 agsvvgawll ygigrllgpe rlrvifirlp lvhvedydkt vafmdehgyk aiffgrfvpg
      121 irslisipag lyampigmft lltaigsgiw ntlfitigyf mgsnwtviep ytdifsnvay
      181 avillvvlwf avklvlrekk rrelglpdpd aeeiteleqe kaeekaepgq gatgsadsse
      241 eraeer
//
LOCUS       WP_010549525             128 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010549525
VERSION     WP_010549525.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..128
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14057
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mprgkvkfyd aekgfgfild dedgqsvyvh attlpegvtt lrpgtrvefd mvdgrrgpqv
       61 lslqllepap svararrqkp edlavmvedl irllddagtg lrhgrypdrg hsqkiatvlr
      121 avadnfea
//
LOCUS       WP_010549566             108 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Brachybacterium].
ACCESSION   WP_010549566
VERSION     WP_010549566.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..108
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11635
     Region          1..99
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mdmqtvapqd vpegahlidv reqaewdagh aptaqhlpas tllqnleqlp etdedlyivc
       61 rsggrsfqva qwlnangfda invgggmdqw fesglpiesd gegeafil
//
LOCUS       WP_010549571             299 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010549571
VERSION     WP_010549571.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..299
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31358
     Region          5..297
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mtawlrglsa fpltplrdgg vdqaalegiv dllaeaavds igvlgstgay tyltreqrrr
       61 vveiaarrsg dlpvlagigh catdevlala edaqhagada vllapvtyqg ltddevvgly
      121 edvarelsvp lvvydnpstt hmhlsleaya ritalpqvaa vkippvpadp aearervaav
      181 ravvpervri gvsgdavgat gllagcdlwf salagalpgp llaisraara graqealehs
      241 arlqglwdlf aecggslrvv aevsrqlglv repvlprplr plahaqqerv aqvlaaler
//
LOCUS       WP_010549631             466 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010549631
VERSION     WP_010549631.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..466
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=51414
     Region          9..397
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mvekgrrera alylrqstfr eesislelqe tagreyaarh gyevvdvqsd pglsgrtfnr
       61 pgvaavmdav esgaadvvil wkwsrlsrnr ldwylaadra qqaggriesa tepidtstsi
      121 grlargmmie iaafeserag dqwketqarr vrnglphdgk prfgyvydpe qkmffpdpvt
      181 gpvfaglyrr fiagetmysl cvwlnaqgip tatgsnvwta gnlrqimdrq favgrvyhqg
      241 vwhpgahepl iteaeyaayk qarktraaap rreasdylla glvrcgvcgr altgaaargr
      301 wfyyrcfasr ftgghshaqv ptrlvedavy dklvetaadi ettaipetrp vavdsaalkr
      361 tiqqhktslg rlavqlaedv isadayaaaa paieqklaaa rdalqaatae haipamhdav
      421 vslvkdwhil ptthrralla ravesvevdf nderrvdvvm rgrptp
//
LOCUS       WP_010549817             305 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010549817
VERSION     WP_010549817.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..305
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=31858
     Region          46..304
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mrlgatlavl llvivlgwga gltlwansri ehvdalseae ntpgttylia gsdkrdgeav
       61 nadgtegart dtimllhkar ggksylislp rdtlvdipgh ggyklnaays fggapllvet
      121 veeftgltid hyveigfdgv sqvvdavghv nlcidqdvdd eksglkmteg chdvggeqal
      181 afvraryfdp tadigrqarq qqfvsalidr atspavllnp itqvrlagag sgalttsdgt
      241 givdvgrmal aarsamgsgs lsipiedpey qtnnsgiail tdeedikaff dsvadgtaep
      301 epaeg
//
LOCUS       WP_010549713              71 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [Brachybacterium].
ACCESSION   WP_010549713
VERSION     WP_010549713.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 71)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..71
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7124
     Region          4..>52
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 msattidfqv tgmtcghcem svreevgevp gvtgvevshe tgllrvgsda avdeaavlaa
       61 veeagysavr a
//
LOCUS       WP_010549831             278 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Brachybacterium paraconglomeratum].
ACCESSION   WP_010549831
VERSION     WP_010549831.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 278)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..278
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30498
     Region          9..275
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mgvrpplgry ikqvwerrsf iwnlsssray srnqgsylgq awailrpvld aavyviifgf
       61 lfhssapgid nraafitigt ftyslfqtsv msglnsvpsn lqlirshkfp ravvplatvm
      121 tetvlfapil vammavvlvt gvlpgmgavv ptwswlllpf aavllavfsa gvamffarlg
      181 arapdianam pfiltlgrya sgamflisam vpdelwlkpl llhqpvaiyl elfraafgne
      241 plipmttglw leatawavgv faigflyfwr aeetygrd
//
LOCUS       WP_010549832             287 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Brachybacterium].
ACCESSION   WP_010549832
VERSION     WP_010549832.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..287
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30616
     Region          26..277
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mtedidfeid penlpdrvdr dkplgapsvv vddlhityrv fgarrsgttk qraslwdkmv
       61 slgrpdtgpi tevpavrgvs fvahhgesig ilgtngsgks tllravagll ppssgrvfts
      121 aepellgvna amlprltger nimigglalg lstkevkeni pgvadfaelg dflylpmtsy
      181 ssgmasrlrf aistirtpei lmidealatg dasfrkksta rieeirgqag tvffvshsla
      241 svramctral widkgvlvad gdvdevadly hayvegrtda ssgaklk
//
LOCUS       WP_010549892             125 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010549892
VERSION     WP_010549892.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10547098
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..125
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13833
     Region          6..121
                     /region_name="bPH_1"
                     /note="Bacterial PH domain; pfam08000"
                     /db_xref="CDD:462337"
ORIGIN      
        1 mdesvsaits wtfveecpip qdvtallvpe eraiaayktf rdsavfttkr livrdaqgir
       61 gkkveiyslp ysainmwsse nagtldlnae ielwtragri kiavgkhidv rrldlliana
      121 vlrss
//
LOCUS       WP_010549903             214 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010549903
VERSION     WP_010549903.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..214
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23813
     Region          12..208
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mtqsvrvqnf gvsrdgigag edqtleqpfg hvdpmallgw gfatasfpsh epgvgtrgfe
       61 drltrdfdhg igveimgrhk fghqrgpwtd dgwigwwgee ppfhtpvvvl thyereplvv
      121 gettfhfvna spaealarak elaggldvri gggvttvref ldadlidelh vsiapveygh
      181 glrlwerpee ledrfhlekv mapsgvehcf lwrr
//
LOCUS       WP_010549923             213 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010549923
VERSION     WP_010549923.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22995
     Region          25..177
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstreprpgr rrpgrprgqd ssvvreaalr aaidliaehg yaatsmaqva eaagispsgl
       61 ahhfpskval lgavldhrda idnvpvseda gtwavfdglv elarinagrr qlvalytivi
      121 geavspdhpa hdwmlrhfev slalledavr egqrtgeiaa daparhiart tislmdglqv
      181 qwlldpsvdm paelgryvee lrrrwgtgpa els
//
LOCUS       WP_010549905              69 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CsbD family protein [Brachybacterium].
ACCESSION   WP_010549905
VERSION     WP_010549905.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..69
                     /product="CsbD family protein"
                     /calculated_mol_wt=7208
     Region          2..65
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mstdekfens kdklggqake glgkltgdke teaegqaqqg kadakdklqd ardtvkgavd
       61 glrgkdtqd
//
LOCUS       WP_010549960             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Brachybacterium].
ACCESSION   WP_010549960
VERSION     WP_010549960.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..243
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26096
     Region          8..112
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
     Region          130..236
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mflenlgida ldpqrlgrfw etalgtttlt dapdifetrl sidgdayldl cfarvparnv
       61 apqrlhldlr ggaereaiaq rlrelgasdl digqgevpwi vladpeggaf cvmeeraayv
      121 gtgpiaalpl dsadpardae fwawlsgwtp apgvaprtlr hpsgrgplle lcpepapkrl
      181 gaknpihldv rlepeddpda vaagiaargg eeffanwgel pwrvfrdpsg nefcmlpavg
      241 aga
//
LOCUS       WP_010549986             406 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endonuclease/exonuclease/phosphatase family protein
            [Brachybacterium].
ACCESSION   WP_010549986
VERSION     WP_010549986.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10505910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..406
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44075
     Region          45..291
                     /region_name="Exo_endo_phos"
                     /note="Endonuclease/Exonuclease/phosphatase family;
                     pfam03372"
                     /db_xref="CDD:460902"
ORIGIN      
        1 mtprlsrrra lvaaaaaglg lpaaatataa eparrggpfq slraatfnas lnrgregqll
       61 edlatgkdaq iravaeviqi nspdilllne fdhddegrga dlfrekylev pqngqspafy
      121 pyaftapvnt gvpsgldlnr dgavegpdda wgfgqfpgqy gmvvlsrypi ltdqvrtfqn
      181 lrwadmpqnl lptefygpei spqlrlssks hwdvpvqigt dvlhvlaahp tppsfdgpek
      241 rnqrrnhdei rlwvdylqpg rrsqwivdda gvrggldpsa pfvilgdlns dpvdgdswpg
      301 aieqllrhpr vqdpkptsdg aveaaetqgg anaghggear ydtadfaept pgnlrvdyvl
      361 parelqivss avywprqgep gseltgshpf ptsdhrlvrv dlqvka
//
LOCUS       WP_010549995             165 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Brachybacterium].
ACCESSION   WP_010549995
VERSION     WP_010549995.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483007
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..165
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17048
     Region          18..164
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; pfam01613"
                     /db_xref="CDD:460266"
ORIGIN      
        1 mahpgvdqde yrrlsdllav glavvstrqg phdllvtvds yldisydppt mglalyglsr
       61 aaeaveeagh cclsllaedq qaladrfgtp gaplqgmlag ieagrtadgd ailpgalahf
      121 alrieqgvda athrlligpv vgmgqggaea gpairfagek relrp
//
LOCUS       WP_010550029             325 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550029
VERSION     WP_010550029.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..325
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33162
     Region          1..308
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(37..38,110,114,117,135,138..140,159..160,164,179,
                     200..201,222..223,225,247..249,297,302)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mraitivgeg elelaelpep tpgpgevlvd vvaagvnrad laqaagkypp ppgaselpgl
       61 evsgrrrdtg eevvallagg gyaevvavpe aqllpapegm glidaagvve aaatvvsnlv
      121 leagmreget vlvhggtggi gtvaiqlaka mdarvlttvg sddalpivaq lgaeqawnrr
      181 iidlpaavre aggadvildv vggsaladnv amlneggrlv iigtlggasg elpigqlmak
      241 rarvigstlr srpvdnkaai leatrylvwp llasgelqip iherlplaea araheilrtg
      301 ghlgkvilev appsgenrrg rrrka
//
LOCUS       WP_010550025             288 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550025
VERSION     WP_010550025.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..288
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30226
     Region          30..284
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 msasttttdr iaarerlaeh ldrldgkall igldvdgtlv dhdgrmtpem rdalrgaast
       61 htvviatgrs lgatlpivea agitrgyavc sngavtvemd peaegghhiv dtrsfqpgha
      121 lrtlrevapd ahyavetadg gfhsttgfqd asfgveatet alddlmelea vrvvvhvpdl
      181 spqefskvia esgvhgveys igwtawldma apgiskasal evirdrlgie rratvavgdg
      241 fndtemlawa evgvamgqap qgvkdvadvv tdsiyedgtv lvlegvlg
//
LOCUS       WP_010550039             103 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550039
VERSION     WP_010550039.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..103
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10955
     Region          3..90
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mtvvvtavfq pkpgkqkela eamrrgieav htekgcelya ihdaedgtvt miekwttaed
       61 ldvhgdsdqv kilradiadl iegpatvtrm apipagtesq gal
//
LOCUS       WP_010550042              67 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Brachybacterium].
ACCESSION   WP_010550042
VERSION     WP_010550042.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..67
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7184
     Region          1..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 matgivnwfn sdkgygfiap edgsadvfah fsaivgtgrr dleenqrvef dveqgpkglq
       61 atniral
//
LOCUS       WP_010550060             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Brachybacterium].
ACCESSION   WP_010550060
VERSION     WP_010550060.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..161
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17915
     Region          62..146
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 maeiirahde dwslvreirl rslstdpsaf gqswekesty edsvweqrvs daawflaveg
       61 dqpvavvavr qeddspaner elqamwvtpg srhsgiagrl aeavfeware dgadtvtlyv
      121 gpentgaral yeslgfsdsg erwqiveddp dgawlkmtrg l
//
LOCUS       WP_010550114             332 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Brachybacterium].
ACCESSION   WP_010550114
VERSION     WP_010550114.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..332
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35449
     Region          18..300
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 msstetssrp vrqkvdltkf awlsiaaaiv titlkagawv mtgsvgllsd aaesvvnlva
       61 avvalialrv afrpaterfl ygrakaeyfs aavegvmifa aagvilvtav erflnprple
      121 nvgwglaisv iaslvnggva lvllragrkh dsitlradgk hlmtdvvtsa gvlvgvalvv
      181 ltgwerldal vafavgvnii vtgiglites vsglldkalp deehevitei lrrrtdgtvt
      241 fhglqtreag qekymnvhvl vpddwtvkrg hdyieglehe lmgvmptlhv lthlepisdp
      301 asyedipeah vpihgedeaa lrpprddada qg
//
LOCUS       WP_010550139             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010550139
VERSION     WP_010550139.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..233
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25310
     Region          3..93
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(51,54,58..59,68,79,83,89,93)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mvwstrelae lagtslravr hyhdegllpe pprssngykh ygvrhliqlm hirrlvdlgv
       61 plaeipslgp stdgyrevle alasettaei drlvkvrgei aqlleepgtw emssgttgst
      121 dgdfltvlsr vldedslqaw rrvgesipda qvladfenlp eeasaemred vaarmadavr
      181 dglaaapeld dpgfgegtsr algtrsigea laelyspaql rvlvrchell sae
//
LOCUS       WP_010550176             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Brachybacterium].
ACCESSION   WP_010550176
VERSION     WP_010550176.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26703
     Region          1..253
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 myarerqrri lellegrgrv tvtalsaefa vttetvrrdl dqlagerrlv rvhggavpps
       61 ttevepdlda rritnveakr riarvaarll pedpraavml dagstvgelv ahlsgrrgpv
      121 ithapaiaqg alahtdlevh vlpgrvrptt qaavgaatve avralhpglv vlgcngldgt
      181 gfttpdpdea avkaamvrga arrvmladss kagarhlvtf atteeidtlv tdedlpaela
      241 aeledagiev lra
//
LOCUS       WP_010550180            1079 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550180
VERSION     WP_010550180.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..1079
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=117337
     Region          181..951
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 miltpdqapv gsprpgrpgg ephpatavry saeageraeq alpaeagaag ivgrtiapge
       61 vlrwfvhpvl deelswgath valdlvlddg srlsqheprd qhgslatarg lgkarilyad
      121 qwndvqvgle alvgrrieev lvevdvpedh eadlledles epaeaappap lhgwidgpsl
      181 avppadpple dpvawvdtrr gtrsafefsr gntlpitalp ngfakftpat dartrrwiyq
      241 hhrthlqgls lthqpspwmg drhqlvmmpl lgespdaspa arerafthed etarpdlyav
      301 aleggigmrl aptdhgavce islpedsgpg hilfegvdah srldaagavf dgrvqgwids
      361 spqegydrad gatrmfvlae vqpapvrvgr aegdsggsvl sfapgtrtvt vrlvtsllgq
      421 dqaqrtfale lagrtleqvr eeahalwtrr lqvleapdat apqrrtlygn lyrlnlypss
      481 hwenrgtaev vepvhaspvl pvrgaatdtr tnaetvpgrm yvdhgfwdty rtawpayall
      541 ypelaaelad gfvqqhregg wiarwsspgy adcmtgtssd iafadlqvkg vplpdpqaty
      601 eaalrnatva ppqpevgrkg getavfrgyv aadaeagesv swsleahind agiaaqaall
      661 aeraeaegdr lraerlrges aylaarsany allfdrttef frgrradgaf avpaaefdpl
      721 ewggdftetn gwtfafhaph dpeglaalhg grdmlrgrle qyldtperad rrgtydttih
      781 emvearavrm gqfgfsnqpa hhipflfhhv gapeeasriv revqrrlfvg eqigqgypgd
      841 edngemsaww lltalglypl qlgtgryhlv aplfetvrvr plgregftlt ahgaggapag
      901 aedvcitgmr vrgaehadsw idhadlrgei eielgaepgd wgtvppspta pgqrpqplwd
      961 lfaadpsqpl idddartelv leaasavldl pelgepmqar fltltssaet ggdpiawrle
     1021 gsddgeswev ldarsaqrfe wrrqtrpfei aspqpclhhr lvvttsegpl rlaelella
//
LOCUS       WP_010550199             106 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [Brachybacterium].
ACCESSION   WP_010550199
VERSION     WP_010550199.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..106
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11937
     Region          2..91
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 milinvkfpv kpefadrwpe iaseftestl aepgnlwfew srsvkepsty vlieaftdeg
       61 agphvdsphf kkmqeefpqy ltatpqiish qidsdgwgpm geitvd
//
LOCUS       WP_010550192             390 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550192
VERSION     WP_010550192.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42764
     Region          4..364
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mseknvrlgi igfgaqggmy aglladgkia gmtlgaiadt dpakkdaaae khagtpfydd
       61 yvamldsgdv davvttvphy lhpemtitai gkgihtltek pagvytkqve emnafaaehp
      121 ettfaimfnq rtnpvytdlk aliesgelga lrhtswiits wwrpqgyydq sewratwgge
      181 gggvlvnqap hqldlwqwla gapkkvfakl afgfqrdiat edevnalvdf gegvtghfmt
      241 stndiigtdr lellfdkgkv vvdksnkvtv yrlsedersl sdkmtmqdva klfrgemdps
      301 slytveekty esawgqqhid vltnfaahvn dgtpliadga egingvrlas gmqlsawtgr
      361 eidlvdypae eylselnkri eeegkfptrs
//
LOCUS       WP_010550398              79 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [Brachybacterium].
ACCESSION   WP_010550398
VERSION     WP_010550398.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 79)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..79
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=8131
     Region          8..75
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mtatagsttr svfraegfsc pscvakiekr vgrlpgvrdv tvkfasarve vdhdpsvtst
       61 deiiaaigaa gyratlsaf
//
LOCUS       WP_010550405             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dienelactone hydrolase family protein
            [Brachybacterium].
ACCESSION   WP_010550405
VERSION     WP_010550405.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..249
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26195
     Region          1..242
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 msattlqipt daddlpgllw lpedldqpvp glvvlqeifg lstymqqrca dlaargyavl
       61 apqlfarldp pvvgiedged fqvwleegma ltsrvpwera eadaiaaiga lrahgavdse
      121 rvglvgfcyg gglafsaaas aaeedrpvsa lvsyygsalp tlldraaavd vpslhhfgta
      181 dafipleqve qirgavtagg treqvrfvlh qgaghafdnp hpglhhagaa eaawqqtlgf
      241 laealpprs
//
LOCUS       WP_010550408             320 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycine betaine ABC transporter substrate-binding
            protein [Brachybacterium].
ACCESSION   WP_010550408
VERSION     WP_010550408.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..320
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33758
     Region          60..313
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(69,71,117,145,175,179..180,227)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mstrrlplsp rgarrpaasp ltrrsaligg aglmglglaa cggggesggg sdgggsggdt
       61 itlgyipswt dglslaylld nrltamgytv eheqiteagv lyaglaqgdv dmfpsawpev
      121 thasymeeyg ddiedlvayy egavlnlsvp qyvditside lagqadrfgg rivgiepgag
      181 ltkatqesvi pgyglddyel vtssttamit elenaidaee divvtlwtpf wampaydmka
      241 ledpegafge pealhhlgrt gfkedfpdaa ewiagaklsd eqfgsledkv vnefgegkea
      301 eaveawleen pdvlppvege
//
LOCUS       WP_010550417             153 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550417
VERSION     WP_010550417.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..153
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16662
     Region          6..152
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 msatfqvtfd ardpgrlsmf wkevlgyvhp gppgfdpttg rdalaawdef ldglgvpase
       61 rndvsaledp egagprlffq rvpeekvakn rvhldvraap glegetrmaa leaecerlvp
      121 lgatrvrrhe peppmsggfi vmtdpegnef cld
//
LOCUS       WP_010550424             327 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550424
VERSION     WP_010550424.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..327
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35364
     Region          1..265
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrfallgtgr isgwfartch dsgiaepaiv ysrsqergee farshdiaaw sddldailad
       61 peidavyvas pipahaaqvr qalaagkhvl cekslavdla eaeelveaak kadrvlleav
      121 rhihdsamet irthlpelgr iwsasiemiq yssrydafrs gtvlnafnpe lgisaladvg
      181 iyplhaavql fgaprrtaam tlslpndfqa satvlldcts tvvtcryskv trgvtpsvie
      241 gedatmtidk iaepseiglh yrdgrtrtlm svparrpgdt mtgelevfaq lveahdvdhr
      301 fhaqtlavqa ivdeitaqag esappvr
//
LOCUS       WP_010550429             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: arsenate reductase ArsC [Brachybacterium].
ACCESSION   WP_010550429
VERSION     WP_010550429.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..143
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=15298
     Region          7..129
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(11,13..18,104,106)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mtarlsvlfv cvhnagrsqm aagwlrelag drievrsags apadsinpaa veamaevgie
       61 ishqkpkilt pesvqasdvv itmgcgdacp yypgkryedw kledpagkgv aevravrdei
      121 rtrieeligs llsrepldip vqg
//
LOCUS       WP_010550469             127 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Brachybacterium].
ACCESSION   WP_010550469
VERSION     WP_010550469.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..127
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=13942
     Region          26..127
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mavvvgfipt evgfkalaaa reeaeqrggp lvvvnvlrag veedprhade qqleiardel
       61 rrttvrvafr qetteddiad vllqvveeer aellvlgvrr qndlarhllg ltvqklllss
      121 psdvlvv
//
LOCUS       WP_010550467             540 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550467
VERSION     WP_010550467.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..540
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=57493
     Region          5..>153
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
     Region          <401..513
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 mpkilniavv gagtmaqavh lpvlrrrwdr fsvaalvdhs prrrreasev wgieeerrye
       61 tvadlvaavr artlsldgvl lstdglhvdd llaivrrgip vmvepplgys eeeiakvaef
      121 eriagrrlvm lahpqqydds varmsehiat kdlrmvdhev lmpasqplfg qahvttssyd
      181 lpteqrtarr kalqaaveag tgdgatqrdr dlyvkglltg vahqmavteg aygpieklva
      241 vrhwpkgvip gsiellgelg sgaqvrlvwh ylpfapeyse tlrvlsarrr mrldlpapsh
      301 gdarstvslr ekksgvvqev attapkgsae lmweafhafv ekgeaplaga aealrqvvll
      361 revlativea dgrsleaepe qdsgteeapg aeegaeaeep saqpeepsae satanavrad
      421 eepadgasap satvevelpg aepapetleq pvtdpsgeqp aaahalaepa aepssdptpg
      481 rapeatpvae paretleqpa apsteevvda wsggaesapa aaedappatv dpavpedprr
//
LOCUS       WP_010550474             311 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010550474
VERSION     WP_010550474.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..311
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32613
     Region          11..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtsttatapt levralskry garaavdals fscspgtvtg flgpngagks ttlriltgla
       61 eadegmalig grryralehp artvgvmlda ralhggrtgi etlrltartl gmprdraeev
      121 letvgleqaa tkrvggysyg mrqrlgigva lmgdpsvlvl depangldpe girwmrrllr
      181 sfadaggtvl lsshqlreve atvdrlvvis egrlvregpl eeltavtgtr vaaldqaalr
      241 raldahgiaf elraggelsv slapedmgrl alreqlvlts lgagagtgle evffaltghe
      301 epsadepapa l
//
LOCUS       WP_010550556             567 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550556
VERSION     WP_010550556.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..567
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60741
     Region          21..556
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mpshtpsaap aaadpalhlr adgisftypg laadrrvltd vslvvpagrp tgllgengsg
       61 kstllrvlag glhpdagtce vpgpvgmlrq elpfgartpl aevvadaler srrlerelit
      121 ageelaggta aaaarydrvl aeatladvwn aprrgeetla glgladlsgd tplgeisggq
      181 rerlalahll iarptswlld eptnhlddea aafvagaiaa hpgpvliash draflddats
      241 aqldldpaes plgeepgglt aytgtfsdyl laryeardrw ehryrteqee ltrlrevard
      301 ahtlgresrs raevkiarkf fadrnavrvs rhvrdaeqrl aqleqdqvrk ppaelelthl
      361 pdaprgagqv qlaladvave grlapvslal sagehllvtg angsgkstll dvvagrlapt
      421 sgtvsrprsl righlrqdde pvpdrtvgah lrraagleed eqpelfglvh prdlarplet
      481 lsrgqlrrvm laavlldppe llildeptnh lalvtatrle aaladwggtv liashdrwlr
      541 rrwdgellel gdtdvhsprp agarrtg
//
LOCUS       WP_010550603             132 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Brachybacterium].
ACCESSION   WP_010550603
VERSION     WP_010550603.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..132
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=13686
     Region          1..126
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mtivvgyaps tqgraalrag iryaertgsp llvaahqhav pgsggaaate eevraeleeq
       61 gadlegvtir rgpdreigef llatiedvqa elvviglrrk spigklnlga sarrvvlgap
      121 cpvltvkdqd pa
//
LOCUS       WP_010550292             132 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MmcQ/YjbR family DNA-binding protein
            [Brachybacterium].
ACCESSION   WP_010550292
VERSION     WP_010550292.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Singarapu,K.K., Liu,G., Xiao,R., Bertonati,C., Honig,B.,
            Montelione,G.T. and Szyperski,T.
  TITLE     NMR structure of protein yjbR from Escherichia coli reveals
            'double-wing' DNA binding motif
  JOURNAL   Proteins 67 (2), 501-504 (2007)
   PUBMED   17266124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10515191
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..132
                     /product="MmcQ/YjbR family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14666
     Region          14..132
                     /region_name="COG3801"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443014"
ORIGIN      
        1 mahpqmfddd dpwlervrei alalpgakek ishgrpafht vkvhcyyggs lkvdgewvph
       61 eqsvmlhlpp reraalaeep rsyvpaylgp sgwlgidlde atdlvelael ieesyrtvap
      121 arliaelear eg
//
LOCUS       WP_010550700             115 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator
            [Brachybacterium].
ACCESSION   WP_010550700
VERSION     WP_010550700.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..115
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12957
     Region          10..104
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 msdavdthlq elrrgtvvla clqllrepgy gyallerlds hglptdantl ypllrrlekq
       61 gfltsewnte esrprkfyst sadgirlaet lqqewralte slssltepdp ahees
//
LOCUS       WP_010550736             611 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010550736
VERSION     WP_010550736.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..611
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=66955
     Region          3..610
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mtaapiedha llsdqrtaal vtregdvdwl cmprfdsdal ftsllgedrh ghwslriadg
       61 evvsrrylpg tmvletqwrs ptgaatvvel lpvdaeraip spdpvahpdg adadlsdlir
      121 svsctegeve vvqelvlrfe ygeavpwvrr sadaagqgvl lavadgdavs lhgpalragh
      181 rshhgrhrls agegadwvlt wfpswqevpa apdveaalaa tsvewsswlg sirvedeyae
      241 pvarsllvlr althrrsggi vaapttslpe dlggvrnwdy rfcwlrdaal sleallahgh
      301 vdaavswrew llraiagdpa rlqimytitg drnlperelv hlpgyesslp vrigngastq
      361 yqadvvgevm ialstmreag vaesrwswpl qkalvrftta hvddpdqgiw emrgepafft
      421 hgrvmvwatf dravravteh glpaseeela ewtrlrdrvr aevlekgvgp dgaftqtygs
      481 tevdasllqi phtgflpada pqmlatvdri eqdlrtedgl llryrtrgqd glpgdehpfl
      541 vcgfwlvqqh aatgrrdeae qlmetllacg ndlhlfaeey dgthrrmign fpqafshlgl
      601 igavdalaaa g
//
LOCUS       WP_010550779             230 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010550779
VERSION     WP_010550779.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..230
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24665
     Region          13..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtsstpsger apdprpartr aaifaaarel sandgevtvn alakragvsr aafyshftgl
       61 ddlmgamlqe mfdaawergr tngaagytiv qhvqhgyamm aayierhhaf lrgaldwkss
      121 hrtfmiltgt maalhvealk rmpdrlpprp giealaltia ggelvhaeqw lvateeaara
      181 gealdatell evmlasapsw yvglgpdepi paaellsstr tygedaadqh
//
LOCUS       WP_010550782             295 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550782
VERSION     WP_010550782.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10897914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..295
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=30350
     Region          8..143
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
     Region          152..280
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mepsarsilv gyddtsaama avrwaaelah dtgagirllh awtwpllgqg lagipvldpa
       61 gprnqasrll ddaaeriaaq hpdvpvtael vagmprevle easagtdllv vgtrglgavl
      121 gtllgsvsrg llhdagcpva iirsdqhrag pvlvaydgsd tageavdvaa dlaaawgstl
      181 rvvhvrtvph vpygsggeaw eagkgtrall degvararar qarvevqsrm leartaaegl
      241 ldaaagarml vlghrglsrg rfgstahatv lhatgnvtvv rhapegwaaa hedvt
//
LOCUS       WP_010550793             341 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010550793
VERSION     WP_010550793.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..341
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34530
     Region          11..320
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mrrrtllslt aatalggalt acgsavtged ssggsggaag tvrvghlpsa lfaplyvada
       61 mgyfeeegvt leltplksgq dgvpmlsndq ldvmvagfsa gmfnaleqgv afkvvgsmgi
      121 spgdpenspt alevrqdlld dgtvseiadl kgrtigvagg pgatggylla amldeggltl
      181 ndveisnlat pdqepaltng svdaatpsap fsssieqagi asplavpakg ttgtgvmyse
      241 tfvgaelaqg fftalakgaq elsadgkqtd evyqiladtl gqdievlkas pmytylpdla
      301 pqpdqleamq avwidaeqit ytepldiagi vdasfaeaat a
//
LOCUS       WP_010550797             179 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010550797
VERSION     WP_010550797.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..179
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19529
     Region          2..172
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mtryrfftat sldgfladeh dsldwllfqp tgeesilpyd dfiaevgaiv tgrttydwvl
       61 ehdgdvegaw vftqptflft hraveqregv tavsgppaeq rgaievaadg kdvwivgggd
      121 laaefaragm ldevclsiap vtlgtgrplm ggrfdlelre lgrsgaflea ryevvgerr
//
LOCUS       WP_010550809             272 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550809
VERSION     WP_010550809.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..272
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28876
     Region          42..265
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mslvrtlril asqrpslppr svadpsrvrr vrhdhvpvtw idpelastat ivhlhggayv
       61 qgesrqtwew leevarragt aaamihyrla prhrypaavd dvlraladmq rgavlrpgrw
      121 vlsgdsagag lalavaqtla atagevpaal llespwsdls redhgeeslk vaarlyagav
      181 prteprlspa lgdltglppv hlvggdrdpl vhdsrrliaa laaagaehev lelpgsghqa
      241 avaadgpaaq earrfqitav raalgidera ar
//
LOCUS       WP_010550815             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF485 domain-containing protein [Brachybacterium].
ACCESSION   WP_010550815
VERSION     WP_010550815.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..135
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=14662
     Region          32..134
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 mttpppaasg pspepglspd rgpasppgaa psptpeqfqa vqkseefgrl rssfrsfaip
       61 mtvaflvwyf ayvllstyae glmstpvlgn lnlgllmgis qflmtflitw lyirhanrnl
      121 dpiaeklrde legeh
//
LOCUS       WP_010550824             112 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010550824
VERSION     WP_010550824.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..112
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12240
     Region          20..106
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mtigadglpe ahahdpeeri avrdnatarr yeavrggevv gimiyertrr rielihtvtd
       61 pehrgegvas vlvrtvlaea raaalpvlvi cpfleswlqr hpdqadgvia ed
//
LOCUS       WP_010550828             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ferritin-like domain-containing protein
            [Brachybacterium].
ACCESSION   WP_010550828
VERSION     WP_010550828.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..262
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29806
     Region          <75..180
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(77,80,141,171,174)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mafdidhfae tslpvkyadl dfdlfdeqpl daqtlrslry mcdveyhtsc fmrdllvtps
       61 hreeeaggfm tvwnreeywh gealarvlgr hgivvdydev kakrvklgwr aalgpmkqss
      121 lsnlvgkdfl avhmtwgaan elsavaayrr lsamvdhpvm tpllkriaqq etrhvayytt
      181 sarrylease rapklvrlvm skvwkpvgsg mmdesevrhv mnhlfahqgd eldkldkrvq
      241 kmhgldglti frnafarlgv pa
//
LOCUS       WP_010550902             445 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550902
VERSION     WP_010550902.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..445
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=47443
     Region          3..436
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mdpsvlvnig lvllfvligg vfagtemaiv nlresqidql eesgprgakt atmvrdpnqf
       61 lsavqigvtv agffssayga stiapslvpv ltglglpeat agtaaligmt liiaylslvl
      121 gelvpkrlam qnalgmtrvv gpplhlfgql mrpviwllsa stnlvvrllg gdpnanreav
      181 saeeikamvr dsdaldqaes rvladvfdas ertvvevmqp rhqvhfldgc qsveesrqei
      241 rdtgfsrypv tgddvddvlg fvhvrdmllv edpvrtrmse lvrpiehipg tvqvlsalnr
      301 mrahadqiav vvdeyggtdg ivtledllee lvgeiydefd adtwpapggl dsilaadgtf
      361 egglilqefe aatdislpdt ggyetvggfl maqlgripea gdtvavdggt levaevderr
      421 vktvrfipgt paegeeqade etpsv
//
LOCUS       WP_010550922             133 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010550922
VERSION     WP_010550922.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..133
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13724
     Region          <3..>127
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          16..43
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(18..19,22..24,26..27,31,34,43,45,47,51..52,55..57,
                     59..60,64,67,76,78,80,84..85,88..90,92..93,97,100)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          45..76
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          78..107
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mtddsldpel ielanallda artgdaetvr afldngaptn lrdasgnspl mlaayhghaa
       61 lvtelaarga dvdllndrgq splagaafkg ltevaralle agadpdlgep sglataryfe
      121 raeiveliea rqa
//
LOCUS       WP_010550938             231 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010550938
VERSION     WP_010550938.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..231
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=23802
     Region          12..>115
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          92..209
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 mnaaptsral arertmariv elgnaqlaes gvaglsvrei arglgmvssa vyryvasrde
       61 lltllivday edlaavveer lagagdgpre rflalggams swalaaperw sllygtpvpg
      121 yaapsettna pgtqvtrevl aiaadaargd rplgespala psvaellaqh lgefdidada
      181 ataaravtaw sglvgvisah lfgqlgpdav algegilrpq ieiladliap r
//
LOCUS       WP_010550984             300 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar ABC transporter permease [Brachybacterium paraconglomeratum].
ACCESSION   WP_010550984
VERSION     WP_010550984.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..300
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32082
     Region          13..300
                     /region_name="MalG"
                     /note="ABC-type maltose transport system, permease
                     component MalG [Carbohydrate transport and metabolism];
                     COG3833"
                     /db_xref="CDD:443045"
ORIGIN      
        1 msthtsqqts vtaqrrmpfg rwmaevgwrh vvgilavafa vfpilfiisa svnplgtvss
       61 sglipkafsl vhyesliagd rgpflrwyan tvivcgtval vqvflstlaa yafsrlrfag
      121 rrigllslll vmmfpaflam iavysmvsgl gkaipflgld slpgyiivll ggslgqvwli
      181 kgffdtvpke ldeaaiidgc shwqvftkil lptltpilat tillalvgvl sefllgsifl
      241 tsndtktlav glygmlegdr snnlgvfaag svmimvpvii lyqflqryiv ggstagavkg
//
LOCUS       WP_010551058             276 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551058
VERSION     WP_010551058.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..276
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=29213
     Region          25..198
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mgelldrlls ltgvledwil qigdawwvhl vvyafaaldg ffptvpsest ivslsslwss
       61 sgrpsiilig laawagaftg dnlgyllgnk igwerfrflr ggkgrravea aenglrkral
      121 vflmtaryip fgrtavnlva gavhyphrlf wprsllstfv wavyscaiga vagawfennh
      181 llaitvalva aivmalvver iiaavhrwld rraerrdaer rdaeaaadte agsavetgtg
      241 vgtgsavgag savgtgpgad aeadaattvh gedspa
//
LOCUS       WP_010551063             111 aa            linear   BCT 01-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551063
VERSION     WP_010551063.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..111
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10673
     Region          1..>60
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mptyvyackn cghrfeqyqs fsedslttcp ecaqealrkv fdsvgivfkg sgfystdsat
       61 sgastvgggs ssdgagssas ssegsapsss agpssggssa gssaqpaaaa s
//
LOCUS       WP_010551069             286 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551069
VERSION     WP_010551069.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..286
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=30138
     Region          29..264
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mnttassaps paqllehalt aahaaaeylr gldrddlsre yktsshdivt ehdrrseeii
       61 vselrrllps arivgeegge rpaaepsgpe qvsfyvdpid gtsnfaaglp lfcisigvti
      121 gdelvagvid apvlgqvfaa adgpatlngr eiipretrpa pdalvlsgyp gqrtgsrfpe
      181 yaanavrtle dsvsavrhlg saalelayva agwadatalt ainswdvaag fhilrraggs
      241 lrtwpgeeva erpdhlqpay vacsgqgrle vldglqdelq alrvgs
//
LOCUS       WP_010551101             506 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Brachybacterium].
ACCESSION   WP_010551101
VERSION     WP_010551101.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..506
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52251
     Region          26..500
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mqqadpspss srtapdaatt tpeaprgald rwfhitargs tipreirggi vtffsmcyiv
       61 vlnpliigtv pdstgmylgg gtepnlpava agtaliagll sifmgawakf plalaaglgl
      121 naylaysvvp lpgmtwggam glvviegvvi lllvlsgfrk avfdavpafl ktaiavgigl
      181 fiaflglyna kfvttangtp vqlgndgslt gwptfvfvag lllmfvlwvr kvpgailiai
      241 vtatalsivi ervlhlgafa pagadgpgnp ggwamnvpav sefpvqlpdf stlltvdpis
      301 gitaagavga svivfsllla dffdtmgtmv gvaagadlvd eqgdiphsqr ilvvdsaaai
      361 aggmggvssn tsfvestsgv aegartglsa vvvgvlflls tflsplvgmv pyeaatpalv
      421 mvgflmmtqi tdidftdvei aipafltiil mpfaysitvg mgagfimyvl lklvrgkars
      481 ihwlmyvial mfvayflrga veglll
//
LOCUS       WP_010551108             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [Brachybacterium].
ACCESSION   WP_010551108
VERSION     WP_010551108.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..316
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33957
     Region          21..310
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mpddfppdlg pllatpstee alsladqllr wlatsgvkiv vilvaatvls lvagwllrrf
       61 fttmvqsgsr isnaastvik rdprsqkaaq arreqraetl snvarnvara viwaiafmmi
      121 lseigvniap viaslgvvgl aagigaqtii kdvvagivml fedivavgdw vdleyaegtv
      181 esinlratqv rgidgvlwtv rngeiirvgn yargfsnavv tldidagadd etvtrileqv
      241 tadlqadpqw kepilapadi sgildvdgnr yqrrvvvqtv pgqqwgvere lrsriragfa
      301 sahvafalpr fveagk
//
LOCUS       WP_010551153             257 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Brachybacterium].
ACCESSION   WP_010551153
VERSION     WP_010551153.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..257
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27526
     Region          14..250
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 msapenapda rpplsvaglr ktfgelvale gvsleiergt ttvllgpsgs gkstllrcln
       61 lleqpdagtl dlgdgpidvg grlpartvrq irsrstmvfq qfnlfphlta lgnvtlapie
      121 nlgldraeae trgrellgkv gladkaeayp drlsggqqqr vaiaralamd pdvllfdept
      181 saldpelaae vvavlsdlaa ehrtlvvvth slafarrvad rvvfledgri lqdggpeeff
      241 sstderlrrf revissv
//
LOCUS       WP_010551178             425 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdopterin molybdotransferase MoeA [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551178
VERSION     WP_010551178.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..425
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.10.1.1"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061599 - molybdopterin
                     molybdotransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=43247
     Region          14..409
                     /region_name="MoeA"
                     /note="Molybdopterin Mo-transferase (molybdopterin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG0303"
                     /db_xref="CDD:440072"
ORIGIN      
        1 msserlspwq wreeilaava pprraervpl eqargrvlaa avrspeqvpa lpiaamdgfa
       61 vrradltapg ttvlpvaael parpgevpdl psgsaarimt gapvprgada vveveatdsd
      121 pfgpapavva laleslpvpg rhvrgageei pldaplalag drvgaglvgl artlgidale
      181 vlrplrvavv vtgdeltads ssdrlgadpl pgavresnga mlaaalaadg ahalpprhcg
      241 ddpadlretl diaageadlv lttggighga ydvvklllge rgagtsrfeh lalrpggpqg
      301 hgtlpggvpv vhlpgtpvga lvgyhlfvrp lldrdgaapr rmllrgegdg prrgpagtvh
      361 alpgrrevaa dgrevvrlvp grrlapygra damvlleseg pvggaapgsg elvgapersv
      421 lvlvl
//
LOCUS       WP_010551196             548 aa            linear   BCT 01-JAN-2025
DEFINITION  inorganic phosphate transporter [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551196
VERSION     WP_010551196.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10475700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..548
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56543
     Region          72..531
                     /region_name="PHO4"
                     /note="Phosphate transporter family; pfam01384"
                     /db_xref="CDD:460184"
ORIGIN      
        1 martsaqdst dapvtkgflg pdrnwhlgag lmtlatvvaf tiwafthtgt dvnafllila
       61 iafglfmafn iggndvansf gtsvgagtlt mkqalvvaav fevsgavlag gsvtetvrsg
      121 ivdlggmaid plafalimms allgaavwll latrmgwpvs tthaiiggiv gaavttglvt
      181 gtggfamvqw geigkiavsw ilspllggia sfllfgaikr rilspaarai algsrgydda
      241 eddddddeed dadeswqrhv pasermtelq qsafaesaal dltpggpgae lieasanltk
      301 kerkaarkve rkaayhalek rvpplaagaa mllaamlvfk gldnvglnis vgggvlmlvm
      361 lalgvwmatt ifaralkkqs isratfimfs wmqvftacaf afshgandia naigpfvavl
      421 dvlktgqiga eaavptaali afgialvsgl wfvgrkviht vgtgltamhp ssgfaaelaa
      481 ativllasvl glpvssthil igavlgvgiv nhaanwrlmr piflawiitl paaagigaav
      541 vlvlramf
//
LOCUS       WP_010551214             209 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Brachybacterium].
ACCESSION   WP_010551214
VERSION     WP_010551214.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22838
     Region          24..174
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtsaqttddh dpagseelgl relkkrqtrm amhraalelv vehglsavta qmiaeragvs
       61 trtffnhwvt kesailging gegaqaiasl rekllvmpar eamrsmmrea ianvpvdrgl
      121 relkkqvmeq epslhlvssg nlqamqtelv eelaealege fardhavilv qvsfaltrsa
      181 faismrrgid pvrafdqvlt lydgsgtei
//
LOCUS       WP_010551207             320 aa            linear   BCT 01-JAN-2025
DEFINITION  SURF1 family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551207
VERSION     WP_010551207.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..320
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=33561
     Region          3..250
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mlrvalrprf lgllalmiva tivcgllagw qwdrahralt dkadgpqqig direvvgvgd
       61 avtneivgdi vtadgrfaag eqvlvpgrri egqdavivvt aflveledgt earlpvargw
      121 lpaedvtged galdpalapa apegevrlsg rleasesasg gvvdgvarei atpllvnewg
      181 spmyagylal detdapltal paaesqfsrg ldwqnigysl qwvafgvffl ylwwrsvrta
      241 yrdelddrre everllaeas gvglrpgpsa gagpadgaep apsadptdrc agadhaagla
      301 psgaapssrp apqqnpdkdv
//
LOCUS       WP_010551231             338 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551231
VERSION     WP_010551231.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..338
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36680
     Region          41..312
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mstdpvlgag ytlhridlgs ddegplrasl ihrepvpgda pradrtppvl lmhgwsdyvf
       61 drdlmdhlgt rghdvwgldl rkygrsilpd qtpteidhls rydeeigasl rrigrstppv
      121 ilahsagglv atlyalrhpg vvrglalnsp wlemhlgpgt rrllerpvhl larrlrsrpi
      181 lpvgddayar athrdlggdy dydlelkppg ghrfpastlk amldghrrla aagplaapal
      241 vmhsdrtait srrgerplha dtvldvrsla aaarrlgprv rvvpvtgarh dvflsdppvr
      301 ataieilddw latdllaapt mtrtgrtagp dasetgas
//
LOCUS       WP_010551245             280 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551245
VERSION     WP_010551245.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..280
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28588
     Region          8..277
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 msssapfrrr aafldfdgtl aesgivpraq aeavlaaraa ghavllstgr pasivasdva
       61 alfdgmitsa gghirigeel lrdvrfpaal arrtvevlea hgaayaleap ealwcsassa
      121 drlerrrrga pvpsagelgr gfadileais vpedpaavsf akisvwsspv pieqlaaevg
      181 pevgalpnsi sedgrgsgel hlaevdkadg lrlaaehlgv giedtvavgd gandlgmlra
      241 agtgvairgs rpevlaaadm evappsghgv eeafarlgml
//
LOCUS       WP_010551270             393 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551270
VERSION     WP_010551270.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..393
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=42585
     Region          16..302
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mttsrprrpr pqvelvrprl silhvlnrvr mrlldiqvwd vagtmtfyll lslfpgavav
       61 vsmmsligie setlsalsgl iteifptldp rpylgaiqav sstgggllgl llgtlgslvs
      121 asngvaafhr alhrvydtre grpflwfrti vfgetvlita vvllaigmii lggeasqrig
      181 efigiplfaf hawnivkwpv llviliigvs layylfpnvr lpryrlmtlg stlsvltlfg
      241 talvagqllv yatrfaevlt alngliaill lmwianivvi tgaaldaefl rarqlatgle
      301 awhklelaph athtldflar dadeaeelgr avaesvrsge plrrergawi vestnplavn
      361 pprrhrvtsd plpeestdtg psadpssqgg spa
//
LOCUS       WP_010551266             347 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551266
VERSION     WP_010551266.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..347
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=37160
     Region          84..336
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mnrnddvelp adwdddsdvg terrrgrraa liafglvavl vigvgivvgs ylnglrnsye
       61 krsvvditra egerpeaeeg tgqnilllgs dkrseeaaaa egvtgqrsdv mmlvhiaddg
      121 esvyitsfpr dlyvdipghg kdrinaalaf ggpslavttv edytgvpidh validfegie
      181 glvdtlggvd vqvpmdfead gieytagtqs mdghealvfv rqrkqfadgd fqrnrnqqav
      241 lkgiadklis adtltdprkl adtietvspy lttdegltag emttlglslr sirgddlhfl
      301 svphggpttt sggasvvatd eeamdvlrea lrtddmgtyy aqyagay
//
LOCUS       WP_010551284             251 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551284
VERSION     WP_010551284.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..251
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26876
     Region          11..241
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mdghsgqnpa vrivglrksy rgrpavdgld levargetlg vlgangagkt ttvelvaglr
       61 radsgrisvl gldpvrdraa lrqvlgvqlq esflhgaltv gelvdlygsf yacprpreel
      121 ldlvelreqa atrferlsgg qqqrvsvala migrprvlil delttgldpa arrrmwrtle
      181 tlraegttil lvshamdeve rlcdrivllr agreiaagtp aevtaaagaa sledafvdlt
      241 gstphaqetl r
//
LOCUS       WP_010551322             486 aa            linear   BCT 01-JAN-2025
DEFINITION  S-layer homology domain-containing protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551322
VERSION     WP_010551322.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Gerbino,E., Carasi,P., Mobili,P., Serradell,M.A. and
            Gomez-Zavaglia,A.
  TITLE     Role of S-layer proteins in bacteria
  JOURNAL   World J Microbiol Biotechnol 31 (12), 1877-1887 (2015)
   PUBMED   26410425
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Mesnage,S., Fontaine,T., Mignot,T., Delepierre,M., Mock,M. and
            Fouet,A.
  TITLE     Bacterial SLH domain proteins are non-covalently anchored to the
            cell surface via a conserved mechanism involving wall
            polysaccharide pyruvylation
  JOURNAL   EMBO J 19 (17), 4473-4484 (2000)
   PUBMED   10970841
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Engelhardt,H. and Peters,J.
  TITLE     Structural research on surface layers: a focus on stability,
            surface layer homology domains, and surface layer-cell wall
            interactions
  JOURNAL   J Struct Biol 124 (2-3), 276-302 (1998)
   PUBMED   10049812
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Lupas,A.
  TITLE     A circular permutation event in the evolution of the SLH domain?
  JOURNAL   Mol Microbiol 20 (4), 897-898 (1996)
   PUBMED   8793886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..486
                     /product="S-layer homology domain-containing protein"
                     /GO_component="GO:0030115 - S-layer [Evidence IEA]"
                     /calculated_mol_wt=52251
     Region          371..413
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
     Region          434..473
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
ORIGIN      
        1 mstpvparss sttaptrarr rlallvlavl iasagvlgaa pgseartppa glggfvpgtl
       61 isdaqmfagt smtaaqvdaf ldqkgasctr gtdgadclkd lrmdtpqrsk daycaaipak
      121 kaasagmiia dvaracsisp kvlltmlqke qglvttrnat pkmlrealgf gcpdfqtcdp
      181 ryagfaqqiy nagvrlqayg dpargyryqa grtydiqysp fafcgygkvt isnrataaly
      241 nytpftptqa tldagsaava ddvcatygnr nfyrlyaqwf gsatgastsr ypvaaplgkk
      301 paapfadvpy dttiffteia wmkhmgystg wgsgasavyr pydqikrdav iaflyraags
      361 paftppkvsp fkdvnskdtv fykeitwahs vglaqgwpdg tfrpyepikr damaaflhra
      421 agapaftgpt rspftdvhrg sevfydeitw mavngystgw sdgtfrpyep ikrdavaafv
      481 yrwkva
//
LOCUS       WP_010551360             299 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551360
VERSION     WP_010551360.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..299
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30275
     Region          94..297
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mstsapdpaa atastsveav avapegehak rrgpgrnlpa aigvglalva vlalsvlvmp
       61 qafpvvaaia mvaavleltr alahgglevp avpllvgvig mvvstvvfga eglmlstaaa
      121 vcvlilwrvs esmgltalrd vaggvfalaw vpflgcflll lmqrdqgaml vllavlgpvg
      181 ndvggyiagv lfgrhpmapg ispkkswegf agslvlgtam vtliavlale lpwwvgvaig
      241 avlvvvstcg dlaesllkrd lgikdmghll pghggvldrv dsillaaptt yvmlevllp
//
LOCUS       WP_010551481             171 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Brachybacterium].
ACCESSION   WP_010551481
VERSION     WP_010551481.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 171)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..171
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19416
     Region          47..144
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mttrrgralg ailtaghrlr riwwrlrrpr tfgvkvllrh peqpelilav rhsyvdqdrw
       61 alpggryrpt retpsdaarr evreelglri rddlaelrtl eartegkrdt ltllsgsadg
      121 veartslelr evrwlrtdla dvpagdpvsr wlrlaiegct draddgtpgp d
//
LOCUS       WP_010551525             263 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Brachybacterium].
ACCESSION   WP_010551525
VERSION     WP_010551525.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..263
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28042
     Region          1..258
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mfivsvcslk ggvgktsvtl glasaalhqg vnalvidldp qgdstlgllg epastldiae
       61 vlssprteti draiiptpws kdaashldii pgtsrsavmd spalnqkdvg rlhqaldkrt
      121 hqydlviidc ppslngltqm alaasdrslv vaepgffavt aadralklaa emheegiapr
      181 lqplglvvnr yrprsvehqy rlaelrdlfg dsvldpviee rvglqqaqgg avplhryega
      241 sgarltedfd allrtvmdsr qns
//
LOCUS       WP_010551542             342 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551542
VERSION     WP_010551542.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..342
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=35444
     Region          196..296
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mstthtsspp prdpvgrvps aaapsaaeps gapvaadtap rpaaapgsap eprsgldper
       61 pfgahlrlaw wkplliipgl lvamvvlqtv ltlivvlvem aafgrdpmda tisplmmavm
      121 nlslaamgpl ailvtalvar vpwrwliasp rraslcrglv yagafsalvg valaltalid
      181 psaagigqfa itsttiglvl vallttplqa ageellfrga mmpllaswvr avrpalvlgm
      241 iassivfglv hmsvdpwlls yyavfglcma amavisrgle apiafhvmnn limmvvgalf
      301 aggggividr svgmggpvml vfivvdlvav glvwlyersq rp
//
LOCUS       WP_010551545             221 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Brachybacterium].
ACCESSION   WP_010551545
VERSION     WP_010551545.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..221
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24179
     Region          14..186
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdlfeplpe sagtrrkent raklvrasld vfvekgidga tvddlvkaag ftrgafyssf
       61 sskeevfial fdevtaelma ianssvesav adveadescs ileaddaqvm lavfegirpf
      121 grqwyllysd aiarslrdea lraelaeqre rmrnqigall ttrleasger allpvedlaq
      181 llmgifidll vreqlegrdv tqlaattilg tlrafiapkt d
//
LOCUS       WP_010551585             565 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551585
VERSION     WP_010551585.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..565
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=61006
     Region          102..553
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 msedrrggrr hddswrgrdd rggrddrrgr ddrgsrrddr gdrrddrggr rddrrdlprd
       61 aqgrersgsr gqggprrgws ssrpsersra stpsrqvale glrlvreeds yanlvlprll
      121 rshrvsgrda afttelfygs lraqgrldai iaacvdrpla kvepalldvl rlgayqlldm
      181 tvaphaatse tvalaraevg aggasfanav lrrvgekdla twiaevapdr ekdptghlav
      241 vhshprwvvr alsdalagng rsrdeidqll eaqnqapavs lvmrpgltdl delidhgasq
      301 grlsifaaaw psgdpggmdl vkqgrvavqd egsqlaalsl algaddlvlt ddahwldlcs
      361 gpggktallg gltidhdadl lavelqehrt elvdravasl reagceittl tadgttigae
      421 rpgefsrvla dvpcsglgal rrrpearwrr tpadvgqlga iqrdlltsal datapggvva
      481 yvtcsphlae trlivadvlk rrddverlda rpavragllp avrdevelge gpdvqlwphv
      541 hgtdamficl lrrlpvptee gtpss
//
LOCUS       WP_010551605             155 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA (cytidine(34)-2'-O)-methyltransferase [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551605
VERSION     WP_010551605.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..155
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=16803
     Region          1..153
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 mvhvflhepa iagntgnair laavtgarlh lieplgfdle daklrragld yhdlaevsih
       61 pdletalaav pdarvfafta htetafgqvq yrredvllfg teptglpeev mahpritsrv
      121 ripmlparrs lnlansvsia vyeawrqlgy dgaga
//
LOCUS       WP_010551724             293 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF817 domain-containing protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551724
VERSION     WP_010551724.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..293
                     /product="DUF817 domain-containing protein"
                     /calculated_mol_wt=32489
     Region          20..292
                     /region_name="YoaT"
                     /note="Uncharacterized membrane protein YoaT, DUF817
                     family [Function unknown]; COG3739"
                     /db_xref="CDD:442953"
ORIGIN      
        1 mapdrvpftp leeridrwaq rrtsalatag gtrrarhvel vvfglkqawa cvfgalmlvl
       61 lvtarvlypd daplaradal vlaavavqva mlalrleslr emgvialfhl vgtamevfkt
      121 avgswayetd gllrigevpl ytgfmyaavg symvrvmrlf dlrftryppl lataalaaai
      181 yanffthhyl pdarwvllaa tlllygrcam slrvhrrapw rrmpviaafl gvagllwiae
      241 nvgtaagawi yphqragwel vpasklvswl llmmvsvvlv tlvhrprrpe raq
//
LOCUS       WP_010551649             315 aa            linear   BCT 01-JAN-2025
DEFINITION  ACP S-malonyltransferase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551649
VERSION     WP_010551649.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Marcella,A.M. and Barb,A.W.
  TITLE     Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as
            templates for engineering
  JOURNAL   Appl Microbiol Biotechnol 102 (15), 6333-6341 (2018)
   PUBMED   29858956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..315
                     /product="ACP S-malonyltransferase"
                     /EC_number="2.3.1.39"
                     /GO_function="GO:0004314 - [acyl-carrier-protein]
                     S-malonyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31937
     Region          1..300
                     /region_name="FabD"
                     /note="Malonyl CoA-acyl carrier protein transacylase
                     [Lipid transport and metabolism]; COG0331"
                     /db_xref="CDD:440100"
ORIGIN      
        1 mlaivcpgqg aqkpgfltpw relpgveell gslsepagid llrhgtesda dtirdtavaq
       61 pllvaagiva asqlrseedl paadvlaghs vgeltaaalg gvlsdedamr lvavrsrama
      121 taaaaeptsm aavvggtred vlaaierhgl hpaninsaaq vvaagsaeki aalgedgpak
      181 arviplqvag afhtpymaaa reelaafapt lspadptlpl vsnaggevvt sgaqyldaiv
      241 tqvaspvdwe acmatfrdrg vtamievapa gtltglakre lkgialanln tpddleaara
      301 lvrehaglah sdqea
//
LOCUS       WP_010551868             387 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551868
VERSION     WP_010551868.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..387
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=40208
     Region          13..>55
                     /region_name="PRK09834"
                     /note="DNA-binding transcriptional regulator"
                     /db_xref="CDD:182100"
     Region          78..373
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mqsthlrehn lsavlralqt apspasragl atltqltkpt vsklveelig aglvaegepv
       61 aagagrpmvp lrpasgtlla igleiaadhi sclgidltga elarrttyhr iaegtaedal
      121 alaaqlvhev reeapelpvv gvtaaipgrl spedgrilsa pgldwadvpv isrlqellap
      181 aawpvgaqnd nrlsvlteid rrpgesflyv rgstgvggav vldgavlega hgwagefght
      241 vvapdgrqcr cgrrgcleay isylslvrqa glsdevried lveelarsss raevigvigr
      301 slglaianal nvldlstvvl sgylapiaee itpvvqetvd rhalaaeagp vaieradala
      361 dpalhgaara alqpvfdapv swvekes
//
LOCUS       WP_010551854             346 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551854
VERSION     WP_010551854.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..346
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36775
     Region          1..265
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 maqrriglig ygdvsvvhvg aieaidglel vgiadvdpta reraaadtgl ptfasaeeli
       61 dalgpdavhv ttphdqhvgp slaalergvh vlqekplaht laegerlvea lagasgprad
      121 ggagapkiai cfqnrynrgs qelhrllasg elgavrgaya svvwsrsaey yaakpwrgrw
      181 etagggllin qaihtldlvq wllgpverte glvsqkkfag vvetedtadl vlhhasgitt
      241 tfyatltapv arpvelevet dnaylevrsg ivggltvrwk dgrvdsfsdr vataggrsyw
      301 gvsheelird fyagldsegp fwigpaeamd slrilkeayr stgvgn
//
LOCUS       WP_010551909             236 aa            linear   BCT 01-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551909
VERSION     WP_010551909.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..236
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=23453
     Region          1..225
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mttlvacshg trspagrtvi ariraalava vpdaavreay vdveqpevae vvaeaasrgp
       61 vvvlplllst gfhtsvdiaa avaphpgava aeplgpdghl vralrdrlaa vsggdaghrp
      121 gdhvvlaaag stdpaaarav ermrdllsar lpapvttgyg agcapglpea vaaaraagar
      181 rviaasyvla pghfaglvhr agadlvsapl gdhpeviava aqryrearaa ialavg
//
LOCUS       WP_010551936             255 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator
            [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551936
VERSION     WP_010551936.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..255
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26487
     Region          1..242
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlseerhrai vsairrggaa tvaalsadlq vseatirrdl dalaeqglvr rvrggatdpr
       61 gsvrpeadpc sfadvaasap aakqaiaala ctqirdgevi aldigttvaa mcpllaersl
      121 tvvtaslavv ralasapaid ivvlggllrp nydslvgtlt esalrqlrvd raflgtagvr
      181 adgavldstp sevpvkrgll evatcsylla dhekfpgsgf levarlprft alltdrplpi
      241 eidlpegeav evllp
//
LOCUS       WP_010551938             277 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010551938
VERSION     WP_010551938.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..277
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29849
     Region          11..273
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mtavpappfh dgssvpqlgy gvwqvedeva advvrqaida gyrhidtaag yqneggvgra
       61 vkaadvpred lfittklane dqgfdsakaa ldaslekldt dyvdlylihw aspqrgkyle
      121 swkalielqq egkaksigvs nfpipqleei iaetgvvpvm hqielhpqfq qselrryhae
      181 kgilteawsp lgqggdilkd pvitaiaeah gvdagqviia whlaignvvi pktvtperiv
      241 snlaaaqlvl tdeeveridg ldradgriga dpanpgf
//
LOCUS       WP_010551986             250 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551986
VERSION     WP_010551986.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..250
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27075
     Region          16..247
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtttaatnap dttttapalc vrdvtvtypd grnpdgserl ntvlhqasld vargefavil
       61 gpsgsgkstl lsvaaglvvp dsgsveiegt dltaldekrr tamrrdrisv vfqqpnllpa
      121 ltvrdqllvt khlagvrgrr lraerdraea mlervgmgqy adrrphelsg gqrqrvniar
      181 alftdpavll vdeptsaldh ersrevvdll vgitrelkva tvmvthdref aedadrvitl
      241 rdgqvedpav
//
LOCUS       WP_010552002             209 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Brachybacterium paraconglomeratum].
ACCESSION   WP_010552002
VERSION     WP_010552002.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21371
     Region          2..204
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mldvsvlpaf llavtvilvt pgpdmafmva tginqgrraa vqgafgvtsa mtiwvlvaat
       61 glgvaltqlp aaldairlag agylaflavt twrragapla easvvpnvfr rgfvvnitnp
      121 kialffvafl pqflgttggt genpfaqilm lglllqltgl ltdlaigsaa glfrdavlsr
      181 prvrclldga agtvygalav llvmgvvhg
//
LOCUS       WP_010552003             142 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010552003
VERSION     WP_010552003.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..142
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15815
     Region          1..134
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mlddldyrli allransrtp vavlarelgv nrstvtsrid rlvdngvieg ftirvsgdie
       61 hdsvqgvmlv atensrspei vrelrgypel eqfhsttgtw dlvlqirarn laefdlvler
      121 vraipgvrtt qtnllfsslr ta
//
LOCUS       WP_010552062             220 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010552062
VERSION     WP_010552062.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..220
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23768
     Region          26..215
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mttspqygpv elisphldes avvrggaqda pivlllhglg sderdlaslv pflppvfeyv
       61 svrgifryvq gfawfdmpva pdrpeaiess aaaveewiaa qdrpvvgaig fsqggavalq
      121 llrrdphalr fvvnlsgfpf paamqgdaal aevrppalwg hggmdplydp ereqavrefm
      181 gahttleeer rpqlghavde ielravaafl qrraadadgr
//
LOCUS       WP_010552079             407 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Brachybacterium paraconglomeratum].
ACCESSION   WP_010552079
VERSION     WP_010552079.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..407
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40953
     Region          13..370
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(23..24,27..28,31,63,116..117,119..121,124,143,
                     146..147,150,225,228..229,232..234,237,265,269,318..319,
                     323,327,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mpssptlslr rrrfalyalf llpglsmsaw vtrtpavrdl ldastaqmgl vlfglsigsm
       61 lgilssgplv mrlgtrpvvl agstlgvval ptialgasmg qplltafgla lfgggmggge
      121 vamnvegadv erlggrsflp slhgcfslgt vigavlgila ngagfpvvph lvataavgag
      181 lllwamraip tgtgrvtaae raaqaatprp aiwkdlrlvc iggvvlamal aegtandwlp
      241 llmvdghgfg atmgslvfal faasmtigrf sggpivervg rsrvllvsal faatglalia
      301 ymdsqvvavv avvlwglgas lgfplalsaa gdsgpdsaar valasvigyl aflvgpptlg
      361 flgeeiglrg alvvplaval laavlspata trrptaeeql gsvadmr
//
LOCUS       WP_010552093             463 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Brachybacterium].
ACCESSION   WP_010552093
VERSION     WP_010552093.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..463
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49313
     Region          1..459
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mststqptdt pattrrrpgl sarhlhfial gsaigtglfy gsagaiqaag psvllvyllg
       61 gavvyfmlra lgemavrmpi sgsfaeytrr flgrwagyit gwmfafemli vcladltaia
      121 iymrfwfpdt aqwiwvaltl livgaanlas vrwfgelefa ftivkvaavv amilggaail
      181 afglgdpatp tglsnltadg gffphgpggm isafilvlfa fggteiigva gteaedpaka
      241 ipkavntvpv rillfyvlai gvillltpwq qitgeespfv qifdtlgvnw aaallnivvi
      301 taalsainad lfgagrvvag marqrlapaa lsrtmrgvpv vttlamlgvl vvgvllnwal
      361 pdevftivas latfatvfvw lmillaqvas rrgmsreera alafpvplwp ygqafaiafi
      421 lftfgimvwq seyhtallvg vgflavmsll yaatgrqrrp vrs
//
LOCUS       WP_010552144             307 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Brachybacterium].
ACCESSION   WP_010552144
VERSION     WP_010552144.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..307
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30542
     Region          30..282
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 melvllaigv glgvgivvga lgagggilav pvlvfllgmp phaatasslv ivlitalasl
       61 phharqrnve wraglvfagv svvgavlgsr lsalvppdvl ltlfgvmlav vaaamlrrgl
      121 rtrrtedaea aalgtaplad gdapiashdd pvldqpgpdt vetadglqhh hgepdlpfap
      181 aappsprlgs viaaasltgf ltgffgvggg fivvpmlvia lglamrrasg tsllvmiiat
      241 atsllarlgt dvqvdwattl vfaagsavgg viggplsaka rpstltllfa allagvaavt
      301 lvetlll
//
LOCUS       WP_010552193             153 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010552193
VERSION     WP_010552193.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..153
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16838
     Region          12..152
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mrrplpfldr tapeawdllg evrravaeqn eaagiatttl elmylrisql ngcafcvdlh
       61 hrravragap ddqvaqlpvw rdspsfdave raalllgetv atlpepmvrd rdlmvardvl
      121 geqafaalew savlmttynr lsvlshhpvp gar
//
LOCUS       WP_010552196             475 aa            linear   BCT 01-JAN-2025
DEFINITION  amidase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010552196
VERSION     WP_010552196.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..475
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49456
     Region          9..460
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtparptmlt qaaqllaegq atsreltdac laaidahdqe lrafitvehd tarstadacd
       61 arraegappr lldglpvavk dnldvagrvt tmgseifrdh vptgsaavvd rleehgavrl
      121 gatnlhefal gvttenphhg icrnpwdtsr tpggssggsa vavasgmala algtdtsgsi
      181 ripaaacgiv glkptygris svgcypeaws ldhvgvltss vadaallldt lsghdprgps
      241 slplppttsr qelddprplr igveeefffa gidpavegiv realegltra gatlvpislp
      301 slsdavfalt vidtaettaf hetqlrrhge lygedvrrlv ecgalatavd yvraqqirsl
      361 vraefarafa dvdviasptl pirtpriget svevggvtrd rdaelmrlvg psnlagipsv
      421 svpcgmldgm pvglqligpa lgegavlraa aaveslvppr ltptpsspts ppprr
//
LOCUS       WP_010552198             458 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Brachybacterium paraconglomeratum].
ACCESSION   WP_010552198
VERSION     WP_010552198.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..458
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49020
     Region          2..439
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtgssaglrr qlglmslial aagavlggwl aeapywfelt gagaalifpi laiilvpigl
       61 afaeltsmlp fsssvdvwas namnptagwa tqwlfflvqv vepplvafif vtaagyfvdv
      121 pvsvrpliai aimvvwyvfs nfnirltgvl aiilflvmvg itvgtsvyyl tsghwqftni
      181 sehgglfphg mmgaiaagsa lvlkyigfam tptmvqetrf aakrmvlvil aglfipavvy
      241 mlatvaiggl aphdviasls vpepelvdrl gmpsiiglla igagllyaft tlmgfwtssa
      301 rvlygasqlr qlppwfmrtn rhgqpyianl vvlgfgiffa aftstnwvqy tyslsvvaag
      361 avyflgclsa lrlrskrpdw ersfraplgt pifilgmavs aaitvigvtl lpanawppii
      421 ayivigalip vamrayrsrt dgdysplvlt pedigkvd
//
LOCUS       WP_010552253             244 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator
            [Brachybacterium].
ACCESSION   WP_010552253
VERSION     WP_010552253.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..244
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25447
     Region          9..243
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mdntpeengs gvgvldkaav vlgaleagpa tlaqlvqstg larptahrla valeyhhlva
       61 rdmqgrfilg prlgelaaaa gedrllasag pvlaalrdht gesaqlyrrq gdhricvaaa
      121 erpiglrdsv plgaaltmra gsaaqillaw eepdrlhrgl lgarftatql savrrrgwaq
      181 sigerepgvg svsapvrgpn grvvaalsis gpieritrqp grlhapsvms sanhltellr
      241 raga
//
LOCUS       WP_010552254             272 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Brachybacterium paraconglomeratum].
ACCESSION   WP_010552254
VERSION     WP_010552254.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..272
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=28481
     Region          9..144
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
     Region          159..269
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mthteapkit vgvfdadesd qavrwaarha atvggalhlv hafvwteldv nvdpisgmpg
       61 sgfrsaadtl lreaaelare rapeveitte vidgnsvpvl vhasqgsdll vlggrglgrl
      121 mtlivgsksl alaarshcpv vvvrgnidgd gpvglvhhes stevvaraad laeaygrdih
      181 lvvrpgtspe qaqeilaata qrialshpsv fvkdvavats dnakqlveas enasvmvvag
      241 erdeggsgki aaprqlvnvl ryantpvwie re
//
LOCUS       WP_010552238             514 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein
            [Brachybacterium paraconglomeratum].
ACCESSION   WP_010552238
VERSION     WP_010552238.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..514
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56781
     Region          330..388
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(353,355..357,365,375..376,380..381,384,388)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mtpqslvera dvaprtaeae tvlriyrrrr eqqaafyvae mqdlaslwse gdeddektlh
       61 alaaaaglrt klgrgenrlr dahvavtdlp acfarvgage lpvdwfewll rsvlrltshq
      121 rrqvdervat wqldaidver fyrelrlrid wygraavqet preqravhlt pspdgdgtgc
      181 ltvvgpipel lalgrrldsa aravqdaqrq aletgapipf dldgdvareg rpmplpalry
      241 avmtrsplat ggvevpepaf risvvvpilt llgrshapat ldgtipipar marelaakap
      301 afervladpa rggyapaasr tyrvsramae nlrlidpvca vpgcdcnvmt vgesdhieef
      361 dlehparggp ttienlhrlc rrhhrmktag lldpvrdett gvtrwrigel avcdsrpdgd
      421 lvtrelgqql rraweqyead lefeailhsg aldespqerl daieeqrwge hlleywsrpd
      481 tggaepddpd gphgpdvpgp pgldprdgyg pppf
//
LOCUS       WP_010552329             280 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Brachybacterium paraconglomeratum].
ACCESSION   WP_010552329
VERSION     WP_010552329.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..280
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29776
     Region          19..278
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mtashpavpt leirgaapip qlgygvfkvd pdiaadvtaq alaagyrhid takiygneeg
       61 vgraiaesgi preelfvttk lwddahaldd aiaaceasle wlgldyvdly lihwavpsqg
      121 eyveawkali alqerglvra igvsnfpaqq laevieatgv vpaihqielh pyfqqrelra
      181 ihaehgilte awgplgqgks dllenpavta iaeahgatpa qvvlawhlah givtipksvt
      241 psrivenlaa aeleltadev aaidaldred grggtdpatk
//
LOCUS       WP_010552375             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FMN-dependent NADH-azoreductase [Brachybacterium].
ACCESSION   WP_010552375
VERSION     WP_010552375.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..205
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22724
     Region          1..205
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mralivrahp ldpsksrsmt madafveelt ahrpdtvvdd vrlyetavpe idldmmtgwe
       61 rlragehfsh ltgaqqnkla lfdqytkqfq sadlvvianp lwnlsvptrl kawidtvcra
      121 gvtfrytaeg eaeglvtdkt vvhlqasggh fgqqdpasly iagmfqflgc tthtlaaegm
      181 dhepdraeei meaallrvre larsl
//
LOCUS       WP_010552407             549 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010552407
VERSION     WP_010552407.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..549
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=59185
     Region          14..275
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(14,38..39,67,73,78..81,94)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,76,93..96,100,102,138,140,
                     142..143,145,155..156,159,176..178)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,76,93..96,100,140,142..143,
                     145,155..156)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(25,100,102,138,140,142,159,176..178)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(155..163,172..175,176..178)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mssrppsapp rlagyeyekl lgsggfadvf lyrqarpqrr vaikvllstv ldesvrhqfd
       61 seanvmaqms thpsivtihq aevsgdhrpy ivmeycsrpn ygvrfrkeri tvaealrvgv
      121 qiagavetah ragilhrdik panilvtdyn rpaltdfgis iaagqgedve dsqgmsipws
      181 ppeffadppr advrsdvfsl aasvysllag qtpferrgqr ntatdliqri aseplpalnr
      241 pdvppelnra lsiamakdpa grydtalafg ralqqvelsl slpvtqmdvl ddrgaapahd
      301 geddelveht rirkvatvdp etgtspggrr rmdpyagvap algaapaaag paswsgasap
      361 saadasestm lrpagapagp vgraplaseh hepeperprt pawpfvtlaa vlvillgvga
      421 tlgvrhffve epeeapstlv napvdpeeap gaprslelqv iapeqeggrt grvkvawelp
      481 enfsqedhfi vqwqdlpany dryavqhevh grnsvvieip pqlaercltv rtvnpngqss
      541 eaekkclng
//
LOCUS       WP_010552494             193 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein, partial [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010552494
VERSION     WP_010552494.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..>193
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          6..133
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(11,13,67..68,71)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            13
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(66,114..115,117..118,122)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(72,77..78,110,113..114,117..118,121,124)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95..97,110..111,114..115,118,122,125,129)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95,115,118,122,125,129)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(123,129..130)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          146..187
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(147..149,181..182,184..186)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mpttqrvayv rvssagqnld rqleaigavd ktyreyqsaa aaserpqlre aikyvregdt
       61 lvvasidrla rslrdmlaim eeleqkgvtv efctqgltvr pgggdlttrl ilhiitavaq
      121 seremirerq aegiaiakkt pgkypgrrrr lnseqigevr navasgipka qvartykisr
      181 ntlyrylqqp asl
//
LOCUS       WP_010552553             217 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MOSC domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010552553
VERSION     WP_010552553.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..217
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24343
     Region          1..172
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mkiistnisk iktlihngke vktgifktpt nepvviekln iigdeqadlv nhggvdkavy
       61 afshnhyeyw qktlenenls sgifgenfti sdldeanihi gdhirigtal levsqprvpc
      121 fklaialnnk nslklftqhy ctgvyfrvle qgvaktgdsv viekkashdi svkklfqaff
      181 dkkyvgyedi llealtlpel avewqeklkk klaikse
//
LOCUS       WP_010552566             305 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudoalteromonas arctica].
ACCESSION   WP_010552566
VERSION     WP_010552566.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32904
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtiigikti iavvetgsft aagdrlglsk alvskyvgiv eqdlgvrlfn rstrrisite
       61 agqsyyasvv pviesyseml dnlsgqtala sgklrvsapv sfgesnlapl mpellsrypd
      121 lsidlvlsdk tidlleegvd lairigsvsd snliarqits yplilcasad yiqrfgapas
      181 vdeleqhatv idsnfkigrh wplvspsgea ltasvnsrvs vnnpqavkev vvagggigli
      241 peivvrddia sgklvqvmqg yktfefglfa iyphrkfvaq kvtsfihflf ekfeakpktk
      301 kpkis
//
LOCUS       WP_010552637             764 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidase U32 family protein [Pseudoalteromonas arctica].
ACCESSION   WP_010552637
VERSION     WP_010552637.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..764
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=85741
     Region          3..292
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
ORIGIN      
        1 msrkiellap ggdvnavkaa ivaganavyc gldtfnarnr asnlsfdeln galrlaheyg
       61 ceifltlnvv ilehemgalf kllnqlvntt ldgiivqdlg lfnivkkhfp tlhihastql
      121 tthnesqvef larigatrvn lsrelnltei kiltdvahkc dvltevfvhg alciafsgqc
      181 ysssvsvgns gnrgrcsqac rdeyeptamg nkhplnlkdn sayfdlpelv aagvdslkve
      241 grikganyvh tvidswrkqi dtfvqtgnli eddsslykvf nrnftnkflt gdmtknmftd
      301 nprdhsfdha neknnaisvv qiydaqqels tqkseidslv kkkiefldis kreltleftg
      361 qlnqpftvni iiedknditl snknekeplr fevqsqmpmq tadksvvdia aidkrfksfs
      421 nanfeiknmd ysnlgnnlsi pfkelarikk qvafllnegk dvlapvelpk lvnhekadkn
      481 kttlsilisd ikdvhlcdlt dgdvyfklpe sfrtdndkyi nvflehpqli pwfpavligk
      541 dfeeavrlle vvkpkliisn ntgvafkavq mgldwiagpl lnttnsyall tlqedlnakg
      601 afisneinkp qmrnikrpnn fkmmysiyhp ilmmtsrqcf fqqtvgckkp ridascmlsc
      661 kkettvtnvk gisfaidkqk ggypsiynhe qflnmdivtd yadkfdefmi dltdigsgdk
      721 ekldkavlla hfqdlisgkt qaadqlnhmv kvktrqqyve glns
//
LOCUS       WP_010552643             155 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Pseudoalteromonas arctica].
ACCESSION   WP_010552643
VERSION     WP_010552643.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..155
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17465
     Region          42..151
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mfgiyaalsp mygeqphiig salpkyqthc ckfnhqrttr ptiihchcsl crknsgtafa
       61 tngfvniddf titkgqalls eysfkvgrtr yfckccgspv yssnnddksr irirlgifds
      121 diteqvlshn fvtskanwek letslpcyek hepgr
//
LOCUS       WP_010552777             293 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Pseudoalteromonas].
ACCESSION   WP_010552777
VERSION     WP_010552777.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..293
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32565
     Region          40..284
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 maikitkhyf inlslavvif aigilairyy nhyvsaytdv tinssvlnes rkvfirlpan
       61 ynpkkaypli iktdgnfnld twdkaltkqa ksekgdkail vsipnlfftd trnrdlvppy
      121 arqdvntqar pegetliepn geadkflafi etelfpylsa kyklsnnrvl sgfsaggsfv
      181 lytlhtrpel fngyfafspa awyddmtvvn nveaflttqa nkvkaptyly lsvggaehpl
      241 mlkafnnles alkanpnnnl awqsainega ehsdnpplsv skalagysaf ikk
//
LOCUS       WP_010552787             241 aa            linear   BCT 01-JAN-2025
DEFINITION  SIMPL domain-containing protein [Pseudoalteromonas arctica].
ACCESSION   WP_010552787
VERSION     WP_010552787.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..241
                     /product="SIMPL domain-containing protein"
                     /note="The SIMPL domain is named for its presence in mouse
                     protein SIMPL (signalling molecule that associates with
                     mouse pelle-like kinase). Bacterial member BP26, from
                     Brucella, was shown to assemble into a channel-like
                     structure, while YggE from E. coli has been associated
                     with resistance to oxidative stress.; The SIMPL domain is
                     named for its presence in mouse protein SIMPL (signalling
                     molecule that associates with mouse pelle-like kinase).
                     Bacterial member BP26, from Brucella, was shown to
                     assemble into a channel-like structure, while YggE from E.
                     coli has been associated with resistance to oxidative
                     stress."
                     /calculated_mol_wt=26259
     Region          1..241
                     /region_name="YggE"
                     /note="Uncharacterized conserved protein YggE, contains
                     kinase-interacting SIMPL domain [Function unknown];
                     COG2968"
                     /db_xref="CDD:442208"
ORIGIN      
        1 mktltlvlgs alalnvlsfd alaaatpdap hiyvkgeatl ttmpdyvqls vgitevdkdl
       61 iaaknktdlt iakaiklvke igvkegdina gqisinrdsq ynrttgnqef kgfkvsrtlt
      121 vklsdinkyp ellqslvnng ineinqtqfl vsnynelhkk aqklaikdar daakefsedy
      181 gvdlkglysa slsplnvqsq pymraekvmm adsapsnyvp dayhageikv tassyavyyi
      241 d
//
LOCUS       WP_010552794             432 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CpaF family protein [Pseudoalteromonas].
ACCESSION   WP_010552794
VERSION     WP_010552794.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..432
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47362
     Region          19..380
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mfnlsskhee vqtslstfee lkkllhdavi eeyeqeptal lssnvlekis alcseipqfn
       61 qssfnqhqqe qvvqavfdei qglgpiaqfm lddqvsdili ndtqdiwidk qgkllctask
      121 fdderhlrrf vdrlldgcgr qvnalmpivd gklkdgsrvh iivppactsa aivsirkfnh
      181 kkinddflvn nhfldknils flksavktgv nilvcgnaga gktsllnvla nsinpnervv
      241 tieesaelnl hhnhvvqlea hdtnsdgkga vslrdlvkaa lrmradriiv gevrsgevid
      301 mlqamncghq gsmttihans andavirlst lvqlhnaqls dthtsslias siqlivhvsr
      361 stngtrtlks igeikrvngg ahfsplysin eaepvqseli dnssviefmk gqganaqelk
      421 allhnnpean nd
//
LOCUS       WP_010552795             291 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Pseudoalteromonas
            arctica].
ACCESSION   WP_010552795
VERSION     WP_010552795.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..291
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32536
     Region          90..284
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mtkldyllai aavitfvlaa svlvslyakn ksnqsakkvn ileekdvltl slrvlglnis
       61 nawfismacs lsssswflak lyypeastsa fiisivvfvt cfiavidlah yklakfehhf
      121 lefietvqsc lstglslqqs mqfadehadp yikkqstlli qrmsmgsdae tsfapliery
      181 ncetvrlfah siithtqsqc dltdmlksvc nmmslrtldr qqlkaklsgt kyaavfsgfl
      241 pyaliplfsy tdptwfepll ndpngiafit vallcqlfgf lwlrlslrvt l
//
LOCUS       WP_010552799             141 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator [Pseudoalteromonas].
ACCESSION   WP_010552799
VERSION     WP_010552799.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..141
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=15983
     Region          37..141
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mkntienmae viefkvtpin ktkrlllvdd dllieivirk mlneenilid fassaieall
       61 mvsqniydii lmdivmpqft gtdamlkirk hadasatkii ahtfsenens dnkyvklgfn
      121 glllkpvkqs vlieniryfl e
//
LOCUS       WP_010552801             333 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudoalteromonas arctica].
ACCESSION   WP_010552801
VERSION     WP_010552801.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..333
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36144
     Region          1..326
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mgsitlkqvt knfdevnvik pldleikdge fivfvgpsgc gkstllrmia gledttsgni
       61 eidgidatkt ppakrglamv fqsyalyphm tvrnniafpl krakvspaei eskianaaki
      121 lnltdyldrk pgqlsggqrq rvaigraivr qpsaflfdep lsnldaslrv nmrleiselh
      181 kslattmiyv thdqveamtm adriavfnag iieqvgtple lyknpvnkfv agfigspkmn
      241 fidapqneda nvscigirpe hitlsteqgt wtgtvgvieh lgsesflhin iegkgtvtvk
      301 adgdcplkyg dsiylsapad kvlkfdnngl tir
//
LOCUS       WP_010552823             254 aa            linear   BCT 01-JAN-2025
DEFINITION  spermidine synthase [Pseudoalteromonas arctica].
ACCESSION   WP_010552823
VERSION     WP_010552823.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..254
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28314
     Region          29..213
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mdikgtcias tidehgpvyv yqtkknlils fdgkiyqsci klnninglsl aytqammaal
       61 ffipnlktam imglgagsia kslyhafpal tihtveyrka vadmaikyfe vpvserlfih
      121 iddaanymkn tqiktdvifs dlyssegmes dqvqssylrd cknaltfdgv lvlnichtkv
      181 gqreafdqll ekefagkils fiieggnkiv fafnnkmpal sedellakah tlqklinvpm
      241 tryagllfnq kwlv
//
LOCUS       WP_010552835             380 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Pseudoalteromonas
            arctica].
ACCESSION   WP_010552835
VERSION     WP_010552835.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..380
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41347
     Region          27..364
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 msaltllnsa depvvfetat aengsligli tlnapkalna lnfemiklle pqlrawqddd
       61 aiamvllkga gdkafcaggd vvslhhamaq gkptslveef ftleykldyl ihtfdkpilv
      121 wgngivmggg lglmagashr vvtetsriam peqtiglypd vggsyflhkm pqsvglflgl
      181 tsasincdda rfvsladhfi dstkydamla qilaakwgkt aslnherltk lltdldnqsa
      241 rmpkgnikan lktiqklgef ttlqeqvdyi lglttddkwl qraqkslkhg cplscalvse
      301 qlktsqgksl lacfkmelgm svragevgef qegvrallid kdgapnwqyk tlsdvpqtii
      361 dsffanrfge nhplnelavk
//
LOCUS       WP_010552877             414 aa            linear   BCT 01-JAN-2025
DEFINITION  AAA family ATPase [Pseudoalteromonas arctica].
ACCESSION   WP_010552877
VERSION     WP_010552877.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 414)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..414
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46737
     Region          18..331
                     /region_name="COG3950"
                     /note="Predicted ATP-binding protein involved in virulence
                     [General function prediction only]"
                     /db_xref="CDD:443150"
ORIGIN      
        1 mkrhidrikg vvpnthkeid ialngrnlii tgsngsgktc llkeldrkvd lligkkqlad
       61 kstieryvqm fkedvhssqn gttkndrakn nlesqiaqle kinsgldiaf idhldfsskl
      121 dngtavlsff eahrrsnits antakgieie rtsilnntpn dtrrnqignn leqhlvnlrn
      181 rrslaitedn dqllasnieh wfsafeeslk ylledetakl sfnsdtlkft iiqankpayt
      241 fqsissgyqa ifdiyadllm rteyfeitae eltglvlide idahlhvslq rlvlpfftrs
      301 fpnlqfivtt hspfvlmsat dtvifdlthn eqieedisly shtavmegll gtkatsthld
      361 nyinevasii nmnkvdyerl ellvgklknv ensldskska fflkglnila ekel
//
LOCUS       WP_010552904             388 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aldo/keto reductase [Pseudoalteromonas].
ACCESSION   WP_010552904
VERSION     WP_010552904.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..388
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42217
     Region          84..374
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(104,109,135,192..193,235..236,257,286..292,329,
                     346..349,354,357..358)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(104,109,135,192)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mvsrrnfika gaalslgsif sasalaeqlk vkmsngsvmq tkgaidksaa lptndvtnak
       61 hyrpesrmgl gglaagngfn tissdaeilt mlnaawdsgi rhfdtspfyg lslserrfgd
      121 llrnkkredy vlsskvgrll tpsaeplens whwadhspfh ykydysasgt rrsiedtlhr
      181 igvasldivy ihdlspqnsd mgddwlkyfd qaakgaipel tkmrdegiik gwgfgvntph
      241 aiykaldmsd pdicllalqy sildhkqald ktfpmldkrg vsavigapln ggflagrnrf
      301 nyspkipgpm qqkfnaisdi askhgidikt aalqfaeaps tvssiipgar tadqikanva
      361 smkvtipsef wselkskqli aenapipa
//
LOCUS       WP_010552929             175 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Pseudoalteromonas].
ACCESSION   WP_010552929
VERSION     WP_010552929.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..175
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19158
     Region          11..171
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mvllidsina irdfldtggq vllvigvlif amwllilerf iyffngfrsy khalkanwin
       61 raerdswnae qireamisra gmrlntnlsl invmvalcpl lgllgtvtgm ievfdvmait
      121 gtgsarsmas gvskatiptm agmvgalsgv fastylqrka krevellqds mvldh
//
LOCUS       WP_010552930             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Pseudoalteromonas].
ACCESSION   WP_010552930
VERSION     WP_010552930.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..455
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49431
     Region          271..448
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mklftqmtki alfaaslsit gasiaaepmn ldsllktlen gqsaqseqnk qreqeftarq
       61 neqvqtlknt qakrnqmlve serletqfee nevklanltd tlskrmgslk elfgvlqqva
      121 gdssnkfats iissqiagrs tfmddlaqkm gstsklasie diekvwfelq remteqgkvs
      181 rfnasviveg gtkaqqevvr vgafnlisng kylefnsstn slseltrqpv srftataeel
      241 qstksgvvqf aldptggsil gllvqapdtq ervhqggtvg yvilgvgvia llislerffs
      301 llimggkirr qlkdsvardd nplgrvmkvk dqfpsvshdt lelklseail rempkvtrnl
      361 tlikiisvva pllgllgtvt gmintfqait lfgtgdpklm aggisqalvt tvlglvvaip
      421 tvflytllnt raknilltiq eqsagiiaer sekga
//
LOCUS       WP_010552940             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GbsR/MarR family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010552940
VERSION     WP_010552940.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..181
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20571
     Region          3..159
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mslseknfaf vmhcgemgsr wgfnrtigqm cglliitknp mtaneiadal sisrgnvsmg
       61 ikelqswqli kvqhipgdrk eyyapagdiw dmanrvfeer kkreieptlt llrdnlldea
      121 snddelyaqk qmgeihnlle tvtkwsselq rltpeqlnkl mklgsgigkv idlkdkifkk
      181 e
//
LOCUS       WP_010552966             511 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Pseudoalteromonas arctica].
ACCESSION   WP_010552966
VERSION     WP_010552966.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 511)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..511
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57703
     Region          <198..>350
                     /region_name="PHA03246"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223020"
     Region          <341..508
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 msersnptdk klkqaidarm avesarkhqv dilcdfaakl slsckgldie ldnrlakfrs
       61 alnkgmsfed lsplvsetlt llknqesvqq tqqrdlfnnv qnagkqlqkt kgltddtrrt
      121 lrnlldnein nvhsvhgyip lldqlisfyh qalitkqdpv idkklptvqs yanklleltn
      181 elvledeatq qikhiknsit asktitalld aaisiidvvv kniskerksa qsflvslnqt
      241 ledlhnsiis tskhsesmev efdslnksie lkiknlneqt qkatsisslk elvdnelksl
      301 sedfiakekl erkdremlss sfneinnrig tlegklttyk krlneqrfks lldgltklpn
      361 raafderydh emhlfnvqps dvtlavidvd hfksindrfg htagditlqv iskalqksvr
      421 ksdfiarygg eefvllmpgv slenatlpld kvrkviknip fkfrekqiei tisvgatqfk
      481 kgdtllkafd raddalyeak nsgrdrlcts k
//
LOCUS       WP_010552991            1022 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudoalteromonas
            arctica].
ACCESSION   WP_010552991
VERSION     WP_010552991.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1022)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1022)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1022
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..1022
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113204
     Region          1..1016
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msfaqlsiek kviswmftll lliggsvsyf dlgqledpef tlkkamvitm ypgaspqqve
       61 eevtfpiena iqqlpyvdyv tsissngksq isvemksnyr keqlrqiwde mrrkindlsp
      121 slpsgvypst ilddfadvyg vmysvtgdgy sydelkdyvd flkrelvlvk gvskvtvagq
      181 qqaqvmvevs trklaqlgia pshifqllqs qntvsnagki rvgdesirlh ptgefkdvke
      241 letllisksg aneliylgdv akvyreyaev pnniirynsq qalligvsfm sgvnvvdvgk
      301 nidehlasle yqrphgihin svynqpqevq ksvdgfiisl leaiaivivv lllfmglksg
      361 iliggilllt vlgtfifmkl faidlqrisl galiialgml vdnaivvteg ilinlkrgqt
      421 klkaavnive qtkwpllgat viavtafapi glssdasgef agslfwvlfi slllswitai
      481 tltpffanlm fkenefknee gqededpykg fifngykail dlalhfrktt lilmvvllct
      541 avigfgsvkq sffpasntpm fyvdywqeqg sdirstlegv kkleeflqke dlveevtstt
      601 gqgaprfmlt yapeksypay gqliirvadr eavatvmqtv rdyssnhals aqlkikpmei
      661 gpstdakiea rfsgpdpvil rqlaataeel igsddgayni rddwrartkm irpqfneqka
      721 rrlgisksdl dnvlltslsg kqvgvyrdgt qllpiiarsp anerlnvesv hdlqiyspvl
      781 gvfvpvtqvv defdvqweds limrrdrkrt itvmadhnvl gdetpaklfa rirgpienme
      841 lprgyqlewg gefessskaq kaifgslplg ylamfavtvl lfnslkqplv iwatvplaii
      901 gvsagllamn apfsfmgllg llslsgmlik ngivlvdqin lelregkspy eavfdsgvsr
      961 vrpvamaait tilgmipllf dvffqsmavt imfglgfati ltlivvpvly tvifridyep
     1021 rk
//
LOCUS       WP_010553102             156 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Pseudoalteromonas].
ACCESSION   WP_010553102
VERSION     WP_010553102.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..156
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17507
     Region          1..140
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mklngachcg kvvftvnskh pypynlcycs icrktagsgg fvinlnaqfs tlevtgrehi
       61 tiyhakigdk ispaerhfck hcsanlwlyd arwpeqvhpf agaidselpi pperthlmlg
      121 skanwvnapi negdkqfeey pdesiaawhk rlnlek
//
LOCUS       WP_010553103             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Pseudoalteromonas].
ACCESSION   WP_010553103
VERSION     WP_010553103.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..157
                     /product="VOC family protein"
                     /calculated_mol_wt=17178
     Region          11..134
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(11..16,18,33,47..48,55..56,58..60,79..81,83..88,94,
                     115,120,128..131)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 mavsaipkgf hsvtpylimn daqkaidfyc dafsaehvmq mplpdggiah aeiiigdshi
       61 mlsdngseeh lkspkelggt alslmlyved vdtvfkkaie lgateirpvh dqfygdrtgt
      121 lqdpfghiwi igthkedvsd eelnnrigni tnqeqda
//
LOCUS       WP_010553122             686 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas arctica].
ACCESSION   WP_010553122
VERSION     WP_010553122.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..686
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76213
     Region          26..671
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkpyflplil pfshtafadn qnndaietit ttasrieals tplplsistl tqaqlnsiap
       61 thieealqrv aganiqrgng qeylpalrsq vlsgagacgg iltledgipl raagfcnine
      121 lfeahsemaq rievlkgpgs alygsnavhg vinvitpdtt qggglvgldy gsygytrykl
      181 ragqdygnsg iginasvtdd sgyrddesve qqkvnirhry snnnllltsg ltytnldqqt
      241 agfitgfesy knedlaqknf dpdafrkars frawsnatwq lnnddvlstt vyfrdqsmdf
      301 fkhflpgtpl etnsqtgfgv qslyqhnlqs nvkvnlgldg eytqadftqs qnkptqgsaf
      361 lvatvpqgkh ydydvnatly apfasvdwql nkwlltagvr yehmqydytn nmlagrtkdd
      421 gtecgfggcr ysrpasakns fsnlspklgv syqyntnntl yanfsrgyra pqaaelyqlq
      481 reqttanlsa eiannaelgi kgiyeklryg vsvyamskhn tiyrdsdfft vnngssrhrg
      541 ieleldyqlt kslalnfagt hakhtytnnq ilnglningn didtaprnia nldltwqals
      601 ntqfalqwhr vgnyytdpen lnkyqghdvl slraqwqvtn nlevlariin ltneayaera
      661 dytsftgdry fpgkprnaml satytw
//
LOCUS       WP_010553116             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudoalteromonas arctica].
ACCESSION   WP_010553116
VERSION     WP_010553116.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33357
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..287
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,222,239,266)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllksiqvf eqvaqqqsfs raaeslnlvp savsrqinel ekwldirlin rttrslslte
       61 dgkayllkls diraqvtelr rsktqqqqik glikitapim igqymlpval aefkelhqdv
      121 dlaislmnrk velveegfdl airvghlnds tmvarnignm rfktvasphy inthgmpstp
      181 kdlknhqcli ntavtnakrw sylidgkstv ikvagsfevn dsqslkafai anqgiaqlps
      241 fyvdaaiqsg elieilsdyv psplpvnlly psqrllsptv ralvdylvpf lnqqkqkw
//
LOCUS       WP_010553164             289 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Pseudoalteromonas
            arctica].
ACCESSION   WP_010553164
VERSION     WP_010553164.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..289
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=32136
     Region          183..281
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mtfyllalsi icvfpyckis imrhplwhyl lalsvvsayf qgyinlyall ltglyvvlyy
       61 calntkqaii ratlstvfiv sslalalhwv pgfnnlpivi neritsdaia ftlyanfdka
      121 maglflcayf ysnkktlkad snkadplnvk qpiliiiatv laaltaalml glvsfnpkvp
      181 gfwlafiain llftcvaeea lfrgllqtkl skiitptrla ilapvitagi falahfaggi
      241 nyvlvsfiag lgygyvfykt qrlewailch wlvnvchffl ftypmlnki
//
LOCUS       WP_010553167             106 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010553167
VERSION     WP_010553167.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..106
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11675
     Region          6..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mqlnpktike lrqqfnwtqq qladacdvsl rtvqrvekeg aaskettmal cavfevrqge
       61 liklddleed etvkaqstqk fivaiaissl isftlgvgcm llitsl
//
LOCUS       WP_010553265             232 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Pseudoalteromonas
            arctica].
ACCESSION   WP_010553265
VERSION     WP_010553265.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..232
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25601
     Region          3..228
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 msgfvfkqfk vehdhcamkv stdgillgaw anlsgaksll digtgtglla lmckqrsnel
       61 ditaveides aytqalqnia nspwpaisik hqtiqrfnsa vkfdvvisnp pyfnhslkgd
      121 nvarntarht dglsfeelin afkrlshggs rfslilpsve svlfielatq nglylnthcq
      181 vkatpnkdis rslmtfsyvk sdiessilci rnldntytad yialckafyl km
//
LOCUS       WP_010553266             106 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010553266
VERSION     WP_010553266.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..106
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11443
     Region          42..105
                     /region_name="BON"
                     /note="BON domain; pfam04972"
                     /db_xref="CDD:428229"
ORIGIN      
        1 mnrfkltial vsfcclflla catkvsaatn mavvssvatq pnlqqaitnt lrtnpnlals
       61 dirvqvknge vdlygeaqtg fqralaqkfl enmdgvkiir nkisvi
//
LOCUS       WP_010553301             317 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ion transporter [Pseudoalteromonas].
ACCESSION   WP_010553301
VERSION     WP_010553301.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..317
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35815
     Region          27..255
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mnephtlrqk maclfegtgq yhraghildi alisliminv vaiviesips vaeqyynefl
       61 vleivsvaif aieylarlwa cvdktqyaam egshtkrrlr yffsplaivd liailpslmm
      121 flfpldlrfl rvlrllrvfk ltrysramql llkafndegs slmaaffima vvlilascgi
      181 yliehdiqpd kfgsipaamw wamatlttvg ygdvvpitpl gkffggvitl lsmgmvaipt
      241 gllassfseq irkrrqffed avheqiqdgt lndtqqehle elryklglsk leankaiktq
      301 lnehnshlfc rhcgkrp
//
LOCUS       WP_010553313             277 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Pseudoalteromonas arctica].
ACCESSION   WP_010553313
VERSION     WP_010553313.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..277
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30188
     Region          10..273
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mknlityqql qaqlnnpalv ifdagmlrpg vlgayspqam lpsakrfdik neladrsnpl
       61 psmvcseqqf thvmqnagvn ndsfivvyed gglfsaaraw wmfkamghhn vkvlsgglkk
      121 wlesdyatqq gyskasgkgd ftanynsayf insqqvvdvi depstallda raykrftgee
      181 seprkgmrsg hipnsrslpf mdllnkgeak plteikaifn dvvgdaqqlq fscgsgitac
      241 vlalfatecg ysnlsvfdgs wsewgasdsl piatgek
//
LOCUS       WP_010553314             340 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 9 protein
            [Pseudoalteromonas].
ACCESSION   WP_010553314
VERSION     WP_010553314.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..340
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38051
     Region          13..335
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mtlpinkkit gtilvihpkf igdavnntta isllrelypn nkiivlvnpl lapifkrddr
       61 fnltvmider hdkkqkksif yqakkikehn vqlaiimksa fsdallctla nikykigykk
      121 ngrswllshk ykinnnhhyi nrycrlvnep hnqpfttsps tyvfskrskl ikadrnkpti
      181 avyygglvkk yrhypssqaf qslalinqtl pshfvlvgdn qeitdnakis tdliensidf
      241 qdltgkttlt elvdiiasvd llitidsgam hiaaatktaf vavvglgtsp wsivepkcen
      301 kislvangss lndaeiikei spekiveaaf sllknkitfl
//
LOCUS       WP_010553320             417 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudoalteromonas arctica].
ACCESSION   WP_010553320
VERSION     WP_010553320.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 417)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..417
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45758
     Region          19..>190
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          139..404
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 miitklayks llnrrasvll tlftiaisvm lllsiegvri dakssfsnti sgtdlivgar
       61 tgdiqlllss vfrightnng vswksyeyit sqrgvkwsip islgdshkgq avlgttldyf
      121 shyrfakkqn ltfnkghpfa ainevvlgse vanklgykln dsivishgmg ntsfhhhddn
      181 pfkvvgilnp tgtpvdktlh iplaaidlih ggkasleheh ehehdehnnl vghpkqitaf
      241 lmgfksplyt lqirrninqy kpeallgimp tvtlkelwem laivekilll fsavvvlisl
      301 lgmlttllan lsqrrrelai lrsvgarpwh lftlisiesl lttllgclvg svlyylvifs
      361 asgylqshag isvnitilsy yelgligvim aagfiiglip atrayfysls dgmsika
//
LOCUS       WP_010553387             419 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Pseudoalteromonas].
ACCESSION   WP_010553387
VERSION     WP_010553387.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18645163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..419
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47703
     Region          54..358
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          79..113
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          122..145
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          157..185
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(158,161..162,165..166,168,194,197..198,201,203..204,
                     227,230..231,234..235,238)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          192..221
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          226..254
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(305..306,308,331,334..335,338..339,341..342,366,
                     369..370,373..374,377)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          328..>393
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          329..359
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          365..393
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrnfskvtal ailmsvsgat lsasvlaapd yakieerkka ktkimgertg kkvikafdly
       61 neekvdeaiv llreiepsnd fdkatvnryl gsmyaqkeky deaikyskqa vapdvlnfad
      121 qeqtlkllgd lyagtekyqe akkayvtwmd ftgeedptvy triaqanyql eqfrdvfepa
      181 dkaiklqkep nkgpyqlklg ayfelkdyan mvkigeeivr vwpddkkawv slgkyylqte
      241 dyqkglatme vaykngyfen eveykvlsnf yslneipfra avtlekavks ekvkrtkqnv
      301 saiasnyhrs kdlekaakyy eeaakfddda elyrkagsll lqsekfsaav vrlnkalelg
      361 sdkkgtiysd laeayyyqgk ykqayaaitk amddprtrkf akgwstyikd kaarngvki
//
LOCUS       WP_010553425             296 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Pseudoalteromonas arctica].
ACCESSION   WP_010553425
VERSION     WP_010553425.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..296
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32611
     Region          10..295
                     /region_name="hydrolase_YghX"
                     /note="YghX family hydrolase; NF041440"
                     /db_xref="CDD:469331"
ORIGIN      
        1 mntspsdhip qeafdwydey ahglmdrrtf mkklgglaal gfsmavltsa llpnyalaeq
       61 vsfndddika tyeefdspdg hgkgkgylat pkniegklpv vlvvhenrgl npyvkdvarr
      121 lakvgfiafa pdalfplggy pgnddegram qktmdrakiq ndfvaaahfl kshansngkl
      181 gavgfcfggy ivnylaavds nlisagvpfy gtpaseslrk nikaplmiql geldkrvnas
      241 wpqyeqdlka nnveytmhmy kganhgfhnd stgrydkdna elawqrtvef fnnkls
//
LOCUS       WP_010553501             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudoalteromonas].
ACCESSION   WP_010553501
VERSION     WP_010553501.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..389
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40890
     Region          16..372
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,141,
                     144..145,148,215,218..219,222..224,227,251,255,304..305,
                     309,313,329,332..333,336..337,340)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 maelaatsts nnplapvigl sffaiasgfl msliplslpa fkldenlapw lasifyfgll
       61 igattieriv vkighrfafi lflslliasv laqlalpntv nwliarfvag favagvfvvv
      121 eswllmtnta ksrakrlgly mtslyggsav gqlaigplgt egstpylfva sllflailap
      181 llitkgqpek qhleklplke iktlshpaml gclasglllg piyglmpvyi saqtdqaqyt
      241 gtlmaviilg gmvvqplvsy lstrleksll mgmfclvgaa gavgilqant laglivsyli
      301 lgacsfalyp iaitlacdsl pmakivsate vmllsysigs vfgpmlaanl sdapngivfy
      361 lagclittci ymfiksikni ragktpvag
//
LOCUS       WP_010553559             157 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Pseudoalteromonas arctica].
ACCESSION   WP_010553559
VERSION     WP_010553559.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..157
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=18380
     Region          10..153
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mqqklerntv iiyssarkng nttahvnsfa eqndvrvicl ddykiapycy dknyknddfy
       61 alfeavlqyd hwvfaspvyw ynttvqmksf idritdymdd etlkpklral rnkdfsllsn
      121 assleapdif vemfkrtfsy lgmqfinhhh kntqsaa
//
LOCUS       WP_010553299             238 aa            linear   BCT 01-JAN-2025
DEFINITION  SIMPL domain-containing protein [Pseudoalteromonas arctica].
ACCESSION   WP_010553299
VERSION     WP_010553299.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..238
                     /product="SIMPL domain-containing protein"
                     /note="The SIMPL domain is named for its presence in mouse
                     protein SIMPL (signalling molecule that associates with
                     mouse pelle-like kinase). Bacterial member BP26, from
                     Brucella, was shown to assemble into a channel-like
                     structure, while YggE from E. coli has been associated
                     with resistance to oxidative stress.; The SIMPL domain is
                     named for its presence in mouse protein SIMPL (signalling
                     molecule that associates with mouse pelle-like kinase).
                     Bacterial member BP26, from Brucella, was shown to
                     assemble into a channel-like structure, while YggE from E.
                     coli has been associated with resistance to oxidative
                     stress."
                     /calculated_mol_wt=26532
     Region          1..237
                     /region_name="SIMPL"
                     /note="Outer membrane channel-forming protein BP26/OMP28,
                     SIMPL family [Cell wall/membrane/envelope biogenesis];
                     COG2859"
                     /db_xref="CDD:442106"
ORIGIN      
        1 mnktpgfyiv iaaiclsigl islgfilkst alsvkemert vqvkglaere viadtviwpl
       61 qfsdadnnle klvsrvekkn davtaflklh gfdddeitig sqsvidkqar eysnenqqfr
      121 yivrsnvivy sdapdkvqna lskvsqlakq diaivqdsye tkveyiftgl ndvkpamvqe
      181 atekarevan kfakdsnskl gkiktarqgq fsisnrdsnt pqiknirvvt sveyylnd
//
LOCUS       WP_010553607             172 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010553607
VERSION     WP_010553607.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..172
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18700
     Region          3..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mskkeallka aenkvrlggy snfsfrelas evgiksasvh yhfptkadlg aelahqytns
       61 flaalgepse lkasgknpid vytqlfrsal vtdrkmclcg llgaesdslp dkvrlevkrf
      121 fnqnltwlsa ahlangdlnp tkaaiqtvsl legammiskt lddnsyfela tq
//
LOCUS       WP_010553608             206 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Pseudoalteromonas
            arctica].
ACCESSION   WP_010553608
VERSION     WP_010553608.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..206
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22412
     Region          1..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkiydvenfp nplrvriala eknatanvef vavdllngeh rteaflaknp lagvpvleld
       61 dgtfisesta iteyidtafe gpslmgetak eravinmmqk raesmvldav atyfhhatdg
      121 lgpeletyqn vawgekqgek arqgfsyfnd vlaqsafvag eqfsiaditl yaglvfagfa
      181 qiaipnelth lvawqekvak rpsvaa
//
LOCUS       WP_010553612             796 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas arctica].
ACCESSION   WP_010553612
VERSION     WP_010553612.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..796
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86112
     Region          7..795
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtthntplyl isalalavsq gvhaqetdqa tpeasqnkgl etivvtgvpr rttimassvs
       61 vssvsleqvq vstprstaea friipgirae stggegnani avrglpvasg gakflqlqed
      121 glpvmqygdi afgnsdifmr ldntvqties irggsastaa snapggiinf iskngenesg
      181 svsttlgldy dsvrtdfeyg tyltdsvrfh vggfvrqgeg pretgytsnk ggqikanltk
      241 dfengyvrly ykhlddksvg ylpmpmysng dsiagfdaqs dtphsalftk tvrlngenqi
      301 ssgdirdgmn pkvdsvgfea vfdldndwri enrfrkssis gnfnspfteq vgsatsiaes
      361 iggagatlsn antgeafndg lamkmvtfdv tmndfgsivn dfkltksfdd dtsltfgyya
      421 stqniamswl wnsyvmelkg dnaallnvtg adgtelseng lyaysafgnc cqrdydteyd
      481 trapyvafst klgdvsidas arydsgearg tyagavtstv dmnrdgeisi peqnvagidt
      541 anaspvnydw nyssysigan yqidpslatf ariskggran adrllfgkvr adgsvakeda
      601 vdevnqfefg vkkrfdslsv fataffaete eqnfeatsqt ffdreyeakg ieiestyfid
      661 awdfrgnltw tdaeiakdal npdvvgntpr rqadliyslm arynyekgaa gvsfigttda
      721 yaqdnndlqf dgytqvngfv sydlsenlni alnvnnlfdt vgiteaeegs vpenniirar
      781 aingrttsvt lkyafn
//
LOCUS       WP_010553633             584 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudoalteromonas arctica].
ACCESSION   WP_010553633
VERSION     WP_010553633.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 584)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..584
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63403
     Region          22..583
                     /region_name="YnjC"
                     /note="ABC-type uncharacterized transport system YnjBCD,
                     permease component [General function prediction only];
                     COG4135"
                     /db_xref="CDD:443310"
ORIGIN      
        1 mnvvsnkvat shgpharksh dmfskivkls prfllvllil pvlgglisvl lpafgyapal
       61 dqttfglqgf tmlwqtpglv nmamlsigtg listllafii tlmilaaffn spwlnriqrl
      121 lspilvipha aaaiavgfli apsgmisrii spwlsgwela pnglfphdsf gisiilgltl
      181 kelpflllma lgvlaqpelg kklrqqhkva lnlgycpmta ffkvilpsly pllrlpilav
      241 layasasvem plilgpntpp tlavaimhwf ndvdlnlrik asagallqla ltggllalwl
      301 ggekaikvlf sdsltngvre yggfywqklt viltalvigf illslialil wsvagfwrfp
      361 dalpeqftll hfksalmqmg splfntlaig lvttlfaiil tllcleseql sdkpisrfts
      421 liiylpllvp siaflfglvw iqqwvnnqaa ffnvvfthll fvlpyvflsl assyrrldsr
      481 farvaaslga apskvffkvk lpqlfapili aaalglaisf gqylptllag ggriatitte
      541 avtlangasr rtsavyaimq malpligfil awglpkyffk sarv
//
LOCUS       WP_010553688             295 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Pseudoalteromonas arctica].
ACCESSION   WP_010553688
VERSION     WP_010553688.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..295
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=32369
     Region          50..225
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mkkvilpall svflsgcaqq lgddvanqel pllsasevia satdndwrvv daqntlkitl
       61 ptgdayieln ellapkhvqn ikklaregfy kntsvyrfve gfvaqggdss gkkliktadk
      121 tvpaefyltt nkplliteln gdgyapvtgf lngfavaqns ahtqtwqvhc sgvfamardn
      181 dinsasteff vtigqgpryl dknitvfgrv legiehfnrl artptegkaf npitniqvlg
      241 dvqsdksifk vmktnssvfk nlisarknrv epwfvkahny vdvcgmpipt krevn
//
LOCUS       WP_010553724             419 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpP1/FadL family transporter [Pseudoalteromonas arctica].
ACCESSION   WP_010553724
VERSION     WP_010553724.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..419
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45285
     Region          9..417
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mkkqlisgla ltctlgsfsa fatngyfthg ygmthkgmag agvalseelm sgannpatfl
       61 pngtelslgl elfsperkyt askvdtfypg afyleaktqk sdntvfaipe faighqlnek
      121 vnigllvygn ggmnteysae sspegtfyag ttgvdlkqlf isptvsykln eqtrlgvspi
      181 yvvqqfeaqg lgnfapfsqs pealtnngtd tstglgiqlg isqdinssls wgasyrssvs
      241 mqefdsykgl faeqggfdlp ssfqlgvayk ltpanqvvfd wqkinysevk sianpitnlm
      301 saplgadtga gfgwndmtiy klgyqwqrts qqkirfgvsy teqpipssnv llnilapgvq
      361 ewhfttgfsh sftnkvqlna mafyspakkv tganylapnq qlsiemkqtg lgvsivwei
//
LOCUS       WP_010553733             298 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010553733
VERSION     WP_010553733.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 298)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..298
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33445
     Region          36..298
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 menvhiltqh vsgrgdflpf saehsptnei tethklvael qtslviedvl aiyakfakql
       61 lnfsglqfqs tlgtaqtsds ntgntpytfd lsidkdhlgq liyfskfplg qaiekklhtl
      121 htalvyplrn ammysrvlkl atkdaltgln nrsqfndfll qklencrryq rpfslmlldl
      181 dnfkqvndnf ghkigddtlk efskvlcssi rgtdsvfrfg gdefallied pefttnkvva
      241 erimclvrks plmskyrvtt svgftlansq dseteifara dkglykakas grncakay
//
LOCUS       WP_010553785             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudoalteromonas].
ACCESSION   WP_010553785
VERSION     WP_010553785.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48455
     Region          17..388
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(24..25,28..29,32,65,115..116,118..120,123,145,
                     148..149,152,221,224..225,228..230,233,260,264,308..309,
                     313,317,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 mtasslnsre kraavslasv fafrmlglfm lmpvlaiygq slegfspiwi gfaigayglt
       61 qavlqipmgr lsdkigrkkv ivgglvvfai gsvvaalads iqmvtvgral qgmgaiasal
      121 lafasdlsrd eqrpkvmavi gmsigmsfaf amllgpivaa swgiagvfwl tailavfgif
      181 ivtmlvpnav nkapkgdtla sfsdikklik hpqlarlnag vlllhltltt ifvvlpsqli
      241 kdglvadhhw ylyipvlfla fllmvpimiv aikkekekqa figsvallti smlamsvwvn
      301 svvgiavcml lyfvafnfle atmpalvsri apasqkgsam ggysssqflg aflggmlggy
      361 vaqttttqav faaaalvgli wliiawkmqv ppkskvislm tkldseehaq tlasqlvalp
      421 gvieatvvrd esrsylkind kefdldqark vagli
//
LOCUS       WP_010553913             198 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Pseudoalteromonas arctica].
ACCESSION   WP_010553913
VERSION     WP_010553913.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..198
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=22731
     Region          6..191
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mseqikcrcp wldttkpdyv iyhdeewgvp lyddtklfef itlesaqagl swytilkkrs
       61 gykkafanfd vdkvaqftqd dverlmldeg ivrnrlkiaa tvnnakcfie iqeefgsfsn
      121 yqwqfvdnkp iisnlnnaed ypaiteasta fakdlkkrgf kflgpttvya hmqacgmvnd
      181 hsndcfrkee iikafssk
//
LOCUS       WP_010553956             286 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S1/P1 nuclease [Pseudoalteromonas].
ACCESSION   WP_010553956
VERSION     WP_010553956.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Romier,C., Dominguez,R., Lahm,A., Dahl,O. and Suck,D.
  TITLE     Recognition of single-stranded DNA by nuclease P1: high resolution
            crystal structures of complexes with substrate analogs
  JOURNAL   Proteins 32 (4), 414-424 (1998)
   PUBMED   9726413
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Rushizky,G.W.
  TITLE     S1 nuclease of Aspergillus oryzae
  JOURNAL   Gene Amplif Anal 2, 205-215 (1981)
   PUBMED   6101052
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181127
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..286
                     /product="S1/P1 nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006308 - DNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=32234
     Region          27..267
                     /region_name="S1-P1_nuclease"
                     /note="S1/P1 nucleases and related enzymes; cd11010"
                     /db_xref="CDD:211382"
     Site            order(32,68,86..87,89,142,146,152,176,180)
                     /site_type="active"
                     /db_xref="CDD:211382"
ORIGIN      
        1 mhnslkysis sallvsaift stdshawgqn ghrivgqiaq shisettkaa ikpyldgesl
       61 aqistwpdem rsapgefwqk kssrwhyina apgksfsfnh dhtknkesvs nilegihysm
      121 qtltdtnstl dakqfslrfl vhlvgdshqp fhagrgedrg gnrikvsffn eetnlhslwd
      181 tklvenenls fteyaqfidt nnseliaqyl qsspmtwvee shnlatkiyk ytnneigysy
      241 iynntpiikt rlqqagirla gllnalfdps akeletalaf ekkqtn
//
LOCUS       WP_010553974             132 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thiol-disulfide oxidoreductase DCC family protein
            [Pseudoalteromonas].
ACCESSION   WP_010553974
VERSION     WP_010553974.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..132
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15200
     Region          1..110
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 miifydgncp lcstemqqlk hadnknlitl edlnasdfse rypyidkdka mnylqaqkqs
       61 gemiygldvt yeawkivgkh swlkifrlpi irffadcgyl lfakyrhpis rflmpntqcs
      121 ngqcglkakg dk
//
LOCUS       WP_010554004             288 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Pseudoalteromonas
            arctica].
ACCESSION   WP_010554004
VERSION     WP_010554004.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..288
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31421
     Region          1..285
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mahdhshshv denqsnkqlt vavvinvllt vaqviggifs gslsliadal hnlsdaaaif
       61 ialvarkvgn kpadgthhfg ykraeilatl fnsstlilig vylifeaiss ylnpqpingw
      121 ivvwvaaial vidlataflt yraganhsin ikaafihnvs damasivvii agtliilyqw
      181 yivdliatvl isvyviyhgi lllkqsckil mqaapsnidt haishaisne fniesvvsik
      241 lwqlddkeny celvistqhl inlptiksfl hdnfnienci ieirpian
//
LOCUS       WP_010553982             140 aa            linear   BCT 01-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein
            [Pseudoalteromonas arctica].
ACCESSION   WP_010553982
VERSION     WP_010553982.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..140
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16169
     Region          7..134
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 msddavtimq nqkiilfdaq cklcsawcnf iiahdkntif klcsvqspkg elllthfgfs
       61 tieyasmvyl engkaytqsh affnvvkqlg ypyklatvfs ilpnrfnnwl ydrialnryt
      121 lfgkyqycri pnpedakhyl
//
LOCUS       WP_010554006             711 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas arctica].
ACCESSION   WP_010554006
VERSION     WP_010554006.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..711
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77695
     Region          32..682
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mlktslclia vaistntlan ennkneytsd qlehvivsgs risenidevp asitvinqqq
       61 iqqhlkvsse lgsllaqmvp glapntgsss nsgqtlrgra plimidgvpq stplrngslg
      121 vktldasaia rievikgats iygngasggi inyitkqars dgkpegeisi ssrfsavkla
      181 esgggriaaa vngkldklsy lltasyeeng vqrdaegdil glqyglsdse tqnyftklty
      241 dfddekqlqf synfyssqqk tdlgdvtgdg nigektyaih vplelqkqgk pqgpegneni
      301 tlkyvdyalf entqmtldly kqnienvfff stalanldeg ysggqsviks dkqgaratfn
      361 sqfdfenvta tliygidaln dktsqplvdg rvwvpemdme svagflqtkw vinddiivka
      421 gvrnesidls vsdyqtlklc ktasqcsvpl nvrgdtinyd attynagiky nltdafspff
      481 sysqgsdisd igrllraatv ddialiqtqa siidnyevgf tsqfenvrfe falyrstsel
      541 gtsneyneit gvyepvrapq eiwgyeglvn ytitqdlkls atysyvegkn teaddylgas
      601 qisppkatan vtwqtndels lamsflyvgd rkrfdknaqg qysgdqgpvs syntfnlsgq
      661 ynvnaqwsgy fgienlfnsd yyparaqayt yggynikglg ttatlgakyq f
//
LOCUS       WP_010554058             791 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase
            [Pseudoalteromonas].
ACCESSION   WP_010554058
VERSION     WP_010554058.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 791)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..791
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86788
     Region          4..88
                     /region_name="ATPase-cat_bd"
                     /note="Putative metal-binding domain of cation transport
                     ATPase; pfam12156"
                     /db_xref="CDD:463475"
     Region          91..790
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msnscfhcle svpngfsanv iiddkaqpmc cigcqavaqn ivdqgmtdyy kyrtvragkv
       61 eqlvpeqlaf iksydnediq defiatndni sevllsvegi tcaacawlie kqllnlntvk
      121 rvdvntstnr amiqwdkttt plsevitsla kigykaypfq sdieaqqkqq takayirrlg
      181 vaglmtmqvm mfafamyfgm fsgmdsnfeq yfrwislvla spvilysalp fltnainglk
      241 akqlnmdlpv slaifgafga scyatfmqvg evyfesvcmf tfllllgkyl efrarlkase
      301 ftanlqkllp ltartinesg eeliiaakkl klndvvlika getipadgel ikgkttvdes
      361 mmtgehqpvt kfighnvyag cvnhdgviei kinkigqntl lnqiirlqhn altkrpklve
      421 itdkvaqwfi acllifaslt aigwyqidpe hafwitisvl vatcpcalsl aiptaltcav
      481 atltrkgvli kqahvletls qitlfafdkt gtltqgkfsl devdiidkqy tkaqvldmaa
      541 mlerysehpi asafdeftpa hrslnnvevh pglgisaqda tnhyaigksg wfnskksnaq
      601 aslyinkqvv arfyfvdkvk sdakklidsl qsqnltchml tgdasdagqk vakqlklesv
      661 qfgcspqdkq taveqwssqn evvamvgdgv ndspvfasah lsiametgad isknsadvvl
      721 lnsdlasigh llnvakqtrr iikqnlalsl lynasilpla alglvapwma vigmsassii
      781 visnslrllk l
//
LOCUS       WP_010554074             295 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010554074
VERSION     WP_010554074.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33255
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..287
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,221,238,266)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     215..219,226..227,230)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mynlsdletf iavvenkgvl aaareqrlsp atvshrlskl erelatvlvf rdsrrvrlsp
       61 ageifytrvg aimealhdae hsigarsssv sgllrvtmpp wifskyvmpr lneleqaype
      121 lkldflitdh fvnvvddaqd vairvgqlnd sgllsrkivn nkrilcaaps yikkygmpks
      181 laqlsehywv clpwqrqlkl fdeqgkthtf nartrftisn sdnmtqaaia ghgiaiksmi
      241 aiyedikngi lvevmpgvma qddapvwflr pqnslttrkt dvfydfmksl flsce
//
LOCUS       WP_010554234             307 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Pseudoalteromonas arctica].
ACCESSION   WP_010554234
VERSION     WP_010554234.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..307
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34625
     Region          6..306
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtkhvqitii dypnalqsav qgfkelffla nriviesqle vqfcvkviqp didldemsqs
       61 divilppnld gdyyytpqpk llqylneahq kgtilcsaca gafilaktgl lnnrvatthw
      121 qladefheaf pkvsleiesl lindgdiisa gglmswidlg leivaqftkp hvmrtlgkfl
      181 ivdtgkreqr yygsfspkln hgnkqillvq hfiqanyskt lnvsvlaala cmsertflrk
      241 fthattlkpi qyiqkirvqk acellestth sfervalnig yddvnsfrkv fikiiglspt
      301 afkerfv
//
LOCUS       WP_010554115             569 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Pseudoalteromonas arctica].
ACCESSION   WP_010554115
VERSION     WP_010554115.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..569
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=63343
     Region          25..229
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          288..569
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mnkiktlfta atlalslasc gdsdldvaps gvlteeqvsn senvdaliia aysylgndhy
       61 tapnflwptg nlragdahkg gngpgdifay halslyqpiv pdmesfppdl idlnnkkwvr
      121 nytgisrans alavianape aiensaakqs elrfirsify fdlkihhkhi pwidetmtqd
      181 qilsatnrel ndqelwdkia adfefaannl pqtqedvgra salsakayla ktllyqayeq
      241 nelhqvinin kdklvkvval vdeieeagvy glfddyannf lfesengkes vfaiqrslnd
      301 gspdgrgswp salnapmagg fgccgfhvpt enfvnafktd qqglplfdsf ndfnydmttd
      361 svdprldhtv amegkpfkyd dnlihggdsw arapgiygnf tamkdlehpd cscrgengpf
      421 pifslntpli ryadvllwka ealieldryd ealpiinrir erakhstdrl hnasiynigl
      481 yasfgskela raalrferrl elgleghrff dlvrwgiake tidsylaiea vrkpylvdai
      541 ftkgkheylp ipnqqiilsg gsytqnpgy
//
LOCUS       WP_010554237             198 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tRNA-uridine aminocarboxypropyltransferase
            [Pseudoalteromonas].
ACCESSION   WP_010554237
VERSION     WP_010554237.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Funk,H.M., Zhao,R., Thomas,M., Spigelmyer,S.M., Sebree,N.J.,
            Bales,R.O., Burchett,J.B., Mamaril,J.B., Limbach,P.A. and Guy,M.P.
  TITLE     Identification of the enzymes responsible for m2,2G and acp3U
            formation on cytosolic tRNA from insects and plants
  JOURNAL   PLoS One 15 (11), e0242737 (2020)
   PUBMED   33253256
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Meyer,B., Immer,C., Kaiser,S., Sharma,S., Yang,J., Watzinger,P.,
            Weiss,L., Kotter,A., Helm,M., Seitz,H.M., Kotter,P., Kellner,S.,
            Entian,K.D. and Wohnert,J.
  TITLE     Identification of the 3-amino-3-carboxypropyl (acp) transferase
            enzyme responsible for acp3U formation at position 47 in
            Escherichia coli tRNAs
  JOURNAL   Nucleic Acids Res 48 (3), 1435-1450 (2020)
   PUBMED   31863583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..198
                     /product="tRNA-uridine aminocarboxypropyltransferase"
                     /EC_number="2.5.1.25"
                     /GO_function="GO:0016432 - tRNA-uridine
                     aminocarboxypropyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=22218
     Region          1..196
                     /region_name="TapT"
                     /note="tRNA U47 aminocarboxypropyltransferaseTapT/TuaA/
                     YfiP, DTW domain [Translation, ribosomal structure and
                     biogenesis]; COG3148"
                     /db_xref="CDD:442382"
ORIGIN      
        1 martlcnhcn falntcicsa itninnkvkv iilqhpseek iakntaklln lcltdcqivk
       61 gennddfsil kslpvsstvl lypnehavnl ddsaeqsnik nithlivvdg twkkaykilq
      121 lttllnqfkt vsfkqlpknr yairkaprad slstleavah slflieqlnp aplynvldel
      181 iqkqtqhmpe hvkaryld
//
LOCUS       WP_010554295             460 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Pseudoalteromonas arctica].
ACCESSION   WP_010554295
VERSION     WP_010554295.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..460
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=49722
     Region          2..453
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mipmdfdwla nvlttdyqgd nqhvlnintd trtvcdgevf lalkgpnfdg hkfiaeakqk
       61 gaigvivqhk vdvdipqfiv sdtrialgai gtavmaqvap ktiaitgsvg kttikemcaa
      121 ilsvhgdvla tkgnfnndig vpltllrlep qhrfavielg anhlgeiayt tamtkpdvav
      181 vcnvaaahle gfgslmgvak akgeifdglk ddgvaivncd sefsqywldk legrnvkrfs
      241 ttekldiwae ditldanara sftlctkdkq vpvtlalpgk hnisnaliaa altsefnvtl
      301 eeianalatm gdvkgrvnli evsdlltvvd dtynanvksv kaaidllsdm qghrilalgd
      361 mgelgedark yhqevgeyal eqgidelftl gvlskyasdv felpnrhfss reqmqqkiqe
      421 sinkvnkktt ivvkgsrssr mellvtdlvn gqqqaingvs
//
LOCUS       WP_010554341             682 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Pseudoalteromonas arctica].
ACCESSION   WP_010554341
VERSION     WP_010554341.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..682
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=77956
     Region          5..406
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mkptafiygr vssdkqtigt sieiqtdlkk akqiasehgc elselitvde gvsgfsgsnl
       61 ktgklkdlle ivkrndliil raldrfsrgs lykvnsiftd llhkgvrfyt tmdnklygge
      121 ssnkvvdaiv svigfnsafe esskkaalnn dyilkritqf ndgirglnna plhhgksipf
      181 hcqlvgedks kvvvkhpknf dvakeiiala lngsglhkii rvvnekhnis rtkqwlkdyl
      241 kshtlygnci lkvqdrtqkv iydgfgetyp kkeyilneyy pavctknewl glqetrkrsi
      301 klrsegqkyy sllsgrqrly cscgkpltvi ygknatqpiy ygcidqiscr nmeqiyvlnr
      361 vvtdavtgdv ykkdtdknsk nreiesnkln geitelqesi nnmlklvedh playgdkfap
      421 kiieskkaie kkqklldevn gqkfissrti eernmipnei rkikdqllng tseqnlengn
      481 kiykiikrit ldknglisie fesgefkacy fpiqnkskgr rmgsflhifn niednlyapm
      541 kedpdfslvt ftreelenkk hvihidkinp slltlfsher timacdkavs hinnylksyg
      601 yfilkssfai nsglsekqwq khkayciaff ekrgmihkie fitknngrns iliisdkklr
      661 lkkintilfl niknykqlat ps
//
LOCUS       WP_010554456             555 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein
            [Pseudoalteromonas].
ACCESSION   WP_010554456
VERSION     WP_010554456.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..555
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=59904
     Region          32..555
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 msnlslknkl lllailplml llislmlssy ylenknqqqn feafqtklis dkqtllstev
       61 eiaskivryq iangseqdak nalrdltfgq ggyffiydtn gvsvfhallg daiegqnkig
      121 mtdpngkkii vglldqarkg ggafnyhfqk pnttglvekm gyaamipgtn wmigtgaymd
      181 didaellkyq tamqehmndk vvtlllialf wvvltiical vaantmvkpi qrmaqslddi
      241 akgegdltkr ldidtndeig qlgeafnmfv sklhgiianv vdvthdvkta ssdintqtrl
      301 iedkllnhnh etdlvatait emsatsheva qntnqvaest qaatqevaka qecvdislse
      361 vsnlmgeinl aaeqvdslsd qskkinsvls viggiaeqtn llalnaaiea arageqgrgf
      421 avvadevrsl asrtqvstle isemlselhn lvsdavaamq asqnscnrsv essraisesl
      481 gavttsvrsi ndmstqiata aleqssvtee inrnvfaiqe ivneltissk ttssvgqhla
      541 argenlgqlv gqfki
//
LOCUS       WP_010554501             312 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Pseudoalteromonas arctica].
ACCESSION   WP_010554501
VERSION     WP_010554501.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..312
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33931
     Region          4..297
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(28..29,32,86,100,102,134,168,257,260,296)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(226,231,246,257..259,262,284,288)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mstllaigec mvelvptgis eckqsfagdt ynalvyakrf antlncalft avgsdvlsan
       61 mlkcwqkegi stqnvittad ynvgiyaist dadgersfdy wrnqsaakhm mslytqkpfn
      121 lglkesdwvf fsgislgild deskqglltl ladlkkqgct iafdpnyrar mwqskshaie
      181 wlerayalsn vvlpglddhr vlfghsssae ivqyctqfdi deivikagsa gmqvyckddl
      241 kascpftpaa kqvdstaagd sfagtylaar mcaqtpqnal emadsvasqv vqhqgailpl
      301 dvyqslnisl gk
//
LOCUS       WP_010554513             277 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pseudoalteromonas arctica].
ACCESSION   WP_010554513
VERSION     WP_010554513.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..277
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30481
     Region          24..273
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mplilkslll lsalicfkls antpysiprs nvveliepvs eraypvyiql pksyqkqpnk
       61 typviyvtda pytfpivaga trfpmnsgkm qqaiivaigy ekgsagsnsr irdytptfak
      121 dwkkqtgnak ghiqflqstv fpfieknyra snlqrtymgh slgglfgati llttpdlfsn
      181 yiigspsvwf dnnallalkv nkpklpirvy isvgsmetpa fgeeqnmveg akqltqkina
      241 lksdnielks vvidganhat afpttaiqgl dwvlgeq
//
LOCUS       WP_010554563             314 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tyrosine recombinase XerC [Pseudoalteromonas].
ACCESSION   WP_010554563
VERSION     WP_010554563.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..314
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=35542
     Region          16..309
                     /region_name="xerC"
                     /note="site-specific tyrosine recombinase XerC; Reviewed;
                     PRK00236"
                     /db_xref="CDD:234698"
     Site            order(162,255,258..259,290)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 msddapnttq lsdswrtpit lfsdylkfek qysahtvnqy vsqlgfaaly fsklcddwfg
       61 vqgehirrys malrskqlsg rtislklsci rslykflkak niaeqshyhn pavgikgpkf
      121 akplpknldv dqmarlleip ddeplairdk ammelmyssg lriselvgan mqdisaange
      181 ilvrgkgnke rlipvgkkal dalkkwltir pqfakpdeia vflssqknri sirqvrlrmq
      241 ewgikqgiss qvhphklrhs fashilessg dlravqellg hsslsatqvy thldfqhlak
      301 vydnthprak krtd
//
LOCUS       WP_010554606            1048 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudoalteromonas
            arctica].
ACCESSION   WP_010554606
VERSION     WP_010554606.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..1048
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=113015
     Region          1..1045
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 minwivsfav krrmlvlalt flfagfgvyn iqnlavdavp ditnvqvqin tkaqgftple
       61 veqritylve tamagipkld ytrslsrygl sqvtvifneg tdiywarqqi geriqsirsd
      121 lpnnvepnlg piasglgeif tysvhaapna lkedgtayna edlrtlqdwv irpqllkvkg
      181 vteinsqggf erqyqvapmp ekliayklti sdvisalevn nsnrgagyie rfdgqylvrs
      241 pgqlktledi antviakrdd apvrikdvan vllgkelrtg aatyngeetv lgtammlige
      301 nsrvvakama dklidvqksl pagviveavy drttlvdkti atvqtnlfeg ailvivilll
      361 llgnvtgali tamviplsml favtgmvgnr vsgnlmslga idfglivdga vivvenclrq
      421 lgvaqhkhgr lltlnerlnv vtaatkevft pavfgiviim lvylplfals gvegkmfqpm
      481 aftvvaalig alifgvtfvp aaiavfvrgk vdetenavmr gvkkvykpll gislklpwlm
      541 vgiatalvlv lgfkvknmga eflpkldegd iamhalritg tgieqsvqmq keleqaildq
      601 pevanvfski gtadvasdpm ppnvadtfli lkpqdewpnp altkaelvqq irtrvndvpg
      661 nnyeftqpie mrfneliagv radvalriyg ddlsvlkefg ekatglmrni agatdvrleq
      721 meglptlsvt pmrdhmallg lsvndiqqtl aaavggvqtg liyegdkrfs llvrldkrws
      781 sdvsalarlp valpkdsnpe lafvplgeva tisiekgpnq inresgkrnv vvtanvegrd
      841 lasfvsdaqa smneslnlps gywleyggtf eqlqsaskrl slvvpvtlll ifgllysafg
      901 slrdsliifs gvplaltggv lalllrdmpl sisagvgfia lsgvavlngv vmlsfikqlr
      961 sdglslfdai hsgalqrlrp vlmtalvasl gfipmalnsg tgsemqkpla tvvvggiiss
     1021 tlltllilpa lyklvhskft kkaeaela
//
LOCUS       WP_010554566             218 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pseudoalteromonas arctica].
ACCESSION   WP_010554566
VERSION     WP_010554566.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..218
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23820
     Region          15..218
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mslefveyaa qsehkatviw lhglgdsgdg fapvapqlnl pselgirfvf phapvqpvti
       61 nggmemrswy diksieldkr adeqgvrdsa akveelinte iangipanki ilagfsqggv
      121 vslhlaprfe qklggvmals tymcvpqkfa deakhtdlnv fmahgsqdnv vphsagrsaf
      181 evltahnmdv swqeypmahq vcaeelqair qwliarls
//
LOCUS       WP_010554617             139 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Pseudoalteromonas].
ACCESSION   WP_010554617
VERSION     WP_010554617.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..139
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15687
     Region          6..138
                     /region_name="COG3565"
                     /note="Predicted dioxygenase of extradiol dioxygenase
                     family [General function prediction only]"
                     /db_xref="CDD:442786"
ORIGIN      
        1 msnclhlaip agdlkvakaf ycdvlgcktg nseegrwvdi dfwgneltlh qsverlptvr
       61 hdvdmgavav phfgihlsed efnglktrie dagieyldkp yrrfigdefe qetffiedpn
      121 gnvlemktmv npevlfkkv
//
LOCUS       WP_010554620             273 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sterol desaturase family protein [Pseudoalteromonas].
ACCESSION   WP_010554620
VERSION     WP_010554620.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..273
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31518
     Region          76..233
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mnseiillal spiflifvcc efikfkryyd ikdslantvl allhqgadai allllmplln
       61 wlydyrlfdi evsvlsiafa fllqdflyyw fhkashhihw lwaahvvhhs stkmnfttaf
      121 rqslmypvag mwvfwlpmil igfepltvfs vvalnlayqf fvhtqivgkl gwfekvfntp
      181 shhrvhhain agyldknfag vliiwdklfg tfveedkskp ckygiigqln snnpvvitfh
      241 qwehllksvy kasgikakcr vlfgyptssi krk
//
LOCUS       WP_010554674             345 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator [Pseudoalteromonas].
ACCESSION   WP_010554674
VERSION     WP_010554674.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..345
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=38247
     Region          221..339
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mninshvlei iqgvigkyce tqsqkfsitl inklqcnyvc lqippeqmia qceafltpal
       61 aavkqcflln leaniqgvsi hyqiddseqv ntldfhglla tkesvslald vrqnvdvltd
      121 ceallksclk msanthdrfg lnfklfnstl resaqledlr hlsgnalidk lnsdslnthi
      181 klcsindiye lsqahklskk ilgwpffdtd litilttfht qtrlsvlvad dslpsqiatk
      241 vmlemlgclv tcaengasal tlaqnepfdl llldermpgm fgsdvaqqlv rqntpnnntp
      301 kviltgltgd eqiaelfdkg ithylqkpvt kavlekfikp wqlas
//
LOCUS       WP_010554711             573 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF262 domain-containing protein [Pseudoalteromonas arctica].
ACCESSION   WP_010554711
VERSION     WP_010554711.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..573
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=65840
     Region          3..570
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 mkieandkei qdifslgyfk iprfqrpysw evdevesfwn dvvkenpeny figsmvvyqs
       61 kkpyfgivdg qqrlttitli lsalrnaflk igennlargi hkyiekanid nedefvlrae
      121 tsfpylqsyi qsfdglklnc evgseelklk kafdfitkkl iesipelssl idnqsqpslf
      181 tnhdtaivqq lkairdkvls lklvfiqlen eedaylifet lnargkdltt pdlvknlllk
      241 klqsksiald kakeawntlt kqfdgisdld vlgayllhyw mskfeytsdk alfskvklhl
      301 kndeskanal iidlnesash ycrmlkpesa vwkkeerdik rlleslnifk vkqqssfvls
      361 llrayysqki slknlkttli kivnfhycfn aitkqrssgs iatkysslai rlseiedknd
      421 fqpilndltn flrtkrpeed efvvkfselq ylsnitkfks iirytlnnml ptaengldin
      481 lnnmtiehii pqsfigngfk eeavasignl iltsedvnsn mlankspvek ikllksisyp
      541 lekavinsdd wstetvnkrt kemaskiyne lii
//
LOCUS       WP_010554799             237 aa            linear   BCT 01-JAN-2025
DEFINITION  spermidine synthase [Pseudoalteromonas arctica].
ACCESSION   WP_010554799
VERSION     WP_010554799.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..237
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27276
     Region          49..>197
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mtekinyins ltgllsdqfi enshsigqli ywhkcsgdhi qvreheqlrw llindtlqsv
       61 idlnnpdlll fphllyldkh wqalkppqkv leiglgggai rnylqhkypk aqitsvekna
      121 diidcytqff ssnknkqllc adaqqilksv qnidwiildl fsqidaprfl feeafykkiy
      181 salnnngvlf inflsqhesq lkqlqqllld vfgcnvspqk itgyvnhivv vtknlnr
//
LOCUS       WP_010554809             234 aa            linear   BCT 01-JAN-2025
DEFINITION  2OG-Fe(II) oxygenase [Pseudoalteromonas arctica].
ACCESSION   WP_010554809
VERSION     WP_010554809.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..234
                     /product="2OG-Fe(II) oxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=26889
     Region          128..220
                     /region_name="2OG-FeII_Oxy_3"
                     /note="2OG-Fe(II) oxygenase superfamily; pfam13640"
                     /db_xref="CDD:463943"
ORIGIN      
        1 mtdfirvvdn alsdefcdef istfaqsphv kqgvtsggvd lkkkdshdlh lnnhpeyaqq
       61 lkhiqqttaq hvfkyveehi fmmigafglk vyhpktgevv dltqenfeev gkpqlpllvq
      121 qifrlgniqa qkyevnkggy pywhsevypq lqhnealhrv llfmfylndv deggetefyy
      181 qnrkiapkkg tmviapgyft hthrgnkpvs ndkyiltswv lfnraeqiyg apns
//
LOCUS       WP_010554838             151 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010554838
VERSION     WP_010554838.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..151
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16768
     Region          1..140
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mldkkdqqll ialqsqarms vsdlasginl sdtpclrrik kleqeniitg yhaainpkal
       61 nlnvlvyafv rlsqnsvsaa eqfeqhvekl phvleccvis gsydyllkii ahdlesyetf
      121 vkhqlgslsc ianiestvvl kqsfskkqlp l
//
LOCUS       WP_010554846             234 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Pseudoalteromonas arctica].
ACCESSION   WP_010554846
VERSION     WP_010554846.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 234)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..234
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25334
     Region          8..231
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mqpvkkailk gfldmlplcl avvpwgilcg slaiqngfsa letqamsllv fagsaqlvai
       61 elmagntpll tilfttfiis srhflyglav rhkvidqpmr wrlpvsfvlt delfafshhr
      121 kayrtktrli yalsagfsfy iawniwtlig ivagtmlpdl tnlgldfaia atfialvipg
      181 iknltslvtv ivagisatll kstgfelwlv csallamaag ystarlttkk evtp
//
LOCUS       WP_010554992             539 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudoalteromonas arctica].
ACCESSION   WP_010554992
VERSION     WP_010554992.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..539
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58170
     Region          13..539
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mtinmrlttg fgvilsmmli ltiigisrvs linnnithmt dvnsvkqrya infrgsvhdr
       61 aiavrdvvli tdqsslstvl ksikelnafy qtssrsmael mgdmnseera linkinqieq
      121 rtqpfiqgvi naknagnlne aerilltdar paftqwlnvi nqfinlqeqa nqtttidtld
      181 iassfkiwmi sltalaflig isvayvisql irnsvggepq eaaevialia qgdlrgdvqs
      241 ccpnsmmasv gvmqsklkti vdsiinssee lsthsasvas gsqqalsaad aqvtytnsav
      301 ssleemsrsi havadsvrqt ednskitaql sqqgsiavqk vaaeieqisv tvkatvtqvn
      361 vlqehvkhig dilsvirsis dqtnllalna aieaaraget grgfavvade vrqlaqrtgd
      421 atgdiekmil qvqentqasv tamettvpqv engltlthea nellhqiqqq andslsnvle
      481 ivestsnqva tvaqistdve eiasmskets mslnsnaqea valadlsntl kkyisyfkv
//
LOCUS       WP_010554995             434 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudoalteromonas arctica].
ACCESSION   WP_010554995
VERSION     WP_010554995.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..434
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48041
     Region          18..416
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 msitipkivv igggagglel atqlghklgk kkqadillid knrthiwkpl lhevatgsid
       61 pdldgvvysa haakhhyrfq lgtfcnidqs nktitlspln delghtilpg rtvrydhlvi
      121 aigsvsndfn tpgikehcyf ldssqqaerf qhslldsftr lhqddnqqqs lniaivggga
      181 tgvelsaely hvsellklyg ltnmsskrlh ihlieagpri lpalperiav sakrellklg
      241 vnvreqtqvk egtaqgfitk deehinadim vwaagvkapd fikdlgifel trsnqiqvne
      301 flqstvdesi fvlgdccaft qadgkqvppr aqsahqmalc veknliatlk qqplrgfkys
      361 dhgslvnlss ystvgnlmgn ltsntffieg riarfmyisl yrmhqraihg saktfalwis
      421 ekvlrvvrpk mklh
//
LOCUS       WP_010555023             334 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Pseudoalteromonas arctica].
ACCESSION   WP_010555023
VERSION     WP_010555023.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..334
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36735
     Region          1..246
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 makvnwgiig cgniahtfak siahcsdaql igaastsmqr akefatpyni qgyesyqalm
       61 qcpnidavyi anthdqhfkt iaqclkhnkh vlsekpitvn aeqlqsltkl akqqncflme
      121 gvwmrflpai vklqqllseg vignvhsvna nfslpgsfad thrlmnpvta ggalldlgiy
      181 pisiadvvfn kapehiksfv hksttgvder staivdygng qfaslasalq qngpteacin
      241 gelgyiripq fvgaktlelh indqdpqyfk ydfsddenfk feiahvtqci lqkqtqssvl
      301 plgtslrvmn imdtlraqwq lqysnavesa eltn
//
LOCUS       WP_010555127             497 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptide MFS transporter [Pseudoalteromonas].
ACCESSION   WP_010555127
VERSION     WP_010555127.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..497
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53875
     Region          2..487
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mssapdsgwc ghpkglstlf ftemwermsy ygmramlvlf mtaslqeegl aftvasaaai
       61 yglytgavyf lglpggwlad rlfggqkavw yggiiimigh iilaiphdys ffiglifvat
      121 gtgllkpnis amvgqlysdt derrdggyal yymginmgsl igyyvcgyfm envgwhwafg
      181 aaavgmaigl vqykltlnnl pehsalpanp lgpkgtsraw igiaafviaa aavttaamtg
      241 aivinptvva gytaivftii ffvyfgviyf tgkltdaekq rmwalflvci asacfwsgfe
      301 qagsslnlfa rdytdrfigt feipttwfqs lnslfiials pffaalwinl skslvspsys
      361 vkcaigliim asgflvmfma ahyaaeglkv apywlvttyf lhtvgelcls pvalsavskl
      421 spkrytgqmm gvfvltysig niiagllagn fdpnnvdeip nlylqialfs igvgvvlvlm
      481 tfkakvwekq gleekas
//
LOCUS       WP_010555173             165 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [Pseudoalteromonas].
ACCESSION   WP_010555173
VERSION     WP_010555173.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..165
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17554
     Region          1..151
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mitltingnk hefsgdpsmp vlwylrdeln ltgpkfgcgm aqcgactvhi dgvaqrscvl
       61 pvaavaglsi ttieglseqg dhpvqqawve hkvpqcgfcq cgqmmqaasl laanptptdd
      121 eivsnmsgni crcgtyprih kaiksaaktm asvqyfdpne qgeev
//
LOCUS       WP_010555137             757 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Pseudoalteromonas].
ACCESSION   WP_010555137
VERSION     WP_010555137.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..757
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83497
     Region          42..739
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkamkrstla tlinatlfsa vagtsfssla aeektakksn qleviqvtar krvenaqevp
       61 vavsalqgdn ldayssagmd irflnakips lsiessfgrs fprfyvrglg ntdfdlnasq
      121 pvslvvdevv qenailkgfp vfdvervevl rgpqgtlfgr ntpaglvkfd tvkpsqefdg
      181 ygsvsygsrg avdtsgavgg altdrlsarv sllwqdkddy idnqapgfea kdeqggytek
      241 aarvqflyeg ddftallnyh trdldgspia franvikpgt nelvdnfend ivyqdaasrs
      301 tqqvesegas lklewelknh titsisawes aeiysradid ggyggfsidd vpvamgpdsi
      361 pffnesadgi pdhdqltqel rlssnfdgdl nyqvgvfyfd eeltienfsy dtsnngvlng
      421 yvrqqqdtta wavfgsvdyt ftddlkvtag lrysdddkdf vayrtispig agplppvkqn
      481 vsddhiswdl sanykvnddi nwygrvansf rapslqgril fgndvttaes etitsyetgi
      541 ksdvldgqgr vnatvfyytm ddqqltavgg ganfnrllna dkttgygfel dsqwvlsdef
      601 natfnlsynk teikdsnlsi aapnrptlni tdpvvdgkvf ldgnslphap ewisnftlry
      661 tkeladgnff asgdisyrsk inmflyesve fegkelietg lrtgytwseg dyeyevaafv
      721 rnlfdeqqvi gavdfnnntg ivneeryvga efkvrff
//
LOCUS       WP_010555246             671 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudoalteromonas arctica].
ACCESSION   WP_010555246
VERSION     WP_010555246.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..671
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=72679
     Region          143..671
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnltvsqriw ggfifitlll liiggnslik ianidrstqk vnqlslpaln ksselqaefi
       61 lmskaaqasf yttsanelap ikahvleqkq lfntlhrelq dvvkndtaln qssqnvekty
      121 lsflstvenl ledkskqlal nkslnaqles ieltaedans vvldiididg feqnyprayq
      181 aannlennfm svvsnstdml tvktlntldi vkneqtyyle evirtvaliq paieqthsdl
      241 ysslkeyvdi lesnikgsng laankkrlid sitltqsela qseqatkmal nqidelvnqa
      301 sdvafklqqg vrsdvdsanl wtwvgmiiat llaiaiaiit vsritkplae vnrildivas
      361 gdmtqrldds akdefgelsk scntlidslr slikgiisrs tqlaaaseqt saitaessqa
      421 irnqqaqveq aatattemss tsqtvsnsaq qalseiknad keaervkgis nnnkatieql
      481 arevddasqv inklhqdsas igsildvirg iadqtnllal naaieaarag eygrgfavva
      541 devrslaskt qestqeiqam ieslqtgaea avtamskgkq ravscveqtd lassaldsit
      601 favsqahdvs eeistaaleq qqvaqeiser lesivaiaeq taeganqtni sssevaklae
      661 elrlsvdefk v
//
LOCUS       WP_010555260             441 aa            linear   BCT 01-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Pseudoalteromonas
            arctica].
ACCESSION   WP_010555260
VERSION     WP_010555260.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..441
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48219
     Region          7..>151
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          247..434
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 matnsiikvf satvlllsan isfaassdda kqsilsdikt aqrtlnktqn siskeqatla
       61 kqiftkqqsl sklreqaavn rrladentls ldqlqtrldt wqqqqqyqln llsrfvrqnt
      121 snsassnest nnqnellsrv isqinnqeqa lypqfkkqsv vlsngelsqa ntlqigpvaw
      181 fsaqtpklmg llnlddesna lkvalvqsts ddnpldntlk qngvgstllt fdpslthlvt
      241 sqaqqesple hlekgglwai piilfacfal tiallkaaql lrlskikmhs qmqlqqffka
      301 enssefagmq qqlfnltlqs ekgqvrddql fnqlihdkhk ldnfigaiav taavapllgl
      361 lgtvsgmiet fkmmtlfgsg dpevvsggia qalittelgl vvaipalvln allsrkakay
      421 ysqlegfalq lsqlekgetn v
//
LOCUS       WP_010555282             328 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Pseudoalteromonas arctica].
ACCESSION   WP_010555282
VERSION     WP_010555282.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36041
     Region          1..254
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnfvivgtnf isdtllaaan tlndfnlygv csravssgea flakhpqnaq akiftsieqv
       61 cqdqnvdavy iaapnslhkq yavmcleagk hvlgekpsaa nskelasiit takkhqrlym
      121 eammtthlpn fvrlqqamvk igtprkyigq ysqyssrydk ykngerpntf lpefangalv
      181 dlgiyplyll ialwgapqsv sasgvlldtg vdgagdvlln yadkqavisy skisqgdnit
      241 eiqgelgrir ieavsqlkkv efianngeve visqpfdehf mkyevehfma lvkqnvlesp
      301 vnthilasnv msvldearkq lgvvypnd
//
LOCUS       WP_010555285             271 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Pseudoalteromonas
            arctica].
ACCESSION   WP_010555285
VERSION     WP_010555285.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10563595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..271
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31086
     Region          10..184
                     /region_name="BMT5-like"
                     /note="rRNA (uridine-N3-)-methyltransferase BTM5-like;
                     pfam10354"
                     /db_xref="CDD:463056"
ORIGIN      
        1 mylnpqwril tvgdgdlsfs naiythlspk allastyddq ttieqkyqhn algnlkahnv
       61 evlnsfdvtn pacwqtlsen qhsfdvvifq fplipafvgr eafenntrqt smnvlnrall
      121 hqfikyaney aldkngpmlc yitskdvkpy rewniegsln nglnadylgq ipfdishfeg
      181 ykirnvdrdk hvkdtsgity vfspksidth tselssrltk payltsnhcp lcrvgpymas
      241 edetkhlnak khqqmlhles dwqqwlnefy s
//
LOCUS       WP_010555299             488 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein
            [Pseudoalteromonas].
ACCESSION   WP_010555299
VERSION     WP_010555299.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..488
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=53361
     Region          <72..488
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mssvarlfti ifsllfiesi gvglyfgtlt qafiiglplc llpiwllrty pdnvvtahvv
       61 aaaimmfsfl hiqqtfglie vhfeifilma vlimfvqwrv fitaiifvav hhlsfyylqt
      121 qnagfyvfdp drlafttvli hagyaivevl vagyiaktlq rerraglsls yateqimkdp
      181 eniklslrad dtksdavvgf ntlldyisdv ikqvqaqses lqknsrelih vheqlaggav
      241 qrtqqtddia nsgsqvahgf klveeeseal ksqvdhitkt vsnaledvhq tdsksrellt
      301 llnhteeqis hlvaaggvis gllneisgia eqtnllalna aieaarageh grgfavvade
      361 vrslanhska ttdkisltlk dlvnnsktst qsmsqcvnfv vdltsisaam kenisamseq
      421 iaavssssds vaqvvaeqag nteliasstd tmrqnqyqdt qivqqltakv qlidvsidvl
      481 eqsiakfk
//
LOCUS       WP_010555300             185 aa            linear   BCT 01-JAN-2025
DEFINITION  TMEM165/GDT1 family protein [Pseudoalteromonas arctica].
ACCESSION   WP_010555300
VERSION     WP_010555300.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..185
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19969
     Region          1..183
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 mevfltstvt vtlaeigdkt qllslllaar frnkgalilg ilaatllnhg lsawfgqwls
       61 nsfsseylpw lvnicfivvg lwllvpdkde dvsskydsyg aflvafvlff iaeigdktqi
      121 atvllgaqyq svfwvtvgtt lgmlianvpv iyagnallkr islntvraia acvfvslgiy
      181 glvti
//
LOCUS       WP_010555315             464 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Pseudoalteromonas].
ACCESSION   WP_010555315
VERSION     WP_010555315.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..464
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50605
     Region          1..428
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfeglglsq slvnavlekg yetptpiqaq aipaiierrd vmaaaqtgtg ktagftlpli
       61 erlssgpkak snhvralilt ptrelalqvs enveeyakhs dvssfvvygg vkinpqmqrl
      121 rkgvdilvat pgrlidlhnq navkfdsvev lvldeadrml dmgfihdikr liakmpakrq
      181 nlmfsatfsd eiralakgli ndpveisvaa knttaksvtq cvyavdktrk tallshlirt
      241 ndwqqvlvfs rtkhganrlv kqlerddivg aaihgnksqg arvkaldgfk sgevrvlvat
      301 divargldiv elphvvnydl pnvyedyvhr igrtgragas ghaisfvtte davdlygier
      361 figeliprae edgfepinpv aeraldarpl pakkpkkkqp fnkpksdssk pnskkpnngg
      421 ngtgprrggs kkpaaktdds tqnpwakres vggngqrrrr tnnd
//
LOCUS       WP_010555343             715 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas arctica].
ACCESSION   WP_010555343
VERSION     WP_010555343.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..715
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79364
     Region          62..682
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mvyksktqkt ylltpvalfi sgvlspfafa ddtpleviev hghaqnkhla lgssesllsd
       61 lgvdfsaagg vsnlpilngl mgdrvkvlvd gadvtaacan hmnpplsyis anqitsynvv
      121 agvsavsagg dniagvisvn sispqysdsn elgwhsgyvs akyssvdngr klgvgarlas
      181 ntfslnyqgs fsdadsyedg nsdvvldrly raqnhsltaa mrddkqqlvi klthqkipyq
      241 gfanqymdmt dntsygaiaq ykrsfensel egqvnwhsvk hemgffseek tgmmrmktda
      301 qdistqlkwr ialdknssil lgqeyynysi ddwwpgiegs tmmgpndyvn inngkreria
      361 afaeyesqin tklwlnagvr iesvntqvge vqpyndgmsm mnmddmssmt msdmstdnti
      421 aaqnfnagdr dktdtivdan flinyqitny delqfglark nrapnlyery swgvstmatt
      481 migwygdgng yignpdldve tahtlsatyi ksakddrwrl stnvwytdvn dyidadivrs
      541 fnsydldnta rnilqftnvd ailygakidl taniyeskql gnwqlhanvt ntrgkrddtn
      601 qplyqikplq tqlgisqqig rfenalswqw vdtksrvdnd rfenqtdsys lvnlsskatw
      661 dsltlsaevs nvfdeyyqlp lggvsiaalk qdssngfeql vgqgrsfnvs vsyaf
//
LOCUS       WP_010555349             145 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Pseudoalteromonas arctica].
ACCESSION   WP_010555349
VERSION     WP_010555349.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..145
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=15307
     Region          5..138
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mtikktasst wsgdiktgkg sistqsgaln kqpygfntrf edkagsnpee lvgaahsacf
       61 smalslalgd agftadkidt katvslnevd dgfsvthial evkariddiq neqfqalceq
      121 tkkscpiskl lnteisldat lqsaf
//
LOCUS       WP_010555350              44 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2256 domain-containing protein [Pseudoalteromonas arctica].
ACCESSION   WP_010555350
VERSION     WP_010555350.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..44
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..44
                     /product="DUF2256 domain-containing protein"
                     /calculated_mol_wt=5414
     Region          2..44
                     /region_name="COG4338"
                     /note="Uncharacterized conserved protein, DUF2256 family
                     [Function unknown]"
                     /db_xref="CDD:443479"
ORIGIN      
        1 mahkklnlpq kicpicnkpf twrkkwqrdw dnvifcserc rrnr
//
LOCUS       WP_010555352             202 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Pseudoalteromonas arctica].
ACCESSION   WP_010555352
VERSION     WP_010555352.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..202
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21942
     Region          14..189
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mfldltvnke lnvysylvgg isprpiawis tlssdgvani apysfftvas cnppvlsvtq
       61 vnprdkpskd tlinllatke cvinivsheq vekmnqscan ypsdvsefda anitkidsqm
      121 vavpsvadsk vryecklrev itissepggg qmmlldivgi ciddevlvdg yidptlldav
      181 grmggdyyat tkdkfvlkrp qi
//
LOCUS       WP_010555363             307 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010555363
VERSION     WP_010555363.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33723
     Region          8..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,192,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mkvsfeqlks mvvfaqiveq gsltaaakql gltravasyh lkkletqlev tllnrstrtm
       61 alteagiayy ercriiteqa naanqqieni ksepqgllki scpvnvgmql ivpaintfkr
      121 qypkikidlq ltddvvdiik ngfdfairgv alsdsnlqat klttmstcic gapdyfthfg
      181 kpktplelad hqwvvyqlgs ktltlskdgk khdiamqgal stnnaaarta fveaghgigr
      241 iplydawpkv qaglleiild dykskdiely gvfppgaags kklrlfidyl kayfvkqhta
      301 lgmlksv
//
LOCUS       WP_010555373             678 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Pseudoalteromonas arctica].
ACCESSION   WP_010555373
VERSION     WP_010555373.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..678
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74736
     Region          17..675
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mgvvlqnlff pkkqaiifat kgviamvmal tiamwlnler pywalvsaif lqlrpqsglv
       61 iekaicqiig tivgglfgil lltqlilypy lalgalalwl gvnsalsamv rqanfvyafa
      121 magvtaaiiv llvmvtpamv ssqsifdiaq arvseivigs icaglvshlf wpvkvkhllq
      181 vqarsvinqt ldylvtelds kgshenrhqq idgimatlgs inedssavry egpkgpgrsr
      241 aanqlsqkvl sllasiqiig rlqrnhadli tptldklisk lkhvfaqike sddfdycaeq
      301 vktlrkeltd yrantvcdsp feshmlnvsl evaadltill rayrsleqrd ktllnapsml
      361 tyrdplagii vgfrtalvfs igafiwintg ssaallimil pvifsimlar iplailqvvi
      421 krllagiiva tfvtifyaln llsqsggqle illlvlagpy flglllladq qtlpyglgfc
      481 ipftilvrps tdmslafsid ytlssaiaif agvsilfwif qlftgpsvql lvhrvfkaty
      541 kdlleinthq tpsiwynrrm adrlirltny dqgshsrait dmaltglnlg hasvrlnsic
      601 enlagdtklk ylnewqrtla dafmlatkgk fdenfkqasd nlynelalsv gdsnqleaik
      661 gmfirinltf ersaskin
//
LOCUS       WP_010555386             519 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BCCT family transporter [Pseudoalteromonas].
ACCESSION   WP_010555386
VERSION     WP_010555386.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..519
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56104
     Region          23..512
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 msttgvtkqh edehsstiky lagvdipvfl isggilvlfa vlalydidlm sswintafaf
       61 stktfgafwq illlstfiig lflafgrtgk vvlgglkkpe intfkwisii mctllagggv
      121 fwaaaepmah fispppifgg esgikeaafn alaqsfmhwg flawailgsl tgivymhlhy
      181 ekglplkprt llypvfgerv mkgafgaivd sccviavvag tvgpigflgl qvsfgleklf
      241 gipdtyttqv ailfgliaiy tlsavsgvtk giqllsrfnv ilavalmlfi llmgptafif
      301 dsyihsfgly innfipmatf radtawldww tvffwgwflg ygplmamfva risrgrtire
      361 mitlisiiap vitcfwftiv ggsgiffela npgvisepfa glnlpaalla iteqlpmgfv
      421 isvlfliltt ifvattgdsm tysvsmvmtg ndhpqtpvrv fwgimmgvma ailisigsgg
      481 isalqsfivv tavpvsfvll pslwtapqia kkmateqgl
//
LOCUS       WP_010555477             331 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase
            [Pseudoalteromonas].
ACCESSION   WP_010555477
VERSION     WP_010555477.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..331
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=36824
     Region          49..330
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mheqnndent evtflpaert fevlsaeaag tgvngieknp avsylmglra essrlamrsf
       61 lnniakmmgy hdlrtcpwgm lerhhvqavl tmltdagkap atinnylaai kgvaveawtl
      121 klistdtyqh iklvksvrgs ripkgralap aevkklfftc esdksaigvr dnailsvlvg
      181 cglrraevvs ldfshynrhn rslkvlgkgn kermaylpdg afqrleswie evrsdipgpl
      241 fsrvrryddv tsermtsqai yhilnsrsve agiekcaphd lrrtfassml engedlitvk
      301 damghaslat tqkydfrgde rlraaskrld i
//
LOCUS       WP_010555526             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: gamma carbonic anhydrase family protein
            [Pseudoalteromonas].
ACCESSION   WP_010555526
VERSION     WP_010555526.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..181
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19301
     Region          1..177
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mairsykgvt psfnssvyid essvlvgnit lgdnssvwpl vaargdvnyi rigkrsniqd
       61 gsvlhlsrat ksnpdgypli igddvtvghk vmlhgcilgn rilvgmgaii mdnvvveddv
      121 iigggslvpp nkrlesgyly vgspakqarp lteqelaflk isadnyvslk deylaeianl
      181 s
//
LOCUS       WP_010555693             192 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Pseudoalteromonas
            marina].
ACCESSION   WP_010555693
VERSION     WP_010555693.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..192
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22138
     Region          1..192
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mqligsvpsp yvrririwal qnncnielis ldifsaqdrp kmanknpark ipilidgdlt
       61 lsdsnsiiry llekigkskl nwpqehlltt inacndslve mllcersgld trsdalffnl
      121 qnerieqtls flnnhlndeq fksceylnis lyclldwisf reltdfsqys elvafhgqfs
      181 erqsaietnp rh
//
LOCUS       WP_010555716             662 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudoalteromonas marina].
ACCESSION   WP_010555716
VERSION     WP_010555716.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..662
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=72026
     Region          129..660
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnrllgrlsi iqlslltsii lmvfifilli qniankwqes qtlqqdiali slldalekva
       61 hnhaverglt agflgsgsae aknkvlaqrq kadasiqhle svsdqltkns tkvsknlsil
      121 fdhnakkaal rtqvdnkaap gafafyskln qialdvaanl ssqikhpvls kdlniaflla
      181 qykerlgqnr gkingtlakk qltsvtqqni alynseidll nqylianlqg qqlqsfnnii
      241 qsadsrkina itntllntes pnftalpaas vwfpmatqqi tqikkvldsq wntvdkdgle
      301 lkeaadttlt ltiiyflvtl viiaylnfhl lstlkkelsq ltslllkaek gdltidirlk
      361 skdelgeisn aihntiyafk dlllgldhsi nsgsklsddm snatktvldd snktlamasn
      421 iataieemaa tsreiagsas etlsssdeln kqanlliedn klsqssitel atgmsdveev
      481 vskmdqqvas issildsiss iaeqtnllal naaieaarag ehgrgfavva devrslagns
      541 kessekissl lgelqsisdq vvssivastk lskatlerfd qaravseqvh tqskvlenla
      601 mnvssaaeqq savasniavd aasvfeyanh eveaarkqee ifnemrlnte tlqhtmknfk
      661 fq
//
LOCUS       WP_010555723             298 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010555723
VERSION     WP_010555723.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32717
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..284
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,219,236,264)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     213..217,224..225,228)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnnehlklfv rvasthniss agaelglspp vasmhiikle eslgvklihr ttrrvsltee
       61 greflphaee ilnainsaka avgagsftpq gtirvaapss fgrmhivpal kafidqhpel
      121 kvdlrqsdsi vdmveggfdi airnaelnds tlvarklard hriicaspgy iaehgepktp
      181 qdllnhncik ligidywsfk tpngiekvkv kgsiridnge sirdacinda gitissiwca
      241 hnalkegtlv qilkdypmds naaiwavyps srllapkvra fidffikyyg eipyweta
//
LOCUS       WP_010555801             319 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Pseudoalteromonas marina].
ACCESSION   WP_010555801
VERSION     WP_010555801.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..319
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35910
     Region          144..303
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(187,230)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(192,195..196,200,204,226,228..231)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(222,250)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mqanscghew vveltcqede shldsalidv lgdllsvnnf aiyinkhvtl qappilinth
       61 snltylepnq aqlilnkatp sktrvihttd dvttyipvnh sdtilgvlii ktkqlitdri
      121 salamyilnv yanqlwilhk srldpltgll nrqtfdkkvm eivtgngfll preqadtkrc
      181 wylaivdidl fknvndtfgh vvgdgviaqv akliknnfri edyafrygge efaivfqsqt
      241 ntdafnaltr lrqrvashyf ehiqqltisi gflelqsadt vssivnqadm alyhskktgr
      301 nkvtschelt lskevrisq
//
LOCUS       WP_010555823             825 aa            linear   BCT 01-JAN-2025
DEFINITION  PilZ domain-containing protein [Pseudoalteromonas marina].
ACCESSION   WP_010555823
VERSION     WP_010555823.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..825
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=94431
     Region          147..253
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
     Region          491..>576
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 maddimlkhe slvnelkqyl gnakfdlifk sktaeltkpe qflikmemsr lsqpverfid
       61 lrglvtgqvk pyehngkqhf mdetaievfe salkqhgkyt lavyeavmnt ennhrvmqke
      121 aaekgnkqeq edllntsvik fasyesraee rmnysikvti eyndkknika stsdislsgc
      181 kiklakrnii rkgqliamrl vgleqdfelg lkngiqyevv avenisrefn hirlkrtyve
      241 nneafdnfle sfihgnkrry kvnldntlda vvskgyeqyy iprvtslyvf lskkddqyyp
      301 slslttenni fiqryftder svpclynvln hkrvsglltq ptavkedyly tfthvssgki
      361 yyysatrtel nnnaklrdlf lgfgsqkesw qcfkiqimps hpddayipls lpnsagskie
      421 klnkppsprv eglvkdvkyi vvltsignsv eqsrykqvty dkalvnqlkl fghakhktap
      481 yldivaleyv nlrshkryly ktdvklhind tvlsghtrdf svmglqlecd qpvsfkkgdi
      541 vfltfpdlqk itkkhalnel kyevmaisks lttvnlkanr vadlphagvs fftqliennk
      601 dklkvseeap kieglstalr nmvtksvcqf plylhkeaah fkvgaigygl yssplhvllq
      661 nfgllsnktd vssiitneqi lnvitpnikd rsrqdpplaf tlainfdprq dkvteaiqsq
      721 cilgedyssf neqiskgiks qiifvmrlyi srtgrpdtdy lsnelsyvsq yalhkakele
      781 ealwsvtgvg dvvditeeal shfeldqqkv dqmgrrkllw lnrsr
//
LOCUS       WP_010555851            1093 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Pseudoalteromonas marina].
ACCESSION   WP_010555851
VERSION     WP_010555851.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19960403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..1093
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=124962
     Region          <52..667
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          <514..681
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mntkkrphlv siktiltila vscfslyalf phtlffedda lsqdytfeks ylhaalntdp
       61 nneklrakla elhialseys natneleklp kskrktelei kllyslwlas ganvddrfee
      121 lslkvsaykp wnediltiak alglnvklaq yyethkkpli aadywltagq pakalllykn
      181 nmsetiaeka ietalganea mqayawwkqy gdqsnikrtl yladlagnke daiiaatkll
      241 qeepnnikyl tqamqlhlan gdangaelll skllkqkpnd kdlhllnwkv krwlnkpkaa
      301 lkefkwlmin kavtaamltd sindatalyl yqdandiyay kaknrqlkgn gftkwmqtne
      361 figdakqelk hierfesing ksvlsqywka kvlhdtgnls glrnlwpiyq gpkneedlmw
      421 larafwlnnd fntaltilkq kqqstddefw sarvdmalrv ndkkeqlyal eqlkslgklg
      481 esdllqyqqi rfegnpkall ahlwqqssls esqlidianl stqindsnav ervynelnkq
      541 rynkalypaw ltlaswyqnq sdlnsayttl nraaklseyn pdvvlvqgwl alqmhdsimi
      601 krilnnyadn nptyawgqll aslsiyeksy nsayfylrkl aiaepsdltt lvnladvmkq
      661 lgyyanatel nhyllqhlpk dkyayrglmf rwagamamph lmqlntldel apetigtaqa
      721 nwwlsrraaq klepwqalql ymtqgefskv kqlfdtntlg kndqlsally lnqpyatmqr
      781 wyeelineps eaqlgflrna rtayfrafev nlspqaglns tqydinvyfp yakgqwklsl
      841 sdqqnlgnng llfaientmt fgrwafnakv dthqgdivsr qglsldsryq wdartqvgvn
      901 lqynaenrqs evllsyaqln katayinyni dnrqsvqlsa aamsftrrdn dstlvngqey
      961 naryqysilk drpiwnayfs aqwqdfdpvn taintnrrpr riviepfrrf algtsfastg
     1021 sltppylgas pswlfdistg yqtlndtidv svssgagwsv lgddlfklql gyqssnkvgn
     1081 sdtqlqlgyy ihf
//
LOCUS       WP_010555048             429 aa            linear   BCT 01-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Pseudoalteromonas arctica].
ACCESSION   WP_010555048
VERSION     WP_010555048.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..429
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47587
     Region          <2..325
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          38..60
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          61..83
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          84..105
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          106..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          129..151
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          152..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          175..198
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <244..>412
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
ORIGIN      
        1 mnnltelksg klvgatrlql veeltifpee ifsladtlev ldlsnnnlst lpdefaclth
       61 lkrlflsfnq fkhipkvlak cpalimvafk gnqisefaln slpkniewli ltdntlselp
      121 edfgnytqlk klalagnqlk qlpssmaqck nlelvrlsan nlthvddwlf elpklawlaf
      181 agndfnkaqc ltkcslenkp lddytlshvi gqgasgvihl aqaansavai klfkgaitsd
      241 gypldevncc lqagdhanli kvlayieqsd qlglvmelid ksfanlglpp sletctrdtf
      301 nddchystha ilkiaqqmvn tlhhlhvrkv shgdiyahnt minqnhdvlf gdfgaatnlt
      361 mlseyqqkql ewievralgc liedllgtvt gddkqselfg emsdmakcam qpslnqrptf
      421 telleelni
//
LOCUS       WP_010556129             357 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Pseudoalteromonas marina].
ACCESSION   WP_010556129
VERSION     WP_010556129.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..357
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41053
     Region          38..294
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(43,46..48,51,62,64,96,115..118,217,219,221..222,224,
                     237..238,241,256..257,260)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(43,47,51,62,64,96,115..118,217,221..222,224,
                     237..238)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(46..48,217,219,222,238,241,256..257,260)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mntqlldqak nvrqgeeldt qkvdawlkqh itqltgepsv tqyaggasnw tycleypeqs
       61 lilrrapkgt kakgahdmgr efklqqalkp vygyvpnmea fcddenilgt dfyvmekltg
      121 iiprknlprg ltptpertkk lcenvldclv elhkvdykqa nlshlgkgeg ytqrqisgws
      181 erftkaktwn vpsgkkvikw lennmpsner icithndfrf dnvvldandy tnvlgildwe
      241 latlgdplmd lgntlaywve pgddflaqat rrqpthlegm ltrkevvayy ckkmnitvgd
      301 ftfyevyglf rlagivqqiy yryhhgqtkn pafkhfwvfv hyllwrckka innqgkv
//
LOCUS       WP_010556171             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010556171
VERSION     WP_010556171.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..143
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15467
     Region          7..140
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mipyiydsld naliaelrkd grasisalad vlkvsrgtvq nrldrlvssg ailgftvrvh
       61 ehieteavra immvevvgks tsqviktlrg ipeltklhtt ngawdlvaei qaanlgefdg
      121 vlrqvreieg ilnsetsill sst
//
LOCUS       WP_010556100             603 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 3 protein [Pseudoalteromonas marina].
ACCESSION   WP_010556100
VERSION     WP_010556100.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 603)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..603
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65167
     Region          12..>435
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mpsikavakp alsleeklgq klmldfryyc eqgtgkhcrt pmtklpesla rvisdynigg
       61 vilfsentqs ieqtitlshq lqvaasksss klplfisidq eggrvarlpr diatsftgnm
      121 sigatykqhg vdfatksatv ianeltalgi nvnyaptidv nmnpdnpvin vrsfgenpqr
      181 vselgaaqva gfesngiits lkhfpghgdt hvdshtglpn vahskstiye qdlapfkhii
      241 akqnpgmimt ahiqypalds stfvsvegkt mikpatmsrt iitdilrgel nykgvvvtda
      301 ldmagisqff tpiqavintf lagvdialmp ieirtpddik kldelikslv havesnqlde
      361 qeitqsaari islknafels tefdpinavv naksiignkq hrkieaelal aaitqvknte
      421 ntlplnlndg qhihiimpdt rkcmamqqai esassssitf scsslqgfdp aqatqsikta
      481 diviagnatp nqsaveiggm ddlkddpnfa lnrreqpqal esllsmankf nkrtvfislr
      541 apydiakfgd yahsvlasya ynvdvdther vsgpaftala kvlvgqatan gtlpvtikpq
      601 kgn
//
LOCUS       WP_010556186             201 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Pseudoalteromonas marina].
ACCESSION   WP_010556186
VERSION     WP_010556186.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..201
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21633
     Region          120..197
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mrylvaliia gvvtfmlflg mqalitggeg amsepakgnv ldfvrlkkee svqkkerkpq
       61 kpptpkeppp pmespqmqss dananannfd fganvdaevn lagglalets dgeylpivkv
      121 apvyprrals rgiegyvive ftvtkqgtvr dpqvlkaepe slfdraamda alkfkykprv
      181 vngeavevag vqnkisfqig g
//
LOCUS       WP_010556211             126 aa            linear   BCT 01-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Pseudoalteromonas
            marina].
ACCESSION   WP_010556211
VERSION     WP_010556211.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..126
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14551
     Region          1..124
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mklsdfemdi mqllwqeepc tasqlhkvll adkqkdkqva yttvktivdr leqkgaierc
       61 glegraivfr tivtqdtlse qampsfmqrf fkgnsrslia hfikeeklnd edieylqtll
      121 knkkld
//
LOCUS       WP_010556337             304 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Pseudoalteromonas marina].
ACCESSION   WP_010556337
VERSION     WP_010556337.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..304
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34881
     Region          5..>152
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msiqvsviip nfnckqylak aissvvrqhn ieceiliidd gstdgsvewl nklqqslpnm
       61 rvikqqncgv vsvrnkaiel akgdyiafld addywtedkl fnqvtymqnn rdcvlsftny
      121 mhvneqyepi idcfsywpef tkfinwnteg yqnlkspmdl llfanvigts svvvkksaic
      181 yvgkfdqsln sasdwdcwlk larignvafs nqvsmgylmr agsitanrqn rltamqiiid
      241 rckndigvvs rfkakarmle cyseyyreig ykfkafclat aafllfphrr nlqhlvhdik
      301 qsik
//
LOCUS       WP_010556346             284 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Pseudoalteromonas marina].
ACCESSION   WP_010556346
VERSION     WP_010556346.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..284
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32291
     Region          154..256
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(157..158,191..192,195,199..200,203,246,250)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mkahifiiit lflsgcaswp degqggwaek yqnyplddeq kdlnytqpee vvrsefehlv
       61 lklellksqd ikacmpaqll kaqiyenrir rliaaqmwed aehdllihyh glnqltqhfd
      121 tvqkltqcav vkenkpalfs vkkqitdlln sdnqfafkaf eitpkyavrl aqaadlvkel
      181 esisillvgh tdsmgemain yelalkraet vkhwlvvygv pvqsittltq gslkpysdep
      241 qtdsvrhsdr rveaivldan tnnlqdnkak slvswtkiik skqe
//
LOCUS       WP_010556403             134 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Pseudoalteromonas].
ACCESSION   WP_010556403
VERSION     WP_010556403.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..134
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14683
     Region          1..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mylgsclcgk vnvkitgnit siihchcslc rknsgtafat ngfvnadefl itqgqdslsg
       61 yafkpgrtry fcaccgspiy sentsdksrf rirlglldsd iaekpishnf vtskanweql
      121 etslpchekh epgr
//
LOCUS       WP_010556444             404 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Pseudoalteromonas marina].
ACCESSION   WP_010556444
VERSION     WP_010556444.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..404
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44539
     Region          27..387
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 msnpnnvsln inhalefidg nalniptlsi ltedgdihps atapaiskht aiklyetmrf
       61 irlldermqg aqrqgrvsfy mqclgeeaav tasaaaldqe dmimaqyreq aalhyrgftl
      121 dqfmnqmfsn eldlgkgrqm pihygsneln ymtissplgt qipqatgyay gqkvkhidak
      181 tgelasiidn vticyfgega asegdfhagl nmaavhkapv iffarnngya istpadeqfk
      241 gdgiasrgvg ygiktirvdg tdalavfaat qkareiastq gepvliesia yrlgahstsd
      301 dpsgyrskde eanyktcpie kfkkwlvkqq wlneeddlka kesiredila alkraevvqk
      361 paleelvsdv ydtpipslvr qynelkehiq khpdaypvts grik
//
LOCUS       WP_010556486             271 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudoalteromonas marina].
ACCESSION   WP_010556486
VERSION     WP_010556486.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..271
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29335
     Region          38..246
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mttptainqt sqiepqraen tsnfllngth knkgeaiiev dslsfsiknn ailknlnftv
       61 gsgeiyallg gngagksttl ktllgfnkpt qgwvkvagke vskaldfvrg ktaylpesat
      121 lyphltaren vkyflsladi nktdeqinaa fnrvalqqaa werpmqtysk gmrqktaial
      181 ailreapifl ldeptsgldp vaidefnqlv relaltgati lmvthdvyga cqvanrigll
      241 ragemvgefd apengridte qvhaafaqrg a
//
LOCUS       WP_010556498             387 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein
            [Pseudoalteromonas marina].
ACCESSION   WP_010556498
VERSION     WP_010556498.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10505910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..387
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43492
     Region          <22..>288
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
     Region          <235..384
                     /region_name="EEP"
                     /note="Exonuclease-Endonuclease-Phosphatase (EEP) domain
                     superfamily; cl00490"
                     /db_xref="CDD:469791"
ORIGIN      
        1 mkfdltfgal ltaaslslna yatdtirvat fnvsmdatny takgepiksd alvkaltsnt
       61 qqikniaeii qrvrpdiill nefdfvpkek gidyfkthyl tvsqneqnai dypytyiapv
      121 ntglatefdl dndgkkskvm gdaqgfgffe ghygmailsk ypidfdkirt lqtfkykdmp
      181 nakmplmpkt genwynakew qalrlssksf wdvpvvidnk avhvlashpt ppvfdgeedr
      241 ngkrnhdeir liadyvanae ylyddngnkg gldaqsrfvi lgdlnaaaeg dkarlettdq
      301 llknplinaq fvpksagakq qyelayaqhf tanwqarvdy vlpstygldi keggvfwpve
      361 sneqyrlikd rsassdhrlv wldlvik
//
LOCUS       WP_010556502             241 aa            linear   BCT 01-JAN-2025
DEFINITION  SIMPL domain-containing protein [Pseudoalteromonas marina].
ACCESSION   WP_010556502
VERSION     WP_010556502.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..241
                     /product="SIMPL domain-containing protein"
                     /note="The SIMPL domain is named for its presence in mouse
                     protein SIMPL (signalling molecule that associates with
                     mouse pelle-like kinase). Bacterial member BP26, from
                     Brucella, was shown to assemble into a channel-like
                     structure, while YggE from E. coli has been associated
                     with resistance to oxidative stress.; The SIMPL domain is
                     named for its presence in mouse protein SIMPL (signalling
                     molecule that associates with mouse pelle-like kinase).
                     Bacterial member BP26, from Brucella, was shown to
                     assemble into a channel-like structure, while YggE from E.
                     coli has been associated with resistance to oxidative
                     stress."
                     /calculated_mol_wt=26350
     Region          1..241
                     /region_name="YggE"
                     /note="Uncharacterized conserved protein YggE, contains
                     kinase-interacting SIMPL domain [Function unknown];
                     COG2968"
                     /db_xref="CDD:442208"
ORIGIN      
        1 mntlklflgs aialstlsln afasstpdsp hiyvkgqatl ttmpdyaqms vgitevnkdl
       61 iaaknkadit makaiklvkt lgvkdtdina gqinihrntq ynrqtgqqef igfkitrtlt
      121 vkltdiskyp tllqslvnng inqinntqfl asnynelhkk aqkmaiqdak kaakelsddf
      181 dvslkglysa slsplnvqtq pymrakemvm adsapgnyvp dayhsgeikv tassyaiyyi
      241 e
//
LOCUS       WP_010556506             336 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Pseudoalteromonas].
ACCESSION   WP_010556506
VERSION     WP_010556506.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..336
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36358
     Region          1..328
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mgsitlkqvt knfddvnvik pldleikdge fivfvgpsgc gkstllrmia gledttsgni
       61 eidgqdatht ppakrglamv fqsyalyphm svrnniafpl krakvsaaei etkianaaki
      121 lnltdyldrk pgqlsggqrq rvaigraivr qpsaflfdep lsnldaslrv nmrleiselh
      181 kslattmiyv thdqveamtm adriavfngg iieqvgtple lyqhpvnkfv agfigspkmn
      241 fidvpngdtn gasslgvrpe hfiisqdtgt wsgkvgvieh lgsesflhvt ltngstvtvk
      301 adgdcslqyg dsvfltaqen kvhrfdkngv tikasn
//
LOCUS       WP_010556522             671 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas marina].
ACCESSION   WP_010556522
VERSION     WP_010556522.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..671
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74596
     Region          21..644
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mktlailtig tlysgyvhan iekltvyghr dgligesisa ssgiigqgei eqrpmlrsae
       61 mlelipgmav tqhsgsgkan qyfirgfnld hgtdfatsid gmpinmrshg hgqgytdlnf
      121 iipesistin yqkgsysasq gdfssagsaq fklvdnvkhq qielsigedn ykravvlgst
      181 nfkkgkliaa aewqgydgpw ddinedvnkk nallryvgka fngdlsisam aydntwnsad
      241 qipqravsqn litqlgsldt tlggsssrys lsgnwqgehl kasayvinyd lnlysnfsyf
      301 lndpingdqf nqqdsrniyg ttlsyqfetk tsginmqhta glelkhddid nvglyntkar
      361 eqlstvrqda lkqtsyssfw eskllftpkl eatagvrydy fdtnvtsita vnsgkasddl
      421 isfkaslnyr ftqllaayan wgqsfhsnda rgstinidpv tgdqaervdl lvksegaeig
      481 irfadekkyn msaalwwlkl dsellfvgda gntepsdask ryglemsayy windqfnidl
      541 easfthsrld indnnnyieg avpvvastgl nwhlskqwqs sirvrhigkr tltddgdkrs
      601 npltvvnssv sykqthwkvd fellnlfnst dhdidyyyas rlagepaqgv ednhfhpiep
      661 rtarltlsll f
//
LOCUS       WP_010556531             534 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Pseudoalteromonas marina].
ACCESSION   WP_010556531
VERSION     WP_010556531.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 534)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..534
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60396
     Region          <188..>277
                     /region_name="PRK10935"
                     /note="nitrate/nitrite two-component system sensor
                     histidine kinase NarQ"
                     /db_xref="CDD:236800"
     Region          <248..534
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mprkvhqssi rkalinliml itaiclslsi sistylsvke qkqlivsklv ilaeivafda
       61 gksvfeddrk teekrlkyfe ktplvknihv ysieqasqkp vffisfnakk tppvplrtds
      121 ieelktprit hedielikpi fhnekvvghv ymrgslesld dyikqkivvd illtllilvv
      181 vyfiainvqk riarpierls mllqdvsknh nydvrapvtd vkeisalsns lnimltrtqk
      241 qltrhekdke eikqlnqgle ekvnqrtial reanqellst lermhqyqtq ivenekmasl
      301 gqmvagvahe vntpiglgit sstllrdkla dlqisfddkk ltsnqlkrfi ddgienldli
      361 yrnlnraadl istfkkvavi qdddvttyin ihklitdvlt sisseleekk pvinincatd
      421 ltvesksepl qqvliqlitn sllhgfvgne nneiqfdvel tgkkltiiys dngqgvdkki
      481 khrifdpfvt skrgqgasgl gmhlvynlvt qalgghilid lekkrgarfi itip
//
LOCUS       WP_010556615             349 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudoalteromonas marina].
ACCESSION   WP_010556615
VERSION     WP_010556615.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..349
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38464
     Region          1..349
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msslilqgvs yhyngtkvie nldltvgkde ivcllgasgc gktttlkaia glveakhgsv
       61 fidgklvsde stfiapehrn igmmfqdyal fphlsvanni afglgkmsqs ekqqrvdeml
      121 qlvhlsgcad rfphqlsggq qqrvaiaral aykpslllld epfsnidtqv rfeliadirr
      181 iikaqqvsav fvthskeeaf afsdtlaimd rgniaqqgtp eqlfaaprsk vvaeflgqgi
      241 ylsaealtat eyktpfgtve sdmqtscypc sgelyvrphq ielvqecqsd klskratils
      301 rrfigsayvy kvviaeqtle veaqygqsfe ineqviikik phtvnffes
//
LOCUS       WP_010556716             162 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [Pseudoalteromonas].
ACCESSION   WP_010556716
VERSION     WP_010556716.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..162
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17431
     Region          1..147
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mvtftingkv iesqasedtp llwvirdevg lkgtkfgcgi amcgactvhl dgqatrscvl
       61 pvgavagkni ttieglnneh plqkawveeq vpqcgycqsg qimqaatlla dnpsptdeei
      121 vnhmngnycr cmaykriksa iqraadesqs avqmfnpneq dv
//
LOCUS       WP_010556751             369 aa            linear   BCT 01-JAN-2025
DEFINITION  arginase family protein [Pseudoalteromonas marina].
ACCESSION   WP_010556751
VERSION     WP_010556751.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..369
                     /product="arginase family protein"
                     /calculated_mol_wt=40355
     Region          55..367
                     /region_name="SpeB"
                     /note="Arginase/agmatinase family enzyme [Amino acid
                     transport and metabolism]; COG0010"
                     /db_xref="CDD:439781"
ORIGIN      
        1 msqeiqafns kvehclcapg dgvftvntak erkaalrnkl ygqtenvdtl wreslnelph
       61 sphkavmlgi ssdcgggilr ganwgplfvr salidqhpec hsfdlgdvrv iphllhdkyl
      121 ndatisncqk alygnenndy yvsplsited vcdsfyatfk dkgifgiggd hsisypltka
      181 ylkakreqgk rtaiihfdah tdllverlgi dlcfgswcth ileflpaphh liqfgirssg
      241 kpkshwentf gvkqhwahei iergaaavaa etiaqlkadn vdevyvsfdi daldaefasa
      301 tgtpednglt pkhaldilsa iadefpitga dmmeiapftd sslvgqasse ttlkegakis
      361 aflinamnk
//
LOCUS       WP_010556786             152 aa            linear   BCT 01-JAN-2025
DEFINITION  NfeD family protein [Pseudoalteromonas marina].
ACCESSION   WP_010556786
VERSION     WP_010556786.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..152
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=16595
     Region          4..151
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mdfiiqnlpq almvlgiial iievavlgls tiillffgls llitgfsmsi gilpdsltta
       61 lwsntvvtai laiglwkplk kmqnrvdtkp vtndfaeltf tldddvtdqg lttynysgis
      121 wklkseqtit agtrvyvmkk dvgvmwvkpv sq
//
LOCUS       WP_010556783             297 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Pseudoalteromonas
            marina].
ACCESSION   WP_010556783
VERSION     WP_010556783.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..297
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32757
     Region          7..295
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mteitthqas rrrllialai tcsfmiiqvi gayyanslav ladaghlfvh nsslfialia
       61 ssfaihlakt fndgyqrael mgglingily laislvilye ggerfihqhe gneleinsyl
      121 msviaglgfl fhgaaawvly kgrkasinvy avflhsffdl istvstfvag vliyftglev
      181 idilssmlia sfvlftgikv iiscikglrl nkaklpkvad ieseitsieh vhnvhnvtvt
      241 rnydglvvga hvvlkkhcti ekhdeacrlk venllaerfr vtssvlqies hechhih
//
LOCUS       WP_010556793             270 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Pseudoalteromonas marina].
ACCESSION   WP_010556793
VERSION     WP_010556793.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10563595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..270
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30943
     Region          10..184
                     /region_name="BMT5-like"
                     /note="rRNA (uridine-N3-)-methyltransferase BTM5-like;
                     pfam10354"
                     /db_xref="CDD:463056"
ORIGIN      
        1 mylnpnwril tvgdgdlsfs qaifehvkpn klvastydsa qtieqkypdn alkklressv
       61 nvlnnfdvts kacwqalksn nqyfdvvifq fplipafvgk eafeastrqs smnvlnrall
      121 hqfikyatef alnpngpmlc fitskdvkpy rewniegsln erlsstycgq mpfditrfsg
      181 ykirnvdrdk hvkdtsgity vfspksstle pqlakqltkp syltsnhcal crvgpfiaee
      241 dqakhfkakk hlqmlrlesd wqhwlntfys
//
LOCUS       WP_010556175             247 aa            linear   BCT 01-JAN-2025
DEFINITION  siderophore-interacting protein [Pseudoalteromonas marina].
ACCESSION   WP_010556175
VERSION     WP_010556175.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Valentino,H., Korasick,D.A., Bohac,T.J., Shapiro,J.A.,
            Wencewicz,T.A., Tanner,J.J. and Sobrado,P.
  TITLE     Structural and Biochemical Characterization of the Flavin-Dependent
            Siderophore-Interacting Protein from Acinetobacter baumannii
  JOURNAL   ACS Omega 6 (28), 18537-18547 (2021)
   PUBMED   34308084
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Trindade,I.B., Silva,J.M., Fonseca,B.M., Catarino,T., Fujita,M.,
            Matias,P.M., Moe,E. and Louro,R.O.
  TITLE     Structure and reactivity of a siderophore-interacting protein from
            the marine bacterium Shewanella reveals unanticipated functional
            versatility
  JOURNAL   J Biol Chem 294 (1), 157-167 (2019)
   PUBMED   30420426
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10153083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..247
                     /product="siderophore-interacting protein"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=27020
     Region          10..228
                     /region_name="siderophore_interacting"
                     /note="Siderophore interacting proteins share the domain
                     structure of the ferredoxin reductase like family.
                     Siderophores are produced in various bacteria (and some
                     plants) to extract iron from hosts. Binding constants are
                     high, so iron can be pilfered from...; cd06193"
                     /db_xref="CDD:99790"
     Site            order(62..65,79,81,83,87..90,127,226..228)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99790"
     Site            order(62,64..65)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99790"
     Site            order(87,90,93,99)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99790"
     Site            order(127..128,150..152,198..199)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99790"
ORIGIN      
        1 makkvrkatv lstqqitphl qrivlgseef tdltsdhigs yvkvlipkng vadfnlktac
       61 mrsytiqnvn ksngaitldf vinmhqgsat kwakaakvgd elaiagpgpk klenyqhshy
      121 vllgdltsvn aikgyikqlp inakidafih aptdadiisl dstrqatwli tttpeveman
      181 alttlqhyeq ppivfmalea glvrelkaal tnthsiprgn ivasgywkkg lnsenykler
      241 qankqta
//
LOCUS       WP_010556794             534 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Pseudoalteromonas marina].
ACCESSION   WP_010556794
VERSION     WP_010556794.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..534
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58006
     Region          3..532
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqsttfdyiv igagsagcvi asrlsedknv svclieaggg dksalvqmpa gvaasvpygi
       61 nswhyntvpq kalnnrcgfm prgkvlggss sinamvyirg nkhdydewek qgnmgwdyks
      121 mlpyfikaen nsafinnplh gvdgplyvqe lntpssvnqy flnacaeqgv plnddingke
      181 qsgarlsqvt qhkgercsaa kayltpnlnr dnltvfthch vkkiniknkt aqgvqitrnk
      241 qqieltanke vilsagains pqilmlsgig pkeqlklhni dvkvvlegvg enlqdhltvv
      301 plfkannsag tfgispkgal qvtkgvadwf skrngcltsn faeshafikl fkdspapdvq
      361 lefviglvdd hsrklhyghg ysihssimrp ksrgtiklan ngshtaplid pnylshqddl
      421 nimllglkkt laimnspafd eiradmvypl dinndqqlie firetadtey hpvgtckmgk
      481 demsvvdskl kvhgvnnlrv vdasimptiv tgntnapvia iaekaadlik aans
//
LOCUS       WP_010556796             331 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Pseudoalteromonas marina].
ACCESSION   WP_010556796
VERSION     WP_010556796.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..331
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36652
     Region          1..254
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnfvivgtnf isdtlldaan tladfnlygv csralssgea flakhpqnth aktftsieqv
       61 cqdecvdavy iaapnslhkq yavmclnagk hvlgekpsaa nsqelkeiia takqnqclym
      121 eammtthlpn ftllkqalsr igtprkyigq ysqyssrydk ykngerpntf lpefangalv
      181 dlgiyplyll ialwgapqsv nasgvildtg vdgagdvlln ysnkqavisy skisqgdnit
      241 eiqgelgrmr ieavsqlkkv efianngkse iiseqfdehf mkfevahfmq liekqqwesd
      301 vntfalsldv mnvldearkq lgviypndkt h
//
LOCUS       WP_010556818             682 aa            linear   BCT 01-JAN-2025
DEFINITION  S9 family peptidase [Pseudoalteromonas marina].
ACCESSION   WP_010556818
VERSION     WP_010556818.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..682
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=76105
     Region          <38..>265
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          <38..147
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          404..656
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mlktslalai glssslafaq saitvedipk vksviqtsis pdgesvaftr slprklyvde
       61 ngsnyselyv vddegverpf itgsvniksl qwsndsktiy flaklkddkf tslyqipvdg
      121 gqaqavmslk gtsissyqls pdnkqlalla mpaadksdke lkklgfkaev yelglknkql
      181 fvvdlakedk plsptainid syvsdvnwsa dsekllvktq ptaliddryt ksmwhlydia
      241 nekvtlsfkt qgklgdaels hdgkyvailg aedqhdpatg rlfiadteta kitewlpnfm
      301 ghvvdfewsh krntlnfian vgtqsfvasi kagsnkykkl vdegqfiatq lsvsdsdktl
      361 alrgnsakhp nevfivrskk akrltdsnsw lndkrfakqe tiklkardgv eldgvlvypl
      421 dykkgtrypl imsvhggpes hdkdgwvtny srpgqmgaar gyavfypnyr gstgkgvdys
      481 klgqndyagk efddlvdfkn hlvdmglvds krvgitggsy ggyasawgat kltehfaasv
      541 mfvgvtnqls kfgttdisne mhlvharsyp wdkwqwyler spiywagqse tpllimhgkd
      601 dprvhpaqsm elyrymkvqg kdvrlvyypg eghgnrkvaa qydyslrlmr wmdnyliegk
      661 kdmpdyeidh aaklkavkda nk
//
LOCUS       WP_010556803             469 aa            linear   BCT 01-JAN-2025
DEFINITION  serine hydrolase domain-containing protein [Pseudoalteromonas
            marina].
ACCESSION   WP_010556803
VERSION     WP_010556803.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..469
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53115
     Region          32..326
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
     Region          353..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          387..414
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <396..>450
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          419..449
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mvqnlvliff lffasyslal dsedikqdks vslatiadsi amqyqqmgwf sgallitkdn
       61 evefassygf qnveekikns iqsrfnlgsi mkdftkvlil qqveagklkl sdklvsfelg
      121 fkqpdadkit iehllnhsag fadifvaeyr qnqlafdtln kkikilinnp llytpgtdrk
      181 ysnygyvvlg vilekvtgkp feellknnif nwvemssttf rpvnsheyqs trytyqyngn
      241 lrkagvtehp spdggiestv vdvqrfyral fysdkllkns dainrhlfam dgshwgaygg
      301 glgvsaavev dldtgyeivv lantdhlvae risgrihsyi kngeyqpvkq leknfafkyy
      361 qskgkqqfyk hfkqvykdng ysrfigrtin evgmellstk swteafdmfe ylvslfpnap
      421 qaydslafay lskgdseaak stfsksltid gsfksdyvsd nyghdnmlk
//
LOCUS       WP_010556913             226 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Pseudoalteromonas marina].
ACCESSION   WP_010556913
VERSION     WP_010556913.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..226
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24247
     Region          3..226
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 makekvvlit gassgigeas aktlvnnghk viltarsedk laelveslge dnalsvpada
       61 tdftelenvv tkglkkfgrl daafanagmg vstagtekgd pdewstmidi nikallwtak
      121 atlphlrqnk ghfiltssaa grkpikgsiy gatkwfaygf gqnlaeemse wncrcttiap
      181 gmvntpffde akpdkldpqd vadavlfaie anqrnnvrei ylmptn
//
LOCUS       WP_010556978             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HD-GYP domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010556978
VERSION     WP_010556978.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12112208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..397
                     /product="HD-GYP domain-containing protein"
                     /calculated_mol_wt=44251
     Region          2..122
                     /region_name="DUF3391"
                     /note="Domain of unknown function (DUF3391); pfam11871"
                     /db_xref="CDD:432148"
     Region          <96..325
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mkklpvskll pgmfvqsvtk qtgrvkiksq gwvktqtsid klikagilev eidpdktlte
       61 tvpekeqtkt patkikrdpw qkthsaaqem nkakklydea ktlqikafkd iksglnidia
      121 pfkelasgfm dsvfrnqdal acltqmrqkd ayllehsinv silmgifakh lniekdiive
      181 lttgallhdi gkiktpdevl nkpgrlteae feimkqhavy skqileesgl tgiavdiagm
      241 hheridgtgy pfgkkgneis qyvrmasivd vydaltaerv yksgmepika fkilkegcpn
      301 sfdgelltkf iqcigihpvg tlvklssqkv glvtesnpam plkpivktfy sakhsrytev
      361 ldidlsnkri edslettvka gdfnidlerf yknsvlp
//
LOCUS       WP_010556968             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ketopantoate reductase family protein
            [Pseudoalteromonas].
ACCESSION   WP_010556968
VERSION     WP_010556968.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..300
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32816
     Region          3..296
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mtnilivgdg aiglllshfl shknnvhvlt rkptcntrfy srknapshni narfinlsdl
       61 aqqpsydvvi ftvkafqvqd afsqvkpyla ansilvvshn gmgnieelip qlntqqalyf
      121 lttsmagfks tqyivqhtge gqsviggcnk laaknsqfis pllqavpnlk vvnnieqlrf
      181 ekllvnvain pltalhnikn gqlrapvfsa timsllyegc rvanakglni aladaldnay
      241 tvmaltaeny ssmqqdiann rpteimaicg yisdqgkryn iktpinnell akiqakksvv
//
LOCUS       WP_010557030             709 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas marina].
ACCESSION   WP_010557030
VERSION     WP_010557030.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..709
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78125
     Region          52..676
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 madlsntqnt ylltplaffv gsifssvvfa edtsleviev qghsqnkhla lgsaesllnd
       61 lgvdfsaagg vsnlpilngl mgdrvkvlvd gadvtaacan hmnpplsyvs anqitayhvi
      121 agisavsagg nniagvisvn tispqysqsn elnwhsgyvs aqynsvnnar kvgvgarias
      181 ntlsfnyqga fsdaksyddg ngdlvldtly rvqnhalsaa irdekqqfvi klthqkipyq
      241 gfanqymdmt dntsygataq ykrvlensel eaqlnwhdvk hemgffsaek tgmmpmntda
      301 sdissqikwr lnlgsnssll lgqafydyri ddwwsavegs ammgpndyin inngqrkria
      361 afaefesqin tklwlnsgir vehvntradd vqpynegmam mamsampmqp snasaaaafn
      421 skehdksdtv vdisvllnyq lthtdelqlg larknrapnl yeryswgvsn mattmigwyg
      481 dgngyignqn levetahtis styiksaqnd dwqvsaniwy tnasdyidad lvrsfnrfgl
      541 entarnilkf tntdavlygv kldlaanihq skalgnwqln anitntrakr ddtnqplyqi
      601 kplytkleis qqlgrfentl swqwndaktr vdnnrlenqt dsynivnlgs kaswgdltls
      661 aqvsnlfdey yqlplggvsi aqlkkgestg feqlagqgrs fnigmsvaf
//
LOCUS       WP_010557047             307 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudoalteromonas marina].
ACCESSION   WP_010557047
VERSION     WP_010557047.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33811
     Region          8..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,192,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mkvsfeqlks mvvfaqiveq gsltgaakql gltravasyh lkkletqlev tllnrstrtm
       61 tlteagiayy ercrviteqa naanqqieni ksepqgllkv scpvnvgmql ivpaintfkr
      121 qypkieidlq ltddvvdiik ngfdiairgv alsdsnlqat klttmstcic gssdyfnyfg
      181 kpktpaelka hkwvvyqlgs ktltlqkegk khditmqggl stnnaaarta fveaghglgr
      241 iplydawpkv qaglleiild dyktkdiely gvfppgatgs kklrlfidyl kayfvkqhta
      301 lgmlkst
//
LOCUS       WP_010557092             532 aa            linear   BCT 01-JAN-2025
DEFINITION  BCCT family transporter [Pseudoalteromonas marina].
ACCESSION   WP_010557092
VERSION     WP_010557092.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..532
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58176
     Region          19..530
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mndmtkkysi dttdyqvgqd niqkwgfdih npvfgisafl vvlfvllslv fdptvtrdal
       61 tstkdaiinq fdsyfmllan afvifciila fsplgkirlg gvkarpdhgy iswlamlfaa
      121 gmgigllfwg vaeptayytg wyhmpmgvep nspqahslal gatmyhwglh gwaiyavvgl
      181 slaffafnkg lplsirsvfy plfgdrawgw mghiidilav lstlfglats lglgaqqats
      241 ginyllgtdy gtafqisvig lvtciaifsv irgieggvkv lsnvnlicaf flllvvivlt
      301 fsdsipavwf tlgayvehfv plsnpfnrpd edwmhswtvf ywawwiswsp fvgmfiarvs
      361 kgrtvrefll vviglptlls lvwmgvfgnm aitqvidkvg plgqngltdi svtlfqvyeq
      421 lpfssfisii sialvlvffi tssdsgslvi dgitaggkid apvpqrifwa tvegmiaavl
      481 lwvggsqalq alqsgvvtta lpfsiililm cvaliqglls eyptykvqsk lh
//
LOCUS       WP_010557157             476 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar porter family MFS transporter [Pseudoalteromonas marina].
ACCESSION   WP_010557157
VERSION     WP_010557157.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..476
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50061
     Region          26..467
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(38,156,159,163,284..285,289..290,293..294,391,
                     395..396,400,423..424,427)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 mtspispssh ssahtlgtcs lfyvifisav aaiggflfgf dsgvingtvs algnafnsss
       61 vatgfnvasv llgcavgala agpladkfgr raimiitaii faisafgsgi sessaefify
      121 rlfgglgiga asvlapayia evappalrgr latlqqlaiv lglfaaflsn yliadaagsa
      181 qnilmldiaa wrwmfwvelv pailflvgvl fipesprylv aqgkvddakt vfskisndsa
      241 daqisdvnss lhsdkkpsir dlfidgskkv hpivwagval svfqqfvgin vvfyygselw
      301 qaagfdesqs lfinvlagtt nivstfiaia lvdkigrkpl llvgsvgmfi slsaltyifg
      361 sagldeagkl alsdnmgtfa limanlfvvf fglswgpvvw vllgemfnnr irgaalavaa
      421 saqwianfai tmtfpimlan iglagaygfy alsalisiff vakyinetrg ktlesm
//
LOCUS       WP_010557221             348 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010557221
VERSION     WP_010557221.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 348)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..348
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39516
     Region          <158..345
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mnnavslshs aqylkkavpm mvkyrmpvtp inyaiwycyf qgnkpslnie ldqvisehqt
       61 ctqskakeif dkhlsdedla lfqemsdkfh ntveniqqdi sitlghsksf stslidsqne
      121 inslidtnsf ndilgcverl tdesiamqds arefqtklsv ayneikdlke alnlskeaad
      181 tdpltgfynr gkfdsdindf creyseqtte sslaalimfd idhfkrfndd fghqkgdevi
      241 klvakkvken ltdkakvyry ggeefcitay fdtindlvaf aecirqeiak lairkkqdvn
      301 nkraisasfg lamlrpftks svlveradra lyiakthgrn rveiapdi
//
LOCUS       WP_010557288             791 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Pseudoalteromonas marina].
ACCESSION   WP_010557288
VERSION     WP_010557288.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 791)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..791
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86233
     Region          4..88
                     /region_name="ATPase-cat_bd"
                     /note="Putative metal-binding domain of cation transport
                     ATPase; pfam12156"
                     /db_xref="CDD:463475"
     Region          91..790
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msnscfhcle svpkgfsatv tiddtpqpmc cigcqavaqn iveqgmtdyy kyrtvsagkv
       61 eqlvpeqlaf iksydnediq defiatsnni sevllsvegi tcaacawlie kqllslntvk
      121 rvdvntstnr amiqwdktat plsdvitala kigykaypfq adteaqqkqq takayirrlg
      181 vaglmtmqvm mfafamyfgm fsgmdsnfeq yfrwislvla spvilysalp fltnainglk
      241 akqlnmdlpv slaifgayga scyatvmqvg evyfesicmf tfllllgkyl efrarlkase
      301 ytanlqkllp ltartltdsg eeliiaakkl klndvvlika getipadgel ikgkttvdes
      361 mmtgehqpvn kfighnvyag cvnhdgviei kinkigqntl lnqiirlqhn altkrpklve
      421 itdkvaqgfv acllvfaslt aigwyqidpe hafwitisvl vatcpcalsl aiptaltcai
      481 asltkkgili kqahvletls kltlfafdkt gtltqgkfsl devdiidnsy skddvmaiaa
      541 ilerfsehpi asafdgytpa khslhnievh aglgisaqde tthyaigksg wfdskktnaq
      601 aslyinkhvv arfyfvdkvk hdaqsliksl haqqltchml tgdasdagkk vakqlnldsv
      661 qsgcspqdkq taveafssqn evvamvgdgi ndspvfasah lsiametgad isknsadvvl
      721 lnsdlasidh llniakqtrr iikqnltlsl lyngsilpla alglvapwma vigmsassii
      781 vicnslrllk l
//
LOCUS       WP_010557327             450 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Pseudoalteromonas marina].
ACCESSION   WP_010557327
VERSION     WP_010557327.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..450
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49873
     Region          12..425
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mikktnkgly trlikgvsan aygqaitvlt qlvsvplfih ywgmvsfgew lilsalptyl
       61 amsdfgigai asnrmvtkna qndnkdvist fhsliafnlv msslififvl flfgimnisd
      121 nigistidrl evthivlvlt iqvlfgmqvn vlcaayrsld kyaegtflsh ttrltewlfa
      181 igaliigggi lsfaiaglfg rivgylvmym rlintsksfs lsikdanfgi ikemikpgla
      241 fmsfplglal siqgmtlvig svlgavavaq fnvlrtlsri ivqmvtmvnq aiwpeitkaf
      301 alldyklmkk lyigasryal yigficvfal ilvddflfsl wlgddfvysv hlfylllgaa
      361 llninsqssw lvlmatnnhn rfsiiflfts fcsvifawll fpiagleaaa iaivlaesfi
      421 lffsvveank viqsslqryv mdvfnlrlky
//
LOCUS       WP_010557356             508 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Pseudoalteromonas marina].
ACCESSION   WP_010557356
VERSION     WP_010557356.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..508
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55731
     Region          1..507
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mnklplyekv gyamgdagan lvwrgalayl avfytdtfgi saaaaamlfl vvrlsdgvtd
       61 iimgmiadrt qsrfgkfrpw ilysapflgl fmvlcfttpn fndtnkliya yvtyigltla
      121 ytvsnvpysa lmgvmtpddt ertklsgfrf agaftggllv mgflpdlvay fgggdnakgy
      181 qltmylfasl lialmvitfv stkerviata seqgclksel fdltknlpfi ilpllsttlf
      241 fyyrdlysgl ffalvmaamt vvikkllnkn kqnltgsqrd mvdlltnkpw lvllgigflt
      301 mmfngikygv iayyfkyhvg nelmagqyfi allivsifga latgklaeim gkrnlfiasl
      361 llsgllttaf ywvpsnniva vftfgcaaef faammptlff smlgdsadys ewknkrratg
      421 liysagtfvq ktgggfagal vlvvlasygy ngmdeltinq tlpamqllms wipaafaflg
      481 aalmliyplt paitqkited lairrsnv
//
LOCUS       WP_010557406             440 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Pseudoalteromonas marina].
ACCESSION   WP_010557406
VERSION     WP_010557406.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..440
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48631
     Region          1..405
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mhftdlgidt rletqlahqg itqptdiqah avptalaghd ifaqsktgsg ktlafllpav
       61 qrvmkqkals krdprvliva ptrelatqvf tqlrlliagt aikavkvlgg enfndqikal
      121 rndpqfvvat pgrladhvtk rslqlsglel lifdeadril dlgfteqlkl indeanhrlr
      181 qtllfsatld haqvdalsrn llkkpkqitl saaneqhsdi tqtlyladhl dhkeallahf
      241 lkqdevgqci iftatradts rlseelnnkg fksvalagdl tqskrldimd sfsrenfkil
      301 ittdvasrgl dllsvthvin fdlpkhaeey vhrigrtgra gfkgtaislv gpkdwasyla
      361 iksflndelk fatidglkak fkgikekkpa atvkakkvtq vkkpqikrka kpkkpaapik
      421 apmnidgdsp mrrkkkpeqe
//
LOCUS       WP_010557439             290 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudoalteromonas marina].
ACCESSION   WP_010557439
VERSION     WP_010557439.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..290
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32468
     Region          10..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,213..218,
                     224..225,227..228)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 marwdgidef iavgeegsft aaarilglsv ahisrhvtal eqrlntqllt rttrkvvltk
       61 egeiflhqik hlqhamddat qglashqttp kgkikltapv mfgetfimpi vhnfmhdhpd
      121 vevianlsne qedlldggfd lairlghlkd sslkarrlse rrfimcaspa ylrrfgepht
      181 lgelhnhqcl vgnssywrvn enerekhiki agrlhcnsgw alvdgakkgl givqlpdyyi
      241 dnelnsgelv piltsyqpkq egvwgvyppr qfvatnvrvl ldylvaglke
//
LOCUS       WP_010557526             295 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Pseudoalteromonas].
ACCESSION   WP_010557526
VERSION     WP_010557526.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..295
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33097
     Region          2..292
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mhnhshshqh gkddrigwaf flnviftiie figgwltnst aimadavhdl gdslsigfaw
       61 ilsrfsdkea sdkfsygyrr ltlfgalvns ivliigsiwv lfeaipklsn pempvvegml
      121 glailgvavn gyavfklkag etlnekvltw hlledvlgwv avlivsivll fvelpildpl
      181 lsigftlfil fnvfknlkst lvlflqaapd ketqerikqs lnefpevngi hhmhfwsldg
      241 eshvltahle lsdnfdvkel iklkqevaak lssyhlshtt iefeflnenc rdeae
//
LOCUS       WP_010557561             218 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Pseudoalteromonas marina].
ACCESSION   WP_010557561
VERSION     WP_010557561.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..218
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23804
     Region          18..216
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 maettlspal qilsgqcrdf itslkhadva hdithiervv rvaiqlceae nanmaivlpa
       61 awlhdcvava knhpdrakas tmaavkaigf lkglgydanl fdeihhaiaa hsfsanikik
      121 tleaqivqda drmdalgaig vsrcmkvggs igrllyspdd pfcttrepdd kkftldhffi
      181 kllniaksmn tpsakaeaqr rthymhafle qlkseige
//
LOCUS       WP_010557605             437 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudoalteromonas marina].
ACCESSION   WP_010557605
VERSION     WP_010557605.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..437
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49542
     Region          5..437
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mlvhyidlsw rsfkrtplvs flmvlaiaig igitmtslsv yhmmsadpip hkssqlfsvq
       61 lqimddgstw wtsdnqplql tyqdaanlyq sqvgaqrlkm vrsgfsvyid sdkvkpfsqs
      121 arlttpeffn mfdleflhgs kwsqqqedna apvvviseel nnklfagkns vgqviyldda
      181 syevigvtkn wpltikyydl nngafnqpeq lfmpfsllea kqlgnwgntn gwkhedvrsf
      241 taklqsemvw iqfwveltte qqkndyenyl laymqeqqkl grfnrkelaf glrdvnqwma
      301 ynnvvsednk ilvalsfmfl avclanilgl llakflrrap evgvrralga nkrqifmqhi
      361 ievamlgllg gllgivfaqf gllgvrqsyn yyeslatmdl smllsaplia istcviagly
      421 pawlvcktnp aiylksq
//
LOCUS       WP_010557621            1049 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudoalteromonas marina].
ACCESSION   WP_010557621
VERSION     WP_010557621.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..1049
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115794
     Region          8..1028
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mstsekglia wfarnpvaan limifilvgg lltaltirkq afpqfesnwv svqavypgaa
       61 pqeveegiti kieenlegle gikrfitysn rgyaqawiei eekydlqeal deikaqvdsi
      121 nsfpagmerp iiqrdkfqqe vmfialygdm tyaqlkelgt dledellalp gvnlvsffsg
      181 lnyeigieis pdklreyglt frdvsnavrn fstnmsagqi rsdngyismr vekqaykgne
      241 feqlplitla dgaqiylgdv atindgfeeg llyskyngkn slmfdiaask dqditdvakv
      301 lknymaekes klpqgvkltp mvdltyylqg rldmmidnmv wggvlvmlvl alflplrlaf
      361 wvmmglpvsf lgaflfmpig flditinmvs lfafiivlgi vvddaivvge sasaeiekhg
      421 hsldnvirgv krvampatfg vlttiaaflp qamasgpgaa fskaigvvii lclifslies
      481 klilpahiaa mnprkpnpkn plhkvrmvvd kglksfvqny ytpfighcih yrytviigfi
      541 cilimsagmf agglvkfvpn pkiqhdfprv vvemnlesse qatletakki eavllsvdee
      601 leaqygqkmi rdlsvslrgr ttaqlmavli epdkrpidtf tlsslwrekl pplpgvktlt
      661 iednlfgggr ddgdvsfrlq gkdtdklkev asllktklqs megvgdvnds lqsatdevql
      721 dlkplaysmg ltladvasqv sfsyygleaq rilregeeir vmirypener nsisnihstr
      781 iitptgvevp lsevaqiniv dgvnrirren anrtvnvwaa intdkvepfa ivkeitdeyl
      841 ptllqnypgv tsnvagrvqe emesadeqlr dfaislmiif allaiplrsy sqpliimsvi
      901 pfgvvgamfg hmvlgmtmsg lsmfgiiava givvndslvm vdfvnkarae gvpikeavmq
      961 agarrfrail ltsvttfigv lpiimetslq aqivipmavs lafgvlfatv itlilipcqy
     1021 valedtkrmi rkwrgkhpiv dgqptttns
//
LOCUS       WP_010557681             342 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Pseudoalteromonas].
ACCESSION   WP_010557681
VERSION     WP_010557681.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..342
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37847
     Region          1..246
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 makvnwgiig cgniahtfak siahcadaql igaastseqr anefathysi kgyesyqalm
       61 qcpnidaiyi anthdqhfqs iaqclmhnkh vlsekpitvn aqqlknltal akqkncflme
      121 gvwmrflpai ikleqllsea aigkvhtvqa nfslpgtfan thrlmnpnta ggalldlgiy
      181 plsiadvvfn kapekissfv hkadtgvdar nitmldygng qfaqlssale qngpteacit
      241 geygfiripw fvgakglelh ingqaiqhfd ypfsddenfk feidhvteci lnkqiqssil
      301 plstslrvmt mmdslrdqwq ieysatvesh dinkntrnkd tq
//
LOCUS       WP_010557481             173 aa            linear   BCT 01-JAN-2025
DEFINITION  EF-hand domain-containing protein [Pseudoalteromonas marina].
ACCESSION   WP_010557481
VERSION     WP_010557481.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Persechini,A., Moncrief,N.D. and Kretsinger,R.H.
  TITLE     The EF-hand family of calcium-modulated proteins
  JOURNAL   Trends Neurosci 12 (11), 462-467 (1989)
   PUBMED   2479149
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11473824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..173
                     /product="EF-hand domain-containing protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18996
     Region          26..157
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
ORIGIN      
        1 mkkltlatti latlslaaca snqgldkids nfasldndsd gfiskveadd dniwghfsni
       61 dtnmdeeisr kefnaymqln tgkvatdsdv sesafkaeia kfdkiessfa sldndsngyi
      121 svvegndddi snhfgymdkn edkrisknef mgyinkygks vaedealesi khs
//
LOCUS       WP_010557732             418 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Pseudoalteromonas
            marina].
ACCESSION   WP_010557732
VERSION     WP_010557732.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..418
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46192
     Region          96..384
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mtnthiqeli apwfenvpda affsaltata igicslfvvy lftrrlmlpg iqkvvtklsp
       61 erigalspml tklnkriagl lccvlflatf dsfypvgela aeilktigqa lliiytgfii
      121 ssivslaaai ynqldfarev piqglvqvvk litfivcgil ivsivleksp tyilsgfgai
      181 aavtllvfkd tilgfvasiq iaanrlvtyg dwiqvdnyga dgevidlgln tvkvrnwdnt
      241 ittiptymlv agsfknwrgm qesggrrikr slnidmnsic lvndefraqi daaiplheyi
      301 rvsalpepvs nlglfrryae gylkqhskin ssltlmvrel qplnhglpie fycfsedkrw
      361 isyehlqaei mdhllavlpi fglrayqsvs gqlspptnag qtekpsikvp nnvvqdph
//
LOCUS       WP_010557767             147 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Pseudoalteromonas marina].
ACCESSION   WP_010557767
VERSION     WP_010557767.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..147
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15784
     Region          18..147
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 msiwyqpitl alckqldegi ngqgtlmktm gieiteigdd ylvatmpaip ahhnpigmvh
       61 gganvvlaet vasyaanfvv dftkfycvgq eisashlkas rngtltatar afhigkrssv
      121 weikitnsrn elccvskmta avverka
//
LOCUS       WP_010557791             398 aa            linear   BCT 01-JAN-2025
DEFINITION  dipeptidase [Pseudoalteromonas marina].
ACCESSION   WP_010557791
VERSION     WP_010557791.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..398
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43591
     Region          36..394
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 miklstlvva vslaltnqaf aeqpvsasdk avklakdtil idthidvpyr ihdtwadvtk
       61 atndgdfdyp ravkgglnap fmsiyipahl efegkgksyq lanqlidgme aiaqrapakf
      121 amasstndie qqfkdgklsi amgmengspi egdlknlqhf fdrgvryitl ahsqsnhisd
      181 ssydirrkwk glspfgkelv tamnnmgmli dvshisddaf yqvmelsktp viashsslrk
      241 ytpgfernmn ddmllalkkn ggviqinfgs sfvtakagaw gkqlkstkes akkqgtklsn
      301 dfdaayrakn pypfaslkqv ldhidhvvel igidyvgigs dydgvgdslp iglkdvssyp
      361 nlvqglmdrg ysggdikkil sgntlrvwkq aeayakkh
//
LOCUS       WP_010557821             358 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein
            [Pseudoalteromonas marina].
ACCESSION   WP_010557821
VERSION     WP_010557821.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..358
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41358
     Region          2..321
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mltllavttg ffllvtllpm sysqhylvrs cdfvrlqvly iagfifassl fllwlnsdth
       61 yiyitlasvi imvlqgkwif pytwlakkev qsasknsehs irimsanvlm snhnseqlia
      121 lvnqhkpdll itlesdswwe eklsvlkkdy phyiecpkdn rygmhlyskf klldaqicel
      181 ieddipsihi lfendeglem qghfihpapp spteedssrp rdselimvak avkkptrpti
      241 vagdlndvaw srstrlfmqi sgfldprkgr gfyntfhagy ffmrwpldhl fhsqgfkvkr
      301 ierlakygsd hfalltelsy enasqqsled kpdelkqeev aeltmskadk rkvprfek
//
LOCUS       WP_010557864            1027 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Pseudoalteromonas].
ACCESSION   WP_010557864
VERSION     WP_010557864.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..1027
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112706
     Region          30..1026
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 miawftknhv aanlllvtll lsglfslssk iplevfpsfe tdmisvgvsl rgatpedveq
       61 gvtirieeav qdlegikqif srssegsgsv tievesgydp relladiksr vdaintfpgd
      121 aekpivalae rkreviavtv ssdygeketr eyaetvrdqi lrlpnvtqve lsgvrdyela
      181 ievsqdtlrq ynlslaqiss aiansssdis agnlkteggd vlisskgqay rkdefasivv
      241 knqadgtiir lgdiatikdd feetpvrtrf ngkqaafidv yrigpqsait vaddvknyie
      301 eqqatlpqgf klsywdddse lvksriatlt snalqggilv lalltlflrp aiafwvfigi
      361 pvsfmgafia mpifgvtlni mslfgfilvl givvddaivt genvythlkt aksgeqaail
      421 gtqevatpvt fgvlttvaaf lplafiegar galfaqipvv vipvllfsli eskfvlpahl
      481 kyiklrhqkg epskleaiqq rfadgfesai lkyyqpilnt alrhklatvs lfvgvffiil
      541 tmitsgwtkf iffpripset vrvnltlptg tpfevtnkyv idmsekaqql qdkyrdpdtg
      601 esvilnilat tggrggvsns gavrfeitpa ekresdigsr elasewrdli gvipgaeslt
      661 fraeigrssd pidvqlsgts ltilqdvadn iknrlatypt vfdiadsmsd gkeelrielt
      721 qqglalglnr vnvagqvrns ffgsqvqriq rgrddvrvmv rlpiderrsi adlqnilint
      781 pdggsvplsh vatltagqsp stinridryr tlnvtadiek nntnmtvlqa dlaqyldelm
      841 qqypgvdykl egeakeqres fgslawalvf vffiiyalla ipfksymqpi ivmsvipfgm
      901 igavvghwim gmdltimsll gmlaligvvv ndslvlvdfi nkkrseggdl ieavklagas
      961 rfrpvmltsl ttfiglmpll fekatqaqfl ipmavslgfg iifatfitll lvpvnymlme
     1021 rfqgwfk
//
LOCUS       WP_010557881             813 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas marina].
ACCESSION   WP_010557881
VERSION     WP_010557881.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..813
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88980
     Region          51..792
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mrakksilsl avslamttgl avsaqvnaaq eqvnqtqaeq eqqnnkndsf ekivvtsqkr
       61 tqslnevpva vsvlnsdqin safannmegl qslvpsvsfr kgtttrnsal tvrgigtisf
      121 siaaepsvat vvdgvvlgrs gqafadlydv drievlrgpq gtlfgknasa gvvnittkdp
      181 sydttgsiet sfyqdneyrf kgvvsgglsd dlaasltvfk gkfdgyidnv ynnekvngyd
      241 regaravfky eptddlnvkf iteyynaddd ccadlealps grnpdskaap nsngivdgva
      301 didldqrkvd hdyesrtidk hsafsvqvdk tigdhtytsi taqrswdnte fregdftsia
      361 gdsnqpvfgv pfqlhdigeq qwdqfsqefr vtsnlsgpfn yvaglfywnm dsqrnftrda
      421 scqnnagqld samafyaqnn lsgaeldaal adldgyaqgl gvscnandiv sataymstef
      481 nnwaafadgt yelsddltml fglrytddev sythrrvsnd vygrrgvgvr patlntdeqg
      541 kaeetnvsgr lgmqydlgdg qmvygtysqg ykgpgfniyy nfnpdndgre iapeesdafe
      601 lgykyassdf vfnfavfkte iegfqannfd csdgtcitrl tnagdvstqg aevdfmwaat
      661 daltltggia yikaeidefn cppevaagsc tdrsgldvpf spdlkyslsa dyfietehgf
      721 nvhvngsyiy tdeqysdlpn nvgefnpaal lpdygilnas vglsfkddaf rvsliaknlt
      781 desyattysg dnfryqiprd aeryfgvsfk arf
//
LOCUS       WP_010557901             519 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Pseudoalteromonas marina].
ACCESSION   WP_010557901
VERSION     WP_010557901.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..519
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=58909
     Region          19..511
                     /region_name="YdbT"
                     /note="Uncharacterized membrane protein YdbT, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3428"
                     /db_xref="CDD:442654"
ORIGIN      
        1 msdftphttq tdagqvqlwq kvspwallyf vvhfgvrfvr dgifnllplg fvfvtqvenk
       61 lfwgqiaaav avsalllysv lyyrnfrfci ssdneillnk gvfkkerltl kfervqnvni
      121 aepfyfkpvt lvncifdaag saaqeavlpg vtqgyaeqmr kqifaykaqq qlepdsevet
      181 deateqsslf isnkeiakfg lmsnmailal aaiaplinvv advlekqlit kvegfyeqel
      241 glvasaalfa iftmfvlvvl iavllsvgms lirfynyqly fkgkkfkria gllerhqlsm
      301 sldkvqsivi kqniiarllk rftveflqas sggamagmaa kknkqtlvlp vlnneqvnsv
      361 cqwiypwfnn salafkqaer alwyknlvly allpsllvav fcyfnefnyf islgvlgvfa
      421 glvtlsyqry gyylheddgr fymvvrkgmi gvhyrvfely kvqsassest ylmrrsglks
      481 lyiqlahgfa fmpyikeqda dfvidftlkq aesdtrswm
//
LOCUS       WP_010557927             230 aa            linear   BCT 01-JAN-2025
DEFINITION  pseudouridine synthase [Pseudoalteromonas marina].
ACCESSION   WP_010557927
VERSION     WP_010557927.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..230
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25754
     Region          3..212
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 msnkirlaky iahagvcsrk qasrlidegv vtvnnrpanh idhvdeqddi ivngqvvkga
       61 adlvyfayhk pvgidcklne ndpaslihhl ptltrvypig rldkdsrgll iltndgdfcn
      121 qlihpdfhqp kryivtvnkp innafcekma agipvdkqit lpcevtkiad nqfsiilkqg
      181 lnrqirkmah ycgfkvidlf rvqfselals nlnlpenhsi qinktdiski
//
LOCUS       WP_010557946             692 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudoalteromonas marina].
ACCESSION   WP_010557946
VERSION     WP_010557946.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..692
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77407
     Region          9..692
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mklsslyial latittntya nstdlehiev kgsffndykv dnangamrts tslldtaqsv
       61 tvisdiiine qlattlgevl sndasltags kqrnrevfnl rgfelssstg ylrdghqhws
      121 hyqqpieilq qvevikgpss ilygqsgpgg linmvtkkpt aqtlfnasad vdqhgstrfm
      181 ldasgaltda edlrargilv kqdvdywrey qngenrerdr flgafivdyd isdnalvrvh
      241 ydrtddeagl dtgawiddna nvigddktir dmswaftdit venagidfkv flndnwqvkl
      301 gyneqtferq rfesaprkpg nyvegdsyes rpydrfddwq fktafidfig efetagvhhq
      361 lligansldy yygqrrtsad sfnfiagqae pnrptvsykt ddtiseteyd yygiyvqdli
      421 tfspqwqlsl ggrydkqtre dannesfvpk vgvlyhpnas atiyasyseg fepqgsdtlv
      481 neddinngmk ldavtseqke igvkwqlfdd rlmlsgalfd iskngtlvte tldvpvgdli
      541 setnqigeqr hkgveltaqg aatdrlfvma stmyldanye rdedlegkrp tdapkwsasl
      601 wtryelndai afnagafyeg erfadsanti tkdaytrvdv gatyklkvsk tdvnlrlnie
      661 nlfdedylag ggtnnvtige gtnvrlaaqf sf
//
LOCUS       WP_010557957             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudoalteromonas].
ACCESSION   WP_010557957
VERSION     WP_010557957.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48409
     Region          17..388
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(24..25,28..29,32,65,115..116,118..120,123,145,
                     148..149,152,221,224..225,228..230,233,260,264,308..309,
                     313,317,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 mtasslnsre kraavslasv fafrmlglfm lmpvlaiygq sldgfspiwi gfaigayglt
       61 qavlqipmgr lsdkigrkkv iigglvvfai gsviaalaes iqmvtvgral qgmgaiasal
      121 lafasdlsrd eqrpkvmavi gmsigmsfaf amllgpivaa swgvagvfwl tailavcgif
      181 iitflvpkav nkapkgdtla sfsdikklik hpqlarlnag vlllhltltt ifvvlpsqli
      241 keglaaeqhw ylyipvllla fllmvpimiv aikkekekqa fissvalltv smlamsvwin
      301 svvgiaicml lyfvafnfle atmpalvsrl apasqkgsam ggysssqflg aflggilggy
      361 vaqtistqav faaaalvgli wlvvawkmev ppkskvislm tklsteehaq tlasqlvalp
      421 gvieatvvrd esrsylkind kefdldqark vagli
//
LOCUS       WP_010557985             356 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Pseudoalteromonas
            marina].
ACCESSION   WP_010557985
VERSION     WP_010557985.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..356
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=40802
     Region          17..317
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mnntvqntls kllklnpett qlstissghi nstwllthfe qrfivqklnt hvfkypaqiv
       61 snaqlieqhl ntkqkqnnyp ldivkhistg nnayltmlne epyrvlnyie hsysedvvkn
      121 peqahqaala fgtfasalhd fdtatlhtvi ddfhnlamrf eqlktamths desrlnrskk
      181 diefclsqqh lvdelkaitq hlpirvchnd tkinnmlycs kthkakavid ldtcmpgfll
      241 hdfgdmvrtf ccaeaedsts ldkvvirkev fealvkgyla plkpilskqe qlslllgaki
      301 mplmlsvrfl tdylnndvyf ktahpehnlv rtqnqlalyk nilvneawmy ktlmkq
//
LOCUS       WP_010557999             347 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Pseudoalteromonas
            marina].
ACCESSION   WP_010557999
VERSION     WP_010557999.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..347
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39391
     Region          2..292
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mllkglilgl ccfcgqiaaq esvtlqlkwt hqfqfagyym akekgfykdv gldvtinpad
       61 ltmpdafsav angdaefgvg hsgilqerin gqsfvamapi lqyspycwmv kdtsdifhpr
      121 dfvnkriskv shndsnelma mltrsgvntr llsvyngdnp sqawienrld amqvylstep
      181 ynmtqrgish rlicpqrygi dvyadilytt gemlstspet vekfyqaslk gwryammnmd
      241 eaiavtqily apnksfhela yeaevlkeyi mpattslghm sipkwrliad lygihqtefd
      301 kvkasfiyky qrpekmelsw mliaamivsv isiplylrlm fskkitv
//
LOCUS       WP_010558033            1054 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Pseudoalteromonas].
ACCESSION   WP_010558033
VERSION     WP_010558033.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..1054
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=115105
     Region          1..1038
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miesiirwsi gnrffvllit liiafgglys lqktpvdalp dlsdvqviik tsypgqapqv
       61 vqdqvtfplt tamlsvpgaq tvrgysffgd syvyiifddd tdlywarsrv leylsqvass
      121 lpdsakpqlg pdatgvgwvy iyaltdksgn hdlsqlrsiq dwflkyelqt vpgvsevaav
      181 ggmvkqyqvq vdpdklrayd iplsliqial qkgnketgas vvemaeaeym vtatgyiqsv
      241 sdiekiplgi neqgtplrig dvatvnlgpq mrrgiaelng egevvggvvv mrfgenaqqt
      301 ingvkekles lksslpegve ivpvydrskl idravdnlws klleelavva ivcvaflfhl
      361 rssivavvtl plgilvsfii mymqginani mslggiaiai gamtdgaivm ienmhkhmek
      421 tpltdenrwq ivakaasevg palffsllii tvsflpvfil eaqegrmfsp laytktyama
      481 asaglaitlv pvlmgyfirg kvvsekknpl nrlliaiymp vlkqvmkfpk stivaailvt
      541 ivgfwpvdki gsefipplde gdlmymptty pgisigkare llqqtdklir tvpevetvfg
      601 kvgraetatd papltmietf iqlkpqeqwr egvtteslka efdklvkfpg ltnawvmpik
      661 tridmlatgi ktpvgikvag peldviqeig qqieqilpev tgtasvyser vaggryikvd
      721 isrdkasrfg lniedvqqvv staiggmnvt qtvegqeryp vnlrypqdyr dspeqlsrlp
      781 vvtpsgqria lgdvadirve ngppgiksen arlngwtfid idgvdvgtyv esakihlann
      841 lklpagysit wagqyeymer akekltyvlp ltlaiivill ylnfrafsev aiiivtlpma
      901 migglwlmyl egfnfsvavg vgfialagva veigvimlvy lnqalaelke kaeeraepis
      961 ddayqdallh gaalrvrpvm mtvatiiigl mpilygtgtg seimsriaap mvggmtsavl
     1021 ltlivlpviy sivkkpelna fnkelskael ksna
//
LOCUS       WP_010558056             310 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Pseudoalteromonas marina].
ACCESSION   WP_010558056
VERSION     WP_010558056.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..310
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34269
     Region          7..295
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(28..29,32,86,100,102,133,167,255,258,294)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(225,230,246,255..257,260,282,286)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mntiyfmgec mvelramsaa tlhqsfagdv ynsavylkrc fpevstsvit algqdnlskk
       61 mrerfeseql dtqyvfshes kvpgmyyiet dehgersfiy wrsdsaakkt veflnaecvd
      121 qlcqgdmfff sgislaivdk tsrdqfwkvl eqlksagvki vfdpnyrarl wdsvedtkaq
      181 yhlafsladi tlpgvedltt lydvhsveav ieylkpyqin eivvkngpes vitqqnntlq
      241 thtiipvktv vdttsagdaf ngvylgarls gksiaaavql gakaagaviq qpgaiapkdv
      301 fqhamveagi
//
LOCUS       WP_010558088             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Dps family protein [Pseudoalteromonas].
ACCESSION   WP_010558088
VERSION     WP_010558088.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 157)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..157
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=17460
     Region          5..156
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 msqvnaigln saksddivks lntllssyqi qymnargfhw nikgrnffel hvkfeeiynl
       61 lllkvdeiae riltldgapl hafsdylevs eikeakgisd gvtavenila gystlikkqr
      121 eilnqagdag degtaslmgd yiseqeklvw mlkayld
//
LOCUS       WP_010558185             296 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010558185
VERSION     WP_010558185.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..296
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=33088
     Region          9..280
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 mleqvkywln fplfkfnerv vtlievlavp lwliasvwls hviikmigkr lakknkdpni
       61 vhlvqrilyv valaiifmtt lsminvpita faflsgaiai gfgfgaqnii nnfisgwilm
      121 gekpirigdf levegvkgvv eeintrstri rrvdgvhmli pnskllentv tnwtlrdklv
      181 rgtvavgvay gtdcksvkri mlevanaqpe tlnedgrapl vffqdfgdns llfevyfwin
      241 sqvegglrlv asnirfelde afktsgitia fpqrdihldg tlnivnksep tnkads
//
LOCUS       WP_010558198             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Pseudoalteromonas].
ACCESSION   WP_010558198
VERSION     WP_010558198.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..308
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32979
     Region          1..303
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mfsslfplvi vallgyvalr shyvstqtig dlskitfsll fplflfinia qadlsgivsy
       61 svfltfyavv istfiittll aprlfkmqst gsavfalgst ysntiivglp vlisvlspsv
      121 aalvfliisf hsavlfgats ifssfatgns fqfrrfcegl lknpllvgiy sglmvnmlgv
      181 dvpgfiastl hlitqgalal alfilganly qyrlagnyqq iisatiikli llplvvllva
      241 rlgfqlsdei tlilvvltac ptgvnayiva cqqnsgqslv agtvvlstlm svvtiplwiy
      301 vlqthlfs
//
LOCUS       WP_010558204             502 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Pseudoalteromonas spongiae].
ACCESSION   WP_010558204
VERSION     WP_010558204.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 502)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..502
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56619
     Region          <8..>139
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          <183..498
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mennetlakl aalerilare rlarkeaekq ledytrelyq qeeavnqtqq evatqqgqle
       61 fltgllaetw rqpslnkiva nylertnnfm tnahnlfvei hadlsyhqfq yhcqstkqqa
      121 sslpdsykqv lrqikrdely qqvtsesesq ifeiesisns pserfsdcvl vplynldlps
      181 gkgvgiaill yesqddiniv klqtlessrs mlsvaierkr aeealqerlv dletsnkmle
      241 qtqqqlvqqe klaslgqlaa gvaheinnpv gfvlsnldtm reyfsdfaei maplnadnis
      301 eqekivamqa kwqsldgdfl fddsheilts svqglervkd ivsdlstfsr mdndeldsid
      361 lnvvieksln vvsnefkyhh evikhllpea nilgnagklq qvfinlfvna khampnggal
      421 tiscerdrnk iivrvkdqgh giekehiadi ftpffttkap gegtglglai sygilqqhna
      481 kvkvhsevgv gtefeiafye si
//
LOCUS       WP_010558222             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase [Pseudoalteromonas].
ACCESSION   WP_010558222
VERSION     WP_010558222.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..233
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=25017
     Region          90..233
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 miadvknwvk ssdsgfgkfc rgsfyaikhi empvvpvlyk ilfalhrssk tiwhntlqfi
       61 yftpmfksqv sgskkrltlq cgmpqvigal aislgddvrm sgiatfcgry hseriaklii
      121 gnnvdvgwqn afsvgtkiel qddvrlagkv flagfpghpl ncaerakgkp dlpeqagdii
      181 ikqgawigtg atvlagvtvg kgaivaantv vtkdvadftl vagnpakvik rld
//
LOCUS       WP_010558019             284 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Pseudoalteromonas marina].
ACCESSION   WP_010558019
VERSION     WP_010558019.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Stukey,J. and Carman,G.M.
  TITLE     Identification of a novel phosphatase sequence motif
  JOURNAL   Protein Sci 6 (2), 469-472 (1997)
   PUBMED   9041652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10107962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..284
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0042577 - lipid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0046839 - phospholipid dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=31540
     Region          90..211
                     /region_name="PAP2_like"
                     /note="PAP2_like proteins, a super-family of histidine
                     phosphatases and vanadium haloperoxidases, includes type 2
                     phosphatidic acid phosphatase or lipid phosphate
                     phosphatase (LPP), Glucose-6-phosphatase,
                     Phosphatidylglycerophosphatase B and bacterial acid...;
                     cd01610"
                     /db_xref="CDD:238813"
     Site            order(110,117,142..144,188,194,198)
                     /site_type="active"
                     /db_xref="CDD:238813"
ORIGIN      
        1 mpvkltigqq ytkasfpywk lisficlmsa vmvsmamnkd ayiasqkdif sisnnalqil
       61 pseiwhnity lgdalilipl lsficlintr mwaamfgavp lafslsylgk nffaiprpaa
      121 vlehqqftii getltaytsf psghtitift aisamvfvll revkiseqgk tywiyislmv
      181 atvvaisrva vgahwpvdla fgailgtvsg lsgeylsrhy skwwnwtkvk pallgyfilg
      241 fcfilfvfti svklpeltii wiaisvsaiv gtyialksil qneh
//
LOCUS       WP_010558228             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Pseudoalteromonas].
ACCESSION   WP_010558228
VERSION     WP_010558228.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..204
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22178
     Region          12..189
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mnlnfsdfsp vqiyhlmtqt iiprpiawvm tdsgeanfnl apfsyftavs snpplmmfsv
       61 gkkptgevkd tvkniietgq cvihiasvdd anlvtqtaat ldhgqsevai ndialcefeg
      121 fsmprvagcn iaygcelyki kemgevpqtl vfveiktlfl gdevvsldhk krikvdadkv
      181 nplarlggge ysgitsafgi erpe
//
LOCUS       WP_010558239             128 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010558239
VERSION     WP_010558239.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..128
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14507
     Region          1..121
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mklgdlekll lhylwqhgcs dvktvfahfe ntrggslnty qstlerlykk gllsrhkegh
       61 afhykarver heligqliks vttdfvgedd gssliaafss mssefnveql dkleslieqq
      121 klklkqqg
//
LOCUS       WP_010558261             234 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010558261
VERSION     WP_010558261.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..234
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25453
     Region          6..234
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mqnntlsvsa ltkqfgnkta vselsfnlhs gevycllgsn gagktttfnm llgnthpdag
       61 evllngesif asnfkldqhi fylpenvsly pefsavenla ylaslasldv ddrtlrdali
      121 qcglnqeald rptrfyskgm rqktaialal lknanlmlld eptsgldpva trefvalikq
      181 lgekgvmtvm ithdlscahl ladrisilhq gkqvaelpqs esfeslesty lslv
//
LOCUS       WP_010558262             671 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas spongiae].
ACCESSION   WP_010558262
VERSION     WP_010558262.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..671
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75077
     Region          30..649
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkisrlplsl stisialcaq favanqdksl esivvigkss svsssnlags fdymgreeis
       61 yqhiddlkel ftkvpgvyls rfnqgivnti lsirgfagdg asphakllid gipanmhagy
      121 geldqlfpia idhiemfrat sdpryglfni agnyqvksrs dssadleltl gsfntreiqg
      181 yfgqeddtls hsyslgyrkn egyrdhtdit kkaisgrwdw qlnsdstlga iarysryegs
      241 apgylseqea rdnptmsady asqdggvken hhislhydta innqvdwavk vysqnfqrnr
      301 wvrfsahsdi qnrfddqdml gaistltwqi dpnwallwgv dlqneeiieq rfgtvgqtre
      361 rddqvvkrnr qfsydtkgsy lqlqhqpndk lnwnvalrvd dlsgdysefa adgtrsdrem
      421 ydfdlvvqpk lnviyaltdn tavffntgrs fqhptgkaaf tsgdinarem thndgaeigs
      481 qwsvdavelr asywvqkakn efvlidgeqk nvgkttrngi dlagnwqvsn aftvwanysy
      541 idteivtpsd sanvtkgnql rsipdftasl gasfdatekl vlrvhldaqg dyyvneenag
      601 kkygdytlln asadyhldwa tiklqlnnlt deyyeyvydf ggvdsngvyq tdtvhspgdg
      661 rnaslslsms f
//
LOCUS       WP_010558269             209 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010558269
VERSION     WP_010558269.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..209
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24490
     Region          30..209
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msalnwryyf dlavfvldai shlkttlnny yslseeafla yknctrsrtv ekgevlyeig
       61 qtpshfaflh rglmrayvid eqgnafnktf faegrfpgsm talltnkpsf maidalekse
      121 ileidfkqfr qamfennelm afhinyleth wllekepkei gylqfeakqr ylnffeefnp
      181 iinrltqyhi asylgitptq lsrikkdlk
//
LOCUS       WP_010558275             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ion transporter [Pseudoalteromonas].
ACCESSION   WP_010558275
VERSION     WP_010558275.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..265
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=29826
     Region          17..238
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mestnpflsk lttlvenklf nnflvavilf navtlglett qfgkqnanil haldfiilii
       61 ftielalkli vyrlrffksg wnwfdfliva iswaptsgal svlrafrilr vlrlfsvvpq
      121 mrrvigalgh slpgmasvig vlgiifyvya vlatklfgqh pdanmqewfg sigasaytlf
      181 qvmtleswsm givrptmelf pqswlffvpf iiitsfavln lfigiivdam qvmheeegkp
      241 eqtfatkedi lrleakidal inkkq
//
LOCUS       WP_010558327             185 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010558327
VERSION     WP_010558327.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..185
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=19831
     Region          1..>58
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mishrgftli elilvivvig vlavvaapkf lslnrdania tlkqvaagld qltdgiyaka
       61 viqhkhkvsn esvtvngvti ntyfgapqei wnnalgdlmd gdfsyvgngy fdlgaslvas
      121 yncqerlcvi dqtpasyvns siqgwglfif pkgyslqdec yayyafaeng sqvtskvast
      181 vdtgc
//
LOCUS       WP_010558377             123 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Pseudoalteromonas].
ACCESSION   WP_010558377
VERSION     WP_010558377.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..123
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13620
     Region          3..108
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 mtiitcvlfl fflfassikv lgwqpfifnt qlaffkkygl trthmylvgl iemaaaillv
       61 aslilkldll mvlgalgiaf tsigalffhf rydtfkdavp alitlvlsgm ilikhygliv
      121 nll
//
LOCUS       WP_010558376             292 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudoalteromonas spongiae].
ACCESSION   WP_010558376
VERSION     WP_010558376.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..292
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32904
     Region          9..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..284
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,219,236,263)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     214..217,224..225,228)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdklecinlf cvvarlnsft aaanelnvtq savskkiawl ehklgfnlfe rsarkinltd
       61 agksylafcv qlveqinvte qmlkgeqakv sgrlkisvps afathmlsqp vsdflnqhpk
      121 vqlevsvndq qvdlykddvd ialraahlpd sglkakklld helcyfaapd yleqngypst
      181 psdlayyqci tyslsrpsnv wfinqqkhsv lefiksdspe fivqmalmgc giagmpkwmv
      241 qdklnegalv elftdcekas lpmyaiykna dyipfkiraf vdylsryfte qv
//
LOCUS       WP_010558383             177 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010558383
VERSION     WP_010558383.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..177
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19781
     Region          5..173
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mtnkvfiats ldgyiadkdn kidwlhqlpn pdgddfgfda fiagidallm grntfemvls
       61 fgvewpyskp vfvlsnslth vpkgyegkvf lvngelqkiv knlaklgyhn lyidggktiq
      121 sflkedlvde miltripvll gggyplfgdl peplgfklla skkyidkvvq nhyirdr
//
LOCUS       WP_010558429             460 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010558429
VERSION     WP_010558429.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18643657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..460
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=51473
     Region          71..326
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          98..121
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..189
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          195..223
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          229..256
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          231..>444
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          338..364
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(340..341,344..345,347,371,374..375,378..379,
                     381..382,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          369..399
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          404..428
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mktinkiiia asfslttaqi naatnvlpne fqievdqptf vlpqfsgpfr ereatvapee
       61 letaerlrsm ldqgkkqavl keleafydie lsvamimlka qlyfaleeys kaekayqval
      121 nrspqlvrah sdlgqlfliq kqykkarsyf akavalgand aviygqlayl nltqfgayaa
      181 isayqqalai epereqwqqg lfvalteakm yqaaeallsd liakspnkss lwlnqavlkl
      241 eqndslgals alelaillgd nresnlktaa qlhlqldsfd ravelinthl snykldlasl
      301 ntyltwlsqr glnsqsqhii dtletkfatf dnktksvill hrakisqenq qlesakkdfq
      361 qalnfnpnhg emliayadfl asqkqftqae tlllraeald ktqkqamlsr aqmyvdlqnf
      421 aaalsvlksv atrypstqgi rqqidileni litkaqhtqs
//
LOCUS       WP_010558425             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Pseudoalteromonas].
ACCESSION   WP_010558425
VERSION     WP_010558425.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..429
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47303
     Region          238..425
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mlrlilgcsf lllafngqse eainqqiink iatskqqlnq lenqinnstl syqnkinkal
       61 nevkalrkqa aaiqrvadeq tlsvekladr vvkwqaqdny qklllqsyfe qkgellsnyr
      121 dsngdliisd tifsklesql tnslipswqq sqivddmgqv nqfnrldlgp vslafnadin
      181 kggliehsan qampnlvkgv yndqdiaqlq qlkqtglaqi tfdptlgnaa klqqnkqgli
      241 shiekggvwa fpilffggls livaliksiq lfslpkvrld fidrvkqhvv ndtsyqqlfs
      301 ktelqlidia kthpisdkrd dqlvaflmry ryqvenylgi vatsaaiapl lgllgtvsgm
      361 intfmmmntf gtgdaatvsg gisealvtte lglivaipsl ilsallsrka kshnarlets
      421 avqlskhaf
//
LOCUS       WP_010558463             138 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010558463
VERSION     WP_010558463.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..138
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15152
     Region          1..123
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mikgacncna vqfeitrdvk diymchcsic rkatgtngig vlvvanadfk wqsgadhiat
       61 wkkpnsdwqt wfcavcgskl pgdndserkf ipvglithga eqfkvrhhiw vdskaswdei
      121 gddglqhpna ygtansnd
//
LOCUS       WP_010558476              71 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010558476
VERSION     WP_010558476.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 71)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..71
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7769
     Region          1..65
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mlkltidamt cnhcantiks aikaldrcal idinladnei kiasmrtkhd littverigy
       61 rinkvngevv t
//
LOCUS       WP_010558597             141 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010558597
VERSION     WP_010558597.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..141
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15723
     Region          5..136
                     /region_name="CatE"
                     /note="Catechol-2,3-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2514"
                     /db_xref="CDD:442004"
ORIGIN      
        1 mnpaikglge tvlrvrdlds mkafyaniig lelikefpkv affkiaegfg ghtqviglfa
       61 eelprafvnd ntstiepacs slhhfaleis sedylsektr lenagcevit aehqwcqwrs
      121 iyvkdpennv velvcydksv v
//
LOCUS       WP_010558590             205 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010558590
VERSION     WP_010558590.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..205
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22761
     Region          44..140
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mqkkshwetv yttkessdvs wfqphavtsl kfinrlncek saaiidvggg astlvddlll
       61 nghtnvsvld lsgaalatak krigessanv gwieaditev rlpkqqfdvw hdravfhflt
      121 tpeersayik nllhalkphg hiiiatfaed gpekcsglpi vrysaeslha efgehfvlke
      181 qryethttpf attqkfvych fvkag
//
LOCUS       WP_010558579             189 aa            linear   BCT 01-JAN-2025
DEFINITION  BON domain-containing protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010558579
VERSION     WP_010558579.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..189
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=20549
     Region          17..185
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mnrtfntlal vtvlsttals vnakdnqwkk easdawidgk aeatllfntq lnsfdintdv
       61 dkgvvtltgk vnhdvdkkla qelvigidgv kevenrltvi pdsknksekd dsqiesdfvd
      121 akiatviktr llfdtdisgt sidvdvegqn vtltgevese aekqlaitia knaddvenve
      181 dnlrvvkqs
//
LOCUS       WP_010558600             196 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein
            [Pseudoalteromonas spongiae].
ACCESSION   WP_010558600
VERSION     WP_010558600.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..196
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21426
     Region          39..180
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 malvaplspd hdsevaelak ffnetlgfcp nsvltmqirp eiarafinln kavmandgrv
       61 taeqkrligy itsantgcry ceahtilaae ryggsderlk hiwqfrlsdl ytdaekaafe
      121 falaassvpn avddaisanl kehwddgevv eilgvislfg ylnrwndsmg ttmeagavaa
      181 gkehlthngw qvgkhq
//
LOCUS       WP_010558574             307 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudoalteromonas spongiae].
ACCESSION   WP_010558574
VERSION     WP_010558574.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34689
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,275)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 makiddmalf vhvvkaggla aagrklglsp asmtarinql emrygtrllt rntrsisltd
       61 vgerfyagcl rvieevente nmlqesqdtl rgnlrisats dfgrqyvapa laefssihpd
      121 vsphlmltds liniidegvd iafrfgnlpd snlisrqlak nrrvlcaspd yiknyglpqh
      181 pkellkhrcl ilersgqpln ewyfeinnkr qlikvaphls csdgevirhw avqghgiafk
      241 slidiredls knklvlllde yvrgfnhsdt evvgvqaiya srqylpmqvk vfltyfeqwl
      301 nhksiki
//
LOCUS       WP_010558604             373 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkene reductase [Pseudoalteromonas].
ACCESSION   WP_010558604
VERSION     WP_010558604.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..373
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40705
     Region          5..341
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(24,26,58,100,231,298,318,320..322)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(24,26,58,100,102,109,179,182,184,231,240,298,318,
                     320..321)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(26,102,179,182,184,321)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            184
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mklslfdpiq lgsvtlknri vmapmtrsra sqpgnipndl matyyaqrat agliisegtp
       61 isgvargysl tpgiyteqqi agwrkvthav herdgkifaq lwhvgrrsst aieglqplsp
      121 saikepdkvy gplpngelgm idttmpkamd lsdiqntvnd fviaaknamq agfdgveihg
      181 ahgylldqfm rryantrddk yggsienrir ltidvcqava naigsdkvgl rispfvsssf
      241 qqhdsdmptl tlallkalap iklaylhlse nignyqpitd tyrkkirsly phpimlaggl
      301 tqelancfln kgmadlfafg tayicnpdlv ermkgnmplt qlannahstf ygggekgytd
      361 yptscslaqk svr
//
LOCUS       WP_010558612             242 aa            linear   BCT 01-JAN-2025
DEFINITION  SIMPL domain-containing protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010558612
VERSION     WP_010558612.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..242
                     /product="SIMPL domain-containing protein"
                     /note="The SIMPL domain is named for its presence in mouse
                     protein SIMPL (signalling molecule that associates with
                     mouse pelle-like kinase). Bacterial member BP26, from
                     Brucella, was shown to assemble into a channel-like
                     structure, while YggE from E. coli has been associated
                     with resistance to oxidative stress.; The SIMPL domain is
                     named for its presence in mouse protein SIMPL (signalling
                     molecule that associates with mouse pelle-like kinase).
                     Bacterial member BP26, from Brucella, was shown to
                     assemble into a channel-like structure, while YggE from E.
                     coli has been associated with resistance to oxidative
                     stress."
                     /calculated_mol_wt=26602
     Region          1..239
                     /region_name="YggE"
                     /note="Uncharacterized conserved protein YggE, contains
                     kinase-interacting SIMPL domain [Function unknown];
                     COG2968"
                     /db_xref="CDD:442208"
ORIGIN      
        1 mkplfylsll alssfafans plpnhrhiai tgygettvkp diavlhfsve ntdkksaeak
       61 aevdkrfntl lkglkkynis ekdivasria vspryeysqq erkqlhvgya asrsiqvtvn
      121 dltmlsdvmd lalsvevnqi qrvemasske eqlqqkavel aienaktnga alansfgaal
      181 gkvysinaqn ydqikhygtm ekmgnarmms admgsvspgt ylqddltfka tinvvfdlkg
      241 kn
//
LOCUS       WP_010558619             246 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010558619
VERSION     WP_010558619.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26438
     Region          4..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mdntpvielt nvskiyfsdd vethalsdin lqinkgdyia isgpsgcgks tllsvmglld
       61 dvtsgsykie gvdtsslnmd tlaelrnlhi gfifqsfnli delsvydnva lpllyrepal
      121 skadidtrvn talkqveidh rvkhkpnqls ggqqqrvaia ralagspsil lvdeptgnld
      181 skngdavmal laelneqgtt icmvthdpry agyakkqvkl ldgkvlnsgk esvsavdvtt
      241 qleaha
//
LOCUS       WP_010558660            1017 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010558660
VERSION     WP_010558660.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..1017
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112944
     Region          25..1017
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnitalafny kkpvllvval lmlngifayf tlpaqedpti tireaivstq fpgmapdrve
       61 qlitrkleee irkipevkei ksssstglst ihvkiydryf nldniwqdlr nkvnnaqgkl
      121 pqgtlpsyvn defgdvsvit laltadgfdm demydiaqhi rdtlygvegt kkieilgaka
      181 eriyleasna klaqlgispl aliselqkqn ivqsggrvdt gsrsfiiept gnfnsipdie
      241 ntyitipgte dfialkdivt ikkgyidppd klayfngkpa iffanamlpe ynilefaprf
      301 ktkiaeieht lpigyqldia tyqadqvekt vkgvsinvlq tlaivlvvvi lflglrtgli
      361 vgaivplvml vtlaimqysg iklermslat liislgllvd ngiviaedfk rrleqgidry
      421 kamvqgckel avpllsssat tilfflplml aehvageytr sislvilitl lsswvlaltv
      481 tpilsyyfik vpkttssdsn efgkltsyya kyeqflhwvl khkalfmaam filfigagas
      541 mkfvakqffp nsdrtqvlvn idlprgtssr etnrqmqeif twfnnkeqfd yiesfsgyvg
      601 fsgprfvlsl npedpaenkg fivlnvtpet diasrvleld tqiearfpnv sarvrkmflg
      661 psdssilkvq vkgpdkeviy qkaqevmavl naapnslnvr tdwenlitki svkvdqhrak
      721 ragltsseia qalesyfsgg vitnfrdqde iipivlrage nernsldrlr tlniyseksg
      781 ravplfqvad fepinqfsii hhedmfrtis iearntklsa edfkalvdeq iqllkhdlpv
      841 nhtieydgvi keskagqkal sanmpmvlgf iiillvaqfn sfrkamvisl tiplsfigav
      901 iglllmqapf gfmvtlglys lagiiinnai vlidriaieq aegkseyqai idacltrlrp
      961 iamttittmm gllpliigkd plfygmacvi afglgvgtvl tlgvvpalya gfyrvkk
//
LOCUS       WP_010558675             327 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Pseudoalteromonas spongiae].
ACCESSION   WP_010558675
VERSION     WP_010558675.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..327
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36153
     Region          38..280
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(44,46..49,69,88..90,116..119,139,165..167,180,184,
                     213,215..217)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(140,167,180,184)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(167..169,174,180,211..212,218,237,240)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mrllitlfil tthiafaddr qaaleashak aatvqnqkai lvtgassgig rtitetlarq
       61 ghfvfagark qrdidalnql tnvqairldv tiqsdidaav ntvkasgkql hglvnnagva
      121 vfgplieipe rdidfqdnvn vmgpyritka fapliienkg rianigsisg lmsstmfgpy
      181 smtkhaieaf sealsaemrk fdvkvsviap gnynsnimkn lkrrlekqgh hfansryqde
      241 ykrfakftnp drsrfkapdd vanavvkalf detphlrylv vpneqeamlp ikntlkkvae
      301 lnashaftfd kkqmlawlsh eidkanh
//
LOCUS       WP_010558708             393 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010558708
VERSION     WP_010558708.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..393
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44366
     Region          <189..384
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          298..381
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 melklesaiq illvgasfgv clfilahlwl kervtsvryl glfyganian ildewfwhfg
       61 vwqvapiltn aylpilylia psfylyvkgl tdpsynnrll anvkhgigfi vsflvcvpyf
      121 vldsdiklar lsapsgtleh lglttlgpti vlllllpfsl cyviaivkll aqhlntiksy
      181 fsnidnrdls wirwsiialc iafavstiri flperlseeg whnilfltfe lfwlvivgvl
      241 sitqgpiyks eveserallc adkqqgkyqn spmqesdier iknklnaama dgfykdpnlt
      301 lrklsdltgi aeirisqvln tamnigfydf inswrikaac ksiersehti levafevgfn
      361 srstfnqafk khvgntpsay rkqlitepna sei
//
LOCUS       WP_010558728             169 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Pseudoalteromonas spongiae].
ACCESSION   WP_010558728
VERSION     WP_010558728.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..169
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19296
     Region          13..162
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mgsdfyqqsi lpyagiiiki craythsqed fddyyqevcl qilrskdsfn agsqwstwvy
       61 kvalnvcltn lkqrkqgekh fvsdalpdev qddlkafnsd dinvlynaik hlseidravi
      121 llyleeksys eiaeiigant ngigvritri kerlnkfina qegtheqin
//
LOCUS       WP_010558782             655 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LTA synthase family protein [Pseudoalteromonas].
ACCESSION   WP_010558782
VERSION     WP_010558782.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..655
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=72787
     Region          16..611
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mltdlkkhlm pylvltlcvl gvlstfrlgf slwqyqhfsn pnallnllig glridlstlg
       61 ylllipalis plalsikalk piwlaclksy lvliltilvf lematpmfie eyglrpnrlf
      121 veylvypkev fsmlmsghsa avfvtlillv aaiklivlpl anyfvfkttg qthatakvkl
      181 vaillllaal ilfargtlgh rpinpayvff sndalvnslt lnstysvfha vkallnekna
      241 sklygamper evinivrqet glptsaftlp nnplfkiqqp sylgakknlv iileeslgaq
      301 yvkrlnglpl tpnidslyqq gwgfdklyat gtrsvrgiea vvtgftptpa ravvkldksq
      361 kgfftlasll qsegyntqfi yggeshfdnm ksfflgngfq tivdfddidk lnfvgswgas
      421 dqdvftqant elnklalqek pffsliftss nhdpfeipne aikpfdytps qlaqyddker
      481 arhkaiqyad lalgefinta ktqsywqntl flivadhdar algqalvpvn nfhipaiiln
      541 sefdnqsyka iasqidlapt llslmgvtnq spmigrdltq stttgralmq yadnfayysn
      601 kgitilqpgk kpkmfdfnsa dnymsekpld hneakvalah alwgslayqn gwhan
//
LOCUS       WP_010558802             676 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas spongiae].
ACCESSION   WP_010558802
VERSION     WP_010558802.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..676
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75469
     Region          34..644
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkalpfrlnt vftaifiasi fhaeaqqsad sneietitif gekkeqtife tgssvhafda
       61 nalnsltnvs eiddlleiip nlvssgmdnn lptvrgidgs gpsvgglasf agtaprlnms
      121 idgrsltyse iafgprslwd mqqievylgp qsyiqgrsas agsivmksnd pvyyfdsaik
      181 vgianhdyrq tavmvnaplv ddelalrfsa drqtknshld ivsyqpagds reisttnirt
      241 klryepsale eltstltfny mdtrapqsen evgsffpker pvydtdstsa dwqivyqisd
      301 avifensvny tdfgyeritd pkgrradfit dgeeifiepi irynpsnasl saitglryfd
      361 sahddvythn rgkndmtget ttrsafaevv ykvnaqftat lggryesetv trvvplfald
      421 ydettdvflp kidinfapke nqafgfksgk gfnsggagls fntftarapm kpysfdteyv
      481 wnyelysrqr ffqntlelts nlfyndydgm qilqthsdgy vsvqnldsan tygaevnlrw
      541 laldnlelsg gvglleseyk knntntkvek elprapsasa nlnlvyrfln sfqfsanany
      601 sssyysdrnn iealkvdayw ranvklaykf nngrialyvd nlfdadditl issefapesp
      661 ltitprtiga nfeyhf
//
LOCUS       WP_010558792             210 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Pseudoalteromonas spongiae].
ACCESSION   WP_010558792
VERSION     WP_010558792.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22129
     Region          1..206
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdlnallifv iaclainlip gpdviyivsn tmkgkmttgl kasmglgvgy fahtlaaclg
       61 lsaiilssal aftlvkvlga aylcylgiks vyamwrgesq vvlndksras dnvflqgiiv
      121 svlnpkvalf flsflpqfid tssadvalql lllgcvfsll atacnllyav lgswlfkran
      181 sarftrvldg isgvllvgla skvlvsdatk
//
LOCUS       WP_010558840             288 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ROK family protein [Pseudoalteromonas].
ACCESSION   WP_010558840
VERSION     WP_010558840.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..288
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=30810
     Region          11..282
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mtscntpfit cvdlggtkla ianiadgkii kshtlpidas lskddfnafl fnnlapfvtk
       61 acrgicigvp glvesdsgfv ievlnikhwq nvalktllea rfarpvlvhn dancftygiy
      121 kseayqgyen lvgvtlgtgl gaglilngrl ytgkqsaage fgsfpyldgi iedycssqff
      181 kkqgldgaat yqqaqagdnr alavfaelgk hlghalvqvv qafnpekvvf ggaiaksapl
      241 fidalqqall kqlpqsvysa lqihytqdtn talfgayqlf leevatge
//
LOCUS       WP_010558842             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010558842
VERSION     WP_010558842.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33609
     Region          15..83
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <201..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrafcekvit ptdaswryhk ylmpylpfsw hyhpeyeicl tlnskgmrhi gdhieeygel
       61 dlvfvgpnlp htwqseanqd gseqivyvaq ipvkwldkla rdhkelqgll pmlarslkgi
      121 kyskecaiea kalfeamdna gatqrlflll dlldkmqhdv eqvtlstpmf afgkqmeqdn
      181 gklnqviefi yqhytdnlya dqlaelahms tnhfhryfkq rtectltefi nrlrigkack
      241 llvtssspis visdqcgfnn vsnfnrrfla fkgctprkfr qqlinhnlin
//
LOCUS       WP_010558885             302 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Pseudoalteromonas].
ACCESSION   WP_010558885
VERSION     WP_010558885.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..302
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32675
     Region          40..298
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mklniasali lalfaahass dtlfetsdwv kdnaftngve gpavdsqgvl yavnykhqgt
       61 igkvlgkdkv etlvtlkngs igngirfdkk gnmyiadyvn hnvltiaakd laqggeladk
      121 vkvfahnakm nqpndlaimd ngilfasdpn wqtsagnlwr inkqgetsll eanmgttngv
      181 evspdnnily vnesvqrkvw rydldgqgnv snkqlliefd dfgldgmrtd kagnlyiary
      241 gagviavvsp kgkllreikl kgqfptnvaf ggkdgktvfv tmqkrgaiet fnvdiagraf
      301 nl
//
LOCUS       WP_010558892              66 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010558892
VERSION     WP_010558892.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..66
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7160
     Region          1..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 msevknriav lraehkisqq aladaisvsr ktistietgr ftpsvtialk lavffnvtve
       61 eifsln
//
LOCUS       WP_010558893             468 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Pseudoalteromonas spongiae].
ACCESSION   WP_010558893
VERSION     WP_010558893.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..468
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51551
     Region          1..385
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mhfsdlnlcp einqaieeqg yesptpiqek sipailagrd vmaaaqtgtg ktagftlpml
       61 emlskgekvr snqvralvlt ptrelaaqvw qsvatyskhl plscqvvygg vkinpqmlkl
      121 rkgcdilvat pgrlldlfqq navkfdqlel fvldeadrml dmgfihdikr vikalpskrq
      181 nllfsatfsd diralakgli ndpieisvap anttaktvtq waypvdkskr tgllkhlikt
      241 nnwqqvlvft rtkhganrlv rdlekakina aaihgnksqs armnalngfk lgdvnvlvat
      301 divargldiq elpyvvnfdl pnvyedyvhr igrtgragas geaisfvtqd vaadlfgier
      361 liqeviprki eagfepqspv pdskldtrpi kpkkpkkpkk pkenastndk vkaeakaask
      421 pkkkssshna kpkngekpkq nskgrsdnng qakrpkrkpn nvkfkank
//
LOCUS       WP_010558905             205 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Pseudoalteromonas spongiae].
ACCESSION   WP_010558905
VERSION     WP_010558905.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21820
     Region          1..203
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdfalwmslv gvcaigamsp gpslavvlsh smtrglkqgl iasvahgvgv giyatlavvg
       61 lagfihefpi aykvilfsga aylvylavni lrqktnhfei annantgnla aaqdgfaiaf
      121 lnpklaiffl alfsqfidpd sitissaaim citvlvidtl wyclvslits hanqkfellr
      181 ygktinnmla iafillairv vvtni
//
LOCUS       WP_010558942             550 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010558942
VERSION     WP_010558942.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..550
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=59710
     Region          21..550
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mntllsnvsv rnkiniisga llfalilfas feiyklnsik ssfeqysrva vklevttlki
       61 nrdvnyvsri nrsimlgddy qsnlakmrer ikdiqshfsq lnslalndnt eqkelkqliv
      121 ksqsstetfl skslqlvqtl sststkaqle qawqtykrdy spvaaksred faalnrkmnq
      181 erevifqatt ndidssisvs iyfavvaalv aailswlvtn niiaplntlr nsindiaksn
      241 dltkrtqvks ndelgvvsha fdtlidnfhg tlqqvvnase qvhqasnmla qssentssli
      301 seqrqetdmv atsmnemait anevsrnaad tatgamdant qassgqhvvg stvtsidkla
      361 qqidtaslsv dklsndsqei grvldvirgi aeqtnllaln aaieaarage qgrgfavvad
      421 evrslasrte ssiqeihqmi eslqngskda valmlqskqq aedsvnnatq agealdlitt
      481 avakindmaa qiataaeeqt svneeinrnv vnistisdnt sqeaantssa stelaalase
      541 lknqvsqfkv
//
LOCUS       WP_010559014             358 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Pseudoalteromonas spongiae].
ACCESSION   WP_010559014
VERSION     WP_010559014.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..358
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41435
     Region          92..335
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mssrykltic alisllagca snkittinnl nadgaslkqg ryinrypgnk typyscdenc
       61 ypptddihce sdmehcqyrg knpkltthsg yqihwlghas feiktpsgkr flfdpvfdef
      121 dwpvnwafqm angferqspk skvqnlsdvd avlyshlhyd hfnkhdiali gnkpkylvpl
      181 nfakhfdrnh ytihemdwft thlvaqtkvh fvpahhfnsr iwvpflyndd nqalwggwvl
      241 eengktlffa gdtgysdhfk diqrqygdid vcllpiasyf hqehetwyry vhtrpedaiv
      301 aandlnckvt ipwgygnasw qmgdhsshsa lfrllhnlki iesdsqfyim negerlsl
//
LOCUS       WP_010559023              91 aa            linear   BCT 01-JAN-2025
DEFINITION  HU family DNA-binding protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010559023
VERSION     WP_010559023.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..91
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9700
     Region          1..91
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mnksqlieli aknndmpktt akrvveslva titqslsegd lvqlpgfgsf slsyhpekqg
       61 rnpqtgeeit iagqnkvafk agsklksain e
//
LOCUS       WP_010559032             650 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010559032
VERSION     WP_010559032.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..650
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=71053
     Region          116..650
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mftklklvqq lsisfgamig lmvllatisf fglrsgyddf veyrglards nlaglvqsnl
       61 lsirlhalkf lkeqnnenin dfnkraklln eqldiartei iepgraklid qsfdkvmaye
      121 qgfsdvvdly akrddivknq ldangaiirq nvseiirtay edgdtdvtyf aaivqeqlll
      181 grlytnkflv sntqddylra taefkevmks vkvledniqs pkriallnet atrlaayqrg
      241 idnvndvink rnniitnvln kvgpeiaeay eevklsvknd qdslgpkvqs rsetttttii
      301 vvsiavvavg vffswfisit irkpiggepk dieyianria dgdltisftk sgnetgiyna
      361 mgemvgtlrh iidslkhatt elirstkild entassmqga ehqmeqlnqa vlsmnemaat
      421 vaditqsaql aadaatnadd qthtgkqvvd ntrsaindlv dntelvsnsi knlenetesv
      481 gsildvirai adqtnllaln aaieaarage qgrgfavvad evrslasrtq ksteeiqami
      541 hklqseakss vdqmnanles arvttekane tnealdsiss svgtirdmnm qiagaseeqn
      601 vvtqqitdsv gqvnemavqt vagaekaaet arglveiaan leglvnrfkv
//
LOCUS       WP_010559056             184 aa            linear   BCT 01-JAN-2025
DEFINITION  GbsR/MarR family transcriptional regulator [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010559056
VERSION     WP_010559056.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..184
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20570
     Region          3..157
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mlltpkiesf vmhcgemgsr wgfnrtigqi mglllmseep lsaislsetl nisrgnvsma
       61 ikelqswrlv svihkpgdrk dyyapagdiw elanrvfeer rkremdptls llrasiidep
      121 anaeeayaqd kmselhdlle titvwaselq smspeklttl mklgsgvvkv ldfkdkvlks
      181 gnsn
//
LOCUS       WP_010559059             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010559059
VERSION     WP_010559059.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..145
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16164
     Region          1..139
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdkfneqilf elsrdssltn iqlaerigls psaclrrvqe lerakiitgy katidteqlg
       61 igfkafitvg lsvhtktaqt qfeeaitlsk evlechnvtg afeyilrvet kdlksykqfh
      121 tnvlgdieqv atitthvvmd svkds
//
LOCUS       WP_010559075             245 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010559075
VERSION     WP_010559075.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..245
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27024
     Region          9..240
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 miisnhqhdi ktatgvmrty ryspvesgsy pciifyseif qqtapiarsa ailashgfhv
       61 lvpevfheln pigtvlaydd agkdkgnqdk wnkpleshds dtvaliefak alpnctgnvg
      121 amgvcigghl ayraalnpni kaafclyatd ihsdtlpate gnnslermsd ikgeihfifg
      181 kqdphvpvdg rikiyqacqq tginfqwqev naqhafmrde gerydaalai qmyqqaaalf
      241 qrklv
//
LOCUS       WP_010559078            1040 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010559078
VERSION     WP_010559078.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..1040
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112646
     Region          1..1040
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mitaavkrgt lvavcvlits ilglvtalni pvqmipdlev rtitvqtgwp gatpqdveke
       61 iiieqerylr glanlsrmvs ysemgsasie lefpfgvdan dalirvnnal sqvpaypenv
      121 dqprlfsssf sgnafmyftl kplagnplel dvdllrdfae dyvrprmesv sgvsevrvgg
      181 gaqrqiqikv nahrlaqrgi slpelrtair srnkdasagd iesgtsryll rvvsrfesln
      241 elenliiark nganillkev asvtldhfet rgtsfsdger tlslsvrres gsnvlaikda
      301 mlpivaelnq qllsqnglel klmsddvkyv rsslknvwvn lalggllatl vmyfflrsgr
      361 atlvgiigip lctiaaflal slfgrtinvi slagvafaig mtvdntivvl eaivqakvng
      421 tskrdaaing vkevwpavla stattvmvfa pilfvqqeag qlysdiaiai sgaiiasmlv
      481 aifivptaia nigkkqelse gkqlqlsnkw lkpaawlsks tkrariavav favgilgsal
      541 wfmpaaeylp egeepkafsm miappsynls emqkigkelr eyfdgyihad sadfiagket
      601 mppldyysms vsvgriwfls apvnpdhinq mmeavtdkfr sypnmrafss rgsiissndg
      661 gtravavdia gsniidlyga aeavyeqanv vfdkpqinsd pgsltleqpl veikprwqrl
      721 aelginnsdf gyaiaamsdg ayvdefilnd dkidmflfsg agnrqnmael asspivtpsg
      781 nilplhalad ltnsnnsnsi rrvdgnrtvt vyiipprdva letaeqfvrn ellpalwqqg
      841 kiaqgikvni sgaadqleat kealssnfii alalsylllv aifthwrypl filatvplgm
      901 aggllglvlv nglnsvlgsi glssyhqpfd mitmlgflil lgtvvnnpil ivdqtrrfvi
      961 eqglsvkqav eqalekrlmp ilmstattlf glaplvlipg dgtelyrgvg vivmsgilvs
     1021 tiltltflpa llvavvkekq
//
LOCUS       WP_010559087             199 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Pseudoalteromonas spongiae].
ACCESSION   WP_010559087
VERSION     WP_010559087.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..199
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21546
     Region          <64..156
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mnklvhaifl tlslsacaeq avdcsvfdeq akskyilpfq kgesykvevs tghyrasngg
       61 vglyavdfnm pigttivaar agevvavreq fedwngkdla enfvfikhad gtvaryfhlt
      121 hlgamveqge qvkqgqiiak sgntgqsggp hlhfdvqtcg pnlpphynqk pcgqtlpvvf
      181 kntkphrcgi eagkvykai
//
LOCUS       WP_010559130             492 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein
            [Pseudoalteromonas].
ACCESSION   WP_010559130
VERSION     WP_010559130.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..492
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=53806
     Region          15..492
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnypwiekan rifsavligq fiitliiaff tdtwfegiai gllivalplf lintapfasv
       61 trhavgiavq lfaalhiqqa mgltelhfei fvmlaflsfy rdwqvilssv lfiavhhilf
      121 fivqsqgasi yifeqghlaf yiltihalfa iteggvlmyv aklthreavs ayklsesihd
      181 vlskegkfdl taftnkqsdg sdyqklmtsl sgfikqtktv segvllrsea vldltndver
      241 atdenvsqin liatateemt vananvasqa seanesasda ftrtdktkqi idssaqnieg
      301 lkgdlaatsq tigelalkcn qieevmnaik sisdqtnlla lnaaiesara gehgrgfavv
      361 adevrqlamk trqnaeqise itaalineas ssveqmdkcl vqaedtvaqa kdasnmmmgv
      421 vdniesmvnn masvasaane qatvsasise stqrlshnse qlkhntnesg qrfkemkndi
      481 enlnrelsrf dl
//
LOCUS       WP_010559165             282 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein
            [Pseudoalteromonas spongiae].
ACCESSION   WP_010559165
VERSION     WP_010559165.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..282
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31837
     Region          34..279
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mqkvfkltil misvwclnva assycdntrs ashtqkntvt vmsaniahgr gtnfsqitss
       61 ieqiktnlna iatkvnqinp divafqeidk aswwsgqfsh vdyllkrtnf qnyvatshvn
      121 awwgdygtal fsklplincd gitfapswpt tnkgfsyakv nlnkqaqdii vvslhldfsr
      181 asvrnkqike lltklkdlna piiimgdfnt dwrwqnsivk tlsdsyglri ynaqsnelnt
      241 fgakrldwim vsqhftfksy ynvegalsdh afvvaelefn el
//
LOCUS       WP_010559199             175 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Pseudoalteromonas].
ACCESSION   WP_010559199
VERSION     WP_010559199.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..175
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19130
     Region          11..169
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mvifadfina irdfldtggs vllvigvlic amwllvierf mflfttyrss kksvitnwfa
       61 reernsweae qikqanisri slklnhnlpm inmlvalcpl lgllgtvtgm ievfnvmait
      121 gtgsarsmas gvskatiptm agmvgalsgv fastylqrka krevallddk lvldh
//
LOCUS       WP_010559212             440 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkaline phosphatase [Pseudoalteromonas].
ACCESSION   WP_010559212
VERSION     WP_010559212.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..440
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47652
     Region          1..438
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mkksliastv llassslaya eapkniiymi gdgmgpaytt gyryfkddks tkyvertifd
       61 elfvglasts pdddtvvtds aagatalsta tksyngaiav dtakkplttm lqiakskglt
      121 talvatsqin hatpasfaah nesrrnydei andyvdvkvd gklavdlmlg ggtkyfirdd
      181 rnlvsefkqa gyqyvddfdk lesikslpal glfsdvafay aidqnptrla dmakktlsll
      241 dnnkrdgffv mlegsqidwc ghandiacam aemddfanai khakqyvdqn pdtllvvtad
      301 hstggltlga nghyswhtdv ikgvnasitk iakalmksdh llttwsdktg ikldksqseq
      361 lamltasaks ekddehkeke alvkhvrqli sdasntgwtt gghtaidvpi laygkgadaf
      421 kghldnteia nqlinyikqr
//
LOCUS       WP_010559200             454 aa            linear   BCT 01-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010559200
VERSION     WP_010559200.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..454
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49178
     Region          269..446
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mlvkkfvksv iaastlftas avvaqpvdld sllktleqgn yqqsqdnqrr eaefakannq
       61 qaamlrsrin erdglisast rletqfeene iklanmsetl nkrmgslkel fgvlqqvagd
      121 tqskfitsnv saelpgrgaf lselaqkmgs ssklasiedi ekvwfelqre mteqgkvsrf
      181 nrdvivagge kvnkevvrvg sfnliadgky ltynettntl seltrqpasr fqssaadlqa
      241 ansgfvdfal dptggsilgl lvqapsteeq vhqggavgyv ilavgligll ialerfvslm
      301 imggkikrql ktdvasddnp lgrvmkvkdq ypdvtydtle lklseailre mpritrnltl
      361 ikiisvvapl lgllgtvtgm intfqaitlf gtgdpklmag gistalvttv lglvvaiptv
      421 fiytllntrs knllvilqeq sagiiaerse kgaq
//
LOCUS       WP_010559214             637 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Pseudoalteromonas spongiae].
ACCESSION   WP_010559214
VERSION     WP_010559214.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..637
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=70895
     Region          9..637
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mtsiddlfgk sgpfalaikg yaprqpqidm aksvalaiak deqaiveagt gtgktfaylv
       61 pallsdkkvm vstgskalqe qlfhrdlpal kkilgkgkki allkgrsnyl cterlnqhva
      121 hvpvddpdvm hqlamvakfs getrsgdmad csgieedakv lpyvtsttdn clgkecpsfq
      181 dcfvrkarvk aiesdlvvvn hhlfladavv kesgfgelip nvncyifdea hqlpniasdy
      241 fasrvstrmv ielvrdirlv yraelfdmiq lgktldklet avfdlrlqfp sesqrgdwqq
      301 mvkqanvyra iervindisf lyqvlklcle rsdkieklfe rtaslkgqle tmydaqkpgf
      361 sfwfettkrh ltfsitplnv serfralvdn atsswvftsa tlavngdlth fakdlglntk
      421 imevydspfd yenqallcip rylpepskse mgfsivsiak qmikaakgrc filftsyrml
      481 nlvadglshs veypllvqgq askrillekf vmhgnsvllg tasfwegvdv rgdalscvii
      541 dklpfaapdd pllqakmksh sgqgndpfys lqlpgavial kqgvgrlird rkdkgvlvic
      601 dnrlvtreyg riflaslpnm artrdlakas aflekik
//
LOCUS       WP_010559305             426 aa            linear   BCT 01-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010559305
VERSION     WP_010559305.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..426
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46662
     Region          253..411
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mklylwlvta llcvvaplka sdviqslqhd insaqaalnk tekqlarens nlsrellnae
       61 navlllrket egviraqdea alsiedvenr lkqwqqqsqy qthlltryls eseitpksdd
      121 ltellalakk sfdetqqrqg lfyqsevvfs dgnthqaeli digpftyfks dnaaglieks
      181 sqhnevavll enahdaltql kdtgsallpi dpsngratms lkqqeniish iskggvwvap
      241 illfalfall isiyklvqla rldkivpavt erlsnlngeh stlklgswqt elveicqrtp
      301 igqlrddslf nalneqkkql dnllgaiavt aavapllgll gtvsgmietf klmtlfgagd
      361 paavsggise alvttelglv vaipallcha flsrkvksyy hqleqcaisl sqfnfnqnie
      421 lhkgaa
//
LOCUS       WP_010559309             447 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010559309
VERSION     WP_010559309.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18641232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..447
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49561
     Region          92..359
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(93..94,96,120,123..124,127..128,130..131,154,
                     157..158,161..162,165)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          118..148
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          153..180
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          187..215
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          221..247
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          255..282
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          328..442
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          331..357
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(333..334,337..338,340,364,367..368,371..372,
                     374..375,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          362..392
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          397..425
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkitlfltll fictsaasss ahvdiaitkp swdfeikygl lsqdaaklta neqtiattik
       61 pllaksdyng awqavkhlei ntlspalaqa vgqialqvkq lahaerafrh alskrpdllp
      121 shralaaiyl klednqkaak ylasaltlgd qdaslfaqla ylhmqqaqpy aaiagfrqal
      181 flqpdsldyk kgllwaltqa gdvneatvll nqlientpne adlwlhlsqi qlqqgkekna
      241 lasievarrl gnnnptnlll iaqlhlnhgs sdaavkllte iinkddpahl tqivnaltvl
      301 inqnnvsqaq vlasvlekhs tklnfkhqsm lltylallae rngktktaeq yltraietda
      361 sngkallqlg qlyqhkkqls qannyyvras sldnykeqaw lfsaqiaidq gqyeraitll
      421 nnayrenptr rdllanikql erlkrvq
//
LOCUS       WP_010559325             646 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010559325
VERSION     WP_010559325.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..646
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=70585
     Region          115..646
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mklsdisirn aliatitlal vlstlfstlf ssnqfnsvfd efneqeyfpa llgkveasir
       61 aelntpials kalaqndfli dwalkgeknd ewpriqqyfa nvkntndaav vfwvsqqsln
      121 yyqndgilkt lsassdrdsw ffqfmhssnt qqvavdvdeq skrltafinv kvnangqdlg
      181 ltglgydisk iidivnqnki gktgyvfllr pdgkiaahpn qafvgkdyqa inkysplsal
      241 lsqsasqqtq lekikldnet yfaatqnled igwqlvalmp tsemsskisk ammltiavns
      301 viagvfivlm vwianrvsrs iasigsklle mgnqggdltm rlddsrqdel gdlargfnav
      361 iannqkmvik lkdielqmaq diqalvdsfd qvtslssnqd alseqvasai temgttvsev
      421 snlaldtant sedavsdtkq sieqmqsstl amnqltqvmg eayqniqela gqaesinsiv
      481 dvinaiseqt nllalnaaie aarageqgrg favvadevrt lasktqsstq eirgqidqfq
      541 rsteivlnam aqgnettskv setsaqsaei lttidrsita vkdmnqqiat ateeqnvvvq
      601 hinesavqia dlskqfndia vadqqqlkrl nhlaselssl iseftv
//
LOCUS       WP_010559386             184 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhomboid family intramembrane serine protease
            [Pseudoalteromonas].
ACCESSION   WP_010559386
VERSION     WP_010559386.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..184
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=19965
     Region          9..183
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mhikqpirii fallailfsv qlvnaisqga vsglgiyprt lnglagiifa pwihhswqhl
       61 lsnaaplavl afitlqqglk rfllvylfis ivagsavwvf afdgyhagas tmvfgliayi
      121 lsnaifsrni fnlilaiiic flyagviysl tqfipgvsws shffgfiagl iagkvfnsap
      181 qkrp
//
LOCUS       WP_010559392             679 aa            linear   BCT 01-JAN-2025
DEFINITION  S9 family peptidase [Pseudoalteromonas spongiae].
ACCESSION   WP_010559392
VERSION     WP_010559392.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..679
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=75414
     Region          69..262
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          195..355
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          431..676
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mskiikttll aglvslsagp aiasdnatwq yedvfnieya aspqvspsgd sivyerrsmd
       61 imsdstrinl wqynlsskah tpllsgkaqy rmarfspdgk klayisneeg dnqlyvrwlq
      121 sgdtarvtnv ehgvssisws pngqwiafsm fkpqeakgif sempkkpkga nwagtakyid
      181 qmsyrsdgrg flphgyrhiy ivpaeggtpr qittgdfhhd gniawsqdge qifisgdrhp
      241 dwqdrpresd iyqinvasge ttnvtkregp daapvispng kkiaylrfdd kklssqnndi
      301 fimnndgsdv enltakldrp ignpkwdtkg rglyfsyddf gqkyvgyvnl kgkitekiak
      361 lggqslgrpy tsgefavvdt nelvvtlana nrpadlamvk kgktrkvtsl nedllahktt
      421 aemgeitvks tvdgrdiqaw yalppnfdkn kkyplileih ggphtaygpn fstevqlmaa
      481 kgyvvvwanp rgstsygedf anlihhnyps qdyndlmdvv dgmvakpyid snnlfvtggs
      541 gggvltawiv gktdrfkaav vakpvinwls faltadgysy ftkywmpgmp wdhvehlwar
      601 splslvgnvt tptmlltgee dvrtpmsete qyyqalqlrk vdsamvripk ashgiaarps
      661 nliqkvgnim awfekyrtq
//
LOCUS       WP_010559462             841 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Pseudoalteromonas spongiae].
ACCESSION   WP_010559462
VERSION     WP_010559462.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..841
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=92107
     Region          35..828
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mkqilsrslm lltpllalsa cgthqadtsk neksattqtd yvqnpaqfvn pfigtkgpfn
       61 hrqaanvvpg avkpfgmfnf gpehaytkel maesegiskr ineddvripv spggynwqat
      121 rlkgfsftrl sgtgclgasg dvpvlpfnqa ikhspasdki nayyganfsh ddetaipgyy
      181 qvgldsgidv rlaatdrtgi aeftfaskeq aklifrtays qlgsgdaftk vdvakgevsg
      241 yvtsgnfcgy lgeynrrdyy tlhfvakida pitgsgayvd dtvspnatss kggmgygdtg
      301 vpewgkgsgl wvdldvnanq pvtmrvgisy vslenarenl ekeqasqsfa qvkgnayaaw
      361 ndalgrvkvk sndsdllttf ytalfhsqfh pnifsdvnge yrgfdqqvht vnanqtaqya
      421 nfsgwdvyrs qlqlislthp nvasdiaqsl fnqanqfngi wdrwthnngp tgvmsgdpst
      481 itianfkafg adkfdvagay qslykaatep teydlsnvgc pvfcrgqkps ldewlslnyl
      541 sdqsnswega setleqvsad falsqlaarl gktkhsqall mrsgywknly npkateqlgy
      601 iqgrnqdgsw kdkfdpfsgh lfvegspaqy lwmlpfdgqg lnellggddv masrldnhfr
      661 kpdgswvlyr dsaeyadvsn qpsiatpwmy lytgkayktq qtvretmkql whntvsgipg
      721 qddlgqmssw yvfsalgmyp fypgradmvl sspafekaki gnisisapna sadhiyidtl
      781 tvngqpsmqs winenhvnap qhleftlstt pnkafgqaea hrppsfstss tvatklvgdk
      841 s
//
LOCUS       WP_010559484             280 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pseudoalteromonas spongiae].
ACCESSION   WP_010559484
VERSION     WP_010559484.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..280
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30584
     Region          48..280
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mkrlvffasa laltgctati kesrfiaqdd ektlysdtfi ntlnaqtprh nvnvisipse
       61 dktttlygvf ldnektqntv lyipgngmsv ekaatnalle laeydydivi fdrrglgase
      121 gtatianlir danvtfdytk qslkadkviv hgyslgsfia aqlaknkavd glvmqgsatn
      181 vddwvdeamp wyskvfvdvq iddafysvdn kqvlsenyvg pllviggadd kqtpailsek
      241 lfnastsaek qlviaenagh gemfksknvq vayqtflakf
//
LOCUS       WP_010559486              69 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010559486
VERSION     WP_010559486.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..69
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7723
     Region          5..69
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 madlqitnqi kmlrfmngem tqkelaervg vtrqtimaie aakyspslev afkiaavfnl
       61 plesvfqyq
//
LOCUS       WP_010559576             319 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Pseudoalteromonas spongiae].
ACCESSION   WP_010559576
VERSION     WP_010559576.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..319
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=35397
     Region          27..316
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mrklllilli fplfcyaewq sdekaimgts vkitlwhhdk shgeaaikav fdemerinql
       61 mspyinssel yrvnknaaiq pvkisnelyl likqaqlisa qtkgafditf asvgflynyr
      121 erispsnqvr dtnqalidyr qvelndknqt vhfkqqgmki dlggiakgya vdnaitilks
      181 qgidsalvsa ggdtkalgkh gdrpwllaiq dprkkgkhai qlpmeneais tsgdyeryfi
      241 qdgvrhhhii dpktghsaak vqsvsiigqq gvmtdalsts vfvlgvkdgl alinsmpsfe
      301 aliidkdrkl hfsngllah
//
LOCUS       WP_010559752             174 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Pseudoalteromonas].
ACCESSION   WP_010559752
VERSION     WP_010559752.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..174
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19243
     Region          10..161
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mlvlmeiwes vrdfvatggq vlyvvaialf lmwvlmiery wfltsvfpkm kkgiianwda
       61 rqdttswyah rireawisea sekldermll iktlvavcpl igllgtvtgm iavfetmatq
      121 gtgnarlmas gismatiptm agmvaalsgv ffstrleaka kmaknklids lphh
//
LOCUS       WP_010559713             385 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: patatin-like phospholipase family protein
            [Pseudoalteromonas].
ACCESSION   WP_010559713
VERSION     WP_010559713.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..385
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43039
     Region          8..374
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mnssgnsskh ktkiallltg ggaraayqvg vlkaiaknlp rnqvtpfaii ngtsagaina
       61 talgcyascy qlavkklehv wknfrteqvy htnfssvfgh ifinmlrsfq sdyenhppas
      121 llnnqplrel lrsvldlkri dnnirndyle alsitassys sgdsvaffqa khanswrrak
      181 rrgekttini ehlmassaip mvfpstkirq gyfgdgsvhq haplspaihl gaekvfvigv
      241 eqpidnkyfg fqphypgist iaghlldtif sdtlradier lerinrtlsl ipardkhkel
      301 kriahfvinp sqnfnaiatq yydtmpvsik mllrsigvkk hsesslvsyl lfekeytqhl
      361 idigyqdgla qldeimafle ftnmq
//
LOCUS       WP_010559803             126 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF423 domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010559803
VERSION     WP_010559803.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..126
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13208
     Region          1..123
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mnrfslaagg ifcalavmlg afaahglksi ispamiavfq tgvdyqfihg lalilfgllg
       61 nsgyklkwas ifaivgivff sgslyllatt gikifgpitp lggvcfivsw llftvsvinh
      121 kpaqvk
//
LOCUS       WP_010559817             335 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pseudoalteromonas spongiae].
ACCESSION   WP_010559817
VERSION     WP_010559817.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..335
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37994
     Region          16..234
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mktalycfll llsistfaev nsesftskal ntqvtfkvsv ptsygtrlnq sypviyvlhg
       61 qwdftlvqsi sdtlkneipe fiivqvigkg eqlqpndtni nenarlfrqh ftselipyik
      121 nnyrtadysi lighsnagrf amkqfltksp lfndyfifsp slddgyivsl aqsvtelkah
      181 lflsianege hmqqpfnslv tmlekhpsls ltnekyaqys hqsskvialv nafqtrfshw
      241 qanyetkiag lapllahysa lqkefgfqvl pskddlirll ayfainnndq evtkiydyli
      301 ahystaaesi teieqyleke gyqsaaklin ssrlq
//
LOCUS       WP_010559869             356 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Pseudoalteromonas].
ACCESSION   WP_010559869
VERSION     WP_010559869.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..356
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39562
     Region          17..345
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mlhifkqwys rkfsdpnsit llmltlglaa afyffgtyii pvmvalviay lldwpvqklm
       61 htgvsrviss tlvmlifsgv vvsivvgiip vlwhqlsnfv qdlpsmleqg kgylmtlpsn
      121 ypelvnpeqv ksilssvegh avtigqtvls tslnslkdvv awlvylilvp llvffmlkdk
      181 hlllagfekf ipkerklisq vwqemnqqim nyirgkifei livgsttfit ftildlryaa
      241 llgtlvgfsv lipfvgaalv tipvalvalf qfgvgsefwy viiaygviqa ldgnllvpll
      301 fseavdlhpv yiivavlffg glwgfwgvff aiplaslvra llnawsmsnq hetvka
//
LOCUS       WP_010559888             464 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudoalteromonas].
ACCESSION   WP_010559888
VERSION     WP_010559888.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..464
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50524
     Region          7..366
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(14..15,18..19,22,54,104..105,107..109,112,132,
                     135..136,139,206,209..210,213..215,218,242,246,296..297,
                     301,305,321,324..325,328..329,332)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mksfpslyft nlfliggtgl lttylalylg qhnvstfwig lltsfyylgl llgsklgyhl
       61 iksvghirtf vantaavtac vaahalsdni ylwlalrliv glsmmcnymv leswlneqaa
      121 pesrgrvfsf ymitsylgmv lgqlalsrfp elgyaplflv cmalslgiip isitrrihpk
      181 plkpiqvslf gyfkkvpqsl tavhfagiin gsfyglaptf aslsgfsaqe ialfmsitif
      241 agllaqwpmg visdkirrsi lirsnavaig vvslalfllp ltqyvayalt fafglfaftl
      301 yplssalans rvededrvgv ssallimfga gaaigsavna qimaffghqa lygstavltv
      361 vmfallsfin skqkaeqpep sdyvvgtsdv tasplaatmd prieettahe qllvvdeent
      421 hsqedlddee fddqeftkqq hpdldvsseq tlkanednkn qass
//
LOCUS       WP_010560056             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit alpha/FixB
            family protein [Pseudoalteromonas].
ACCESSION   WP_010560056
VERSION     WP_010560056.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..308
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31977
     Region          2..308
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 msvliiaehe hgvlkndtak vvsatqklgk sitvlvagfn vaavaeaask iegvsnviva
       61 dnaalehqla enmadlvvdl agdyshifaa atttgknfmp rvaalldkvq isdiievide
      121 ntfkrpiyag naiatvqsse dkhivtvrss afdvageqap vavssfdavk enalssfvsq
      181 qeteserpel taadviisgg rgmqngenfa llngiadklg aaigasraav dagfvpndmq
      241 vgqtgkivap qlyiavgisg aiqhlagmkd skvivainkd pdapifqvad yglvadlfdv
      301 lpeleasl
//
LOCUS       WP_010560109             367 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Pseudoalteromonas].
ACCESSION   WP_010560109
VERSION     WP_010560109.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..367
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39990
     Region          17..354
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mavvtfetkn tdngfvigia tlnvekalna lnlemielly nqlldwqsde kvsmvllqga
       61 gdkafcaggd vvslynamht gepsnyietf ftkeyrldyl ihnyakpicv wgngiimggg
      121 lglmagashr vltessriam peltiglypd vggsyflnkm ptqvglflgl tgasvnaqda
      181 lyiglgdtvi ehqfkselid slistkwstn adenhqalsh llttfnaksd inlpanvesh
      241 navfaamaev deltdkvdai lsfetddkwl traqkglshg splgahlvyq qlnranglsl
      301 kacfqmelgm svrcgqlgef kegvrallid kdnapqwqfd aisnvdsdvi asffnvewsn
      361 ghpltdl
//
LOCUS       WP_010560125             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Pseudoalteromonas].
ACCESSION   WP_010560125
VERSION     WP_010560125.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..193
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21625
     Region          1..187
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 msefltanwl lisilvvfiv ifyawyvsii tkrnameeaf sgidvqlkkr tdlipnvlai
       61 akkfmtheke lleevtrlrt dvlnaassnn neqrfklegq lenslsglmi avenypelks
      121 datmldaqrt yadveahisa arrnfnsanr vlrnaiqvfp gniiaamvgv kamaffeise
      181 serqpvnaae lln
//
LOCUS       WP_010560174             447 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: replication-associated recombination protein A
            [Pseudoalteromonas].
ACCESSION   WP_010560174
VERSION     WP_010560174.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..447
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=49420
     Region          1..437
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msnlsfsfap eirplaarmr ptnlsqyigq khllsegspl ynailagrch slilwgppgv
       61 gkttlaevia hhadanvirl savtsgvkei resvasakdh lamqgqrtll fidevhrfnk
      121 sqqdaflphi edgtfifiga ttenpsfsln nailsrarvy qlkaleqqdl mqaihsalnn
      181 deqlqqkqie idnaaiekla lagdgdarrt lnlleqaidm adqqndkliv senvlanvlp
      241 ahiakydkgg dlfydlisaf hksvrgsnpd galywlcril agggdplyvg rrllaiated
      301 ignadpramq valnawdiyh rvgpaegera laqaaiylas apksnavyta fkqakhdian
      361 epsfevphhl rnaptnlmkd lgygaeyrya hdepgayaag ekylpeeian rkyyqpterg
      421 leqkikakld ylteqdnlat rkrydrd
//
LOCUS       WP_010560218             789 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010560218
VERSION     WP_010560218.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 789)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 789)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 789)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..789
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86553
     Region          4..88
                     /region_name="ATPase-cat_bd"
                     /note="Putative metal-binding domain of cation transport
                     ATPase; pfam12156"
                     /db_xref="CDD:463475"
     Region          91..789
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mskncfhcle pipagislsi tfendekpmc clgcqavaea iidqgmsdyy kyrtdsagkv
       61 qelvpeqikm fqsyddediq sefltkqgdi aeillsvegi scaacawlie kqllnlghvv
      121 rvdvntstyr amvkwdqsnl klstiiesla rigyraypfq qdheeqqkrq taqsyvrrlg
      181 vaglmtmqvm mfafamyfgm fsgmdegfeq yfrwislvla tpvilysalp fltsairglk
      241 akqlnmdlpv slaifgayga scwatvfetg evyfesicmf tfllllgkyl efrarlkase
      301 ftanlqkllp ltarlvndee eiiaakrlkl ndkvmikage tipadgilid gktsvdeamm
      361 tgehaavakt vgdqvyagtv nhdgvisiev nqigqdtlin qivrlqhqal tsrpkiaeit
      421 dkvaqwfvac llvfasitaf swyhiepeha fwvtiavlva tcpcalslai ptaltcavak
      481 ltqqgvlikr shvletltkv tdiafdktgt ltegkftlld tklfddsvsl eqvyalaktl
      541 etysehpisk afteldvppv aisdveietg kgisaefqqq tvaigkanwh cqvadtthdv
      601 flylnervia gfklqdkird haadtlsalk annlqlqvlt gdpslagkql vssldidhvk
      661 tgcspsdkqk eveqlshqgk ivamvgdgvn dspvfnsahl siamasgadi skntadvvll
      721 nselngisrl fntakltrrv ikqnlaislc yngsilplaa mgmvppwvav igmsassliv
      781 ignslrllk
//
LOCUS       WP_010560226             311 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)-dependent alcohol dehydrogenase
            [Pseudoalteromonas].
ACCESSION   WP_010560226
VERSION     WP_010560226.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..311
                     /product="NAD(P)-dependent alcohol dehydrogenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34405
     Region          19..308
                     /region_name="MDR1"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08267"
                     /db_xref="CDD:176228"
     Site            order(37..39,42,125,129,150..153,155..156,174..175,178,
                     193,211,233..234,255..257)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176228"
ORIGIN      
        1 mkglvaenrq lvikrdlnmp lvgegevlvq vksttinlid lefakgkydl flklarnnht
       61 vktgiefsgl vatdghafkk gdrvfgyvnl lksdkthqef vsvheqyiak ipanlsfsha
      121 aalplgalts yvalnelvnl tsnskvliig asgglgvyai qiakragshv taltgdkhlq
      181 flksfgaddv idyhasples lkdkydvvld lsntklykqv khllvsdgvf ipaepnkhfl
      241 sfvmnafrkr ktkylyvdkg dsakltqian wvaqgeiqtc vdseflfedy qsaisrflqk
      301 grrgrvvlnf e
//
LOCUS       WP_010560280             230 aa            linear   BCT 01-JAN-2025
DEFINITION  M48 family metallopeptidase [Pseudoalteromonas spongiae].
ACCESSION   WP_010560280
VERSION     WP_010560280.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..230
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=26854
     Region          3..224
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 msikyqlkrs knrktlaiki kakevfvyap mhlkqdfieq wlmqkqgwin khlekqikrv
       61 dvasvltqkt ltilgeeinl ifvegqvksn velvdgvlsi ntsrrvknvs dkqlaliadf
      121 aknkltnycs akaqrlakqi kesfhsvsvk hvrsrwgacd srrrlqfnlq lvsaplwvie
      181 yvvahevahl kvmdhsrrfw htvesiypdy rkaehwlken gykldvfkle
//
LOCUS       WP_010560360             150 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Pseudoalteromonas].
ACCESSION   WP_010560360
VERSION     WP_010560360.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..150
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15465
     Region          7..147
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mktllttlts sqagyaalal rlpigiifma hgaqklfawf ggyglegtga wmesiglapg
       61 ylmalmagsa effgglfill glltrpaala lagtmivaif tvhfenglfm snngyefgla
      121 llaasislvf sgagkaslda lisdkltqha
//
LOCUS       WP_010560389             426 aa            linear   BCT 01-JAN-2025
DEFINITION  YeaH/YhbH family protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010560389
VERSION     WP_010560389.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11148708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..426
                     /product="YeaH/YhbH family protein"
                     /calculated_mol_wt=48783
     Region          13..420
                     /region_name="DUF444"
                     /note="Protein of unknown function (DUF444); pfam04285"
                     /db_xref="CDD:427839"
ORIGIN      
        1 mahfidrrln gknkntvnrq rfikrykrqi keavsdaiak rsvtdvetge sisipsrdmq
       61 epifhqgkgg krdmvhpgnd qfsqgdrikr plggqgqgag egdasdsgeg qddfvfsisk
      121 deyldllfed lalpnlkqnq lnklvqmkth ragysndgvp snidivrslq gsvarriamt
      181 agkkrqlael eqklaeltkn kkdnqseial lekeieqlkn kiatvpfidt fdlrfrnyek
      241 rpepsskavm fclmdvsgsm dqatketakr fyillylflt rtykdievvy irhhtqakev
      301 deheffysqe tggtivssal klmdeiiker ydseqwniya aqasdgdnwa ddspqcsdwl
      361 tnkilpvtry yayieittra hqslwreyqv ladthenfai qhiksvediy pifrelfkkd
      421 ttadva
//
LOCUS       WP_010560420             176 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010560420
VERSION     WP_010560420.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..176
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20071
     Region          1..>126
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mskkeqtkql ilttawqlfk engyqntstr diamasgvan gtvfshfksk idilkagfsd
       61 qldevllnas kkdkshtaie rmshyakaly pfylsqrefs rellgtimwq hselapqlar
      121 fkhqlihdnn anahhadvii dlyfmtllyg lnhpeinene lvtqlekkls llnvpn
//
LOCUS       WP_010560445             616 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010560445
VERSION     WP_010560445.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..616
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=67915
     Region          114..616
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 msikrsflsl saliilamav masliwystn qmaelgsela lskelsnnml mlrrhekdfl
       61 lrknekyvdk fnqrivlikq nihalhnald tipslklqls dthdlieqye tqfltlvald
      121 krigltkdqg lrqafnlaet qlkeavlttg dtnaissmvr lvllendfqs sldiaaknqa
      181 qeklstvkty lttydtvsat atlanfenaa anladalkqr glseeeglrg alrgsihqve
      241 stlnqlttgi naeisdtlqv skkqgamvsg litvvisiil lwqtyriihr lhsanekmad
      301 ishgngdltq hieldgedel seftdsinef idttaeivre ikhkgeavek gahhsaelsl
      361 rsqtaiedqk nntlavkqav selvkaveli aqssvdveas veqaeqdmre gtdvmsqtht
      421 nmgllksqve stseimselt lssreiegvt svisditeqt nllalnaaie aaragetgrg
      481 favvadevrt lakrtqqstv eigkmiktlq dlvvrseqam eqslsltsem ndsldtares
      541 mdrnkqslda irdrviqiag atqeqmytvk evesatenis vsaeqlfids censqnchal
      601 etdaqnmkqd varftv
//
LOCUS       WP_010560469             284 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Pseudoalteromonas spongiae].
ACCESSION   WP_010560469
VERSION     WP_010560469.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..284
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31592
     Region          <5..281
                     /region_name="bifunc_ST_SDO"
                     /note="bifunctional sulfur transferase/dioxygenase Blh;
                     NF040641"
                     /db_xref="CDD:468609"
ORIGIN      
        1 mnvtiesffh kqsstisyvv fdnrslkamv idaavdfdia sgnvgyqfad siihyidshh
       61 ldvdwileth ahadhvsaaq ylkqklgakv atgkhitqvq qhfnkvfnfd iptdgsqfch
      121 lfddgevfyl geeavtvmft pghtpdsvty ivdgsafvgd tlfmpdsgta rcdfpggdas
      181 qlyhsiqrif elgndthlym chdyqpngre vsvvtsveaq kqynvhlkhg itqhdyvktr
      241 esrdadlavp klihpsiqvn inaghfpeae angttylkip ltfn
//
LOCUS       WP_010560476             384 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Pseudoalteromonas spongiae].
ACCESSION   WP_010560476
VERSION     WP_010560476.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..384
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=43830
     Region          262..384
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mtvtsegrla nrhpdivlit hceeevhgvn eiireqfdsf rcivkddavi etinqlkpkv
       61 vlfalatvke nitlytlmik sqvlnenhys vllcnnkesi lafgcclrnl fnsyfthqpl
      121 yerfrlkliv fegltrceve qtfydelvsv vknqdsdlne lielglsykk nvldkldtsk
      181 leveriknev skeeqgelkq llldkiqteh lqpllssles visdnlttml akmmsahanl
      241 qsaevtqnnn paqaleqfdi neqdekrilv vednhiyrem isdvlskegf iihqvddgln
      301 avkkiktdry dlilmdlfmp hlnglkttkh mrqvgknkkt pvialsgnkn keivkkwash
      361 glagyivkps tkaeiltvik rvld
//
LOCUS       WP_010560535             215 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Pseudoalteromonas spongiae].
ACCESSION   WP_010560535
VERSION     WP_010560535.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..215
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=24052
     Region          60..215
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mtllrntlla ltsaailsac wfqdpavkqv eqfiseqkvd kqdekwrtkl tlppklefap
       61 dttyywvlkt slgemkfelf hktapmhass tiyltklgfy dsltfhrvit dfmaqggdpl
      121 gngqgfpgyr ysgefeplvs hdqkgllsma nagpntdgsq ffitfratph ldgkhtvfgk
      181 lvsdeavldl fnenatrfgk pkqqliiqsa hiite
//
LOCUS       WP_010560543             759 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Pseudoalteromonas].
ACCESSION   WP_010560543
VERSION     WP_010560543.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..759
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83584
     Region          41..742
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkylqkskla kliqgslfss lvlsgaavaq geeagaesaq leviqvtark rvenaqevpv
       61 avsalqgdnl dayssagmdi rfmnakipsl svessfgrtf prfyvrglgn tdfdlnasqp
      121 vslvvddvvq espilkgfpv fdvervevlr gpqgtlfgrn tpaglvkfds vkpsqefegy
      181 galsystfns vdfegavggg ltdnlsarvs vlkqtrddyi dnrapnnfin dvtggydeqa
      241 ariqflyeag dftallnyht rdldgkpivf hanaiekgtn kpvagfdpev iyqdsvqfat
      301 qqvesqgssl kleydfedht ltsitgwesa eiysradvdg gygcgndfvf gcptpemgpg
      361 fiflasesad aipshdqisq eirlasnfag dfnyqvgayy yneeqtietf gfdglggdfn
      421 wgyvfqeqdt tawavfasad yhvsdklkvs gglrysddkr dfravrlvtp gdfnnidlek
      481 sanpedshvs wdlsaayklt ddvnlfaraa nsfrapsvqg rilfgdevtv adsetinsie
      541 fgvksdvldg rgrvnattyy fqmddqqvta vggsanfnrl lnadktvgyg leldsewilt
      601 delfatfnis ynktelqdns lflqgcfnct itdpfvegkg ysldgnslph spewisnftl
      661 ryskeigdge ffaytdwsyr saidfflyes vefegealle ggirsgylwe agdneyevsa
      721 fvrnitdeqv figgvdfsnn aamvnqprim gvefkvsff
//
LOCUS       WP_010560561             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheW [Pseudoalteromonas].
ACCESSION   WP_010560561
VERSION     WP_010560561.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..243
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=27235
     Region          93..228
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mtkqlfanek vmkqyldall qediardsva npvenllsdv evkaaehqqa ttekviakpv
       61 vkelviapev kvevveavev alppartqda tydddefqal yfevagltla vplkalggiy
      121 qlgevnqifg kpdwfkgvml hreqklnvvd sarwvmpeky nkkleealny qylimlgesn
      181 wgllaerlid nvslshqdik wrdkggrrpw laglikekmc alinvsamte lldqgldsqd
      241 dda
//
LOCUS       WP_010560619             396 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid aminotransferase [Pseudoalteromonas].
ACCESSION   WP_010560619
VERSION     WP_010560619.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..396
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43003
     Region          1..395
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(101..103,129,182,213,242,244..245,253)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(104,139,206,251..253,289,292)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            245
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mfanlkplpt dpilglmaky rqdtnpnkid lgvgvykteq gdtpilscvk kaeafrlene
       61 tsksyiglag dlgfcakmes lllgehkall enrvrtaqap ggtgalrvaa efiakanpna
      121 svwvttptwa nhiglfsaag ltvkeypyyd yenkgllfde mmatlktvpk gdivllhacc
      181 hnpsgmdlna eqwqqvadla kevgftplid iayqgfgisl eqdaaglrll aetvdemiic
      241 sscsknfgly rerigacsii sessavadva nsvllsvvrs iysmppahga aivdtilgse
      301 eltaewhqel aemrnringl rstivealhs rgvaqdfsfi ekqhgmfsfl sitpeqierl
      361 qkeysiyivg ssrvnvagvs qanldyfada vatvik
//
LOCUS       WP_010560622             101 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: STAS domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010560622
VERSION     WP_010560622.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..101
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11215
     Region          10..100
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(21,23..25,31,53,55..57,59..61,64..65,87,91..92,94)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            56
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mslnkalspd gklftieikg kfdfnlvqsf rsayadvgvs tpkviidlre tdymdssalg
       61 mllnmkkslg dsvssihitn crpqikkilq isrfdkkfdi d
//
LOCUS       WP_010559578             808 aa            linear   BCT 01-JAN-2025
DEFINITION  LamG domain-containing protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010559578
VERSION     WP_010559578.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Hohenester,E.
  TITLE     Structural biology of laminins
  JOURNAL   Essays Biochem 63 (3), 285-295 (2019)
   PUBMED   31092689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Sasaki,T., Fassler,R. and Hohenester,E.
  TITLE     Laminin: the crux of basement membrane assembly
  JOURNAL   J Cell Biol 164 (7), 959-963 (2004)
   PUBMED   15037599
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10597119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..808
                     /product="LamG domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=87947
     Region          337..497
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
ORIGIN      
        1 mriflslllm allsgcgsds evkeqpkppi ddsgefvysg paaetadiqq fkiavwdnlv
       61 gndkcgachn eqgqspqfar rddinlayga ingfinltsp kdsllvtkva gghncwqqsd
      121 svcadilttw isewaqtdnt attidfddpi lkvpgssksf passalfsty vhpilqqnca
      181 nchsssasfp vapyfaepna daayqvaqak idlnqpelsr fvlrlgsefh ncwsdcesda
      241 almqeaitqm adaiptnqvd dalvlskalk ltegivanng nrfeqhiiak wefksgqgft
      301 aydtsgvepa anltingdvs wvggwgikln ggraqastsa saklhkmlta tgefsleawl
      361 vpdnvtqegp ariisysggd drrnftlgqt lynynfllrd nttssngdpm lstpnndevl
      421 qatlqhvvlt fdpvngkriy vngnlisqqe dnqgvlsnwd asfalvvgse tssnfkwrgq
      481 vrmmalhnra itpeqiaqny dvgvgekffl lfsvselidl prsyiiaevs qfdsysylfk
      541 epfflsldsn vspqaialeg irigingkes plgqsfanlk ttlgsnyssq tgqplsrlgs
      601 lipleqgpnn defflsfdvl gehqfvrvpg elppfpiefp aelssdigik afseinfsma
      661 qmtgistkla eiaqtyeqlk qqlptvntld gfvaanqmai sqlaikycsa fiedpalrsn
      721 afadfdfntt pdvaftpert lqfssglshy llgqelasap qydsmqqeln aliqrlnrcp
      781 qdcdaartli iakascsaiv gsaatiik
//
LOCUS       WP_010560716             438 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Pseudoalteromonas spongiae].
ACCESSION   WP_010560716
VERSION     WP_010560716.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..438
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50126
     Region          1..>120
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mivthlqsst qivemgeirv ltdpwltege yygswyhypp faeselsllq ydyiyvshih
       61 pdhlseatln klpykkpili hkysspflkr klellgfevi elnnttpykf kngsqltiya
      121 adncnpelcs kflgcghiet kfgstqidsl alfshggkhl lnlndcpyel ashtilkngl
      181 dqldidllmv gyagagpypq cfqfdsielk nnaakakqiq flqqalnfie lvkpkafapf
      241 agtyilgsry ahmnehrgvp slgdatcyle antpsnckgl llnqhdkydl tiqqlikstk
      301 avptlkqymn hitkqplayd ndvwddnele dlmlnsyfrf kskadeinys sttylviese
      361 kvcftmsldk kptqtfkgsq vpqpyvrltv ehnllhrllr gpkyahwnna eigshiqyer
      421 kpntferaly hclcffhq
//
LOCUS       WP_010560791             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HDOD domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010560791
VERSION     WP_010560791.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..282
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=31993
     Region          7..260
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mieidnkils dvaagftipa kpdilqalqd elnhepelyr vadiiaadva tsaavlkiin
       61 spyyglarti sdirqavmfl glenitslvt gyllkqaydq skcslplnrf wdnandianv
      121 sciiaqhlks plppenlhli glfhdagtpa mairfegyth llqehrends nllihkeekk
      181 yktnhavvgy ylatswnlpk qicqiilqhh sndffnasnd kferscfacl rlaenlvhva
      241 rnfrpepqwh aieqlvldtl qldeydfqdl kedveeylis sh
//
LOCUS       WP_010560852             350 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010560852
VERSION     WP_010560852.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..350
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38604
     Region          10..347
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mslqgpfndi cilrlsaigd vchavstvqa iqrhypnaki twvvgkieam lladlpgvel
       61 vvfdkkqgka ayhslkehfk grkfdvllhm qvalranlaa rvitakvkvg fdwnrakegh
      121 flftnhriaa ekeahvlegf rgfakaigvp hyepswqmpv seddrsyake tlsplgdkvl
      181 vlspaaskae rnwlperyae iadyavqqgf sivitggpte levtlakqie namkstalnl
      241 vgktnlkqll cvlenaslvi apdtgpahma vtmgtpvigl yahsnpartg pylyqdyvve
      301 vyhqnlkkqt gktatqlpwg trvkgkdlmh qisvdsvkem fdrvvnekal
//
LOCUS       WP_010560872             198 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010560872
VERSION     WP_010560872.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22038
     Region          1..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mskgqetkqq ilatalkiat qssldnltig glavatgmsk sglfshfksk etlqlnvltf
       61 anelfqstvi qpinreldpl gqllslcenw ldwyenqakt cifisaavef ddqpgaihdr
      121 vkqdlanwlg ylthkvtqvi sagqfkqnvs aeqfvfelya lylgsqsmsw lgvedaehsr
      181 fktalnqlie rhraeesv
//
LOCUS       WP_010560891             162 aa            linear   BCT 01-JAN-2025
DEFINITION  CinA family protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010560891
VERSION     WP_010560891.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..162
                     /product="CinA family protein"
                     /calculated_mol_wt=16963
     Region          7..160
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 milpahisel aaklgasltn kklwittaes ctgggisyal tdtagssayi drcfvtysnd
       61 akhellgvkq eileqfgavs ketieqmadg ainatnadva iavsgiagpg ggtkdkpvgt
      121 vwiavkvldk lsvehclfag nrsevrlqvi eyslkkaiel in
//
LOCUS       WP_010560895             127 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010560895
VERSION     WP_010560895.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..127
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13981
     Region          <49..119
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 mtllllsaai saapinleqm vapsdldnvk vvpltsnqda sqfliyvkks vplhihkehs
       61 emvyivdgeg qmqlgdktft ikkgdfvkid entphgvkvt ssqplkvlst qtpeyfgkdk
      121 hrvdnhe
//
LOCUS       WP_010560899             128 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Pseudoalteromonas].
ACCESSION   WP_010560899
VERSION     WP_010560899.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..128
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14459
     Region          20..97
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 myplvnkfyq nfkvrgraks hdrvwvikae nqivaaakls lkdgqfllsg vftapcfrgq
       61 klasrlikti aldyrkpfft faynhlvswy qscgftehaa paelapffsa yqnqgrqivc
      121 mlankdca
//
LOCUS       WP_010560963             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Pseudoalteromonas].
ACCESSION   WP_010560963
VERSION     WP_010560963.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..201
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21953
     Region          7..189
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 metsavlsll palilfsisa tltpgpnnil laysganfgf rktlphivgi rigmtcmhla
       61 mllglgklfe qypmlhqvls afaasyiiyl aikiargkpn ssnssaspmt fsqaalfqlv
      121 npkswamllt lvtaltlpne qywpsallgv ivfnlatlpc sffwvgvgry lkgflqnpqk
      181 lkrfnlvmat lllltlplif y
//
LOCUS       WP_010560984             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010560984
VERSION     WP_010560984.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..218
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24821
     Region          5..212
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mfdyhfsktl vdellsyagn sytlkkgkll aeqgkplskl ilvrsgtisf sydvgngrrl
       61 llgqldcqnt lvgevealnd rpciysmtcq sevtynliel kywrellqek pelalytaks
      121 iaekfienqq inlnklllpl sfniakdcla ryqdetvtml kpypkvsaea erfatteray
      181 rrvvsdlveq glvqrteqgl kpldedkled fidsfasr
//
LOCUS       WP_010561014             399 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HD-GYP domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010561014
VERSION     WP_010561014.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12112208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..399
                     /product="HD-GYP domain-containing protein"
                     /calculated_mol_wt=44631
     Region          2..124
                     /region_name="DUF3391"
                     /note="Domain of unknown function (DUF3391); pfam11871"
                     /db_xref="CDD:432148"
     Region          <98..327
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mlktilisdl kpgmyvqgvv kqqgsvkvks egwvrtqtai nklaksgile vsvdpdkfid
       61 lnaeknndss enaietpkfd ptkatasfss eankakklyt eakqlqskaf ddiragrkid
      121 vapfkqvasg fidsvfrnqd alacmtrire kdayllehsi nvsvlmsifa khmgferevi
      181 helatgallh digkikvpda ilnkpgkltd aefdeikrha lyskeilees elsdiaiqva
      241 gfhherldgk gypfglkgde inqyvrmisi vdvydaltak rvykdgmnpi qafkiirsdc
      301 pnsfdselva rfiqcigihp vgtlvklksq klgivsqsnf eqplkptvkv fysakhqhyt
      361 evqdlnlasn riddelessi kpedfgidli kffrnaffd
//
LOCUS       WP_010561015             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HD-GYP domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010561015
VERSION     WP_010561015.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..389
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43132
     Region          38..321
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 msitpdgkik lpitklevgd fveevtkqlg avkvvqtglv rnyfalqalk kkgvievlvd
       61 psrskkstqq qtttftkkak iesqleaald wqdrahaiid dtlaraksht pidisglqsl
      121 aqqvltltrq hkeavalvvr ckmsnallns hllrvavsla qfcihqnyqp lasehmvlag
      181 llsrvgyqml pdnlrlpddk lapmlrvkkq qhisqlqkll rvsgqpdehv srliseqnel
      241 ldgsgypnql dfdklnsaqr ifsiaimyds lvcgfdhtka vgsaaayrel mehspnhydp
      301 dllqtfiqai gvypagtlvk lcsgrialvv enqqqltkpr vkvfynaefn hhlavriidl
      361 aesddsiegt asaqrydldi adlisedgi
//
LOCUS       WP_010561025             148 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GatB/YqeY domain-containing protein
            [Pseudoalteromonas].
ACCESSION   WP_010561025
VERSION     WP_010561025.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..148
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=15997
     Region          1..147
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 msllaqlkda qkdamrakdk vrlgairmvl aaikqkeide qvtlgdaeit silvklvkqr
       61 kdsesqyrda gredlaevea neikvleafl pkpltdeeil tlideciass gasgmqdmgk
      121 vmgllkakae gradmgklsg likqklsa
//
LOCUS       WP_010561059              63 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2065 domain-containing protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010561059
VERSION     WP_010561059.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..63
                     /product="DUF2065 domain-containing protein"
                     /calculated_mol_wt=7113
     Region          <15..62
                     /region_name="yjeT"
                     /note="Uncharacterized conserved protein YjeT, DUF2065
                     family [Function unknown]; COG3242"
                     /db_xref="CDD:442474"
ORIGIN      
        1 msfdvlllaf alllifeglg palfpakwre ylreiaqlad pqlrmigval iligwllfmw
       61 lkp
//
LOCUS       WP_010561091             250 aa            linear   BCT 01-JAN-2025
DEFINITION  HesA/MoeB/ThiF family protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010561091
VERSION     WP_010561091.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..250
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26935
     Region          5..247
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 msslsnqeli rysrqlllpe idenaqlklk aarvliiglg glgspaafyl aasgigqltl
       61 vdhdevelsn lqrqilykis higqskskaa gktlqalnnq isistlsqkl deqnakalie
      121 ncdlvldcsd nfktrylvnr lakqfakplv sgaamgwqgq lcivdnkndn apcyeclfan
      181 qgvssaqncd tlgvispllg vigaqqaiaa illllgednl pqflqfdaqs fkqsafsfat
      241 sqtctvcnkr
//
LOCUS       WP_010561116             261 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010561116
VERSION     WP_010561116.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..261
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28882
     Region          23..184
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(26,28,109)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(55,108..109)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            107..109
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mnqrdvpsyn ieqlndkknk ycvcvfvine gdkvrkqier mqplseqvdi iiadggstdg
       61 slelgflkeh evttlltktg pgklsaqmrm afdyalaqgy egvvvvdgng kddisaipsf
      121 leklsegwdh iqgsrfipgg kaintplsrh lglkilhapl islsagrrht dttngfrays
      181 skllcdsrva pfrkvfeaye lhyylairas rlgfkvcevp vtreypktgk tptkispikg
      241 nllilktlfk aashqfnpge e
//
LOCUS       WP_010561151             135 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010561151
VERSION     WP_010561151.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..135
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14627
     Region          2..80
                     /region_name="T4P_ComGE"
                     /note="competence type IV pilus minor pilin ComGE;
                     NF041013"
                     /db_xref="CDD:468942"
ORIGIN      
        1 mkcvkgftli evliaaiilf tslaiiadif kgstllanka setarmyqvh ptaisaiksq
       61 lkdkvkvtka adangqiiif gveynwlaqr vvfnspppds isgaeypnvy giydvtveak
      121 lgdkiqdftf kaatw
//
LOCUS       WP_010561185             274 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carbon-nitrogen hydrolase family protein
            [Pseudoalteromonas].
ACCESSION   WP_010561185
VERSION     WP_010561185.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..274
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30355
     Region          2..264
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(42,94,111,115,128,153..154,156..157,178)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(42,111,153)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(112..113,134..136,154,157..161,163..164,186..187,
                     190..191,193..195,197..198,228,258..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mivvlqwtvs akpssnldyl rqqlvalrde hvndpllvcl pegfacfdak ahdlmafann
       61 sapfidqvcq lakqfnvwis agtipiaegt kyyaaslmvn qlgevvaryn kihlfdvdvd
      121 dakqnyresn ttiagkdlvv vdtpfgkigl ticydmrfpg lfgalrtlga eiilvpsaft
      181 vptgkahwlp llqaraienq vylvaaattg thdngrqtyg hsviispwge ieamlgdean
      241 nivylpnmdk ltdvrqkmpl lshnqfnyef kheq
//
LOCUS       WP_010561153             399 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [Pseudoalteromonas].
ACCESSION   WP_010561153
VERSION     WP_010561153.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..399
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=44052
     Region          1..398
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mefdysaidk sgsrhqgvis atskleaqkk lakdgltpis ikevseglsi eslfgnkvsl
       61 dqlefftsel slllesgvrv dkgidiirqs nvhpaltrll nqiatslkkg tslseafaqh
      121 eelfgplyvs lirigessgn laqvlarlsa dlkfqkdlrs qivtaltyps viffvcimav
      181 yfvltfivpk msgiftdleq apwytqmiin vsnffidyql fivggvvasl ialvyglkkp
      241 evkewfyltg skipgvksii ltserirfsq smammleagl qldatlslst gtlkhpelir
      301 darlaskqlk sgkqlsqvla ktrifsdffl siikvgeetg rlprvfseva srsrqdleqa
      361 ikkfttllep lmlmfmggfv ggivitmlms mvsindvaf
//
LOCUS       WP_010561212             269 aa            linear   BCT 01-JAN-2025
DEFINITION  ion transporter [Pseudoalteromonas spongiae].
ACCESSION   WP_010561212
VERSION     WP_010561212.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..269
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30608
     Region          15..224
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mftamqsqfq riddskafqa fvifvivvsa lsvgahtyal pvwmenllll ldkgitvffa
       61 veiairfias kgpkaffskg wnifdtiivi gsllpvagst vfiarllrif rvlrlvsmvp
      121 elrmlvnali kaiprmgyia llmfvifyiy aavgsmmfse inptlwrdvs ismltlfrva
      181 tfedwtdvmy etmavyplsw iyylsfiflt afiflnmmvg vvlevmtqeh dnfvkentde
      241 ldepatkgev lelkaqilel nkllserlk
//
LOCUS       WP_010561261             177 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Pseudoalteromonas spongiae].
ACCESSION   WP_010561261
VERSION     WP_010561261.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..177
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20337
     Region          6..176
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mhqaqeellv laaqsgntka ftylcrhyqk avtrfaykls ndpqivhdav qnawlkiann
       61 lhklndpraf kswlfkavrw svydlmraak rdketiandi dvldivastk peslelgsli
      121 eqlpdidkqv ihlfyleemq liqiaevlev plgtvksrly rarkalqksv edkqdey
//
LOCUS       WP_010561256             454 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TrkH family potassium uptake protein
            [Pseudoalteromonas].
ACCESSION   WP_010561256
VERSION     WP_010561256.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..454
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49763
     Region          25..437
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 miasyatsdh lahavkkrkk lfgappfils aaflalillg tvllklpisv hepiswiesl
       61 ftatsavtvt glvvvdtgsr ftlfgqvvia lliqcgglgl mtfaivtlla lggkigffer
      121 tvakeafnqt dsstlittak svlifaltve figmliltly wraelgwads lfhsffytis
      181 afnnagfals snslesyvdd pvinftitgl fiigglgfsv wmdikrnrrw krltvysrlm
      241 iigtvlinav aiiaiyciey nnpntlvpls esgkwlaawf qavttrtagf ntlpinqled
      301 astmlmlvlm figggslsta sgikvvtfmv lilatysylr rdnqiyvfnr eisretirka
      361 lalamvsimi twlaifvlsl tekadmldiv fetvsalgtv glsrgltgel stfgeliiif
      421 mmymgrlgpl tlayflatpr qkklryaetk laig
//
LOCUS       WP_010561285             535 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein
            [Pseudoalteromonas].
ACCESSION   WP_010561285
VERSION     WP_010561285.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..535
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58964
     Region          6..535
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mrhhsiqhki falltvtgil vlvaslltgq kqqselahqt ieqnikilad nyfdsintmm
       61 ltgtmanrei lrqkilseeq ikdihiirgd kinkffgpge anqapqnqqe nealngteqi
      121 hfsksedgsn litylkpvva senyrgtncl gchqategei lgavkisysl dkvdaavtrn
      181 swisfailtt ifvitfatlg wlfrkflier lrvigksmrl asqnndltih vedktndelg
      241 rlannfnlmm aafkgnisql sesskvlihs aekiyasaet teqainqqkq gtdsvaaain
      301 elessssevr ntthfasers dtsnhlaets leiaestees inglalevrt aakqvselqn
      361 rtlevgkvle visniaeqtn llalnaaiea arageagrgf avvadevrtl anrthdstde
      421 ikrtienlqs ealdtvntmn rssedadkra eqvkkvalal kdisehmkei nqlntqiada
      481 teqqnlaaee inqsviaisd naetslvdah eskqvsesll slareldqqv rkfkl
//
LOCUS       WP_010561352             688 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas spongiae].
ACCESSION   WP_010561352
VERSION     WP_010561352.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..688
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77313
     Region          26..658
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mklysliplv liapcamatd allddierit itsqridktp ldvssnitvf deetirslni
       61 snldellnfv pnfnmqaitg dyayiqvrgl prnyeqstls vfidgvpyss lyglnlpmnn
      121 iasvevikgp qgnlfgrntr dgiivintkk ptddisglae vgfaelgqts ikgnvsgali
      181 sdklwlnlgg nwtkrdgtvn ntllnsdvdp ineyatyakl yfeadnlsar lslnydekdn
      241 glapyvvaqp pldngddlei glnienefkq tnigyalsld wqinhwtlss itshleidtk
      301 avfdadysdq pygsyhssih ekdlyqefka tyqspnsdid wllgasynrn kqnnannypl
      361 famttrakle rtnhlayvdl nwqlndvlqv qvgtryfned vsadthyanm gypvpsiets
      421 aktqqsddrf lskaainyqf idnqrlyfsy gqgylsagts wlmeytddig irhgmgldyk
      481 pelsnnfelg ykadfdelat slelsifnte lkdyqhfhat vfgfsrvtni dtvksqgael
      541 nltsrildsv twqmsagynn ahveslntrh snldtskndk ipmtprysva nslmfsnqis
      601 sdiqldasis wqhsgdlyfd fketqkqsas nvfnanlsln fqeawtaslw vnnltdqrvq
      661 qfrivmpgsa lanyitprqv gvtfarsf
//
LOCUS       WP_010561420             270 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010561420
VERSION     WP_010561420.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..270
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29483
     Region          21..268
                     /region_name="COG4798"
                     /note="Predicted methyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443826"
ORIGIN      
        1 mktllnlais aaiatasitv ahattlqdtv ksevrsdknk ardefrnpqq tlnffglskd
       61 mnvveiwpgg gwyteiiapm vaekgkfvaa hfpsgtdigy fnkhlpkyqa kikntpalsk
      121 teitefhpkf spemapagsa dmvltfrnlh nfymtsdemm qstldaafka lkpggvlgvv
      181 dhklpenldt eafrqsgyik qsvveaaakk agfklvassg vnanpldqaq yekgvwtlpp
      241 tlalgdkdka kylaigesnr ftlkfvkpkl
//
LOCUS       WP_010561448             396 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [Pseudoalteromonas].
ACCESSION   WP_010561448
VERSION     WP_010561448.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..396
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44417
     Region          85..391
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mskveklisl wvkeafphld wlpqvlsics gvlllviiyy varclvlpgf ekltvyisph
       61 rlgqlkplfs klnrrlagfi csvvfvsgfr yfylpgdege vfyrsigqii aiiysgfifs
      121 svisiagaay nqlsfakevp ilgiiqvakl itfivtsili isvlidespa yilsgfgala
      181 avlllvfkdt ilgfvasiqi aanrlvkdgd wiqfdqygad geieelglnt vkvrnwdkti
      241 ttvptyalis qsfknwrgmq esggrrikra ihldlnsirl idsdfletlk snefitqvls
      301 neeldnakaq snvklfraya eeylrqheal nhnltlmvre lapsaeglpv elycfsadkr
      361 wipyehlqad imdhllasln mfglrpyqhv tgqltg
//
LOCUS       WP_010561468             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator [Pseudoalteromonas].
ACCESSION   WP_010561468
VERSION     WP_010561468.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..301
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=33812
     Region          4..127
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mlilrilvvd dskatleivr rslegfgyrh lsikktnnpi dalsiigqwq philltdwnm
       61 pelsgialik airkkqlktq igmittidda kqleqaqkag adfvlskpfd dqelyekllp
      121 lvqgaeqsei ildeieelse glalpnlaql ekslvkltsn eltintikaq vfdesklpci
      181 mavfedcetq kirsvtlldi yaactlaksn pnvtnghiqr viktkrpsky vmetsqqilq
      241 kvavafldhq srkslrlknt nfidqsfpkl enlyktpanr rldisiqipp laqgrvtiig
      301 f
//
LOCUS       WP_010561453             115 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Pseudoalteromonas].
ACCESSION   WP_010561453
VERSION     WP_010561453.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..115
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=12409
     Region          19..103
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mlktipdlik lasehvvkmd aaqakseiak nngllidvre paehaiknav gainiprgvl
       61 emklveiekd aerpiylhca tggratlaae qlqrigynkv tvisckaenv cdtfc
//
LOCUS       WP_010561517             230 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010561517
VERSION     WP_010561517.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..230
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=26307
     Region          6..222
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mnycyrlfdw alpnlcvcch qpvrapakic riclsdiarl nfkssanllh rpdinklipn
       61 ptfdslfavc wyqhpvsawl kglkfnkqlt ykaalhqlik aqvkdaqaeq nwqipdvlmp
      121 vplhwqrrvv rgfnqseeiw qrtsiavdtq sitrvkrtkp qselnkrark tnikeafscn
      181 lihqyqhvai addiittgyt vneiakllks agvkqvsvwv faisdptkps
//
LOCUS       WP_010561537            1033 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010561537
VERSION     WP_010561537.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..1033
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=112425
     Region          27..1033
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mlqwiiqtsl kykvlvllla amlailgvys vkqtpldaip dlsdvqvivk tsfpgqapev
       61 veeqvtypls tslmavpkak tvrgfsffgd syvyiifedd tdlywarsrv leylnqvtan
      121 lpsdakptlg pdasgvgwvy qyalidktgq qnlaqlrtlq dwflkyelqs vagvseiatv
      181 ggmvqsyqvv veplrlmqyg vtltqvksai enansevggs vlemaeaeym vrsrgfltdl
      241 aafkaiplgi inddgsplll ehvatirlgp qmrrgiaeln gegevvggiv vmrdgenalt
      301 tianvkakia qitpslpegv eivtvydrsn liersvenlq sklieemivv alvcliflmh
      361 arstlvavic lplavlagfi lmrlmginan imslggiaia igalvdaaiv mvenchkhle
      421 qyraetgena kgkahwqlvs kaavevgpal ffslilitvs fmpvfaleaq egklfsplay
      481 tktfvmaaaa llsvtlvpvl mgylvrgnip seqnnyltra lvaiyrpild lclkvpkftl
      541 lvaiviaass yyplsklgse fmpeleegdl lympttlpgv siaeageilq qtdrliktqp
      601 evlsvfgkvg raetatdpap ltmlettiql kpksewregv tlesiiaelq asvnfpglan
      661 awvqpiktri dmlstgvktp vgiqisgddl aqieqigrdv eriladvpgt lsayaeraqs
      721 gryidisprr kdaakyglni adiqtlvkya lggasigqsv qgkerfpinl ryprryrdqi
      781 eelktlpfls ptgawvtleq vadieikdgp amiksengrf iawtfvdlap dvvigdyiaa
      841 akaalgndll lpakhsirfs gqyeymervt sklellipit laiifiilyl afnsslqatl
      901 vmltlpmala gslwfvylld yqlsvavavg mialagvaae fgvvmliyln qalkqhkdil
      961 tavkqgsvqr vrpkamtvlt ivigltpiml gsgtgsevmq kiaapmlggm visplvsmlv
     1021 lpcayyllyr ikk
//
LOCUS       WP_010561652             189 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010561652
VERSION     WP_010561652.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..189
                     /product="YceI family protein"
                     /calculated_mol_wt=20232
     Region          1..189
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mlrslfsial latsfsslaa wqlqndsskl sfvsvkkdti gevhhfktls gtiaddgkls
       61 leidltsvet nipirnermq smlfntkafp tltlsadvsk elaamknapt hvfsvpatls
      121 lngiektlsi evfvartsqd dllvsamtpv vinasdfnld tgvaalqkva glpniaravp
      181 vtfvlhfak
//
LOCUS       WP_010561677             686 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas spongiae].
ACCESSION   WP_010561677
VERSION     WP_010561677.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..686
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75308
     Region          39..656
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mptaksiasf klstlklvis aslysgftia edeqelesie kiivigekad rtlkdtassv
       61 sviteetlrs iqnitvsqav seipnvvtlt gavpdirgvs gngsasgfng vtggararvs
      121 tlidgvaepf madltgdsgi wdveqievfr gpqstsngrn slggliyikt kdpsydwega
      181 arvgyrnqdq yvdtsvmasg plideqlafr ftgqllsges ydnsviyedh dptfdldelk
      241 ttrlkakllw epsalddfsa lltisdnsek gdtgrkyfka anpwdyiptg qrymdtdstt
      301 vsakfdykas nniafdllia gmdyqwgfet ydskvedrqi ltteeqnlti dgkmrfglnn
      361 dalygfvgla yfereqdyes vggseyhghd esdskaiyge vsyifaddft liaggrveke
      421 sqyrdyfgkk lsvldqdnti tlpklvlqya isdattatvs arkgynsagg aldwfageyy
      481 yydsesvntf etgirsslnn gninvsanlf yndysdyqat nlqrrisnid svvtyglete
      541 isamvtqdlr lnaglglmns eikddspgye singnelssa pgitanlgas ywftdalsak
      601 asisfvddyy getsnteeri agdytvarvs lnyelenwii nafinnltde kavtvyqpvq
      661 pggrlpdgya avvdprtfgg sityrf
//
LOCUS       WP_010561766             279 aa            linear   BCT 01-JAN-2025
DEFINITION  HDOD domain-containing protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010561766
VERSION     WP_010561766.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..279
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=30697
     Region          13..231
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mstenallti lvekinndtl vlptlpevav kvreaadnpe vnlmdmgdvi ahdpalsarm
       61 ikvansaflg ravkvstlnq avtriglrqi kniatamame qlfvsknkvv keylskswqk
      121 tvdvassait llslhlkdnk hsslnidtit laslvynigi lpilteaerh qevfanpqfl
      181 aqaiqklggr igghimrawd ftdefvevae lwanpeykpe npcyvdfirm aaisegllnv
      241 adkekslqay vdkgvlsdvs vlesdeysel lndvksmfa
//
LOCUS       WP_010561774             128 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010561774
VERSION     WP_010561774.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..128
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14362
     Region          4..128
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mnknkrvpts aelnilnvlw riqpatvrtl hehisesqki gyttvlkmlq imhekglvtr
       61 destrahvys aaysvehtqs sllsdivnka fggsrfdlvm ralgdektsa keineirtll
      121 dslennnk
//
LOCUS       WP_010561831             259 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Pseudoalteromonas spongiae].
ACCESSION   WP_010561831
VERSION     WP_010561831.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..259
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29050
     Region          3..259
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 maffdthchi dfdefendrd kvladsahfn vshmlvpgvt laqsakllcl entqditfyk
       61 alglhpyfly ehqegdferl atlakshref lvaigecgid rsiekldyqq qlfiqhiela
      121 nqlslplvvh hrkshdliae afkilkpkcg giihafsgsa qvanyyveqg fklgvggtit
      181 yaraqktrdv iasmpienlv letdapsmpl ygfqgerntp sqitrvfdel celkgietqs
      241 arimlaeqly ssscsvlri
//
LOCUS       WP_010561852             339 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010561852
VERSION     WP_010561852.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 339)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..339
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38742
     Region          <129..319
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mqkdllnsvv kitrhrdvds lelsllstis eflqpteaal ykdlsrfngk giessasllc
       61 deqgkihwrs reiieeptke lqcclesact islqdksgne trwipvvidd qvsgavyiva
      121 khlssseqvt lnalcriyen yltilneser dkltgllnrq tferkikqll edqlhshntp
      181 qlqgnrnkry desswlaild idhfkqvndt yghvcgdevl ltlaqkmqlf frssdlifrf
      241 ggeefvvvfe pttlehitak laefqqyvrd nkfpfveqlt lsigfsrmsp ydfpisvien
      301 adkalyvakn sgrnqcvyyg nildedsqeh psaddvelf
//
LOCUS       WP_010561983              92 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010561983
VERSION     WP_010561983.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..92
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10188
     Region          26..>75
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mtslsaeqrk eilaklesdv annvitigel vkqvrtqlyg mtqtqyakfi kvsdktlrdi
       61 ekgntdprvs vlnkilapgg fqlsvravrr ei
//
LOCUS       WP_010561993             219 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010561993
VERSION     WP_010561993.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..219
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=24258
     Region          1..>216
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mnfiayyrvs tqrqgqsglg lesqqsvvad yinrqegall hqytevesgk nnnrpelaka
       61 lqhcqltnst livskldrls rdlhflssvm qsnikficcd qpnsgplvlq vlaavaeeer
      121 raistrtkla lteakkrgve lgnpnfnevr ntctsnahsq fmtntkkyre ailpvienvk
      181 aagtttlkgi aeelnrlgfk srtgkqfyps tvrgligqn
//
LOCUS       WP_010562033            1029 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010562033
VERSION     WP_010562033.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..1029
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112952
     Region          1..1008
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 miltdisvkr pvfatvinll lltfglvafs mlplreypdi dtpivsvsts ytgassevie
       61 tkitqvlenr isgiegvksi nsssrngrsn itiefnidrd idaaandvre rvsraldslp
      121 eqvrppevsk sdsdespiaw fvlnstsmns lqlsdyaqry ivdrlavvdg vanvrlggqr
      181 eysmkvwlnr damaakgvta deiervlrqe nvelpageie svdrdftvri arsyksqsdf
      241 qnlvikrgds gylvrlkeva dvrleavdee nlfrgngkdm iglgivkqak antltvveka
      301 reeiekikrs lpegttiqds ydssifires iaevyrtlai amalvvavif lflgsvratl
      361 ipaitvpval igsftflygm gysinlltll alvlaiglvv ddaivmleni hrrvelgepp
      421 llaayrgare vgfaivattl vlvsvfvplv fmegrigslf tefamatsaa vifssltalt
      481 lspalcskil kpsekaskfs hkidalfskv engyenllrn nvassksmll llifaglasy
      541 llfkqlpsel tpkedrgtff immngpegas yennaqnmaq ieeklmpyqe ngelsrvlir
      601 vpgwggrggv aivgmadwde rkrdtwqvmg eisgkltdvt dvrafaimrs gvggrgnsrp
      661 vefvlqgnsy eeladwrdri lararenkgl vrldhdyket fpqflvsidk nkaadlgisi
      721 sqigrtlesm lgqrrvttfi drgeeydvil kgtkadfsdp knissiylks rnndlvplds
      781 liaideqata arlnrynrmr aitisanlaa dyslaealdf lnqvameend iegaidykge
      841 sqmfyegasa mtyvfilalt vtflvlaaqf esfvhplvim ltvplglvga ltglfftnss
      901 lniysqigiv mliglsakng ilivefanql rdkgvaftea lisaskqrlr piimtslttv
      961 mssvplvlas gpgsesrmvi giviltgvvv atlltlfvip sayymlarnt qspettekai
     1021 ndqasdhpl
//
LOCUS       WP_010562017             447 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudoalteromonas].
ACCESSION   WP_010562017
VERSION     WP_010562017.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 447)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..447
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48923
     Region          19..203
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          138..436
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mslltlsrks llnrfssiai ttiaialsit llllierarv dakasfhntv sgtdlivgar
       61 tgstelllfs vfrighptnn lsftsyqdit skrsvkwaip lslgdshkgf svigtnndyf
      121 thyryankqn lafskghafe qvnhvvlgsn vakklhyhlg dsivmshgag ntsfhhhddh
      181 pfkvvgilas tgtavdnsvh vplvaidnih gsatpsisqk hqaderhdhd hdhdhhddhq
      241 hhseqrdehs klpalsnael tgqpkqisaf llglkspifa lqlqrnisqy kqepllaimp
      301 kftlrqlwev vgvfekallv isgavvvial lgmltnllas lsqrrrelai lrsvgasprt
      361 iftllgleal litvcatlla iafyylvill lanmlgsisg ihlqlmalsq yqmsllagii
      421 llgtlfgclp aykayryals dgltikv
//
LOCUS       WP_010562069             179 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Pseudoalteromonas].
ACCESSION   WP_010562069
VERSION     WP_010562069.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12134272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..179
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20502
     Region          7..156
                     /region_name="Acetyltransf_3"
                     /note="Acetyltransferase (GNAT) domain; pfam13302"
                     /db_xref="CDD:379112"
ORIGIN      
        1 mqpsssrlny sfitekdidd lyqldqdpav mkylnggkpt tmeekhtvfl prmakyanke
       61 kgwglwkvni kesgefigwi lvrpmhffnd etdtqwhnle lgwrfkqssw gkgyateaan
      121 alveqialmp eythisaial kenagsigvm eklgmtfvke ymhsdplgdi pavyyerel
//
LOCUS       WP_010562076             601 aa            linear   BCT 01-JAN-2025
DEFINITION  ferrous iron transporter B [Pseudoalteromonas spongiae].
ACCESSION   WP_010562076
VERSION     WP_010562076.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Marlovits,T.C., Haase,W., Herrmann,C., Aller,S.G. and Unger,V.M.
  TITLE     The membrane protein FeoB contains an intramolecular G protein
            essential for Fe(II) uptake in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 99 (25), 16243-16248 (2002)
   PUBMED   12446835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     gene            1..601
                     /gene="feoB"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0015093 - ferrous iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
     Protein         1..601
                     /product="ferrous iron transporter B"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0015093 - ferrous iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65760
     Region          1..598
                     /region_name="FeoB"
                     /note="Fe2+ transporter FeoB [Inorganic ion transport and
                     metabolism]; COG0370"
                     /db_xref="CDD:440139"
ORIGIN      
        1 mkrillvgkp ncgksllfnq ltglkqkvan fpgvtvelks gqfndfevvd fpgtyslntl
       61 skdeqiavek lneainqddt evivnvldat rlerslvfal qvqhlaqqhn kkvvfalnli
      121 delqrfnhqi dvaqlakdln apvfalsakt ligvtefqkg lveiakapfq qnlhsdpskn
      181 vqsakalakk yaiasdivlk kqnvidnfll nsvfgavaff timfllfqsi ftwaaplmdg
      241 vemligdtaa lvtgllpsgm mqdftadalf ggvgsflvfv pqimvltfii glledsgyla
      301 raalichkpl sffglsgrsf ipylsahaca ipaimaarti esprkrlitm mtiplmscsa
      361 rlpvyallve vfipadhtvl gifnlqgiaf falylfgivm alivsallsk skmteqsqse
      421 mpfilelpty rmphwkplmh rvlnsgiyfi kraapvifmv svviwvlgyf pqnadlehsl
      481 lgqfgqfiap vfeplgvdwr ygvaimmsfl arevfvgalg tlygmegade niaglasqim
      541 adglplgtgi glmlfyvval qcvatvatik aemgnaklaw alfvvyglva yclaalahyf
      601 i
//
LOCUS       WP_010561981             444 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Pseudoalteromonas spongiae].
ACCESSION   WP_010561981
VERSION     WP_010561981.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..444
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=50738
     Region          <146..438
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mklkkrvkra ktqlkklele qgknfkltkl ydclyvkstd gdvtavfrkq vrgkrpyitl
       61 gkltknycve kalsdcwene ksmlthgfvd qeftelqkri nsietlndla cefflhhdei
      121 nfptgkeplk elpalqkkyq qyaqsyiget lvasidrkhi irvmnkvyek spqsqcplcs
      181 mysvcehcen lddyaalans vlyvlkrvle lgvqygiikk nvaatikakd vgykpqsnrr
      241 alimqelatl vkrleksmes epanvcavyl lllfgarkme lvkakisefr meliplkggl
      301 nfeedmcwvl qttktgatra kfitplmkky ldrlvelnng skyllpsrts askspyisas
      361 tlnkfiaria sdlkfvvhel rhttrtllsn leipddvgds yithskkkyl hdalhlyskr
      421 keaaidlsnl ietlikrane gtks
//
LOCUS       WP_010562154             626 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein
            [Pseudoalteromonas].
ACCESSION   WP_010562154
VERSION     WP_010562154.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..626
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=69117
     Region          141..626
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mellqrltik arlqlnaffv gaamfilllv ilyeasvmlk lntaiqltee laihegvlrk
       61 heknflfykn vdslelfdne fkllknkssn lnellqeldi stktlaglng iidqynadfn
      121 evvalqrrig lhpkdaaygn lraavhqvet llkkqnnyql ladmlqlrrn ekdfmlrldk
      181 kyltrfnnni nvfksniqqa dfdssyrsel ltlldtyqre fsalvsaqea lgldlesgal
      241 gkmaasvaks dvlvdrmtae tkeaieqsad ftstvaiiif vlstvvvmtl vymtsrsiil
      301 pvnkvcdiih tirstndltr svqsagqdei armtgdfdsf indfknlife vkqalgilns
      361 atenlantta etsdgmreql headmvataa temqatiqdi shnteaaakk aestnesamq
      421 gkqevdstva riseltnslt hasdvvtqle qdavtigsvl dvirgiaeqt nllalnaaie
      481 aarageqgrg favvadevrs laqrtqdstq eiesiistlq qrtqevvsvm ercktqgsss
      541 seqavqagtl lysisedvqt imdmstqiat aideqnqvas evnknvikir diaeqaatha
      601 qtnaqtseev stqaevlhra iekfnv
//
LOCUS       WP_010562104             406 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010562104
VERSION     WP_010562104.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..406
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=45884
     Region          <59..405
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 msslymqlye kiektffftl trkifgnlsf lfafqvitli wlyqeltdng hidmsywfia
       61 lisigsffft cfymhflivr pinalkktlt dinekgadla thlpqftfde frelseqynt
      121 fvsrleallk qvyekaelae mtnqnvtksm tetnrigeeq lalsntifta seevsqslnq
      181 isqntqmtfd anvenlskvh tsaneignlv tkiqrmtell gsfattvggl kensdnirki
      241 ltmveefsdq tnllalnaai eaarageagr gfavvadevr slsvkvndat rqindfinqm
      301 ntlvgetnre teqlieqsss aessiantnd vfsqmtkele snqsqlqeiv aavhqlehtq
      361 qqthssvqqi velghmakdk itnanensre lqcqtsdtkk dleqfi
//
LOCUS       WP_010562187             401 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dipeptidase [Pseudoalteromonas].
ACCESSION   WP_010562187
VERSION     WP_010562187.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..401
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44244
     Region          36..397
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mkyliktsli asaimatfta gatqytasek avklaqenll idthidvpyr iyhkwddvsk
       61 ateggdfdyp rgvkgglnvp fmsiyipanl efegkgksyq lanqlidgme alaqrapdkf
      121 aiatstadve aqfkqglmsl amgmengspm egemanlkhf fdrgvryitl ahsqsnhisd
      181 ssydirrkwk glspfgkdlv kemnkigmli dvshisddaf yqvmelsevp viashsslrk
      241 ytpgfernmd dkmllalken ggviqinfgs sfvtsaagaw gdkmkaarkq aketfgenss
      301 qvkdfrkays aknpypfasl eqvlnhidhv vkligidyvg igsdydgvgd slpiglkdva
      361 sypnlvqgll drgysdkdii kllggntmrv wreaesyakk h
//
LOCUS       WP_010562245             133 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010562245
VERSION     WP_010562245.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..133
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=15315
     Region          11..133
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mlvlitrvif mdisnsefev lqalwrvhpa daqtvvdeln kekdwhektv ktllgrmvkk
       61 gaisfekngr syiyspvlei eayqvqeses lierlfngri aplvtgfakn knlskqdide
      121 lkhlidkwek nnd
//
LOCUS       WP_010562324             218 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pseudoalteromonas spongiae].
ACCESSION   WP_010562324
VERSION     WP_010562324.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..218
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23550
     Region          15..217
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 msldaviiep qsshkatviw lhglgdsgdg fapivpelnl paelgvkfif phapiqpvti
       61 nggmamrswy diksldldkr adeqgvqqsa aavqqlidae idngiapsni ilagfsqggv
      121 vslylaprlp yqlagvmals tymcepaklk lekqqaslnv fmahgsfddv vptgagkaah
      181 qtllelgyev swqeypmthq vcleeikair twlvsrln
//
LOCUS       WP_010562346             214 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Pseudomonas extremaustralis].
ACCESSION   WP_010562346
VERSION     WP_010562346.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..214
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=23965
     Region          4..191
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mtqrilvilg hpsnaslcst ladtythaak iaghevrvlr lgdltfdpil hdgyqqiqpl
       61 epdllsaqsd ilwathltfv fpiwwggipa llkgfidrif lpgfafkyra gkafpdkllq
      121 grtahllvtl dtppwyyrwf yrmpgihqmr kttlafcgiq piktllfgpv lgstpaqrst
      181 wlkqagalve kgsfhvhrhs rttighdrqg dssl
//
LOCUS       WP_010562360            1062 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type I restriction endonuclease subunit R
            [Pseudomonas].
ACCESSION   WP_010562360
VERSION     WP_010562360.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1062)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1062)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1062)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1062)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..1062
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=118940
     Region          7..984
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mshihhecel erhiveqlaa agwlvgksad ydaaralfpd dvlgwleesq pqamaklham
       61 ngtgtrdvvl drlvkqlenk vdggtvnvlr ygfavagggt lamsqglped drnetviqry
      121 asnrlrvvpq lrfsldktde idlaffingi pvatvelktd ftqsvqaamq qyrmdrkper
      181 ksggfepllt fkrgavvhfa msdsdirmtt klagdstffl pfnrgndgaa gnppgdndsy
      241 pvsylwkrvl qkdnwlhifh ryvlqerkea qdlngktyfk eglifprfhq wegvtkmida
      301 vriegagqpy liqhsagsgk tntiawtahs lirvrrpdge pyfhsvivvt drqvldqqlq
      361 daiqqiehqa gvvcaidrqq sslpksqqla kamldgvpii vctlqtfpya qkailgetsl
      421 rdrrfaiiid eahsstggst addlryvltg qsedewdrls keerlsvwqs srsrpgnasy
      481 faftatpkhs tlslfgrprn aaqpvnqenp papfhlytmq qaieegfild vlknytgynv
      541 afkigsefvd dkrvdeksar rklakwlsln pvnvgqkvel ivehfrknva hllggqakam
      601 vvtssraaav kyhlalldyc qrkgydnvqa mvafsgevpn sdvqetglpa dhqfsetnln
      661 pglngrdmrk vfdtpdyrvm ivankyqtgf dqpklvamyl dkkisgveav qtlsrlnrtf
      721 pgkdktyvid faneaeeila afktfyrdaq vadiqdpniv ydikqrldgm fiyeaaevea
      781 fgeaivnrnv thqklysltq satdrfngkl ktlndgidqw ekaweaahdn gdekgmeysd
      841 vqraeycmgr delmifsesl tkfvrtyeyi aqlvefgdpa leafasyarl lrkrlkgvsa
      901 eqvdlddlkl shykikkgeg laglsavgea pelygitdng lrdardrekk ylteliekln
      961 nafgkditdt dqvafavhvs eklrgdtvvm aqvqnntmdq amkadlpska iqaiasamss
     1021 htsmatklls destrdvflt vvyellkkda giellsstrt si
//
LOCUS       WP_010562375             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010562375
VERSION     WP_010562375.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24091
     Region          14..135
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mppqererei ieeavrffae vgfegtlrel aerlgithqn lfryfatkea lidrvyqevy
       61 lsrwqpewea mlkqpgktle arlidfykay lpaifrydwv rififaglkg vdisqrylsl
      121 iqtkviepva melrelscek ppgetlssae levawglhge lfylaqrrwv ydmtvpedld
      181 rfieisiirf lhgapaamqa ltrdgan
//
LOCUS       WP_010562379             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010562379
VERSION     WP_010562379.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22345
     Region          2..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkpryddtrq hlldtghrmm vvkgftgvgl neilqaasvp kgsfyhyfks keqygqclle
       61 dyfrnylanm derfaatgnt arerlmgywq kwlesyckpc deqkclvvkl saevadlsev
      121 mrltlrdgtd qiierisgcl eqgqldgslp qgdayrtala lyqlwlgasl lsklhrnsrs
      181 lenamattlm mlvpeea
//
LOCUS       WP_010562392             374 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkene reductase [Pseudomonas].
ACCESSION   WP_010562392
VERSION     WP_010562392.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..374
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40973
     Region          5..355
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,235,309,329,331..333)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,235,249,309,329,
                     331..332)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,332)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqselfktt qlgpytlknr ivlppltrsr ssqpgniand lmatyyrqrs gagfmvtegt
       61 qieprgqgya wtpgihspeq iqgwrkvtda vhaeggvifa qlwhvgrvsh tslqpggeap
      121 vapsairadn vkvfietgpg tgaladpstp ralstkevke lvelyaqaar naldagfdgv
      181 elhcangylv nqfisahtnq rddeyggslq nrlrflreit lavagvvgke rmgvrfaplf
      241 attdedrvyl glveedphqt yieavkilee vgiaylslae adwenapelp etfredvrkt
      301 fsgkilyagk ytaergnrvi kagwgdliaf grpfianpdl pariannwpl npvdpssmyg
      361 gtdkgytdyp tyks
//
LOCUS       WP_010562469             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YdcF family protein [Pseudomonas].
ACCESSION   WP_010562469
VERSION     WP_010562469.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..253
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27882
     Region          34..253
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mpiryfikql llppgiflll lalawwlrrs rprlagccfa lglggmwlis lpvmvewgar
       61 alesapplar edwstlaqra daivvlgsgr ergdpawgad qptgiglerq ryaarlakas
      121 glpvlttggl hygtppseaq lmavsmqddf gvavrwkeer srttwenaqm saeillpegi
      181 krvvvvtqaw hmprsvwsfe kagftvvpap vgflgvdnar plggwmpefk svwqsgqlin
      241 eavgqvgyrl fyr
//
LOCUS       WP_010562452             438 aa            linear   BCT 01-JAN-2025
DEFINITION  bifunctional DedA family/phosphatase PAP2 family protein
            [Pseudomonas extremaustralis].
ACCESSION   WP_010562452
VERSION     WP_010562452.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..438
                     /product="bifunctional DedA family/phosphatase PAP2 family
                     protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=47039
     Region          8..206
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
     Region          231..399
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(301,308,323..325,367,373,377)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mgqwldsmtg wltlnpqwla vavflvacve claiaglivp gtvllfaiaa lagsgalsls
       61 etlllgflgg llgdgvsyyl grhfhqnirr lpglrhhpew mngaetyfhk ygiasllvgr
      121 figplrpmlp mvagmcdmpf prfaavsiva aagwtvayll pgwatgaafr lplpagfwpe
      181 agvvaaclav llglslnssl rghrratlwi gcasltslia vfigyphlnd fdqglsalvq
      241 ehrsawldev mvrvtqlgef kkmlvasavf tvllllarqw rhavfvaatl agaalintgt
      301 klffargrpe ilsepltsfs mpsghasgaf afflalavla grgqptrlrl twmllgcipa
      361 afialsrvyl gahwptdila gtllamtvca fsltacqyrs plpampqktw wlllpvlvav
      421 lsfialsgts hallryay
//
LOCUS       WP_010562514             253 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2076 domain-containing protein [Pseudomonas extremaustralis].
ACCESSION   WP_010562514
VERSION     WP_010562514.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007341
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..253
                     /product="DUF2076 domain-containing protein"
                     /calculated_mol_wt=26821
     Region          1..233
                     /region_name="COG3416"
                     /note="Uncharacterized conserved protein, DUF2076 domain
                     [Function unknown]"
                     /db_xref="CDD:442642"
ORIGIN      
        1 mnseeqtlid glfsrlqqae tdsaprdaqa earikehmtr qpavgyymtq silvqehalk
       61 sldaqnkqqa qqiqqlqdel qraksqaaqp apasggflss ifgggprdpq ptqsapassg
      121 ggwrepgrps fgqpapqqny gapqqnyqqp qapaapigsg flggalktaa gvaggvmlae
      181 gisslfnhns qqpqvveeii revpapasdn snwgnddqkf agndswgsnn adnfadsdys
      241 dnsssfdddd sfv
//
LOCUS       WP_010562519             444 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Pseudomonas extremaustralis].
ACCESSION   WP_010562519
VERSION     WP_010562519.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..444
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48486
     Region          1..390
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtfatlglie pllraletlg yqtptpvqaq aipavlagrd lmaaaqtgtg ktaafavpll
       61 qlltmegpkv aansaralil cptrelaeqv hasvaeyaqh lplttyavyg gvsinpqmmr
      121 lrkgvdilva tpgrlidlfr qnalklnqlq tlvldeadrm ldlgfseela niyrmlpkkr
      181 qtllfsatfs deirtlagqm lndplsievs prnvaantvk qwvvpvdkkr kaelfvhlmr
      241 kgrwkqvlvf aktrngvdal vdklqglgin adgihgdkpq atrqrvldrf kssdvqilia
      301 tdvaargldi edlplvvnfd lpivaedyih rigrtgragn tgeaislvca devnmlsaie
      361 mltrqtlirk meadfepehr vpdtdasgqv vkkpkkpkkp ktsggggkrn lgkwvdsgev
      421 apaepsikpv rkvpvfntgp rkkk
//
LOCUS       WP_010562358             315 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GIY-YIG nuclease family protein [Pseudomonas].
ACCESSION   WP_010562358
VERSION     WP_010562358.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Dunin-Horkawicz,S., Feder,M. and Bujnicki,J.M.
  TITLE     Phylogenomic analysis of the GIY-YIG nuclease superfamily
  JOURNAL   BMC Genomics 7, 98 (2006)
   PUBMED   16646971
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10179942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..315
                     /product="GIY-YIG nuclease family protein"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34239
     Region          52..141
                     /region_name="GIY-YIG_unchar_2"
                     /note="GIY-YIG domain of uncharacterized hypothetical
                     protein found in bacteria and archaea; cd10447"
                     /db_xref="CDD:198394"
     Site            order(52..54,70..72)
                     /site_type="other"
                     /note="GIY-YIG motif/motif A"
                     /db_xref="CDD:198394"
     Site            order(54,70,72,80,84,122,139)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:198394"
     Site            122
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:198394"
     Region          243..296
                     /region_name="DUF4357"
                     /note="Domain of unknown function (DUF4357); pfam14267"
                     /db_xref="CDD:433823"
ORIGIN      
        1 mnpgrsirlf lvdgtpngll taeimnwtgh vltgprskla elvqrpecgr tgvyflvgpd
       61 pdnnlrskvy igesddvakr lkqhnrpeas egtaggkdfw ekvclvtskd qnltkthvky
      121 lesllisian qvgrcellng tahdygslpe sdradmaffl eqirtvlpvl gfdflreltk
      181 psaavstspa ipvshsprfn levprysisa qgqeidgeff vlkgskarae wvgtergyqg
      241 lfkqlvgegv mvaqgsnnlv fsddyafssp saaaavvcgr sangrtswvv egtgqtyaaw
      301 qdqqlnsvtp epeae
//
LOCUS       WP_010562525             325 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Pseudomonas].
ACCESSION   WP_010562525
VERSION     WP_010562525.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..325
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35735
     Region          122..287
                     /region_name="Abhydrolase_6"
                     /note="Alpha/beta hydrolase family; pfam12697"
                     /db_xref="CDD:463673"
ORIGIN      
        1 mnkrsgwllg lllitsptwa aehgvkevsp drfhlesgdl slglsqdwrq plpqvtrali
       61 ivhgrlrnaq tylqsgveaa eraglgsttl viapqflnas dvkrnhlddr llrwngndwm
      121 agapstgpgq issyaaldqi iehlgnrqrf palkeivvag hsgggqvvqr falighdhpt
      181 lqtegirlry vvanpssyay fsparpvtfd aascpgfndw kyglqhlpay akgqsaerle
      241 qayvsrdity llgqqdtdpn hpaldkscaa eaqgayrlir ghyyfddlqq rhpqlrqtlv
      301 evpgvghngd gmftspegqk vlfak
//
LOCUS       WP_010562548             121 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudomonas].
ACCESSION   WP_010562548
VERSION     WP_010562548.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..121
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13781
     Region          7..103
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mteqasdrrr frriafdakt elrqngkewp vqlvdlslkg llaqrpgdwk gnkalpfdvd
       61 irldpktpik mqvrlahdah gllgfvcqhi dldsishlrr vielnlgdqh dldrelaall
      121 e
//
LOCUS       WP_010562535             431 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Pseudomonas].
ACCESSION   WP_010562535
VERSION     WP_010562535.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..431
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44760
     Region          1..429
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mleklfqlka hntnvrteil agittflama yilfvnpsil getgmdkgav fvatclaaai
       61 gstvmglian ypialapgmg lnafftytvv lhmghtwqva lgavfisavl ffilsifrir
      121 ewiinsiplp lrsaiaagig lflalialhn agivvsnpat mvglgdlkqp apilatlgfa
      181 livalealav rgavligila vtivsiamgf tpfggvtsmp pslaptflql dikgaldigl
      241 vsvifaflfv dlfdnsgtli gvakraglmd knghmpkmgr aliadstaam agsllgtstt
      301 tsyiesaagv saggrtglta vvvailflla lffsplassv pafatapall fvavlmtsgl
      361 aeidwdditv aapvvitala mpftysiang iafgfiawta ikllsgryre lnpalvilsi
      421 lfviklgwfn a
//
LOCUS       WP_010562578             379 aa            linear   BCT 01-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Pseudomonas extremaustralis].
ACCESSION   WP_010562578
VERSION     WP_010562578.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..379
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41496
     Region          <38..100
                     /region_name="DUF3391"
                     /note="Domain of unknown function (DUF3391); pfam11871"
                     /db_xref="CDD:432148"
     Region          <78..299
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mlkcnefyyl apdsetrpyw sdltgnapsn apcamgcaps paetavssdp ataqapaata
       61 ipptcmkdel vaaqeictra kaavvemfsh vrmgralele nigalvddia ssiarhpnaf
      121 islarlksld dytymhsvsv calmialgnq lnfpaeltrr agmagllhdi gkmaipgail
      181 nkpgrlndde vqlmrthpqe gektllataq mcdmvvdvcl hhhervdgng yphqlagdqi
      241 slfarmaavc dvydaitsdr aynqawdpav aiqqmstwdg hfddevfraf lksvgiypvg
      301 sivqlksgsi gvvieqhpas lltpkvklff lpvlniyitp rivdlsdpeq tdriiarvpp
      361 qrydfknter fwlndevpe
//
LOCUS       WP_010562619             469 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF262 domain-containing protein [Pseudomonas extremaustralis].
ACCESSION   WP_010562619
VERSION     WP_010562619.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..469
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=54051
     Region          17..441
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 mtnlsmeaiq tqqatelssk iisvfellmd saldipqyqr pykwtgknin qlfsdiaihk
       61 dksayrlgtv vfhheggtrn ivdgqqrtis lllaaraliq rnneeklkrk dlrerllkle
      121 qamvnpgfts eisqknihsn ylevarivsr adfteahidf flnkcqvvav alndvseafq
      181 ffdsqnargr dlephdllka yhlrefsprd eqlkaatvar wensdtdela tlfsqylyri
      241 rnwskgvsar yfskddgdlf kgvnidtvts ypyveqlria hhfvdnyngq yerkidsrel
      301 gfpfhldqii ingrrffeli shyqgkvari saeswnghel vgaegldgya ktimdtlnsy
      361 partrtgdcy vramfdclli yyidkfghad israiekifi wayslrlkmq vvqlasmdnh
      421 vlennlfrli kdatrpadfi nctlpvlsgq kstrtgeiet lfkamkyye
//
LOCUS       WP_010562699             105 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Rieske (2Fe-2S) protein [Pseudomonas].
ACCESSION   WP_010562699
VERSION     WP_010562699.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..105
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=11318
     Region          4..105
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mkflcpsdal apnsslgfev dgikllavrr dgivyfyinr cphrgiplew qpdsfldtsa
       61 sliqcathga lflietgeci agpcagqslk alpgredeqg lwvql
//
LOCUS       WP_010562725             253 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010562725
VERSION     WP_010562725.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..253
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27500
     Region          40..226
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mklaslgdsr rgpaqiwnsa pqlaqippia paslvtpgar vvivaphpgd evlacggllq
       61 slstlehplk lisitdgsas hpgsdvwpar rlsvvrpqes aealrrlgmp lhslkwirgg
      121 fcddalaase aqlsqfiary lqpgdvvfst wrhdgnddhd tvgrasakac slvgarlyel
      181 piwawhwpar egaiipwhra rkvrldtwsv arklhaahay asqlagdpqi glapmlaqvl
      241 lermrepyei vfv
//
LOCUS       WP_010562728             252 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010562728
VERSION     WP_010562728.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..252
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27732
     Region          39..225
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mranpiigqg tplqrwqass rlaelpligv etlvpeghra viiaphpdde vlgcggllqg
       61 laalgrpmql isvtdgsash pgsrrwpver lsvvrpqesa lalrrlgvpl qelkwlragl
      121 adsqvaared elarfiqrhl nptdvvfttw sedghcdhea vgraslraar avgatvyelp
      181 vwtwhwacpe dsrvpwhrar kvplsdeaia rkrhaihafv sqlegdpqig lppvlapyvv
      241 erllqpfevv fl
//
LOCUS       WP_010562751             313 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Pseudomonas
            extremaustralis].
ACCESSION   WP_010562751
VERSION     WP_010562751.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Grant Pearce,F., Hudson,A.O., Loomes,K. and Dobson,R.C.J.
  TITLE     Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and
            Evolution
  JOURNAL   Subcell Biochem 83, 271-289 (2017)
   PUBMED   28271480
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Laber,B., Gomis-Ruth,F.X., Romao,M.J. and Huber,R.
  TITLE     Escherichia coli dihydrodipicolinate synthase. Identification of
            the active site and crystallization
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 691-695 (1992)
   PUBMED   1463470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..313
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0009436 - glyoxylate catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33514
     Region          9..272
                     /region_name="DHDPS-like"
                     /note="Dihydrodipicolinate synthase family; cd00408"
                     /db_xref="CDD:188630"
     Site            order(12,44,47..49,136,164)
                     /site_type="inhibition"
                     /note="inhibitor site"
                     /db_xref="CDD:188630"
     Site            order(44,47..49,136,164,209)
                     /site_type="active"
                     /db_xref="CDD:188630"
     Site            order(48,53..54,82..83,107..108,116,120)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188630"
     Site            164
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188630"
ORIGIN      
        1 msdtiftgci palmtpctaa rtpdfdalva kgrelveigm ravvycgsmg dwpllteaer
       61 qegvarlvaa gvptivgtga vnsreavaha ahaakvgaqg lmviprvlsr gasataqkah
      121 fsaileaapt lpaviynspy ygfatraelf fdlrrehpnl igfkefggga dlryaaehit
      181 shddsvslmv gvdtqvvhgf vncnatgait gvgnalprev lqlvalskqa akgdakarrl
      241 aaeleaalav lssfdegcdl vlyykylmvl ngdtayalhf netdvlsdaq rhyaerqyal
      301 frqwytnwsa eqc
//
LOCUS       WP_010562763             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cysteine hydrolase family protein [Pseudomonas].
ACCESSION   WP_010562763
VERSION     WP_010562763.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..201
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21644
     Region          7..177
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mnphttalvl ieyqndfttp ggvfhdavkd vmhasdmlan tattvqqarr lgvkiihlpi
       61 qfaegypelt trdygilkgv sdgsafrags wgaqisdait qeagdilveg krgldgfatt
      121 gldlvlrnng iqnlvvtgfl tnccvegtvr sgyekgynvv tltdctatft deqqhaaenf
      181 tlpmfsttlq hseflrglda q
//
LOCUS       WP_010562780             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: arsenate reductase ArsC [Pseudomonas].
ACCESSION   WP_010562780
VERSION     WP_010562780.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..163
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=17106
     Region          2..135
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(7,9..14,104,106)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mkvlfmctan scrsilseam fnhlapqgfq avssgsfpkg qvlprslstl qaagistegl
       61 yskgndafeg sppdlvitvc dkaageacpv yfgpavkahw gledpsdvng deasvqaafd
      121 atletiatrc raffalpfsq ltpvqlkael eriaglqavr htg
//
LOCUS       WP_010562779             263 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010562779
VERSION     WP_010562779.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..263
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28322
     Region          20..141
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          177..257
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msavqhawlg hyeissttct gltfarhshd ecvigvnlvg eekvwldrse faagpgsitl
       61 ynpgqiqggg aadgapwqfv slyvtaeqla adlglaqmef dralcfqpdl arrlatavkg
      121 alsgdglvrd lnedalvlll aevvnlsgvr lpgtvasgkg ligraqella ehlhqalpld
      181 rlgdelglsk fhllrtfqke tglsprqwam qlrtrrakgl lrkgvaasev ahdlgfadqs
      241 hlnrhfraay gmtpghyqsv lkp
//
LOCUS       WP_010562784             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AzlC family ABC transporter permease [Pseudomonas].
ACCESSION   WP_010562784
VERSION     WP_010562784.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..231
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24718
     Region          10..226
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mstavphyaf argaiavipl slacapwgll agsmaidaqf tplqaqglsa ivfagaaqlv
       61 aigmvksgas lisivlttll ltsqhllygm hlrptvsplk arwrmslgfl ltdeffalvs
      121 hydretfnrw yalgvgltfy iawnlftlag ivlgksipgl dqlglefsia atfialitpv
      181 vrdvptlvcv avslwfsvwl sflhwesavv vsgvlgmsag ffckrlgvgq r
//
LOCUS       WP_010562788             234 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YoaK family protein [Pseudomonas].
ACCESSION   WP_010562788
VERSION     WP_010562788.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..234
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24909
     Region          23..227
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mlpsprkpyv naalahqqrw rgrigmtlva slsvlagmtd aigfmasgdf vsfmsgnttr
       61 lavaisegdl glmgrllllv atfvagnalg vmvsrfsrrh alplllciat llcgatllpf
      121 ndmlptllaa iiamgmlnaa veevnglpvg ltyvtgalsr fgrglgrwll gerrdgwrvq
      181 lvpwmgmfvg avigallqqq mglkallvsg imagllglvs lkiprrwhlg fmpr
//
LOCUS       WP_010562816             380 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerate kinase [Pseudomonas extremaustralis].
ACCESSION   WP_010562816
VERSION     WP_010562816.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..380
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38940
     Region          2..374
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mkiiiapdsf kdslsaegva qaiaeglaqv wpdahviqcp madggegtvd avlaacngel
       61 rrqtvcgplg gavearwgwl adshtaliem aeasglqlvp pgqrdacsst tfgtgelira
      121 aldagaerii laiggsatnd ggagamqalg vqlfdaadqa lspgglalar laqvsldnld
      181 prlaqvrfei aadvnnplcg phgasaifgp qkgadpeqvq qldaalghfa dhcakvlpkd
      241 vrdepgsgaa gglgfaakaf lgaqfragvd vvaelvglda avrgadlvit gegrfdaqtl
      301 rgktpfgvar iarqhdvpvi viagtlgdgy eqmyahgvaa afalpsgpms leqacneapr
      361 llreraadia rvwrvarrsq
//
LOCUS       WP_010562817             427 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [Pseudomonas].
ACCESSION   WP_010562817
VERSION     WP_010562817.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 427)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..427
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47546
     Region          1..341
                     /region_name="COG3950"
                     /note="Predicted ATP-binding protein involved in virulence
                     [General function prediction only]"
                     /db_xref="CDD:443150"
ORIGIN      
        1 mqikrftlvn frgiekmeld fegkktvalv gvngvgkssi ldalaitlss ltarmvgqps
       61 ksrsiakddi kvgadytrlh vetklfenyn vdwaialnrk agkggkhpse rssdlsrlne
      121 aadsvehgig qyeviggksi elplavyydv hravldvplr vrehlvnaia egyddalghg
      181 gadfkrffiw frnqedlene nsrdipgyrd pelsavrrai etftgfkdvr vrrkpalrmt
      241 vlkgelefnv lqlsdgekcl lamvgdlarr ltllnrevpd plqgkgvvli deldlhlhpg
      301 wqrtvvanle ntfpncqfii tthspqilge lpaesvmllk dgqylghper slglrsgevi
      361 eelmgglsqn qnvsqqlrki yrnlddddle saqihlaqlr ekvgkipdvl evqasidslr
      421 sleegea
//
LOCUS       WP_010562875             320 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Pseudomonas
            extremaustralis].
ACCESSION   WP_010562875
VERSION     WP_010562875.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..320
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=34643
     Region          20..206
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     Region          130..294
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mlevlsaegl ralladwqpl rglnlaggdy rgvdlsnarl edvdargaqf ngamltqsyw
       61 kdcrldganf sdstadslym nacslqgasf mnvrwnktsw aqchgedldl sgaqlqaftl
      121 secrvprirl aaaqlsksqw srcdltgldg qsahfakarl idcqldqarf glaslqqcaf
      181 desslsgadf havqaegasf yrckgaapmf vgahlkgalf nashfdsvdf seavlemail
      241 idaqmpgarf drallryadc tallaprasf vaadvtgmna haadftqadw qqsnpqaiqp
      301 vdterlaaeq wrpaslgksr
//
LOCUS       WP_010562903             259 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas extremaustralis].
ACCESSION   WP_010562903
VERSION     WP_010562903.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..259
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28407
     Region          60..240
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msrvydylde tfavcdaevr klvrdptell sraiqpvlwl avfgqvfsqv rgiptgnlry
       61 ldfmapgila qsilfsaify giaiiwerdl givhkllvtp ahrsalimgk afaaglrglv
      121 qaavvylvai alhveirwev mpmltvaagv fvgscifstf slviacivkt rerfmgigqv
      181 ltmplffasn aiyplelmpd wlkviavcnp ltylvdalrs smivgghsvy alstsftvml
      241 svfamlllla arlypglar
//
LOCUS       WP_010562926             229 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dienelactone hydrolase family protein [Pseudomonas].
ACCESSION   WP_010562926
VERSION     WP_010562926.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..229
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24555
     Region          21..218
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 maspfgvsgs elqyrkfnfs gfelagdlrl pqgtdclvil vhgsggghsn prnhyiaeyl
       61 arhgmgtlvv dlltrteqrw dnltgvlrfd iplladrlsq vidatardtq lrklgvglfg
      121 astgaaavlv aaarspsvqa vvsrggrtdl aaealplvsa ptlqvvgged pmilrlnvqt
      181 cqtlhceqrl eviegathlf kepgaladva rltgnwfeqy lhkehtcts
//
LOCUS       WP_010562977             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Pseudomonas].
ACCESSION   WP_010562977
VERSION     WP_010562977.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..231
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25168
     Region          16..231
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mlelrpfnal ggahhgwlda hhhfsfaeyh dpkrmhwgnl rvwnddiiap gtgfpqhphr
       61 dmeiityvre gaishadnlg nkgrteagdv qvmsagtgia hseynleatp tkifqiwiip
      121 neaglppswg akpfpkgdrq gfvtlasgks gdseslrira darlvaanlk agesaeyrld
      181 sgrraylvpa tgvievnglr aqardgvaie qeqvlrvtai edseivlvdl a
//
LOCUS       WP_010562989             414 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Pseudomonas extremaustralis].
ACCESSION   WP_010562989
VERSION     WP_010562989.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..414
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43919
     Region          8..400
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mknpcsyrad asyewkavtl lalgfglvsi drfmimplfp vimkdlnlny qdlglitgvl
       61 svtwgisslf tgklsdrfgh raiivpavil fsllagfsgl angllslmli ravigaaega
      121 ftpasivatl dvskpsrhgl nlgiqqaamp lfglalapil vtqllhvvaw hwvfvmvmvp
      181 glivglllhk vlrntdstea aehtmthdat shrwtdifts rnvslnilgm mcwltvlvvl
      241 gaflpnylld ymglsleqmg fvlsaigfgg aagtillpcl sdrigrkpvm ilsviggvas
      301 lyllinigad ttrlfaalff tvffdfglic ltvgpsttes vparlmstas gfvvgigeif
      361 gggiapslag yvahnhgiqy tlilaigama tgllitlaik etapvrtaav lktt
//
LOCUS       WP_010563005             118 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Pseudomonas
            extremaustralis].
ACCESSION   WP_010563005
VERSION     WP_010563005.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..118
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=13441
     Region          3..115
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 msqyrisdaa rtdiidilrr sqtqfgdqar qryqalilaa lqaiastpyr igshernela
       61 pglrsyhlvy srqqakhphg tvksprhvvf yrvandevie vvrllhdamd vqlhlpdd
//
LOCUS       WP_010563065             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: gamma-glutamyl-gamma-aminobutyrate hydrolase family
            protein [Pseudomonas].
ACCESSION   WP_010563065
VERSION     WP_010563065.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..253
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27097
     Region          9..246
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 malkpligvt acvkeiglhp yhvsgdkylr avsvaalglp viipsladlc eikdllhyvd
       61 gllftgspsn vepfhyqgpp sapgtahdpq rdattlpllr aavaagvpvl gicrgfqemn
      121 vafggslhqk vhelpgyrdh readdpriev qyapahpvai qpggafeamg lageiqvnsi
      181 hsqgidrlgd glrveaiapd glieavsveh sqafafgvqw hpewqvlsnp aylrifqafg
      241 dacrrhaaqr rpl
//
LOCUS       WP_010563078             337 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide deacetylase family protein
            [Pseudomonas].
ACCESSION   WP_010563078
VERSION     WP_010563078.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181098
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..337
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37274
     Region          3..>59
                     /region_name="PRK02888"
                     /note="nitrous-oxide reductase; Validated"
                     /db_xref="CDD:235082"
     Region          56..328
                     /region_name="CE4_Sll1306_like"
                     /note="Putative catalytic domain of Synechocystis sp.
                     Sll1306 protein and other bacterial homologs; cd10978"
                     /db_xref="CDD:200600"
     Site            order(70,72,155,159,194..196,286)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:200600"
ORIGIN      
        1 mslvnlqrrt flaqagagaa vltagtllgt asaaatqagp gnvapapagr pakggfwpgn
       61 trlvvsismq feaggqplkg tdspfprvdf pdsvptdpat ntwfaygyre giprmldlwd
      121 rhgvkvtshm igdavkrhpe lareivargh easghgprws sqfamsreqe rtflrqaasm
      181 lqdvtgqpvr gyncnwlrrg pntlsllqel gyvyhiddvs rdepfieqvn gkdfvvvpyt
      241 lrnndivlie grnyspsqfl qqvkldfdql yeeagsrrrm msisahdris gtpqmvrvwd
      301 eflryanshp gvafmrkdai aqytlespls lresetl
//
LOCUS       WP_010563090             230 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010563090
VERSION     WP_010563090.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..230
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24620
     Region          3..229
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mtfdlygfgp alaagalmtv klalsalclg lalglagala ktspykplqw lggtystivr
       61 gvpellwvll iyfgtinamr klgelldipd lslsafaagv ialglcfgay atevlrgaii
      121 sipkghreag valglskfri ftrlimpqmw rvalpglgnl flilmkdtal vtvigleeim
      181 rhaqiavtvt kqpftfymva aliylgltsl smvamhflek raargfvrtt
//
LOCUS       WP_010563210             184 aa            linear   BCT 01-JAN-2025
DEFINITION  PilN domain-containing protein [Pseudomonas extremaustralis].
ACCESSION   WP_010563210
VERSION     WP_010563210.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..184
                     /product="PilN domain-containing protein"
                     /GO_process="GO:0043107 - type IV pilus-dependent motility
                     [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=20376
     Region          4..182
                     /region_name="PilN"
                     /note="Type IV pilus assembly protein PilN [Cell motility,
                     Extracellular structures]; COG3166"
                     /db_xref="CDD:442399"
ORIGIN      
        1 mktrinllpw rqalvarrrk yflalllafa avalaavwla nqvidqaidr qvtrndhlgt
       61 dvdildarik tiddlqaqsq qlarrmkvvq dlhdgrssga rlldqlaram pegvhlhevv
      121 akgdtlnirg taessqdiar lmrsleases shsarlqqvr tdgangqnef qlmvhqaess
      181 eaqp
//
LOCUS       WP_010563242             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Pseudomonas].
ACCESSION   WP_010563242
VERSION     WP_010563242.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..256
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28489
     Region          1..249
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mrrvvfnqkg gvgkssiacn laavsasegy rtllvdldaq anstqyltgl tgddipmgia
       61 effkqtlssg pfskknrvdi yetpfdnlhv itataeladl qpkleakhki nklrklldel
      121 sedydriyld tppalnfyav saliaadrvl ipfdcdsfsr qalygllaei eelkedhneg
      181 levegivvnq fqaraslpqq mleeliaegl pvlpvylass vrmreshqen kplihldprh
      241 kltlqfvelh nllena
//
LOCUS       WP_010563280             465 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PIG-L deacetylase family protein [Pseudomonas].
ACCESSION   WP_010563280
VERSION     WP_010563280.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..465
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52252
     Region          180..>367
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 msrkqqllkr hrrnkrigvl iglvllvvig vcvawwlpfv lgvlawvahe awfadhlfya
       61 pgedyqyrfs adaqrtdvrl eggrlrvdsp leaeatlvla ikvksgwlgr fldpaveivd
      121 gdrrdrqtfe rgvnglryln lsglapalma gelrlrgrfc slqgapglwa wttpdyskqr
      181 vmviaphadd aelaafglys qaenpwivtl tageieaehy qhmgldpvea arikgrlraw
      241 dsiavprwag vpqahcvqlg yfclqlpamr aapdqpiasr eadlsdirlf rqlnpfplpa
      301 dldgqptwnn lladlrqlll sarpevivlp hplldphpdh icaqqaviea lqglawqptt
      361 vlgyanhlhd ndrwpmgdag agialpplfd dtlelrpcsl plslaqqrdk amalgmmhdl
      421 qpappfkrrv rrwlqrvlag rapspygene ffrkavrrhe lfwhl
//
LOCUS       WP_010563313             511 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HDOD domain-containing protein [Pseudomonas].
ACCESSION   WP_010563313
VERSION     WP_010563313.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..511
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=57245
     Region          23..>206
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 manekttppv rpnslaawik clddvrlpvp qashdrvcka irdnrsslrd iaelmqssps
       61 lvlsvmrean shthgslaep aenlevalnr lglkraedll arlpsvpmse ipvafrqlvl
      121 vsrhasqqan glfgsrlarl wqdihwgsll flsplwpmal aypklldewe lrvihkgesa
      181 rtveqqlfgv rlldlclglt etwhlpiwvs qgyklllneq rllvkalhia rvddplrqqq
      241 lldaetnlrr wlnqpantvl langlamsaq eswtcphtqr wqyltalylq qplgevqqqv
      301 hqqavinard tvmpdlwhpa lsliwpwhvq kihhgllpap pptaealalw rkrctellve
      361 psrfanamhl ttcakealva sgmqrvmllm tdraqstlrv hqidglpkda anlsldvvhs
      421 tllqrlleks aqvrltpdnh tqfsallppi lrrlfagehl llrslscngk vvmvmvadqg
      481 ggpfsettvq afgktaqcie kalhcftnrg a
//
LOCUS       WP_010563441             992 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Pseudomonas
            extremaustralis].
ACCESSION   WP_010563441
VERSION     WP_010563441.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 992)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 992)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 992)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 992)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..992
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=113676
     Region          4..983
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 msatesrieq dliakladlk ytlrtdirdr aaleknfrek fedlnrihlt dsefqrllds
       61 vitpdvynaa qtlrninsfe rddgtpfnyt lvnikdwckn hfevvnqlri ntdyshhryd
      121 vmllingvpv vqvelktlav sprramqqiv dyksdpgngy gktllcfiql fivsnrtdtw
      181 yfannnsrhf sfnaderflp vyqfasednk kithldsfae kflakctlgq misrymvlva
      241 seqkllmmrp yqiyavkaiv dcihqncgng yiwhttgsgk tltsfkastl lkdnpdidkc
      301 lfvvdrkdld rqtreefnrf qegcveentn tetlvrrlls ddyadkvivt tiqklglald
      361 gnnkrnyker leplrnqrmv fifdechrsq fgenhkaike ffpnaqlfgf tgtpifeqna
      421 syqqiegqqa syrttddlfq rslhqytith aiedrnvlrf hidyfkpegk nppkpgegla
      481 kakvietila khdaatsgrk fnavlatasi ndaieyfeaf ktlqakkqge ndtfqplnva
      541 cvfsppaegn kdvqqiqedl pqekednqqd pegkkaaltr iiadynarfg tnhrigefdl
      601 yyqdvqkrik dqqysntdlp haqkiditiv vdmlltgfds kylntlyvdk nlkhhgliqa
      661 fsrtnrvlnd skpygnildf rqqqkpveea itlfsgekvg iareiwlvdp apkvidslqa
      721 atqkmadfmq sqalayaped vanlrgdaar sqfvnlfkev qrlntqldqy tdlseeqkaq
      781 isqivpseql qsfkgvylet akrlkdqqdk qgdqappevq qldfefvlfa savidydyim
      841 gliarmtqqk pgkltmnreq ligliqsdak fiderddiae yirglpvgea ldeaairsgf
      901 drfkaekkar eladiasrhg lapdalqgfv deilrrrifd gerlselmap lnlgwkartq
      961 kelvlvedlt pllhklaqgr eiaglsayee er
//
LOCUS       WP_010563468             309 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas extremaustralis].
ACCESSION   WP_010563468
VERSION     WP_010563468.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 309)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..309
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33773
     Region          19..309
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mslalsqppm rrfsnllyrk pnlylamllv ppliwfgaiy lgslltllwq gfytfddftm
       61 avtpdltlan faalfqpsnf diilrtlsma ivvsiasaii afpiayymar yttgktkaff
      121 yiavmmpmwa syivkayawt lllakggvaq wfvqhlglep llqfvlgipg vggstlstsh
      181 lgrfmvfvyi wlpfmilpiq aslerlppsl lqasadlgak prqtfmqvil plsvpgiaag
      241 siftfsltlg dfivpqlvgp pgyfvgsmvy aqqgaignmp maaaftlvpi vliavylsiv
      301 krlgafdal
//
LOCUS       WP_010563474             170 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheW [Pseudomonas].
ACCESSION   WP_010563474
VERSION     WP_010563474.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..170
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=18376
     Region          19..158
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 msdlatkrga vpaakkalfl vfhigserya lkatevaevl prlplkplah aplwvagifa
       61 hrgamvpvid lsaltfgtpa qartstrlvl vnykpepwld arwlglileq atetlrcdpa
      121 efkpygldnp qapylgpvre dalglmqwig vadlltdevr allfaagpsl
//
LOCUS       WP_010563476             232 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheW [Pseudomonas].
ACCESSION   WP_010563476
VERSION     WP_010563476.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..232
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=24805
     Region          83..226
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 msspdvldta gldltladtq aiddcwnrig ihgdkscpll adhihcrncs vyaaaatrll
       61 dryalqqddh rpvaaeaged ivtrsllmfr lgeewlgiat rclvevaplq pihslphqrs
      121 rallgvanvr galvaclslv ellgldatsh gaiagrimpr mliiaaqdgp vvvpvdevdg
      181 ihaidertln aastsgaqas grftqgvlqw kgrslrwlde aqllsavtrs lt
//
LOCUS       WP_010563500            1021 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Pseudomonas].
ACCESSION   WP_010563500
VERSION     WP_010563500.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..1021
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112105
     Region          4..1018
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mgfnlsewal rnrqivlflm illavvgtls ytklgqsedp pftfkamvik tnwpgataqe
       61 vsrqvterie kklmetgeyd rivsfsrpge sqvtfvarda mrsaqipdlw yqvrkkvgdi
      121 rqtlppdiqg pffndefgtt fgniyaltgd gfdyavlkdy adriqiqlqr vadvgkveli
      181 glqdekiwie lsnlklatlg lplaavqqal qeqnavstag ffetpservq lrvsgnfktv
      241 eeirafpirv gdrtfrigdv aqihrgfndp paprmrfmge daiglavamr dggdilvlgk
      301 alegefarlq knlpagmelr kvsdqpaavk tgvgefvrvl aealaivllv sffslgvrtg
      361 mvvalaiplv lamtfasmyy lgiglhkisl galvlalgll vddaiiavem maikmeqgyd
      421 rvkaasfawt stafpmltgt litaagflpi ataqsstgey trsifqvvti allaswvaav
      481 vfvpylgekl lpdlakihaa khgtdgpdpy gtpfyqrvrr lvewcvrrrk tvvvltlllf
      541 igsvalfrfv pqqffpasgr lelmvdlkla egaslsntaa qvkrleallk dhagidnyva
      601 yvgtgsprfy lpldqqlpaa sfaqfvvlak tieereslrt wliqtlneqf pdlrsrvtrl
      661 engppvgypv qfrvtgenig evralarkva arvrenphva nvhldweeps kivylnidqd
      721 raralgvsta nlskflqssl tgssvsqfre dnelieillr gtvhertels llpslavptd
      781 ngksvalaqi atleygfeeg viwhrnrlpt vtiradiygk eqpatlvqqi lptlegvrae
      841 lpdgylldvg gtvedsargq nsvkagvplf ivvvltllml qlrsfsrtam vfltaplgli
      901 gvtlfllvfr qpfgfvamlg tialsgmimr nsvilvdqie qdikaglapw qaiieatvrr
      961 frpivltala avlamiplsr svffgpmava imgglivata ltllflpaly aawfkvrkda
     1021 a
//
LOCUS       WP_010563571             302 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudomonas
            extremaustralis].
ACCESSION   WP_010563571
VERSION     WP_010563571.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33783
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 msemddlaaf avlieagsft vaaeqlgcsk gqlskrisql earysvvllh rttrrlslta
       61 agaallpqaq alvvqvdrah qalarlkddl agpvrmtvpv slgetffdgl llefskqypq
      121 vqielelnnr yrdlardgfd lgvrsgaien erlvakplla whemtcaspa yleqygepqt
      181 padlvahrcl lnshysgree wlyhqqhell rvrvsgtfas nhynllkkaa lvgagiarlp
      241 syvlpaelad grlrwllrdy qtrsmpmylv hpyqgglprr tqvladylvd wfkrsgeald
      301 rl
//
LOCUS       WP_010563619             203 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Pseudomonas].
ACCESSION   WP_010563619
VERSION     WP_010563619.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..203
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22321
     Region          13..203
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mqaaqgyrwg lkaaalllis tvlsgcgint iptldeqaka awgqvqnqyq rradlipnlv
       61 evvkgyaahe qdtltaviea rakatsiqvd astldnpekl kqyqqaqdgl sgalsrlmvv
      121 serypdlkan qnflalqsql egtenriava rrdfiqavqa ynteirtfpg rlwhsvmysd
      181 lpiratfeat sadadkapqv kfk
//
LOCUS       WP_010563625             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Pseudomonas].
ACCESSION   WP_010563625
VERSION     WP_010563625.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..290
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31125
     Region          5..290
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mptpnihgii gytitpfsad gqrvdldalg rsidrlidsg vhaiaplgst gegaylsdae
       61 wddvsaysle kvgkrvptiv svsdlttaka vrraryaeah gadavmvlpa sywklseaei
      121 lahyaaigds igvpimlynn patsgtdmsv dlilrivkhv envtmvkest gdiqrmhqlr
      181 rhsdvpfyng cnplaleafa agakgwctaa pnlipqlnld lyeaalandl tlarelfyrq
      241 lpllefilkg glpatikagl rltglevgdp rlpvfplgda gieqlktllq
//
LOCUS       WP_010563678             273 aa            linear   BCT 01-JAN-2025
DEFINITION  HDOD domain-containing protein [Pseudomonas extremaustralis].
ACCESSION   WP_010563678
VERSION     WP_010563678.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..273
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=30343
     Region          15..239
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mnklaeevqq alvtaidnde lvlptlpeva lkirqaaedp eisishlskv igrdtalsar
       61 likvvnspll ratqevtdlh taitrlgtny ssnlaiglvm eqifharsev veqkmrdvwr
      121 rslevagvsy alcrshsllk pdqaalgglv hqigvlpipt yaedhyells dpvslnhmie
      181 sihpmlgdkl lhgwdfpeml vnlpgqylnl erdsasldyi dlvqiavlyc hrgtdhplad
      241 vqlsnvpamk klrvdpysds lraeldears mfy
//
LOCUS       WP_010563633             213 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Pseudomonas extremaustralis].
ACCESSION   WP_010563633
VERSION     WP_010563633.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22253
     Region          1..197
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mspslllavl asgfiygitp gpgvlavfgi gaargrraga gflcghllgd vvwcstalia
       61 ivgarevgst afdvlgvlsg lylfwlgwra irtqrrggda pqgaarhpfw hgivfgltnp
      121 kaypvavatf tallssrael ltwsmlpsli ilsfvgglla yailigvvga qrvrtvyqrh
      181 eilitrlcgv mfigfainal ahalpglfgs kpa
//
LOCUS       WP_010563696             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010563696
VERSION     WP_010563696.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33038
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..292
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(111..112,114..115,118,122,124..130,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 miinfdlndl qafravvdkg sfsgaaeair isqpalsrri eklesaldvk lferttrrvs
       61 ltmvgraflp qverilddld ialmgisnva strmgnvtia cvpstayyfm phvisefhkl
      121 ypkirirvld asagevcnav esgeadfgvs fsgsladeve felllqeryv lacrrdhpla
      181 grvsvpwaea yehdyisvdk tsgnrflldq alrgvrvkkp sicethhvtt miglveaglg
      241 vamvpsiamp addhpilvsv plvepqvmrn vglikrrgrt lppaaleler lvretpfrsa
//
LOCUS       WP_010563790             307 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudomonas
            extremaustralis].
ACCESSION   WP_010563790
VERSION     WP_010563790.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33096
     Region          7..>122
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mesfgsiecf vrsaeggsfa eaarhlsltp aavgksvakl earlgvrlfq rstrrltlte
       61 agkvflqevs gslttiqnav anlasaegrp vgtlkvsmgt vfgnryvvpl lgefmrrfpd
      121 ispdwhfdnr qvdligqgfd aaigggfelp qgvvarklap ahrvlvasph ylaqrppvlv
      181 pedlsrckgi lirspqtgri rswqltsger eqrplvlkpg mtmsdseaac casaqglgia
      241 lvsmpmavpf ldsgavvrvl pdwyvddgni slyyaehkll pgktrafvdf iieqfaeqgl
      301 gqifsav
//
LOCUS       WP_010564019             393 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter permease [Pseudomonas extremaustralis].
ACCESSION   WP_010564019
VERSION     WP_010564019.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..393
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43142
     Region          2..393
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mqnqigapkq klsfsdpkvr awlfqiitiv avvslgwylf nntqtnlqhr gitsgfdfle
       61 rsagfgiaqh lidytesdsy arvfviglln tllvtvigvv latllgfiig varlspnwmi
      121 nklatvyvev frnippllqi lfwyfavflt mpgprnshnf gdtffvssrg lnmpaaqaad
      181 gfwpfvasvv vaivaivlma rwankrfeat gvpfhkfwag lalffvipal califgaplh
      241 wempklqgfn fvggwvlipe llaltlaltv ytaafiaeiv rsgiksvshg qteaarslgl
      301 rpgptlrkvi ipqalrviip pltsqylnla knsslaagig ypemvslfag tvlnqtgqai
      361 eviaitmsvy laisisisll mnwynkrial ier
//
LOCUS       WP_010564035             311 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Pseudomonas].
ACCESSION   WP_010564035
VERSION     WP_010564035.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..311
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33898
     Region          4..218
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mselilhhyp qspfaekarl mlgfkglswh svhispvmpk pdltaltggy rktpvlqvga
       61 diycdtalia rrleqekagp alfpqglelv aqgfaawads lvfahavalv fqpeslavkf
      121 akvppemlqv lvadrsklfs ggtaarvqld qalhqwpaiv grinqqlqhq qgdflfgeps
      181 iadfalahpl wflkgssvta plvdaypavt twlervlsfg hgtatqmsae qaldvarnat
      241 paevpderfe dlngykagqq vsiaatdygt davagellfv greelilrrt deragtvhvh
      301 fprmgfrlqa q
//
LOCUS       WP_010564050             303 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010564050
VERSION     WP_010564050.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33015
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..292
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(104,108,147,162,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 matprfdgve lflqivesgn lteaaerlnl trsavgkgla rlearlgtcl lqrstrrqrl
       61 tddgqayyeh clralaelea aesvlesgrq qprgrlrasl plafghhyaa palwglldrf
      121 aqleidisfs drlidvaqeg fdlavrigal pdtdrlsarr lgeqaiglaa apaylqrvgr
      181 ierledlagh rgiayrcnap rlewelndaq grphrarvas plmmddlqav adaaiagagl
      241 awlpswliah yvlrgqlvav lpsyreqpap ihviwptaah mpaktryaid alvagtpscl
      301 ags
//
LOCUS       WP_010564216             209 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010564216
VERSION     WP_010564216.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22733
     Region          9..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mssetksarq tildtaqsiv grkgfsavgl neilqaadvp kgsfyhyfss kdafgvvlld
       61 tyfdnyvqgm qqlfdqpgvs qpaklmrywq cwidnqtgct dagkclavkl gaevsdlsep
      121 mrlalqrgts rtiellavam argvadgslv lqhspqdlar qlyalwlgas vmgkitrtst
      181 pfdealrltr qvlgcpehtd ihtdrgtgt
//
LOCUS       WP_010564054             116 aa            linear   BCT 01-JAN-2025
DEFINITION  glutaredoxin family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010564054
VERSION     WP_010564054.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Shelton,M.D., Chock,P.B. and Mieyal,J.J.
  TITLE     Glutaredoxin: role in reversible protein s-glutathionylation and
            regulation of redox signal transduction and protein translocation
  JOURNAL   Antioxid Redox Signal 7 (3-4), 348-366 (2005)
   PUBMED   15706083
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Fernandes,A.P. and Holmgren,A.
  TITLE     Glutaredoxins: glutathione-dependent redox enzymes with functions
            far beyond a simple thioredoxin backup system
  JOURNAL   Antioxid Redox Signal 6 (1), 63-74 (2004)
   PUBMED   14713336
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..116
                     /product="glutaredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12815
     Region          44..116
                     /region_name="GrxC"
                     /note="Glutaredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG0695"
                     /db_xref="CDD:440459"
ORIGIN      
        1 mlggvfkkvl lvllvvvviq nwgkiervfn psqvvseqtr asarvvlyat ewcgyckqir
       61 rfldqkgipy qavdidkdaq arkayealgg ggipfvdvng tlireyspek imaale
//
LOCUS       WP_010564229             370 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudomonas extremaustralis].
ACCESSION   WP_010564229
VERSION     WP_010564229.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..370
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40171
     Region          5..369
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mndtspsdie fcnvvkryga vqavnglnfs vrrgsfhsfl ggsgcgkttt lrmiagfeqp
       61 trgevrlagq nvagvpafer pvnmvfqhya lfphltvaqn iayglryrtp rpdkktqlrm
      121 adealemvrl sgfgqrkpse lsggqqqrva laralvnkpt vllldeplaa ldrklrkemq
      181 sellrlqrev gitfvlvthd qeealsmsds isvmhngsii qtatpeqlye tpasryvadf
      241 igesnlfngt vrrlhgnavv lrtaqglelt spltptgqal gadaegciav rpelisiaga
      301 gaplarevsl pgcvedriyl gncteyrvrt qafgvvcvrv prqqedvqaf ehgaavsvgw
      361 dhanglamal
//
LOCUS       WP_010564263             239 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pseudomonas extremaustralis].
ACCESSION   WP_010564263
VERSION     WP_010564263.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..239
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26071
     Region          37..239
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mlklfalmlt lvagaaqada tlhtdlplsy leqtqgdarn qplviflhgf gsneqdlfgi
       61 kdalpsnwty lsarapmavd sqgyrwftkt pgdgdydgvs adlqssarli edfvtqatak
      121 yhtrsdrvfl vgfsqgaims yevalrqpql vrgiaalsgs vlpvlkaelk pdprldklai
      181 fighgtldqa lpyasatqan evlvglglkp tfhtypgmth tiseleirdl ntwlqthlr
//
LOCUS       WP_010564310             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Pseudomonas].
ACCESSION   WP_010564310
VERSION     WP_010564310.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 304)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..304
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34112
     Region          38..298
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mfsvlkphrw kltllllaan lglilhlacg elksvsewvw ldifgeggsa llalvwlglv
       61 lksrpagrvt nylalglsci ffswwidsld efirlpasit wdhwlesgpm pvgmilltig
      121 iyhwhreqla isaqmekrer lfrehrlfdk ltplagadyl krqladslqd srdqqqplsl
      181 laldldnfaa inrayghaeg davlqalshl lllnlrrqdl lcrlagdrfv vllpntgerq
      241 arelalelqh avrslahktr lqgerlqlaa ttavvmalde ppqdllkrln lalarakqpl
      301 aksa
//
LOCUS       WP_010564315             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Pseudomonas].
ACCESSION   WP_010564315
VERSION     WP_010564315.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..255
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27800
     Region          177..254
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mtamtmhnpt lamaprqpsg vwrnslaasl avalhvgvga almlgwstek ppvdaprvmh
       61 tqlvmlpaap vpapvpepla vtppapepaa vpavvkptvd pqvqarklek aalarkrvee
      121 kkveqqqqrq ateqrnrele qqrlnqerla aatpratapa svpafdsrqy qplskeapdy
      181 peraldkqie gdcsveytvn tqgrvehpkv legchplfir pslaaaatfr yqprivegka
      241 vavpavrntf hyrik
//
LOCUS       WP_010564377             174 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Pseudomonas extremaustralis].
ACCESSION   WP_010564377
VERSION     WP_010564377.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..174
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=19159
     Region          29..173
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mtesqtafel lldidhrcrl laadlpsqet rlqrwsgigf rlgqhwyvap mgevaevlhe
       61 prctlmpgvk pwvkgvanlr grllpvmdlg gflglelsrp rpqrrvlvve yndlfvgllv
      121 devvgmqhfa qdallasasp gapfihgqfd gdplwqvfsp falaqspgfm dvaa
//
LOCUS       WP_010564408             284 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Pseudomonas extremaustralis].
ACCESSION   WP_010564408
VERSION     WP_010564408.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..284
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30538
     Region          12..281
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mslaqlinpq qlaerqksag lvildcrfal edpdygrcsy seghiegaqy adlerhlsgp
       61 vakgvtgrhp lpaadtfveq lrvwginada dvvlyddgpg afaarawwll awlgkrdgvf
      121 ildgglrawh aagfplslda pviepgtfvg tpdhrlvlda ehlqkrlgqp gltlidaraq
      181 prfrgdvepi dpvaghipga qcaafnenlg sdgrflpaeq lrqrfaaqlq grspdelvay
      241 cgsgvtachn lfalslagyp lgklyagsws ewitdparpi atgd
//
LOCUS       WP_010564412             531 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [Pseudomonas].
ACCESSION   WP_010564412
VERSION     WP_010564412.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Khan,M.W. and Murali,A.
  TITLE     Normal mode analysis and comparative study of intrinsic dynamics of
            alcohol oxidase enzymes from GMC protein family
  JOURNAL   J Biomol Struct Dyn 42 (19), 10075-10090 (2024)
   PUBMED   37676256
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17335521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..531
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57147
     Region          49..531
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
     Region          78..297
                     /region_name="GMC_oxred_N"
                     /note="GMC oxidoreductase; pfam00732"
                     /db_xref="CDD:366272"
ORIGIN      
        1 mpvpdlfrdg largwkthng aaldhdltle advaiigsga gggttaeils aagykvllie
       61 egplktssdf klleheayts lyqegigrms kdgaitilqg ravggttlin wtssfrtpda
      121 tlshwaseya vkghssaema pwfekmeqrl giapwamppn anndvirkgc eklgyswhvi
      181 prnvrgcfnl gycgmgcpvn akqsmlvtti pstlekggel lylaraerlv ysgdhinsle
      241 cvamdercva ptgrkitvka rhyvlagggi nspallmrsn apdphsrlgk rtflhlvnfs
      301 aalfdevinp fygapqsiys dhfqwqdgtt gkmsykleap plhpalastl lggygtdnal
      361 dmsqlpntha mlallrdgfh pdspggsvel rgdgtpvldy qvspyawdgl rrafhsmaei
      421 qfaagaksvk plhhdaryvk tlaearslid glnlelhrtc lgsahvmggc amgeepknav
      481 adslgrhhql rnlsihdgsl fptsiganpq lsvygltaql asalaerlkt a
//
LOCUS       WP_010564431             756 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Pseudomonas
            extremaustralis].
ACCESSION   WP_010564431
VERSION     WP_010564431.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 756)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..756
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80144
     Region          158..755
                     /region_name="P-type_ATPase_Cd-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux
                     ATPase; cd07545"
                     /db_xref="CDD:319845"
     Site            order(409,411,717..718,739,743)
                     /site_type="other"
                     /note="putative HM ion binding site [ion binding]"
                     /db_xref="CDD:319845"
     Site            order(453..455,518,534..536,565,605..607,627,630,633,652,
                     655)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319845"
ORIGIN      
        1 msdslhtphk hehghdhdhd hdhgpkkltp vhdhghgdsc csgtpaptlv klgqaptass
       61 rlstfrieam dcpteqtliq nklgklagvq qlefnlinri lgvthdlpnt apiieavksl
      121 gmqadpveeg tpaaelpakk hwwplavsgv galgaevlhf tnaaptwvia mvalvsilsg
      181 glttykkgwi alknlnlnin almsiavtga vligqwpeaa mvmflftvae lieaksldra
      241 rnaisglmqm tperatvrqa dgswvelevn nielgaivrv kpgerigldg dvtagtstid
      301 qapitgeslp vektvgdkvf agtinqagsl eyqvtaaann stlariihav eqaqgarapt
      361 qrfvdsfskl ytpavfllal gvavipplfm aaawfdwiyr alvllvvacp calvistpvt
      421 ivsglaaaar kgilikggvy legghklnyl aldktgtith gkpvqtdylm lvpdvearvq
      481 alaaglaars dhpvslaian aavdkslpvh lvdnfealag rgvrgdinge tyhlgnhrlv
      541 edlglcspal edklfalekq gksvvllldk sgplalfava dtvkdssrea ieqlhelgik
      601 tlmltgdnth taqaiaaqvg idqaqgdllp tdkllaieal ygqghrvgmv gdgindapal
      661 araeigfama aagtdtaiet advalmdddl rkipafirls rqtssilrqn ialalvikai
      721 flvvtflgla tmwmavfadm gvallvvfng lrllrk
//
LOCUS       WP_010564477             559 aa            linear   BCT 01-JAN-2025
DEFINITION  GspE/PulE family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010564477
VERSION     WP_010564477.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..559
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=61114
     Region          17..547
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mpvdrrlelr pllpplieag lingdiaqrl anlptdpdrh pleciaaegp cletltqwla
       61 rhagqpylri dplkievaki vplmsyafaq rhailavavd aqtvtvasaq pyvtrweagl
      121 aqvlkrsikr vvanpqdiar cigefyrlak svngaeqkav apgqsdllnl gagdqepdan
      181 dahivnivdw llqyafgqra sdihvepcre qgrvrfridg llhdvyqfpp qvtmavvsrl
      241 kslgrmnvae krkpqdgrvk tkspagveve lrlstlptaf geklvmrifd pqvllkdfdq
      301 lglsdgdqqr wramtrqtsg iilvtgptgs gktstlyttl kqlasrevnl ctvedpiemv
      361 epafnqmqvq hsidltfarg irallrqdpd iimigeirdq etaemaiqaa ltghlvlstl
      421 htndapgais rlqelgiahy likatllgvm aqrlvrllcp dckrvagdah eaigcaqcrh
      481 sgyqgragvy eimtvdedlk alitpgadvq alrrtaiarg mcslrmaglq kvkaglttva
      541 evlrvtpgds dtnplsvgr
//
LOCUS       WP_010564464             213 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pseudomonas
            extremaustralis].
ACCESSION   WP_010564464
VERSION     WP_010564464.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23692
     Region          12..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mttrpaaprk prarsrarid aildaartll aaegvaglsi ynvaeraqip pssvyhffas
       61 vpallealta dvhaafraai qapidheslk hwrdlsyive qrmltiyeqd aaarqliltq
      121 hgltevtqad rqhdlelgdl mlevfsrhfe vpslpadvdv falalelsdr vyarsvhqhg
      181 litprmaeeg mrvfdayvgl ylpmylpkrp tsv
//
LOCUS       WP_010564517             211 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Pseudomonas].
ACCESSION   WP_010564517
VERSION     WP_010564517.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..211
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23570
     Region          2..188
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mlqqflhdfg yfalflgtff egetilvlag flafrgymdi nlvvvvaffg syagdqlwyy
       61 mgrkhgrkll arkprwqlmg dkalehirkh pdvwvlsfrf vyglrtvmpv aiglsgyspv
      121 rylilngiga avwaaalgaa ayhfgavleg mlgsvkkyel wvlgallvlg falwlrrrfk
      181 nariarqaca daearltvep apveppktpv e
//
LOCUS       WP_010564478             306 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SPFH domain-containing protein [Pseudomonas].
ACCESSION   WP_010564478
VERSION     WP_010564478.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..306
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33094
     Region          4..287
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mqigtvlllf vglaiailfm gfkvvpqgyq wtverfgryt ntlkpglnii ipvmdrigrk
       61 invmesvldi ppqevitadn atvqidavcf fqvvntaqaa yevnnlehai rnllqtnirt
      121 vlgsmeldam lsqrdginek llktvdeata pwgikitrie ikdisppadl maamsgqmka
      181 erikraqile aeglrasail taegkkqaqi leaegsrqaa flesearerq aeaearatqv
      241 vseaiasgnv qavnyfvaqk yidalgklas annskvilmp leasqvigav ggigeivkat
      301 fdskkg
//
LOCUS       WP_010564542             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010564542
VERSION     WP_010564542.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..262
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28536
     Region          10..257
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvalapavsa saglalrieh vshgfaldgl hlpvlervsl evapgefval lgpsgcgkst
       61 llrlvaglep adsgrlladg kpilgpdpsr vvvfqdptly pwrrvwdnva iglhaqgllk
      121 thaakvdeal ekvglshfar ayprqlsggm aqrvalaral vnqprllild eplgkldslt
      181 ritmqkelid lwqrqgytal lvthdveeal llanrvivfs drpakiqaql sidrpyprhr
      241 ddpylvdlrr qilgllglge nw
//
LOCUS       WP_010564621             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010564621
VERSION     WP_010564621.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..254
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28346
     Region          7..252
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtedtikrra kgldrafdil dflkevgqpl rpndiasgig spkstvyelv asllerrile
       61 tvgkdghvyl grqlyflgqa hlrhfdlsre adhalqeivs qthetaqmcl lngrkytval
      121 mregerhfri ssdigenapi pwtasgrlll ghlsdqqivd lidpddfilp dgerlaldtf
      181 laqirqasld gffsfdsvad tfthcfaapv rdaqgvsiat lcivaprada lknyndyrrv
      241 liesannlar rine
//
LOCUS       WP_010564611             104 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SCP2 sterol-binding domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010564611
VERSION     WP_010564611.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Burgardt,N.I., Gianotti,A.R., Ferreyra,R.G. and Ermacora,M.R.
  TITLE     A structural appraisal of sterol carrier protein 2
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (5), 565-577 (2017)
   PUBMED   28284963
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Dyer,D.H., Wessely,V., Forest,K.T. and Lan,Q.
  TITLE     Three-dimensional structure/function analysis of SCP-2-like2
            reveals differences among SCP-2 family members
  JOURNAL   J Lipid Res 49 (3), 644-653 (2008)
   PUBMED   18084051
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Bun-ya,M., Muro,Y., Niki,T., Kondo,J. and Kamiryo,T.
  TITLE     New aspects of sterol carrier protein 2 (nonspecific lipid-transfer
            protein) in fusion proteins and in peroxisomes
  JOURNAL   Cell Biochem Biophys 32 Spring, 107-116 (2000)
   PUBMED   11330036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007129
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..104
                     /product="SCP2 sterol-binding domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=10903
     Region          7..104
                     /region_name="SCP2"
                     /note="Putative sterol carrier protein, contains SCP2
                     domain [Lipid transport and metabolism]; COG3255"
                     /db_xref="CDD:442486"
ORIGIN      
        1 mtdvanvvet mkakfnpaaa agldvifgfr ideskhfnli vkdgacalqe genpdanvtl
       61 vtdsdtmagi vsgetdgmqa fmggklkveg dmmlsmklse lfps
//
LOCUS       WP_010564619             260 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_010564619
VERSION     WP_010564619.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..260
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28893
     Region          10..258
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mnqpqttqpl ldirglrkqy gavevlkgvd lsmqrgnvvt ligssgsgkt tllrcvnlle
       61 efqggqitld gesigyreva gkrirhperv iaqhraltgm afqqfnlfph ltalqnvtlg
      121 llkvkkmpkd eavalaekwl drvgllerrn hfpgqlsggq qqrvaiarai amnpslmlfd
      181 evtsaldpel vgevlsvikg laeegmtmll vthemrfaye vsdkivfmnq grieeqgssk
      241 diferpqspr laeflknirf
//
LOCUS       WP_010564624              91 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptidylprolyl isomerase [Pseudomonas].
ACCESSION   WP_010564624
VERSION     WP_010564624.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..91
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=9980
     Region          2..>87
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mkaqarhilv ktseeaeqlk qriakgeafd vlakkystcp sgkrggdlge vrpgqmvgvi
       61 davifkkpvk vvhgpikskf gyhlvqvfyr d
//
LOCUS       WP_010564630             525 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudomonas extremaustralis].
ACCESSION   WP_010564630
VERSION     WP_010564630.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 525)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..525
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57368
     Region          1..521
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msdnlieird lcvafggqsv vrnlsldvrp geclalvges gsgksvtals ilqllpeagt
       61 etrgsvkyrg qeligasast lqklrgdria iifqepmtsl nplhsiekqi getlllhkgl
      121 ggkaaqaril ellelvgiqk peerlkayph qlsggqrqrv miamalacep qlliadeptt
      181 aldvtvqrki llllkslqqr lgmslllish dlnlvrsmaq rvcvmhagei veqadcetlf
      241 tapqhpysql lldaepsgep vcsearetvl evhdltvqfp lggglfqrkt ylravdgisl
      301 svqrgktlgi vgesgsgkst lgqailrlld stgsirfqgv aleslnhhqm rpwrkqmqvv
      361 fqdpygslsp rmsvqqiise glevhapcsl aecdaqviqv lkdvgldpas rhryphefsg
      421 gqrqriaiar alvlkpalml ldeptsaldr tvqkqvvall relqekyglt ylfishdlav
      481 vramahdmiv ikdgkvverg ashdvfeapq hpytkellaa armpl
//
LOCUS       WP_010564634              93 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptidylprolyl isomerase [Pseudomonas].
ACCESSION   WP_010564634
VERSION     WP_010564634.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..93
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=9771
     Region          3..>93
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 makatarhil vsteekcnel kaqieggadf aevakanssc pssrqggdlg sfgpgqmvke
       61 fdtvvfsapv ntvqgpvktq fgyhllevts rqd
//
LOCUS       WP_010564701             261 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Pseudomonas].
ACCESSION   WP_010564701
VERSION     WP_010564701.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..261
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27142
     Region          6..261
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mevgnfgfvi aglivgfivg mtgvgggslm tpillwfgin patavgtdll yaaitksggv
       61 lvhsknknid wtitgwltlg svpavlltlw flaslhtdps amnavikqal gvvllltala
      121 ilfkksllaf aqrhagdgyh mnprnlnglt vvtgvvlgtm valtsigaga lgtvalfily
      181 pflatrrlvg teiahavplt lvaglghagm gnmdwhllgf llmgslpgiy igshmtgkip
      241 dgvlrpclal mlmvigyklv f
//
LOCUS       WP_010564710             199 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Pseudomonas extremaustralis].
ACCESSION   WP_010564710
VERSION     WP_010564710.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..199
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20934
     Region          1..192
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlssllpfml fafvasitpg ptnilvlsns arygfkaalp iilgactgaa glvllvgsgf
       61 gqslvhwpkv qtamqwigia wlsllawqif saptralema atdkplglig aaglqlinpk
      121 twmmalavvs vfagngsdrq hqvlslslvf flvalpclga wavlgagsgr vlrspeamrr
      181 fnrcmavlll gstwlsvli
//
LOCUS       WP_010564780             195 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Pseudomonas].
ACCESSION   WP_010564780
VERSION     WP_010564780.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..195
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20776
     Region          1..195
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslilsmaaf alatsitpgp vnvvalssga rfgfvasqkh vfgaavgftv llvliglglh
       61 evlvrwpllt qliqwggvaf llymawklav ddgrldaqga atapsmlyga imqwlnpkaw
      121 lacvagmglf vadgdarqvw lfaglylvic ylsvacwaya gtflrrylsn pqgvrlfnrs
      181 maallvasvg yllma
//
LOCUS       WP_010564775             358 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: microcin C ABC transporter permease YejB
            [Pseudomonas].
ACCESSION   WP_010564775
VERSION     WP_010564775.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..358
                     /product="microcin C ABC transporter permease YejB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042884 - microcin transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39299
     Region          1..357
                     /region_name="YejB"
                     /note="ABC-type microcin C transport system, permease
                     component YejB [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4174"
                     /db_xref="CDD:443333"
ORIGIN      
        1 mlayivrrll liiptlfgil linfviiqaa pggpveqmia klegfegats riagggaevs
       61 vagsssyrga qgldpalike iekmygfdks aperlwimvk nyatldfgds ffrdakvidl
      121 ikekmpvsis lglwstlimy lvsiplgiak atrhgshfdv wtssliivgy aipaflfail
      181 livlfaggsy fdwfplrglt snnfdelswg gkitdyfwhl alpitalvig nfatmtlltk
      241 nsfldeinkq yvvtakakgl tnhrvlyghv frnamllvia gfpsafigif ftgsllvevi
      301 fsldglglms feaainrdyp vvfgtlfift llglivklig dltytlvdpr idfasreh
//
LOCUS       WP_010564782             120 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Pseudomonas].
ACCESSION   WP_010564782
VERSION     WP_010564782.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 120)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..120
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13550
     Region          4..119
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mkiratvice hegrilfvrk arskwalpgg kverderpvg aaereleeet glnvdgllyl
       61 qelkasdtvh hvfeasvvnv rearpcneiv dcqwhpygav delnatdvtk rivksflrrl
//
LOCUS       WP_010564801             340 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010564801
VERSION     WP_010564801.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..340
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35413
     Region          7..339
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnaitdnkpa tlptksrrrl ptelsiflvl igiglvfevf gwivrdqsfl mnsqrlvlmi
       61 lqvsiiglla igvtqviitt gidlssgsvl alsamiaasl aqtsdfsrav fpsltdlpvw
      121 ipvamglgvg llagaingsi iavtgippfi atlgmmvsar glaryytegq pvsmlsdsyt
      181 aighgampvi iflvvavifh ialrytkygk ytyaiggnmq aartsginvk rhliivysia
      241 gllaglagvv asaraatgqa gmgmsyelda iaaaviggts laggvgritg tvigalilgv
      301 masgftfvgv dayiqdiikg liivvavvid qyrnkrklkr
//
LOCUS       WP_010564824             714 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas extremaustralis].
ACCESSION   WP_010564824
VERSION     WP_010564824.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..714
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77979
     Region          28..714
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mvlrfrpvvt srfalgllls ggigsslaae ielpavqiqg qdesgyrsdt asvggfdaap
       61 lldtpasisv inaamikdqq arllsevlrn daavgdsyap igyyenfvvr gfslnaassy
      121 kingrtitge qnvalenkqq vevlkglagl qsgisepggv inyvtkrped vrsvtvstdd
      181 rgsgylatdv ggwfgseqqf glranvahed lhsyvehang qrdfvslafd wnispdavlq
      241 ldaeyqnkqq rsvpgyqllg gtevphdasp kkllghqsgs kpvgidslnl ngtfdyrfsd
      301 qwkgsvsaah skvviddyss fawggdthgl gnyftsagny diydyrspdd trrddevqaa
      361 ltglfdtagl gheltfgtsa frrvidkraa vnewlgsani dqeaptyapt dvplndshra
      421 ldsrqyglfv tdrirfneqw qtvlggrevr ldekafdsdg nqarhtqqyv flpqaaliyk
      481 pienlslytr yskglslggs apwfasnkde tlapttsrqi eagvkydwhr isfaaavfqm
      541 rqayqyakpd gagnftyvqq gqqkntglel sangwatdrl qiassvaair arvtgsgtpd
      601 yeghqainvp vlrasvyady alpwvnglav lggvqysakk yanrtgnvev gdyavvnvgs
      661 ryttkldgye tvfrlsvdnl fdkrywrdag eymgddylfq gapltarlsa tvnf
//
LOCUS       WP_010564896             331 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Pseudomonas extremaustralis].
ACCESSION   WP_010564896
VERSION     WP_010564896.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..331
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=35327
     Region          17..307
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mktstetqry slngetmgtr ytalfyaeag ldtdainral aqavgrvdqq mstwkadsdl
       61 nrlnaapeqv wlpvpeelvt vlaaalrvgq qsggafdiav gdlveawgfg pgassvteqp
      121 ldtlaprsal sanaaltvdt qrhqvrkrap lqlnlnaiak gfgvdelarc ldgfgltdyl
      181 vgidgemrar gskpdaqpwv vaiekpcrgv revmgvmelc daaiatsgdy rhwidvkgrh
      241 yahtmnpatg aplcnsvaav tvvaascmla dawatalmvl gesegprvaq argmdalfvl
      301 regdrlreis ivggilqaqi dsrptqprpr t
//
LOCUS       WP_010564934             641 aa            linear   BCT 01-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Pseudomonas extremaustralis].
ACCESSION   WP_010564934
VERSION     WP_010564934.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..641
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68611
     Region          5..457
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          572..637
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(594,603..605,612)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            604
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mstltrvlva nrgeiacrvm rtakamglst vavhsaidrd arhcreadir vdlggskaad
       61 sylqidklia aahasgaqai hpgygflsen aefaraieaa gliflgppas aidamgsksa
      121 akalmetagv plvpgyhgra qdldtfrdac arigypvllk ataggggkgm kvvedvsqla
      181 ealasaqrea lssfgngqml vekyllkprh veiqvfadqh ghclylnerd csiqrrhqkv
      241 veeapapgls veqrramgea avraaqaigy vgagtvefll dargefffme mntrlqvehp
      301 vteaitgldl vawqirvaqg ealpitqaqv plighaievr lyaedpsndf lpatghltly
      361 resapgpgrr vdsgveqgds vspfydpmlg kliawgedre qarlrllsml defavgglkt
      421 nlgflrriig hpafaaaeld tgfipryqde llpqagplsd efwqaagsaf iqslpagdgp
      481 wadtrgfrag lpaeislhls cngqdrrmtl adnaaqlrge qllierqgvr rallavrseg
      541 tvflrwdgem hgvslfdpia aveanhshqg glsapmngsi vrilvevgqa veagtqlvvl
      601 eamkmehsir apqagmikal fcqegemvae gcalveleaa g
//
LOCUS       WP_010564987             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Pseudomonas].
ACCESSION   WP_010564987
VERSION     WP_010564987.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..158
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17066
     Region          1..142
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtenpllara trfvsalrhc qvlgiaahya deegitlvmp yashlvgdps tgvihggalt
       61 slmdtacgma tlcvlpefev cptldlrvdy mhpaephkpv ygfaqcyrvt tdviftrgfa
      121 yqddrqqpia hvvgtfmrmg krlkgtqglg etikggqa
//
LOCUS       WP_010565001             103 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF485 domain-containing protein [Pseudomonas].
ACCESSION   WP_010565001
VERSION     WP_010565001.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..103
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=11298
     Region          2..103
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 mndsiylsiq nsprfkelvr krerfawils aimlglysgf illiaygpql lgakinptss
       61 itwgipigvg lilsafvlta iyvrrangef ddlnnailke aaq
//
LOCUS       WP_010565017             293 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010565017
VERSION     WP_010565017.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..293
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31719
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..287
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,222,239,266)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrltametf vhvvetgsfs aaakrlgigq pavsksiaql earlavrlvm rstrgltpte
       61 aglaffekak raieqandad daargagagl sgnlrisaav tfarmhiiph lgpfleqhpe
      121 mtvdvvlddr slnlveegid valrmgnlsd sshtarkige spcvilgtpa yfarfgepat
      181 pqdllqhqai iytrvegshw nftrgdtqfp lvahgrvrvt aaegvraavl shlgltlsst
      241 wmfapelasg evktvlddwh lpardlwavy ptgrmasaka rafveyveql lkr
//
LOCUS       WP_010565071             166 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Pseudomonas].
ACCESSION   WP_010565071
VERSION     WP_010565071.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..166
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18403
     Region          1..155
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mirsmlyatd lglyapyvmq halalartfk adlyvihvve piglfaesvl qsyldekaln
       61 ewqnqglstv matieqrvld sfreelgdge qdlklirsvr viqgdpcevi ldqlrrlsvd
      121 llivgshsha tgastplgrt aarvlqlstv pvylvpslqr rrsddv
//
LOCUS       WP_010565104              66 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010565104
VERSION     WP_010565104.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 66)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 66)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..66
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6680
     Region          1..61
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mfvlnvsgig cgscvskitk aiqsldskat vsvdraagkv tvesseppeq vrktvealgf
       61 psqisa
//
LOCUS       WP_010565171             369 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010565171
VERSION     WP_010565171.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..369
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39269
     Region          11..335
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mnevwrwlhr lrmvwavlaa falgsllila agknpmaayq alfkgaffdy hglantlvkm
       61 cpmllaglav iipmrcglli vgaegqiyig glaaaavaly lpqmpamlhv llcllcllag
      121 mlggglwgai pgylrakrgi nevivtllmn yvainivsyf aggpmmqega pypysaeise
      181 dlwlplllsd tdthigvlfa allslltfvv fkyttigfsm tavgkspqaa ryagmsvnrn
      241 ligsmiadga iaglagaiev lgvkyrlyhl fspgygydgi vvafmtslnp llatfsaffl
      301 aglstgaqym qraigldvta iealrglivi fvaagliwkl nlqkrnnpla kaasipsqkn
      361 taegltdgr
//
LOCUS       WP_010565203             329 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010565203
VERSION     WP_010565203.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36130
     Region          1..325
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msfvsvqhlq kgyagtpvfs dinceiakge fvtllgpsgc gkstllrcia gltsvdsgki
       61 lldgqdivpl spqkrhigmv fqsyalfpnm tveqnvafgl rmqkvnadds hkrvqevlql
      121 velkelagry phqmsggqcq rvalarslvt rprlllldep lsaldarirk hlreqirqiq
      181 relglttifv thdqeealtm sdriflmnqg kivqsgdaet lytapvdvfa agfignynll
      241 dadkasqllq rpisgriair peaielsrsg eldalvrshs llgnviryri eargvelvvd
      301 vlnrsaddlh pdgqrlalsi dpsalceva
//
LOCUS       WP_010565206             268 aa            linear   BCT 01-JAN-2025
DEFINITION  alkaline phosphatase family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010565206
VERSION     WP_010565206.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..268
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29699
     Region          2..257
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mkhnvilvvl dglnfevaqh amghlqayvg tgraalykle celpslsrpl yeciltgvpp
       61 iqsgivhnnv srlsnqrsif hyatdagltt aaaayhwvse lynrtpflaa rdrhtddkal
      121 aiqhghfywn dhypdshlfa daeslrlkha pnfmvvhpmn iddaghkygl dtpqyrnsar
      181 sadiiladyl qgwldagyqv lvtadhgmnn drshngllpq erevplfvvg dafslnadaa
      241 pkqtdlcgtv cellgvphdk pvcrellk
//
LOCUS       WP_010565211             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_010565211
VERSION     WP_010565211.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..248
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26901
     Region          14..242
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 msvaqqlkva svgptldfdk vsltlgrtti lddvsfqvep gsihalvgpn gggksslikt
       61 llgqtphqgr lslqwpatpg tigyvpqale fdrglpmtvd dfmaamcqrr paflgvsrhy
      121 aaaigealer vgmqdkrkrr mgalsggerq rvllaqglip apqllvldep msaldeagiq
      181 vferllndwr lagitvlwie hdleavgrla drvtglnrrv lfdatpkeal tpdrlltlfs
      241 thprspvq
//
LOCUS       WP_010565271             436 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010565271
VERSION     WP_010565271.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45883
     Region          19..423
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(31..32,35..36,39,78,136..137,139..141,144,164,
                     167..168,171,254,257..258,261..263,266,294,298,350..351,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msttyneaat aaptnstarv atasivgtai efydfyiyat aaalvigpvf fpqssgtaqm
       61 lasfltfgia fiarplgsal fghfgdrigr kstlvaslll mgvcttligl lpgydsigaw
      121 apillcvlrf gqglglggew ggaallaten apkgkrawfg mfpqlgpsig flaanglfli
      181 lamslndeqf rswgwripfi lsavlvmvgl yarlklhetp vfadavakqa pvkvplvelf
      241 sqhwlpvllg aasmvvcyal fyittafsls ygvstlgysr etflgllcfa vlfmglatpl
      301 aalasdrygr kpvlivgavl ailsgftmep llthgstwav alflalelfl mgvtfapmga
      361 llpelfptrv rytgasaayn lggivgasaa pffatklvam gglsyvggyv saaallslia
      421 vlclketrnn dlnkvt
//
LOCUS       WP_010565290             374 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010565290
VERSION     WP_010565290.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..374
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41157
     Region          1..>280
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          188..367
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mnslanifwl gikdlralsk dlmmilfify sfgisiymqs tgagetvhna svaivdedns
       61 alsrsiaglf yppyfqaakm isaadidrtm dkglytlvvv ipprfeadvr kgrdievqvn
      121 adatavqqas lgggyiqnmv tdevtryrqq mqrtaglssd lvirrafnpn gtqswfravv
      181 gladqlsmli iiltgaallr erehgtiehl lvmpltafei alakvwssgl vimigficsl
      241 lfvvqgvldv piagsrgvll lgtliyifat aaigiflgtl artmaqfall mmmavmpmmm
      301 lsggmspies qpqwvqyvtw ffpsrhyvgf mqaivyrgag ldivwkefvt vlvmgvtflv
      361 mslllfrqsv atlr
//
LOCUS       WP_010565304             649 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LTA synthase family protein [Pseudomonas].
ACCESSION   WP_010565304
VERSION     WP_010565304.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..649
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=72142
     Region          18..634
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mgflktapmr ylllvtgawl viflltrsvl lithldevgg nllpvfgvgl lydlgflaya
       61 alplglylll cppalwrrrg hrwflqavlt vslfamlfts vaewlfwdef gvrfnfiavd
      121 ylvysdevln nllesypigk llsllamlai vlslalrkpf naamsaplpp lrgrlldala
      181 lllvvglslq lisqdspraq ggnayknela sngpyqffaa frnneldytq fykslptdvv
      241 akqlraelse pnarfigqdp ldirraitnp gtprkpnivl vtiesfsaky mgsngdgrdl
      301 tpnldalrkq slyfnnfyat gtrtdrglea itlaipptpg rsivkrigre sgfaslgqql
      361 saigydsvfv yggrgyfdnm naffsgngyr vvdqssvpet eisfknawgm adedlykqtl
      421 kladadyakq qpfllqlmtt snhrpytypd gridiksgng rdgavkytdh aigqfleaar
      481 qkpwfdntif vfvadhtags agkedlpitn yqiplfiyap klidarenaq lasqidlapt
      541 llgllnqsye stffgrnllq dnplpprvvv gnyqhlglfd gkdlailspr qglrrhdqal
      601 gesqelqvgs ddpliqrait yyqaasygfk qqllgwrapk deapvlser
//
LOCUS       WP_010565307             226 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Pseudomonas].
ACCESSION   WP_010565307
VERSION     WP_010565307.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13412423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..226
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25989
     Region          15..226
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
     Region          55..149
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mptpiklefs ekyddehare yllkhqdnla rrlshkrdeq larsalamag epglvldlpc
       61 gagrfwplla ekpnrviiga dnsasmlkva tlaqpadvvk rvrplqtsaf didlpnnsvd
      121 cifcmrllhh igdpehrlai lqefqrvtrd sviislwvdg nfkawkrkrl enrrrkkgeq
      181 dgyqnrfvlp aatveaefeq agfrvqesld fiplyamwrv yvlrkr
//
LOCUS       WP_010565331             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010565331
VERSION     WP_010565331.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..283
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=31604
     Region          15..271
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mnaplqghta snphttapll avdnvsleyr tpervvrath qvsfeidpad ryvllgpsgc
       61 gkstllksia gfikpcegei rllgqkveqp gpdrivvfqe fdqlppwktv kqnvmfplla
      121 sktlprreae qralhyldkv glsafadayp htlsggmkar vaiaralamq pkillmdepf
      181 aaldaltrrk mqeellqlwe evrftllfvt hsieealvvg nrilllsphp grvraeihsh
      241 qydlhslggv efqasarrih rllfdeapea erelgfadir iay
//
LOCUS       WP_010565423             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Pseudomonas].
ACCESSION   WP_010565423
VERSION     WP_010565423.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 269)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..269
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28832
     Region          1..257
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkktllshpv kalalafglf ssalfaaeap lkigttaafa ipleaavaea gkqglkvelv
       61 eftdwiapnv slaagdidvn yfqhipflen akaaagfdlv pyapgiinnv glyskkfksi
      121 ndlpqgasva iandpinsgr glqllakagl islkpgvgyk ateedivanp kkikilqvea
      181 vqlvraydda dlvqgypayi rlsktfdaes allfdgldhp eyviqfviqp ksktdprvik
      241 fvdiyqhspv vraaldkslg klyqvgweg
//
LOCUS       WP_010565480             355 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Pseudomonas].
ACCESSION   WP_010565480
VERSION     WP_010565480.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..355
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38692
     Region          45..347
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mlyqevgqis tsyaaerrtf rlrqdrvalw lllgfaffav pwlgndywfs ailvpllvls
       61 laglglnllt gyagqlslgs aafmavgafa aynlqlrvpg lpllvsfalg gviaalvavl
      121 fglpslrikg fyllvstlaa qfvvewvltr fswftndnas gvitspplli agldfssprg
      181 ryvltlavva alfwlgknlv rselgrnwma vrdmdtaaav igirllktkl lafaisgfyl
      241 gvagslwafa ylgtvephgf dlsrsfqvlf iiiigglgsv lgnflgaafi vlfpillahl
      301 fallpaglmd agqleniqkm lfgaliiafl ikepqglarl wqrfrqrarv wplry
//
LOCUS       WP_010564821             325 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Pseudomonas extremaustralis].
ACCESSION   WP_010564821
VERSION     WP_010564821.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..325
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34312
     Region          4..322
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 msthlstdql lhaytvmrti rdfeerlhve fatgeipgfv hlyagqeasa agvmahlnde
       61 dciasnhrgh ghciakgvdv fgmmaeiygk ktgvcggkgg smhiadqekg mlgangivga
      121 gaplaagaal asklkgsqgv avaffgdggs negavfeamn lasimklpcl fvaenngyae
      181 atgsgwsvac kdiaeravgf gmpgvivdgn dffavhaalg vaverarkge gptlvevkls
      241 rfyghfegda qtyrgpdevk nlreshdcla lfrqrctaeg wldsaqferi dgevaqlied
      301 avrlaksdlk pqaadllsdv yvayr
//
LOCUS       WP_010565491             387 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Pseudomonas].
ACCESSION   WP_010565491
VERSION     WP_010565491.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 387)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..387
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41432
     Region          118..378
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mtldpptila lsvalaaaaa lyltiewrsv repsllfwsa gfatvtlgst lallrssgyl
       61 migiwlangl lvtahvlfll gvarftqvrl splwllmllv wlgmlmlpad lpgskamlav
      121 qsllvalptl rassllrphg kslsvgavql ryvllihglf yvakalsvli pgtlidlaaf
      181 kgeiiqislv egamaimlia lsmtgseryr reqqiarlaa rdpltalynr raldlraprl
      241 laqvspaqpg alllididhf ksvndlhght agdrllials emiravvpqg alaarlggde
      301 fvillnpast qqivelgssl reqfqqlaaq tfatpqsvtl siganlfdqp psslavlieq
      361 gdttlyeskr ggrdsirlvd rtggssg
//
LOCUS       WP_010565509             210 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Pseudomonas extremaustralis].
ACCESSION   WP_010565509
VERSION     WP_010565509.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..210
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=23847
     Region          10..201
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mdkpglisdd sgqthcawrt aapeypryhd hewgvpvadd vqlyekicle gfqagmawit
       61 ilrkreqfra afegfdfrrv aqygeadiqr lmrdagivrn rakivsainn arracelvde
      121 tgslarwlwt fepgaeerpt vvdmaywtan ptspasvrls kalkkrgwty vgpttmyalm
      181 qatgmvndhl egcacrprie alrrhfkrpt
//
LOCUS       WP_010565530             371 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010565530
VERSION     WP_010565530.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..371
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39726
     Region          1..276
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrelgiglig tgfmgrahal afnnaravfe lpftlklaal adadterarr catawgfaqa
       61 hgdwqalind ptvdvvaitt pnhlhypmam aaiaagkavy cekplavsle qadtmrraaa
      121 aagvvtrvgy nyqhnpmigl arqliaggel gelisfqgef sedfmadpas pwswrcevnh
      181 aggaladlgs hllsmarhlm gdvlsvcadt qtvhaqrpvs qgsaertaia vddqvhallr
      241 fangargtvs sswlkhgykn hlsfvisgtq gtlafdqerl nelrlcragq dgfqrllagp
      301 alpgyaafsp aaghqlgyne lktlevqeli mavagqgadg sdfeaaweve qlatairlaa
      361 reerwvkpqd l
//
LOCUS       WP_010565549             217 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010565549
VERSION     WP_010565549.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 217)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..217
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22720
     Region          12..215
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 meflnafshl dwaqvlhltg qhitlvgiav ilaivvgvpl gvlmtrfptl agplqasatv
       61 lltvpsialf glllpfyskf gqglgpmpai tavflysllp imrntylalt gvepgireaa
      121 kgigmtfgqr lrmvelpiav pvilagvrta vvmnigvmti aatigagglg vlilasisrs
      181 dmsmlivgav lvsllaifad lllqwlqrsl tpkgllk
//
LOCUS       WP_010565612             309 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010565612
VERSION     WP_010565612.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..309
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34335
     Region          22..89
                     /region_name="HTH_MlrA-CarA"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators MlrA and CarA; cd01104"
                     /db_xref="CDD:133379"
     Site            order(23..25,39,56..58)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133379"
ORIGIN      
        1 mtvalqdepg vdvaqaleng wlpirevarq tgvnavtlra werryglivp qrtakghrlf
       61 ssdhvqriht iltwlnrgvp vsqvkglids aqalpdaven ewqtlrqnlv saigelaerq
      121 vddafnqama lypprtlceq lllpllqale qrwqgqfgaq mervfflswl rskfgariyh
      181 nnrqlhgapl llinhsdlpl ephlwlsawl assadcpvev fdwplpvgel alavehlkpr
      241 avllysskal nvttltkllg gvdcptvmtg psvcihqael svlthdipal fvaedplsah
      301 qlliqrgll
//
LOCUS       WP_010565659             725 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Pseudomonas].
ACCESSION   WP_010565659
VERSION     WP_010565659.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..725
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80290
     Region          31..715
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtplpaplrw lhslewrrgf fdwarsdgvt wvyifkvlia afatlwlamr lelpqprtam
       61 itvfivmqpq sgqvfaksfy rflgtltgsa vmvllialfa qntelflgsl aiwvgictag
      121 atrnrnfray gfvlagytaa mvglpalahp dgafmaavwr vleislgilv stlvsaailp
      181 qtssaamrna lyqrfgvfal fvtdglrgrs kreafestnv rfiaeavgle glrsltvfed
      241 phmrrrngrl srlnsefmsi ttrfnalhql lerlradaad hvvaeikpgl qdlaevldgf
      301 sgraltspda vrlvnqlsvy kdglpakvrs lraifqqgnp sedeqldfht ayellyrfvd
      361 dlhnyaqtha sladhthare qwdetfipkt nwlaclasgl rasfilivlg sywvatawps
      421 gatmtliaaa tvglsaatpn pkrmafqmac gtfigalvgf vemffvfpwi dgfpllcvml
      481 apviifgafl nsrpqyagvg vglliffstg svpdnltvyn pyafindyia mvigmlvcaa
      541 agaiilppns rwlwrrleqd lreqvvyais gklkglassf esrtrdllhq ayglavgqpq
      601 vqrdllrwmf vvlevghaii elrkeqailp vhpayaesqp wrqairvmgr slvrlflqps
      661 asnlerglia vdhaisrvqa tdepfaphfd tsalrrvksy lhfirtslld pqsplaalkg
      721 aphas
//
LOCUS       WP_010565661             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010565661
VERSION     WP_010565661.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34979
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqsmraf scvaeagsft aaavqldttt anvsravsnl eahlqtrlln rttrrialte
       61 agkryllrce qilayveeae aeasdaharp agqlkvhtmt gigqhfvida iaryrrthpd
      121 vtfdltlanr vpdlldegyd vsivlaselp dsgfvsqrlg itysiacasp dyvkakgcaq
      181 rphdllnhsc lrlvspvvll dkwtfngpeg qesvaintsp flvnsadamk taitsgmgvg
      241 llpvyaaieg lrngtlvrvm pnyrsqelnl yaiypsrqyl dakiktwvey lrgslpeila
      301 ahqaelaaye lsgslggvrl an
//
LOCUS       WP_010565710             210 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Pseudomonas extremaustralis].
ACCESSION   WP_010565710
VERSION     WP_010565710.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22443
     Region          1..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mylaefltva lihllavasp gpdfavvvre svthgrragt wtalgvgsai flhvgysllg
       61 iglivsqsiv lfnalkwaaa ayllyigfra lraqpakpaa egelhrevge rtargaftag
      121 fvtnglnpka tlfflslftv vinpqtplai qagygvylav atalwfclva mlfsqqrvra
      181 gfarmghwfd rtmgavliai gvklaftsmk
//
LOCUS       WP_010565712             332 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Pseudomonas
            extremaustralis].
ACCESSION   WP_010565712
VERSION     WP_010565712.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..332
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=35559
     Region          3..332
                     /region_name="rsmC"
                     /note="16S rRNA (guanine(1207)-N(2))-methyltransferase
                     RsmC; PRK09489"
                     /db_xref="CDD:181902"
ORIGIN      
        1 mdprsevllr qaelfqgnll lvglpaddll grlpnahgws whagdqaald arfpersqfg
       61 vnapersfda aviflpkske ltdyllnava srlpgaelfl vgekkggies aakqmiplgk
      121 prkldnarhc qlwqvtvana pqavalesla qvfdvplaeg plkvvslpgv fshgrldrgt
      181 elllehldkl psghlldfgc gagvlgaavk rryphntvtm ldvdafaaas srltlaangl
      241 eaevltgdgi daapmglnai lsnppfhvgv htdyfatenl lrkaakhlak ggelrlvans
      301 flkyqpliee hlgvcavkae gngfrvyrak rg
//
LOCUS       WP_010565777             292 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Pseudomonas].
ACCESSION   WP_010565777
VERSION     WP_010565777.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..292
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31892
     Region          <6..291
                     /region_name="bifunc_ST_SDO"
                     /note="bifunctional sulfur transferase/dioxygenase Blh;
                     NF040641"
                     /db_xref="CDD:468609"
ORIGIN      
        1 mrvklhvegf fdaathtvsy lvldeatlhc aiidsvldyd pksghtttts adrliarvse
       61 lnakvewile thvhadhlta apylkeklgg kigigsqist vqevfgtlfn tgsdmprdgs
      121 qfdhlfvnde sfsigtlhct tlhtpghtpa cmtylisngs etaafvgdtl fmpdygtarc
      181 dfpggnartl fqsinkvlsl padtmlylch dyqpggrevq fastvaeqra hnvhvrngis
      241 eeefvamrtk rdaslemptl ilpsvqvnmr aghfpepesn gisylkipln va
//
LOCUS       WP_010565744             306 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010565744
VERSION     WP_010565744.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33239
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like_2"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08471"
                     /db_xref="CDD:176160"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176160"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176160"
ORIGIN      
        1 mdrfhemqvf vtvaeeegfa aaarrlntsp psvtraiaam earigtqlla rttrslhlte
       61 agqrylddcr rilaeleeae daaagsysip cgqltvtapv lfgelyvapv lgayleqfpl
      121 vninallvdr vvnmtdegvd vavrighlhe pdqqaikvge vrrvvcaspg yldqhgrpqh
      181 paqlrdarlv tssasqrvse wtfaeggqpl tvaieprlvv tannaainla rlgwgmtrvl
      241 syqvaaavaa geleivledf epaalpiqvv fhprgrvpak vhtfvdflsq qlgqdvalnp
      301 trqrrg
//
LOCUS       WP_010565863             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Pseudomonas].
ACCESSION   WP_010565863
VERSION     WP_010565863.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..265
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28907
     Region          2..252
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 makvfaianq kggvgktttc inlaaslvat krrvllidld pqgnatmgsg vdkhglensv
       61 ydlligecdl gqamhysehg gyqllpanrd ltaaevvlle mqmkesrlrs alapirenyd
      121 yilidcppsl smltlnalva adgviipmqc eyyaleglsd lvdnikriae llnpnlqieg
      181 llrtmfdprl slmndvsaql kehfgdqlyd tviprnirla eapsygmpal aydktsrgai
      241 aylalagemv rrqrrnsrta aaqpt
//
LOCUS       WP_010565892             288 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter permease [Pseudomonas].
ACCESSION   WP_010565892
VERSION     WP_010565892.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..288
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30284
     Region          14..276
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mhftahlwmp fldfvfmrra ligglvlacs taplgvflil rrmsligdav ahgilpgaal
       61 gfwfaglslp altigglgag lsmaglsawi trrtglreda slaaiypisl aagvlilgla
      121 gkrldllhll fgsalavdet tltgmlwvsg fsliamgliy kpllldtldp lflqtvsrlg
      181 plahglfltl vvlnlvigfq aigalmvvgl mmlpaiasrf wsrrlpvlia isavlgclsv
      241 wfglllsfyy slpsgpaivl vagggyllsv vfgpvhgllr rppslssq
//
LOCUS       WP_010565902             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Pseudomonas].
ACCESSION   WP_010565902
VERSION     WP_010565902.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..161
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18125
     Region          5..147
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mepgnaqlsm tvlmtpdman fsgnvhggtl lkyldevaya casryagryv vtlsvdqvif
       61 repihvgelv tflasvnytg htsmevgikv vtenirersv rhtnscfftm vavddqrkpa
      121 avpplqphns edkrrfvqak qrrqirqele kryqeikdda p
//
LOCUS       WP_010565903             587 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Pseudomonas extremaustralis].
ACCESSION   WP_010565903
VERSION     WP_010565903.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008671
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..587
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=63844
     Region          1..540
                     /region_name="RosB"
                     /note="Predicted Kef-type K+ transport protein, K+/H+
                     antiporter domain [Inorganic ion transport and
                     metabolism]; COG4651"
                     /db_xref="CDD:443689"
ORIGIN      
        1 mhaisfiqdl avimlvagvv tilfhrlkqp vvlgyivagf iigphtppfg lihdegtikt
       61 laelgviflm fclglefslr klfkvgataf iaafleivlm iwigyeigrw fgwntmdslf
      121 lgailaisst tiivkalndl kmknqrfaql ifgvlivedi lgigiialls siavsgtvss
      181 gevfstvgkl slfmivalvi gillvprlla yvarfesnem llitvlglcf gfcllvvkle
      241 ysmvlgafli gaimaesrql ikierliepv rdmfsaiffv aiglmidpqi llqyawpiav
      301 itvavvlgkm lscgigafia gndgrtslrv gmglsqigef sfiiaalgmt lqvtsdflyp
      361 vavavsaitt lltpylirga dplslkiaav ipkrmsrvfg mygewlrsiq pqgegamlas
      421 mirriilqvg vnlalvvaif faggyfaari ggylegwigd pswqkaliwg galllslpfl
      481 iaayrklkal smllaemsvk pemagrhtqr vrrviaevip ilsllvifll laalsasilp
      541 tnkllmliav vaaavaavlw rwfirvhtrm qvalletldn hkdtpeh
//
LOCUS       WP_010565943             438 aa            linear   BCT 01-JAN-2025
DEFINITION  TldD/PmbA family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010565943
VERSION     WP_010565943.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..438
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47393
     Region          25..437
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mnnfkalvqw lnqaitdkeh fhlgyaaess efvrfnhakv rqagqvqqas ltlklindgr
       61 hadlditlag epeldrqrla aglqqlretl pllpgdpyll lnhtawqnhn eqarplpela
      121 hvledisqaa agvdlvgfya agpisrgfas sdgafgwhqa nsfnfdfslf hangeavkas
      181 yaghewnsae ftrrvqqare qlaflgrplh tlapgeyray lapaaleeiv siitwggfsa
      241 qaiaskgssl qrlyageqsl splvtvdeqi sgslspafsa egyprsdvtl ikagqaegql
      301 vnsrsaaeyg lsangasgde spsalqmaag slaqadilkq lgtglyisnl wylnysdlpa
      361 arltgmtrfa tfwvedgeik apvstmrfdd svyqllgsql ealtaerell lsastysqrn
      421 tasnllpgal vkrltltl
//
LOCUS       WP_010565409             638 aa            linear   BCT 01-JAN-2025
DEFINITION  lipase family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010565409
VERSION     WP_010565409.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Wong,H. and Schotz,M.C.
  TITLE     The lipase gene family
  JOURNAL   J Lipid Res 43 (7), 993-999 (2002)
   PUBMED   12091482
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Cygler,M. and Schrag,J.D.
  TITLE     Structure as basis for understanding interfacial properties of
            lipases
  JOURNAL   Methods Enzymol 284, 3-27 (1997)
   PUBMED   9379943
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..638
                     /product="lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=72617
     Region          208..387
                     /region_name="Lipase_3"
                     /note="Lipase (class 3). Lipases are esterases that can
                     hydrolyze long-chain acyl-triglycerides into di- and
                     monoglycerides, glycerol, and free fatty acids at a
                     water/lipid interface. A typical feature of lipases is
                     'interfacial activation,' the process of...; cd00519"
                     /db_xref="CDD:238287"
     Site            order(257..258,260..268)
                     /site_type="active"
                     /note="active site flap/lid [active]"
                     /db_xref="CDD:238287"
     Site            313..317
                     /site_type="active"
                     /note="nucleophilic elbow [active]"
                     /db_xref="CDD:238287"
ORIGIN      
        1 mtrpsyplpi telqvraeqt rffhkdgspr ehnpalkpgd efiqvevrdl vkhsahlppp
       61 iidrkypped iliralnelr fspapvatfg vgllsnrhtl lqvrplrafr pmlstdnqfc
      121 alnlyqlaim anlsycdfgq hpakdpvdrv sfpldpsvgh ffgealsnyr eswkvdnaqs
      181 pnhryyplye evpyskrfei lpfdptlyeq nkpgenqehp aklhffddts thwfsakstq
      241 afithhdevi lisirgtlel adwwrdvdaa qvpfeegkgk vhrgfyeayk alkkfiqdyl
      301 frfyvgqkii isghslggai alllaealrn atdnnydvll ytygaprtgd atfvaaaepl
      361 ahhravnnnd mipsvpapwm narrsiwipg fkamfitnpv lgalifvagl vrvggapyqh
      421 hgtlhhfmlv pfnpkemssi lwrpgcdsie qaactralak dgdlpyrdgw itqlmslgdh
      481 siprayipls watlrrwqqt qetrgtlvte reyalvdqal ktmrfkveek srhmrynqrd
      541 ltdadylqad ieltresdkl ahslqrlerl rishlsladv ygsaaqspal eialarwkdq
      601 rentlqvqia mipepdpaee lfasladkpr pldldsli
//
LOCUS       WP_010565975             545 aa            linear   BCT 01-JAN-2025
DEFINITION  GspE/PulE family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010565975
VERSION     WP_010565975.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..545
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=59272
     Region          3..543
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mseqthqwqa laaqrgisls ryllevleqa pdqlatiarp lglraiapqq lsehwrfdll
       61 alplalihnv lpvdhegepc lvlgdpftla srywlqssat lrqlplamsl pgavkaqltq
      121 aeasqrvmqp fgeadengpv gqaaqeisls siarddnpvv rlvnsmlfda lqsrasdihv
      181 ettpqglvik yridgvlqqm gqasgmdmae qalsrlkvls eldigerrvp qdgrfkmkiq
      241 grevdfrvsi mpsihgedav lrildksqrg eslslanlgl dadtiarirv lasepygmll
      301 vtgptgsgks ttlyaalset ntgekkiiti edpveyelpg vlqipvndkk gltfarglrs
      361 ilrhdpdtil vgeirdgeta giavqaaltg hlvmssvhan safsvlerft ymdvdpasfv
      421 ealngvvaqr lvrrvcpdcg vetrpdadia rlaqlpeaql dngayregkg cdacrhtgyr
      481 grlalaevls lndsikegll krssastlre lardaghvfi rdialahaal ghttlkeihr
      541 visly
//
LOCUS       WP_010565976             394 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Pseudomonas
            extremaustralis].
ACCESSION   WP_010565976
VERSION     WP_010565976.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..394
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=43044
     Region          10..393
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 midfdarivr dghlhtlrvq aldvdqarhq lqadgaqvis lqarrqlrwp grrarfalgl
       61 fiqelvvlld aglvlveave tlrdkaapgi nrqvmsdlla smyqgnslsk alqlkpevfp
      121 slliatvass ehsgqlsval rryhhfeahl eavkkrvsga lmypmvvlsv galilvfllf
      181 fviprfaavf davadlpata rlmvwwgdlv qtqgnllltg lvlavgglvl llrsaafkqr
      241 aarllwkips lgaqrtlfvl arfyrtagml lmggmpvvta valsgallpa erqadlrham
      301 tdiqagqpls tslarhqltt avaerllrvg eqsgelaamc eriaqfhdea leraielfsk
      361 vfepllmlvv ggliglivfm lympifelag siqg
//
LOCUS       WP_010566080             401 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Pseudomonas
            extremaustralis].
ACCESSION   WP_010566080
VERSION     WP_010566080.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..401
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43850
     Region          7..127
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          126..399
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msltiadvla lqglesmrlr agaagldnsv rwpyvaentg iaewvlggel vfvtginhpr
       61 deanllqlld eacqrqvagl viltgpayiq aipprlldaa eaagmplieq pyslkmvlvt
      121 qaigsaliqs eqlgrsrhdv lerlltgdyq sldlllhraa qlglalgghw qvaqlqlegs
      181 ellfaqddaa qveaqlarqh dnisrrlrql ssvlpvlgra gqwtlllpap davaalanrq
      241 qlaswlnpln lrlaplklfi glsaaahppm rlaqaqdear qaltaarrfs eraglcvyde
      301 lgvlkllsgv rdralldqfl nerlgpllrh drhhgpslmp tleawfheng nlvaaaqrla
      361 vhrntlthri qriealcglt ldnaynrldi gialmiwrls a
//
LOCUS       WP_010566097             608 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Pseudomonas
            extremaustralis].
ACCESSION   WP_010566097
VERSION     WP_010566097.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..608
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=68287
     Region          10..600
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mvdlknepqs aidahgiigd mrsaalvndr gsidffcwpe fdspsifcal ldtpdagtfq
       61 ltpdlpnarr eqiylpdtnv lqtrwlsdda vveitdllai sdevddlpll irrvrmvsgq
      121 apihlrcavr hdyarastha aidqgtvcfs aagqpglrls sshpltlddn aavasftlyq
      181 gegaefvlgg qddervdssc tdlalahtlt fwrgwiaqsn yrgrwremvn rsalalkllt
      241 srkhgaiiaa atfglpetpg gernwdyryt wvrdasftvy afmrlgfvde anaymrwlrg
      301 rvsdgcgqsr kikilygidg rqqlpethld hlcghggatp vrignaaveq iqldiygelm
      361 davylvnkyg eaishegwkh tvevvdqvce iwnrkdvgiw emrgeqhhfl hsrlmcwval
      421 drairlaskr slpapfarwd qtrqaiyadi wsqfwneerg hfvqhigsta ldgsmllmpl
      481 vrfvaatdpr wlstleaiqd slvrdgmvyr yrnddnpidg lqgtegafta csfwyvecla
      541 ragqvekahl efeqllryan plglyaeefd nqarhlgntp qalshlalis aacfldrkls
      601 gekttwqp
//
LOCUS       WP_010566186             469 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Pseudomonas extremaustralis].
ACCESSION   WP_010566186
VERSION     WP_010566186.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..469
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50910
     Region          1..461
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 msgphsssge lkrglknrhi qlialggaig tglflgsagv lksagpsmil gyaicgfiaf
       61 limrqlgemi veepvagsfs hfahkywggf agflsgwncw ilyilvgmse ltavgkyvhy
      121 wwpeiptwvs aaaffvlinl inlanvkvfg eaefwfaiik vvaivgmial gsyllvsgsg
      181 gpqasvsnlw ehggffphgv gglvmamaii mfsfggleml gftaaeadqp rtvipkainq
      241 viyrilifyi galvvllslt pwdslletln asgdaysgsp fvqvfsmlgs ntaahilnfv
      301 vltaalsvyn sgtycnsrml lgmaeqgdap rvlakidkrg vpvrsilasa aitlvavlln
      361 ylipqhalel lmslvvatlv inwamisfsh fkfrqhmdrt gqvplfkalw ypygnyvcla
      421 fvvfilviml mipgiqvsvy aipvwvafma vcywiknkrk aqatrsvle
//
LOCUS       WP_010566216             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudomonas
            extremaustralis].
ACCESSION   WP_010566216
VERSION     WP_010566216.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33214
     Region          1..293
                     /region_name="trans_reg_YafC"
                     /note="DNA-binding transcriptional regulator YafC;
                     NF040888"
                     /db_xref="CDD:468824"
ORIGIN      
        1 mkarsdelqi fvsviecgsi saaaeqvgqt psavsrtlsr leakldttli nrttrrmdlt
       61 eegkyffers klilaqmdel eehlssrqqk pagrlrinaa vpfmlhgivp yiaefrrlyp
      121 diqlelnsdd liidlleqst diairigala dstlharslg ctplhilasp aylqrhgtpt
      181 svaelaehtl lgfsqtetln hwplrhvegd rwliepgiaa ssgetlrqla legqgiccls
      241 nfmtiddint grlvpvleaf ntgyrqpiha vfyrnsqlal riqcfldfiq aklaryac
//
LOCUS       WP_010566316             422 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aspartate aminotransferase family protein
            [Pseudomonas].
ACCESSION   WP_010566316
VERSION     WP_010566316.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..422
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45237
     Region          30..411
                     /region_name="ArgD"
                     /note="Acetylornithine/succinyldiaminopimelate/putrescine
                     aminotransferase [Amino acid transport and metabolism];
                     COG4992"
                     /db_xref="CDD:444016"
ORIGIN      
        1 mnlfnlrrpa aslddliiea prndfpgecl mptvarppqv fvrgqgswlw dsddrayldf
       61 sqgsaanslg hspkvlvnal adqaqalinp gyglhnrpql nlverlchrt gsdqayllns
      121 gaeaceaaik larkwgqlhr ggayriisas ngchgrsfaa msasastcen rfepqlpgfs
      181 hvplndlaal haavdaktva imlepiqsea gvilatehyl qgverlcrel gillildevq
      241 tgigrcgtll aeerygvrad iitlgkglgg gvpvaallar gkaccfevge legthhgnal
      301 masvgvavld tvlehgfleh vresglylse glarlayryd hgqlrgdglm wgltlsddsa
      361 ddvvnaalhe gliinapqpd clrftpaltv sksnidemll rlarafsrvq aaqlqcrkgi
      421 av
//
LOCUS       WP_010566325             148 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010566325
VERSION     WP_010566325.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..148
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16049
     Region          4..138
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 msvldeidrq liaalqlnar esvamlarql giarttvtsr larlektqvi agygvrlgqr
       61 vadgglqayv gitvqprsgk evlrrlstma qvqqlcavsg efdyvawlrt dspeqldqll
      121 dqigsvdgve ktttsiilsn kldrgqpi
//
LOCUS       WP_010566372             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MOSC domain-containing protein [Pseudomonas extremaustralis].
ACCESSION   WP_010566372
VERSION     WP_010566372.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..268
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29327
     Region          1..268
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mlrlsalyry plksgkaevl qqigldklgl dgdrrwmlvd easgrfltqr avakmsqlsa
       61 lwnasggltl sspgyaplev plpggdaelr gvtiwrdtlr vpdagdeaaa wvsefigkpt
      121 rlvqmplera rttqagfgkd ddqvafadgy pllligqasl ddlsqrigrp memlrfrpnl
      181 vieggepfae dgwkrlrigd vefravkpcs rcilttidpq tgersadrep fatleayrkt
      241 eegaifgqnl indgaghlev gmpvtile
//
LOCUS       WP_010566375             640 aa            linear   BCT 01-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Pseudomonas extremaustralis].
ACCESSION   WP_010566375
VERSION     WP_010566375.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..640
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69961
     Region          4..447
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          573..639
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(596,605..607,614)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            606
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mptftkilia nrgeiacriq rtaqalgyrt vavysdadaq alhvqmadea vhigpapvqq
       61 sylnipaild aarrtgadai hpgygflsen pdfaracqqa gltfigpspq aielmgskrr
      121 sklamleagv pciagyqgsa qddgslqrea erigfplmik asaggggrgm rrvqqredll
      181 eqlrtarsea lnafgsdeli leqalieprh veiqlfgdsh gqliylgerd csiqrrhqki
      241 ieeapcpvmt palrqamgea alkagravdy vgagtvefll drdgrfyfle mntrlqvehp
      301 vtelitgldl vnwqlqvaag qplpltqadv slsghamevr lyaedpaqgf lpqtgevvrw
      361 epaagvrvdh gmlegqcisp fydpmlgkii ahgatreear rkllravedt lllgvasnqr
      421 lladllkhad fidgdfstgf iaehfsdipr htasaeqlal aaalfyrhsa arhhqglsgw
      481 hnnatlpwry rlavnddiqd itvsvlehdr lqvngldish lttdgrwatl vingirrrva
      541 yhlegtqlwl psvtvinrtq qvaarqadvg sgtvkapmdg aivdvrvstg drvtqgqlll
      601 vleamkmehp lkagmdgvvk gvqviagdqv rnrqvlleie
//
LOCUS       WP_010566376             255 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Pseudomonas
            extremaustralis].
ACCESSION   WP_010566376
VERSION     WP_010566376.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..255
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26837
     Region          4..250
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mntllleahn gvlhitlnrp ecrnamslem vnelsavlaq ldsqaravvi sgagghfcag
       61 advkdmarig gtpqlqalnr afgtllqave alpqvvivvl qgavlgggfg lacvsdiaia
      121 dhkaqfglpe tslgllpaqi apfvvkrigl tqarrlalta arfdgieaqr lgvvhftehd
      181 pqalaqrlde vlgdvlrcap ganartkall lasveqplgp lldqaaqwfa eavngeegie
      241 gtqafvhkrk pswck
//
LOCUS       WP_010566401             380 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: patatin-like phospholipase family protein
            [Pseudomonas].
ACCESSION   WP_010566401
VERSION     WP_010566401.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..380
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40327
     Region          2..372
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mrptepvtgl ilsgggaraa yqvgvlaaia ellppgapnp fpvivgtsag ainavtlasg
       61 amdftaaikr ltafwqgfrs hlvlrsdwpg vihqasrfcl hsllglgarv pvalldsspl
      121 rellqerlnl dgiddairrq hlhavavtaf gyesgqavtf yqgggaivpw lrhrrigvpt
      181 eltvehllas saipllfapv kldleyfgdg avrqsapisp alhlgasrvl vvgvsgnprg
      241 neptaqrsyt gqqptlaqig ghmlnstfid slesdielle rlnqfshlqp adsaarglap
      301 vdvlviapsq pideiaarhr qelpaalrlf lrgpgatkts gagvlsyllf eagycselie
      361 lgrrdalakr eeitrflgla
//
LOCUS       WP_010566547             333 aa            linear   BCT 01-JAN-2025
DEFINITION  ADP-ribosylglycohydrolase family protein [Pseudomonas
            extremaustralis].
ACCESSION   WP_010566547
VERSION     WP_010566547.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..333
                     /product="ADP-ribosylglycohydrolase family protein"
                     /calculated_mol_wt=34077
     Region          4..333
                     /region_name="DraG"
                     /note="ADP-ribosylglycohydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG1397"
                     /db_xref="CDD:441007"
ORIGIN      
        1 mtaqsralga fyglalgdal gmptqslsre qvrarfgait gledagadqp iapnmpagsi
       61 tddteqaili gellvagqgk iepivlarrl ieweavmrak gsqdllgpst qraidmilag
      121 htpqesgryg ttngaamrit pvgiaadvsd pesfiqaviq acqvthnttl gissaaavaa
      181 vvsagingvd lgealnigtq iaqqaqshgh wiaggristr iswartlsvg sgdkalfadl
      241 lyeligtsva sqesvvvsfa laqqvavgal dafealclaa slggdtdtia ailgamlgac
      301 lgmqcwpqal ieqvkavngl dlqalvqgll alr
//
LOCUS       WP_010566543             398 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010566543
VERSION     WP_010566543.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..398
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41092
     Region          1..345
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mhstspvntk lfalfclasf llslsygstf llslliqlrg gnehdagsvi stamlstfva
       61 vvvsghlada wgaaraiagm glllvvaclg faltpglged lkgfglalgl gwgvfytlgp
      121 iivamlvepr qraryfalls gsmlsgigag pllgraasal tlplttafhi aalasligvv
      181 mfwrlgahlk rqanapvaki swvairqvls skaafailmv glggcvfggl ssfqtsyaaa
      241 hgldyslffa gflsaaitsr lliagfvvkl dayraacgls gvmlgsivlf afgvsgnfsy
      301 llaaaslgvg ygltysving lvaneapsgt tpqalllfsl ayfvgvfgfp wlagkiivdy
      361 glsalmlsvl tiaalnwlit varliarria apkivqvs
//
LOCUS       WP_010566637             378 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar ABC transporter permease [Pseudomonas extremaustralis].
ACCESSION   WP_010566637
VERSION     WP_010566637.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 378)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..378
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39851
     Region          4..378
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mnqlkqlftr ykmlalviav aviwlffswq teggfvtprn lsnllrqmsi tgilacgmvl
       61 viisgeidls vgsllgllgg laaildvvyh lpllanlslv alcglmigla ngymtaylri
      121 psfivglggm lafrgillgi tggttiapvs pslvyvgqgy lpyhvgvglg vllfaltlfl
      181 twkqrrnral hglaahsrar dvlrvvviga vlagfvttln rydgipvpvl lllvllgvfs
      241 yvtsqtvfgr rvyavgsnme atrlsginvq avklwifgim gvmcalaglv ntarlaagsp
      301 sagnmgelda iaacfiggts mrggsgtvyg allgalvits ldngmsmldv dsywqmivkg
      361 silvlavwvd vstragrr
//
LOCUS       WP_010566552             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010566552
VERSION     WP_010566552.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25592
     Region          9..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mhkeprkvre frrreqeild talklfleqg edsvtvemia davgigkgti ykhfkskaei
       61 ylrlmldyer dlnellhsad vdkdkealsr ayfefrmrdp qryrlfdrle ekvvkghqvp
      121 emveelhkir asnferltll ikgrisegkl edvppyfhyc aawalvhgav alyhspfwsn
      181 vledqegffq flmdigvrmg nkrkhstelp qvpvetpat
//
LOCUS       WP_010566142             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Pseudomonas].
ACCESSION   WP_010566142
VERSION     WP_010566142.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Lindquist,J.A. and Mertens,P.R.
  TITLE     Cold shock proteins: from cellular mechanisms to pathophysiology
            and disease
  JOURNAL   Cell Commun Signal 16 (1), 63 (2018)
   PUBMED   30257675
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20378504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..200
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21889
     Region          1..112
                     /region_name="CSP_NTE_dom"
                     /note="cold shock protein N-terminal extension domain;
                     NF041604"
                     /db_xref="CDD:469488"
     Region          133..196
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mlkivhlltg vaalllsfip slqpeslpyl qqhdalylal fgllnltlap vipywnkgtr
       61 hqlqnlvsal lvltvvvqtl tllapmpevg ghpaillslv ialvaivlhl aisfyrsspa
      121 aasqnydmtn rdtgtvkwfn tskgfgfisr dsgddifvhf rairgeghrv lvegqrvefs
      181 vmnrdkglqa edviaalprr
//
LOCUS       WP_010566646             347 aa            linear   BCT 01-JAN-2025
DEFINITION  LLM class flavin-dependent oxidoreductase [Pseudomonas
            extremaustralis].
ACCESSION   WP_010566646
VERSION     WP_010566646.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..347
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38540
     Region          32..347
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mkfslfvhme rwdesishrq lfedlteltl maeaggfstv wigehhamey tispspmpll
       61 aylaakttti hlgagtiiap fwhplrvage calldvisng rmevglarga yqvefdrmag
      121 gmpaasggqa lremvpvvra lwqgdyahdg diwkfptsts vpkpvqkpnp pmwiaardpd
      181 shnfavangc nvmvtplmkg deevldlknk fqtaldnnpg vprpqlmvlr hthvhavddp
      241 egwkvgakai skfyrtfdaw fgnkevpvng flapspeekf agrpefelds lhktamigta
      301 aeiiprikyy qelgvdefsf wcdnslphae kkkslalfie qvvpafr
//
LOCUS       WP_010566661             441 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Pseudomonas extremaustralis].
ACCESSION   WP_010566661
VERSION     WP_010566661.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..441
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45637
     Region          26..440
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 minrllgksl fgllaasafa plaqaadapt lntgstawmv taavlvlfmc lpglalfygg
       61 lvraknmlsl ftqcfgvagl vgvlwviygy smvvdttgmv egqvtfnsfv gglsraflag
      121 mtpaslvgdi pegvfvtfqm tfaiitpali agafaermkf saallfmavw ftlvyapvah
      181 mvwggsgalm hnwgvldfag gtavhinagv aalaaclilg krkgyqntpm pahnlsltma
      241 gaamlwvgwf gfnigsgggl ngtsgivmln tqlgacagil gwmftewfkv gkpsalglas
      301 galaglvgit pacayvgvgg alaigllcgv fcylsvtvlk rrfgyddsld vfglhgiggm
      361 igavltgvfc vpsmgglveg vtmggqvvaq ikgvllttvy cfvvswiilk vvnalvglra
      421 hesveemgld laehnerayn h
//
LOCUS       WP_010566673             248 aa            linear   BCT 01-JAN-2025
DEFINITION  PAS domain-containing protein [Pseudomonas extremaustralis].
ACCESSION   WP_010566673
VERSION     WP_010566673.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..248
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=28582
     Region          14..246
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 mrespeawaq tppahlmdcf paallhlrdn gqiahfnlaw aelmgppgae rnlvdyvhqe
       61 drplwrqalh elrrrpetsf nqrlrfvhpc gelrwfevsl krgpqgfylv agditahkrr
      121 eialqasqrs smslldsmpg liyrgrnnrd wtmefvsagc lqltgypaer lvdnheftyn
      181 slilaedady vwrevqyals rqepfelnyq ircadqsikh vwekgvgiya dtcevlgieg
      241 aiferktp
//
LOCUS       WP_010566678             276 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas extremaustralis].
ACCESSION   WP_010566678
VERSION     WP_010566678.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..276
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29002
     Region          4..189
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mspiwnmark efcdglrnrw llaisllfav laigiawlga aaagqlgfts iaatiaslas
       61 latflmplia lllaydaivg edesgtllll ltyplgrgqi llgkfvghgl ilalatvlgf
      121 gcamlaiall vddvqlglll wafgrfmlts tllgwvflgl ayglsslcae kstaaglalg
      181 vwfffvlvfd lallallvvg kgqfspqglp wllllnptdv yrlinlsgfa sgtqsmgvma
      241 lgsdlgvapl alwacllawv gvplalayal frrraa
//
LOCUS       WP_010566461             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycerophosphodiester phosphodiesterase
            [Pseudomonas].
ACCESSION   WP_010566461
VERSION     WP_010566461.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..240
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26766
     Region          1..238
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mtliyghrga kgeapentlt sfqeclkhgv rrceldlhls mdgelmvihd ptlkrtadrr
       61 gkvveysaad lvkmdarkgg pgwikpcpip rleelfekcd fdhwqlevks asrtraattv
      121 lairemavrf glmdkvtvts ssrevlkaav eltpdlsrgl vaeyawldpl kvaqnygcei
      181 lalnwtlctp erlekaqrqg lhvsvwtvne palmrrladf gvdslitdfp glatatleny
//
LOCUS       WP_010566687             180 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: gamma carbonic anhydrase family protein
            [Pseudomonas].
ACCESSION   WP_010566687
VERSION     WP_010566687.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..180
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19211
     Region          1..176
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mtlrtyqnht ptlaagafvd isavvigdve igadssvwpl tvirgdmhri rigartsvqd
       61 gcvlhithag pfnpdgfpll igddvtiahk vmlhgctvgn riligmgsiv mdgavveddv
      121 iigagslvpp gkklesgyly vgspvkqire ltdkerafft ysaanyvklk dlhlaegfdr
//
LOCUS       WP_010566704             211 aa            linear   BCT 01-JAN-2025
DEFINITION  SCO family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010566704
VERSION     WP_010566704.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..211
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22844
     Region          53..193
                     /region_name="SCO"
                     /note="SCO (an acronym for Synthesis of Cytochrome c
                     Oxidase) family; composed of proteins similar to Sco1, a
                     membrane-anchored protein possessing a soluble domain with
                     a TRX fold. Members of this family are required for the
                     proper assembly of cytochrome c...; cd02968"
                     /db_xref="CDD:239266"
     Site            order(84,88,174)
                     /site_type="other"
                     /note="Cu(I) binding site [ion binding]"
                     /db_xref="CDD:239266"
ORIGIN      
        1 mtrtqktvfi lvaivalimg ltvnkvlsgk gqgdpaalid agiillpqsr qlppvsmtnq
       61 dgqpvlvnel kgkwsllffg ytfcpdicpt tlaqlrqiks elpkeavdkl qvilvsvdpn
      121 rdtptqlkqy lgyfdpqfqg ltganvddvq klsnavsipf ipadtskpny tvdhsgnlal
      181 igpdgtqrgf iraplnnqkl iaqlpgllqr k
//
LOCUS       WP_010566732             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010566732
VERSION     WP_010566732.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..267
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28422
     Region          8..249
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 msrlprapse avievrglcn rfgsqsvhen ldldlykgei lavvggsgsg ksvllrsivg
       61 lrrpsagevr vfgknlsnlp eqerslverr fgvlfqkgal fssltvtenv alpliehagl
      121 sradaehlaa vklalaglpl saadkypasl sggmikraal aralaldpdi lfldeptagl
      181 dpigaaqfdq liltlrdalg lsvflvthdl dtlytitdrv avlsqkkvlv adaidvvset
      241 ddawiheyfh gprgraalda aqslnev
//
LOCUS       WP_010566842             323 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Pseudomonas
            extremaustralis].
ACCESSION   WP_010566842
VERSION     WP_010566842.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..323
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34910
     Region          11..322
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 maverstvel gvliyqgaql aavhgltdlf gvanriaaeh qsmqlpllrv shwqvdahgi
       61 parvfdshpg vdqpmmavlv ppsidefgee qappallewi rqqhaagtvl ggvcigsiml
      121 arsglldgrs atthwssaks fairypevrl eadkpivddg dlittaglma wselglrlvd
      181 rlmgpsiaad tarflviehs dsasqcgsnf apilghgdaa ilkvqhwlqa sgavdvsvaa
      241 maqeagleer tflrrfrnat glkpteycqh lrvgkarqml eftngtidhi awtvgyqdps
      301 afraifkkit glapsdyrsr fgv
//
LOCUS       WP_010566849             482 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: catalase [Pseudomonas].
ACCESSION   WP_010566849
VERSION     WP_010566849.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..482
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53674
     Region          2..481
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 msqnkiltta sgapvadnqn srsagprgpl llddfhliek lahfnrenip errvhakgsg
       61 aygtftvtkd ithytsaklf esvgkqtptf lrfstvgger gsadterdpr gfalkfytee
      121 gnwdivgnnt pvffirdplk fpdfihtqkr lpqsnlksaq mmwdfwshsp ealhqvtilf
      181 sdrgipdgyr hmhgfgshty slinakgerh wvkwhyktkq giknlapaea arlagtdpdy
      241 aqrdlfgaie rgdfpkwrvc iqvmteaqan ahyenpfdvt ktwsqkefpl ievgelelnr
      301 npqnyfaeve qaafgpsnmv pgvglspdrm lqgrvfayad ahryrvgtnh qqlpvnaprc
      361 pvnsyqrdgs mafgsngggt pnyepnsyad apkqapqyae palalsgaad rydhredtdy
      421 yshagalfrl msdeqkallt nniagamagv ssdvvqrqlq hfykadpayg eaiakalgvs
      481 rn
//
LOCUS       WP_010566944             223 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Pseudomonas extremaustralis].
ACCESSION   WP_010566944
VERSION     WP_010566944.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..223
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24153
     Region          36..197
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mllrlllfcg latvatstla mtlykstdah gevffsdrqt pgaqafviqe rrtervsrpv
       61 lerpkprypq payryplpwr ggpfrltqgp ngsfshtdak sryamdiamp egtpiiaars
      121 gvvmnieneq vgrgndasgn fvrvqhddgt qgvylhlkqg svsvrpgqrv rvggalglsg
      181 ntgnssgphl hfvvqqhtea glvsipyefn qpvgtlpnfa lgn
//
LOCUS       WP_010566951             382 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Pseudomonas].
ACCESSION   WP_010566951
VERSION     WP_010566951.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..382
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40162
     Region          4..366
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mnapvviigt glagynvare frkldsetpl llitaddgrs yskpmlstgf gknkeadgls
       61 maepgtmaeq lnaevrthtr vsgidpghkr lwigeeavay rdlilawgae tvrvpvegda
      121 aelifpindl edyarfraaa agkhrvlvlg agligcefan dlilggyeid lvapceqvmp
      181 tllhpaaaaa vqagleglga rfhlgpvlnr lqrsadglea hlsdgkvilc dlvvsaiglr
      241 pridlaaaag lqvnrgimvd rhlktshani yalgdcaevd glnllyvmpl mtcaralaqt
      301 lagnatavsy gpmpvtvktp vcplvvsppp rgtegvwsve gqgadikalc rdasgrllgy
      361 altgsavmek lalnkelppl la
//
LOCUS       WP_010566973             277 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pseudomonas extremaustralis].
ACCESSION   WP_010566973
VERSION     WP_010566973.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..277
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30085
     Region          58..249
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mgtltwirrf ngtlghlapq avankmrraf mtprdlpprd welpllaqse ritlrfglsa
       61 lrwgqgpavl lmhgwegrpt qfaslitalv dngysviald gpahgrspgr eahvllfara
      121 mleaaaelpp lhgvighsmg gasamlavql glrtealvsi aapsrfldvl cgfthlvglp
      181 ararsafiqe veltfgmplk hldvahyqmn ipglvvhaed dtfvpvrasq aiheawfdsr
      241 llrleqgghq kvladprvie gvlallagrr lqarqta
//
LOCUS       WP_010567017             325 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010567017
VERSION     WP_010567017.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..325
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33357
     Region          4..323
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mktttspgkt ggnfyglgty lglagallam ialfsvlsdh flsydtfstl anqipdlmvl
       61 avgmtfilii ggidlsvgsv lalaasavsv ailgwgwsvl paavlgmaca alagtitgsi
      121 tvawripsfi vslgvlemar gvayqmtgsr tayigdsfaw lsnpiafgis psfiiallvi
      181 viaqlvltrt vfgryligig tneeavrlag inpkpykilv fslmgllagv aalfqisrle
      241 aadpnagsgl elqviaavvi ggtslmggrg svistffgvl iisvlaagla qigateptkr
      301 iitgavivia vvldtyrsqr asrrg
//
LOCUS       WP_010567072              61 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CsbD family protein [Pseudomonas].
ACCESSION   WP_010567072
VERSION     WP_010567072.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..61
                     /product="CsbD family protein"
                     /calculated_mol_wt=6238
     Region          3..61
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 msstsdkvkg vaneavgnik qgvgkvtgnd klrvegviqe kkgevqkavg dtkdaikkat
       61 k
//
LOCUS       WP_010567084             281 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: D-hexose-6-phosphate mutarotase [Pseudomonas].
ACCESSION   WP_010567084
VERSION     WP_010567084.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..281
                     /product="D-hexose-6-phosphate mutarotase"
                     /EC_number="5.1.3.15"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_function="GO:0047938 - glucose-6-phosphate 1-epimerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31771
     Region          29..269
                     /region_name="D-hex-6-P-epi_like"
                     /note="D-hexose-6-phosphate epimerase-like; cd09020"
                     /db_xref="CDD:185697"
     Site            order(73,95,99,159,161,202,235,257)
                     /site_type="active"
                     /db_xref="CDD:185697"
     Site            order(73,99)
                     /site_type="other"
                     /note="phosphate binding residues"
                     /db_xref="CDD:185697"
     Site            order(159,257)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185697"
ORIGIN      
        1 mhehplqrff kslrerpvfa werfqmrdvl vidhplcqav fsrqgaqllh fqprgqkpwl
       61 wcaakwpqvg airggvpvcw pwygrhpsen awpshgwarl idwklldsst ddegvrlhwq
      121 lqlcdwqvdl hahlgetlel rlctehqdel pcqlshalha ywrignvgev alsglegaqg
      181 ydqlnrqvcq qegelrvdgg cqrvfqhege lhlkdhawqr elcidtgdsa dtvvwhpgsr
      241 pllgvsfnea sgfvcvesam agaslapger ahlslqarag a
//
LOCUS       WP_010567099             484 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TrkH family potassium uptake protein [Pseudomonas].
ACCESSION   WP_010567099
VERSION     WP_010567099.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..484
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52794
     Region          69..483
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 malpalriig fiigiflitl aiamvvpmat lvifertqdl psflwaslit fvagltlvip
       61 grpehvhlrp rdmylltvts wvvvcvfaal pflltqrisy tdsffesmsg itatgstvls
      121 gldsmspgil mwrsllhwlg gigfigmava ilpllriggm rlfqtessdr sekvmprshm
      181 varlivaayv gitilgslaf wwagmglfda inhamsaist ggfstsdesl ahwkqpavhw
      241 vavvvmilgs lpftlyvatl rgnrralikd qqvqgllgll vvtwlvlgtw ywwttnlhwl
      301 dalrhvalnv tsvvtttgfa lgdyslwgnf slmlffylgf iggcsgstag gikifrfqva
      361 yillkanlnq lihpravikq kynghrldee ivrsiltfsf ffaiticaia lalsllgldw
      421 mtaltgaast vsgvgpglge tigpagnfas lpdaakwils lgmllgrlei itvfvlcipa
      481 fwrh
//
LOCUS       WP_010567215             319 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Pseudomonas
            extremaustralis].
ACCESSION   WP_010567215
VERSION     WP_010567215.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..319
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34866
     Region          2..317
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigyllsd dfqvmslatq tvfeyanlva papfyaieif sitggmvhss iglgaqtrav
       61 dspgladtwm vtgvnkplei gpcdstlefv rnaaqqarrv agvctgafvl aqagvldgrr
      121 atthwayapa lqrlhpqisv egdrifitdg slwtsagmta gldlalsmve qdlgadiars
      181 vahrlvmhqr raggqsqhsq mldlapksdr iqnalnyarq hlhrplsvee laeavhlspr
      241 qftrvftaet gqspakaver lrleaarvmv eqsrhsldvi aretgfrdrr hmrevflrgf
      301 gvppqairrd vrgvnsalg
//
LOCUS       WP_010567217             172 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Pseudomonas].
ACCESSION   WP_010567217
VERSION     WP_010567217.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..172
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /note="This protein belongs to a clade of uncharacterized
                     proteins related to peroxidases such as the
                     alkylhydroperoxidase AhpD."
                     /calculated_mol_wt=17457
     Region          40..172
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtrlaaltle qapagsraal eglqkglgfi pnafktlaha paalngylal aqalgkssls
       61 gaerevaala tsevngcdyc iaahsffgak aglseedirq arsgslsava alarqitesr
      121 gqlsdaqiaa aheaglsdsk ivevvaqvtl ltltnylnnl agtaidfpps ah
//
LOCUS       WP_010567223             290 aa            linear   BCT 01-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Pseudomonas
            extremaustralis].
ACCESSION   WP_010567223
VERSION     WP_010567223.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..290
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31698
     Region          1..253
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mieqaqieqf qrdgflmveg vlsldevaal qhdfdqwvee srghdqgwgs tvdgrarfdl
       61 egdhrpdhps lrrvssptei spayervalh srmaaiaaql vgssgarfhh skinsklpht
      121 atqvkwhqdf lftphsnddi vtallmvsev tpqngplnvi pgshkgplws hwqaqrftga
      181 vddsvveqhc qqpvacygpp gsvcfmhtrl lhasspnete lprtlfigvy aaedalpfge
      241 nplpsahagl lvageesgli rstdnqlrlp qkprgasffv qqagqdsata
//
LOCUS       WP_010567226             225 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF1028 domain-containing protein [Pseudomonas].
ACCESSION   WP_010567226
VERSION     WP_010567226.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..225
                     /product="DUF1028 domain-containing protein"
                     /calculated_mol_wt=23369
     Region          2..211
                     /region_name="COG3342"
                     /note="Uncharacterized conserved protein, Ntn-hydrolase
                     superfamily [General function prediction only]"
                     /db_xref="CDD:442571"
ORIGIN      
        1 mtfsvvarca etgqlgiais sssiavgarc pwlrpgvgav asqnitlpsl gpqvldlleq
       61 glapgealas vfagqehgdy rqvtvidhlg rtahfsgaht lgvhgalsge qcvaagnmla
      121 dpgvidamvr afeqaaghla drllaamqag qaqggeagpv hsaallvvdd vlwpivnlrv
      181 dwadedpiga lerlwqayhp qlqdyidral nphiapgyav pgddr
//
LOCUS       WP_010567252             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas].
ACCESSION   WP_010567252
VERSION     WP_010567252.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12134272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..190
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21623
     Region          11..151
                     /region_name="Acetyltransf_3"
                     /note="Acetyltransferase (GNAT) domain; pfam13302"
                     /db_xref="CDD:379112"
ORIGIN      
        1 messptlits rliltplqls daadiqrlfp hweivrfldi nvpwpyppdg altyvrdral
       61 paiaagrewh wmirmaddps nsigsiclyd qpgnnrgfwl apqwqgkgyi geacevinay
      121 wfetlgravm qvpkaagnqa srkvseregm rlvdtqqghf vsgsllkeiw emtqeqwlkr
      181 kanlqsrrld
//
LOCUS       WP_010566663             559 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Pseudomonas].
ACCESSION   WP_010566663
VERSION     WP_010566663.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Gournas,C., Athanasopoulos,A. and Sophianopoulou,V.
  TITLE     On the Evolution of Specificity in Members of the Yeast Amino Acid
            Transporter Family as Parts of Specific Metabolic Pathways
  JOURNAL   Int J Mol Sci 19 (5), 1398 (2018)
   PUBMED   29738448
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Vangelatos,I., Vlachakis,D., Sophianopoulou,V. and Diallinas,G.
  TITLE     Modelling and mutational evidence identify the substrate binding
            site and functional elements in APC amino acid transporters
  JOURNAL   Mol Membr Biol 26 (5), 356-370 (2009)
   PUBMED   19670073
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..559
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59493
     Region          23..474
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; pfam13520"
                     /db_xref="CDD:404414"
ORIGIN      
        1 meattfeavp qaassvgslh rkidwrgafw vasgvpalvl fsigaiaatv gkpawivwiv
       61 silfgfiqaf tyaeiaglfp hksggasvyg avawvryskl iapvsvwcnw lawspvlsig
      121 sglaagyilt alfpadalin twqltlldlg wvktglslri natfaigmli lltvfavqhg
      181 gilrsarltl vlgvtslipl llvgvvplft gdaaqanflp lyplahdaag qvidgpwnis
      241 gwslmagglf maawstygfe tavcytrefk dpkrdtfkai fyagllcilv ftlvplafqg
      301 slglgqlvtp avldasgavv tpavysglls paiysgmgvg qamadsiggg kvvanivlim
      361 lvlatllaim tsmsgssrtl yqasvdgwlp kylgrtnehg aptaamwtdl sfnlllllms
      421 dyvfvlaasn vsyiifnfln lnagwihrld rpdwvrpyka ptvllaaggv lsfvnlacmg
      481 lgadiwgagt lvtglllall ilpvfcyrhy vqdkgrfpaa mlsdlhiqdd dgqrragwlp
      541 yatliagvlv vyachqlva
//
LOCUS       WP_010567277             223 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pseudomonas extremaustralis].
ACCESSION   WP_010567277
VERSION     WP_010567277.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..223
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24286
     Region          27..220
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mrnqrfsdvi rephtglffr kggntvapkg rlillhgvgs neanlaplad alpealevll
       61 lrgplqigpq gfawyqvnft sagpsfnqeq aeasrqllsr fidalpampt viagfsqggi
      121 msasvgltep eqvagfalls grmlreleph iasaerlnsv rafiahghqd nvlpiawahe
      181 adawltrlgv dhethfypmg heivaqelad fsqwltdtlp lrp
//
LOCUS       WP_010567310             695 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudomonas extremaustralis].
ACCESSION   WP_010567310
VERSION     WP_010567310.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..695
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78193
     Region          50..679
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mpafttlpra kalpvspskw slltcglfal tplpcalaet akvedstltl gtvtvqgssa
       61 ssgplstssv lssvdilgad ilekmpvnys welfsrapgv iltefnqgtt sgkisfrgfn
      121 gegevnavkl lidgipsnsn dgnmpfmdmi fpmeldsiev vrgtsdaryg lnniagnvnm
      181 ltrtggdytk arirygsynt qetqlakgie tsnwtqnyff ayqksdgyrd haeadkfsls
      241 gkwfytpddn syrigliarh yeteaqepgy lseedahqhp smtnsynatd kgtrrmnqvs
      301 vhfdtdladt lawsaktyvn tfddrrwtqy wrtssqqerd ayetqygalt sltwrpqvsw
      361 lydfalegga dmqqqqnkse ryrtkdrvrl aqtrdqqfdf dtygayvqae ikpfeslkiv
      421 payrvdkiqg dftnemtgmd ydindyglik qpklsvvysp wkvasiyanw grtfqvgtga
      481 aaykipprdt dlapsinegw etgvkftpan widgrvaywq qeasgevsrr lndpsgesdn
      541 vgetrrwgyd aqvnlhpndr tdiwmayswq yskilqpsat lpnskgqeid hiphhlynag
      601 vsykatrdlq ltawmngqtn yylerentkg tyggyvlmnl gatyqvtesv svdlqlknlt
      661 nryyeyvwyd pdgaqaslhs pgdgralytg vtldf
//
LOCUS       WP_010567340             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Pseudomonas].
ACCESSION   WP_010567340
VERSION     WP_010567340.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..161
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=17124
     Region          11..153
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 miepgiykdv mssfpsgvtv vttldpdggi vgitasafsa lsidpalvlf cpnyasdtyp
       61 ilrdskrfai hllsadqtae ayafaskgke kakgiewhls elgnpllaka taiiecelwr
      121 eydggdhaii vgavknlilp eqpvtpmiyh kgklgplptl a
//
LOCUS       WP_010567347             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010567347
VERSION     WP_010567347.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 305)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 305)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 305)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..305
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32711
     Region          60..294
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mkmtattptg salgaagavs rnagapslaq rwrgagnlip allflglffl apliglllrg
       61 vlepvpglgn yeqlfansay arvllntfsv aglvtlfsll lgfplawait lvprgwgrwi
      121 lnivllsmwt sllartyswl vllqasgvin kalmamgiid qplemvhnlt gvvigmsyim
      181 ipfivlplqa tmqaidpmil qagsicgasp wtnffrvflp lcrpglfsgg lmvfvmslgy
      241 yvtpallgga qnmmlpefii qqvqsflnwg lasagaalli fitlvlfyfy lklqpespvg
      301 asnar
//
LOCUS       WP_010567349             384 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010567349
VERSION     WP_010567349.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..384
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41587
     Region          14..371
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msaviqdavq npgqtlvslr nlnkfygefa avdnisldik dgefltflgs sgsgksttls
       61 mlagfetpss geilvggqsl vnvpphkrdi gmvfqryslf phlsvrdnia fplairklas
      121 aerekrvdam lklvqleqfa hrrpsqlsgg qqqrvaiara lvyeprillm deplgaldkk
      181 lredlqdelr qlhrrlgiti vyvthdqeea mrlsqriaif shgkivglgs gfdlyqnppn
      241 afvasflgns nflklkaqgn aaaafegqsl sirltsglrs eqdvllmvrp ekalalsveq
      301 aaeqplaagw nevsaivgev lflgesqtcs vktlggtsmt vkalsaagmp lktgdpvrvr
      361 watadacvyt ewaesdlnka agah
//
LOCUS       WP_010567359             539 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudomonas extremaustralis].
ACCESSION   WP_010567359
VERSION     WP_010567359.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..539
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=57905
     Region          1..539
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mtqlttaqri vigfaiapla lvglvfyalh dlatlkqqse qivqqdwpki apimviatgv
       61 rdngrntrdl lidpdsqqtq eaigttrqri tqafatlepl fdtaegkaay arlkthrety
      121 vaaftqvqal ikqgareqgl aqlkqqvvpa elevfkslda lmamqgrlfv ereqaaqtly
      181 dqarrtmigl lllcvalvva aavivtrsvt rplggepdev arvlshiaqg dltidvplgn
      241 saegsvmrnl hqmrqnlnqm vrqiaasvdg vassseelsa vssqtssslq sqgqeieqaa
      301 tavnemtaav devarnavst seasrlseqt aqrgraqvqe tvasintlat gvvetseriq
      361 qlagrvqdis gvldvirsia dqtnllalna aieaaragda grgfavvade vralahrtqt
      421 stqeieqmig nirqdsehav aamhtssdrv qatlgvaqrs gealdeitrs isqinernlm
      481 iasateeqal varevdrnlv girnlsqqvl qgalhtetag hdlagmagel hqtvarfkv
//
LOCUS       WP_010567417             776 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudomonas extremaustralis].
ACCESSION   WP_010567417
VERSION     WP_010567417.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..776
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83303
     Region          28..748
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mhqtlkrmfl csaciylpiv ahaqemelpt iqvigsspva gdsidrdkvp tntqslvadd
       61 fdrnksasvl dtlsqqtpgl qisdvqgnpf sqdinlhgfr asatqgtpqg lavylngvri
      121 neafgdtvnf dlvpsvaidr advwtsnpvf glnalggain lqlkngftyd gleaevtggs
      181 fgrigsslqy gaqkdnwafy tsgeeihedg wrdhsssrik rfytdlgykd dvrefhlnls
      241 aasntlgvig ptpveelarr yssvytfpqt tennmlmvgl ngkvslnddw avqsnlyvrh
      301 fdqkhvdgnt sdvaacagdp tqlclgdava qnagsgqnls ssllpgtgln qgiagsidrt
      361 hvnsdtvgas lqttydgsfl tlnnhfvaga nidysslsfs gsnelgtiad ttidpyvvgs
      421 gityqtsdgl iqpvklrakn tyqglfssdt ldltdrlsat lgarlniaqi nlsdalgnsp
      481 eltgdhryar lnplagltyk ltpdmsiygg yseanraptp lelgcanpak pcllegflvs
      541 dptlkqvvsr tyetglrghs tvnadstidw klsafrtdns ddivsqpssv vpgygyyvna
      601 gktrrqglda yvqyrtsdws ayttlayvda tyqsnltlts annpeadang niavargdki
      661 pgispwqlkm ggdykltsal tlgadmlans sqyyvgddsn hnaklagyav fnvhsdyqlt
      721 ktiklfakvd naldrkyaty gtfaavgdip slglsnpqti tpaapramya gfnvkf
//
LOCUS       WP_010567423             434 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Pseudomonas].
ACCESSION   WP_010567423
VERSION     WP_010567423.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..434
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45154
     Region          21..433
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 msialvgigf almlllmfls ipvavsiitv galggyllfg pplvdmmggv lwtslnnpsm
       61 laiplfmllg elllrggmad rmyealavwm grlpggllha niascalfsa tsgssvataa
      121 tvgtialpal sarnypvrps lgslaaggtl gilippsvnm lvygslanvs vgqlftagvi
      181 pglllslcfs lyiflahgka gthapqtpai plrvklamlk hlvapliifg vvmgsiyggl
      241 atptesaalg liialvlvai ngklstdlli scsmqaaktt gmviivlaca lmlnvtmamv
      301 glaqtvtewv atlgmnqlsl llllivfylv lgmfmdamsm lvltvpiavp mvmavgvdpi
      361 wfgifivlmc eialihpplg mnlfvvhgvr kdggsfndvi mgslpyvfvm igftlltmaf
      421 pvivtwlpnl magq
//
LOCUS       WP_010567446             171 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010567446
VERSION     WP_010567446.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..171
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17682
     Region          <43..169
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(48,50,54..55,58..60,62..63,67,70,79,81,83,87..88,
                     91..93,95..96,100,103,112,114,116,120..121,124..126,
                     128..129,133,136,145)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          48..79
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          81..112
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          114..145
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msdhpkrmse deaaefaeqv fdvarkgdaa mlaallakgl panlrnhngd tllmlsayhg
       61 hadavkvlle fkadpliand knqlpiagaa fkgnlpvvka liaggtpvda assdgrtalm
      121 maamfnrvdm vdyllgqgan pkatdaqgat alaaaqtmga rdtaaqlekl v
//
LOCUS       WP_010567449             695 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LTA synthase family protein [Pseudomonas].
ACCESSION   WP_010567449
VERSION     WP_010567449.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..695
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=77305
     Region          33..680
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 manpdalsqq rasnrllqpt vkshlaytll calvmmvmfs llrlallvyn remildtpas
       61 tfleafangl rldlrlvvyl ivplllalfs vramaargff rfwltvassi alflglmemd
      121 fyrefhqrln glvfqyvked pktvmsmlwy gfpvvrylla wavgtvilsm afkgadratr
      181 prgpfsggsi gtrqvapwys riavfvvcll vavtaargtl rqgpplrwgd vyttdsnfan
      241 qlglngtlsl iaaaksrfse ersniwkatl dqplatqtvr dmlvlpqekl vdtdiaavrr
      301 dytppaektl piknvvvill esfaghsvga lgrpgnvtpf fdnlskegll fdrffsngth
      361 thqgmfatma cfpnlpgfey lmqtpegshk lsglpqllsa rkfndvyvyn gdfawdnqsg
      421 ffsnqgmtnf igrndfvdpv fsdptwgvsd qdmfnrglee lkareggkpf yallqtlsnh
      481 tpyalptplp vekvtdrgsl nehltamrys dwalgqffek arkepyfket lfvivgdhgf
      541 gneqqitemd lgrfnvpmlm iapgiqekfg ardhtvgtqi divptimgrl ggetlhqcwg
      601 rdllnlpegd kgfgvikpsg ndqtvalvtg drvlvlpkem ppklwqyelg aeptgklite
      661 spdesmlkqk lesflqtatk slldntagvv ngkpd
//
LOCUS       WP_010567489             662 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-1,4-glucan--maltose-1-phosphate maltosyltransferase
            [Pseudomonas extremaustralis].
ACCESSION   WP_010567489
VERSION     WP_010567489.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 662)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10571012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..662
                     /product="alpha-1,4-glucan--maltose-1-phosphate
                     maltosyltransferase"
                     /EC_number="2.4.99.16"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009313 - oligosaccharide catabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0030979 - alpha-glucan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=75154
     Region          22..204
                     /region_name="GlgE_dom_N_S"
                     /note="Alpha-1,4-glucan:maltose-1-phosphate
                     maltosyltransferase, domain N/S; pfam11896"
                     /db_xref="CDD:463388"
     Region          209..563
                     /region_name="AmyAc_GlgE_like"
                     /note="Alpha amylase catalytic domain found in GlgE-like
                     proteins; cd11344"
                     /db_xref="CDD:200482"
     Site            order(262,266,277,279,322,354..355,357..358,392,394..395,
                     423,481,534..535)
                     /site_type="active"
                     /db_xref="CDD:200482"
     Site            order(340..342,349..351,364,397..400,402,405,427,429..430,
                     433,437)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200482"
     Site            order(394,423,481)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200482"
     Site            order(426..428,445,448..449)
                     /site_type="other"
                     /note="acceptor binding site [chemical binding]"
                     /db_xref="CDD:200482"
ORIGIN      
        1 mtaetrvpee sklplsqall lpriaiestt pvidggefav kavvgqrisv tskvfadghd
       61 klavmirwrp lqdeswhsvv mndvgndgwe gaftvnvqgp heycieawid tfasfcyelr
      121 kkheagapvs lelqegrnlv lqaaersdne lrdrlmmlyh alsglleteq valflhedsa
      181 ylmtqadhra ylsistvypi dvereaaqfa swyelfprsi sdhparhgsf ndvhtrlsmi
      241 hdmgfdvlyf ppihpigrsh rkgrnnalta gpddpgspya igseegghea ihpqlgsrdd
      301 frrlvkaaae hgleialdfa iqcsqdhpwl kehpgwfnwr pdgtikyaen ppkkyqdivn
      361 vdfyaaeaip slwtelrdiv vgwveegvyt frvdnphtkp lpfwqwlisd vrakypdvif
      421 laeafttpam marlgkvgys qsytyftwrn tkaelaqylt qlnaspwrec yrpnffvntp
      481 dinpaflhds grpgfliraa latmgsglwg mysgfelcea apvpgkeeyl dsekyeirpr
      541 dftapgniia eiaqlnrirr qnpalqthlg lklynawndn ilyfgkrsed gsnfvlvavn
      601 ldpfnaqeaf felplwelgl pddaqtqged lmnghrwiws gktqwtrlep qmpfgiwrit
      661 tp
//
LOCUS       WP_010567543             215 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Pseudomonas].
ACCESSION   WP_010567543
VERSION     WP_010567543.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..215
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23285
     Region          8..185
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mnmnllhdit fyvmyaamai aifitiergi yfayvrrqar altevlgahv hserdlpesl
       61 srrdslplnm vmpvlaqkas qgsrkdlddv ietqylttra plarslwiie tittaapllg
      121 llgtilgiid tfkalasagv sdpgqisggi gtalfatglg iaialfcvvf hnffqdsler
      181 indqlkilli raatgarvqg evphlvstpl hsrta
//
LOCUS       WP_010567571             413 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thiolase family protein [Pseudomonas].
ACCESSION   WP_010567571
VERSION     WP_010567571.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 413)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..413
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43648
     Region          12..409
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mkrigqysaf adaaifeavr tpwvdlggal sqvspidlgi kvgrevlara gidplavdsv
       61 lagsmaqasf dayllprhig lysgvaqsvp algvqricat gfellrqaae qlrdeaqlvl
      121 cvasesmsrn piaaythrdg frlggavqfk dflwealydp apaldmiata dnlarrhgls
      181 reavdryard shqralqaqr dgawvdeivt vdnqvfeleg yrprgislar radavtedsh
      241 prsttlaala rlravhpdgv qtagnscavv dgaaaalvgr asactrpala rllasavvgv
      301 apefmgigpv pairlllqrs glslddigrf eineaqaaqv lavvqeleld sgrlnvqggs
      361 lglghplaat gvrlvmtlar qlrahnlryg iaaacvgggq gmallienpa yra
//
LOCUS       WP_010567600             230 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010567600
VERSION     WP_010567600.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..230
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24524
     Region          1..211
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mlrikglnvq rgngsqahcv qlpelalarg qivaitgesg cgkstlleai glllapvsva
       61 qfslagrdva alleaddqps ladmrarslg fvlqnggllp flnirdninl prrllgldsq
      121 ssfvdnaisa lsleplldkl pqalsigerq raacvraiah qpaliladep taaldphnar
      181 llfelllslv eqsglcaliv shdwelvrsf dlprliavsr pgethfeasr
//
LOCUS       WP_010567601             658 aa            linear   BCT 01-JAN-2025
DEFINITION  vWA domain-containing protein [Pseudomonas extremaustralis].
ACCESSION   WP_010567601
VERSION     WP_010567601.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 658)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10076759
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..658
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=71090
     Region          232..394
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cd00198"
                     /db_xref="CDD:238119"
     Site            order(239,326,354)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238119"
ORIGIN      
        1 mtllkltlaa clclssgwal aadkpllqeg kktlfqrvlt tpgchlspaa gappgaeqpp
       61 fsrfyvyeha kagnadwiev gpdsfgktsg wlpaactvdw kmqltlaftn panrdrlmff
      121 kergtlegil dapdpvsvia plraklkqna papgvlaqep eyfidmqkqf yllpvlsgee
      181 vmteggfrtr ilnvasvska daalvqstqa gatatssqag idaasqlkef saavvfvids
      241 tismdpyier treaiskvya qiakenlgrq vkfglvafrs stqavpgley vtkmyadpnt
      301 vkdgadfmak vadlkqakvs sksfdedsya gvmqaidkvd wkpfgaryvv litdagalda
      361 ddklsktgln aeqvrieasn pgvaiytlhl ktsagskdha kaeaqyqvls tfsgtntsly
      421 ypvdagdina fgskvdalat aitgqvkaay mgedaigsam nakappaeqk lvddaaligh
      481 amrlaylgek tgsqappvfq awiadrdpik qnvpttdvrv lltksqlsdl sdvlkkilda
      541 anegmispsd mferlrsvaa tmgtdpnqlk qngtaklsel gvlgeylddl pyhsevlnld
      601 eetwkswdgl aqekfirtls tklrhyqiyn advdrwvsla dgsdarenvy pvplemmp
//
LOCUS       WP_010567620             236 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010567620
VERSION     WP_010567620.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..236
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=26369
     Region          11..236
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mtlenfaqwl idvdllqryg prmlegllvt gklvaisftl gallgllial arvsnnlllq
       61 rssalyvycf rgspllaqlf llyyglgsfk gfwqdvglww ffrdawfctl laftlntaay
      121 qaeifrgsll svsqgqheaa kalslkrstt ffkvilpqsl lvaigplgne lilmvkasai
      181 aslvtiydlm gvtklafsrs ldfqvylwaa vlylliveii rrvlkrvear lgrhlp
//
LOCUS       WP_010567621             239 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudomonas extremaustralis].
ACCESSION   WP_010567621
VERSION     WP_010567621.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..239
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25831
     Region          49..237
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 miehlsllsf asggwgqall agalvtlala laclpvglpl glglalaars kkpwlrsfat
       61 lfstvfrglp elltlliiyy gcqigaqkil aamgyetqvt intflaamva fsfvfaafss
      121 eiwlgafktv hkgqyeasaa lglskattfr kvvfpqlvri alpglsnnwl sllkdtslvs
      181 tislvdlmrq tnlavsvtke plffyavacf gylffsalsg rafawierhf srhlrsaqp
//
LOCUS       WP_010567643             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010567643
VERSION     WP_010567643.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34043
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mlrfddlqlf vraadlgsls aaarvmdlsp avasaalkri eqqlgarlla rstrslrlta
       61 egegfleyar aalgsldegr rllasgqdhv sgvlqlsaps dfgrnqllpw ldefqrdypq
      121 lsvrlllgdr iadlfrqpvd ialrygeped sslialpvap qnvrvlcaap sylarhgepr
      181 hleqlaqhnc llymlgsrvh dhwsfhdgkr dvsltvsgdr fsddadvvrr wavagvgiay
      241 kswldvstdv lagrlrvilp elrgertpln llcahraqls kpinllreml vsrcatltaq
      301 wpdrvsst
//
LOCUS       WP_010567683             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carbon-nitrogen hydrolase family protein
            [Pseudomonas].
ACCESSION   WP_010567683
VERSION     WP_010567683.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..282
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30413
     Region          4..269
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(40,98,115,119,132,157..158,160..161,182)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(40,115,157)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(116..117,138..140,158,161..165,167..168,190..191,
                     194..195,197..199,201..202,232,262..263,266..267,269)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 msfaviqmvs qsdvlanlaq arrlleraaa ggaklavlpe nfaamgrrdv adigraealg
       61 egpilpwlkq tardltlwiv agtlplppkd hpnakpnacs lliddqgeiv arydklhlfd
      121 vdvadargry resddyafgs dvvvaqtpvg rlgltvcydl rfpelyselr aagaelisap
      181 saftavtgaa hwdvlirara ietqcyllaa aqggvhpgpr etfghgaivd pwgrilaqqd
      241 qgeavllaer dsseqasira rmpvvnhrrf fsqgaqrpas er
//
LOCUS       WP_010567720             430 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [Pseudomonas].
ACCESSION   WP_010567720
VERSION     WP_010567720.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 430)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 430)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..430
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47900
     Region          1..403
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mltniiikgf ksyreqrlpl spltlmigan asgksnalea frflcwlgqg qklsvlrhrv
       61 deseqilrgq ikdlpyhqgr sftlgcetdd ldwnslsvei alredelhiv hesissplqk
      121 fplyrieqss sglstdvrva ynnfstggkk pqitctdqia ilnqlassal fdsghkkaqk
      181 vipqttehfq yllantlfld pvpalmrgds ypdkklrgdc snlsgvlytl wqdeearpai
      241 iefikslpeq dvkdvnffed rrgrvslelv enfgsvernw svellsdgtl rvlaiaaall
      301 sapaestlvi eevdngvhps rarqllktmr eqaelrgvrl llsthnpalm dalpdsalgd
      361 vvfcyrdpqd gdsrlvrlad lqdyaglvsq gplgelvtng ivdrfvkspv tvtqkrqnal
      421 nwlrkmqgea
//
LOCUS       WP_010567822             364 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010567822
VERSION     WP_010567822.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..364
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40516
     Region          2..360
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 msltlehvsl vasgqtwidd anlrfeagsf nvllgrtlsg ktslmrlmag ldkpdsgril
       61 mngvdvtqkp vrlrnvsmvy qqfinyptmt vfeniasplr qagvsnelih skvletakml
      121 riekflqrhp lelsggqqqr tamaralvkd aelilfdepl vnldyklree lrqemrelfa
      181 arhtiaiyat tepnealalg gtttilhegr viqsgkaaev yhqpqtvlaa elfseppinl
      241 mpgrisgnev sfanfvhfpl nvdlrpigeg efrfgvrpsh islvpsnddd lelavtveva
      301 eisgsetflh vrsehfllvl hlpgvheydv dapirvyipt hklfvfdgqd rlvqapgrrv
      361 arva
//
LOCUS       WP_010567916             801 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA translocase FtsK [Pseudomonas].
ACCESSION   WP_010567916
VERSION     WP_010567916.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12144184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..801
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=87609
     Region          22..194
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <303..796
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mkkttatpkt vvpawrqhlh yrlkegalia igalclflmm alltygkddp gwshnskied
       61 vqnfggpags ysadilfmvl gyfayifpll laiktwqifr qrhepwlwsg wlfswrligl
      121 vflvlsgaal ahihfhaptg lpagaggalg eslgdlarkt lniqgstlmf ialflfgltv
      181 ftdlswfkvm dvtgkitldl lelfqgaanr wwaarverkr mvaqlrevdt rvnevvapst
      241 pdrreqakvk erliereqal skhmserekq vppviapapp kpaepshrvq kekqvplfvd
      301 savegtlppi sildpaekkq lnyspeslaa vghlleiklk efgvevsvds ihpgpvitry
      361 eiqpaagvkv srisnlakdl arslavtsvr vvevipgktt vgieipnedr qivrfsevls
      421 tpeydnfksp vtlalghdig gkpvitdlak mphllvagtt gsgksvgvna milsilfksg
      481 pedaklimid pkmlelsiye giphllcpvv tdmkdaanal rwsvaemerr yklmakmgvr
      541 nlsgfnakvk eaqdagtplt dplykresih deaplltklp tivvvvdefa dmmmivgkkv
      601 eeliariaqk araagihlil atqrpsvdvi tglikanipt rmafqvsski dsrtiidqgg
      661 aeqllghgdm lymppgtslp irvhgafvsd devhrvveaw klrgapeynd dilagveeag
      721 sgfdggssgg dddaetdaly deavafvles rrasisavqr klkigynraa rmieamenag
      781 vvtamntngs reviapgqmr d
//
LOCUS       WP_010567977             288 aa            linear   BCT 01-JAN-2025
DEFINITION  pirin family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010567977
VERSION     WP_010567977.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..288
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31075
     Region          12..278
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkkligiyts prahwvgdgf pvrtlfsyds mgkhispfll ldhagpadft pteqrrgvgq
       61 hphrgfetvt ivydgevehr dstgaggtig pgdvqwmtaa kgilheefhs qafarsggvl
      121 emvqlwvnlp akdkmadagy qtivdgdipv lalangaghl rliagefagt qgpartftpi
      181 dvwdlrlnag kpvtldlhag rntalvilrg tvrvngedva rpgqlalfer dgsqltless
      241 ddakvlllsg epidepivgh gpfvmnteqe ihqafadfqs gqfgrmhd
//
LOCUS       WP_010567563             760 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Pseudomonas
            extremaustralis].
ACCESSION   WP_010567563
VERSION     WP_010567563.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 760)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 760)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 760)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 760)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   6  (residues 1 to 760)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   7  (residues 1 to 760)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11706914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..760
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81705
     Region          30..607
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Site            order(307..311,460..461,488,505..506,509..510)
                     /site_type="active"
                     /db_xref="CDD:319763"
     Region          625..754
                     /region_name="Hr-like"
                     /note="Hemerythrin-like domain; cd12108"
                     /db_xref="CDD:213983"
ORIGIN      
        1 mlakwldpll llltaltlla ggialvgqkp ewasvcwaag slvmcavlli eivrrlarre
       61 agvdlialls itaallfgqa lvsavialml atgrtlefft kqradrelra lidraprfaw
      121 lqeadglrkv pveqvelnqt vlvrlgevip vdgrllspaa tldesalsge slpvtrrege
      181 qlhsgvsnvg apilliatrt aaqstyagiv qmaeaarrsr apfvrladry avffipltll
      241 iaglawhlsg dplralavlv vatpcplila vpiafmsgis raarrgilik dgttlealag
      301 vkqvfldktg tltsgharlq sievnglsdp qrllglaasl aqasthpicq aiveaahqrr
      361 lplsvpqvve espgsglcgr vdgqqvrfgt lsfahegaaa tdwvaamlrh mdylacsgsf
      421 idvdgklvgl lvfsdnvrre tpqtlrrlrn rgiekivmlt gdrletaemi alsagidelr
      481 agltpedkvr avqqaglhas tlmvgdgind apalaaanvg vamgasgata saqaagvvll
      541 vdrldrlvea ldiarrtrsi arqgvlagmg msllamgvaa lgylppliga mvqegidvvi
      601 ilsalraqgp lwkqrkqqlt aeyidrlqhe heqlaavlnd lhqmandfaq rplaqaqtdl
      661 valvdklqts laqheheden tlypvltrsm pgedpmstms hahreifgli hllarmssdf
      721 saapatapad eiqhqlirld tlvrlhfdqe eelfhyldwr
//
LOCUS       WP_010568062             318 aa            linear   BCT 01-JAN-2025
DEFINITION  RHS repeat domain-containing protein, partial [Pseudomonas
            extremaustralis].
ACCESSION   WP_010568062
VERSION     WP_010568062.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         <1..318
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          <39..161
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 ehhadrhrsy lyepdsfrpl allegfgpdk ttpyhyqldh lgtpqeltaa dgeivwsahy
       61 raygeiarld sgkidnplrf qgqyfdqesg lhynrhryyn pdigryltpd pvklaggina
      121 yqyvpnptgw vdplglsscp gadgckptat arkpaesvdh gepalpqltr aerqaridkl
      181 aeanayrrld elekatpgah flekhgaqtt lesqlervkt aknpttgave vytsgpkkgk
      241 lkyppaathy lshkdqlnsi yraqlifrqn drfaslkpmd mgkiigegys rdgkysqqrk
      301 arvilnkdgk pktaytel
//
LOCUS       WP_010568227             420 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Leptospira broomii].
ACCESSION   WP_010568227
VERSION     WP_010568227.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..420
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=48594
     Region          1..>197
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mkfidlfagl ggfhialtkl ghdcvfacei deelrniysd nfgirpegdi rkinlksipk
       61 hdilcagfpc qpfskagfqk gfncpdygdl feyvykiikf hnpkfvflen vpnivkhnng
      121 ktwktivdkl enigyninhn vlsphfygip qirervyiic tkkyipsfsw pghkktkdls
      181 iksildtdpq nykplsknki qcinawqill dklpkdieii spmwamefga nypfeeytps
      241 kigfsklknf kgsfgkslkt vnennissli ptyaltkedk fpkwkiefik rnrefykqnk
      301 svidhwlhli kefppsfqkf ewnckgekri iwnnliqfra sgvrvkrpvt spalismttq
      361 qlpiigwqkr hmtfeeclkl qslnklkylp esntgkfrav gnavnanive iiaksvfsqi
//
LOCUS       WP_010568268             193 aa            linear   BCT 01-JAN-2025
DEFINITION  lytic transglycosylase domain-containing protein [Leptospira
            broomii].
ACCESSION   WP_010568268
VERSION     WP_010568268.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..193
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21017
     Region          <77..192
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mkltdlpafq silsrmeeir gipdkfihkt denrtdvvpp tstqesfsdi lnsklsdiep
       61 arnvrgdldt lglsgfiqqe sarngldpnl vksvikaesd fkpnaisrkg aiglmqlmpg
      121 taemlgvedp fdpaenisgg tkflgdlvkr fgdtdlaiaa ynagpgavek hkgippfket
      181 kdyvkkvnrf wkg
//
LOCUS       WP_010568107             297 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas
            extremaustralis].
ACCESSION   WP_010568107
VERSION     WP_010568107.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..297
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32620
     Region          31..184
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <182..297
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mlltrhldan aplvslierl tprdgfspth lpgvqvlras cdvargpqiy epslmfvaqg
       61 skvaylgprt leygaghyli qampvpfece tfamapgapl lgvtvgidrv vlgelvmamg
      121 mhagppptaq tlesmssvvl ddamrgcver llqclhdple srimgparvr ellftalrgp
      181 qadvlralve qqgqfsriat alnhlhahya eplnietlag yahmsastfh ehfkrctlls
      241 pvqylkrlrl lkaqqlllve gmgvaqaahr vgyqstsqfs reykryfern pgeeraa
//
LOCUS       WP_010568273             218 aa            linear   BCT 01-JAN-2025
DEFINITION  cysteine hydrolase family protein [Leptospira broomii].
ACCESSION   WP_010568273
VERSION     WP_010568273.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..218
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23848
     Region          32..204
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mnrilltslf lisfpsfvfa dkkptfdvrk tavlimdyqn aiisggylkt segvllkadk
       61 vlsearkfgl pviyivvgfr sgfpeispnn lmfnsikksg gfgqdpkllg ihpsvspkpe
      121 divitkhrvg aflgtdldmi lraneintiv mfgvatsgvv lstlrhasda dyksivlkdl
      181 cadkdpethq vlmekvfprq aeiissddfl ealtksak
//
LOCUS       WP_010568274             281 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Leptospira broomii].
ACCESSION   WP_010568274
VERSION     WP_010568274.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..281
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=31678
     Region          42..279
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mikkilistl avflillcqv gyvykqatgv pgnspvatle vpkdpgkriv vcmgdsithg
       61 rvsydyvngl asdtdlekfs fvnaginsrl aynllqkade vialkpdfit iligtndvka
      121 slsaeesery iklwrlsesp skklfvnslr klimrlrset nakialvslp plgevllskp
      181 ylrsteysde irkiaeaeri lylplheemd avlrskgqsn ipeyrmdlpa myvaiflhya
      241 mfqdwnsisd mrnlhfltdn ihlnqrggdi vqklikkfll e
//
LOCUS       WP_010568279             395 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Leptospira broomii].
ACCESSION   WP_010568279
VERSION     WP_010568279.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..395
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43618
     Region          8..382
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(18..19,22..23,26,58,109..110,112..114,117,137,
                     140..141,144,220,223..224,227..229,232,259,263,312..313,
                     317,321,337,340..341,344..345,348)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 mkaitksiwv lsfislftdi asemlypilp lylksigfsv lligilegfa eataglskgy
       61 fgnlsdasgr rvpfvqwgyf lsalskpmma lltfpvwifs artldrfgkg lrtgardall
      121 sdeatpetkg tvfgfhrsmd tlgavigpic aiiylhffpe dysslfywai ipgfiaviis
      181 rflkekkkvs tsptikptgf fsflnywkes pisyrrlsia llifalvnss dvfllmmvks
      241 kgftdlevia vyifynliya iasfpigils dkiglrrill lglglfsivy fgmafaekke
      301 lfyllffiyg iyaastegit kalitnitss ndsataigtf aglnslaall assfagflwy
      361 vfgaptvfiv sslvtilvll yltsvkiedm krkpq
//
LOCUS       WP_010568348             434 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Leptospira broomii].
ACCESSION   WP_010568348
VERSION     WP_010568348.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..434
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48200
     Region          8..399
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mplnrkskkk vvvigagfgg lqaikklsrd edlditvidk knhhlfqpll yqvatavlsp
       61 adiaiptrsl vgdkenvtvy lgevdkvdlk erkvyfqdhs enydflilaa gartsyfgnd
      121 hwkkyttglk nlkdaleirt klllsferae leenkeiaks llnyviiggg ptgvelagsi
      181 aelsheivrn efhtidpals kitlieaspr llmafhpnls efaktrlekr gvevlvgtkv
      241 inideegvhl dgctirssni iwaagvqana isqalgvpld rtgrvmvdey cnieghpevf
      301 vigdianftk nlerplpgvs pvamqqgrya aslifgdlkg kkrsifkyvd kgsmatigrq
      361 davaqvglwr lkgffgwaaw lfvhlfyqvg fknkvsilit wfwsyltfra earliqdevg
      421 sdgisnptak ekrs
//
LOCUS       WP_010568377             250 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Leptospira broomii].
ACCESSION   WP_010568377
VERSION     WP_010568377.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..250
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27278
     Region          1..249
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mivvsianqk ggegktttsl nlawglarrg kktliididp qanstgifln pdsleksmhn
       61 ifqakakvrd vmvpthvenl siapsrlala eaetvaaivd apyilrdala dlekdldfci
      121 idcppslsif tinalvasny viiplqaekf svdgilglqq tinsikkrin pgleilgalv
      181 tqlkpqtllt ktivpvltky frifensisd gvavgeshla kksvfeynka srqaqeyegf
      241 veeflnelkk
//
LOCUS       WP_010568411             165 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Leptospira broomii].
ACCESSION   WP_010568411
VERSION     WP_010568411.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..165
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=18880
     Region          62..165
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 manaevnqvk pkegnaehsr flepfqqfsr eidrsledlf mdfgnfklwa rptfmksglp
       61 kvnlkenkes yileaelpgy nskeveigik ghvltlkgek keshdekkee yhlhesvhgs
      121 fyrsfklpes vladkinasm kdgiltltlp kseeekgqtk kieik
//
LOCUS       WP_010568456             474 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Leptospira broomii].
ACCESSION   WP_010568456
VERSION     WP_010568456.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..474
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52115
     Region          6..460
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mlsklnskak eltngikagy asteigitav etlaqiylle fyvlvvglkp slfglamlva
       61 ilwdaisdpl mgtisdrtas kmgrrrpyii sgglllgvsv yflftpplie sqigkffyll
      121 gmyslvntfm tvlavphial ggelsferee rnkifgwrlf fanlgllsgl llpaifagtg
      181 sdlflsrsss smivgvvlvl tallafnvtk grdfrlenlq ikkspktgff hsfssvikng
      241 fflpllfafi iaalartlns sigllyykqr llledaqvvv rillpfvffl lvsipfwlfl
      301 akkygkkrps fwgslglgim tviayplfpi gsytapliaa fvggicagsi llfdslvadv
      361 vdydelitgd kkegayfgfw kmatkvvrav glaflgfile aigyregavt qapelgwrlt
      421 ilfgpvvgsf filsalvfar mplvdskhkr iqtllvrrra frtkmgtmre aarg
//
LOCUS       WP_010568467             476 aa            linear   BCT 01-JAN-2025
DEFINITION  UTP--glucose-1-phosphate uridylyltransferase [Leptospira broomii].
ACCESSION   WP_010568467
VERSION     WP_010568467.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10484167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..476
                     /product="UTP--glucose-1-phosphate uridylyltransferase"
                     /EC_number="2.7.7.9"
                     /GO_function="GO:0003983 - UTP:glucose-1-phosphate
                     uridylyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0005536 - D-glucose binding [Evidence
                     IEA]"
                     /GO_function="GO:0032557 - pyrimidine ribonucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006011 - UDP-alpha-D-glucose metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53279
     Region          39..436
                     /region_name="UDPGP"
                     /note="UTP--glucose-1-phosphate uridylyltransferase;
                     pfam01704"
                     /db_xref="CDD:460300"
ORIGIN      
        1 mdsmkaesea liqakmleag lsvefisdfl lkvdevrnge tgivkweevg dldsstdeis
       61 lesieskgrp npsvlnelvv iklngglgts mglsgpksli eikngmsfle ivarqiefir
      121 keyeievpll lmdsfstleq sraelkrigf sqsfptsflq hkvprllkss lkplevpgde
      181 neewcppghg diwftlletg ildsliekgy kvafvsngdn lgatvhpgil rymmeeelef
      241 cmemtpktla dkkggaifrr tvdgkklnyq lletaqvppn hmnefegvsk frsfstnnlw
      301 irldalkerl vsgkfslsli vnpkkidgke vlqletamgs aiqnfpkakg iiiprdrfap
      361 vkkcedylvr rsdaytlnsd fsitmteerk saglgevivq mddnyykkit dftsrmkalp
      421 slvrctslrv egdvlfdvpl eiegdvtitn pnplqkkvse lgknrisget irfrft
//
LOCUS       WP_010568470             218 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Leptospira broomii].
ACCESSION   WP_010568470
VERSION     WP_010568470.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..218
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24550
     Region          139..216
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mnarlltvrd silswyegtn lwdrclygsi lvhflcfgty yivthlkpge idsdrlefqd
       61 ievdiqeipp eliggenspa pvekeewveg sdkdgkdped ndidpnklsg dgtdkdgfly
      121 aymgdkpptp iidfdlrdyf pekaklqgis yadtilevrv dehgnlidak vlkagikgyg
      181 fedaairvvr aarwspgyvk grpikmnhri pvnfkldd
//
LOCUS       WP_010568583             266 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Leptospira
            broomii].
ACCESSION   WP_010568583
VERSION     WP_010568583.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..266
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=28747
     Region          146..257
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mtikpfdwki fvilliaatf gllaiipysl alqagvlkqt qlsmplpvlv tiqivaqvsi
       61 fgmiiaiglf fanrtgleip ileayfkgep irvkirsilp isgilgivas llialldvyl
      121 fqpalkvelg dkasvllnsg aatpaawkgf lasfygside eillrlclms ffvwcgrfls
      181 kkrskgkqsa tvfwianivt alvfglghlp atsmilpltp lvivraivln glagvafgyl
      241 yftrglesam lshfacdlvl hvvlvl
//
LOCUS       WP_010568593             287 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Leptospira broomii].
ACCESSION   WP_010568593
VERSION     WP_010568593.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..287
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31666
     Region          33..270
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mhdnklnpva dstavrvalw ralhmqvdsp pyvleddigl rlaapdegwr srpdmdpnft
       61 klfrasilar arfiedlvve esgkgvrqyv ilgagldtfa qrrpdlasdl rifevdqpsh
      121 qawkrqrlid lgygipewlr lvpvdfesgg swweglvaag fdanrpaivt sigvsmyltk
      181 eaivamlnqv atlalqstfv mtfllpfela dpnvrpglea aargaqasgt pfisfftpte
      241 mlslaresgf kevqhvsaaq ltqlyfanrt dglrppknge elliatt
//
LOCUS       WP_010568596             124 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Leptospira broomii].
ACCESSION   WP_010568596
VERSION     WP_010568596.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..124
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13796
     Region          11..98
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 makmkkiiyw tstiwlalgm lstgtvqvfk vktegdftan lgypvyflti lgvwkilgvi
       61 vlllpkfplv kewayagfff amsgaafshi asgtvkeifp slllllltvi swyfrpqdkk
      121 vilg
//
LOCUS       WP_010568624             437 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Leptospira broomii].
ACCESSION   WP_010568624
VERSION     WP_010568624.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..437
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48661
     Region          110..430
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrifilwllc vvmsgsvysq evsrssnssc agrmdlrrit icvleaspey rteqlklkei
       61 sgrkliasyl fpsnpvasay lahrkgttse ggplgtgpap iatnyqtlvt qeiyvggkre
      121 kaqqvadeey kvqagrleav rrnmlsrtis atlrysgfkr efegtkqlye vakdlrdlsa
      181 aranegvapa mdvdvaraee lrlwkllkqa erkmdsakge llillnlnpd asleleitgi
      241 alkelpndvv slvkialanr peigvsenei ilaarrleqt rlqripnlti ggfiqsdgfn
      301 ekvagaqvsl pltlwrtyeg eirsassvke qaqenariqe rnvrmeivna vssylalrte
      361 ieqydasylr dldkdldllk ealrtgrikv vdalnsqril tgaklnfils rteyalaqve
      421 lvraiglsfe dniqeik
//
LOCUS       WP_010568640             347 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Leptospira broomii].
ACCESSION   WP_010568640
VERSION     WP_010568640.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..347
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38882
     Region          30..283
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(30,33..35,38,57,59,90,109..112,218,220,222..223,225,
                     235..236,239,254..255,258)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(30,34,38,57,59,90,109..112,218,222..223,225,
                     235..236)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(33..35,218,220,223,236,239,254..255,258)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mkdvelkerl esylgnrlkg kveianmisl sggacqenfs aditvadgsd kglyqtvyrt
       61 dkgaallasl sridefkvcr mafeagvktp epfwlesdss vtgnpfyfmk risgkangrf
      121 ivkdpslnkt rkqltqelae nlakihsvtp eqckdaalkt vlasgqdlsd ktvaksstkn
      181 lrlqlegmne pypamemiln wleknplpsd kivlihgdfr tgnfmvtpeg lqgivdwefa
      241 hwgdrhedlt wlcmrdwrfg klnkeaggfa drkefyeaye kaagvvldsk kvtywevmgn
      301 lrwaigcigq aerhlsgkdk gielaaigrr acemeyeamr lieesls
//
LOCUS       WP_010568661             399 aa            linear   BCT 01-JAN-2025
DEFINITION  NHL repeat-containing protein [Leptospira broomii].
ACCESSION   WP_010568661
VERSION     WP_010568661.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chaudhuri,I., Soding,J. and Lupas,A.N.
  TITLE     Evolution of the beta-propeller fold
  JOURNAL   Proteins 71 (2), 795-803 (2008)
   PUBMED   17979191
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10146633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..399
                     /product="NHL repeat-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=40477
     Region          71..398
                     /region_name="NHL"
                     /note="NHL repeat unit of beta-propeller proteins;
                     cd05819"
                     /db_xref="CDD:271320"
     Region          80..130
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          138..188
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          196..236
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          252..305
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          314..355
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          364..398
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
ORIGIN      
        1 mnqfkplali lvaliialsc kprhdnkdnl lvallaasat qsnctttpvl tlgesatlvl
       61 gqsgftmsas gtaqnqfkqp sgiavdskgg qwisdatnnr vlhfpngvat ggnadvvlgq
      121 snftssgpgt tqstlttpqg lavdsngglw vvdsgnhrvl hfpsgvatgg nadlvigqan
      181 ytsgtnattq srlssphava idsaggiwis dggnnralhf psgiasggna dlvlgqsnyt
      241 sgtggvtaqn alndprglav dlnggiwive yannralhfp ngtasggnad rvlgqinyts
      301 sagqftrtqi slyqpqgiav dsnggiwvgd tgnlrvlhya ngvangggad kvlgqsdytn
      361 igktgptads vgaaavlals scgqlwvgdt tntrvlyfp
//
LOCUS       WP_010568731             146 aa            linear   BCT 01-JAN-2025
DEFINITION  arsenate reductase ArsC [Leptospira broomii].
ACCESSION   WP_010568731
VERSION     WP_010568731.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..146
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=16662
     Region          5..136
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(10,12..17,105,107)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mkkpnvlvlc tgnscrsqia egwlrvyakd kaviysagie thgvnpkail vmkeagidis
       61 khtsnhiney kdvefdyiit vcdhaqehcp yfpskaerfh qnfpdpakat gteedvlnkf
      121 rdvreqirky seefaqkhll yktnsf
//
LOCUS       WP_010568738             103 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Leptospira broomii].
ACCESSION   WP_010568738
VERSION     WP_010568738.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..103
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11891
     Region          19..60
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mksnpgnsky kfvakdfykl lelqnwkcyl tgrnlepent naehiiplrk ggehkfinic
       61 fvveplaklk rfyteeeiin laadiikfkg lkhgliisqk kkk
//
LOCUS       WP_010568804             412 aa            linear   BCT 01-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Leptospira broomii].
ACCESSION   WP_010568804
VERSION     WP_010568804.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..412
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45890
     Region          81..>316
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mklnhnfiis iliscvigcn pekikiggay qlgdippgil eveakedpfl nglkvemtdl
       61 pghddlifds ekklgyassm dgwiwkldwa rgkssqwlrp pvnpagmqys dsnknkilvc
      121 asrlggepye etdrvglyev eiatkklkpl vldlpkteke efekvytsse rrpillrdlt
      181 sansrpfslc ndlavsadgn riyitepfer paasmgsgav peaiglyphg klwmydrkte
      241 svslvlngft fvdgilleen psgmeesvif tetskfrilr afisgknegk sevlfenlpg
      301 ladglerdek griwtgiikr rsglinfvhg npwmksvllp lpqwilpisk ktgflvldtk
      361 aekalyyslh dgskirdisv avpfggrvyf psfdrssrgl yslavpelkl ae
//
LOCUS       WP_010568884             175 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cyclic nucleotide-binding domain-containing protein
            [Leptospira].
ACCESSION   WP_010568884
VERSION     WP_010568884.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Wang,Z., Jiang,Y., Lu,L., Huang,R., Hou,Q. and Shi,F.
  TITLE     Molecular mechanisms of cyclic nucleotide-gated ion channel gating
  JOURNAL   J Genet Genomics 34 (6), 477-485 (2007)
   PUBMED   17601606
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Kaupp,U.B. and Seifert,R.
  TITLE     Cyclic nucleotide-gated ion channels
  JOURNAL   Physiol Rev 82 (3), 769-824 (2002)
   PUBMED   12087135
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Canaves,J.M. and Taylor,S.S.
  TITLE     Classification and phylogenetic analysis of the cAMP-dependent
            protein kinase regulatory subunit family
  JOURNAL   J Mol Evol 54 (1), 17-29 (2002)
   PUBMED   11734894
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Aiba,H., Fujimoto,S. and Ozaki,N.
  TITLE     Molecular cloning and nucleotide sequencing of the gene for E. coli
            cAMP receptor protein
  JOURNAL   Nucleic Acids Res 10 (4), 1345-1361 (1982)
   PUBMED   6280140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10034975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..175
                     /product="cyclic nucleotide-binding domain-containing
                     protein"
                     /GO_function="GO:0030551 - cyclic nucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=19977
     Region          32..145
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(100..101,110..112)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(132..134,138..140)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
ORIGIN      
        1 mnplqlpiwk klfkkkgtsn peiirflret svfgklkrrt lneiarlvhv rkyvegeeif
       61 rqgeagagfy mifdgkvtir sirdgieldl ahldqhsffg elslfseerr tataiaseps
      121 tllgffqpdl keiietkpki gieillsltg viverlqktn qllekayykg kqknv
//
LOCUS       WP_010568825             293 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Leptospira broomii].
ACCESSION   WP_010568825
VERSION     WP_010568825.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..293
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33059
     Region          26..264
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mayqhkefyi qssrdntkly cqawikpdan rvlvfnhgfg ehsgrygnli nyfkdsdvsf
       61 ygfdmrghgk sdgkrghadt felfvddlad fiqevrrrek kdkilllghs mggvvvirya
      121 leginqdylh avvacspalk ipantfqkfq iavagflrkl spgttldanl dvnlishdpe
      181 vvkayvedpl vhgkisfsmg yelfqqgeia nkkaailrtp ililhglgdk iadpagslef
      241 ynhlvyknkr iktypgfyhe tmnevspdke tvlkdikefl dslvpektgq kkn
//
LOCUS       WP_010568885             364 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Leptospira broomii].
ACCESSION   WP_010568885
VERSION     WP_010568885.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..364
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39756
     Region          13..364
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 msesrplsty viriiffllv gaaiaffvlg lklliipial slilfyifng sinyfeslgv
       61 prilsvaglm ilvcipiywi atevaspivs tleplmknwr qdmedakfky lvvgfkiqfn
      121 dfpagweeti rpeelvqkia dmvqgevvgl vsiiptligy lvvtplfafl fllngngvyk
      181 nivslvpnry femtimiaan ineqitnylr slviqsaiit ivamigfsvi glryfyifal
      241 fvgiansipy lgpiigavpp lfmtltqgst ifyakgitdg mgmyelmgai liviviaqav
      301 dnffvqpvii sdavslhpiv vvgavtvggt llgiagmlva vplaailkvt iatlyrsmkd
      361 hnll
//
LOCUS       WP_010568921             224 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Leptospira broomii].
ACCESSION   WP_010568921
VERSION     WP_010568921.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..224
                     /product="YceI family protein"
                     /calculated_mol_wt=23695
     Region          45..220
                     /region_name="YceI"
                     /note="YceI-like domain; smart00867"
                     /db_xref="CDD:214870"
ORIGIN      
        1 mklmitksdl largrfvffg lilasiylag lqsktdaapk agvckftldp ektslewkaf
       61 kftekngvgg kftklgitgy ktgkspeaal kglkfalepi dldsgnperd akikgaffga
      121 lksggrisgh fvsakfdstg sagtgivkls lngitkdlpl tftlengelf kvkgsinltd
      181 wkassavaal nevckdlhtg kdgksvlwpd ieisitstlk tacp
//
LOCUS       WP_010569023             224 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira broomii].
ACCESSION   WP_010569023
VERSION     WP_010569023.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..224
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24403
     Region          12..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrkvetakhi lrgeatrkrv ldlavkvati eglealtigr madaagiska gllghfgtke
       61 dlqiatvrag rekfirkviy pirsvpegip rvfalidswv dyvrqseggc ffasvsaefd
      121 crpgavrdav ssmikewqlg lakviedakk lghlksdvvp kslafafqgy elalnlmfql
      181 lgekeavhea kaamhqliln sitlsgkral akdsnfgknl slnq
//
LOCUS       WP_010569050             178 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira broomii].
ACCESSION   WP_010569050
VERSION     WP_010569050.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..178
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20634
     Region          13..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprktktnrp vfeerradil eaaievfatl gyhkvttadv skvagisqpy iyrffdtkea
       61 lfleviqlvy driyrefeki hgkkatlled lirayedlmk kypneillqi qtwgiaeeni
      121 qklvkksivr lkeqvktkfe nagfkdsenq akdflargfl cnlafalhap eltyqrkg
//
LOCUS       WP_010569071             310 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leptospira broomii].
ACCESSION   WP_010569071
VERSION     WP_010569071.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..310
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34044
     Region          7..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mqiksvvsik nlsktyasgf qalknvslei regeiiallg pngagkttli siicgivnps
       61 sgsvtvagyd iirnyrqtrs liglvpqelt vhafetvwat vsfsrglfgk ppnpayvekv
      121 lkslslwekk dqtiitlsgg mkrrvliaka lahepsvlfl deptagvdve lrkdmwnivr
      181 slrdngvtii ltthyieeae eiadrvgiin ngelilveek selmhklgkk qiiidlissl
      241 nsipsslsnh eleivnnglq lvytydsngk qngitsfldd lrkagigfrd lnttqsslee
      301 ifvklvkesk
//
LOCUS       WP_010569137             421 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Leptospira broomii].
ACCESSION   WP_010569137
VERSION     WP_010569137.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..421
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=47522
     Region          9..408
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mfhqvrryql nksseailrs ghpwiltgni ssaasifkdg dwlrlvsgtn evlgfgiysa
       61 sgpigirilq rgkefsletl rkillsalek rkqlrsvtda yrilhgende ipgitvdkya
      121 ntwvvqvysk slyrlarlvm rllysasdiv depkparill isphrtgdap ssvprflrgs
      181 sdlpfeekif mknlefkaki pgqkgglfld vrnlrmtlle rkelaqdrnc lhlfchtglt
      241 slcmqaagaq sivsidgsre sllefasqlt evapgnafeh knvkvsigih eliradlfka
      301 wdflehrkfe livldppnla ptqasipsar kayrafiaks lehlepggdl vllscsgrip
      361 eqefekigre tiasqgwnyr nlvrlspepd hpirkefpeg ryfkvhlyln vnrlksytst
      421 e
//
LOCUS       WP_010569144             316 aa            linear   BCT 01-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Leptospira broomii].
ACCESSION   WP_010569144
VERSION     WP_010569144.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..316
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35057
     Region          63..265
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 maknyirfsk gknidwgrte ngkvfplnag dlstkefldf lkknpkknns tnfplkqisi
       61 lspitapcqi icqganyrqh liesgldpdd ksynmfftks daslsapige virpdhvkll
      121 dyeielgivf gksidskiev naknvseyva affmandvsa rdiqlpqmqw ykgksyrtfl
      181 pagpvlavle qgdfdllatl eltllvndqi rqhdtasnlv fkpaetitel sqfcnvspgd
      241 illtgtpsgc alrapsklvq kiggilsert kwklfikgqs krieylkpgd ivkssirtad
      301 rridlgdqil evvqgs
//
LOCUS       WP_010568208             183 aa            linear   BCT 01-JAN-2025
DEFINITION  retropepsin-like aspartic protease [Leptospira inadai].
ACCESSION   WP_010568208
VERSION     WP_010568208.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of aspartic peptidases, and those of unknown catalytic
            mechanism
  JOURNAL   Methods Enzymol 248, 105-120 (1995)
   PUBMED   7674916
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Rao,J.K., Erickson,J.W. and Wlodawer,A.
  TITLE     Structural and evolutionary relationships between retroviral and
            eucaryotic aspartic proteinases
  JOURNAL   Biochemistry 30 (19), 4663-4671 (1991)
   PUBMED   1851433
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Davies,D.R.
  TITLE     The structure and function of the aspartic proteinases
  JOURNAL   Annu Rev Biophys Biophys Chem 19, 189-215 (1990)
   PUBMED   2194475
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..183
                     /product="retropepsin-like aspartic protease"
                     /EC_number="3.4.23.-"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=19945
     Region          44..122
                     /region_name="Asp_protease_2"
                     /note="Aspartyl protease; pfam13650"
                     /db_xref="CDD:433378"
     Site            order(51,53,55,77..79,118)
                     /site_type="active"
                     /note="inhibitor binding site [active]"
                     /db_xref="CDD:133150"
     Site            51..53
                     /site_type="active"
                     /note="catalytic motif [active]"
                     /db_xref="CDD:133150"
     Site            51
                     /site_type="active"
                     /note="Catalytic residue [active]"
                     /db_xref="CDD:133150"
     Site            order(77..80,84..87)
                     /site_type="active"
                     /note="Active site flap [active]"
                     /db_xref="CDD:133150"
ORIGIN      
        1 mqkpnasaft aksnrlerel fspvqispal vylteiqkln ppavqlsaiw dtgamrtvlt
       61 tkviqklgik pistmrimga tgqgtcnvye ldlilpnnir vpnlqiaeva nlgnhdglig
      121 mdiialgdfa vsnvngktwf sfiyppngrg idfidrihsa hslnhlqnss pggnsirkts
      181 rrr
//
LOCUS       WP_010569226             239 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leptospira broomii].
ACCESSION   WP_010569226
VERSION     WP_010569226.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..239
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26698
     Region          2..229
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 midirnlevs ygkskvvkdv sfrveggnil siigpngsgk ssliksiigl vkpssgsiff
       61 envsrsaqtr aegsigympq spsfpknlti lelvdffkkl epfdeetfse myenlglrsq
      121 edkkigslsg gtkqkvnilq cfsskkdiyl ideptasldp yvshilkell rskkkegall
      181 ifsthilaev edvadrflll sdgsllides pkeflrksgf eslqlslmef wnreyknkr
//
LOCUS       WP_010569341             139 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Leptospira broomii].
ACCESSION   WP_010569341
VERSION     WP_010569341.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..139
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15728
     Region          36..138
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mrhqvdlfhq mrrmqnrihn lfdpvwesgr afpalnvysn edritvtaev pglspedlei
       61 tvahnlltih geikdpaqes gaklrrlers rgkfkrtlel pvavdsekvq atvkdgvltl
      121 tlpvqesekp rkikietqa
//
LOCUS       WP_010569343             294 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Leptospira broomii].
ACCESSION   WP_010569343
VERSION     WP_010569343.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..294
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33693
     Region          34..294
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 misniiqkfg keeaidqkwd lvirpkegwf slhlvdlwny kdliflfvkr dfislykqti
       61 lgplwyiiqp lastviytii fgkianvstd gvphfifyls gtvlwsyfad cliatsntfv
      121 anagifskvy fprlavpfsi visslikfai qfatflafys yfilkgatle mqwsvillpf
      181 filqiailgl gfgvmvssmt tkyrdlsllv afgvqlwmya tpvvyplslv perfkflynl
      241 npmanlienf rfsflghghl dlyawaqswi italvffigi lifsraerdf vdtv
//
LOCUS       WP_010569378             256 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Leptospira broomii].
ACCESSION   WP_010569378
VERSION     WP_010569378.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..256
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29405
     Region          4..>168
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mtqlvsiimp vynaekfiaa siesvlnqky gawelllvdd qskdssreim qtyskkdsri
       61 ksifkernsg sadsrnqgil aargryiafl daddlwdpef lseqiklmqd ekvafsfssy
      121 rivdesdrei lkpymatggp ityrqnllyn rvglltaiyd tetlgkmyfd vslkslrddy
      181 alwldilkki pysvgnpkil asyrvrkgal tsnkknvilp hfrmlknrek lgwipaafyt
      241 gvwgivalkk yyfnri
//
LOCUS       WP_010569423             425 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Leptospira
            broomii].
ACCESSION   WP_010569423
VERSION     WP_010569423.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..425
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=47240
     Region          79..420
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mdeswrkvve neekigayvs nafryillvf fafqllanlh tgnawingig islftvitvg
       61 hsviirtcpr waisvysyia lvsdfviisg vlisytflas pdnlgfalkn piqsffffpl
      121 afslvqfrlr lvllsvmlyy tfyfgffaya aylgkityav dwkdyvmgpn llladaftgr
      181 plvylilaff fcfgilrtli mirrigeaea qrsllsryfs pgmvtemman pdvltgrrqt
      241 atilftdirn ftalsenmdp ielgkflssi retltecvfe fggtldkyig davmatfgtp
      301 ypsddpaada ikalscgkrm lerlgdfnak rmangyppvs igigihtgev fsgnietsqr
      361 aeftvigdav ntasrieslt knfgkeflvs eetwklagan fngetlppiq vkgreklvtv
      421 iavgi
//
LOCUS       WP_010569568             304 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leptospira broomii].
ACCESSION   WP_010569568
VERSION     WP_010569568.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34087
     Region          4..220
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mgslqanrlt ksfsnrpalf eigfsvpkgr itgllgpnga gktttmrllt gflepdagtv
       61 sygdislhen piqvkrnlgy lpewapiypd ltsqeylefi grarglqggi lqhriremre
      121 lcdlgdyffs eigtlskgfk qrvalagtli hdpeyiilde pssgldpiqi nqirsiirsf
      181 grekvlilst hilqeveeic dhvlilhkgr liadmsvkei nrgdsillva ktdletlerc
      241 fkntdieile skdsgnakef hlrsdtnspe flfekirsas fpvlefrpvr rslesvfqef
      301 taip
//
LOCUS       WP_010569616             207 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Leptospira broomii].
ACCESSION   WP_010569616
VERSION     WP_010569616.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..207
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22726
     Region          6..207
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mdflailvdf fsgfgqgfay iavfatlllc gfglpipedv slvsggviag lgyanehimf
       61 avgmagvlfg dgtvfllgri ygvrvlqipf iarfitperf ekvqekfsqy gnwvvfmgrf
      121 mpglrmpiyl tagtsdrisf frfltldfia aaisvpiwvy lghygasnld tlrhwmhqgq
      181 atvfgivgav lvialvtfyi kkklaar
//
LOCUS       WP_010569718             437 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Leptospira broomii].
ACCESSION   WP_010569718
VERSION     WP_010569718.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..437
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47913
     Region          2..437
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mavesqgklr hpkglfilfl vemwerfsfy gmrallvlfl tkewllsdpe anriygvyng
       61 lvyltpifgg fladrflgyr ssiflggllm mfghlslaid gsitfflgla llilgngffk
      121 pcistvvgri yelegksdlk dsgftifyfg intgavlgtw acaniadiyg whygfgvaav
      181 gmltgllifa flgrkiagea flpgkdknsk igsegsqlds sstglvtagr irailvfssv
      241 tivfwasfeq mgsslnliid ryvdrnfygw eipaanyqsl npifvilfsl giswawrkle
      301 asgihvssvt kfcsalitla cgflilsvvt svssgkfssg wivlailfht igellispvg
      361 lslitklapa rmasmmmgif flssffghvi agelaglmgg renlsvffli fvifpglvgi
      421 flflfrkkle ywmhgvr
//
LOCUS       WP_010569724             467 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Leptospira broomii].
ACCESSION   WP_010569724
VERSION     WP_010569724.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..467
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52567
     Region          99..441
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msaqrtfsii iiflvslpif seakrleeil eilakehpea kslagvshah kshsdasgil
       61 pdpkigfayr nyptrngysl ngnraldtpt mtgmefsvsq efpfpgklgt ekriskimen
      121 eatlgylvgv nrmlgdffir lnrfqriekk kqingrildl lnaqksiteg yysagtvplt
      181 galkasiakt damekeaeyn tnlkdltsql eyykvldrvs lsdlfqinld sfleeslqrl
      241 nslansgvpa vedtpdykil laeekrlkeq tkltkysiap qtevffsymk rksqtfsadt
      301 gplnyslmdt teyrgdlfsf gvnmrvpvws alkwnsitge tehlaevgkd svdktraqmv
      361 seinrgievi rgtsnqiqiv ekklipemek aarasaslya pgkaniqdtl laqtevlnak
      421 irledlrerk netilnmlkl lsliyqdqkv prhekhqpev tlgrgre
//
LOCUS       WP_010569767             427 aa            linear   BCT 01-JAN-2025
DEFINITION  YncE family protein [Leptospira broomii].
ACCESSION   WP_010569767
VERSION     WP_010569767.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..427
                     /product="YncE family protein"
                     /calculated_mol_wt=47678
     Region          <285..404
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mriywnllir ltivfmglls geiasqslkk iesykvqnra daflkldanr yvlvgqknen
       61 wdslekhkvt frlfdmrdrk tfdlsppiae faasnpdvfi datpirtfsn grsfvqfntn
      121 lvffdgtkgg lilknrsrpg qpksiertiy ldwdigsnki nwsktiseld qfenldikvg
      181 pnsvesksil rnlmisigid skngiyyyri ekdkdnlgwp ssisilsfsi dskkieevas
      241 fsiekitggn nfyselgita ssdfsklail eyselvwkkl vkghvldlks gkmidfaipv
      301 spygvafdpt nenllilsne tgklvktnls sleqetfdsi kgarnlifsn tgkfvfvfvh
      361 gglvevrswp slkslkkisv sslqtgqsaw epggsvfssd gtyatipesd avsqlgksgf
      421 hlfsine
//
LOCUS       WP_010569890             194 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Leptospira broomii].
ACCESSION   WP_010569890
VERSION     WP_010569890.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..194
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22562
     Region          15..184
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msekakiwet latrmkksqe gdsreyelll rqvrdilraf lvsrishidd redllqeili
       61 gihkarnsyr pdrpfapwlf siaryktidh lrkskkrdrt ilaemedfaq iqnpekeeaw
      121 mlaegietwl svlderqrei lkmakihgys ireisektgl sesnvkvivh rsvqkirkvf
      181 sgeegsqtgp gtsk
//
LOCUS       WP_010569911             290 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Leptospira broomii].
ACCESSION   WP_010569911
VERSION     WP_010569911.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..290
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=32394
     Region          54..269
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mnrlliisli svvvigackn npyseqkyrp epytlpqvtv hrldqnylgl pdkpgiyavi
       61 qtsqgdlvae lfdkdapktv qnfidlaqge keftarngqk qkkpfydglt fhrviegfmi
      121 qggcpngdgt ggpgyrfede inakslgldk qrvgqvpyyt gqlqrvviqe mgiksmrefe
      181 dkkeefeknf eqaknlsvme vlyrlgyryn evvnshrsik galamanagp ntngsqffin
      241 qvdtphldgl htifgqivrg sevvdkivas gnsksvirhi livdrrtanp
//
LOCUS       WP_010569987             278 aa            linear   BCT 01-JAN-2025
DEFINITION  undecaprenyl-diphosphate phosphatase [Leptospira broomii].
ACCESSION   WP_010569987
VERSION     WP_010569987.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..278
                     /product="undecaprenyl-diphosphate phosphatase"
                     /EC_number="3.6.1.27"
                     /GO_function="GO:0050380 - undecaprenyl-diphosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30938
     Region          3..275
                     /region_name="UppP"
                     /note="Undecaprenyl pyrophosphate phosphatase [Lipid
                     transport and metabolism]; COG1968"
                     /db_xref="CDD:441571"
ORIGIN      
        1 mesflnalir siieavtefl pvsstghlfl fssffpfseg gefddlfdif iqsgailsvi
       61 vlyhdrflrh gqlsvnyllg keknpegilf vsqilvgcip ilvagflfkg kldvikarsd
      121 lllilgsawi sggilillse iwfrkssqih npepvrlkda iligifqcaa lipgvsrsaa
      181 tivtarflkk darhsaefsf flavpvllsa gayklykyrh ilngdtlpil afgflasfll
      241 cilvirwflk ylqshsfdaf giyriilgla vlifykln
//
LOCUS       WP_010570002             153 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Leptospira broomii].
ACCESSION   WP_010570002
VERSION     WP_010570002.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..153
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=16570
     Region          2..152
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mpfakfvtnr gtfsvlldie kapvttgnfi elakkgfyng lifhriipnf miqggcpsgt
       61 gtggpgykik defhpdlknk kftismanag pntggsqffi nvrdnlyldn rhavfghvte
      121 gedivlgise tetgpgdrpv qpvvietlei iet
//
LOCUS       WP_010570025             781 aa            linear   BCT 01-JAN-2025
DEFINITION  inorganic phosphate transporter [Leptospira broomii].
ACCESSION   WP_010570025
VERSION     WP_010570025.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..781
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=86349
     Region          1..282
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mdifliivgv mailgvmdll vgvsndavnf tnsavgaraa srrliliisa vgilfgalss
       61 sgmmevarkg ifhpeyfslg elmflflavm vadiilldly ntlglptstt vslvfellga
      121 slamailkte tvndafriin sesalkiifg ivfsvifaff aglflmfvfr lifsfrlekt
      181 irlfgglfag lattiviffv lltamkgstl idkdllkwig dnfrqiiits ligfsvffqi
      241 lvfsgvnvlk fvvllgtasl amafasndlv nfigvpiasl qtheliklsn wntntlavgl
      301 agevptpnll llgaalimif slfrskkaet vtqtevslgs qgetiesfqs slvarvfvqi
      361 algiyrpiki ilpkgirtwi gerfsntask eivkihenda fdllrasvni liasglilig
      421 tiqklplstt fvtfmvamgt sladgawqke navnrvsgvl tviggwfmta ifasmmgavi
      481 attffyfgfp avvavlagtl flvllfnrih gqrkaayden ieklvninrh pekalaktvs
      541 silgsliiak kamnnvysgf ingkkkdfkq tgkllknikk myensisnfl tlankhfder
      601 efqsihpvtn algyidriae nitnilrsss nnidsfrsgl skderedlkd lrklaeegfe
      661 llvdsdkips lldkarskkk vkelsdikir iyknqmrrir kgdsrlksst syfvvveelv
      721 dinenlmgla eelhhvlpwa eemrkqlqkp nnvsngrhai lpfeekkekg kkrkkkklka
      781 e
//
LOCUS       WP_010570048              86 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Leptospira broomii].
ACCESSION   WP_010570048
VERSION     WP_010570048.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..86
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9743
     Region          30..83
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 meneelldre ennptrfsrn iaswkpgitv rilrkihgys rkelaeklgg veveyvtsie
       61 kgkltigknl arklaeifei saeifv
//
LOCUS       WP_010570145             387 aa            linear   BCT 01-JAN-2025
DEFINITION  sialidase family protein [Leptospira broomii].
ACCESSION   WP_010570145
VERSION     WP_010570145.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..387
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43761
     Region          <46..>98
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          47..98
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mkiripiiff yfallslfll yscstierra astekfleik gvgafgifdp svvmdrqlnk
       61 iymsysavdp syrwpvehph tvstrlaysi dkgltwndsg ivineaedel gqklslklfg
      121 rspkpmtwnq evsslifdas aprserwklf whryplidge rkfeygwiaf kqaespeqla
      181 iakeiklfsg kyydsaadqy lgtpqvrlne ihselrdcaa ftepsafire nslylalsca
      241 dgnlpwngrq illsrrdgnw nyagilldnr rdseglliag nsftgfsape liavrnktyl
      301 ivtpttnden payhgcmvfe iedlesaril reakslkisk vipgnselhn gacsylnvss
      361 etggfllsqa ypdsvkvfri vrteikl
//
LOCUS       WP_010570151             120 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Leptospira broomii].
ACCESSION   WP_010570151
VERSION     WP_010570151.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..120
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=13043
     Region          29..111
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mnndklflsv ivllttmqig cgkndegrei pnwleqgalv vdvrtpqefa vehypgaini
       61 pindlhshlg elgpkqgkii lycqsggrsa raktilkeeg ftevrdaggi rnlfsvasqk
//
LOCUS       WP_010570154             157 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Leptospira
            broomii].
ACCESSION   WP_010570154
VERSION     WP_010570154.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..157
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17878
     Region          14..144
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mkqrinvyek ggnamkplfg lgtylaksiv ekslldlinf rvsqingcay cldmhskdlr
       61 akgeteqrly mleawretpf ysdreraala waeaiteike trvpdevfeq arkqfseeel
      121 idltlsiiti nsfnriniaf rtpagtyqvg qhaalik
//
LOCUS       WP_010570155             145 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Leptospira broomii].
ACCESSION   WP_010570155
VERSION     WP_010570155.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..145
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16008
     Region          35..136
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 manpinsiqg keeavlsese kkakwiktak wiywvitlsf vvtmlmaavm llagvsynve
       61 givhlgypiy vckilgvakl lggifilqnr frilkewaya gysfnllgaa ashsfsgdsf
      121 gaiitpivil smvllsyrqw ktgwm
//
LOCUS       WP_010570168             202 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Leptospira broomii].
ACCESSION   WP_010570168
VERSION     WP_010570168.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..202
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23761
     Region          4..194
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 merilyshsi sinsyrarli lnllnlefse itvdllrseq neeqfkkinp lsqipvlmen
       61 ditiwdshai siylaekygq dkwfpqniqn raavlqwlff danelhngig larvhykfki
      121 gkdgetyqkr gkkalsvlnd rlenrdwiel nkptladvsc fpfcavskda kidineytnv
      181 qkwmerfsnl enfvpfrkfe rk
//
LOCUS       WP_010570185             117 aa            linear   BCT 01-JAN-2025
DEFINITION  PilZ domain-containing protein [Leptospira broomii].
ACCESSION   WP_010570185
VERSION     WP_010570185.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..117
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12522
     Region          17..112
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mditsiitdr ihswdlfelf viaingeaiv vgnvsdisdt glsiqidsgn yqnfedgspi
       61 rcvisgssmk eikfagkiir tetvatsfgv kgfmaiefsn palaseqlka lisaysk
//
LOCUS       WP_010570187             530 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Leptospira broomii].
ACCESSION   WP_010570187
VERSION     WP_010570187.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..530
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60205
     Region          45..478
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mgkfrrkysl ilnlliilil fyqllsarvi aapskedenl kitltleqav migttnsvil
       61 rtleakkeif kmliterwre flpkvgvqyf glrninvgsa dniyndvrlt vqqlvfdgge
      121 aslnletskl nevlnekdfk inyaklklei qkayfktlga kgkvflarkt lekmeesysk
      181 sqaeykqgfi pkiqlietas rlrqaqyslq kykneygqsl lelkqilnld yqlqlnleen
      241 lftdfilapp rldvmnviar areeredvkk srvviqrlkd ektiaenywi pklyvggyag
      301 rngdrlplqh diygvnfnlt fplgsntvqt ngnlgvqkdg tgiqtypgfg nqfvgpglng
      361 ynssqikfwd nlsyarkive gevqlseail nrkslenqig levqksadkl lesweiikia
      421 nskvllqwes lkiastkyrv gqakredmla aeseyvksqe eltdalsiya tgcyelaftg
      481 tiegeinkli qykkgkgnsl isallnnehi ddiflpddik gksiqglied
//
LOCUS       WP_010570304             142 aa            linear   BCT 01-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Leptospira
            broomii].
ACCESSION   WP_010570304
VERSION     WP_010570304.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..142
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15945
     Region          13..136
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 maftssglkd sdivffdgac nlcnasvtfl ididrkkrlh faslqsataq sfltltesid
       61 llgegasiil ytkgrifrks raileilrlv glpwslgyag ivippfildw lydfvakrry
      121 rwfgksdscr vptaelkerf ln
//
LOCUS       WP_010570403             444 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Leptospira broomii].
ACCESSION   WP_010570403
VERSION     WP_010570403.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..444
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51327
     Region          107..262
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mekinlitia ipffflligl elffswykkr glyrlndsin dlsagvssqi fgiifktiif
       61 laylwvyqnw rifdlpawps ervswmpshd llgisvgtws msivlfvwva cfvlydlayy
      121 wnhrlshevn flwaghvvhh qseeynltva lrqasfhslf swvfylplal lgfppivtil
      181 ngelnliyqf wihtkaidkl pswfeaifnt pshhrvhhgi npkyidknhg gtlivfdkwf
      241 gtfqkeeevp vygtvkplrs fnplwanvhy wwemfelawk ssrwidkikv fvavpgwrpq
      301 elggqypipe vsektfkkyd vslptgltay slvwfaatva gtfamlvkis vipvnvqyti
      361 filsflslis iggildlkrw alymeparla iliatailfg fskanlaiig glvflsvawf
      421 llyrqsfssw keidpskeiq srta
//
LOCUS       WP_010570476             334 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Leptospira broomii].
ACCESSION   WP_010570476
VERSION     WP_010570476.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..334
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37578
     Region          10..198
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(13,15,106)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(53,105..106)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            104..106
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 maskppllsv vipiyneekt ipelakrlns llkilktkfg fdsadseilf vndgsrdesa
       61 eilkelcest pgfflvnlsr nyghqlaita gidvargeav avmdgdlqdp pefvadlfek
      121 mkdgfdvvya rrrtregesi fklitahlfy rtlkkltkfd ipidtgdfri msrrvtdvlv
      181 smreqhryir gliawigfrq tgleydrder fdgetkfslg kmlkfaldgi tsfssaplkl
      241 ssylgfsaaf agalytiyil ylklftnnti qgwtsvmivv lilggiqlla lgmigeylsr
      301 vndqsknrpl yviekiystd tapkqkekkk saks
//
LOCUS       WP_010570479             272 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Leptospira broomii].
ACCESSION   WP_010570479
VERSION     WP_010570479.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..272
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32400
     Region          106..245
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mtelvqkigy egyyvfslvt lwvrylfmag layffvwyvf rdklkhriiq srlpekekiy
       61 yelkysaltl fifaasgilv ywmkeqgwtl lyekvsdygv aymvfsival illhdtyfyw
      121 thrlmhhpll fkkmhlthhr stnpspwaaf sfhpyeavve agiiplaali lpmhsiallv
      181 fffysnflnv lghlsfelfp kgfldnkflr whnttthhnm hhryfncnyg lyfniwdrlm
      241 gtnhpkylet frevtnrdpe evsitdantq na
//
LOCUS       WP_010570579             279 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Leptospira broomii].
ACCESSION   WP_010570579
VERSION     WP_010570579.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..279
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=31749
     Region          13..201
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
     Region          229..273
                     /region_name="DUF6576"
                     /note="Family of unknown function (DUF6576); pfam20216"
                     /db_xref="CDD:466367"
ORIGIN      
        1 mayysggfgi evtpvvrrll flnlgvfvle filklaspqi lglflgifgl vpdfvlhkff
       61 vwqvltyafl hdpnsifhil fnmlslwmfg stleaywgsk nflkfylvsc igggilplfa
      121 hllgfpqgti vgasgglygl liafaliwpn relyyfaifp ikakyfvlil llligftsss
      181 sgvavtahag galfgalyff ynnklkyklg fslpsfslsr wfqkrkmkrw qeemhsreka
      241 kdevdrllek isrdgmhsls rkekkflkea stkyydske
//
LOCUS       WP_010570592             112 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Leptospira broomii].
ACCESSION   WP_010570592
VERSION     WP_010570592.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..112
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12509
     Region          2..101
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(18,20..22,28,52,54..56,58..60,63..64,86,90..91,93)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            55
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mldhkvqdgv livylkgrld vsianeveen lndlidnqgh trvilnmqdv dymsssgfra
       61 cistlrklna kegalkicgi kpavkrifdv ieltslfdir etedealksf rs
//
LOCUS       WP_010570601             194 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmD family RNA methyltransferase [Leptospira broomii].
ACCESSION   WP_010570601
VERSION     WP_010570601.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002368
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..194
                     /product="RsmD family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0031167 - rRNA methylation [Evidence IEA]"
                     /calculated_mol_wt=21713
     Region          10..188
                     /region_name="RsmD"
                     /note="16S rRNA G966 N2-methylase RsmD [Translation,
                     ribosomal structure and biogenesis]; COG0742"
                     /db_xref="CDD:440505"
ORIGIN      
        1 mkppkkgkgl riqtgdlkgr vipspvspeg ksnftpaifk kslfdilesl qlqgrlnlsd
       61 safldlfags gqigiealsr gfakavflel awdryeslkg vlsrldrehl vlrkdafrfh
      121 kdfdltqthk vyfidppysf wekkepkika mvediiaees gaaviaiqsp talnwdgfep
      181 rpfgrnvlnv rvlv
//
LOCUS       WP_010570715             524 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Leptospira broomii].
ACCESSION   WP_010570715
VERSION     WP_010570715.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..524
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59395
     Region          177..506
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkeywnskri flfrgvsvgi ifwgfslfpe sleesefgkg ktwntsrlir yamensvqak
       61 iarldldnse ydwekengky nfignvtana qntvnlplpq ytlqgrnits ntisgglska
      121 ftsgttlgvt vadnryetda gkrpeqqgti aqqfaqpslh fgsigftlkq dllknvfgyq
      181 qkrnldmsrr ssavrrldam ntlsrtvvqs ilafwnlsla eenlrtaall aksvknvkdi
      241 taskirlgva eeyesgqwna lliaaenqlr qtklerdrtr rdllvslgkd petpvelets
      301 leerfdpsks eaqeldeafl hrydfrsmll qkqnaisale varngllpsl yvsgtynsrq
      361 ydrnfpqdfn gvgvgrytqn saeikmetpi gndtaraefk naqtqnkkid llleqtkdqv
      421 ktdvrqgler iritydvlve skknleqaek fytgilpryr fgrttsvnvk naldlvaqar
      481 yglmqakvny ntalvqyels kgtlfqkygm daeevlnqti gdlr
//
LOCUS       WP_010570815             218 aa            linear   BCT 01-JAN-2025
DEFINITION  class II aldolase/adducin family protein [Leptospira broomii].
ACCESSION   WP_010570815
VERSION     WP_010570815.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..218
                     /product="class II aldolase/adducin family protein"
                     /calculated_mol_wt=24286
     Region          1..183
                     /region_name="AraD"
                     /note="5-methylthioribulose/5-deoxyribulose/Fuculose
                     1-phosphate aldolase (methionine salvage, sugar
                     degradation) [Amino acid transport and metabolism,
                     Carbohydrate transport and metabolism]; COG0235"
                     /db_xref="CDD:440005"
ORIGIN      
        1 mnidkakklv rdtgirllka gliarswgni sqridedhfv itptgrtyed lrpdeivrvn
       61 rhdlthvgri kpsyekglha aayelrsdig avihthqlqa svvaaahrev pildtemkki
      121 iggpvyctsy slpgtkklir maiealdrsg skavllanhg tlcigkdmed afnvalvler
      181 vckkfieqef lkisgkrsas reairewyvq nfgveakt
//
LOCUS       WP_010570723            1048 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Leptospira broomii].
ACCESSION   WP_010570723
VERSION     WP_010570723.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..1048
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=116333
     Region          1..1046
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mierlidesl knriptlala iaiigfgiws witlkkeayp dvgdtqvtvi allpgkaale
       61 verritlple rglnsvpyvl trrsktifgl svlqyvfeeg vsdfvarqll lerlqaielp
      121 aeanvsiapl tgpvgeiyry tieasenwtp mdlrtlqdwv ivpslrqtpg vadilnfggl
      181 ekqyhiitsp nrllrydltl pdlldairsn nrntggnvlt rgdqgfvvrg lgaiqtkedi
      241 rnivvtavsg tpiyvenlas veeyprrpdg ifnytlrdpl tgelrtresg iqgiiamrrg
      301 enpsevierv yekiryinsn llpegvrlip tydrtelvdy tvktvrstlf egvsivmlvl
      361 ifflgnvrsa lvvasmipis llfafimmkl tgipanllsl gaidfgiivd gavvmveniy
      421 rrysfakrts qagiqftefl sitrsstiev greiffsiai iifaylpift fqrvegklfs
      481 pmaftlsfai igsllftltl ipvlmcisyk vkmqsaypgk mewsnpildr iksfyhslls
      541 rllnssekvv iyslsivliv itfgyyklgt eflpdldegs inircffpvg inlksseqyl
      601 pviresimkq eqvlsvlnql grndegtdpy gpnrleilvg lknydtwrek itkkellqrl
      661 kaglqedlpg vqfvfsqpil dnvteavtgs vsdlaillng edldqlrnla kkildivrei
      721 pgatesgleq esdqaqltvt idrkrsarfg invsnildtl eaaiggtevg tlyegskrfd
      781 imvrystdyr sslesvknll vtsqsggrip lselasielk dgptiiqrqd gkrqisirtn
      841 irgrdqgrfv eearskvekl islpegidir wggqfenltr aasrlrivip atligifcil
      901 liifrnprya llamsgvpis iaggilallv rginfsvsag vgfvslfgia tmtcvlfvsr
      961 mirlqqenqt etlrssvlaa adlqftprim tillallgll paavasgigs dvqrplatvv
     1021 vggltaelfs lvfipslfyl inrkqald
//
LOCUS       WP_010570900             110 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Leptospira broomii].
ACCESSION   WP_010570900
VERSION     WP_010570900.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..110
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12278
     Region          3..98
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(19,21..23,29,52,54..56,58..60,63..64,86,90..91,93)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            55
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 meisirksge tnviglsgsl diytsidlkn ffeqnidrin nsvvinlekl nyidssgigm
       61 likqlnyvqe lngkffianm kpaiekvfkv agltsyfqtl seseftakyp
//
LOCUS       WP_010570960             209 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Leptospira broomii].
ACCESSION   WP_010570960
VERSION     WP_010570960.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..209
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23506
     Region          6..77
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(16,18..19,21..22,25..26,70,73..74)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(16,55..57,68..69)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(55,67..68,70..71,74)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          88..201
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(91,98,159,162..163,166,170)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(91..92,95..96,99,135)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(98,102..103,106..107,167,170)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mndlilvign knlsswsfrp willkqagvp frevslklft peyssvieky spskkvpvlh
       61 dgdlwiwdsl siseyiaekf pqlwpkdpst rakarsvsae mhsgftglrs nlgmnftgri
      121 kgkeippeal kdidriiqiw tenlqsfggp flfgkdftva dafyapvvsr fitydvnlpd
      181 lasqyvrtis glpaykewea eaakelesa
//
LOCUS       WP_010570973             207 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira broomii].
ACCESSION   WP_010570973
VERSION     WP_010570973.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23920
     Region          18..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mhdktnsssp pstdssardr iisaalrlfy akgypntgin eiletagsfk ktlyihfpsk
       61 rdlgksylsl qeasilalie rimrrekvys kfikswirvv krgikshyqf gcpianfanq
      121 theddefrrl ttdfirrwqk lfenylseig iqkkkkatle qiretaeail lyyqgamqly
      181 gmsgdmkyln rlekellkle ndlgsfa
//
LOCUS       WP_010571002             268 aa            linear   BCT 01-JAN-2025
DEFINITION  SH3 domain-containing protein [Leptospira broomii].
ACCESSION   WP_010571002
VERSION     WP_010571002.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..268
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31043
     Region          37..>120
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 mifikilrsl livaciyfcn pivkskpekk ltekfgvirg ndinvritgn vnskkisslk
       61 kgdvvkiler sesaeeinny yeywykilir driegwvfgr yimifndkpl sekqianlya
      121 pkgsynekdf fdkavsqygk nyyisipdgi lvtskivtyd fheetqfeyf dltsntpfvi
      181 yhslkpdrvi nsnlcllvis fqnitlynks tegdnfygsl pgsqylksde mnggvyflde
      241 ldytvtevsn kttakykirn cifekmkn
//
LOCUS       WP_010571070             231 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Leptospira broomii].
ACCESSION   WP_010571070
VERSION     WP_010571070.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..231
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26522
     Region          5..185
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(8,10,91)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(38,90..91)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            89..91
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mklsivipcy nekqtiknil etvrkvpfkd keiivvddys adgtrellqt pafkklydrl
       61 vlheknqgkg aalrtgfqsa tgdivivqda dleydpfeip ividpiykgk advvfgsrfm
      121 gnrphrvvyy whrlgnlvlt tlsnmftnin ltdmetcyka frreiiqsiq ikenrfgfep
      181 eitakiakip giriyevgis yygrtyaegk kigwkdgfra iycivrynlf g
//
LOCUS       WP_010571105             140 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Leptospira broomii].
ACCESSION   WP_010571105
VERSION     WP_010571105.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..140
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16219
     Region          1..124
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mrylhamirv ldldaaldff cdklglketr rsehpegkft lvflsegspn apeieltynw
       61 dqkerytfgr nfghlafeve niyqvcerlq skgviinrpp rdgrmafvrs pdlisiellq
      121 rgkslepsep wksmqntgew
//
LOCUS       WP_010571098             252 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar phosphate nucleotidyltransferase [Leptospira broomii].
ACCESSION   WP_010571098
VERSION     WP_010571098.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10118673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..252
                     /product="sugar phosphate nucleotidyltransferase"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0003977 - UDP-N-acetylglucosamine
                     diphosphorylase activity [Evidence IEA]"
                     /GO_process="GO:0006048 - UDP-N-acetylglucosamine
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=26571
     Region          9..>246
                     /region_name="GlmU"
                     /note="Bifunctional protein GlmU,
                     N-acetylglucosamine-1-phosphate-
                     uridyltransferase/glucosamine-1-phosphate-
                     acetyltransferase [Cell wall/membrane/envelope
                     biogenesis]; COG1207"
                     /db_xref="CDD:440820"
ORIGIN      
        1 mniskeavav vlaagkgtrm ktdqpkvavs lngkpllihv idhlresgvg divvvvgykk
       61 eevqalcagi pdlkfaeqkd qlgtahavls aehsinghsg pilvacgdvp mitgktfrsl
      121 iathnqngfs atllsakvdn ptgygrivrn gsgeviaive ekdadaeqkk ideintgtyv
      181 fdsealfdsl rkignsnaqg eyylpdlval ykkegkklga vvlkdsgesq gvnspqdlea
      241 lsailkgevp ak
//
LOCUS       WP_010571121             319 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Leptospira broomii].
ACCESSION   WP_010571121
VERSION     WP_010571121.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..319
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32211
     Region          3..318
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 msnvlivgel kdgelkkisr eitsagrkia dalggkvtav llgsgvdkfa gelaavgads
       61 iitvnageyn aetwanlvag vikdknpsvv llphtsqgkd ysprvavkvg agiiadvvgl
      121 svdggkvvak kpiysgkayg nfkvtspvam ftvrpnsqev gqkagagave aaspsagdak
      181 vkivssdlsg gnkvqlaeas iivsggrgik gpenwpilqg ladvlgaalg asraavdagw
      241 iphshqvgqt gktvspncyi acgisgaiqh lagmgsskyi vainkdgdap ifkvatygvv
      301 gdlfevvpal tdefkkvlg
//
LOCUS       WP_010571129             507 aa            linear   BCT 01-JAN-2025
DEFINITION  HDOD domain-containing protein [Leptospira broomii].
ACCESSION   WP_010571129
VERSION     WP_010571129.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..507
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=58069
     Region          236..480
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mninwyhfek egyylsvrnv nerierlnpl yirittlnrn vdkllnvlld rylvyldais
       61 lkesvfsilr esvmnavkan skriffsenn lnisnpddys kgmanfkkem irdkeryael
      121 lekvkfhcli tmafnrtsfl mrvsnnapii aeelrrvenr igksreyndl gevfadhadd
      181 segaglglam sllmlknegi egdcyklkae gaitsayiki pldfkhrnvs yqrtveiiae
      241 idklptfpen lnqimslisk pdssitqite svsrdvslst nilklansas faqgrkvetl
      301 deaikrigls elnnillslg tkkileeryn efeqiwerss lsayicrrlg ermgwkktfl
      361 tnlvcaallh diglvlmlsl epeivaklte ltgknllast lgleeaalgi thtslgsmic
      421 ekwnfsdtir vaaeyhhrpl makkesrdvv favylsdwii dcyegkadpa aihwevlqhf
      481 gfkkdeewke fgdkiineyk afqrqsr
//
LOCUS       WP_010571158             406 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Leptospira broomii].
ACCESSION   WP_010571158
VERSION     WP_010571158.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..406
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=45902
     Region          6..>129
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
     Region          110..>175
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          194..389
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msngffqivn fpkgsyvive gkkeahnffi irqgkvrvar enqvvgedpn qllgpgdffg
       61 vvaamsqhaq iesaialtdv sliqvsydqf gtliqkntpv amkiiryfsm klrqfdstit
      121 rlsfrsavee dpnqlfaige yyfnqkntlh aayafqkylq ylpngqfatq aklklqtmnq
      181 pvasapidyt kfnrsysdne mifcehepgr elyiiqhgrv kitkivdsne vllavlqsgd
      241 ifgemalldn kprsasaiaw geeiqllain kanfegmvka qpqlatrlit llseriwtay
      301 kqlanllitd pqgriadtll tlaeknrvkv vpkanynfei gtkdllkmig laypkdenlv
      361 ldlisknkfi kldqgklsct dlveleklvq ifrkksqmdm klkkra
//
LOCUS       WP_010571200             174 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Leptospira broomii].
ACCESSION   WP_010571200
VERSION     WP_010571200.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..174
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20412
     Region          14..86
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mstidliilg ilikrpmnay eivqyvendq vdrmikisvp aiyksckrlf qagyligkte
       61 kegenpekvi ysinaagkky fyelirnfss kvqpfyidfn avilnldrld reeglatllt
      121 lkkqifawkk wilehekdmk sapfpvksii kqyrmtfsal fdwieqtire fkke
//
LOCUS       WP_010571204             240 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira broomii].
ACCESSION   WP_010571204
VERSION     WP_010571204.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..240
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27635
     Region          41..190
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkdkniaevy hyyldngsae ketsssvrgr enligrdfpl rkskeriiaa alqlfsekgf
       61 fethipdial rakigvgtiy rnfrnkdhlf nesfrkclsd flsflereig dhsdrrekff
      121 llwtgissfs kerpsefffl nrffssahld tesladflrl kfklavyfrs dyaddfsdtc
      181 aslvigsflg lvrlqsdesg fpdqriirra aeilwsglsq mnsldesqit rsegvdqnid
//
LOCUS       WP_010571208             192 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira broomii].
ACCESSION   WP_010571208
VERSION     WP_010571208.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21851
     Region          4..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mavrdpedkk erilssalrl ftergfaatp mpelakeagi gagtiyryyk skeelvnely
       61 rfwklkfhda lqkgfpknas akerffhlwk algnfyqeyp esfeflelhs hspyldeesr
      121 kvtsetmqhl aafledaksr gevrtelgsm elvslcygaf vgmvklakgg fvkldkkall
      181 rageilwrgi as
//
LOCUS       WP_010571234             262 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Leptospira broomii].
ACCESSION   WP_010571234
VERSION     WP_010571234.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..262
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28251
     Region          22..256
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mkniliifsi lmliassvsa kvktetveyk qgdttlegfl aypegkdkka pgiilvhdwf
       61 glgentkara kqlaalgyva faadiygkgv rpksieeaak lagsfregdr kllraraqaa
      121 ldalksqsnv dadnlailgy cfggtaalel artgaplkgt isfhgglstp kpeesnvikg
      181 kvlamhgadd pfvkaeevaa fqeemrkaki dwqfvsygga vhsftikeag ndnskgaayn
      241 ekadhrswve lrnflkeifp sk
//
LOCUS       WP_010571323             196 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Leptospira broomii].
ACCESSION   WP_010571323
VERSION     WP_010571323.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..196
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23052
     Region          11..193
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkqeepilcd padwaciqkv lagdydsfee lvlryeslvy sqarkafrne seaedftqdv
       61 flkafeglst fkgrakfstw ifsiarneii rryrkdhpev etplfeevst elssekssaq
      121 eshlleketk ekirslvdkl pelyrkpisl hyfenmsykd isenlnlkmn tlksyifrgk
      181 eilrewlkke netgkd
//
LOCUS       WP_010571412             128 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF423 domain-containing protein [Leptospira broomii].
ACCESSION   WP_010571412
VERSION     WP_010571412.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..128
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13718
     Region          6..128
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mefknsknlp lflaaffgft gvafgafgah glksilspdl ltifetgary qlihsvvlmi
       61 lslsnkwses kelrigywli lsgilifsgs lytlsitgik ilgaitplgg iafllgwgfl
      121 gysgikgr
//
LOCUS       WP_010571435             273 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Leptospira broomii].
ACCESSION   WP_010571435
VERSION     WP_010571435.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..273
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31258
     Region          33..257
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mrlhsilgif ifilflllfg igflfyynqs kliffpeslp edfrysfqyp yeeividlpd
       61 gekiyalhfq aspnpkgtil yfhgnagslr twgaicedil pngwnllitd yrsygksrar
      121 ltelgmyeda erwysylqnr igspeeriii ygrsigtaia vnlaakkspr sviletpytt
      181 ladlaaiyyp iipswllsfk ldsrskilni sspihifhgt edeiipfsqg ndlykiaies
      241 gkkvelvriq ggshndlsff seykrelkri lsl
//
LOCUS       WP_010571493             242 aa            linear   BCT 01-JAN-2025
DEFINITION  type I 3-dehydroquinate dehydratase [Leptospira broomii].
ACCESSION   WP_010571493
VERSION     WP_010571493.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10786388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..242
                     /product="type I 3-dehydroquinate dehydratase"
                     /calculated_mol_wt=27291
     Region          27..235
                     /region_name="AroD"
                     /note="3-dehydroquinate dehydratase [Amino acid transport
                     and metabolism]; COG0710"
                     /db_xref="CDD:440474"
ORIGIN      
        1 mvnpekifii ltldeeeffn lkelpaadfl eirldlfqns kdkaaaisea ieglnahtil
       61 tyrqpedssl kaksiwtqed vapllknlnn gkhyldleld kdnsifanvd eadfgivqsi
      121 hsftgimgle elefyfrtva eeslgakhtg lpfdrilkia vmpnsesdve afrnsslkis
      181 qlvqkqsprl gycsimmger gqkdrifper lgsrftytcl gepkapgqin lktllferne
      241 ks
//
LOCUS       WP_010570898             224 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Leptospira broomii].
ACCESSION   WP_010570898
VERSION     WP_010570898.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Hahn,Y., Lee,J., Seong,C., Yoon,J. and Chung,J.H.
  TITLE     Structural analysis of phylogenetically conserved J domain protein
            gene
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 325-333 (1999)
   PUBMED   10542335
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Cheetham,M.E. and Caplan,A.J.
  TITLE     Structure, function and evolution of DnaJ: conservation and
            adaptation of chaperone function
  JOURNAL   Cell Stress Chaperones 3 (1), 28-36 (1998)
   PUBMED   9585179
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13623565
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..224
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=25604
     Region          6..82
                     /region_name="CbpA"
                     /note="Curved DNA-binding protein CbpA, contains a
                     DnaJ-like domain [Transcription]; COG2214"
                     /db_xref="CDD:441816"
     Region          7..>169
                     /region_name="PRK14291"
                     /note="chaperone protein DnaJ; Provisional"
                     /db_xref="CDD:237661"
ORIGIN      
        1 mdaiwidhyr ilgvtsdaet evikarfrkl akvfhpdngi tgsseiflki vrsyqilikp
       61 dersrfdsel rarrkdsttq pslqtflipp sriifsaqav efakrgllra girnrdrrry
      121 tgiyhdiclr lkdeelagki laeiplvvrv lcpecrgsdl ncgscngkgt yksfrylkws
      181 sgpgtlvpgr iytldlsgfr pdtfthfkkr hlkvkielyk gdkk
//
LOCUS       WP_010571535             253 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Leptospira broomii].
ACCESSION   WP_010571535
VERSION     WP_010571535.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..253
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27370
     Region          3..252
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgkivsisnq kggvgkttts inlaanlaai gkkvlivdfd pqgnsgsglg leintlpkts
       61 yelligecsa necirrtdle nlhiipsnin lsgaeadlla eenrefrlkd aisllrteyd
      121 yilidcppsl gvltinalca adsvmitlqt eyfalegltq lmkiislvqe klnpsleleg
      181 vlltmydkrt nlaqqvaedv kayfkdkvyt tviprnikls eapsfgksil sydpegvgaq
      241 syrnlaleva gkn
//
LOCUS       WP_010571548             152 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Leptospira broomii].
ACCESSION   WP_010571548
VERSION     WP_010571548.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Ko,T.P., Lin,J.J., Hu,C.Y., Hsu,Y.H., Wang,A.H. and Liaw,S.H.
  TITLE     Crystal structure of yeast cytosine deaminase. Insights into enzyme
            mechanism and evolution
  JOURNAL   J Biol Chem 278 (21), 19111-19117 (2003)
   PUBMED   12637534
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Carter,C.W. Jr.
  TITLE     The nucleoside deaminases for cytidine and adenosine: structure,
            transition state stabilization, mechanism, and evolution
  JOURNAL   Biochimie 77 (1-2), 92-98 (1995)
   PUBMED   7599282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..152
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0001882 - nucleoside binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17574
     Region          21..117
                     /region_name="nucleoside_deaminase"
                     /note="Nucleoside deaminases include adenosine, guanine
                     and cytosine deaminases. These enzymes are Zn dependent
                     and catalyze the deamination of nucleosides. The zinc ion
                     in the active site plays a central role in the proposed
                     catalytic mechanism, activating a...; cd01285"
                     /db_xref="CDD:238612"
     Site            order(30,46,57..59,87,90)
                     /site_type="active"
                     /note="nucleoside/Zn binding site [active]"
                     /db_xref="CDD:238612"
     Site            order(55,60,64,88..89,92..93,96..97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238612"
     Site            order(57..59,86..87,90)
                     /site_type="active"
                     /note="catalytic motif [active]"
                     /db_xref="CDD:238612"
ORIGIN      
        1 mdlneilpyl peflerfhdl rpenrdeips ftriyknsvf lceasnlvev sqdssrhsei
       61 iaiakakell rdryltdcll ittlepclmc agtillsrip kvayllpakq gegisslsfe
      121 tiysrnffpd lllirteetr isfqeffhdk rn
//
LOCUS       WP_010571536             291 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Leptospira broomii].
ACCESSION   WP_010571536
VERSION     WP_010571536.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..291
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32042
     Region          30..250
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 msakpkalgr glgnlipvse ekalkeagge galreiklse irpnpdqprr tfsedslrel
       61 setikahgvi qpivvketgv gyeiisgerr yracklagfm kipaivkkas enqalemali
      121 eniqrenlnp ieealayktl cdklglkisd vatrvgknra tvsnlirllq lpdsvmdlvk
      181 ngriseghar pllaiadrkk teqlayqiae kgltvrqvee ivsnlteetp vkdkkkvkkk
      241 evdivelenk frkkysmkvd ishssssgkg klsiaypsld alqkildalg l
//
LOCUS       WP_010571555             124 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Leptospira broomii].
ACCESSION   WP_010571555
VERSION     WP_010571555.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..124
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13641
     Region          26..121
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 menqvysgss ivfmeamdls dvisypivdv iegnpdakik vlrtkgartg lmhvsvisaq
       61 pskfhykfky deafqliygh lailldsgeq iemkpgdilt vpaghdsife iyepslkfvv
      121 vtcs
//
LOCUS       WP_010571572             120 aa            linear   BCT 01-JAN-2025
DEFINITION  PilZ domain-containing protein [Leptospira broomii].
ACCESSION   WP_010571572
VERSION     WP_010571572.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..120
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13783
     Region          21..117
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 merleigekt ssygeadala dkrfyirfrk enkvrishge ewldgvlidi smmgvslfsg
       61 rdwpigsrlk imsqlfscql daeiirkdel rtgnryalvf hdltdsaiie ilnkiakfre
//
LOCUS       WP_010571584              96 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF433 domain-containing protein [Leptospira broomii].
ACCESSION   WP_010571584
VERSION     WP_010571584.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Sala,A., Bordes,P. and Genevaux,P.
  TITLE     Multiple toxin-antitoxin systems in Mycobacterium tuberculosis
  JOURNAL   Toxins (Basel) 6 (3), 1002-1020 (2014)
   PUBMED   24662523
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..96
                     /product="DUF433 domain-containing protein"
                     /calculated_mol_wt=10836
     Region          8..70
                     /region_name="COG2442"
                     /note="Predicted antitoxin component of a toxin-antitoxin
                     system, DUF433 family [Defense mechanisms]"
                     /db_xref="CDD:441983"
ORIGIN      
        1 mdkilfhqdr ivshpsvcgg kpvikgtsir vlevldmifl gfgleeilge ypqlleedvr
       61 aclqyasrrl hspllekals qgwvdnrdqp yqicnk
//
LOCUS       WP_010571620             365 aa            linear   BCT 01-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Leptospira broomii].
ACCESSION   WP_010571620
VERSION     WP_010571620.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..365
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40612
     Region          71..>271
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mlrsiylnpf lrivfpilsv isllfvsilv gwnktdpefy svdspipqge dnalffseav
       61 hegkisepfa ialdskgwiy tgssdgniyr iktdgkvevf artsgrplgl afdgkgnlvt
      121 clsgvglafy dpqgkenila rqdeqgntlg nlygldiasd gtvyftevsr kfsydssyle
      181 elesrpngri laykpkdqsi tvvldevyap tgialssree flvyaekyrh rvtrfwlkgk
      241 ktgkeqffit hlpgspalih sdkkdafwia lsaprhklid kiqekpilkk yvaalpvffk
      301 pkegtftyil gmneagdvtf altdssssrv gsttaaiefg rglllagnas dkiwkwkfet
      361 lesff
//
LOCUS       WP_010571588             187 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Leptospira broomii].
ACCESSION   WP_010571588
VERSION     WP_010571588.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..187
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=21483
     Region          1..178
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mdkprsycsy irslgpnean ehkayhntey gfpletddel fgrlileinq aglswttilk
       61 kkenfyeayh rfsvekvsky kqkdvdrlls nagiirnklk ieatihnanv irsiqkqsgs
      121 fsswldshhp ksrdewtklf kktfkftgge ivnefllstg ylpgahdsdc ptakkisrlk
      181 pawsrvk
//
LOCUS       WP_010571626             430 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Leptospira broomii].
ACCESSION   WP_010571626
VERSION     WP_010571626.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..430
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50434
     Region          81..235
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mekniielit paffvlalae viwvlvtkkp fyrykdsvnn laagvymqif tvfitlglia
       61 iyawayqnfr lftlaenswi awvacyvlad ffyywyhrfa heinifwgsh vahhqsedyn
      121 ltvalrqgil qntfslpfyl plavmgfppl mfmlviqinf ayqfwihtri ipklgwfewv
      181 wntpshhrvh hgrdpkyidk nyagtfiiwd rlfgsfreee eepifgivkp mttwnpiwaq
      241 fhyfqelfdl swrtkswkdk flvwfkapgw kpadlgksvv ppeidrstyk kydtqipitl
      301 tiytilqflf amgasmvyie fkkelplpem ivlgfyvlwt lwtigaifel ktsgivlelv
      361 rlasiavlty vypfdfthvq kltallpmei vislpfmmki talvsfavlg afllsqkrff
      421 tvkgysakta
//
LOCUS       WP_010571700             301 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Leptospira broomii].
ACCESSION   WP_010571700
VERSION     WP_010571700.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..301
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33525
     Region          <20..165
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrlfpilgli laafhlstfa endkvinfll pvktdgienk vssvfgesrg dhfhngmdis
       61 sngesvlamg egkilytrfg eddpygeefg tgnsvwldhg ngvytsyyhl kdgrltgflq
      121 drliargeki gmtgntghss gahlhfvviq dfgkkildpm kflppiedev spqignllvh
      181 vgdkytqind geninvsqpf pvtvgvsdag kktgqrrgis qiqaflngep lkkagfsalt
      241 ydhgewknpe gfrfselyfr dqyylgnldf rngentikil awdfrgnlge ksftfyvtri
      301 r
//
LOCUS       WP_010571647             393 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Leptospira
            broomii].
ACCESSION   WP_010571647
VERSION     WP_010571647.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..393
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=44818
     Region          8..387
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 msldfrskfs grfefesgen dlylkvkelr dsgkeiidlt vsnptkvkit ypseailhsl
       61 srsesltyep tpqgilsare avskyyqern iqvspgdlfl tsssseaysy ilklfcdpgd
      121 evlipapgyp lfefltlleg ikfrtyslns eanweidfes fesnlssktk liflvspnnp
      181 tgsllsdsef arlvdlsesr giglvldevf idylhderkt prfktnrvpl fmvngiskil
      241 glpqmklswi hvdgperwkl eckerleiia dtflsvntpi qfalpellew rkmiqgqisr
      301 rirrnlqslk glisdskrli frsptagwya ilgshffqdp dayclqlles entlvhsgsm
      361 fgfpdeefil vislipenel feeglsrtlr fsk
//
LOCUS       WP_010571713             460 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Leptospira broomii].
ACCESSION   WP_010571713
VERSION     WP_010571713.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 460)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..460
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51160
     Region          39..253
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          156..460
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnflfsrtpl vllltsryir gsraagllsl ksrvsfvvma vgvsllivvl sifngfqrqv
       61 keslwqggsh itiesnsgag eitdyqkiis wiektpelkq rivsveggiq shgliqnynt
      121 fypviiravp vsnvddlllt rlpnfprvvh ynrdelaqmn renyivigke meglynfslg
      181 rqltlavpgg rfslgkgvev svenfrvsgf fktgnyqfds ryvymslpia qrffklrnsv
      241 nqitlkvksl ddlsyckrkl lrlfsepdfe revevsssls vrtiaeeqen flaalklekt
      301 iisiivflfi ilaalgmvas vyslvrakrk sigvlkalgl pssdillift lnamlvgila
      361 sliggvtgif lansleniin gieeimnmlg pdisvlfgae wspvelvpkr iyyfdkipvd
      421 idiafifmvt taatilsgia gyfparwaas lnpvdtirnd
//
LOCUS       WP_010571750             145 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Leptospira broomii].
ACCESSION   WP_010571750
VERSION     WP_010571750.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..145
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=16095
     Region          7..>132
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msinilefin nisvktylsg etvfeekdms tgmmyflfcg eleisktydg evriirklta
       61 gsffgemali skipraagar visdkakigs ldkdmfhkig qtnpkffsil lstmierlvs
      121 veeeigklss lssvnleeik prvdv
//
LOCUS       WP_010571760             205 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira broomii].
ACCESSION   WP_010571760
VERSION     WP_010571760.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23527
     Region          11..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtlvatrpkr rtrnslnkqt ivqaameilt edgidglsmr riaekldcsv aspyshfksq
       61 qdiikilisq geaqltetlr eaklhgknay ekltriarty yefsgnnqel hkvmfntvhg
      121 hmhrkafpkl ptsyrvflet iregcrsgef iiteeeypsl artmyswmyg iivldmtgml
      181 kkrgmgdpld egflffrkil lgdei
//
LOCUS       WP_010571774             259 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Leptospira broomii].
ACCESSION   WP_010571774
VERSION     WP_010571774.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..259
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28222
     Region          5..236
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 msirsdllpl fesisreage qilkyfdgks eyslkdpmqv ltdadlashe ilfeslhref
       61 sgipiileeq enseplptsy ivcdeldgtt lfsrgmsefs vimayveagk pvagciyfpa
      121 tgsivlserg kgttvdgrkv fffgesdlsr sivsleinnt ladedfvwia nvvknslasr
      181 slaatgagfr elllgktdlf lnfngakvwd faagaiavee aggillskeg rplewdkirm
      241 sgvickdsgl issvfrlkp
//
LOCUS       WP_010571784             138 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Leptospira broomii].
ACCESSION   WP_010571784
VERSION     WP_010571784.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..138
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=15318
     Region          1..>88
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mkplilvvdd ndryannlkt ylenlkcdvl ravdaaqgwe yyaknkdkls avitditmet
       61 qtsglwlirr ihkdgfkgik viattgfdvf gvmaisrlvl ptfagisfmv pkvplkagkv
      121 lmlptgliqe sfelsirk
//
LOCUS       WP_010571848             359 aa            linear   BCT 01-JAN-2025
DEFINITION  SH3 domain-containing protein [Leptospira broomii].
ACCESSION   WP_010571848
VERSION     WP_010571848.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..359
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39739
     Region          28..>98
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 msqvrqyitk ailailicla fpivggeadg vryvlitsgv lnvrespesg kvlftlnkga
       61 kvrllsdtss qdwakvkldd grtgfvsrky lgstppetld sykliglvws gydpkelpvf
      121 vplaffskng wqaakdeyef dykfrsgveg nlpsvaliag nkgpgfaatn pttygcqqlp
      181 aikvkptall dskisylvhs admalnsipl helsqadady elfrslaett wkargypetq
      241 wlrskiqevy efktskketf isgriafseg iaerrylyll arksgtdrvl iayeksdkls
      301 qelgtyggyf hlvgvvyree dpvpvliftd igydssiksl yelrngtlql ilrgagdac
//
LOCUS       WP_010571875             183 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Leptospira broomii].
ACCESSION   WP_010571875
VERSION     WP_010571875.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..183
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20994
     Region          3..169
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mgeqefsrfv estreivlaa vsrylyerfa yaiddvaqet ylraykalqk gqfrgdsklt
       61 twlytiarne sirmneilgr eetkaekagk rseeerrlet asensddsad lptwekakiw
      121 vlqlpesyrs vlqyylsgys ekqiaealgv pagtvksraa rgkemlrrmq nserreggti
      181 wge
//
LOCUS       WP_010572052             328 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome-c peroxidase [Leptospira broomii].
ACCESSION   WP_010572052
VERSION     WP_010572052.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..328
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=35702
     Region          52..325
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mikkrliamt gfllfailac gpsektkllm edakrnfgti pakmpgsqnd tpelvklgek
       61 lyfekklsvn dtqacsschn isgkgagvdn lptspgalgk ngdrnsptsl nagfhvaqfw
      121 dgraadlkaq akgpilnpge mamsseaave kklseipeyv elfakafpkq ekkitydnla
      181 eaiaafertl itkdrfdefq ngnhrslnse eqkgldafvs tgciqchngp llggnsfrkl
      241 gqvnsyenve dkgrftltkn aadlyvfkvp slrnvaltgp yfhdgkvktl deavkkmafi
      301 qlgkelssee igsivsflka lsdknrsn
//
LOCUS       WP_010572025             236 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Leptospira broomii].
ACCESSION   WP_010572025
VERSION     WP_010572025.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..236
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26063
     Region          1..230
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mileqtqlsi ddggimhafi arpdhgpspa livlqevfgv nhhikdvaqr fakegfytia
       61 pelfhrtapp gyegsyedfr aarphfsait ietlesdlka tyswllsrse vksdligsvg
      121 yclggkvsfl ansflplqaa asyygggiap sllsycerqn gpillvwagl dknilpehyr
      181 svsdslrkhn khyveaifsd anhgffcdar saynkeaaqq awsltvsflk tylmis
//
LOCUS       WP_010572070             148 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2147 domain-containing protein [Leptospira broomii].
ACCESSION   WP_010572070
VERSION     WP_010572070.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Barison,N., Cendron,L., Loconte,V., Proctor,E.A., Dokholyan,N.V.
            and Zanotti,G.
  TITLE     Protein HP1028 from the human pathogen Helicobacter pylori belongs
            to the lipocalin family
  JOURNAL   Acta Crystallogr D Biol Crystallogr 69 (Pt 8), 1387-1394 (2013)
   PUBMED   23897462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..148
                     /product="DUF2147 domain-containing protein"
                     /calculated_mol_wt=16276
     Region          1..147
                     /region_name="COG4731"
                     /note="Uncharacterized conserved protein, DUF2147 family
                     [Function unknown]"
                     /db_xref="CDD:443765"
ORIGIN      
        1 mkrifispyl illflipgsl ltqplpvtgs wktvneqgke esvveiyeqg gkifgkvtsl
       61 aepndkdgkp arctecdgae knkpvlgmvi inglsadgdk wsggrildpn dgvwykcflr
      121 lveggkklev rgyvgfsllg rtqywikk
//
LOCUS       WP_010572098             651 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Leptospira kmetyi].
ACCESSION   WP_010572098
VERSION     WP_010572098.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..651
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=73582
     Region          15..646
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mlkkipsnlr ivsgftigyl ilfsiyricf lfafsskfas ssvsdvllaf lagirfdlsv
       61 caillgpfwi lsaihplnrf rvysifwgiv pillffwaga hligdvlyfg etnkhlgyeg
      121 fvflgpelai ilksffvght ilailsfaai atllpfsifq yiqkelytfd psrkksellq
      181 llilppvifl lvrggfqsrp lrasdamise tyivnqlvln giftsvmdik nqsiprnlfv
      241 syedsivsvr keidypgatf vsekypilre tketnpntpp nivlvllesw tgkyaytngt
      301 illqgkkiap hfenlirqgt yfssffasgg rttngllstl tgipdgpglt vvrtpqilsr
      361 fgglgtilks vgyetfflhg gdvnfdnmnf lfshwgfdti lgqeyfdslg kykpgpwgyy
      421 dgdllnelhe ilmrqrapfl avtltltthy pyktpeqede vfsapleead yfnvyryadk
      481 sihnflekak kapyfkntvf ifvgdhahhr nldyfedrni pfliyspgri pskidpriss
      541 qldviptilg ivgkkvrfsa mgrdllsedi sggvayfafg nfigwiegnw ifysltdkvr
      601 ispfsivpri geteeckttp akceayhtka ksfwnlsyel mnsnliyppk k
//
LOCUS       WP_010572136             448 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Leptospira kmetyi].
ACCESSION   WP_010572136
VERSION     WP_010572136.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..448
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=51061
     Region          8..255
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(12..13,15..18,20,33,35,69,88..90,94,96,133,135,
                     137..138,140,151..152,155,172..175)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(12..13,15..18,20,33,35,69,88..90,94,135,137..138,
                     140,151..152)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(16,94,96,133,135,137,155,172..175)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(29..30,61,66,71..74,88)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(151..159,168..175)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mkdrflilqd tageggfgki dkaedielsr evaiktldpl fkdspsnedi erfrreaknl
       61 aklthpnipa iydisfmpne kdfkiyfqwi ngtslksyiq qrgyltlqea tkyfkficla
      121 isyahkhqii hrdlkpanii itddlescyi vdfglslnka dysrvtgdsa igtpgymspe
      181 qenggevder sdiyslgvil yeclsghrpr vgdynnlsaa nesipvtlda likeclnpkd
      241 triksveefl kkltesqrpk stlsdvlssg slaeiqtnls sitvqgfnsl pvgqkrlika
      301 rikdlvdvnk qhlnqalssm lctivplsin depdfeyyyk eslrfgfekk mtdnwigdiq
      361 vreavanvik eleknalliv snlifalwer nhreselqek wfyhdlrevf qgilinefcs
      421 deiaqqiggl ledlnykshk ehleknsn
//
LOCUS       WP_010572107             180 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma carbonic anhydrase family protein [Leptospira kmetyi].
ACCESSION   WP_010572107
VERSION     WP_010572107.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..180
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19815
     Region          7..174
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mksnyqiley mgkkpqihes vflapgsqvv gdvvigknss iwfqtlvrgd vnyirigenv
       61 niqdltvihv ardvypveig nnvsighrat ihgcklkdna fvgmcatlmd dvevgefafi
      121 gagalvtpgk kippgvlvmg spgkivrdit dkereiitrt tgnyiryken ylqdpfysrs
//
LOCUS       WP_010572204             443 aa            linear   BCT 01-JAN-2025
DEFINITION  glutamate-1-semialdehyde 2,1-aminomutase [Leptospira kmetyi].
ACCESSION   WP_010572204
VERSION     WP_010572204.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11477879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     gene            1..443
                     /gene="hemL"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0042286 - glutamate-1-semialdehyde
                     2,1-aminomutase activity [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
     Protein         1..443
                     /product="glutamate-1-semialdehyde 2,1-aminomutase"
                     /EC_number="5.4.3.8"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0042286 - glutamate-1-semialdehyde
                     2,1-aminomutase activity [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=48023
     Region          18..443
                     /region_name="PRK00062"
                     /note="glutamate-1-semialdehyde 2,1-aminomutase"
                     /db_xref="CDD:234607"
     Site            order(130..132,158..159,161,220,253,255..256,281)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(131..132,158..159,220,253,256,281)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            281
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 msrqttnskl isdswkgkns eelferakkv spggvhspvr sfrsvggtpv ffasangatl
       61 tdiegkeyid yclsfgplil ghrdpeveev vretaglaws fgaaepysle laefitsqip
      121 waekvrfvns gteavmsalr varaatgrek ilkfdgcyhg hldallvkag sglagesssd
      181 sagisataia ntlvlpldde kavekvfete gkniaaliie plpanyglli qrkeflnqiv
      241 eiakkhgtlv vfdevisgfr tgfqgmagll gikpdlvtyg kiigggfpvg cyagrkdlld
      301 lvapsgpvyq agtlsgnpfg mraglatlkk aqrdsiypal ddrtkiltse mirllnrksd
      361 qeweavthss lfwfrkktqt pvrridqipe ghkegfakvf hallkygiyl apsgyevgfl
      421 swahddgvia ktleiadkal kel
//
LOCUS       WP_010572213             235 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Leptospira kmetyi].
ACCESSION   WP_010572213
VERSION     WP_010572213.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..235
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26327
     Region          25..225
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makrsdfagm dlltafgeke sskseiplsd iapnpaqprv fgkeevsdlv esmkrlglie
       61 pivvrksgkk yqivagerrf qaakilkwns iaaietsase drcfemalae nekrkslnpw
      121 evgraiqflr kekrktaeev skvlgftery vkqlssiarl dqksvadlir sgkdasvknl
      181 eellkqkegr ggemisprkt apakvtvqls klnsqqrekf lkelstlkkk ygikd
//
LOCUS       WP_010572280             307 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Leptospira kmetyi].
ACCESSION   WP_010572280
VERSION     WP_010572280.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..307
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33269
     Region          6..274
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mklgsevliv gggpaglsaa lalgrmsrta licddnrprn apsshlnnfp trdgihpaew
       61 rrlvrkdlek yktisffegs vvsveksvfg fnakfssgdt asfrkiilay gvedrplpvp
      121 gfrelwgksi fhcpychgfe irgsrialis nsemtfhmls lvndlasdli lltngkaifs
      181 eeqksllkrn nvrlieeqit gflhegerln aitlandtii erdaaffqpi lpfklkstig
      241 eelgcektqf glykvnerga ttvdgvfacg dsvsmghsvl laaasggmag agtvasllge
      301 kfegmsh
//
LOCUS       WP_010572537             241 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leptospira kmetyi].
ACCESSION   WP_010572537
VERSION     WP_010572537.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..241
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26689
     Region          13..234
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msrstlgeav kvkpaiacrs lsksfgepps favknatfsl ergefvaltg rsgsgkstll
       61 ymlsgldkps agqvfldgid ifemeskeah rfrnsnigfv fqfhyllpel taienilmpa
      121 rktdrhvakr ddarrllnef glehckdkfp sqmsggeqqr taiaralild piflfadept
      181 gnldttngdk ameilkrinr engttvvfvt hdpdyaalaq rrihmvdgev nsdqiqtkna
      241 r
//
LOCUS       WP_010572635             227 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Leptospira kmetyi].
ACCESSION   WP_010572635
VERSION     WP_010572635.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..227
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=25884
     Region          10..124
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mkvaatysll laeddesnae llirhleryn fdvdhvvdgi aaeiklrktr ydliltdnrm
       61 pklsgldlle ripetnrttp iifltvsner dtiiqaahnk rlvayllkpi dtqvliekic
      121 salgvrvdsl idkkeypfei lpftntdqgi gvgielkgcp ygrsieklvq eisfflkelp
      181 slrsilikvn peffyfkngg qllsslrdrl aikyeirked iiiqaeh
//
LOCUS       WP_010572701             220 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Leptospira kmetyi].
ACCESSION   WP_010572701
VERSION     WP_010572701.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..220
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=24406
     Region          48..215
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mksarfqsvf vfqnillflf ffcvngcvgk eheqqglsal lpligpllkv giigdslsqr
       61 sdgfglrekl gsrftvtdys vsgrdvpgwt qaigtafteq qdvlilelgt ndvsgyptdq
      121 fpnhyenlig tiqsktnsai ivtilpptiq pgyranifqi npylrslgsr yptadmetvf
      181 lemektiply pvtdpihpnp vgydlmgtvy adtirkfyvr
//
LOCUS       WP_010572734             322 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Leptospira kmetyi].
ACCESSION   WP_010572734
VERSION     WP_010572734.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..322
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35887
     Region          5..309
                     /region_name="UDP-GlcNAcDh_Arch"
                     /note="UDP-N-acetylglucosamine 3-dehydrogenase; NF040723"
                     /db_xref="CDD:468687"
ORIGIN      
        1 mtervklgvi gtghmgqyhv nvaktlndat lvgifdadvd rakqmaekhk tsafatidel
       61 iskvdalvia vptflhheia kkallankhv lvekpiaett eqakelvkla adknlvllvg
      121 hverfngavl elgkivkdpl liesrrlapf nprikdvgvv ldmmihdidi vlnlvnspvk
      181 klsasgtkvl snhedianvl lefengclas itasratqak irtlnitqkd vyimldftdq
      241 eielhrqats dilllseeik yrqesiveki fvhkdnplkq ehehfircir ketepivnrn
      301 sdvstleiay qilseihgts kk
//
LOCUS       WP_010572785             303 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Leptospira kmetyi].
ACCESSION   WP_010572785
VERSION     WP_010572785.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..303
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34849
     Region          <125..235
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 mslirlksff lndrikfsfy gillflclmf vdchqtniip sqfprdgesf kgvsftsksy
       61 vlgyfegghd raecpegirs fkifrsitdf fvhifvggly dtrsveiecv riklnfdsiv
      121 rskgfvlrgv yfnsnsdrin eesfeildel seilranpgl kilitghtdl nggekqnril
      181 slkrakstke yllaqgidts rmeirglgss rpiqrsldes asfqnrriei satrndenes
      241 vkkriepeds ppeeytstii lrngrklygn itkqtekdvy venkdglqil skrkirkiky
      301 nhr
//
LOCUS       WP_010572840             243 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Leptospira kmetyi].
ACCESSION   WP_010572840
VERSION     WP_010572840.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19424354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..243
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27192
     Region          28..237
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
     Region          65..165
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 msrdfellne vignqekeks tmdyiepfeg eraskyesni vtmipfysgi selvatlilk
       61 sipsgskila agcgtgadfr sllkvapdry ritgvdpsad miaiaqknfp gaelicapvs
      121 sldpnrkfsa atllfvlhfl pddgtklsll kdissrlepg gtfilfdlhd sqsdmeivfe
      181 elslylkefq gwekdalkty vdrvkglkri atpryeelfr eagfkswkki fqayhvggwq
      241 lfl
//
LOCUS       WP_010573064             417 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Leptospira kmetyi].
ACCESSION   WP_010573064
VERSION     WP_010573064.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..417
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=46949
     Region          22..412
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mkadseghkn hsvkptrkkf tekirlkprs wvnlgysian seegtfflkn aipgesvqtv
       61 plkqsgslfw gvaseieavs qerissdcga fprcggcsyr hvtykkelei kkfllqetle
      121 rslsknhiqi peieilsgkp ngyrntaqiq lgfvgskria gfyeefshsi vnfpeegckn
      181 lpdemnsaff eflkkekngs apisksktls frleknrvvp ykkesvefre tvsipdpkei
      241 vwqipaggfs qinrfliapw lekifdlvpn hqnrilelyc gsglisialq sktknwigye
      301 lssdsvkqar knvsqngiss fdfktlnlet dsidsaeald ssfwimnppr aglskkvsqi
      361 lcdrkpdgfl ysscnhttla rdlsavldag ykisnitlvd ffprtkhfev ivkaern
//
LOCUS       WP_010573079             122 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Leptospira kmetyi].
ACCESSION   WP_010573079
VERSION     WP_010573079.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..122
                     /product="VOC family protein"
                     /calculated_mol_wt=13384
     Region          6..118
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 miivegidyf lipaenpeas akfysdifdf esvdeksgey vvmgldsini klqkisgfkn
       61 slgeskipvl sfvldvddft eaiaeleenk isivrgpetn sggeflhfld pagnvleisy
      121 kd
//
LOCUS       WP_010573082             260 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Leptospira kmetyi].
ACCESSION   WP_010573082
VERSION     WP_010573082.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..260
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28298
     Region          7..254
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mnesstvlys teqqiavlll nrpekrnais kellstlhes ivkakketsv ralvlggigp
       61 sfcagadlke rttmsptevk rflddlkncf lelenfpypt vaaldgdafg gglelalccd
      121 fillkndvri gltetrlgii pggggtqrlp rrigvpkake miftgktida etalsyglan
      181 siwhdsslpa akmlaeeias hsapialqla kkaiaegygq diltalktes kyynetlkte
      241 drlealkafq ekrkpifkgr
//
LOCUS       WP_010573172             128 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF423 domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010573172
VERSION     WP_010573172.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..128
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13292
     Region          5..127
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mtgkqktili lsslsgflgv algafgahal ktvitpdlla vyetgnryhl ihsilplila
       61 ltgfvnrnka awissilfla gilifsgsly vlaitgiril gaitpiggvs fliawallgf
      121 saigsknd
//
LOCUS       WP_010573115             658 aa            linear   BCT 01-JAN-2025
DEFINITION  beta-galactosidase [Leptospira kmetyi].
ACCESSION   WP_010573115
VERSION     WP_010573115.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 658)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 658)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 658)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..658
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=76045
     Region          1..623
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
     Region          616..656
                     /region_name="Glyco_hydro_42C"
                     /note="Beta-galactosidase C-terminal domain; pfam08533"
                     /db_xref="CDD:400716"
ORIGIN      
        1 mifgadyype qwtkkdweed frimkemgls svrlaefawa mmepkegkyd fsffdhildl
       61 vrkhgmtail gtptatfppw lskkfpdiiq erdgiqrtig trrqacfssp nyrkavvkiv
      121 tamakhfgnh psvigwqidn eighegsdid hsstslkafr vwlknkykti qnlndtygnv
      181 fwgmlydsfd qipvpgrhva snfhpsliqd fyrfhsdtii dfvklqaqil rkfsvgrplt
      241 tnlypspflp iidmaelaty ldyvswdnyp twgeqeepfp hpfisamqqy nrglknlpft
      301 vmeqisgfqg hdllgylpap gqtklwtkhs iahgsnaiyf fryrtarfgq eqlcygildh
      361 dkektdryfe lqkgiqeise yaddfteelf pasvavvhdi enarnwkhqp istglkfspv
      421 pwsqlgydie matwfsgmnv lnvnthfrpa skidfkdyki iilpmytmvt dsvferleef
      481 vreggtlilg frtgakdlng wmydsqipgp faemagvkvr kfeavgnqkv kfrfrffpgt
      541 cskiceilep ttaevwaryt dgkkfykgap vitantykkg rviyvgasle plsfvllyrr
      601 ilkeakipft fygpnvekiy rtgrkqnyei finhsgkktl aglkmldpye vrilpkkk
//
LOCUS       WP_010573207             318 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leptospira kmetyi].
ACCESSION   WP_010573207
VERSION     WP_010573207.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..318
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35747
     Region          15..232
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnqnshslkp edsvidvrnv ikrfkntvav ndlslqiqkg efvallgpng agkttlieml
       61 egiqepnggs isilgttwkq netflrskig lalqetrfmd ritvqetldl fgtfykskke
      121 rlneilelin leekqktyvg nlsggqrqrl algvsilnyp eilfldeptt gldpgarrdv
      181 wkildrlrqn kttmiltthy meeaetlcer iiimdkgkil dqgtlpellg rtdggeiirl
      241 smedgsnpes wipssgmykf fwnsgksear iyvsaiadyl pelmrtisns gkklnalech
      301 kktlddlfls mtgrglee
//
LOCUS       WP_010573208             363 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Leptospira kmetyi].
ACCESSION   WP_010573208
VERSION     WP_010573208.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..363
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40466
     Region          168..362
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mkqifqlvsi qlkefyrepg ilfwafvfpi amagvlgiaf knrgseevki ailensyqie
       61 elkkildsss ieksdsnqsn dktatpnpgs lpslkflils kqdairdlkr gklnvivert
      121 hdgkihfsfd sdnpngqrdy llilakirsg ktdfesqvdr ldskgtryid ylvpgmlamg
      181 vmnsclwgvg wnliemrmkk llrrmsatpm nklyfllsff ftrlivtave saillgftll
      241 tfensfegsi gaallvylag nfafacigmf igsraagsqv gnglvnavtf pmmvlsgiff
      301 syqnfpevvl pfirnlpltl madslravfi egaglmfvip tvisllvygi vflfigsrif
      361 rws
//
LOCUS       WP_010573256             504 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpP1/FadL family transporter [Leptospira kmetyi].
ACCESSION   WP_010573256
VERSION     WP_010573256.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..504
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55914
     Region          26..501
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mkilklkrtf giglligigf akeikagsyg diygahpaaa gmgsavtaiv nnssavfynp
       61 aglgrlsegd lilasiekea rtngaenpen kdaapppppa dpndpanqqp tvvgpwykrf
      121 wadtkegftk evfkykpanr persvhevsf qyhyanpdsh ttaprnqnit kirdsfvglg
      181 ltlnlndmfd mgrglrfgin alvpgsgnll tlndqnptvp rylqqgisne rptimgglgl
      241 eiwkdrlfag vgftataggt gsilmkdvpi spdpvsansq viltvkplvn ptyglqfsyg
      301 kfslgasykr etvtqidpvp araqttllgi qldfdlaild gfnprvfsyg vafrpndrlv
      361 lsfdmnrelw sqfkmsrike kyseafylhd ttnfrigaey slfkflktri gfatrptplp
      421 ampgannwmd sdrniyslgf syifspttfk fmnrlrkpvi fdivfenhql kamevnkyhp
      481 ternpnysyg gyiwtvgvsm tiff
//
LOCUS       WP_010573272             195 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Leptospira kmetyi].
ACCESSION   WP_010573272
VERSION     WP_010573272.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..195
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21786
     Region          21..170
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mrdseesllv khnggsyvmf lptdltsike lrsalrnsls encfsskdil nielaadeai
       61 tnsisanvkv ssdetiicrw vikdckftmw imdygsglks eklecipadi rvsnlkdylt
      121 cvknhqekks eilpwkgsqv phrnigrglq iiqslmdtfk imyhcgegki ssnpdekniq
      181 gsiielsfda skhta
//
LOCUS       WP_010573291             472 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2779 domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010573291
VERSION     WP_010573291.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10567422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..472
                     /product="DUF2779 domain-containing protein"
                     /calculated_mol_wt=54911
     Region          268..394
                     /region_name="DUF2779"
                     /note="Domain of unknown function(DUF2779); pfam11074"
                     /db_xref="CDD:431641"
ORIGIN      
        1 mntyqprpdf dpyehqyisp kqksllrels hsfypdsknv rysesetrri lrsgkgvrsa
       61 cletdkfsik teyilpneek pgtfeivvlk asssfkkqhi teiafqkfvt eesgfpvskc
      121 tllfvnskfl fqgeikiesf fvrkdvteev alkdketkes ayslydllsr knlpsryvsr
      181 lcshprncsy pgiclnpkvp gdiftlregk eesgklyekg ilhlkdiqei esltprqkiq
      241 iqtmrtglpy tnqkvfqeff gkleypmyfl dfesinppip vyqnsypfqh vpflfslhvi
      301 rkdvseepes fyyiedgivd prkgileklq ewilpggsil cfndkferrc leesaaafpe
      361 fkgwlksiqd dfvdlakpfw eydyyhpdqk gstslktilp vitgqtyknl riqsgqmans
      421 eflraktepm teseksaiek nlieyckldt yamvlilrki qewvrshpnp da
//
LOCUS       WP_010573297             242 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Leptospira kmetyi].
ACCESSION   WP_010573297
VERSION     WP_010573297.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 242)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..242
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27104
     Region          5..179
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mfqnikwiff kevkvffgtf maplvfggta flnslfvlil nfnsgtnyvd ttvitflsfm
       61 stiiiamlil amgsiteern rgtleflfta pitdleivag kfafgtlicf lisvfvnglf
      121 piflysfwka plyivvsgti gvfllgifsf aiglfgsslg knqmtsllis ivivltlwvs
      181 gyfsylfdsv trkilyhlhi fshfiafckg vlplngivff vsgalfflyl tvkvlesrrw
      241 rg
//
LOCUS       WP_010573336             258 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Leptospira kmetyi].
ACCESSION   WP_010573336
VERSION     WP_010573336.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..258
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28189
     Region          3..257
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkqilcianq kggvgkttta vhlafglalk gervllldld aqgnatsvft aenslpvste
       61 egrekslyki frdggdprei liqtrieglk igpshsslae vdvmlsgkid gffhlrdsle
      121 likdefdyai idcppslsmi tlnafvastg llvplqvskf sldgieaile ahkntvkrfn
      181 pslkvfgavl tmfnprttls qtlepmiepy lklfssripp svsveeahmm kqtlfeyqpk
      241 gkatksyqgf veevlalg
//
LOCUS       WP_010573418             193 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Leptospira kmetyi].
ACCESSION   WP_010573418
VERSION     WP_010573418.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..193
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22613
     Region          8..178
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkdksyiell enakagdlks wtelqnrfsr fayqhavkil kdedlsedvv qesfwdlyrn
       61 lnaikvleaf pillkravik hgdrilrkke nqslvfadlq qfeqnageth ltyfekerse
      121 ailknvnrls pedrkliely yyknftldei sksqgktlsf ikkrhlklkd ilrdgigeiy
      181 rpeaclrfls vaa
//
LOCUS       WP_010573455             113 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010573455
VERSION     WP_010573455.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..113
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12280
     Region          6..104
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(22,24..26,32,55,57..59,61..63,66..67,89,93..94,96)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            58
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 matltiqekk egnllvlqvh geidaktapd lklklessig ngvtqivcdf sgvsyiasag
       61 igvlnsilkf lkeksgelvf snikkevrdt mdlmyftkki rifesvkdal aaf
//
LOCUS       WP_010573482             137 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Leptospira kmetyi].
ACCESSION   WP_010573482
VERSION     WP_010573482.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..137
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=15592
     Region          1..>93
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mkksvlivdd ndryannlkv wfeqkgfetv ravdaaqgwe iyskdknrfh tivtditmet
       61 qtsglwmirk ihkdgyqgnk iiattgfdfp gvmffsssil pwfagigwmv pkvplkqgtv
      121 vflptslkkk irfetvv
//
LOCUS       WP_010573485             123 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010573485
VERSION     WP_010573485.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..123
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13823
     Region          22..112
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(31,33..35,41,64,66..68,70..72,75..76,98,102..103,
                     105)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            67
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 marvefdsly iettktslpn kevqlvvfng kvtnsnsfei srkihfifee evfniildls
       61 aleyinsvgv atiltliktv dqhsgkivig glnhflenvi rlmelpkkve iyhsveeakk
      121 afa
//
LOCUS       WP_010573543             126 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Leptospira].
ACCESSION   WP_010573543
VERSION     WP_010573543.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..126
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14309
     Region          20..114
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 madtkslfnd sfeyrdpalq krknarvkvt ldaemsikgk qerhpvtild igtggvalds
       61 rmtmfegdri hlharingke ltleaeiirs sgkkmnsifv niadehknei qelihkkffe
      121 kdkkls
//
LOCUS       WP_010573546             182 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Leptospira kmetyi].
ACCESSION   WP_010573546
VERSION     WP_010573546.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 182)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10632273
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..182
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20544
     Region          2..33
                     /region_name="Nudix_N_2"
                     /note="Nudix N-terminal; pfam14803"
                     /db_xref="CDD:464323"
     Region          37..158
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04511"
                     /db_xref="CDD:467545"
ORIGIN      
        1 mkfcsscgss vtykipegdn rsrhicdncg tihyqnpkvv vgsipvweer illckraiep
       61 rkgywtlpag flenretvee gaaretleea naeikivglq svysiphisq iymffladlv
      121 dgkfsvsses eevklfaine ipweelafts vyfalkeykd spvknslhmg strnrnyppk
      181 es
//
LOCUS       WP_010573673             235 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Leptospira kmetyi].
ACCESSION   WP_010573673
VERSION     WP_010573673.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..235
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25865
     Region          22..232
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mqssynrple mvgpieavhl pgnpdaytvi lfhgyganay dlsplsayld lpdgtnwlfp
       61 ngvleipvmp gyngrawfpi dmealqramm tggyrdfsdr ypaglesare kamemirtlg
      121 vpmekiiigg fsqgamlatd ivlhsevspa gllilsgtli setdwkrlae kkkeykffqs
      181 hgrmdqvlgy paakkleqll igagwkgemi afpggheipe vvlrgmnlyl rnitg
//
LOCUS       WP_010573696             398 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Leptospira kmetyi].
ACCESSION   WP_010573696
VERSION     WP_010573696.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..398
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45224
     Region          <114..252
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrnqivalif ilflslglfa epgdlkgeck pkewicvltr ndnnkiefyv qnrspsgefp
       61 fslyfnfsdl enyrpdvtlp fpyvskgsae pqkvftlnli nndkdrsyss siyvragdfn
      121 apknknviyr lpfesasrig qgyngkfthn gqfpyaldft lpegsavvaa regivitted
      181 kyklggttpy ykdkanfiqi lhkdgsiaey ahlkykgvlv qvgqtvrtge kiglsgntgf
      241 ssaphlhfhv fkptsdfqil dsfptafetd egvldelkeg vvywnpsvml pagkvffeed
      301 lkicsdilqk kpvnceesfn aqkrpilile irkprkydlq vevcspdsic kridwalqpd
      361 rifsvlsfdw slfpqqsgky riqvindiei iktwiver
//
LOCUS       WP_010573705             110 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010573705
VERSION     WP_010573705.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..110
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12188
     Region          3..98
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(19,21..23,29,52,54..56,58..60,63..64,86,90..91,93)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            55
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 meinhrksge tnivslsgsl diytsidlkt ffetninkdn knvvvnlekl nyidssgigm
       61 likqlnyvqd lngsffianm kpaiekvfkv agltsyfkti spaefssnfp
//
LOCUS       WP_010573841             145 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Leptospira kmetyi].
ACCESSION   WP_010573841
VERSION     WP_010573841.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 145)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 145)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 145)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12153064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..145
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16425
     Region          10..>111
                     /region_name="AAA_33"
                     /note="AAA domain; pfam13671"
                     /db_xref="CDD:463952"
ORIGIN      
        1 mneeeaksii lirglpgagk stlakilsen gkypvlsvdd yftdsstgqy rfdysknhla
       61 ykhceerark aaengtskif ldntftlswe mepyfqiasd fgytifvltv enrhngknih
      121 siddeslkkm askykirllp eelss
//
LOCUS       WP_010573737             206 aa            linear   BCT 01-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Leptospira
            kmetyi].
ACCESSION   WP_010573737
VERSION     WP_010573737.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..206
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22426
     Region          2..203
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mdlsyyieli gvgffalsga laaaekkshh hdifsafftg fitaigggtl rditlgnypv
       61 awvrdenvlw ailigfvitl lfanywpklk relfvfdsig igiytvigtk islatgvnpf
      121 gsvilgmisa ifggvirdtl inevplifrk eiyataclag atlyvllgyl nvnsdwntgl
      181 svclvvliri vavrfnlslp tfrlpq
//
LOCUS       WP_010573853             308 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Leptospira kmetyi].
ACCESSION   WP_010573853
VERSION     WP_010573853.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..308
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34798
     Region          84..306
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkknsirnaf vavlcllsla fllwslwnpl pivkfvlryt dvmerirkns plppkgvald
       61 htvevikvkn ttaiwldrkn sfqgvlvylh ggaylkgpfe tqwkyvsrmi rktsmaalvi
      121 dykmppgfpf phglegslel irelqkegsl anrwfllgds aggglalaia frlretkssl
      181 pqglilmspw ldlnmdnpnv dlvapedpml kkkflidsan qyapnadlkn plispvygdv
      241 kglppillqt gtsdillpdi rkfyekcken gvsiryeeyp eafhvfmmln plkearraid
      301 sqkefllr
//
LOCUS       WP_010573874             301 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Leptospira kmetyi].
ACCESSION   WP_010573874
VERSION     WP_010573874.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..301
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33766
     Region          53..300
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mskrfllkgi lgfifflliv ciggawyfae vllhprpphq cklehyifcn dpkadlglny
       61 envkyktsdg meisawwvpa nrpsdkvmis ihgrgatrre glryvklfhd qginvilpdl
      121 rdcgesqksf ssmgfherkd lqatldfvks kgmkstgilg fsmgaatsvl fmaeqpeiki
      181 gifdsgfadf vevvsfvakr dfglpkypll pfviffyetr gnletddlsp ekaiglispr
      241 pvlifhgtad ngvpyehglr lekaakepke lvtvvggeht klwqkdeklv sskilqliqk
      301 l
//
LOCUS       WP_010573891             276 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Leptospira kmetyi].
ACCESSION   WP_010573891
VERSION     WP_010573891.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..276
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31280
     Region          14..272
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mtekalnqsv vlnngismpi fglgvwktks gkecteavln aleagyrhid takiysneed
       61 vgkairesgi prkeifittk lwnadqgsdk arkalessle klgidqvdly lihfpvtskr
      121 mdswkelera yhdklcrsig vsnytithla ellkdsqitp avnqveyhpf lnqvdlfdyc
      181 kkhkiqleay splahgqkie dpkiakiakq ygktpaqili rwaieqdivv ipksvkkeri
      241 ienskvfdfk iseadmktln sldenfrtcw dpseva
//
LOCUS       WP_010573903            1090 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Leptospira kmetyi].
ACCESSION   WP_010573903
VERSION     WP_010573903.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..1090
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=118881
     Region          1..1077
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnlaslsikr pifitctvll ilvagylsln klgvdlfpnv tipvvtvtvp ypgaapneie
       61 tlvakpvede lstisgvkrv ksicnegvgt vvveftletd vkyaeqqvrd kvssvkpklp
      121 ddakepvirr idpadqpili ialradlpea elydianeev kqillttkdv gnvniyggrk
      181 reihveldrn klkehmipaf vvanrlasgg mnipagkvsk tdkelvyrti nefqspqeir
      241 dtpislfgne vpikigqlge vkdtvedets rayfngkkav fllvykqsgs ntvavaqavk
      301 kkvseinldl akrkgspelt aandssitid nniydvketi iigiiltiiv vllflgsvrs
      361 tlitglalpn sllgafilma iagftvnvmt llalslavgl liddaivvre nifrhremgk
      421 tareasiegt kevtlaviat tmtviavfmp iafisgvvgq flrefgltvc fallislyda
      481 ltiapmlsay fggkignhgn kpghghdaip eittqsakgk tktkgaaatt aleeiayski
      541 rsqnnaskgi lskifspilt vlgklesgld silsifnvfq swleekyasi lkftlkrpmf
      601 ilssavlifv vslvltkfip ktflpaqdeg kfsvtldmpp gtsvekmaqv aqqvdqkirs
      661 ykeiklvamf ntnrntnmfv emvpsknrtm nttqfkaflr keltefsfan pivkdidnvg
      721 ggqrpftltv sgqrgdvved yakklfarlq kspalldvdt syragapefr vvpdrerevl
      781 lgvpgttigt elrtlvegtt pavyrengve ydirvrlkds qrdlkdnfyn sfvpnfnnrl
      841 ipiqnvakae ettglatinr lnrnksveiy advnpkgpgm ggameevaki sqselplppg
      901 vkigysgqae sfkemgtsma iamglgvlfi ymvlaslyes fitpiaimlv lplalcgafi
      961 alfltqksld ifsmigliml igvatknsil lvdftnqlld qgkemkeaiv eagrerlrpi
     1021 lmtsfaliag mlpiaiglne asrqrtsmgv aiigglisst iltlvvvpaa fsyierlnqf
     1081 vrrnspnpda
//
LOCUS       WP_010573904             202 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira kmetyi].
ACCESSION   WP_010573904
VERSION     WP_010573904.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23006
     Region          3..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msamdqddvk hrimdkalel flkygyaktk meeiarilki srktlykhfe nknhllfeil
       61 trkhgimssk iqeiseddsl svhekiqain efkicqfpsg anefileird qapdhyayik
      121 evrmesvsks vqalikqgie kgeirkelnp tifaallnsa iemtatpell lnsplsmaql
      181 qgeiheilfy gimtcpmssk ss
//
LOCUS       WP_010573940             266 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Leptospira kmetyi].
ACCESSION   WP_010573940
VERSION     WP_010573940.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..266
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29428
     Region          17..260
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mglidqdtid lgsgskiltl slnnpetrns mtremglefk kiidglieap eknkprvvil
       61 tgkngifsag gnfellksfs trdyetnkkt mfefynlfls vrrldipvic aanghaigag
      121 fslafacdir vfsneskyqf nfvklgihpg mgssyivkel fgthianrll flaetlngee
      181 afrlglcnds vpqkevlgra temaialses aplalselkk ntydkeklea alrkeaesqa
      241 rnfissdfke tikaieqkrk pvfkgi
//
LOCUS       WP_010574022             355 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Leptospira kmetyi].
ACCESSION   WP_010574022
VERSION     WP_010574022.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..355
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39128
     Region          13..355
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mrdpakkels eyfirtsffl ivaftivvsl wglqllavpm vmallifyaf ngtinnlesl
       61 gvprilsiai lmlvisipiy lfinsvappi vstlnpllkn wkqdldeakf kyltvtvnlq
      121 fnefpsswne tirpdelikr iaelmheqvk gfvsyvptli gymiitplfa flfllngngm
      181 yknlialipn ryfemalmvt ykineqltny lkslmiqsai icvvsglgfy iiglpyfyif
      241 glflgvansv pylgpimgai pplffalvig gtgatelmts ilivvliaqi idnffiqpiv
      301 isgsvslhpi vvvgavtvgg aalglvgmli avpmaailkv tiqtlyssmk dhnll
//
LOCUS       WP_010574026             370 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Leptospira kmetyi].
ACCESSION   WP_010574026
VERSION     WP_010574026.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..370
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41933
     Region          1..286
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtripvllig lgriasllek dtlrnhpcth agaifsaegk krfslvgaid pieerrdrfc
       61 kdwnipktlc fesfkkwand lsssrnqktk tenrlsngss fdladclvii atpsethyel
      121 akkaidfgfr rllvekpvch slplarklak lcaetgtdlr vnherryhpv yrqvrrwiqe
      181 etygpvktir asvltsarap graildktgp lfhdgthavd llvwylgmpd rvvsvlrsyp
      241 nspveeqala lmtypkgetv fleaggmrny fqfeldiqtt darflvgnde vrywkskpsr
      301 kykgfksltp vsisekssag snpflnlyds lfrhfsgkps gitgdmeenl qiltlldtir
      361 rraekrilev
//
LOCUS       WP_010574128             183 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira kmetyi].
ACCESSION   WP_010574128
VERSION     WP_010574128.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..183
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21361
     Region          1..128
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 makdtrdlil ktslklfseq gyhgttmrqv askasmslgl ayryfdskea ilegiieshd
       61 kilkryvtde vvanpsredl ivnvsesiit lvkenedylr lywnlmlqpk ihrlkrrnih
      121 lvnmiffets kktirsikpn ytefeiknla sttigyminy ltnkkefsld dfrnylvhtl
      181 knt
//
LOCUS       WP_010574243             144 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Leptospira kmetyi].
ACCESSION   WP_010574243
VERSION     WP_010574243.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15740
     Region          5..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mqrfikkilv pvdgsesskk alemgiaiak aanasltvle vveefgplpg yyekapegkd
       61 rvkwiseqrf ekihspldes peiqwdrlvl egypadtive tatkgnydmi vigsrglsav
      121 grflvgsvsd rivhhatcsv tvvr
//
LOCUS       WP_010574361             216 aa            linear   BCT 01-JAN-2025
DEFINITION  toll/interleukin-1 receptor domain-containing protein [Leptospira
            kmetyi].
ACCESSION   WP_010574361
VERSION     WP_010574361.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Nimma,S., Gu,W., Maruta,N., Li,Y., Pan,M., Saikot,F.K., Lim,B.Y.J.,
            McGuinness,H.Y., Zaoti,Z.F., Li,S., Desa,S., Manik,M.K.,
            Nanson,J.D. and Kobe,B.
  TITLE     Structural Evolution of TIR-Domain Signalosomes
  JOURNAL   Front Immunol 12, 784484 (2021)
   PUBMED   34868065
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Essuman,K., Summers,D.W., Sasaki,Y., Mao,X., Yim,A.K.Y.,
            DiAntonio,A. and Milbrandt,J.
  TITLE     TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes
  JOURNAL   Curr Biol 28 (3), 421-430 (2018)
   PUBMED   29395922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..216
                     /product="toll/interleukin-1 receptor domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=24415
     Region          4..95
                     /region_name="TIR_2"
                     /note="TIR domain; pfam13676"
                     /db_xref="CDD:463954"
ORIGIN      
        1 mkafisystl dkyvaakiqn ildrfgiesf lahediqvss ewqsvilnel krsdlfvall
       61 skdyetspwc eqeagiaafr emtlvflsld gtipkgfvgk tqsakvreet lsicdlipgi
      121 ircnfsfgtn livdligksh sfrqaeknfq lilpyvsqmk ksqikellkr sannrqvyda
      181 gicrkryips llkdyrylls kktiailetg dvknas
//
LOCUS       WP_010574392             326 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Leptospira kmetyi].
ACCESSION   WP_010574392
VERSION     WP_010574392.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..326
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36716
     Region          20..222
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 makrkyrngl slfgysifhp inlflianvl iyilqlfagg tgileyyfal tpsrvfhgyy
       61 wqifsygflh eaygtpfihl ffnmyvfvmf gglickyipa wkftivyvas ilmggiavll
      121 aplfvevlgi hypmdlfqtt tlgasggvtg ilvlfgilfp etevfliffr mkaryaawif
      181 vgggfvadvi svyyfhspfv vsnschlgga vgatlvapwi lkgnffdsgn ifpkpeikee
      241 pspkpqsrsl sedldsqtrk nrdllgelar knsfseketf ltplqqtnvn lcppptfqpe
      301 dpfclrcewl pncslrklrm dqesgn
//
LOCUS       WP_010574436             741 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Leptospira kmetyi].
ACCESSION   WP_010574436
VERSION     WP_010574436.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 741)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 741)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..741
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81456
     Region          93..485
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mkkislfyif liflfiislg filqfgqsle lekesfhssq ieaqknpqaq knsikpverp
       61 dfldveavgk mfsghlkqpl srlllqlivi iiasrlfgkl stmlgqpsvi geilagillg
      121 psllglvfpe gfqllfpkes lstlqilsql glllfmftig meldlkilrn qaesavvish
      181 ssimfpfllg aglayfiyvp lapqgvdfia fclfmgigms itafpvlari ilekgltktt
      241 lgslaltaaa addvtawcvl aivvtivnag sfssgilmiv mslsymllmw kgilplmkra
      301 gnlyttkesm tktitafffl fiflsawvte aigihalfga flagvvmpdk kelrsnlvdk
      361 iedfsltvll plffaftglr tkfgllsssg lwpiffvilf vavlgklggs aiasrlsgkn
      421 wkdslaigml mntrglmeli vlnigydlgv lseeifsmmv lmaltttvmt gpglklverf
      481 faknelgakl gantsgmlis faqhsrglel lkiayglfpe kkkerevtav hlspdsnise
      541 thaekyesss ftpmkelsrd lninlktiyk tstnitkdii rivdegnygl lligaarsff
      601 sddilggkir tilnetdcna gilfssqled vknihilfgr ekdlellqia krlaanynsk
      661 lsivdlngsv neiptrikqs lkkdkvkils setgsadwkq fdlilcdldi wenhpefrvn
      721 elpkggglll irsvdgslle s
//
LOCUS       WP_010574456             445 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Leptospira
            kmetyi].
ACCESSION   WP_010574456
VERSION     WP_010574456.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..445
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=50349
     Region          66..444
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mnlfrsikka fqtldrksmp dsvlevlkae erngiiitny frylialffl vqiivnvhng
       61 dnefnliafs iyliltlaht iiirvcpdsv iqvfnyitlf aefalilgvl lfytftvqni
      121 dlgfalkntl nlfflfpiiy sllqfrirfv fialflfyai yytilwiavs tnqltytndw
      181 gryisgpevl iadvvagkpg lyfcfavmis mgifrtvsmv rrigiaegqk telsryfspk
      241 ivnemmenpg tlqsgnrqiv silfldirnf tamsenmdpk elgellsefr kimmecvfen
      301 ngtldkyigd avmatfgtph pspsaevdar navgcgvimq krlaewnllr ksegktpiai
      361 gigihtgevf agnigsdlhr eysvigdavn tasrieslck vlkksflisk etmellggky
      421 tlnrmprvkv kgkeeplqvy evmwg
//
LOCUS       WP_010574463             320 aa            linear   BCT 01-JAN-2025
DEFINITION  transketolase family protein [Leptospira kmetyi].
ACCESSION   WP_010574463
VERSION     WP_010574463.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..320
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34499
     Region          12..316
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mgapststat ekatrdgygd alhelgasrq dvvvldadls gstktnkfak afpdrffnvg
       61 vaeqnlvgha aglalsglvp fassfamfls grawevvrns vvypflnvkl vashggvtvg
      121 edgashqcie dfaimraipe mtvicpsdyn eckqiihaia dykgpvyvrv grpnvpvier
      181 enykftigka evmregkdvl viangvlvne amkaveelak eginatllnm atikpidkea
      241 ilkyakecka vvtceehnvi gglgsavsef lseeypvhvl kvgmkdqfgk sgtwkelldy
      301 fglrsknive takkaislkk
//
LOCUS       WP_010574531             158 aa            linear   BCT 01-JAN-2025
DEFINITION  cyclic nucleotide-binding domain-containing protein [Leptospira
            kmetyi].
ACCESSION   WP_010574531
VERSION     WP_010574531.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Wang,Z., Jiang,Y., Lu,L., Huang,R., Hou,Q. and Shi,F.
  TITLE     Molecular mechanisms of cyclic nucleotide-gated ion channel gating
  JOURNAL   J Genet Genomics 34 (6), 477-485 (2007)
   PUBMED   17601606
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Kaupp,U.B. and Seifert,R.
  TITLE     Cyclic nucleotide-gated ion channels
  JOURNAL   Physiol Rev 82 (3), 769-824 (2002)
   PUBMED   12087135
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Canaves,J.M. and Taylor,S.S.
  TITLE     Classification and phylogenetic analysis of the cAMP-dependent
            protein kinase regulatory subunit family
  JOURNAL   J Mol Evol 54 (1), 17-29 (2002)
   PUBMED   11734894
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Aiba,H., Fujimoto,S. and Ozaki,N.
  TITLE     Molecular cloning and nucleotide sequencing of the gene for E. coli
            cAMP receptor protein
  JOURNAL   Nucleic Acids Res 10 (4), 1345-1361 (1982)
   PUBMED   6280140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10034975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..158
                     /product="cyclic nucleotide-binding domain-containing
                     protein"
                     /GO_function="GO:0030551 - cyclic nucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=18100
     Region          14..128
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(83..84,93..95)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(115..117,121..123)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
ORIGIN      
        1 mqhtkeeilk qiylfsnfte delgaiaekt eykvydqgds ifhegneaka ffvviygtlk
       61 vlastekgdd vnvttiatgd hfgelpyldp gkrsasveam ersellripy dhlkavfekd
      121 knaslkfyqa ishflakrlr mlthdltyar elrkryti
//
LOCUS       WP_010574567             658 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Leptospira kmetyi].
ACCESSION   WP_010574567
VERSION     WP_010574567.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..658
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=74302
     Region          11..657
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnrstkyfdk lstiwddfep rkgqiqlsqk ieeslfngth liaeagtgvg kslaylipaa
       61 lssmereepv vistetkslq qqlllkdipm vskilgtdlr aevamgasny vckrklnhvm
      121 rdgtfgpemi phidsfnrwi rttesgrkqe ytgtasydfw nkitreadnc lgrncpnfsh
      181 syyflerekw krcnilivnh hllaahiasd fnilpefsrv ildeahnfpd iigssfrqei
      241 rsqeiqkllq qiwlpnkntg vavsigssel kdlvtkagds ltsffnalsg evplnfyspq
      301 rikrplkldk gafasvlagi teilqkhlsk iskdsddite kesalvleml sgrmeeiavg
      361 letfrqvddp slvywieppd qnskeiyyki cmepmspdei irdlfasrmq sviftsatls
      421 tsgndfkyfk kkigdlptsn ltvpspfpyq knallyvpre irdpvadpdg yhadlakqil
      481 wliemtqgnt fvlftsfksl klvyeairph tdlplfsqsd lgpdgakqmy letpnsvlfg
      541 vstfwqgidi rgdklrsvii aklpfqvpnd pvletksekl kesggnpfae lqlpyactvl
      601 kqgfgrlirs gtdtgvvsil dprmftktyg kdllkslppa kliqnredlr refdnlpk
//
LOCUS       WP_010574660             731 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Leptospira kmetyi].
ACCESSION   WP_010574660
VERSION     WP_010574660.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..731
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82757
     Region          2..719
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mdpllvglne eqkkavlqvs gpvlilagag sgktrvithr ianllvnhgi dricavtftn
       61 kaaaemlerv kglvpfipan lqiktfhslc lyilrreasf fgfesgftvy dttlqesllk
      121 qvvkdlsldp kfykpsmlgn yisglkdkml speaylekeg rtdfsktvsa iykeyekrkd
      181 asrafdfgdl iwktvqlfqk spdaiakyrh kweyvmvdey qdtnkvqyel vlllagekkn
      241 lcvvgdddqs iyswrgadig nilnfekdfp nstvikleen yrsssniila askvisnntq
      301 rkqkeiftnn psgspvvlne feneseeahg titrirsays sgteykniai fyrtnsqsry
      361 feealrnvgi pykifggfrf fdraeikdfi aylnvvsnpl dsvsllrivn ypprgigdsg
      421 iekirefsle kgislletlg qediplkkaa kskgkelynl fsdlieksek dsspseiale
      481 llnrsglmsy lkeegteesv arlenlqeli nsieeyekns dspsleeyln qislltseed
      541 tkeltdyvnl mtvhnakgle fkmvflsgle egtfphsmsl edshlgdeee rrlfyvaltr
      601 areelfmsyc rtsrkfgkve dripsrflse vpkecfgdrg ygarertarr pqgpplaskv
      661 reteeefdtg fspapspdna flkpgdrvkh kqfgigtilt vsgkdkntkv airfgnvekn
      721 ffvaytplek l
//
LOCUS       WP_010574671             222 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Leptospira kmetyi].
ACCESSION   WP_010574671
VERSION     WP_010574671.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..222
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23991
     Region          6..222
                     /region_name="carb_red_sniffer_like_SDR_c"
                     /note="carbonyl reductase sniffer-like, classical (c)
                     SDRs; cd05325"
                     /db_xref="CDD:187586"
     Site            order(10,12..15,35,54..55,79..82,102,127..129,145,149,
                     174..178,180,182..183)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187586"
     Site            order(55,61,96,101,104..106,109,112..113,131..137,143,
                     146..147,150..151,154..155,157..158,161..162,221..222)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187586"
     Site            order(103,129,145,149)
                     /site_type="active"
                     /db_xref="CDD:187586"
ORIGIN      
        1 mtprnvfitg snrgigleft kqfiakgdrv falcrkasnd lvklkptqif eevdvlnsns
       61 irdlsaklld tkidilinna gilipdnlqs ldeenvftqf lvnalgplki vkallpslga
      121 naklifltsr mgsiadnssg syygyraska alnaiavsla rdlspkgisv gifhpgmvat
      181 emtgrqgipt tesvqglier ieslnlnnsg kffhqngeel pw
//
LOCUS       WP_010574696             201 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Leptospira kmetyi].
ACCESSION   WP_010574696
VERSION     WP_010574696.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..201
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22416
     Region          3..201
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 meflnilvni fseygyiavf lvlilcgfgl pvpedislvs ggviagfgka dphymflvgm
       61 agvligdsav fligriygvr vlqipfisri vtperfakvq dkigrygnwv tfmarfmpgl
      121 rmpiyltagt sdrisfyrfv aldfmaavis vpvwvylgyf gaynfdtlmr wvhngqltvl
      181 gllgtvlllf giaywirkkr s
//
LOCUS       WP_010574781              87 aa            linear   BCT 01-JAN-2025
DEFINITION  HPr family phosphocarrier protein [Leptospira kmetyi].
ACCESSION   WP_010574781
VERSION     WP_010574781.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..87
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=9278
     Region          1..86
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 mkeillkine ngtgmharpa svfvncaskf pceitvvkdd vvvngksimg lmmlalapgn
       61 efkiqvagek edealealsn ivnndfv
//
LOCUS       WP_010574810             550 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Leptospira kmetyi].
ACCESSION   WP_010574810
VERSION     WP_010574810.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..550
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60133
     Region          35..549
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mseakyslen pfqstsepdv pktrglyeea nelgkdllsk plagggvdri lvqhskdrmt
       61 vwerikvlte qepnilyqnw gksldgaslv tgilningrd vaiyghdftl ragsmdatng
      121 sklarliyma gehgipligm ndsagayvpa gvggldgyse aftalrkisg vvpslmlmfg
      181 fnagggaylp rqgsfmiqcd ntffgltgpg vvksvlgedi saddlggpkv hgqsgvvdiv
      241 tgdelgslrt alrllsylpd nnhsfapfhp tsdptdrfiy eeeilfkktf nsptgmntpf
      301 ditlylqnic dhgqyfeiqg qrsrnlvtaf grigghvvaf vannsavssg qidisaarkg
      361 trfirfcnly nipivfledt tgflpgkeqe qngivlegrk lldsiidirt prltliirna
      421 fggayacfns yhvgadmvfa lptariavmg pagkdyvykd evsaiqreyq envkkgmsek
      481 eaivvrdkkl qvlstqyeke lmnpkealsl gsvsrivlpg ttrsilfqnl dylirhykpa
      541 plsgpqrefe
//
LOCUS       WP_010574830             134 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Leptospira kmetyi].
ACCESSION   WP_010574830
VERSION     WP_010574830.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..134
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14750
     Region          16..118
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 mesqtvskgq lwtgrilsgl aiafllmdgv gkffldympk eamedaakla ypnsvmpwlg
       61 ttlivctlly afpktsvlga illtgylgga vashvrilnp wlshilfpvy lgffiwggly
      121 lrnlevralv pwkk
//
LOCUS       WP_010574847             665 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Leptospira kmetyi].
ACCESSION   WP_010574847
VERSION     WP_010574847.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..665
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74622
     Region          1..628
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mswkeelnpa qleavltqeg pvlvlagagt gktktivsrl ahlvssgipa ssillltftr
       61 kaaremilra ssigdskcad vqggtfhsfc sgvlrrfapv lgissdftil deadvldvfq
      121 flrnekdfgk tksrfpsnet lvsihgeiqn tgknlqaile kdypqfiqrf editlifgdy
      181 kiyksersll dyddllyftk dllsnhpgvr stlsekyrfv mvdefqdtnk vqahiaclla
      241 sehsnlmvvg ddaqciytfr gasvrgildf pkifsntktv fleknyrstp ailnlanavl
      301 hnfaekydky lftdnengpv pavlqftdel eeaegiadil lqkkeegipf qrmsvlfrag
      361 wnsnqlelvl akrnipfvkf ggrkfietah ikdllsflki llnpldsvsw irvlklipgi
      421 gnaksndlle kirmssgsfe vlseekgssi ekylspllnl yrkhkegssv vkniaadfid
      481 yyrvllekny ddykrrsedl dsvlgfalky dslgaflsdl tmdsaslsld kikpdnqesd
      541 llnlstvhsa kglefdvvfv lnstegvfps nkntdteeer rlfyvaitra rkelfltrps
      601 laqsrsgpyy tklsrflsei qspekvyelk lmsgksankd sfasqgtpak pandsfariq
      661 dyfgn
//
LOCUS       WP_010574904             104 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: STAS domain-containing protein [Leptospira].
ACCESSION   WP_010574904
VERSION     WP_010574904.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..104
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11446
     Region          10..102
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(22,24..26,32,55,57..59,61..63,66..67,89,93..94,96)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            58
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 menfnteilt egttctiriq gsislknafa lkeliikkhg egftdivldf sgdayldssg
       61 igaifnsqky vterngslkl knisrdvmti lkianldkhl diir
//
LOCUS       WP_010574953             434 aa            linear   BCT 01-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Leptospira kmetyi].
ACCESSION   WP_010574953
VERSION     WP_010574953.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..434
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=47175
     Region          2..434
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mprnykpeti alhggqspdp tttsravpiy qttsyvfkdt dhaarlfglq efgniytrlm
       61 npttdvleqr vaaleggvaa latasgqaae tlallnives gqeivasasl yggtynllhy
      121 tfpklgikvh fvdpsdpenf rkavndktra fyaetlgnpk ldtldleaia kvahesgvpf
      181 ivdntlpspy linpiehgad ivvhsltkfl gghgtsiggi iidsgkfnwg ngkfknftep
      241 dpsyhglkfw dvfgkfepfg gvniayiika rvqglrdtga alspfnawqi lqgvetlplr
      301 irkhsenala vaeylskhpk vswvnypglk tdknyalakk yhkrdlygai lgfgikggva
      361 eakkfidgle lfsllanvgd akslaihpas tthqqltpee qasagvtpdf vrlsvgleni
      421 edilfdleea lkkv
//
LOCUS       WP_010574958             254 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leptospira kmetyi].
ACCESSION   WP_010574958
VERSION     WP_010574958.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..254
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27856
     Region          1..241
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mepfaielkn vhksfgkrki lagmdlhvkk getlvilgps gtgksvtlkh itgllepdag
       61 dcyifgesis rvspkvktkl rarmgvlfqs galinwltvf dnvalplreh klasqekike
      121 ivmeklklvd mviakdnfpn disggmkkra giaraittnp eiilydepts gldpvmsnvi
      181 nelvlkiqke tgaaqvvvth dmssaymiad risfvykgki vftgtpqeiq nsdneliqqf
      241 ihgkttgpmi letk
//
LOCUS       WP_010574979             224 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Leptospira
            kmetyi].
ACCESSION   WP_010574979
VERSION     WP_010574979.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..224
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25812
     Region          13..>158
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mivqekkpqe lledriftvs nflsvsrvfl lpffiaftkt yisspektef llyamltcll
       61 avltdyldgf larllhqesv lgryldpvcd kivtvgglsv ivhyfrfplw iliayivrei
      121 lgvwlgsfly lkrgiqgkpn wwgkfgvglv aiavlwymci pliefripge silkhpeisg
      181 yvlvlillag ifayskrywn ivfhpesiqi dpedkktrkk yelv
//
LOCUS       WP_010575025             448 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010575025
VERSION     WP_010575025.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..448
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=51986
     Region          <17..244
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(49,53..54,57..59,61..62,66,69,78,148,150,154..155,
                     158..160,162..163,167,170,179,181,183,187..188,191..193,
                     195..196,200,203,212)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          49..78
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          80..112
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          148..179
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          181..212
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 metqhidsrl wkeigkykad lkkiegylqq gadvncksge fggredwdns plhiavnaer
       61 ldivdllleh ganinaknre gytpiykipw krkegfelfr slrqrgadlh aktdtnislv
      121 hcaalgenlp ileyllenel elnqqndhge tplhwtvhyh cfksaqflln hgaaidiqnr
      181 dgrtvlheas qreyqklikl flefkadrel adaegkkard laqkertill ldkglvrnhd
      241 pelnslvqsf sidqkeslda irveireqlq nefsridrkn liecvakpll dlksewegsy
      301 pdalvvvfew agsaqtpfsg yafprgytrf evtqnsivfr eetedktsdq ssefsedend
      361 ddeeenpfgd pvfedyengi efsdafegie eildrtdrde ywivknlyns flafllqetf
      421 sriferdsfw flfgvehdqk pfllfksn
//
LOCUS       WP_010575057             206 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Leptospira
            kmetyi].
ACCESSION   WP_010575057
VERSION     WP_010575057.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Sinha,S.C. and Sprang,S.R.
  TITLE     Structures, mechanism, regulation and evolution of class III
            nucleotidyl cyclases
  JOURNAL   Rev Physiol Biochem Pharmacol 157, 105-140 (2006)
   PUBMED   17236651
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..206
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016849 - phosphorus-oxygen lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0032555 - purine ribonucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=22908
     Region          46..193
                     /region_name="CHD"
                     /note="cyclase homology domain; cd07302"
                     /db_xref="CDD:143636"
     Site            order(49,51..56,91,93..95,98,149..151,155..156,159..160)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(51,95)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(56,68,71..72,75,79,91..92,143,150..153,156)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
ORIGIN      
        1 mafrrtigas asedrlekli qdrlkpgadk skidqriwdl fgedwcvift dlsgfsrgve
       61 kfgiihflqt iheserilip iiedhdgill ksegdsflvi frnvgkgies aikmqqelvs
      121 ynqdkipeek illcvglgyg kvlkigdtdv fgsevntask lgedmaeage ilvthsvyeq
      181 vsekhlkfet lseapagtsk ayklvy
//
LOCUS       WP_010575060             292 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Leptospira kmetyi].
ACCESSION   WP_010575060
VERSION     WP_010575060.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..292
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32767
     Region          2..262
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mirlehfpal kktktsshkn ppilfvhgaw hgawcwkdcf vphfqkagye vysmdlrghg
       61 nspngngsfr wnsirnyvqd veevlgrlpe tpilighsmg glvvqktlek tnapkavlla
      121 svpphgvfri tlellvkfpt kflkvlgtls llplvedkki arelffsesi gekkaleyas
      181 kmqnesflaf ldmllfclps pkkvktpilv lggekdrffv pwevkrtaka yqteaeifsg
      241 ighnmmldtg wekvadriea ylgntpalav etkkqksapk kkakpkkkak kk
//
LOCUS       WP_010575069             484 aa            linear   BCT 01-JAN-2025
DEFINITION  catalase [Leptospira kmetyi].
ACCESSION   WP_010575069
VERSION     WP_010575069.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..484
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54751
     Region          2..483
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mskktlttag ghpvpqnqhs vtvgargpil iqdthliekl ahfnreripe rvvhakgaga
       61 ygtltitkdl skysrasvfs kagkqtplfl rfstvagekg sadterdprg faikfyteeg
      121 nwdlvgnntp vfferdplkf pdfihsqkrd pvtgyknpfr mwdywakape alhqmtilfg
      181 drgipdgyrf mngygshtfg lwnakgerfw vkfhfksmqg iknlsaekas alagtdpdya
      241 trdlfeaier kefpkwkfcv qimpekeaet ykfnpfdltk vwshkdypli evgvmelnan
      301 pknyfeeveq aafspsnmpp gigaspdkml qgrlfaypda qryrlgvqyq qlpvnkarns
      361 vnvyhrdgsv kfqydgnydn yepngfdgpa qdssyseppl risgdadryd shqgnddysq
      421 agdlyrmmsa eererltsti astmrglpkg livanlkhfy kcdpeygtkl aektgvnvad
      481 lkkd
//
LOCUS       WP_010575070             195 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010575070
VERSION     WP_010575070.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..195
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=21573
     Region          <33..>156
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(47..49,51..52,56,59,68,70,72,76..77,80..82,84..85,
                     89,92,101,103,105,109..110,113..115,117..118,122,125,134)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          70..101
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          103..134
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mnsqsqtgfa dlgqgrisrq alsdfsdawt qyrksmraen pvfdsarngd vdslriqips
       61 lsdleeknak gytllmlaay ngreeavrfl isigadvnst dlggnsilmg aafkghakiv
      121 elllqagadk nyknskgqda fqfsnlfgrt evsalledss snqnrtrtrv rfdrflsflk
      181 swilflsqlt kgekq
//
LOCUS       WP_010575124              73 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF167 domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010575124
VERSION     WP_010575124.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..73
                     /product="DUF167 domain-containing protein"
                     /calculated_mol_wt=8072
     Region          1..71
                     /region_name="YggU"
                     /note="Uncharacterized conserved protein YggU,
                     UPF0235/DUF167 family [Function unknown]; COG1872"
                     /db_xref="CDD:441476"
ORIGIN      
        1 mkftvlvkpn skkvffrkee dgsitvavre palegkanea vieafseamn lpkrkirils
       61 gekgkrktve vdl
//
LOCUS       WP_010575162             401 aa            linear   BCT 01-JAN-2025
DEFINITION  CapA family protein [Leptospira kmetyi].
ACCESSION   WP_010575162
VERSION     WP_010575162.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..401
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=44640
     Region          60..378
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 msfyrsklfi tcsfvflfls clpeflknss sensetdsps alailqdkid avlhpehnhd
       61 pellkvlagg dvmfnwgird tiqkhgeiap veglkslfge adfrmvnlet pvvasktees
      121 kkayiftahe kdldslkflg vdmvflgnnh sfdhgpngmv etlsilkknd ilnvgagkkl
      181 pevldplrls lkgsdlrihs vtaiaeqahy atpfksgvap fllpslqssf ferrpplkrg
      241 vpysppvriv slhwgveysp fptpdqrkia ralidsgvkv vighhphipq gielyrggvi
      301 lyslgnlifg srnsylnhnl iailhirknv letvelvpif gkfqkedhki rpvqgqeake
      361 flheiavlss elgtklrvee erafldlttn stltpaskrk k
//
LOCUS       WP_010575205             230 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Leptospira kmetyi].
ACCESSION   WP_010575205
VERSION     WP_010575205.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..230
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26482
     Region          3..220
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mrkiliiaah pdddilgcga fifkhrndce frvvfiaegs tcrfsadqiq ssealkqiei
       61 rtasakksle vlgvndykfy dlpcgrldqv piidinkiie neiktfkpet vmihsetdvn
      121 ndhrivarsl amaarpvwpd cdlnilsfev lsttewnltd pfvpnlfeei sedclkkkwe
      181 alecyyteik efpyprsyvg letlaryrgm qsgfklaeaf kiirwknkfq
//
LOCUS       WP_010575240             138 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Leptospira kmetyi].
ACCESSION   WP_010575240
VERSION     WP_010575240.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..138
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15485
     Region          36..137
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mnefrifedf hklqnrfssf wdpfsanggs ayptlnihkg adeititalv pgidpnslei
       61 tvsgnqlrle gdalanrpkd sydtnrverf hgkfrralel paevdsektt aefkngvlvl
      121 tlpiresvkp rkiqiktn
//
LOCUS       WP_010575256             154 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Leptospira kmetyi].
ACCESSION   WP_010575256
VERSION     WP_010575256.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..154
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=16690
     Region          2..149
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 msseidhqyi lfslgdeeya ipislvdeii kisnliripk aksyfagimd irgkvvkmvd
       61 lavkltvprd geveydraiv vkvngqsvgi ivdkvanvvl fppesinppp psvkgisgry
      121 itgigkkddr fiiiidveki lgseelaelg snvg
//
LOCUS       WP_010575296             296 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010575296
VERSION     WP_010575296.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13837771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..296
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=32685
     Region          7..53
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
     Site            order(8..9,12..14,16..17,21,24,33,35,37,41..42,44,46..47,
                     51,54,63,65,68,72..73,76..78,80..81,85,88,97)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          35..63
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          51..295
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          65..97
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          99..126
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          130..161
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          163..232
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          234..265
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 maqkisvhda sqngdlemlr lliekgenin aknkngftpl hlaknletak lliqsgadvn
       61 ardkdsgntp fhvsiqfnqt liakllieng adinakndsl rtpiffadre stlkfllesg
      121 avlddqkdaf graplyysil herlkvakll iqsgadinvr dergmtplif airselfefs
      181 kllieqgadp nlkdekdgrt slmfllggtf lkknldlaes ilqkgadida tsnsgstalh
      241 fatfhndlea vrflldrgaq tnlknrfdkt plniaiennh aeivallkef peskns
//
LOCUS       WP_010575328             347 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Leptospira kmetyi].
ACCESSION   WP_010575328
VERSION     WP_010575328.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..347
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=38439
     Region          6..240
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mffneialfi tayasfllsa icgggaglil ipvlgaflpi qfvpaalsig tfassasrlf
       61 affqkirfdi vrwflppava avwlgawliq yvnplfmeaf igiflisnlp ilfkkensse
      121 kyqkpktfyl aiigflagfv sgitgavgll fnkfylrsgm skeeivatra aneiflhlik
      181 lvlyalfgli ngktiligsi valaalastw smkkvlnwin eilfrkigyf amtisgvlll
      241 sqsaigfass nradvsfvpi qkgaeaklgw qqasfsleft wdegfeieqv vpitdltper
      301 qsnllntkrd lnakililea vysfdknsye ayfygdgkli rkiefke
//
LOCUS       WP_010575453             674 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Leptospira kmetyi].
ACCESSION   WP_010575453
VERSION     WP_010575453.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..674
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77394
     Region          1..656
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mklnpeqeka vrhvdgpili fagagsgktr visnriahli enagvpagki valsftnksa
       61 remeervrkm iprqklkgiv lstfhslgln ilkkhigllg ykhpflllnq ndqegfvttl
      121 liankvelkk akvsevlgki sriknsgpsy reyldsslve sdqianlifd syqnslkeqn
      181 sldfddlill pgvllkefpe vreeyhkkfq yfmvdefqdt nqtqyvflrs lmgenrnlcv
      241 vgdddqsiya frgsdlslil gfendfpean vvrllenyrs tqviiqgans liknnlsrrs
      301 kelfssipgg rkiryiermd ekdeaayvvd cireemikda rvgsqiailf rtnfqtrpfe
      361 eelrsrsipy klvggynffd rkevrdmisy irliantrdd asllrilnyp krgigpgsis
      421 lihekaahmg eslyeilfrv cespdfipsl qkkiqseiyn fvnliertkk kfstapkmyf
      481 afrefiqevg iekeilleek dekvakarsf nlselvnmms yfeenhdspe kptlfdfinr
      541 lnllmedetp seedkednrv qlltihqskg lefdsvyvag meegilpnsr vlteessvde
      601 errllyvamt rakkhlcltg aanrrkfgeq matqasrflt eidsetmdwv sndevrqqet
      661 ddffaelekl ktgs
//
LOCUS       WP_010575454             192 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Leptospira kmetyi].
ACCESSION   WP_010575454
VERSION     WP_010575454.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 192)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..192
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22097
     Region          55..184
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mkpfnpeeyd plsnlwsksd rkdmiqtpif klvswhttsp dkkvskdffh lesldwvnvi
       61 altpenkill idqyrhgihr fsleipggia ekktllesaq aelveetgyv seeweylgkv
      121 tgnpailnnw chtfvaknvr klhdqdldds eqieifetpl rnvpkliedn ilhhgmmvaa
      181 lgmyfiknpi qn
//
LOCUS       WP_010575506             293 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Leptospira kmetyi].
ACCESSION   WP_010575506
VERSION     WP_010575506.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..293
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33701
     Region          16..292
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 msfeidflks inpfillkln erglaeelil ivyfilflil sykviilvld ffkptidvts
       61 rynrrkmarm sfvilglitl lpvvfsglsy lptvmglaga givislkdit lnfvgwffih
      121 gsngfevgdr ieiegvrgdv inigmnrftl meissdpksd qstnrlvhfp nhfvilrqvi
      181 vvkdkmnyvw demrikipyd sdfekaeell ngiirnnaii dqgeidytlq elsknylvrl
      241 gktspivyls leeggilfsl rylthvrerr dmktkishqi lkefkqfpgi ril
//
LOCUS       WP_010575549             812 aa            linear   BCT 01-JAN-2025
DEFINITION  penicillin-binding protein 1A [Leptospira kmetyi].
ACCESSION   WP_010575549
VERSION     WP_010575549.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 812)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..812
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=89390
     Region          12..706
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mksiglhrts kallviallg glffgyilse vdeggelaml asyqpttptr lydingvvfa
       61 elykhkqqll kyqdipphvv qaflsvednn ffnhfgidfm ailragivnv isgrikqggs
      121 tltqqlaktv lqnrkrsfar kfiealftlq ieqeyskeei leiyfnliyl ghgttglasa
      181 advyfqkdvs dldiaeaaml arlpkapvky spfknpaisk gahlsvlrlm aeqgyipadk
      241 vqsihddfwn kywpvvitqs psqstwgnrl nkaphfteyv rqklekelge dkvytgglkv
      301 yttldarkqe iaqeelsrai kkhddlvsgv tvnysggadr glvglyylmg sifpvgmpfv
      361 sklddkanyr valerelida adiltiltpg enesaaisef qkqtavfgkn lhvegaaiti
      421 epstgyiqtm vggyeftpkn qfnratmarr qtgsafkpfv ygaaiqervv gsgtgimdap
      481 lttlteegeg wspqdfdgdf lgmvplsral slslnivsvq vflrtgpdav idfssrllgv
      541 npnrfppspa lalgiaeltp lemalgyati anngrrvipf svryvidqsg nvvyneeikv
      601 qeelqrqakd gsiqvisegt ayilkkmltn vamagtaamg lrdpdkgnyr gtaagktgst
      661 ssftnawycg fdpnyttviw lgfdkssisl grgqaasvla vpiwgrmynr fyggqnypsf
      721 gedimpdevq gggtcayngl spkpgvcpvt qnltlkpitv agvtkavmgn rqcdgerdhh
      781 ksmdfreflq keyqisdeel gktdrkfkpr te
//
LOCUS       WP_010575644             100 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF485 domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010575644
VERSION     WP_010575644.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..100
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=11436
     Region          1..99
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 mktpahklvd epefkklvst rwivsftlla llfvsyygyi ltvafypell vrkvgsfsnv
       61 gilasalvil fswfltliyv vwanrsydkn vnslkrkled
//
LOCUS       WP_010575663             262 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Leptospira kmetyi].
ACCESSION   WP_010575663
VERSION     WP_010575663.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..262
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=29103
     Region          7..>249
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 msripflefk evsktfslgk gntfsavdrv sleiekgeif giigttgagk stllrfpnll
       61 erpdggrill dgsditdlqg knlrrhrqki gmvfqqfhla snrtvfdnia fplkvsgtgk
      121 aeiarrvrel ltlveipeke tvypaqlsgg qkqrvgiara lanhpelllc deptsaldpe
      181 ttrsilkllk qiretlsiti lvvthemevv reicdrtaim drgkiveldd thsffanpks
      241 eaakkilgsf ydsktfaenr ip
//
LOCUS       WP_010575707             182 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Leptospira kmetyi].
ACCESSION   WP_010575707
VERSION     WP_010575707.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..182
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21193
     Region          9..168
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msvtldnvey lyksyydklk ffflksgitt etaeelcqet fikvynhrek fdatkgsest
       61 wvysiarnel idfyrrshke knlvefsswe nlvssyessv ykleeqkilm eklkksisll
      121 kepersivil hcihgksiae tseqtgvaqr tvsrrlvsal tllreelkml gidktwlegv
      181 ke
//
LOCUS       WP_010575739             412 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Leptospira kmetyi].
ACCESSION   WP_010575739
VERSION     WP_010575739.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..412
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46318
     Region          70..386
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 miailknrrs pfylattfli lllfalfast lafiftgvli lillihplll nwigklygqe
       61 diadevhfak tkdgwnlalh rhippqpnrq lapvlvvhgi atnkfvvdld rrhslpyylk
      121 lrgyevyavs lrgcgrsyhe sptryedftf ddivkydvpa midkvkkisg sdrvsyvghs
      181 mgamilyshf cmsehkkdtk diaafvslgg pgnlnhigit ligllsrfpr arkmldlkfg
      241 asilaplage lytpideily npkvtssktv kkimknaien isdgvteqfm hwietkrmhs
      301 lngfydyvel qknisvpalf iagekdviat peavrsvyen agskkkefrv iskangssdd
      361 yghaclvmgd raeddvfqyv esflkkhglr sqpgiaakik egilstfsrf rr
//
LOCUS       WP_010575785             391 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Leptospira kmetyi].
ACCESSION   WP_010575785
VERSION     WP_010575785.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..391
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43624
     Region          1..385
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdftipkeve eikkkirdfv etyaipaevh ydydhgrmpe kiteelrkkv kelglwtphl
       61 pksegglgld mvgtaiifse lgrspiapyl cncdapdegn mhllhiaand eqkkkyyypl
      121 vegkirsafa mtepppgaga dpqtlttnav kdgtdyiing hkwyctgang agflivmskv
      181 adsfrrttmf lvptdapgyt mvreigvmgs hgpgghcelk fenvrvpesa ilgrvgegfk
      241 wsqerlgpar lthcmrwigl arrsmeiare yaikrevfgq riadhqgiqw mfaesaleie
      301 sgymltlkaa htlrsgedar qiismakwqv setlckvidr aiqicgshgy grdmklelfy
      361 rdaraariad gpsevhkmvi grnlvsgksd f
//
LOCUS       WP_010575817             426 aa            linear   BCT 01-JAN-2025
DEFINITION  amidase [Leptospira kmetyi].
ACCESSION   WP_010575817
VERSION     WP_010575817.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..426
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46348
     Region          15..426
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mkeqapnsee nikdteytyl sinelgelir nrkvspvslv sdclkrierl npllnafitv
       61 tteqalqeaq vaereiesgn wkgplhgipi gikdmfdtag ikttaafvhf qnripkrdai
      121 avtrlkdaga ivlgktnqhe laagttsvqs hygtvhnpwn enyiaggssg gsaaavaagl
      181 cyatldtdai gscrlpascc gvfgfkatyg fvnlqgvldg epvdesiltl ahagvmtrsa
      241 qdtailfkal ldpqddrnkk ilewkfnanr tasfkigfpk nlnaseeirt nfeavkkkle
      301 algntlceid vplspdfdls rvqehrsdaa kilfsdcdvl ilptttqtvl kiadasaqgp
      361 lalssantff anyygipais vpcgfssdgl pigfqivskq neeerilela dryqnetyrr
      421 lkhpil
//
LOCUS       WP_010574949             275 aa            linear   BCT 01-JAN-2025
DEFINITION  flagellar-coiling protein FcpB [Leptospira kmetyi].
ACCESSION   WP_010574949
VERSION     WP_010574949.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wunder,E.A. Jr., Slamti,L., Suwondo,D.N., Gibson,K.H., Shang,Z.,
            Sindelar,C.V., Trajtenberg,F., Buschiazzo,A., Ko,A.I. and
            Picardeau,M.
  TITLE     FcpB Is a Surface Filament Protein of the Endoflagellum Required
            for the Motility of the Spirochete Leptospira
  JOURNAL   Front Cell Infect Microbiol 8, 130 (2018)
   PUBMED   29868490
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Eshghi,A., Pinne,M., Haake,D.A., Zuerner,R.L., Frank,A. and
            Cameron,C.E.
  TITLE     Methylation and in vivo expression of the surface-exposed
            Leptospira interrogans outer-membrane protein OmpL32
  JOURNAL   Microbiology (Reading) 158 (Pt 3), 622-635 (2012)
   PUBMED   22174381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF047844.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     gene            1..275
                     /gene="fcpB"
     Protein         1..275
                     /product="flagellar-coiling protein FcpB"
                     /calculated_mol_wt=31922
ORIGIN      
        1 mklqklflvv lvaistavfs qqnsnadqks qsdaqlgqsi leterkldek vfelnqrltr
       61 htvlmkmkvr vlpfrtvlfk gkanndecvp ainqedpann cirvevydfi rdeerglnkn
      121 vqgslakyme iyyegqnsnd peprteaprn inklkskiyr nnmiledkii sevmdrgpnt
      181 qpshndkvev ffqkdnypey grpetpaekg vgkyilagve ntkthpirns fkkefyikhl
      241 dqfdrlftki fdyndqlgne nykenvdalk eslry
//
LOCUS       WP_010575832             216 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira kmetyi].
ACCESSION   WP_010575832
VERSION     WP_010575832.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23728
     Region          24..>131
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnpkskpkna tngssivrsk pplqersqar valvletaer mlaklgpeet sipeiakksg
       61 vprasiyqff pdkyslfthl aekhlakvge ilaakgskdt klswqklvrv lvnaasdyyd
      121 stpvasilvl ggpfsrnayl aqeitidhig agvriqlskl dkpfllpkkp dvatlgveia
      181 facmkrgyyq enriskmmrd qatdaviayf sswess
//
LOCUS       WP_010575833             145 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Leptospira
            kmetyi].
ACCESSION   WP_010575833
VERSION     WP_010575833.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..145
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16603
     Region          12..144
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 metrlnyatv ypeslqamlk meefakqggl dpvlyelvki rasqlngcaf cinmhtkdlr
       61 tmgeeekriy lldawkeaqf ytekekaale ltevvtkisd kgvpdetyer vrkqfnekef
      121 valivlinti nswnriaist gmtak
//
LOCUS       WP_010575887             329 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome-c peroxidase [Leptospira kmetyi].
ACCESSION   WP_010575887
VERSION     WP_010575887.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..329
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=35455
     Region          53..326
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mkqstvgllc lallgsvlvs cgpsektkkl iddskkifgt ipdkmpggea dtpelvqlge
       61 klyfekrlsa ndtqacnsch nvvgkaagvd nlptspgafg kngdrnsptv lnagfhvaqf
      121 wdgrakdlke qakgpilnpv emampsaaev ekkisgiaey kdlfakaypk etnpityenl
      181 agaiaafert lktqdrfdef qkgdhkalss eeqeglekfm atgctachig pllggnsfrk
      241 lgqvnpyent vdkgrqsltk naadafvfkv pslrniaitg pyfhdgkvat leeavkkmah
      301 lqlgkdlsds dtksivtflk altdknrsn
//
LOCUS       WP_010575895             173 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Leptospira kmetyi].
ACCESSION   WP_010575895
VERSION     WP_010575895.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..173
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20197
     Region          1..171
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mklsqdhdfs lfyqnykdsi ykvirflsnd peevediaqe vflniykafp nfspergsfy
       61 twaaaiaknt yftyrknrkk dlllqenasi eslpaeddfi rtieakivee elreiiatlp
      121 epeksiillk einnftlekt sqalnissrt vsrkllkald llreelerrk vvl
//
LOCUS       WP_010576021             382 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Leptospira
            kmetyi].
ACCESSION   WP_010576021
VERSION     WP_010576021.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..382
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=42577
     Region          <122..381
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mkeilnwlss ppsraleake lietlnqkii eagipvwrff tsiptmhpev mvrsiiwtrg
       61 eetqvvliph dglqqqqykd spifliregq kdfirckltg pdadlsypic vdlqekggtd
      121 ycifvsvfgt dirsaiswtt dapggfteeq ieslnsirsv lslrldlesr kfavnellev
      181 ylgpnaskrv lsgefrrgtg etiyaailca dlrdfsslse nnspkrivev ldnyfeltaq
      241 piqeekgeil kfigdailav fpaeedshka claalsaark iknsviqwnt ehpdsqihlg
      301 malnvgdvvy gnvgakdrld ftvignavnq afrveslckd fgenilttee fanktgmenf
      361 ellgarqlkg itgerniysp rn
//
LOCUS       WP_010576235             384 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Leptospira alexanderi].
ACCESSION   WP_010576235
VERSION     WP_010576235.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..384
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=45254
     Region          82..>153
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mrfwkkvlgy flfltfsfli leivlsifdp eqvmvksfdr qvlfrfypdr tgrilseeys
       61 vsvktnsdgf rqsvskensy pivvfgdsft egwgveasev yvevansflp kdkqirnlgi
      121 hgaspsfyyl qfpfyyerfr pktlilqifd ndlddnekle vfmdksdpsg myfpkpslsv
      181 kifgetisnf vketttyrli kriiftiqkv pnpilyyreg kepkirvlth eesigkygkl
      241 kplgdqistr yggqfefysk pnnerwvsll krqreslerl ygfcrdkgve lrilyvpake
      301 ffstsgitgd lkvfglefal ernphwklln dfcrthelvc ydlvrtlags dserlyfpyd
      361 ahwnrnghrv vgeylfreir keyr
//
LOCUS       WP_010576248             200 aa            linear   BCT 01-JAN-2025
DEFINITION  LemA family protein [Leptospira alexanderi].
ACCESSION   WP_010576248
VERSION     WP_010576248.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..200
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22661
     Region          9..200
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mktkihpklf lvvtltlasf vssncgynti qeedeavtas waeilnqyqr radlipnlvn
       61 tvkgyafqee kvfvevtkar agvgsiqade ktlnnpelfk kyaqaqtqmt salsrllvva
      121 enypqlksne nfrdlqaqle gtenritvar nryiqavqky nvtirkfpnn ltakffgfdt
      181 kpsftvenek eiskppevkf
//
LOCUS       WP_010576309             135 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Leptospira alexanderi].
ACCESSION   WP_010576309
VERSION     WP_010576309.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..135
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14746
     Region          16..>89
                     /region_name="DoxX_3"
                     /note="DoxX-like family; cl46314"
                     /db_xref="CDD:480654"
ORIGIN      
        1 msishsskkk lllyclriiv afillqtlfy kftgasesva ifsklgvepw grigtgilel
       61 aasillflpg wnwlgsflgl glmsgaifsh vfvigieqen dggllfllal gnaiicslll
      121 wlekdtlmav lrkrf
//
LOCUS       WP_010576439             646 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 36 protein [Leptospira alexanderi].
ACCESSION   WP_010576439
VERSION     WP_010576439.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..646
                     /product="glycoside hydrolase family 36 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73505
     Region          242..552
                     /region_name="GH36"
                     /note="glycosyl hydrolase family 36 (GH36); cd14791"
                     /db_xref="CDD:269892"
     Site            order(248,281,318,391,395,435,450,454)
                     /site_type="active"
                     /db_xref="CDD:269892"
ORIGIN      
        1 mkailrykvy ensftssfei sgkgaktysd cgnfslslgh kktgknetfk phlewigeqr
       61 pkagteilnl eielpphmld epkifqqgyq swslstvhsl sdadesprln flrysqenfy
      121 tnhsgvggdw qsegmillis stkdshyfag aigpgeqgvk frvlspqrke elenskkksw
      181 ipdsgisliy dfyryedfrg nklsltpiav trftigpeaf lkkyfselgk thkvklsttp
      241 vptgwcswyq yytkisekii lknlalvkek klpiqffqid dgyqkeigdw litndrfpgg
      301 mrllaeeirr ekltpgiwla pflvrkksef yqkypeailk drdgkpvpal wnphwgmdyt
      361 ycidvthpts rdflenilkt ivkdngysyl kldflyaall pgwtydrsis phkrytdtir
      421 firkvvgkdv fllgcgapiy psiglfdamr igcdvapfwe rektrilakd khalsteral
      481 inditrssmh rnlwyndpdc llvresknhm tpaqtqlmas vmavsggmil vsddlslige
      541 erlallkkil elgvkcrskt pvpigfasgs fpsalynpag flgiwnpsee entieiqvpf
      601 vsklkqfpdy wtgkvpesle yfsrsgvlkl klpafgsvvl qtakvv
//
LOCUS       WP_010576471             185 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Leptospira alexanderi].
ACCESSION   WP_010576471
VERSION     WP_010576471.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..185
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20927
     Region          2..181
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkivfaini ttdgfcshtd miadeelhky ftdllrtasl ilygrityql mvpfwpevak
       61 dqsmsevgne farvfnsldk vlfsttlkqv eetntrlvrg niveevlalk qqpgkdifag
      121 slsiasqlse rdlideyrfv vhpvvagkgp rlfdtvrpqe slrldflgse tfqsgvvalh
      181 yrkht
//
LOCUS       WP_010576486             192 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Leptospira alexanderi].
ACCESSION   WP_010576486
VERSION     WP_010576486.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 192)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..192
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22218
     Region          55..184
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mkpfypeeyd phsnlwskrd rrdliatpif nlvswhttsp dekiskdffh lesldwvnvi
       61 attpenkill idqyrhgihr fsleipggia ekktllesaq aelveetgyv sqdweylgkv
      121 tgnpailnnw chtfiarnvr klydqdldds eqieifetpi rniprliadn ilhhgmmvaa
      181 lgmyfiknpi qn
//
LOCUS       WP_010576629             256 aa            linear   BCT 01-JAN-2025
DEFINITION  YdcF family protein [Leptospira alexanderi].
ACCESSION   WP_010576629
VERSION     WP_010576629.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..256
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28605
     Region          37..255
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mstilfsisk latlilfplp lvlllllfag aklkkwkekf svwvpvlilw llstsnvsqk
       61 liqsleiyyp plpleqvpqa nvilvlggmv stlsihdepv dlsnsaerlt etvrlyrakk
      121 apkilfsggs gnllyqtvpe sepagrflrq mgipdsslil esksrntlen knfavellke
      181 hgwtsvilvt ssfhmkrsve ifqekgitii pfptdfrtqk svltldnffp stgclensti
      241 sikewigilv hkirns
//
LOCUS       WP_010576664             208 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Leptospira alexanderi].
ACCESSION   WP_010576664
VERSION     WP_010576664.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..208
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23974
     Region          5..77
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(16,18..19,21..22,25..26,70,73..74)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(16,55..57,68..69)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(55,67..68,70..71,74)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          90..201
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(93,100,161,164..165,168,172)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(93..94,97..98,101,137)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(100,104..105,108..109,169,172)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 midlqlvigd kkfsswsmrp willkennip fteisltlnt pefhekirfy sdagkvpvla
       61 dgdvriwdty siveylaetf peknlwpknk tlravarsvv aemhsgftdl rknlsmnlve
      121 klhgktfsee vwkdirrief iwkkcldsyq gpflfgkeft iadafyapvv grfitygikt
      181 gpetseyvsk isnlssykew vngalkkd
//
LOCUS       WP_010576714              97 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Leptospira alexanderi].
ACCESSION   WP_010576714
VERSION     WP_010576714.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..97
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11143
     Region          17..82
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mdseepipwi seeelakqrr iakdlrktpw wkkkkgtgic hycgkkfppe eltmdhlipl
       61 akggksikan lvpackecnf skknklpfef dsereen
//
LOCUS       WP_010576741             130 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Leptospira alexanderi].
ACCESSION   WP_010576741
VERSION     WP_010576741.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..130
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14239
     Region          13..114
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 mnqekiktii ywiataltaa nyafagyayl nrgpeviagi tqlgyplyfi silgvwkllg
       61 aiaitvprfp llkewayagm ffnltaasvs navagtemih aifplialvi valswalrpa
      121 drrlegiwhl
//
LOCUS       WP_010577027             107 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Leptospira
            alexanderi].
ACCESSION   WP_010577027
VERSION     WP_010577027.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..107
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=12136
     Region          2..105
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mvisqyevyl inldptvghe ikksrpcvii spnemnktig tiiiapmttk srsyptrvel
       61 tfqgkkgwiv ldqirtvdki rlikklgkid pktvnkmkli ikemlvd
//
LOCUS       WP_010577104             129 aa            linear   BCT 01-JAN-2025
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Leptospira
            alexanderi].
ACCESSION   WP_010577104
VERSION     WP_010577104.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..129
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13893
     Region          9..115
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 msetilkilk gkkcdscgfq ttesliacsq cgnskiseir fsgkgkiyty tvvhvgfghl
       61 tqrapyvlav veleegikam gilegevsdv pvtesvkidl pvqfqrdepg igfifglvss
      121 pksreksip
//
LOCUS       WP_010577161             282 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Leptospira alexanderi].
ACCESSION   WP_010577161
VERSION     WP_010577161.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18772646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..282
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=32488
     Region          4..138
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Site            order(41,44..45,48..49,51,75,78..79,82..83,85..86,109,
                     112..113,116..117,120)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          41..68
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          54..>232
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          73..103
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          108..136
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          149..177
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          182..213
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          219..247
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msfpalirsa iqrenqreft kafnlykeal sftanpktil kirnrqawcq yhigntretl
       61 nlfheiitky pnepesylyy snylikisnf kqakkiltkg idlypdqlel yltlasllkd
      121 tdrsneaiav lkqalaqekl srgrgilrkd iwaelghlyy qrgnynsalv slktsmrmds
      181 denflhydmi aqcylkvsdh knalkfidly vqyfgesdsd iliikaraha qlgeshlaca
      241 sllqaysmen glklnaedmi dfapllqtgf fdtlenveie ep
//
LOCUS       WP_010577271             375 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Leptospira alexanderi].
ACCESSION   WP_010577271
VERSION     WP_010577271.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..375
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40406
     Region          59..>183
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mkiglgiqkv qsrfrrivlv vsflvflsga nsisaayere iltynlvgrg fnvlettyyk
       61 invvhyrkps ggpiiingkt vlfvhgfgdn saffeplake linqgkathv yimdlpghga
      121 stmtrgtapv panvsqlsvg nygdalrall nqmigtekrk ittivghsig glviqmiqsk
      181 frdggsslld afgientili asdipsalpw fgadapitdp nsakgfvwnf kaekvvetqp
      241 fppqvitglf vetpddfyin tkfavngvpv tgaptpaqle vmsnlepyta aanivgldps
      301 gqttnavsrl svspniwngf nlkvvwlekg vffnqseteg laqylkaesh aitisdpeat
      361 hgapfskpsl flslf
//
LOCUS       WP_010577279             124 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Leptospira alexanderi].
ACCESSION   WP_010577279
VERSION     WP_010577279.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..124
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14011
     Region          22..112
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(31,33..35,41,64,66..68,70..72,75..76,98,102..103,
                     105)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            67
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 makvefdsly ietvrtslpd kevqlvifng kvtnsnsfei srkihfifee evyniildls
       61 nleyinsvgv atiltliktv dqhsgkivig glnhflenvi rlmelpkkvq iyhsieeakk
      121 afss
//
LOCUS       WP_010577319             275 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Leptospira alexanderi].
ACCESSION   WP_010577319
VERSION     WP_010577319.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..275
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31396
     Region          13..271
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mqnvlnqtvt lnnglsmpil glgvwktksg kecreavlna leagyrhidt akiysneedv
       61 gkairesgis rkeifittkl wnadqgsdkt rkaletslek lgidqidlyl ihfpvtsqrm
      121 dswkelekay hdklcksigv snytishlte llknsqitpa vnqvefhpfl nqvdlfeyck
      181 khkiqleays plahgqkved pkiveiakky dktsaqilir waieqkivvi pkstkkeriv
      241 enskvfdfki seedmkilns ldenfrtcwd psevv
//
LOCUS       WP_010577375             260 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Leptospira
            alexanderi].
ACCESSION   WP_010577375
VERSION     WP_010577375.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..260
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28408
     Region          7..254
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msesstilys tekeiavlll nrpekrnain iellsalhka ilkakkeksv rvlvlggtgp
       61 sfcagadlke ratmsskevk rflndlkncf lelenfpypt vaaldgdafg gglelalccd
      121 fillkndiri gltetrlgii pggggtqrlp rrigiakake miftgntida ktafsyglan
      181 siwhdsslpa akmlaeemas hcaplalqla kkaisegygq dirkaletes tyynktlkte
      241 drlealkafq ekrkpifkgr
//
LOCUS       WP_010575909             273 aa            linear   BCT 01-JAN-2025
DEFINITION  Fpg/Nei family DNA glycosylase [Leptospira kmetyi].
ACCESSION   WP_010575909
VERSION     WP_010575909.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..273
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=30819
     Region          2..264
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpelpdlvvi rerlipelvg ktvqsieivd plvvrnltgs aveeiysgss fqsverngpf
       61 lnfafenlni vihpmlsgrf sldpkykkkd lcvriltngp vlnyaddtrm gkvyflkpdd
      121 igqipkykeq ginllsdeft eesliramgk srqqtrvflm dqsrlsalgn ayadevlfaa
      181 kihpktpcnq lspedkslly ksikevlsss ieyvrnkhap ldvkvrdhvk vrnrknepcp
      241 vcgttirran vlgydsffcp tcqpakgeqf ikw
//
LOCUS       WP_010577460             128 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF423 domain-containing protein [Leptospira alexanderi].
ACCESSION   WP_010577460
VERSION     WP_010577460.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..128
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13430
     Region          5..126
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mtgkqkaili lsslsgflgv algafgahal kpiltpelfa iyetgnryhl ihsipplila
       61 itgyvnnsqv iwfssilflt gilvfsgsly ilaiagikil gaitpvggia fliawgllsf
      121 yailskad
//
LOCUS       WP_010577523             329 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leptospira alexanderi].
ACCESSION   WP_010577523
VERSION     WP_010577523.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36489
     Region          6..329
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mttfpllqik nfsldllsen rwlpvlqdln fevrqgeils lvgesgcgks ltslaltrli
       61 psniskvksg eilyqgkdll klsseemrki rgkeisyvfq epfaalnpll kiqdqmieay
      121 lmhispnrke alekaeflls svgitdikqr lysypnqmsg gilqrisiam almcnpklli
      181 adeptsaidv tiqaqlvell ldlqkqnems ilfishdfgl vgtianriav myagkiaeig
      241 dtdsvidspk hpytedllrs ipslaksved lqpiqgivps pdqypigchy strcqavmsl
      301 ckeskpklls mhsngephls acflaknre
//
LOCUS       WP_010577528             436 aa            linear   BCT 01-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Leptospira
            alexanderi].
ACCESSION   WP_010577528
VERSION     WP_010577528.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..436
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=47589
     Region          3..284
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mreiktvtvl gangtmgags aaivasfgka kvhmlardtn kakegiekai gsvktdtirp
       61 rlvpgsydad lekavsesdw vfelvaesye vkepinkria sarkpgtivs tvssglsier
      121 lskafdedgq khyfgthffn ppykmilcel vshkgsdkkv lkqlgeyldk vlgravvytn
      181 dtpafagnri gfqlinevaq iaekysdkgg ialmdaimsg ytgramapld tadfvgldvh
      241 kaivdnlyem tkdaahstfk lpgyfqklid kgdlgrkagg glykmsktpd gkkeklvyni
      301 gadlyepvpk feidfirqan rriseadytg amnivkeakg feadlaryfi aryvsyslsi
      361 vgevvdtkem adlamgtgfn wapasafvdf lggpkdtiql iekaklpvpe vlakakvgkp
      421 fyelkeklda rslfkg
//
LOCUS       WP_010577594             169 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Leptospira alexanderi].
ACCESSION   WP_010577594
VERSION     WP_010577594.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..169
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19360
     Region          1..164
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdqkefteli dstkhivlsa ikknlfdefh dsiddvvqet yfraykslsa nkfrgdssvs
       61 twlytiarne slrmnqkrsr qtalasklke kvildnslqe keavsvgftd felkdllail
      121 pwkyksvlsl vgegykeqqi aeklsipegt vksrafrgkq ilkkffvdk
//
LOCUS       WP_010577628             314 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Leptospira alexanderi].
ACCESSION   WP_010577628
VERSION     WP_010577628.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..314
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35154
     Region          4..310
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mshlilipvc iaggwilkrg kifpentglv lgnfvvyisl pslilanvpt mrletsliyl
       61 asmpwilfgl svvffyiigk ffhwnsetri vttlccglgn tsflglpilr vfygeeitns
      121 vliidqfgtf lclaipgfil slsilskndr erngkpvesi lkklftfppf lallfsfllr
      181 fftiselihs vlkilgetlv pialftvgfq mefptldsks eksenfiqpl figliyklll
      241 apmvifltyr flnvnlnhlr vvvleaamap mitasivsiq mgfrpalsav fpgvgilisi
      301 ptlflfymfl enff
//
LOCUS       WP_010577667             192 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Leptospira alexanderi].
ACCESSION   WP_010577667
VERSION     WP_010577667.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21471
     Region          7..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meqlssrerl iqttaqllqe kgyhgtglkd ilklsgtpsg slyhhfpdgk eeltaaaiqr
       61 agerlekqie atienhpdly ralreftnhl sqelidsrfq kgcpiatvvl eiaaendriq
      121 kvcssiylkw qnllssflqk semkedqvks vsilllavve galvlcrahr siepleivrk
      181 qlesilstli pa
//
LOCUS       WP_010577804             155 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Leptospira alexanderi].
ACCESSION   WP_010577804
VERSION     WP_010577804.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..155
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=16705
     Region          2..149
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 maseidhqyi lfslgdeeya ipislvdeii kinnliripk akdyfagimd irgkvvkmvd
       61 lavrlniprv sgevaydrai vvkvsgqsvg iivdkvanvv lfpsesinpp ppsvkgisgr
      121 yitgvgkkdd rfiiiidvek ilgaeeltes gsnag
//
LOCUS       WP_010577839             658 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Leptospira alexanderi].
ACCESSION   WP_010577839
VERSION     WP_010577839.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..658
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=73920
     Region          11..657
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnrsleyfdk lstiwddfep rkgqiqlsqk iedslfngth liaeagtgvg kslaylipaa
       61 lasiekeepv vistetkslq qqlllkdipm vskilgtdlk aevamgasny vckrktnhvl
      121 rdgtfgpemi phlnsfnqwi kttesgrkqe ftgtashdfw srvtreadnc lgrncpnfsh
      181 syyflerekw krcnilivnh hllaahiasd fnilpefnrv ildeahnfpd iigssfrqei
      241 rsqeiqkllq qiwlpnkntg vavsissnll kdlvtkaget ltvffnalsg evplnfyspq
      301 rikkplkldr gafaavlaei aeilqkhlsk lskdsedise kesalaleml vgrineiatg
      361 letfrqvddp nlvywieppd qsskeiyyki cmeplspdei irdlfasrme sivftsatls
      421 tsgndfkyfq kkignlqasn ltvpspfpyq knallyvpke irdpvgdpdg yhadlakqil
      481 wlielthgnt fvlftsfksl klvyeaisph tdlplfsqsd lgpdgakqmy letpnsvlfg
      541 vstfwqgidi rgdklksvii aklpfqvpnn pvletkseql kesggnpfae lqlpyactvl
      601 kqgfgrlirs gtdtgivsil dprmftksyg kdllkslppa klvqnredlk refsnlpk
//
LOCUS       WP_010578003             469 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Leptospira alexanderi].
ACCESSION   WP_010578003
VERSION     WP_010578003.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..469
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53887
     Region          78..455
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrkiftflll lwmvpilseg nnpsstgsdp glgipespnq spnpiqrevs evssdkertl
       61 dlktaeeklw knnllllasr fnidarkagi eqaglyanpn ifidqsifae ptqryfdftr
      121 sgqtvvqiqq lfllggkigk rvrvaelnar mgeqefydla relvsklrkl fyaiyyyrqa
      181 isfydqslea lgrtvtsaem gykrrailqa evlrlkalyf flkkereeln irilereadl
      241 rvllnddsfr sadvkivpmi venqldnlep gklkrdelle larnkrpdlk kaiqalryee
      301 anlelqhana ipdlafgpmy nrggtafqny wgitaqlnip ifdrnqgnik asekailsrk
      361 qelkntllev enevavsiet arlkdelykk frntytkeyt dlskdmilsy ekryitilef
      421 tdffetyrss vvemlklqtd rmdaiegvnf svgqgvlipk lsqpaaeek
//
LOCUS       WP_010578008            1106 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Leptospira alexanderi].
ACCESSION   WP_010578008
VERSION     WP_010578008.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..1106
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=122999
     Region          4..1048
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mkvlnliiet alryrfftla tavlllavgv wswldirkea ysdiadtqvr lvakfpgkat
       61 leveervtmp iervlhstpn livrrsrtin glvvfqfvfe egtddyfarm rlmekvrdav
      121 ipeevsptla pmsspvgevy ryvvesttgn htpmelrtiq dwivipkllq vsgiadvvtf
      181 gglpkqfhvv tspekliryn vtvgdvidai ksnnlntggn fllqgeqslp irslgairtp
      241 ediedivvkt vngvpvfvrd igsveishpi psgvlgytvq ndqeglidvd savqglvamr
      301 rwvepnafgd rvrakvqein erympdgtrl rntydrgdlv kytlrtvgtt llegiavvsl
      361 vviffigslr asivvvatip fallfsftmm nasgisasll slgavdfgiv vdsavvmven
      421 imrryknatp aekqkgiirf tydcatevgt evlfailiii laylpifsfe riegrlfkpm
      481 aftlsfaifg allftmtvvp vlmsyfyrry fesknpgpie whnpvyewve rkyekivhyl
      541 verskrvvti aftgvtglli vgmmslgtef lpsldeggft lrlyfpvgis lpeakkfvpk
      601 vrkiiysneq vnmilsqygr nddgtdplpp nrlevyvglk dyknwhekit keqllirmrn
      661 dleeglpgvk vsfsqpimdn lseaimgtia dlavfvsgqd lkemrhiaqq ildivskmkg
      721 aseygieqeg papqlvirlk ravaarygin isdiqdviea avgmepisyl yegpmdtppk
      781 eralfgiavr fakdyrqsar eianipiisp kgeriplsel aditqedspt mifrqdgkrt
      841 itvrlnvrgr dqggfvselq ervkkevkip dgfevryggq yenlarvgkq laivipvtig
      901 iifgllfmly rdlrsvival sciplsllgg iyallargyy fnvsagvgfi slfgiatmag
      961 ilfvskanhl rhddimmsvr esailsavtq lrprlmtmll allglipatm asgvgsdvqr
     1021 platvmvggl asalflvltv mpslyilimg teedlkkgsh faskglssgd yasphpdeiy
     1081 stidyeeesv tqvrdeknek kpspqr
//
LOCUS       WP_010578090             404 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Leptospira alexanderi].
ACCESSION   WP_010578090
VERSION     WP_010578090.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..404
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47429
     Region          9..384
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mishfpsgir vefldsisli skqewncisd pkspfleydf lkslevscci gpstswiqry
       61 cvlwkedrls aviplflkfd sygeyifdfq waqfflqagl kyypkglvai pftpangkri
      121 lydtrlslke vcsylipell qfcekedlsg vhflflekee aeilseygfa trlshqyhwi
      181 nggyssfddy lgamkskkrm qikrereivr syeleirvle gneisrsdmd tiwnfysdth
      241 srkwgsayln rkffdssfes fldrivlvla yregkpiagt fnlrkgdfly grywgcteyy
      301 phlhfeccfy qlieyairen ikvfeagaqg ehkflrgfpa vptysshrif hagarnaier
      361 flkeerlhmq emiqetnehs plkevqtnvh fqtettsdlg syep
//
LOCUS       WP_010578147             444 aa            linear   BCT 01-JAN-2025
DEFINITION  TldD/PmbA family protein [Leptospira alexanderi].
ACCESSION   WP_010578147
VERSION     WP_010578147.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..444
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48215
     Region          3..444
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mnldssveyv ldvckkkrld qydlvgsesk evgielfrkr vsntelsnsr gigirliqsg
       61 kpgysysekl seealfqmve dalaqakisd pldidlpgps klpkinirsy eesleslgfe
      121 wlkstgekld dlawsvggki envpysyagk twsrfilans nglyhseksn lisagvalva
      181 tdgktkkmgg ytrsgldldr ispelivsta aerslallga rpvksgsyni vlsnrispqv
      241 fgmfsspfsa dsvqkglsrl egkigsqias qnwnvfcdph isdypgsrll daegvltskk
      301 aviengilqt ylynlesakk egvvptgnav rsyggrvgts fnnyvvpkgd ktleellgnf
      361 seciyvlkle ggsgcsavsg eisigvqgiy ykngipvhpv dsitmnlnff dllfriegis
      421 neyndsyssi kvpdilirea siag
//
LOCUS       WP_010578274              73 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF167 domain-containing protein [Leptospira alexanderi].
ACCESSION   WP_010578274
VERSION     WP_010578274.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..73
                     /product="DUF167 domain-containing protein"
                     /calculated_mol_wt=8314
     Region          1..71
                     /region_name="YggU"
                     /note="Uncharacterized conserved protein YggU,
                     UPF0235/DUF167 family [Function unknown]; COG1872"
                     /db_xref="CDD:441476"
ORIGIN      
        1 mkftvrvkpn skkiffrkee dgsitiavre lalegkanea viemisreme ipkrkirivs
       61 gekskrktie idp
//
LOCUS       WP_010578415             138 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Leptospira alexanderi].
ACCESSION   WP_010578415
VERSION     WP_010578415.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..138
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15331
     Region          36..137
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mnefrifedl hklqnqfssl wdpfllhggs aypalnihkg vdavtitali pgvepenlei
       61 tisgnqlhln getptnapks tqgvnraerf hgkfhrtlel ptevdsektv aefkngvlil
      121 tlpvresvkp rkiqiqtk
//
LOCUS       WP_010577010             143 aa            linear   BCT 01-JAN-2025
DEFINITION  SET domain-containing protein [Leptospira alexanderi].
ACCESSION   WP_010577010
VERSION     WP_010577010.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Qian,C. and Zhou,M.M.
  TITLE     SET domain protein lysine methyltransferases: Structure,
            specificity and catalysis
  JOURNAL   Cell Mol Life Sci 63 (23), 2755-2763 (2006)
   PUBMED   17013555
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Dillon,S.C., Zhang,X., Trievel,R.C. and Cheng,X.
  TITLE     The SET-domain protein superfamily: protein lysine
            methyltransferases
  JOURNAL   Genome Biol 6 (8), 227 (2005)
   PUBMED   16086857
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Yeates,T.O.
  TITLE     Structures of SET domain proteins: protein lysine
            methyltransferases make their mark
  JOURNAL   Cell 111 (1), 5-7 (2002)
   PUBMED   12372294
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459262
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..143
                     /product="SET domain-containing protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16599
     Region          16..132
                     /region_name="SET"
                     /note="SET domain-containing protein (function unknown)
                     [General function prediction only]; COG2940"
                     /db_xref="CDD:442183"
ORIGIN      
        1 mqlrkkisrs rifhekdfei kassisgigm glfpkenvnk gdtigyytgr iltdkianss
       61 kycgskyllw ickdhwiyge gkesnytrfm nhsskpnvkl vvsvrwktar feairkvkvg
      121 eelffdygde ywintdidpv ern
//
LOCUS       WP_010578522             535 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Leptospira alexanderi].
ACCESSION   WP_010578522
VERSION     WP_010578522.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..535
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=61884
     Region          212..526
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mvssqnvlrt prgesffkne vrnfpkqyrd evgalsrfkl sifflgktes rrmrgfkpgk
       61 fantifvfgf lgfvfplswi ypevipfeph fvteekksef dekkspifqe eqtqtevgan
      121 pipsfsgkii dwdvekltey avsnnplyla ekqnmrierg kvitaslyrn ptiqlqqqfi
      181 gvpggggssg pqilgangsq gghmevapal yqdldvygvv slrskvakks feavlgefdn
      241 fdrlfrlrlr qnywayiflt nlvdynkefy enysdllelt kfrvekgdis pleyerlele
      301 riqvekfyrd alvrrqlvek elrilsgire aegifafkte mrfksledlg lrlrdstitt
      361 vnrpdiaale ervkekklni dlqrrealgy vqvggewrik gnehyagvfa aiplplndrg
      421 qgkvlsakee hkkfelalea kkrevdeeie askkellare dllakyerin llqknkqleq
      481 ksriayvrga sdqvtflqae knyltvlrdy yevlylyyna veiykaavgk ktere
//
LOCUS       WP_010578652             266 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Leptospira
            alexanderi].
ACCESSION   WP_010578652
VERSION     WP_010578652.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..266
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29557
     Region          15..260
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mgfidqdtid lgsgnkilkl sfnnpetrns mtremglefk kiidgliett eknrprvvil
       61 tgkndifsag gnfellksfs nkdyetnkkt mfefynlfls vrrldipvic aanghaigag
      121 lslafacdir vfaneakyqf nfvklgihpg mgssytvkel fgthvanrll flaetlngee
      181 afrlglcnds vpqkevlgra teiaialses aplalselkk ntydreklea alrkeaesqa
      241 rnfisadfke tikaieqkrk pvfkgl
//
LOCUS       WP_010578736             231 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leptospira alexanderi].
ACCESSION   WP_010578736
VERSION     WP_010578736.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..231
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25398
     Region          12..231
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtspniadpk ririsnlrks yqsgklqtev lkgleldips ssvitlmgps gsgkstflni
       61 lsgidkpdsg evfvngkslh lmnekeltky rreetgivfq ffhllpylna lenvavplyi
      121 sgigkkqarn taeealekvg lssrkfhkpd elsggeqqrv aiaralckrp sliladeptg
      181 nldtknaenv iqllidlqkq ygftlfivth dqklgslgef rlkmtdgtla d
//
LOCUS       WP_010578861             152 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Leptospira alexanderi].
ACCESSION   WP_010578861
VERSION     WP_010578861.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..152
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=16680
     Region          2..152
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mptavfktnf gdfsvyidqe kapitagnfi klakdgfyng ltfhrviknf miqggcpvgn
       61 gtggpgykiq defhkdlkne kytlsmanag pntggsqffi nvrdnfyldn rhavfgkvtq
      121 gmniveaise metgfhdkpt ktviietitv se
//
LOCUS       WP_010578922             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Leptospira].
ACCESSION   WP_010578922
VERSION     WP_010578922.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..201
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22547
     Region          3..201
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 meflnilvni fseygyiavf lalilcgfgl pvpedislvs ggviagfgka dphfmfligm
       61 agvligdssv fligriygvr vlqipmisri vtperftkvq dkisrygnwv tfmarfmpgl
      121 rmpiyltagt sdrisfyrfv tldflaaiis vpvwvylgyf gaynfdtlmh wvhngqllif
      181 gvlgtvfllf gvvywirkkr s
//
LOCUS       WP_010578998             394 aa            linear   BCT 01-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Leptospira alexanderi].
ACCESSION   WP_010578998
VERSION     WP_010578998.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12112208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..394
                     /product="HD-GYP domain-containing protein"
                     /calculated_mol_wt=44614
     Region          2..131
                     /region_name="DUF3391"
                     /note="Domain of unknown function (DUF3391); pfam11871"
                     /db_xref="CDD:432148"
     Region          <131..335
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mkkfavselk pgmrfskpvy ldkenlfits ntpvtdsdld rlnrfgiqev mtagellqld
       61 aqsdlnvlet niedmivntf vddelqplka vydnlnriki sfgnlfrest qviqdvfkkt
      121 leekplevap vreiaesltd fvrsnqnisy lilannpsgy ylynqianat fyslilgkll
      181 eysrpkmidl gisclladig mckvpssise kneqlseeef kaimkhtilg yqilsqkmkl
      241 knnlaivalq hherydgngy pqklagtaie eqariyaiad nfsalvtnrp hrkkilphea
      301 iksmismdvg kfdlklvrtl lnhlslypvg scielsdkri gvvlgpnldk pirpyiriik
      361 deygtmvrnl ilvdllketn lfisrpvdlq eita
//
LOCUS       WP_010577456              72 aa            linear   BCT 01-JAN-2025
DEFINITION  transcriptional coactivator p15/PC4 family protein [Leptospira
            alexanderi].
ACCESSION   WP_010577456
VERSION     WP_010577456.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Calvo,O. and Manley,J.L.
  TITLE     The transcriptional coactivator PC4/Sub1 has multiple functions in
            RNA polymerase II transcription
  JOURNAL   EMBO J 24 (5), 1009-1020 (2005)
   PUBMED   15692559
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Kaiser,K., Stelzer,G. and Meisterernst,M.
  TITLE     The coactivator p15 (PC4) initiates transcriptional activation
            during TFIIA-TFIID-promoter complex formation
  JOURNAL   EMBO J 14 (14), 3520-3527 (1995)
   PUBMED   7628453
REFERENCE   3  (residues 1 to 72)
  AUTHORS   Kretzschmar,M., Kaiser,K., Lottspeich,F. and Meisterernst,M.
  TITLE     A novel mediator of class II gene transcription with homology to
            viral immediate-early transcriptional regulators
  JOURNAL   Cell 78 (3), 525-534 (1994)
   PUBMED   8062392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10491384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..72
                     /product="transcriptional coactivator p15/PC4 family
                     protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0003713 - transcription coactivator
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0140297 - DNA-binding transcription
                     factor binding [Evidence IEA]"
                     /GO_process="GO:0060261 - positive regulation of
                     transcription initiation by RNA polymerase II [Evidence
                     IEA]"
                     /calculated_mol_wt=8162
     Region          13..62
                     /region_name="PC4"
                     /note="Transcriptional Coactivator p15 (PC4); pfam02229"
                     /db_xref="CDD:460501"
ORIGIN      
        1 mgiiirevdk grgevirvev seykgtkyln lriwytdkdg ekkptqkgia ippelydeik
       61 kaiieaenev ks
//
LOCUS       WP_010579019             434 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Leptospira alexanderi].
ACCESSION   WP_010579019
VERSION     WP_010579019.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..434
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48806
     Region          4..433
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mdlqsqnlns hpkglpvlff tetwerfsfy gmrallvlfl tkvfhfsdpd anriygiytg
       61 lvyltplagg yladrylgfk ksillgttlm mfghlslafe tkpfffcgla lliigvgffk
      121 pnistvvgri yeeenkthmk dsgftifymg inlggflgpl fcgyfsesfg wgygfgvaaf
      181 gvlfgilifl fgqkrfsdrv fepgkkhrid egnryspltk eekrrvviil iftafaiifw
      241 avfeqigssm nlfidrhvdr nwfgydiptp ffqslnplli lilapivasf wtalskrnwk
      301 pdtsirfvyg ffilglgfli ltlatldfrl ghrisaiwlv ltvvcitvge lftspgglal
      361 itklapshfg gfmmgvwfls sffgnilage laglmktdsf ptffgmfagl afagggalyl
      421 vrkkfrtwmr gvdf
//
LOCUS       WP_010579125             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Leptospira alexanderi].
ACCESSION   WP_010579125
VERSION     WP_010579125.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870074
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..321
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35879
     Region          11..229
                     /region_name="ST1585-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Sulfolobus
                     tokodaii ST1585 protein; MBL-fold metallo hydrolase
                     domain; cd07726"
                     /db_xref="CDD:293812"
     Site            order(71,73,75..76,160..161,179,229)
                     /site_type="active"
                     /db_xref="CDD:293812"
ORIGIN      
        1 mltyekevfp glytidcdyi spgvacaylv vegkeaafve nntnhavpil leelrkvgrk
       61 pedvkyiiit hvhldhaggt gllakyctna tilahpkaap hlinperliq ssiqvygeen
      121 fkklygeilp vpkervkspe dgeeirwgnr ifkfyytrgh anhhfcihds lsngiftgds
      181 fglgykdfav gknpilypst tptdfnseea mdtvdkilst gadkaylthf gvwkdlesga
      241 rqmkqglyam qnilssgers glegnallef ctgrvrayle relstqgill gkkeemllef
      301 dskinaqgla fqierkkrsk i
//
LOCUS       WP_010579194             160 aa            linear   BCT 01-JAN-2025
DEFINITION  Dps family protein [Leptospira alexanderi].
ACCESSION   WP_010579194
VERSION     WP_010579194.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..160
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=18047
     Region          3..155
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mkdidigise knretinagl qklladtyil yfkthsyhwn vtgpqfntlh lmfqtqynel
       61 wlsidliaer iralgfyaps sshqlgklts iheeggvpha edmvrhlvsg hetvirtara
      121 llpaadeggd evtldlltqr levhektawm lrsllivent
//
LOCUS       WP_010579356             166 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Leptospira].
ACCESSION   WP_010579356
VERSION     WP_010579356.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..166
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19363
     Region          1..157
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdalyreysg rifdflykys sgnpevamdl mqdtflnffr kysdsdvdre qairllytia
       61 rnrsinysrk fstvkesgns emqdfqeekl sfvrkaelkd leerllicld eleedekyal
      121 ilrfmedysl atiaeimnis vstvsrlivk atakvteiae kknlkp
//
LOCUS       WP_010579236             386 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Leptospira alexanderi].
ACCESSION   WP_010579236
VERSION     WP_010579236.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10083122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..386
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=44636
     Region          <271..375
                     /region_name="SGNH_hydrolase"
                     /note="or GDSL_hydrolase, is a diverse family of lipases
                     and esterases. The tertiary fold of the enzyme is
                     substantially different from that of the alpha/beta
                     hydrolase family and unique among all known hydrolases;
                     its active site closely resembles the typical...; cd00229"
                     /db_xref="CDD:238141"
ORIGIN      
        1 mkeylaffkd pkfwipvlil illetgmqfg cyrpflkkns yaanvlritn hvldkqkefd
       61 pdvlvvgtsv ayqglsiptl nrelaplgkk iqsiaipgte livqdlavlk tlphfknvkt
      121 vihvfeittp wvgqkflnlh tlamisefdr sevypriydf gydvnaddli yitlksiayr
      181 rdiqdlilsp skrikdigkr fkkenhhpwd yensyrekis mypiadipdc vaktnpangq
      241 pipegsdrfh kkaifdtcii asnplthane devtkqyfdr lkilhdeirr igrengqdir
      301 ivgvvapysq liqqwrlper nevwkrelar iypydpipll dyqdildgpd ngdyyydlih
      361 lnsigmqklt iafakdlkal lkeenk
//
LOCUS       WP_010579416             218 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Liquorilactobacillus vini].
ACCESSION   WP_010579416
VERSION     WP_010579416.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..218
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=24873
     Region          28..208
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(109,116,131..133,176,182,186)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 millkrdfrw liagivascl ficltlivkl nthwiskfdi sfekiilatg gtnsdqlfsi
       61 iaffgspian llltmilais iwvkqknifn llwimfvqvg gdalvllfki iiarprpqnq
      121 vitdygfsyp sghtfsttif ifiilfiivp llddqetqfa vsllaifwlg lvafsrlylr
      181 nhfpsdvlgs fflaiswwel mrsfyltlkv nfsekmge
//
LOCUS       WP_010579463             137 aa            linear   BCT 01-JAN-2025
DEFINITION  GtrA family protein [Liquorilactobacillus vini].
ACCESSION   WP_010579463
VERSION     WP_010579463.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..137
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15915
     Region          12..137
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mkkagifktt gfkfilvgiv ntlfgtaimf lcydlfrlsy wwssaanyff gsilsfilnk
       61 yftfqnhahe wqqilkftvn illcyliayg lakplirnwl smdsqfiqdn valllgavlf
      121 tvinyfgqrf wvfnsqk
//
LOCUS       WP_010579484             437 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Liquorilactobacillus vini].
ACCESSION   WP_010579484
VERSION     WP_010579484.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..437
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49709
     Region          4..436
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msktfeqfgl qpfilqalkk infqqptpiq qeiiplimak ksvvgqsetg sgkthafllp
       61 iinqlnakqq tvqavittps relayqiyea arqilafepe lvvhnyvggt dklrqiekln
      121 hrqpqlvigt pgrildlike qaldihlvns lvideadmtl dmgfltdvda iasamptdlq
      181 mmvfsatipv klqpflkkyl atprmvklte ptllsptidn fllstkgktr nqliyqlltl
      241 gepylalvfa ntkervnelt dylrsqglrv akvhgdlppr krkqtmkaiq nleyqyvvat
      301 dlaargidiq gvslvindel pkeleffvhr vgrtgrnglp gtaitlygpd ddtkvvelek
      361 lgikfipkvl qngelkttyq rnrrqhrrfk qqqlapkmig lvkkerrkkk pgyrkkikqa
      421 ikterqrqqk ierrrkp
//
LOCUS       WP_010579496             312 aa            linear   BCT 01-JAN-2025
DEFINITION  ACP S-malonyltransferase [Liquorilactobacillus vini].
ACCESSION   WP_010579496
VERSION     WP_010579496.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Marcella,A.M. and Barb,A.W.
  TITLE     Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as
            templates for engineering
  JOURNAL   Appl Microbiol Biotechnol 102 (15), 6333-6341 (2018)
   PUBMED   29858956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..312
                     /product="ACP S-malonyltransferase"
                     /EC_number="2.3.1.39"
                     /GO_function="GO:0004314 - [acyl-carrier-protein]
                     S-malonyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34377
     Region          1..308
                     /region_name="FabD"
                     /note="Malonyl CoA-acyl carrier protein transacylase
                     [Lipid transport and metabolism]; COG0331"
                     /db_xref="CDD:440100"
ORIGIN      
        1 mkvgilfsgq gaqfsnmgld fyqnskayqe tlkrlsgylq kdlvafcknq hnellqtknv
       61 qtaitafglg vfhqlqqdlp tietvamlgl slgeytalma agafdektgi rllqaradym
      121 qadaeqtdgs mvavlradvq kvakicqqvt gevkhfvgia nynteqqvvi ggqseavqra
      181 ittmkdqgik kvislkvsga fhtplfknts qklanyltnv svrnwqipvi sntttekfvp
      241 nklkitlakq vispthfadc lknlqknyqp dllievgpgk tlskfanrtl pdvpvvaigk
      301 wetyqkfltt ik
//
LOCUS       WP_010579528             206 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Liquorilactobacillus vini].
ACCESSION   WP_010579528
VERSION     WP_010579528.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..206
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21611
     Region          3..200
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mkigfvgagh vtqvlaglfi kaghsvvltn khglaklqpv ieklgpqaqa gslaqvaqqe
       61 lvilavpfka vfdldsklfa dsalvdatny lprrdgayee vqthqlassq lvakhfpgar
      121 vvkafntlpv anlndlsqkg lagnptalpl agdagvklqv aglmrqlgft pydvgdlaas
      181 qkfqadtplf lfasneaglk rkfasl
//
LOCUS       WP_010579656             770 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK [Liquorilactobacillus vini].
ACCESSION   WP_010579656
VERSION     WP_010579656.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..770
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=84537
     Region          <298..769
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 marrkttrkk rknnftlspq ivglifiaws llgifqagfl gvaclnvfrl ligdfgllgl
       61 villawgiyl lafgkepaih lpqlagsvvm llglclwltv cffskldlht hfinitwqyl
      121 wadlstnssg ghvgggflgs llysltyflv gqlgsyiiav limiagfcll tglsftktlh
      181 qfskgfiwli sqiatglklt gswihsklks whskrqqlva srqveaekaa qadlavkkel
      241 psatkqitde ntssltqtvi qtgnwqndsa qtpatetqtp ssdellatkp hvkddyqlpp
      301 isllqevkaa dqsleykkie hntqilqqtf ksfgvaveik railgpsvtk yelhpavgvk
      361 vskivnladd lalalaakdi rieapipgks ligievpnqq istvsfrsim eeqpadpqhp
      421 lqvpigrdis gkvvpadlqk mphlliagst gsgksvainc iitsllmncr pdtvklmlid
      481 pkkvelgvyn gvphlltpvv tdarkasral hklvaemehr yelfaktgqr nlkgynqmia
      541 rqnqetgshe plmpyivivv delsdlmmva sneveaaiir laqmaraagi hmilatqrps
      601 vdvitglika nvpsrmafav ssgtdsrtii dtngaekllg rgdmlflpmg lnkpirvqga
      661 fisdqdvvnv vnfikqeqta dydeklivsd eeaqtdatee qpedelfpev lkliaheqac
      721 sismlqrrfr igynraarlv deleakgivg paegskprkv fidqqpkddq
//
LOCUS       WP_010579764             424 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Liquorilactobacillus
            vini].
ACCESSION   WP_010579764
VERSION     WP_010579764.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..424
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=45633
     Region          8..419
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkkfkvgrls lgwqiligll lgiicgvify enktaitamq nigtmfisli qmivlpivis
       61 cltvgianmg dikklgrvgl ktliyfeimt tiaiilgliv gnlfhpgdyi dihqlhsesi
      121 gqyvqtahkv qhsgiwstim giiptnvfgs lsdgsmlpii ffcvffglgt aaigergkii
      181 idflqavaev mfkvtdwvmh vapigvfali gstvaqmglk alaplgyfiv layatmaifi
      241 iiimglaart fglnnwhilr tikeemilaf stasseavlp kiiakmqhfg vsegivsfvv
      301 ptgytfnldg saiyqslaal flaqaygihl slsqqvtlvi vlmitskgia gvpgasfvvl
      361 latistigvp vqgltfiagi drlvdmgrtv vnvagnslaa viisksekef dfqknrkylq
      421 qlgk
//
LOCUS       WP_010579771             486 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Liquorilactobacillus vini].
ACCESSION   WP_010579771
VERSION     WP_010579771.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..486
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51445
     Region          1..484
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mkkffkleen ktnvsteila glttffamay ilfvapsilg stgmptqaif latilasvvs
       61 tlimavfanv pyvqapglgl atffaytvvl qlgfswqqal alvflcglin vtititkirr
      121 liikaipeil qhaigggigi fvayigikna gflkfitdqa givsingtty hanlthfkng
      181 vtsvvsnggv tpslinfnqa apilaligli ltaflvvkkv kgailigiia ttllgvpmkv
      241 tqlsavnnns llmafhqlgt tfgaafsqqg mgslfqdpgr fllalmtifa fslsdifdti
      301 gtfigtgkrt gifskqdeke ffnghgfksk mdrslfsdai gsvvaaifgt snvttfvesa
      361 sgigvggrtg ltsltaavmf llssllapvi aiipdaatap alivvgimmm gsfknidwtn
      421 ledaipaffa svfmalcysi sygiaagfif ylavklakgk fseihpmlvi ctglfilnfv
      481 vlafie
//
LOCUS       WP_010579803             414 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase, partial [Liquorilactobacillus vini].
ACCESSION   WP_010579803
VERSION     WP_010579803.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..>414
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          40..414
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mttdlteltl pngelimnad rlkeyginkf tqelnngnqp laavkaqsva dvqavmkfan
       61 shqlpvtara aatsivnssa gldgglvldl samnrilkis ipdqiaivep gvmngdldqa
      121 vrksgyffap dpgskpissi ggniatnagg msslkygttk qsvyglkvvl adgtlvklgg
      181 ptfknntgyd ltdlfvgseg tlgiiveatv rlmplpfgnp vtglatfenm kqlsigvqkl
      241 sgsglypsmm ealndtsiea ldrlegtnla gdgasallif qldsaaagsv saskkllqaa
      301 galqisvtdd adyaqkiiki rqdyyqaeaa ygrlvvedva vplsklpdla afveklkftt
      361 kvkaflggha gdgnfhpnia ipkdsqglpt dvqaaidqif eyvislggti sseh
//
LOCUS       WP_010579851             447 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase, partial [Liquorilactobacillus vini].
ACCESSION   WP_010579851
VERSION     WP_010579851.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         <1..447
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          6..442
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 raphaeihld deiaakhaan gkaestidgr ilayvavgdk ddirgvlkta ikfhlpivpq
       61 tadtstviga dglnggiils larmnkivev neddllavve pgvinqdldq aarqhglfya
      121 pdpaskpiss iggnvstnag glsgvkygat kdsvlglkvm langkeikvg grttkqafgy
      181 nltqlfvgse gtlgiiteit lrlfpipigk kiygvaffdn maklaegvha lrisglypsm
      241 legldgktvq aldqykqthy aksasssmli fmfddagetq lqisqkilqe qgawkiqitd
      301 dpaqgekliq lrrdmlpavf angkyyimed mavpssklae madyivqvgd elqvniytag
      361 hagdgnlhpt llwndqpqap anvieatrrl fhkaldlggt isgehavgms knqwnneelg
      421 edvdvlqhqi ktlfdpmnil npkrkin
//
LOCUS       WP_010579855             261 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Liquorilactobacillus vini].
ACCESSION   WP_010579855
VERSION     WP_010579855.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..261
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28707
     Region          1..261
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mkqrvitavi allifiplai igktpfdila iilglialse ilimrkkllv spealfsgla
       61 afmllvpttw lgflpsnssr ftifyflmlv lllytvitrn rfsfddaavl lmgglfismg
      121 fhylmaarqa glstlfflll ivwstdtgay lfgrkfgkhk laphispnkt wegsiggtll
      181 alvvgiifnf iwpqitnwal aagmilllsi vgqlgdlves alkrfygvkd sgrilpghgg
      241 ildrfdsllf vlpvahfmfl i
//
LOCUS       WP_010579909             206 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase
            [Liquorilactobacillus vini].
ACCESSION   WP_010579909
VERSION     WP_010579909.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..206
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=23679
     Region          <120..195
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mrknpflttv aiwlglmavf vllhffyllg hftganrvlv tdpllllllw glnhyllkfk
       61 infnlqlkfr qicqinslpl ilafffiiai isqqtytaah fidslwlala aalfeefffr
      121 gillnnflak santyrnylm avflssflfg lthlvnlaaq swsatllqma nafvlgimla
      181 alylrtgklg wpiflplyfr fywdfa
//
LOCUS       WP_010579962             629 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Liquorilactobacillus vini].
ACCESSION   WP_010579962
VERSION     WP_010579962.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..629
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71391
     Region          6..530
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          560..626
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mqtlriegls ktygektlfe dlnliinehd rlgligvngt gktsllnvla gvdqadqgnl
       61 ikpndyriay lkqkpeleaa dsimtaifkg aapvfkatqn yqqalrvysq ypndqqkeqn
      121 yltaearmnq laawdaesqv ktiltqlkit dldqkvgqls ggqvkrvgla qvliqdpdll
      181 ildeptnhld fssidwleey lagfkgalmv vthdryfldh vaqkileldh gklyiyegny
      241 rayvgqkaer iagkaefehk qkqlykkela wmrtgakars tkqqarinrf nqlqagvsqk
      301 aeeteanlnl gqqrlgkkvi elkhaslkid khriiddfsl liqadqrigi tgangagkts
      361 flnilaaqlp ldagelivgp tvkigyyhqq faqlppdtrv idylkataqq vvdkngnrls
      421 vvqllerflf prymhgvlir klsggeqrrl yllkilmqqp nvllldeptn dldiqtltil
      481 edyledfqgt vitvshdryf ldkiaeqlli ftgngqverf tgmlsvylkq ikskinkvek
      541 aqpkkqvkvq eqtgskkktk ltyaekieyg qleeqidqle sqktklnqqm tqvpgndfsq
      601 ladlqqqidq ldieidqkmn rwdelsqfa
//
LOCUS       WP_010579966             283 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Liquorilactobacillus vini].
ACCESSION   WP_010579966
VERSION     WP_010579966.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..283
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31640
     Region          46..244
                     /region_name="BD-FAE"
                     /note="pfam20434"
                     /db_xref="CDD:466583"
     Region          <219..283
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mkytvdiple rdglwldsnl tytqvpgwlg kttrdlklsv irhfakagsk rfpvifwfag
       61 ggwmdtdhni ylpnlvdfar rgfivvgvey rdsnkvsfpg qledaksair yvranadkfq
      121 anpkkfiamg esagghlasm lgvtngqkkf dvgnnlnvss diqaaipwyg vvdpltakqg
      181 stsndfdfvy rnllgaepes apqldqqanp ltyinqqtvp flilhgdqdv vvpfkdserl
      241 yqklidnqip adlyqiknag hmdlkflqpa vfkiiekfla rvl
//
LOCUS       WP_010579994             125 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Liquorilactobacillus vini].
ACCESSION   WP_010579994
VERSION     WP_010579994.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..125
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13548
     Region          3..111
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mlltvdlqss ipiyqqirnq ivaqvaaglv rpgeklptir alanqlqvnl htvnkayqql
       61 aqegfidllg rrgaiivqps tknlqqtkks fqqavteava qgvscsalqq lviqtyqqlk
      121 agktv
//
LOCUS       WP_010580007             394 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase
            [Liquorilactobacillus vini].
ACCESSION   WP_010580007
VERSION     WP_010580007.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..394
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42142
     Region          1..392
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,173,204,233,235..236,244)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,197,242..244,273,276)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            236
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mkfakrvlqv spsatlalsn qakaltasgv dvinlgvgep dfntpaqika aaiqaiksgk
       61 sdfytaavgi lplrqaicqr lkqdfkvdfr pnqvavtvgg kfslyalgqi lldpgdqvli
      121 plpywvsyge qvklaggepv fvqpaadgfv svaqleaqrt aktkaviins pqnpsglvys
      181 kalltaignw aiehdimlia ddmygkliyn ghsftsliel gdrirqqtil vsglskayam
      241 tgwrvgytva spaviaklgv vlshatsnia avsqyaalaa ltgdqavvea mrqafekrln
      301 tvypelialp gfelpqkpqg afylfpkvaq avriagfntt eeftaavlae ahvalvngaa
      361 fgmpdhvrls yatdlaslqe airrlkefmn khqa
//
LOCUS       WP_010580102             246 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Liquorilactobacillus vini].
ACCESSION   WP_010580102
VERSION     WP_010580102.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27676
     Region          3..244
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 maleinnlvg gysqipvlkk isfqvrpgel vgliglngag ksttinhiig llepqqgsik
       61 innvtlkqdp rkykkslayi pempllypel tlkehldlti kaydlnptva wklarqllkv
      121 frldnkltwf pakfskgmrq kvmivcafit qadyyiidep flgldplatr dlleliskek
      181 krgagilmst hvlstaqtkc dyfvllqagq ikaqgdlael ekqsqisshq lediyfaltk
      241 edrqye
//
LOCUS       WP_010580180             211 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Liquorilactobacillus
            vini].
ACCESSION   WP_010580180
VERSION     WP_010580180.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..211
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24370
     Region          12..208
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 madlcvnlvp lfnalpqdek mqieklvqhk nyqkgeviid ptindnlviv adgnakqytl
       61 dedgyenvlq ilhtgdyige dwlfgqenin nyveatehse icllkrqdll klmhkqpels
      121 irllelnivk vsemqkqihl lalpkvedrl lkylqtyade igknnftlpl kmkdlalylg
      181 ttpetlsrkf allkkqgqlk rqlrrielfe n
//
LOCUS       WP_010580244             821 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit
            [Liquorilactobacillus vini].
ACCESSION   WP_010580244
VERSION     WP_010580244.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..821
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91402
     Region          1..803
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 menlftpsar qvlfiaqkqa kdfrhqaigt ehlllalaie kngiagkvlk qfvitetdvr
       61 eeierltgyg dlkktkaylp ytprakeils laseeaqgmn apkigtehll lalikdnell
      121 svrileslnv dikqlrqtif hklgfsetql kknlknkvks agtptlnsla rdltrlaaee
      181 kidpvigrkk evrrviqvls rrtknnpvll gepgvgktai aeglaqaiin gevpenladk
      241 rvmvldmgsl vagtkyrgef edrvkkiide iyddghvilf idelhtliga ggaegaidas
      301 nilkpalarg evqvigattl defqkyiesd salerrfaki miaepsasdt lkilqglrpr
      361 yeahhqlkik dsalqaavtl svryisdrfl pdkaidlmde asarvhinhs gsakkltakk
      421 delhqlsiek lsalteerfe daaairkrel slrknieqlr ekqaagdyqd aveaediaqv
      481 vsewtgvpvt qmnksettrl ielekilhqr vigqqqavsa vsrairrars glkdpnrpig
      541 sfmflgptgv gktelakala eamfgsenai iridmseyme kystsrlvgs ppgyvgydeg
      601 gqltekvrqh pysvvlfdei ekahpdvfni llqvlddgyl tdskgrkvdf rntiiimtsn
      661 lgatalrdek qvgfsrkntq ndfqamstki kevlkqtfrp eflnrideti ifhqldkdel
      721 hqivklmake vldrvreqnv kikitpaaid lvaekgfdpe ygarpirral qtevedklse
      781 mlitgqikvg svvsvgasrg kivinvkesk qdlkksavsq k
//
LOCUS       WP_010580248             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Liquorilactobacillus
            vini].
ACCESSION   WP_010580248
VERSION     WP_010580248.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..277
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30430
     Region          1..277
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mkkqiinqin ehlssmtpve qkiaavilqq pmqvtewtia nlaaqaqvsq asisrfchnl
       61 klagfhalki elakivgvns nlekneptsv tnfltqvsqg ksaeiqqtla nfaneqinqv
      121 lerllncril qvagqgntfp vaadavyrfn qlgimaitsa isetalaqtl nltdqdillv
      181 isnsgeskqi lkqekiakqr gltiiaitnr ndspislaad frlktaarpp llqstyyysr
      241 laamtvieal fllmiakqpa rskkikqhee liadtkv
//
LOCUS       WP_010580345             376 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Liquorilactobacillus vini].
ACCESSION   WP_010580345
VERSION     WP_010580345.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..376
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43390
     Region          12..208
                     /region_name="HAD"
                     /note="haloacid dehalogenase-like hydrolase; pfam12710"
                     /db_xref="CDD:432733"
     Site            161
                     /site_type="other"
                     /note="HAD signature motif III"
                     /db_xref="CDD:319763"
ORIGIN      
        1 mdiaekqpvv aicydfdktl spddmqaqgf iqsvgynvks fwnesnnlak qaemdqnlaw
       61 myemkkaagk tlftrqalmk ygsqvqlfpg veewfdriqd ygdkvgvkve hyiissglke
      121 miegtkvgrk fkkifassfl fdrddvaiwp aqavnytnkt qflfriekgl ldlndqrvnd
      181 hfspaqlkvp frnmiyigds dtdvpcmklv nsrggysigv ydvksndksk vykmmrdkri
      241 kyfapadytp nhaldrlvkd iiertakneq lerryyscqn eviandsrel veernktnli
      301 laledsgsfa rtykiiakmk kikswnsqet ksiikialen sqvryiansd elkpffyqlm
      361 gnqksdlidq lkkila
//
LOCUS       WP_010580399             285 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Liquorilactobacillus vini].
ACCESSION   WP_010580399
VERSION     WP_010580399.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..285
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30413
     Region          1..285
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mkigfigtgv mgaaiaenll kagqklavyn rtkskadqlv akgavwcdsp aqvaktsevv
       61 ftmvgfpqdv eevyfgeegi fktltpgsav vdmttskpsl aakigqyaak hdfaaldapv
      121 sggdigakqa tltimvggsk taydrllplf kiigqtttyf gpagagqhak manqimiagt
      181 mtgltemlly trkagldeqk ilkalsngga dnwsmenyvp rilkndytpg ffarhflkdl
      241 rialeeadnm gldlratana krlyeimvdv kglgdqgtqg liniy
//
LOCUS       WP_010580412             301 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Liquorilactobacillus vini].
ACCESSION   WP_010580412
VERSION     WP_010580412.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..301
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33167
     Region          4..301
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mlktlifall piivtiflgy faasknyfnd ydsqkfvrlv mnfmlplsvf agiwqtprki
       61 iisdlplagw llismlgcyc lmllinlrhh slqsatlfam svadpsvpfv gsailpllfg
      121 sstsaitigi ctliinilll pivfsslnhe hsfrkrilgt lkkplvisal lgfilallgw
      181 kmpselvnsf ellgkgaggl aifaigivly trkiltnriv vltvleknll fplviwliml
      241 glrlptelqk iviltlaipt atmpttlgiq ynlaeselas iqfwstifsf vtlslfllil
      301 s
//
LOCUS       WP_010580440             325 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Liquorilactobacillus vini].
ACCESSION   WP_010580440
VERSION     WP_010580440.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..325
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36980
     Region          <3..319
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mgfllailne iiqqlvkndp qkfltycgkw tklslkfsgp iiwltkkisk iflrkslksi
       61 peegqnktsa vflkeiidqq gkfnegtfqm lkgvvslqqk ivrevmvart dafmidiknd
      121 ndrnidaivq lpysrvpvfs eskdnivgiv hiknllyaar eegfehikir rvmqpalfip
      181 etlpvdkali klkktrnqma ilfdeyggvv glvtledlie eivgeisdes dqpkpkyqqi
      241 snyeflvegr lpldefnakf ktnlqkddid tiagyliacy geipaddshv evkmtnmklv
      301 teqvsegril kirvilppkn klnlk
//
LOCUS       WP_010580447             301 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Liquorilactobacillus
            vini].
ACCESSION   WP_010580447
VERSION     WP_010580447.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..301
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33731
     Region          39..288
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 meaqnlkknk fafvkrlvak ilkkvaaini nnaaiviayy allaivpmii lignllplin
       61 lkastiltyl etavpktvyq tlkpiilsfl dhgngglisi salvalwavs rginslklaf
      121 ntaygvenvq nifvtrmisi lvtflfivml aiiimvfsfg qsvldyltpi lnlsrdlngi
      181 fgkvkwpitl aflvlilgam yyflpnakvh fwlilpgtli tsaswlllaq gfsfyvryft
      241 ksvlgygtlg tfivllfwln ysawvvmlga vlnaaleeti yhqirprkdr inryllhrir
      301 k
//
LOCUS       WP_010578854             158 aa            linear   BCT 01-JAN-2025
DEFINITION  cyclic nucleotide-binding domain-containing protein [Leptospira
            alexanderi].
ACCESSION   WP_010578854
VERSION     WP_010578854.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Wang,Z., Jiang,Y., Lu,L., Huang,R., Hou,Q. and Shi,F.
  TITLE     Molecular mechanisms of cyclic nucleotide-gated ion channel gating
  JOURNAL   J Genet Genomics 34 (6), 477-485 (2007)
   PUBMED   17601606
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Kaupp,U.B. and Seifert,R.
  TITLE     Cyclic nucleotide-gated ion channels
  JOURNAL   Physiol Rev 82 (3), 769-824 (2002)
   PUBMED   12087135
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Canaves,J.M. and Taylor,S.S.
  TITLE     Classification and phylogenetic analysis of the cAMP-dependent
            protein kinase regulatory subunit family
  JOURNAL   J Mol Evol 54 (1), 17-29 (2002)
   PUBMED   11734894
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Aiba,H., Fujimoto,S. and Ozaki,N.
  TITLE     Molecular cloning and nucleotide sequencing of the gene for E. coli
            cAMP receptor protein
  JOURNAL   Nucleic Acids Res 10 (4), 1345-1361 (1982)
   PUBMED   6280140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10034975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..158
                     /product="cyclic nucleotide-binding domain-containing
                     protein"
                     /GO_function="GO:0030551 - cyclic nucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=18088
     Region          14..128
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(83..84,93..95)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(115..117,121..123)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
ORIGIN      
        1 mqhtkeeilk diylfsnfte delsaiaekt eykvyeqgda ifhegndaka ffvviygtlk
       61 vltstekgdd vnvttiatgd hfgelpfldp gkrsasveam ersellripy dhlkavfekd
      121 skaslkfyqa ishflakrlr mlthdltyar elrkryti
//
LOCUS       WP_010580461             423 aa            linear   BCT 01-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Liquorilactobacillus
            vini].
ACCESSION   WP_010580461
VERSION     WP_010580461.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..423
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46548
     Region          1..421
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mktlyersla vlppvaarat elgvtkgrgi yllgedgqry ldfaagvgvv ncghnhpkiv
       61 taieeqlqql ihgghnvvyy psyielaekl tkrvgqdyka yfsnsgaean egavklalsv
      121 tkrngiiafs rsfhgrtllt aaltasnary rqnyegvlpp vyhvdfpdid nsklneqqei
      181 qrcldqlqql ftniltpqqt aciivepvqg eggylpapks flaelrricd qygillifde
      241 iqsgygrtgy lfakdyygie pdiltaakgi anglplsavl gktkymdqwl pgahggtfgg
      301 nplacaagva vldimdeefl ttvrqkgeff kqglrqlqqk ypvissvrgl glmigvefrs
      361 vdqkqpltel vakirqealk rklillncgv ehnvirfipp liveknqlqq alkildesla
      421 asl
//
LOCUS       WP_010580533             165 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Liquorilactobacillus vini].
ACCESSION   WP_010580533
VERSION     WP_010580533.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..165
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=19179
     Region          1..144
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mdqyvvfksh dqyfalpvqv vtriietddf islpdvpdfv lgvfehqkhm ipiidlrrkl
       61 fnefttksda akvilcdwkd qhlglyveni igiehlketd yekeltqadl khdyigkflk
      121 lkdqvvisle leflfdnqqs enltstvekf ekteenanvd ksqad
//
LOCUS       WP_010580565             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Liquorilactobacillus
            vini].
ACCESSION   WP_010580565
VERSION     WP_010580565.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..282
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31045
     Region          1..256
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 meakitqrik qiypqlgsss qkiadyllke elpasmtlae iaqacqvsla tvsrfarslg
       61 fknfsqlkwa llhqltqnes tnervtqadn slkvagkvla anmttlketf allnevdltq
      121 avklicsaer laffglggsn ivaedayhkf lrvpltvlys seyhlallqa srltakdcai
      181 lishtgnnqd illlakvlrq nqvpaivits dpesplvrlg ticfysisgn lhfqsqafis
      241 mtsqlaltdc lylltarsfg taatviydhq qaivdlrhhf kn
//
LOCUS       WP_010580597             229 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Liquorilactobacillus vini].
ACCESSION   WP_010580597
VERSION     WP_010580597.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..229
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25961
     Region          1..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 miklekinky yqqgdqhyhi lkninlkidq gefvsimgqs gagkstlini igflddqfeg
       61 nyyyfdrpih nytrkqfsrl rnqnvgfvfq nfeliknlsv aenvalplly agqqrkmigq
      121 qvaqalkqvg lagserkkpt nlsggqqqrv siaraiitrp kfliadeptg aldsqtskei
      181 melfknlnqq nqttiimvth dervahqgqr iirildgqii adeqievna
//
LOCUS       WP_010580598             391 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Liquorilactobacillus vini].
ACCESSION   WP_010580598
VERSION     WP_010580598.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..391
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42282
     Region          7..391
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mlfvkllkta wqslrtnprr slltifgivi giaavitiis lgngvkakll nelqatstgk
       61 qttkinyysn ngsnkmgfaq ndveqikgnf sslaqvkvln piskittsaq igsqpknisv
      121 tllqkpvtgi kliaghqlnq ydlavaspva linrktakkq yhdpanaigt sveikhvdyr
      181 vigvytsnvs ryqtnfllpk kvfyqnlsan sgntlkltfn qgvnvsketk qivkflkkng
      241 tqhknghyey fdlgkllksi skvideltif isaiagislf iagigvmnmm ytsvsertqe
      301 igirlavgaq pnsillqfll eavmltvsgg llgfalggll aklislalpf kailtlnsfl
      361 lafgvsafvg ivfgilpakq aanknlidil r
//
LOCUS       WP_010580656             528 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Liquorilactobacillus vini].
ACCESSION   WP_010580656
VERSION     WP_010580656.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..528
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57932
     Region          1..448
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpkkislfsi imltlssiig sgwlfgsgma aqiagpaaii awilggviig vialnyielg
       61 tmfpasggms qyaafshgtl lgfiagwanw islltiipie avaavqymss wpwawanwtr
      121 gfvahgnvtn qglvivflfm laftllnfws lklltsftsl ialfkmaipl ltililfftg
      181 fhsgnfaqta gfmpagsaai ftattsagii fsynafqtti nmgdeiehpe knifrgivis
      241 fgismviytl lqvafigavp shqlvisgwk gidfqspfad iaillnlnww advlyldafv
      301 spfgtgvsfv attsralaam tttrhlptfl gklsqkyrtp rrsmvvnlfl glimvigfrn
      361 wgalsnvist stliayltgp vtlisfrrma pdwkrpfklk gahflaplay llaslaiywa
      421 kwpttievfg vialglifyi yyefrqpagk qkvfqsfkga rwlvfellwl timsligsqq
      481 fggndwlpyp tdfgmvlvgs lgcyllgvhd ayasdeteyg hslnekik
//
LOCUS       WP_010580658             234 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Liquorilactobacillus vini].
ACCESSION   WP_010580658
VERSION     WP_010580658.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..234
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24676
     Region          1..220
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 msgfwgeffg tavliilgvg cgagvnlksn yahgqnwmfi slawglavtf gvyvagqlgs
       61 qghlnpavtl gfaafgffpw hevvpyllgq flgafvgaav viiqyypqfk vsktptqgnq
      121 vgifstapai qnplfnflse viatfvfift llnlgnftqg lkplivglli tvvgqalggt
      181 tgfalnpard wgprlaytil pvpnrssanw gyawvpmfgp laggllagal qsvl
//
LOCUS       WP_010580754             342 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Liquorilactobacillus
            vini].
ACCESSION   WP_010580754
VERSION     WP_010580754.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..342
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37922
     Region          25..341
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mnqelewieq iapdmietlv qrfmiirhiy weqpvgrrtl aqemglterv lrtetdflkk
       61 qklisvsrsg mmvtekgkel tfglrkivdn lvgiqqqevd lakflgishc mivpgntdhq
      121 akvidsmgkl vekaleillp lghnivavmg gttmakiahc ltpklsdnrd lifvparggv
      181 getvaiqans vsaamarrtr gkhrvlyvpe qlsmhaytpl lsepsiqqvi qlirnsdavi
      241 hsigqamkma errdmnneii amlkrnhavg eafgyffdes gkivykipri gvqledlakm
      301 kcvlavaggt skakaivaym khapsqtwlv tdegaansil ke
//
LOCUS       WP_010580756             396 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphoglycerate kinase [Liquorilactobacillus vini].
ACCESSION   WP_010580756
VERSION     WP_010580756.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..396
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41982
     Region          5..396
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 makltvsdld vkgkkvlirv dfnvpikdgv igndnrivaa lptikyvteh ggkailfshl
       61 grvkteddkk kltlrpvaer ladlikkpvt fvpatrgpql eeaigkmndg dillventrf
      121 edldgkkesg ndpelgkywa slgdvyvnda fgtahrkhas nvgiasnmeq aaagflleke
      181 ikflgnavdn pvhpfvailg gakvsdkigv idhllgkadk iligggmtyt fyaakgmkig
      241 nslvekdkve laksimekag dklvlpvdsv vaekfsndvp nkvvegeipd gymaldigpk
      301 svalfedvlk daktvvwngp mgvfemsnya kgtlevgkfl gtlsdattiv gggdstaavq
      361 qlgvadklth istgggasle ylegktlpgi aavsdk
//
LOCUS       WP_010580855             162 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Liquorilactobacillus vini].
ACCESSION   WP_010580855
VERSION     WP_010580855.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..162
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17673
     Region          5..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlqqynnilv pidgskeael afkkavavtr rngdsaklhl lhvvdtrafq nissfdtamv
       61 eqvtetakkt lekyvaeaqk aglknvdysi eygapkviia kevpadkdid limigatgln
      121 averlligsv teyvtrtaac dvlvvrtdld nkpvlnekks kk
//
LOCUS       WP_010580857             439 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A
            [Liquorilactobacillus vini].
ACCESSION   WP_010580857
VERSION     WP_010580857.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..439
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=48029
     Region          1..425
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mnkplayrmr prsidevigq qhlvgpgkii rrmvtakmls smilygppgt gktsiasaia
       61 gstkyalrtv naatdskkdl eavaaeakls gtvillldei hrltkpkqdf llphlengri
      121 iligattenp yiaispairs rtqifevkpl neaeiklaid raladkergl gqskieldps
      181 aknflaqath gdlrsvlnal elatkstptn qqgkiyltlq iieeclqhka lvqdkdgdah
      241 ydvvsafqks irgsdtdaal hylarllaag dlisanrrll tiayedigla npsaaahtva
      301 avtaaekigl peariplaaa vielclspks naaisaidqa ltelkkgnyg eippylkdah
      361 yqgakqlghg ldykyphdfe hdwvaqqylp sklknhsyfr pkgnsryela lkeryqrlkt
      421 sqqqqlaalk skiekkdns
//
LOCUS       WP_010580884             269 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Liquorilactobacillus vini].
ACCESSION   WP_010580884
VERSION     WP_010580884.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..269
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29659
     Region          5..264
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,194,216..218,220..221)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mqpklialdl dgttlnpqaq itsktkivlk kaqaaghlvt ivtgrpyrls anyydelklk
       61 tpminfngal ghiphfhwkk eyqktfprei iselldqkqk igikviaaea kesllidqpq
      121 nlksnffpaq vseqqilkks slksdpaavt llvekaqetk iahwlkasfg syvnvgvwgg
      181 dspiieleph gidkafglay laknlgikrq nilafgdehn dqemieyagl gvvmqngtsa
      241 lkkaadeitp ldnahdglan flqeklqld
//
LOCUS       WP_010580915             460 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Liquorilactobacillus vini].
ACCESSION   WP_010580915
VERSION     WP_010580915.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..460
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51238
     Region          17..455
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mglfgklrrk vlddttpiql vviaylilif itffllnlpi fyqknakpsw ldtfflavss
       61 vsvtglttvp lqqvlnhwgi illefifqvg gfgvtmlttv mmilsgkkis lhqrqmiqvd
      121 mnqprlsgtv rlsysifilm vvlqlvfgvi fslyfswqqn wehlksaffn gfyisvtavt
      181 nagfditgss lapyehnhlf llivmlliii ggigfpvlve ghqwlmfklh dhgngvfrfs
      241 lfsklavffa viffiggaim ifltefkgql asepwpqkim tamfysastr naglqleslk
      301 hfqtatllvf sllmfigasp ssvgggvrtt tvgilllyla afirgrrhvn ifgrrigddd
      361 iqkaivvtnl sillcllavl ilsvtekysl vslifevtaa fgttglslgi taglslvgkw
      421 viiclmfigr vgmlyllllf vskkeqdfny rypsekviig
//
LOCUS       WP_010580928             240 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Liquorilactobacillus vini].
ACCESSION   WP_010580928
VERSION     WP_010580928.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..240
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26896
     Region          1..214
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtanilmtir diskvygqhi vlknvdldvy hheflalvgk sgggkstllr liagleqpnn
       61 geikqsdrli ektndkarmm fqedrllpwm svldnitfas kntqaqkeak nlldlvglte
      121 yadvyptkls ggqkqrlala ralfahpdll lldeplgald altrrnmqdl iikvcqkkqi
      181 ttilvthdin eavrmanriv likdqgikev fenpyqgint teakekrali addilekiln
//
LOCUS       WP_010580807             106 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Liquorilactobacillus
            vini].
ACCESSION   WP_010580807
VERSION     WP_010580807.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..106
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12156
     Region          1..>85
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdtdqkilla vqaliqkygv rkftvdqlas slhiskktiy nhfnskdqii giyikqitns
       61 nynkvkslvt sdlpflekir aiireehsyk lpvsaledik nyypdl
//
LOCUS       WP_010580943             157 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside 2-deoxyribosyltransferase [Liquorilactobacillus vini].
ACCESSION   WP_010580943
VERSION     WP_010580943.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..157
                     /product="nucleoside 2-deoxyribosyltransferase"
                     /calculated_mol_wt=17800
     Region          6..152
                     /region_name="RCL"
                     /note="Nucleoside 2-deoxyribosyltransferase [Nucleotide
                     transport and metabolism]; COG3613"
                     /db_xref="CDD:442831"
ORIGIN      
        1 mnkiylaapf fsdqqqqriq lvktalekns tidsksiflp qehqfeeeef gsrawqqyvf
       61 asdvrqiyra dvlvaildyn lengdnegds gtmfeigvaf anhtpivviq fdpqknlnlm
      121 iaqsltayfd asqnglqdls nynfdelksk pakrpvi
//
LOCUS       WP_010580941             341 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase
            [Liquorilactobacillus vini].
ACCESSION   WP_010580941
VERSION     WP_010580941.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..341
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=38334
     Region          175..258
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mppvfllfin kqlasrtkky ytfiktevkv lqwikqiisk ksflqkkitk ivgvtliyyl
       61 ifqvgasgvf lflkhvlkwp lqrlnqsgwp ylaailfgfi fiilisskqd wqrywqtgpq
      121 kmtaktflsl iailltgqia aslfaqfles vfqlfglsvl aqlkdatqhs esfsmllyaa
      181 vfgplleelv frgfvlqsln kinsvlailg saylfglyhv nfvqspfafl iglvlgytal
      241 tyglfwslll hifnnfvlgd flnqllrlvp tiaaneissg lilfggiigv lvlaaksqli
      301 kawfsklkls rqfiklyfgn hlvilitvsv viiaclslgr v
//
LOCUS       WP_010581008             335 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Liquorilactobacillus vini].
ACCESSION   WP_010581008
VERSION     WP_010581008.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..335
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37903
     Region          1..252
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mikfatigth witkqfieaa qqvgwqltav ysrqqasaqk fadqfigpik tfteldefla
       61 sqdfsvvyla spnslhfeqs qqallagkhv ivekpacsnp temkqiikil rqhpelyyfe
      121 aarhfheplf qqvkqaikql sviqgahlty ekyssrydaf lagqepnifs lefsggalqd
      181 lgvylvyaai awfgypqsad yrpqklrngi dgrgiailey prfqvilkfg kttnsylase
      241 iyglkqtlil dspaklnelk madeqgnvqs lartttenpm laevkdfdql lnkpasliak
      301 qkmedwlala vqvnqlmyql rqsaelsfpa dekyi
//
LOCUS       WP_010580954             430 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Liquorilactobacillus vini].
ACCESSION   WP_010580954
VERSION     WP_010580954.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..430
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44831
     Region          122..414
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mdeedknqvs kiqisnenkk qrppknngyg kvllvaligg vlgggivagg yqyyqnnsat
       61 vensqgttkv snvkvnvstq stkafnkikn avvsveayse ssssnaldgl fgsgsnddtt
      121 esegsgviyk ktgntafivt nnhvisgadk veillnsgkk lkatvvghds itdlavlkin
      181 aqyvkqvasf gnsndikvgq talaigsplg skyatsltqg iisakkrtid ttdssgmttg
      241 qttviqtdaa inpgnsggpl inldgqvvgi nsmklastns ssdsstsveg mgfaipsnev
      301 vkiinelvkn gkisrpalgi slvdlsyiss tdrksvlklp ssvsngvvvl kvsnnspakn
      361 aglqkydvit slgdkkvkgl atlrealykh kigdtvqiqy yhdgslktan vkltleandk
      421 ntttssnsgn
//
LOCUS       WP_010581095             447 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Liquorilactobacillus vini].
ACCESSION   WP_010581095
VERSION     WP_010581095.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..447
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48727
     Region          2..431
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mnndqglarg lknrhvqmia lggtigtglf lgsgksihsa gpaivlayli tgiicfwlmq
       61 amgdlllsdl tkhsfidfva kylgkkvgfv tgwtywfcwi tiamadltas glylqywfpn
      121 vprwlpgmvi lllllaanlt avglfgetef wfalikiaai vgliitgvvl vmigfktqha
      181 tasvmnlfny ggffatgiag fvkafqmvtf gfigieligv tasetqkpqm tipkaineip
      241 lrvilfyvgs mlaliciypw nqipadqspf vqvfkligvp aaagiinfvv ltaaasacns
      301 sifstsrmlf slsrgrqssl akklshlsrr qvpansilfs tavigivvia nfvfpntilf
      361 sfiasvattc flfiwamiic ahlkcckqtk lpfkksrrpi tdylvlgfll fvawvmcldk
      421 mtliallaav iwllvlwlls svtiqag
//
LOCUS       WP_010581169            1181 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Liquorilactobacillus vini].
ACCESSION   WP_010581169
VERSION     WP_010581169.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 1181)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1181)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1181)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1181
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..1181
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=134627
     Region          5..1165
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 msvnfyfgka scdhhhflid rlaqksrvdp qghffylvpn hikfaaevkv lkqlrqtsgn
       61 qglyaqknvq tfsftrlawy flkdtpifki prlskagnqm lvaailqdkq aeltifkanq
      121 vqigfvsqla aqlselqqnl vttaeltqla ksplsanlqa klhdltlvyq eyqqksqqqf
      181 ignegvlnll aenlqqrdls hdyfyiagfs hfnqqerqlv evlikkaaev nlalvgdres
      241 fltkqdpnsl fyrssclyqa larsqasvkl lpitnapkte stsllnledy wirnsrlefv
      301 ptsaaqstds lqlfkaadrq tevrqvaiki rqllqqeqgh yrdfvvmtrh ldlyrniiep
      361 ifqqagipff idlqhemssh plvelisalf diqanhyqyd dvmrllktel llpqtatgqp
      421 ldlgefrdcl dltenwilkt glngsawlqs adwqvfrfet tdtdqvltsq qekqtqqvnl
      481 irhfvqatlp pffeklmqah tgrqaaeilv nflvetgvar qlltwrdqai aagdlaaasr
      541 peevwntfvq mldeyvlifg drpvelelfk elllngfaga qysqvpstld qvtitetgma
      601 qlqnaqtafl igatsavmpd qttqpallsd sdrlqladyl pleqadlaqt sniqlasesy
      661 laylafmlpk krlvlsypqq esdgqelkas pylkqlaaqf aldcpliaae ppagisvtdf
      721 grffvgnsrt tlsqllnlar knqkqlplsf qplakwlkqd pqvgqlakrv faslsyrnvp
      781 eklqpkivdg lygktintsi skleefytnq yayflkyglr lqerdvfels pantgeffha
      841 aldhlhrnla aqhtsiaeis sqqlqqqirs itqellrlpq fqilnssnrm qylsrqlakt
      901 irqvswtihq qlqrsqvrpf ktevlfgqvg sqeglrplef qlsqqhavrv rgkidridll
      961 qkdqqtylgi vdykssqhkf nfrdayygvs lqmltyldal iknfdlllpk mqpdpagavy
     1021 lhlqdpkldl kdvlqtpfeq awlkknkyeg lllaepelle lldqeltqdk sgvslvypfr
     1081 rrkdgsyaat gkndpqlitk nqlklllwhn elliqqaaak ifsgdlaidp vlwpdkrsam
     1141 qyspfkaimq fdamlaenny hqlskmsaae vlekiqaers k
//
LOCUS       WP_010581183             883 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Liquorilactobacillus vini].
ACCESSION   WP_010581183
VERSION     WP_010581183.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 883)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..883
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=96545
     Region          4..882
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mkshyyqlkt kkvlkmlhss eqgltasqve qrqkesgans laeqknhsla ekfiaqfkdl
       61 miiiliiaav iagitgdlsd amiiflvvil naafgvfqet kaenaiqalk emttatsrvk
      121 rdgqvkviks selvpgdlvi leagdiipad lrllqssslk ieeaaltges lptekstapl
      181 seaelplgdr enmafmntnv tygtgmgivt aigmqtevgk iakllsetkq titplqqsit
      241 hlskllsili laiavivflv gtivnqtsfl amlltaisla vaaipeglpa ivtitlalgt
      301 qvmarkkalv rrlpavetlg ateiiasdkt gtltqnkmsv eklylpdeli taknyqptas
      361 dhliqsmila ndtqiteqgl tgdptetali qfnlnqqfkv aalqkdfpri aslpfdserk
      421 lmsaivkaad gdiimytkga vdellertnq ifdhgtirli teidrkqikq anqqlatqal
      481 rvlafayrpm ekfssnvqps pilenqlifv glvgmidper pevkqaivqa ktagirtlmi
      541 tgdhkttaaa iaqrlkiiaq pteenivtgs qlekmseael krrvpeisvy arvapehkvr
      601 ivkawqqrgk ivamtgdgvn dapalktadi gigmgitgte vsknasdivl addnfatiit
      661 avhegrrvfa niqkaiqyll sanlgevltl ffmtllawdi lapaqilwin lvtdtfpaia
      721 lgiekaeanv mknrprgaks nffsngvlas iiyqgilegs ltlgvywlai qfpfhhsnel
      781 ihadaltmaf atlgliqlfh afnsksihet iftrrtfnnr ifnwsiiisa cllfstilip
      841 afnatfkvta lnwqqwsivl lggilmlliv etvklvqrql qkf
//
LOCUS       WP_010581187             143 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Liquorilactobacillus vini].
ACCESSION   WP_010581187
VERSION     WP_010581187.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15787
     Region          5..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 meddfkkilv gvddsedall afryamkrar atnaeliivs vlesnemsvy qalnkdyihg
       61 eredlekhil kyqklaqdag vkkvrsivae gnageaivkd viphvqpdll iigsyskkgl
      121 arhfgsqaay makyapvsvl vir
//
LOCUS       WP_010581189              59 aa            linear   BCT 01-JAN-2025
DEFINITION  CsbD family protein [Liquorilactobacillus vini].
ACCESSION   WP_010581189
VERSION     WP_010581189.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..59
                     /product="CsbD family protein"
                     /calculated_mol_wt=6306
     Region          8..59
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 maknldsakd qvagkvkete gkvtndkare lqgkgqnllg kakdklaeak eevknklnk
//
LOCUS       WP_010581199             480 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Liquorilactobacillus vini].
ACCESSION   WP_010581199
VERSION     WP_010581199.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 480)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..480
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51450
     Region          174..382
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnfikrawln virkkgrtll lilimsaill fvfaglliqe aaskavdnak qsanatvtls
       61 anrsnafrql rkhkqqkslt fssvnlktvr qiaksgyvkn yntlsstngt aksfkaiktt
      121 ttnqpagpig ekskssssss slsldgvtst altsafsegt nkivsgrglt vndqgtnhtv
      181 iekqlakqnd ltvgdqikvk vsgklvklki vgiyrassas tsqtqpqmsd pantlylssk
      241 fvgklkgtpq kvdsvsftmt dpakassfik qakksinttk fslttndavy qtmltplnni
      301 ksfsqkiiwl vciagtailt llvilmvrer ryeagvllal gekkskviwq fftelflvml
      361 vssvialigg kyagnlmskq liqqttaqtt svsggqtggm pggggnsqgm iqgnsqgqkq
      421 paqgrsnasa sqkqsstlnl kisvknvlel lgfglliifi avilgtinil rwppkkiltm
//
LOCUS       WP_010581294             190 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Liquorilactobacillus
            vini].
ACCESSION   WP_010581294
VERSION     WP_010581294.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21568
     Region          3..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvkkilsrek iitaeiqlik ndtllnfsil adhlgvkpqa lypyfknqmd lnyvilsetv
       61 nklnellktq llgltgkaal fqlalicrne gleniklfhf ivtlplknap tftkksidel
      121 rnifnsllat afkhaeiqll agrmirnliy gellnvgtgw fvdkkisqse sfkwmiqesl
      181 dsldkadknf
//
LOCUS       WP_010581295             192 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Liquorilactobacillus
            vini].
ACCESSION   WP_010581295
VERSION     WP_010581295.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22774
     Region          4..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkltdqqmya aimelikqkg pkfttedlar klhtskrtiy qrfaskeqli sqmidflftd
       61 ltrraeslkn dpslsayeki ekyvrdfpst yqigyilrys relerlypkq wqqfnqrvne
      121 isttfyrill ndahtremsa tekkllalml rkttqillng dflreqeldf waaisamhei
      181 ifhgifkakt dk
//
LOCUS       WP_010581351             256 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Liquorilactobacillus
            vini].
ACCESSION   WP_010581351
VERSION     WP_010581351.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..256
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26805
     Region          13..256
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 msfffififl iiagflagll asvaglasla sypalllvgl ppvlanvtst talvctgigs
       61 tvsslkelhg hwnkvlvltl lstggsilgs lllllapaas fekvvpffil iagslllass
      121 rktshlqlns qklpefwlnl lsfggiflvg gytgyfgaag gvitlaillv iinedfatvn
      181 amknflgfas nliatvifif kaqiawkmvv plgiglligg ylgpvivrha nihllrilia
      241 laafglagyl fitayl
//
LOCUS       WP_010581403             488 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 3 protein [Liquorilactobacillus vini].
ACCESSION   WP_010581403
VERSION     WP_010581403.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13386244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..488
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53797
     Region          13..>418
                     /region_name="alph_arabinopyran"
                     /note="exo-alpha-(1->6)-L-arabinopyranosidase; NF041610"
                     /db_xref="CDD:469494"
ORIGIN      
        1 mfeekikeli ykmslkekaa fcsgedfwfl kanqalgipk vmvsdgpngl rkqeakadhl
       61 gieksvaavc fpagclsaas fdpqvtealg dslgrecqhf dvaailgpsv nikrsplggr
      121 nfeyysedpl vagkmatgfi kgvqkhhvgt sikhfaansq etrrmtsssn vdertlreiy
      181 lpafemaike akpwtvmssy nringeyvgd nqhfltdllr kewgfdgmvm sdwggvnnrv
      241 kslkagldle mpgtgqvttd qlieavktgd lkeeqldqav grilefilky vskhqrnapl
      301 dlehdhqtaq kiaeesiill knedqvlpls ankkvafigq yakkpryqgg gsshinsfkv
      361 vsaldaaaqn gltvdyaqgf vdndqkdaek lllaavktak nsqvavifag lpdslegesw
      421 clgdnaacgv llqsttrvtw haektpqidi eqrylqtegt kkelrvydlv dtrliladlf
      481 aklklcys
//
LOCUS       WP_010581478             242 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Liquorilactobacillus vini].
ACCESSION   WP_010581478
VERSION     WP_010581478.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..242
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=26479
     Region          8..235
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mrkpvigita gnlkihdakr tfvnqndiqa iinaggipvl ippqvkdeld rylkicdgfy
       61 fpggpdvspl cfkeepnpgl sfvetardrl eidlikkaaa agktllgvcr gmqvinialg
      121 gnvyqdltkq ftepqkllqh aqkgdineas hhvkivagth lakmfaestl tvnshhhqav
      181 rrvaaglrva araddgviea iesenslqil avqwhpeflv etvpamqlif ddfiqrilvk
      241 ls
//
LOCUS       WP_010581472             411 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Liquorilactobacillus vini].
ACCESSION   WP_010581472
VERSION     WP_010581472.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..411
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=45841
     Region          92..317
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mdkndkknfd fvetplrrsp hynshrkisn hmlrkkicga lliillisfy svgayayyll
       61 setkttihqt yqktnvkklr nvsqvlkqkk pvsilllgtd tgalgrtdkg rtdtiivati
      121 npttkkatlt siprdtqvki agssssygki nsaytiggvs stiktiqntl hipidfylli
      181 nmgglrklvd dlngitikpl ltfnysyahv kkgktvtlng kqalaysrmr ysdpegdygr
      241 qkrqkqvika ivnkalstet itnyksilkt lennmqtdlt yndmitletn ykdaassiks
      301 yvlqgedati nglsyqvata kekrktsnri raslnlnpst ddfvgeinsy snyknsynsr
      361 sstgnyygng tssndhydny gkssesyshy sqtfssdtss ayksdnygfg n
//
LOCUS       WP_010581491             368 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Liquorilactobacillus vini].
ACCESSION   WP_010581491
VERSION     WP_010581491.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..368
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40852
     Region          2..344
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 msielqkitk sydtnlvled vsvriatgef faivgpsgcg kstllrmiag lipisagilk
       61 ideqvvnqlp pqdrkltmvf qnyalfpfln vaenvafglk arrlakdeva qrvkqalelv
      121 nlsdfaerkp relsggqrqr valaraiasd akiclmdepl snldaqlrgk mrseirelqq
      181 qlgltliyvt hdqveamtma drimvlhdqh vqqigspaqi yqqpqntfva nffgtpqinl
      241 ltvqhavsdq laldsflkfe lptkltagty qvgirpgdll vdfnqsqtna avrnleylgn
      301 qsvihakldh geeiritvan hlavginqrl lvtakpnfiv fdqqqravlf vrggkqdgtd
      361 qiqqfqqa
//
LOCUS       WP_010581492             108 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Liquorilactobacillus vini].
ACCESSION   WP_010581492
VERSION     WP_010581492.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..108
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12177
     Region          6..97
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mkqapllkga legcvlaiis eqdfygyqli qqlhqsdlks inggtlypll aklekngalt
       61 syiapspdgp drkyfhltpt gfeqltdfkk hwfdfskqtt eilrrftk
//
LOCUS       WP_010581502             321 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Liquorilactobacillus vini].
ACCESSION   WP_010581502
VERSION     WP_010581502.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..321
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34852
     Region          4..321
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mhvfltsvss vtvivlimal gyvlrkkkwf sdsfgkniss litkialpas ifmavmnnlt
       61 rekllglstg ivfpilgvvi gyliawltvk vlkirpgrrg ifmngvvnan tifigmplnq
      121 alfgdratty fliyyivntv stwafgvfli snddptnlkt hqthqinwkk ilpmplvgfl
      181 vaivwmllkl pvpnfagetl syvgalvtpl sliyigivla daglnnmkld rdstlallgr
      241 fvlspvvlii liklgaasgi elptlmsqtl vvqsatpmla vlpilaneah gdvnyatniv
      301 tistvafiiv vpvlmgilqf i
//
LOCUS       WP_010581542             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Liquorilactobacillus
            vini].
ACCESSION   WP_010581542
VERSION     WP_010581542.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..243
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27703
     Region          4..242
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 midlkdftpt eiliynylvs hvnevaklsi rqladtihvs sasimrcikk mgfdsfyalk
       61 felkqqseka kcqqfakgfd teiftlnref fnrpllqqys qefksfkqla qevnnimffg
      121 igtsgilaqy garqfsnfgi navynidpfy plsdrlkqns qtiafmlsvs getsqnidqa
      181 vrlkekkfhv vsitdnsyct laklseinfa yniqpevikd tlnvttqipv iyileslarn
      241 fas
//
LOCUS       WP_010581564             240 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Liquorilactobacillus vini].
ACCESSION   WP_010581564
VERSION     WP_010581564.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..240
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27370
     Region          5..234
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mktvkyqfva etirqrilkg vykaksimpd qnslasefnv srltvkkald llahegliyk
       61 qsglgtivlg vipikaands panafdglsq qhtgekvesk iisfevhfpn qdlqtkldik
      121 kddpvyeirr lrilngdpli lehtfmpvkl vpglnedilh ksvygylhqq lhlkfggayr
      181 kiratlpdkl dikylqaqkn dpmlefeeiv wlnngeniey atsrnrydkr sytvldvndf
//
LOCUS       WP_010581667             429 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Schlesneria paludicola].
ACCESSION   WP_010581667
VERSION     WP_010581667.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..429
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48176
     Region          40..415
                     /region_name="BcsL"
                     /note="Acetyltransferase involved in cellulose
                     biosynthesis, CelD/BcsL family [Cell motility]; COG5653"
                     /db_xref="CDD:444374"
ORIGIN      
        1 mpqlaekmtn iaqdlgssda vpsqplkmts phpvaphvef wvetvpgids lvaiqrewdd
       61 laanaieqnp fyeswmlieg vkcfganvdl qfdlvwqrnp rpnqppflvg lfpleckrsf
      121 ggvplrlrrv wqhkylyycv plvrrgvatd vlhalfdsms hgpqraaale lhhldlggpf
      181 aqtllevtse raastftves ynralirpas sfdayinsam tnhnrkevrr larrlseigv
      241 pevrvltavd dldtwlnhfl qmeaagwkgr estalasddv srayfksiaq aafargqlmm
      301 vglflnqqpi alkcnflage gsfafkiafd eafsrfspgv qlelenvrll hqmpntkwmd
      361 scaaqhhfmi griwqerrti tkvivstgrr fdnlavglla glsfarkafr rtpdrcanpt
      421 lkpqgtnde
//
LOCUS       WP_010581678             287 aa            linear   BCT 01-JAN-2025
DEFINITION  pirin family protein [Schlesneria paludicola].
ACCESSION   WP_010581678
VERSION     WP_010581678.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..287
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31165
     Region          14..277
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mwksvrgivs dipqhwvgdg fpvrslfsyq dsdefdpfll ldyagpykfa paevtrgvge
       61 hphrgfetvt ivyqgelehg dssgshgtig pgevqwmtaa sgvvheefhs aqfareggtl
      121 emvqlwvnlp akdkmsppry qgilnsqipi kalpdnagtv rviagecfat pgpamtftpi
      181 nvwdcqlnag ghvefaipag httllivqkg eirigdstak avelvslhse gdqvridsas
      241 esrvlvltge plrepvigqg pfvmntrdei rqaiqdfqsg rmgrlah
//
LOCUS       WP_010581683             443 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Schlesneria paludicola].
ACCESSION   WP_010581683
VERSION     WP_010581683.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..443
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46879
     Region          11..411
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(22..23,26..27,30,65,112..113,115..117,120,144,
                     147..148,151,241,244..245,248..250,253,284,288,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mpthtrrlhy awiiagvtff vllatagvrs apsvlivple defgwsrati saavsinlll
       61 ygligpfaaa lmerigvkkt vlislavias gvalttfmsa pwqlmllwgv vvgggtgmta
      121 lvlaativnr wfvsqrglvl gvltastatg qlvflpvmay ivkqygwrpa alliaavlai
      181 vfplvalflr drpsdlglqp lggdpesaet sfastapatp pigalsalre gfrshnfwll
      241 agsfyvcgas tnglvgthli pacldvgmpe vraagllamm gifdlagtta sgwmsdrfdn
      301 rvllswyygl rglsliflpf altegswglt lfavfygldw iatvpptvrl aadsfgrara
      361 simfgwivaa hqigaataaf gagairswsg nyeraflisg alclmtaamv lqirrgpqpt
      421 dapidtdend pvpdmnlsle sgq
//
LOCUS       WP_010581712             249 aa            linear   BCT 01-JAN-2025
DEFINITION  leucine-rich repeat domain-containing protein [Schlesneria
            paludicola].
ACCESSION   WP_010581712
VERSION     WP_010581712.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..249
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=27721
     Region          <86..>220
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          89..112
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          113..136
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          137..160
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          161..184
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          185..208
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          209..233
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
ORIGIN      
        1 msredlnrve pnrviawlar rrmplmfgtv gvvllipvfl altilipfls errvarhves
       61 mggtfsteyf gpewltpslr tqfplfdrit vvnlnrgknt drvvpslcll khletldlel
      121 sdvsdeglks lgrlsqlrgl glnhtgiadi glgylrpltg lqglhldgtk itdagvkhlq
      181 smshlqilkl sntlvsdagv evlfdlhelq ilnlaesrvt rrgfvslrqa lpncelpvif
      241 dmhlpmsvf
//
LOCUS       WP_010581724             533 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Schlesneria paludicola].
ACCESSION   WP_010581724
VERSION     WP_010581724.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..533
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57355
     Region          19..525
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mpasinvsel twcapdrppl fsklclnfgp vrtglvgrng vgkttllkli sgelqplsgr
       61 isvngslgvl rqtvqvppne tvadhfgvta dwailkraer gdatadelad idwtletrmt
      121 aalgrvglda mpdtllttms ggqrtrvgla aliikepqfl lldeptnnld regreavidl
      181 vtiwrsgviv vshdrellev mdsiveltsl gatryggnws tyrelksqel aaakhdleda
      241 ekrvadvart aqttaerhar tsgvghanaa kggaprillg arkdrsekts genarlaerr
      301 reqaqddaev arerieilqp ltvclppthl pagktvlkfe svtvgyfpdr piltnlsfsi
      361 igperiavvg pngsgkttvl alastglkpw qgtvevltay aildqrmcll dpatsirdny
      421 lrlnpgsden acrmalarfm fradtalqnv atlsggqllr aglacvlgga tpppllivde
      481 ptnhldidsi eaveaglqay dgallvvshd epflnaigit rrlelprapq llt
//
LOCUS       WP_010581734             277 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Schlesneria paludicola].
ACCESSION   WP_010581734
VERSION     WP_010581734.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..277
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29227
     Region          22..263
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mtfrpfadad ngpsaaessl vgqvavvigg tsgigralsy vlsqrgcrvy aasrsggrsa
       61 sttqvdmdnr sqrepdvpmi teltcdvanr sdvdrlfqni vhsqgtldiv vnsagigrgt
      121 hsrnavaaam hleesewqev cdtnirgmfl varaaagymi pqgrgqivni ssarsarrgq
      181 pfasaysatk maalamvqal geelapygir awsmlpdava tdliaktnla krgamnpihl
      241 ghaiadllsl pfdarwtepl lapfgseslp hstgvms
//
LOCUS       WP_010581792             204 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Schlesneria paludicola].
ACCESSION   WP_010581792
VERSION     WP_010581792.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..204
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23030
     Region          4..178
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mefqtlldrv ksgdqdaaas lvdnyeplvr rfirfrltsp slrrtfdsld icqsvlskff
       61 veisagdlel ndpaqlrall ltmarnklyd rvrdaqadrr dvrrmegtgd ealaqvaqpg
      121 espsevmaak eilnlvqeql sdderylieq rmsgtpweql aaqlgaspea lrkrmtraid
      181 daakrigfre nandvkstql rser
//
LOCUS       WP_010581760             280 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Schlesneria paludicola].
ACCESSION   WP_010581760
VERSION     WP_010581760.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..280
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30000
     Region          1..261
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mrsicvmnqk ggvgktttsv nlaaglaklg rkvclidldp qghaslhtgv dafgqtptvy
       61 dvfsgrksla dvkqlavdnl wvvpsdldla atevelvdap gremilrgai erlcqqqpfd
      121 yivmdcppsl gvltvnalta akevfiplqp hflalqglsk lfettalvkr rlnrdlvvsg
      181 ivlclyetst rlaaditddl mrfleqsdpk apwknarife srirrnikla eapsfgqsif
      241 dyaakspgal dyaalvsevv aaevaiapps vdpasgpiaa
//
LOCUS       WP_010581865             213 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Schlesneria paludicola].
ACCESSION   WP_010581865
VERSION     WP_010581865.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..213
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23848
     Region          4..192
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mknlflvrha esqhhvgelt ggwtdvpltv vghrqarlla qffavqlhgr naqvyssdlk
       61 rcretaepia salqcnavft pelrelnngt aagrtkteas klrrppvepi ldwvpyqgae
      121 swrnlyrriv tfadglnrnd davvilvtha yaliclvnwf mriaddnlva nimydaapgs
      181 ithlrvgdqd crtigflnss shlenlsecr wnl
//
LOCUS       WP_010581910             358 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Schlesneria paludicola].
ACCESSION   WP_010581910
VERSION     WP_010581910.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..358
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39972
     Region          72..357
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 markknaips yllhqssgqa rvrvnghdyl lgeylspesm vqygalvarv nanlpplspl
       61 akstseedpg psvaelivaf kahaakhytk ngvptseidc yeacyrilrp lygltpikdf
      121 gplalkavrt kmiekkwars ninvmvgrvr rmwkfavene mvsvdvltrl qsvspllrgr
      181 dhgapdrpkr havdqvhiea vrqrvrplvr dlidlqlatg arsgellalt pamidrtket
      241 wttvlddhkc ahhglrrmip fgkkareiis kylsddpdkp lfdiertsyc ravtractda
      301 kiprwsphwl rhtyvtrara elgveaarav aghtttdmtd vyssqmdala iktaealg
//
LOCUS       WP_010581994             197 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Schlesneria paludicola].
ACCESSION   WP_010581994
VERSION     WP_010581994.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..197
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22711
     Region          16..197
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mrpgsytnft llqrlrlapa dpiawaefvk wygqkiyvwc rawglqeada qdvtqdvflk
       61 lsgrmkdfay dpslsfrawl ktvtlhawqd hiqkhrrsgq atgsdfvlnq laaieakddl
      121 fqrmedaaqq ellkeaaarv rlrvetrtwe afqllalqdr tgievaellg mkvatvfvar
      181 skvqrmlrde iarldre
//
LOCUS       WP_010582041             288 aa            linear   BCT 01-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Schlesneria paludicola].
ACCESSION   WP_010582041
VERSION     WP_010582041.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..288
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=31910
     Region          52..197
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 maqdyealdp lfgdlvhran fqsdedarql enalsaelkt virdtdatqs krmnalmflr
       61 iqkdpefldv vldlfddpdq hlwhvihpsk smlqdsrlrq kymekldgpd lknsgeaava
      121 laiagevclf prfadwldng dephrnvaie alrllnaaes lavlqqfwde gkgdedtrls
      181 vagalfdsgd prgrdfleti alqakglasv aaatsvyvag rcreipvgph rqdglklmlh
      241 ilndgdleak qgmvnqiwnf erlphaftad grdeavvwvg sqlesppg
//
LOCUS       WP_010582071             365 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Schlesneria
            paludicola].
ACCESSION   WP_010582071
VERSION     WP_010582071.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..365
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40277
     Region          25..349
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mssapptapk rltkaakwvl glsclnlial caisyliygv setwwvgtvl tyaprapylv
       61 pavvllvasv cwhresigin lvsaavvlvp imglsvplel wmngppksen atsltilscn
      121 vqsfepkfek vleeiatfnp divalqeafr gdprldayfr dwstlqhghy wvgsrfpikl
      181 irdceveqfg grtagmlvei etpagpivla nihqmtarfg lkelnrktli ngdgtkeled
      241 fegerylesi airqavqesr gerplivcgd fntpassslf qkhwgdlqsg fdiagfgygy
      301 tspckgnrfw pdnqpwarid hilcsndwtf qscqigesdg sdhrlivaha llsaknraan
      361 rgiad
//
LOCUS       WP_010582108             374 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Schlesneria paludicola].
ACCESSION   WP_010582108
VERSION     WP_010582108.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..374
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41044
     Region          182..371
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtsllniwwl glkemrslls dvvmvifvgy afslaiyvqa tgtssevnna siafvdedrs
       61 alskelinaf ypprfqepqa isasqiqdam dnglfmfvvt vpprfesdlk agrnpdiqln
      121 idatamqqas iganyvksit nnriqnflkr tnettapsik lvvrklfnpn adsswyksvv
      181 aiinqitllt ivltgaavir erehgtlehl lvmpltsfei avakvwangl vilvataasl
      241 vlvvqmtlkv pfagsyalwf vgvvlylffa talgiflgti srsmaqfall iilvvvalql
      301 lsggstpves mpewlqyltf llparhfvsf sqviiyrggg iravwleflm vggiglgffi
      361 yslalfrksi avtk
//
LOCUS       WP_010582073             203 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Schlesneria paludicola].
ACCESSION   WP_010582073
VERSION     WP_010582073.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   6  (residues 1 to 203)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   7  (residues 1 to 203)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   8  (residues 1 to 203)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..203
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22348
     Region          30..198
                     /region_name="PRX_like1"
                     /note="Peroxiredoxin (PRX)-like 1 family; hypothetical
                     proteins that show sequence similarity to PRXs. Members of
                     this group contain a conserved cysteine that aligns to the
                     first cysteine in the CXXC motif of TRX. This does not
                     correspond to the peroxidatic...; cd02969"
                     /db_xref="CDD:239267"
     Site            67
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239267"
ORIGIN      
        1 mrltarifav alfagsslya gqynevlnig daaptwqelp gtdgkmhals dfqdkdavvv
       61 vftclscpta vdyearfeel akkyggptsn vgfaaicvnr vaadrldklt dranekklsf
      121 pylydesqki akdygaiftp efyvlnkqrk vvymgamdda tdadkvtkry vedalaaalk
      181 gseapvteti argcrvryvr drk
//
LOCUS       WP_010582168             318 aa            linear   BCT 01-JAN-2025
DEFINITION  SCO family protein [Schlesneria paludicola].
ACCESSION   WP_010582168
VERSION     WP_010582168.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..318
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35564
     Region          70..217
                     /region_name="SCO"
                     /note="SCO (an acronym for Synthesis of Cytochrome c
                     Oxidase) family; composed of proteins similar to Sco1, a
                     membrane-anchored protein possessing a soluble domain with
                     a TRX fold. Members of this family are required for the
                     proper assembly of cytochrome c...; cd02968"
                     /db_xref="CDD:239266"
     Site            order(104,108,198)
                     /site_type="other"
                     /note="Cu(I) binding site [ion binding]"
                     /db_xref="CDD:239266"
ORIGIN      
        1 mttvdrptlt acaivslrlv lamimsllid stafaqrftt gspyrtpagq sptaellrdi
       61 gieqqldsql pldavfhdem grrvplgeff dhrpvvialv qyrcpmlcsq vlngflktsq
      121 avpleigrdy qfiaisfdar essdlaaekk kqysrayrrs gaangmhflt gdqdaidrit
      181 rvigfryryv ertdqfahas glmiatpkgr lsrymygidf apqdlrwgle esaiqrigsr
      241 vdqilllcyh ydpltgkygl aisnllriag gltifglgty lafmfrnerr rsklfpaenr
      301 ailpmgasds tlkelsqs
//
LOCUS       WP_010582299             683 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Schlesneria paludicola].
ACCESSION   WP_010582299
VERSION     WP_010582299.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..683
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74893
     Region          250..585
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrwmrsirwi nallmcgaif gcknsrpvsy lgeadlqyyk drslaieysn vdqptsedvv
       61 nsqrphtvrd rghdeiwemp llqavhlavq nnkmirtrgg nltllqtpqn apsiydaalr
      121 dtgflfgsrg veaaladfda sftsqlvfgk navvanslnp faatgagfvn ntdtgaltst
      181 lqktmanggt islnhnvnyv gtnapsqlfp ssyngiaqvq yvqplwagsg veynriagpa
      241 raglgavtgv sqgvaiarin tdisladfen avmtmvkdte dlywelylay rqfdtdnanr
      301 dsllrtwqev kakmdvgatg gnasneaqar daylearanl enswagilaa enalrkqlgm
      361 pvndgklirp sdnpldgeyv aqwestlida ltrrlelrkq kwqikslelq riaaenvtnp
      421 qlnfiggyqv ngfgnnllsn tnvdgttaag ynsfygamar adqtgwnlgl qfsmplgfra
      481 ahaqlrniel qlvkaraals aqeldishei aetmqridis ymtartyldr kvaterrvqa
      541 tqaeyeagvr datldlvlra qasnaaaeia yytslvnynk aitelhmrrg tilendginl
      601 tegewnavaq qeavrrawar sfatpnnwlk tepaefaspv pypktdiypg vpdsdgilpt
      661 aapvdgmqps dqqvepgaet tsy
//
LOCUS       WP_010582306             371 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010582306
VERSION     WP_010582306.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..371
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41411
     Region          4..251
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgqkqvnvam vglgfgaefi piyqshpnan vyaicqrnae hlsaigdrfk iekrfttyad
       61 vlkdpnvdfv hinspipdha smsiqalkag khvmctvpma ttveecrqic elvkqtglky
      121 mmaetvvysr eflfikdlye kgelgkiqhl aashpqdmdg wpaywqkmip mhyathvvsp
      181 clglvngrae yvscfgsgtv rddiaqksgn kfaveschik ikdsdltahi wrflydvarq
      241 yresfdvygt kksfewtlve gephvlhtak kpeheiaskv evpdfahrlp epirkftqsi
      301 qdadhlsfiq ggghggshph lvhemvsali edrdpwpnat lsanwtcvgi lahesalkgg
      361 avmplpeftl s
//
LOCUS       WP_010582373             491 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF1501 domain-containing protein [Schlesneria paludicola].
ACCESSION   WP_010582373
VERSION     WP_010582373.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10538392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..491
                     /product="DUF1501 domain-containing protein"
                     /calculated_mol_wt=54897
     Region          68..490
                     /region_name="DUF1501"
                     /note="Protein of unknown function (DUF1501); pfam07394"
                     /db_xref="CDD:429441"
ORIGIN      
        1 mvtptifgfe erhcqaeksv fdrlneltrr hflgrvgtgl gatalasllq rdavagpagr
       61 dhfpakvkrv iwmfqsgaps qmelfdhkpr laefhkqelp asirmgqrlt gmtsgqssfp
      121 vvaskfqfaq hgqsgmwmse llpytskivd dlclirsmht eainhdpait fiqtgsqlpg
      181 rpsfgswvdy glgtmnenlp afvvmisksg tkgqgllarl wgsgflpseh qgvklrgvgd
      241 pvlylsdpqg mdregrrqml dglaelnqle fadvgdpeik ariaqyelaf rmqssvpelm
      301 dlsqesektf emygedarkp gsyaanclla rrlvergvrf iqlyhrdwdh hgglpermvq
      361 qcketdqasa alvqdlkqrg lldetlviws gefgrtvycq gaitdttygr dhhprcfslw
      421 magggvkggl tfgetddysy nivrdpvhvh dlqatilhql gidhtrltyr fqgrdfrltd
      481 vhgrvvneil s
//
LOCUS       WP_010582474             322 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Schlesneria paludicola].
ACCESSION   WP_010582474
VERSION     WP_010582474.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..322
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35968
     Region          5..185
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(8,10,94)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(41,93..94)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            92..94
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mklsivipvf neaesldelh aqiaqvvseh sldceiifvd dgskdkswkv irqlakadss
       61 vrglrfrrnf gkaagltagi raargelilm mdadlqddpa eipkfieklg egfdvvngwk
      121 lrrldpwhkv ypslvfnwlv armtglelhd hncglklfka evgreirlyg elhrfipvla
      181 nargfrvtel avnhrarqhg eskygyrrfm rgfldlftvt fligygqrpq hmlgaaglvs
      241 fgmgvigsay laltwflmhv iplfkptpig grpllaysia lmllgaqais lgllaelivy
      301 ytsresdtfs vtdevgkpeq iv
//
LOCUS       WP_010582525             260 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Schlesneria paludicola].
ACCESSION   WP_010582525
VERSION     WP_010582525.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..260
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29125
     Region          9..234
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 msartgpvrv laihahpddi elqcagtlvl lkqlgciisv atmtpgdcgs aelsadeias
       61 vrrmeaersa emlgadytcv efrdlsithd ndsrrrvtel irrtrpdlvi tappidymsd
      121 hevtsrlvrd acfnascpny vtlqwdpaap tsqiphlyyv daiqgidyyg rplatdfivd
      181 isttfeeklk mlachesqre wlrrqhglde yldgcrrwsa arglqirvey geaftqhrgh
      241 pyphdnlles llgpkvvvat
//
LOCUS       WP_010582554             317 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Schlesneria paludicola].
ACCESSION   WP_010582554
VERSION     WP_010582554.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..317
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34155
     Region          52..>220
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mltpscwsfc vlaaenggia tvgavnwipt iivcvlllvg licfsymtka giiarattke
       61 avrqpvfllc lalavvvlli nyvvpfftlg edvkmlkdcg latilitgll iavwtastsv
      121 adeiegktam tllskpinrr qfvlgkyigi fqailwymlp vvtvflvliy fkvsydakeg
      181 skeipthaer ivevyqvlpg vglllmeiav msavsvaist rlpmvvnlts cfaifvvghl
      241 tgllvqagvl klefvqfmar liatilpsld lfnisaavat gatvppdylg wsaiycasyc
      301 caaillafil fedrdla
//
LOCUS       WP_010582557             353 aa            linear   BCT 01-JAN-2025
DEFINITION  ZIP family metal transporter [Schlesneria paludicola].
ACCESSION   WP_010582557
VERSION     WP_010582557.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..353
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37759
     Region          38..330
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mgicrlsava aivtmlvsps ilcagehgra adgtffsmts itilavycgl ialsslgggv
       61 lptlirlthv rmqllvslig glmlgvgifh qlphavaimp aqteggtsal dwcmwwlmig
      121 llltffmlrm fhfhsheple edgvhthdca hdhdhghshd hghghdshsp kkaswigifl
      181 glslhtlldg valaaavqad alhfhehsgf alpfgfgtfl gvvlhkplds lsiaslmatg
      241 gwtrramqiv nvgyslmcpi gaalfcigiq rysgvrgdvv agalamsagv flcislsdll
      301 pevqfhshdr lrlslallvg vgsawligyf epkhshgptt npaiqemqpe hqh
//
LOCUS       WP_010582599             484 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Schlesneria paludicola].
ACCESSION   WP_010582599
VERSION     WP_010582599.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..484
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=52023
     Region          83..479
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mpigvpafis laaalcfagr fdctdrlsds evwilrlrhl vqrhefsgla aieidntqnv
       61 laktlrrvis dmssvaspae fvpatqaela rfmaenavqa rktlrpvggr taltypvapt
      121 dvaismselk rivdypardm titveagiri delqsqlaaa gqrlpidiaq agratlggai
      181 atntsgprrf ghgtfrdfvi gisavdsmgd lfkaggrvvk nvagydickl migsrgtlgv
      241 itqatlklrp laetsallwl nmttleqiep aletlqlsqa rpvavevlnp saaklvataa
      301 rcathpnasv lclglegtrr evdwqvdtll qelstcgiqs qeriaepdaa rlwaaltefp
      361 tcaddpltfq anllpsqcid fasratqqgv avqvhagngi vigqlpeeaa tieratsilr
      421 dlrrhaksar gnlqilhcdp ewtgqmpmng dpepgtnlmk rlkqqldpqn llnpgqlvdv
      481 ghvs
//
LOCUS       WP_010582626             226 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Schlesneria paludicola].
ACCESSION   WP_010582626
VERSION     WP_010582626.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..226
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25020
     Region          8..215
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 mlvtaeiisl tvdhirnvla ndssghdwwh idrvrrtale iarqeqadlg vvelaallhd
       61 iadwkfhggd ehagpraare wlernhvdpt vvdavcgiva gvsfkgagva temptlegkc
      121 vqdgdrldai gaigiarafa fgghfgrpmh dpetphqlhe sfaaykakhs ptinhfyekl
      181 lllkdrmqts tgrrlaaqrh afmeaylkqf fsewnadfgr qspvna
//
LOCUS       WP_010582641             473 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Schlesneria paludicola].
ACCESSION   WP_010582641
VERSION     WP_010582641.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..473
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=51484
     Region          2..458
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mkrltirnlm latggrlrdl ntpdtefdrv sidsrdvrrg difwalrger edghnftaqa
       61 lerqahlcvv sadraerltg pmlivddpls algrfgnwyr rqmdamvigv tgsvgktttr
      121 elifsalsdh fegtrspsnf nsqiglplsl leldqehefa vlemgaseig nirrlcelal
      181 pevgvitavg aahlesfgsi eaivetkgel leqlpttgfa vlpgddstvr qmadrapcpv
      241 ifvgqgddnh iqatdvaihn rclqfscega rfslplsgrh lisnalcaia iglevgmspc
      301 aiasglakfs plagrgrmtq vgtwtvidet ynasplavsa acrlladtst pamsqrllvl
      361 gdmlelgpsa aheherigql aaqlcvdrll tcgrhaddia rgaaragmgs hqivaakdve
      421 tllavldcwl qphdtllvkg sratrmerii ewlrdraqqe ehqrqikpqr yca
//
LOCUS       WP_010582657             367 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010582657
VERSION     WP_010582657.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..367
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40728
     Region          7..267
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mshrvcrwgi lsaaniarkn wlgirnaens vvtavasrsl dkaqqfidec qahssfdpkp
       61 vavgsyeell krpdvdavyi pmptglrkew viraaeagkh vlaekpigcd saeaaemiaa
      121 cqkhkvqfmd gvmfmhsqrl nklreaiddg rsvgplrrie tsfsfcgtde faksnirssg
      181 eleplgclgd lgwynirfsl wvmnylmptr vsgrmlneak rtdsrasvpt efsgelffan
      241 gvtasfycsf ltavqqwati agtagyidvq dfvipyfgne vsfrvrnagl nqvscdfnme
      301 dhtrrvsvpe ysngwgnaqe tnlfrnfsql vlsgktdnhw pdialktqqv ldaclksars
      361 ngaivtl
//
LOCUS       WP_010582674             279 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Schlesneria paludicola].
ACCESSION   WP_010582674
VERSION     WP_010582674.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..279
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31953
     Region          46..234
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(49,51,138)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(78,137..138)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            136..138
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mvpeefdsnv rpysqewyat lrstlggtac hqlglyaipd dfvlsvvipi yneertlrvl
       61 idrvravpik kelvlvedcs kdgtreilkq lereaadnpd pmneirvsyh evnqgkgaav
      121 rtgfslakgd aiiiqdadle ynpseysrll rpiiqgvadv vygsrflgdq ehrvlyfwhs
      181 ignkvltlvs ngftnlnltd metcykvftr ealadiwgtl kqnrfgiepe ltakiarrkl
      241 rvfemsisyh grtyqegkhi gmkdgfqalw cilrywwkd
//
LOCUS       WP_010582714             148 aa            linear   BCT 01-JAN-2025
DEFINITION  FHA domain-containing protein [Schlesneria paludicola].
ACCESSION   WP_010582714
VERSION     WP_010582714.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..148
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16452
     Region          2..95
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mrahlipvkg rgrpiqitrd itvvgrqedl cdvclkkssv skmhcvivrt dgllfirdlg
       61 stngtkvngq rvvrgallpg delafagekf rvemgpgdpd pepdrdmenq htemielpvk
      121 aaeenfleyq leplkssnsd vkfleehe
//
LOCUS       WP_010582825             593 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Schlesneria paludicola].
ACCESSION   WP_010582825
VERSION     WP_010582825.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..593
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=63570
     Region          246..573
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mdgrlpridh tsgpswfrsf vcrhrvllra aplmlcvggi aenqsdaadr fslfrrqnsa
       61 trpadrtsnp srtestrsev lptaaidsts alppspakgi adkdqtglvp sstlkrfpqq
      121 qiaassesat drpinleedv tpidlpaalr lagynspqvl vaqqrmlaaa arqqlaaaqi
      181 lpnlnigmny nehtgalqrg sgsildvqrs slyigggtna igagtvnipg lqynlnvgea
      241 yfgylvsrql aassqfgtqa tqnntllqla taycqlvqaq garaiaiqir ddaaeiarit
      301 asfakvgqgr padaeraaae larreadila tqvavveasa rigqllnles svqlqsnenw
      361 avpraivpdl iplpeliais lyqrpelsdr raqvhaamlq lqsakmllfs pqviaglsdg
      421 afgggsdvna altgksqfgn fanrvdadli mywsvrnmgc anralvkaat arlaatsweq
      481 tqqlndirae vadafartqa saaqldirqq avlssqqgyr adlerarage grpievldsl
      541 rllamsqrdy ldtitgynqa hyalyvaigq ppadllarpa ienessenlp epe
//
LOCUS       WP_010582749             378 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010582749
VERSION     WP_010582749.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..378
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42448
     Region          2..377
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 makplrigmv gygfmgrths nayrkvshff dtehqpvlka vcardtekvk afadrwgyes
       61 iesdwrkmve rkdidaidic tpnnlhhdia iaaaangkmi lcekplsmda aegekmceav
      121 eaakvintvw ynyrrvpavt fakqlidsgk lgrifhyran flqdwtisad lpqggaalwr
      181 ldaaaagsgv tgdllahcid taiwlngsvk nvtamtetfi kerkhnltgk mekveiddac
      241 aflcrfgngs lglfestrya rghkalytfe ingefasikw dlhdlhrlqw fdhrdegkmr
      301 gwrsihvtdg dhpymshwwv pglqigyehs fvhhvadflq gvdkgesvgp tfrdaletqr
      361 icdavlksak sgnwsevg
//
LOCUS       WP_010582935             327 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome-c peroxidase [Schlesneria paludicola].
ACCESSION   WP_010582935
VERSION     WP_010582935.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..327
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=35318
     Region          41..309
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mntplvrrls lmvvlaagsv gaaetqsilv vvhpkenpst aekialgqql yfdgrlsadn
       61 kvscatchdp akgfsngeqf atgvegkkgg rnsptvinsa fqnfqfwdgr artleeqalg
      121 piqnpiemnm kmddvvakln qiegyrkqfq qifgtdvtad giakaiaaye rtivsrdapy
      181 drfkagdtaa msesaqrgmk lffgkancsa chagpnftdn gfhniglpsd degrhviskt
      241 lgdkgafktp tlrevaksap ymhdgslktl eevvahyikg gsphpqldea lyplklstee
      301 itdlvtfmke glsspsypah tvpelpq
//
LOCUS       WP_010582988             349 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Schlesneria paludicola].
ACCESSION   WP_010582988
VERSION     WP_010582988.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..349
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37099
     Region          12..332
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtssntilaa nvsdlllaha eqadrsinwp aeswnalgqa gmlgrsipae fggtavepva
       61 fqlgmeeiss sclttafils qreaavrqll kgpahlqqry lpslvdgsay vtvglsqltt
      121 srqhlgpvlr atptsnggyc ldgeipwvtg adhaigivag atlpdgqqll vvipadrlrg
      181 mietplplaa lvgsrtslir crqveleadc vlmnptdnvl gklggggldt sclaigltga
      241 vvrylqheae rrpdllpiae rfesawrsaq grlhqlaqsv adsgqtlelr ldctklalrs
      301 aqaglmiakg vgfvsphpvq rwvrqamffl vwscprpvae gvladladf
//
LOCUS       WP_010581954             311 aa            linear   BCT 01-JAN-2025
DEFINITION  S1/P1 nuclease [Schlesneria paludicola].
ACCESSION   WP_010581954
VERSION     WP_010581954.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Romier,C., Dominguez,R., Lahm,A., Dahl,O. and Suck,D.
  TITLE     Recognition of single-stranded DNA by nuclease P1: high resolution
            crystal structures of complexes with substrate analogs
  JOURNAL   Proteins 32 (4), 414-424 (1998)
   PUBMED   9726413
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Rushizky,G.W.
  TITLE     S1 nuclease of Aspergillus oryzae
  JOURNAL   Gene Amplif Anal 2, 205-215 (1981)
   PUBMED   6101052
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181127
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..311
                     /product="S1/P1 nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006308 - DNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=34675
     Region          20..291
                     /region_name="S1-P1_nuclease"
                     /note="S1/P1 nucleases and related enzymes; cd11010"
                     /db_xref="CDD:211382"
     Site            order(25,80,93..94,107,158,162,168,197,201)
                     /site_type="active"
                     /db_xref="CDD:211382"
ORIGIN      
        1 mrfivafiac ifagqscsaw segghhliav lafdeltsdv rssvldllgh hprfeqdfki
       61 pekvrdpdrw migraafwpd varrtsfdrp kwhydvfina tvgdfedvpl sprlppddat
      121 latkelnikq airlcrkvlk dknqppadra ialcwichlv gdanqpchsg slyskrlfpt
      181 gdrggneipt kqgrnlhalw dnllgpkfde gdvlrraaev rdsgeflgaa evaksqrgke
      241 pecwlmqapt gyvydkdvir aieqaeinga klepiqlske ylsragtlak elaaraamal
      301 aailredfed n
//
LOCUS       WP_010583001             416 aa            linear   BCT 01-JAN-2025
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme [Schlesneria
            paludicola].
ACCESSION   WP_010583001
VERSION     WP_010583001.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 416)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..416
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=45274
     Region          10..411
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mttasqtefd veavrrdfpi lsqrlqhdrp lvyldtaats qkprvvidkm vecfehynsn
       61 vhrgihqlgd rmtteleaar ekvqrfigap evdeivftsg ttmslnmvah gwarkflkpg
      121 devlvnameh hanlvpwqla vkatgatlkf ipltadgrld ltnidalitt ktkllavtam
      181 snvlgtinpi delaqrvhav gglicvdgaq svphditnvk tsgidflafs ghklygptgi
      241 gvlyarksll eamdpflagg hmirevfeqt stwadppakf eagtcafvea valgtaidyv
      301 qslglkaisd yehqlsayah rrlaevsglr vlgpglehkg aiasfvvdgv hphdlsdlld
      361 regvairagh hctmplhdll evtstarasf afynttgevd alidalqgar kvfrlr
//
LOCUS       WP_010583006             441 aa            linear   BCT 01-JAN-2025
DEFINITION  CpaF family protein [Schlesneria paludicola].
ACCESSION   WP_010583006
VERSION     WP_010583006.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..441
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48894
     Region          43..426
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 maaptvsssr grgpssnemd fdslkrlihg klvekldlsr lgelqgetlr reirlviehl
       61 cdtenallnr sererlieev ldetfgygpl eillkeqgva dimingpknv fiekngriqr
      121 sevtfrdnah lmqildrivs rigrridets pmvdarlpdg srvnaiippl aldgpsltir
      181 rfgskplgle dllrfgaftp eialvlegai karlniiisg gtgsgkttll ntlssfiqnd
      241 hrvitiedaa elqlqqehvl rletrpanie gkgrvtatdl vknalrmrpd rivigecrgp
      301 esldmlqamn tghegsmtti hantprdavs rletmismgg ielpiralrq qfagavdlii
      361 qvqrlqggpr rltyitevln meqdqivmqd lflfkqdgid etgrafghfe atgvrpsfmp
      421 rlesagvklp snlfaqrplg r
//
LOCUS       WP_010583092             648 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Schlesneria paludicola].
ACCESSION   WP_010583092
VERSION     WP_010583092.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..648
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=73884
     Region          24..418
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 msrcrddefv prrgnelrvv svsristprq drksnddqea fnqgfirdrt tfpcfvhsik
       61 tqaggecldr aelfelieli esgewdvvic edlgricrrn yaiqicemce dsgtrliain
      121 dnvdtakddw mqnsyfatmr hesynkdtsk rirrtqrhrf vqggnlpkqi wgyirplgak
      181 tddeiqkdpe aepvirkifq rledggsyaa vadwlnsqni ptgpacrtrq wngtllgkfv
      241 kndllvgmry hnrekskrin ksgkracipa ppeellerhc phlafldvay rdhvlslvkd
      301 rnknkgrptd geqpnprlgm ptkrtlfpsq haicgicgrk mlmtcqsagr qqitcsggmd
      361 hkcwhslyvd vdltqreisr avlaeirsld gfvskflqql etairkdssn dqaertrler
      421 lvneltrkik nltkfiadhg dsaeirdqls eyvaerktaq yelskfdrpr pasivipkme
      481 eiatlveetf aelgkddeah rllcrvlpsi iirpvelcds mnvepqaive ldlsplaehl
      541 aghslpsfas pkrlvvnlfe prpyvqhapq lgaieqrgsv vstgyalgls lgeigmarkl
      601 frimrerglq spwvpindpp srgwkgkrhl hpryqfeplp gferpvtd
//
LOCUS       WP_010583137             154 aa            linear   BCT 01-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Schlesneria paludicola].
ACCESSION   WP_010583137
VERSION     WP_010583137.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..154
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=17578
     Region          17..148
                     /region_name="SUKH_6"
                     /note="SMI1-KNR4 cell-wall; pfam14568"
                     /db_xref="CDD:434043"
ORIGIN      
        1 msvkindskp qlskkklsav ekrlkidlpe dyrqfmlthn ggwpepsefk ygdgpytdsc
       61 vdwflsiydg eysnfeeyfe qfkgdeprmp telvpialdp ggnlvcisth gpnrgkvffw
      121 dheeeasdgq vpdyrnvytv ansfteflsm lttl
//
LOCUS       WP_010583178             432 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Schlesneria paludicola].
ACCESSION   WP_010583178
VERSION     WP_010583178.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..432
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46142
     Region          23..398
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(33..34,37..38,41,73,130..131,133..135,138,158,
                     161..162,165,238,241..242,245..247,250,273,277,330..331,
                     335,339,355,358..359,362..363,366)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mvngptfqpv khdpyeafry asfrrfavsy vlavvgsqvl satvqwdvyq qtkdafvigl
       61 vglinaipvi lfalpaghia drfsrkrvll vtqvplalcp aalavlrawn peglslvvtl
      121 sllginatal tfarparssi vpnlvprvaf snafawmssl fetaawvgpa vsgllivfdv
      181 awsylmsalc lavcfaitlf lprdepaeat khewgwgsls aglrfvldsp lllaamtldl
      241 lavllggaty llpvfaerlg vqsigygwmr aapalgafmm avlqahrtpt mragrtllws
      301 vaafgaativ fglsqdfwls lvmlfiigas dnisvvirqt lvqsltpdtm rgrvsavnqv
      361 figasnelgg lesgvtaklf gpiasvvggg igtilvvvgv akkwpqirql rslkelhaav
      421 eaksehdadv ve
//
LOCUS       WP_010583187             213 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA-uridine aminocarboxypropyltransferase [Schlesneria
            paludicola].
ACCESSION   WP_010583187
VERSION     WP_010583187.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Funk,H.M., Zhao,R., Thomas,M., Spigelmyer,S.M., Sebree,N.J.,
            Bales,R.O., Burchett,J.B., Mamaril,J.B., Limbach,P.A. and Guy,M.P.
  TITLE     Identification of the enzymes responsible for m2,2G and acp3U
            formation on cytosolic tRNA from insects and plants
  JOURNAL   PLoS One 15 (11), e0242737 (2020)
   PUBMED   33253256
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Meyer,B., Immer,C., Kaiser,S., Sharma,S., Yang,J., Watzinger,P.,
            Weiss,L., Kotter,A., Helm,M., Seitz,H.M., Kotter,P., Kellner,S.,
            Entian,K.D. and Wohnert,J.
  TITLE     Identification of the 3-amino-3-carboxypropyl (acp) transferase
            enzyme responsible for acp3U formation at position 47 in
            Escherichia coli tRNAs
  JOURNAL   Nucleic Acids Res 48 (3), 1435-1450 (2020)
   PUBMED   31863583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..213
                     /product="tRNA-uridine aminocarboxypropyltransferase"
                     /EC_number="2.5.1.25"
                     /GO_function="GO:0016432 - tRNA-uridine
                     aminocarboxypropyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=23793
     Region          9..196
                     /region_name="TapT"
                     /note="tRNA U47 aminocarboxypropyltransferaseTapT/TuaA/
                     YfiP, DTW domain [Translation, ribosomal structure and
                     biogenesis]; COG3148"
                     /db_xref="CDD:442382"
ORIGIN      
        1 mnyklshhrc prceirrplc fcayipdivl ktrvlilmht leqvlptnta klvykslpns
       61 niivhgrkde rlsadslhep griplllyps shatelspef vaslsgpvtl ivpdanwrqt
      121 qkfvrrepal vgiphvripa gppseyhlrv qrdesgvctl eaiaralgii espdaqakle
      181 lllrvmvert lwsrgrlmae qctisgipae aft
//
LOCUS       WP_010583200             622 aa            linear   BCT 01-JAN-2025
DEFINITION  arylsulfatase [Schlesneria paludicola].
ACCESSION   WP_010583200
VERSION     WP_010583200.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..622
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68077
     Region          102..554
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16142"
                     /db_xref="CDD:293761"
     Site            order(110..111,151,204,206,327,381..382)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293761"
     Site            order(110..111,151,204,206,327,382)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293761"
ORIGIN      
        1 mrripllsmv stlaiggllg yaaaltdlrs paqaapsvas stapvidaai ppdatasipv
       61 pagldqpras ccstglsnqd qlalashnql vaasltqagk kpnilviwgd digitnisay
      121 sdglmgyrtp nidrigsegv rflhyygeqs ctagraaflt gqhgirtglt kvgfpgapmg
      181 msqldpsigg llknlgyatg qfgknhvgdr neslptvngf deffgnlyhl naeeepelpd
      241 ypkdpayraq fgprgvlkck asdkddptvd prfgkigkqt iedtgaltkk rmetiddets
      301 aaaidymqrq hkaskpffcw fnatrmhlrt hvraehrgry khgdseyidg miehdetvgs
      361 llkslddlgi anntivvyst dngphmnswp dgamthfrse kntnwegafr vpclvrwpgv
      421 ikpgtvtnel mshndwvptf csiagepdiv akcakgytan gikykvhldg fdqsallktv
      481 sgpaggdspa ksardkffya dddgllvair qgdykyvfae qrlagtlgvw aepftklrlq
      541 kifniyqdpf eradftsnty wdwnlnhign vygtmqevfk fietfkefpp rsfppsfvpa
      601 tlmeqtleai kesrrraaeg ak
//
LOCUS       WP_010583230             317 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Schlesneria paludicola].
ACCESSION   WP_010583230
VERSION     WP_010583230.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..317
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33336
     Region          1..316
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mflgieiggt klqlgvgrgd gsdfvaferl dvnpaaggqg irdqikevgr klvaahsvqr
       61 aaygfggpif gsrgivqtsh qiagwdqfpl sqwteqelgv ptklgndcdv aalaeasfga
      121 grdahsvfyv tvgtgigggl vfnrkihgtd rpasaeighl rpgldatsyk qtieshaagp
      181 giahatrirl esmrqageat rdlhdfrerc ggnfeqlttk aigeaaaagn qlareqyvaa
      241 trvlgwgiaq mitllapevv vvgggvslvg eeiffaplra avqqyvfppl kdsyrlvpae
      301 lgesvvvhga lalarse
//
LOCUS       WP_010583234             276 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Schlesneria paludicola].
ACCESSION   WP_010583234
VERSION     WP_010583234.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..276
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=31749
     Region          24..265
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mhfrqfvlli avtglivlaa drvqaehegk vqilllgdst teasipkkll pqgpqledvi
       61 rqllaaekdl pptnvmnlgl sgeyirrlld serydrlask lpgldfvlir yglndnarre
      121 nfaenfpkdy helinrlktd hpratiivtt vipyldeats qrlndlnrqv akaenvrlfd
      181 iypryaeelk rgpdmlnyrr yplekipenr refvkpylsa dnpplvevld nrldvhfghl
      241 pgwysdrhpn hagyhvigde takyltplir ekfvkp
//
LOCUS       WP_010583329             114 aa            linear   BCT 01-JAN-2025
DEFINITION  circadian clock KaiB family protein [Schlesneria paludicola].
ACCESSION   WP_010583329
VERSION     WP_010583329.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..114
                     /product="circadian clock KaiB family protein"
                     /GO_process="GO:0048511 - rhythmic process [Evidence IEA]"
                     /calculated_mol_wt=12793
     Region          23..94
                     /region_name="KaiB_like"
                     /note="KaiB-like family; composed of the circadian clock
                     proteins, KaiB and the N-terminal KaiB-like sensory domain
                     of SasA. KaiB is an essential protein in maintaining
                     circadian rhythm. It was originally discovered from the
                     cyanobacterium Synechococcus as part...; cd02978"
                     /db_xref="CDD:239276"
     Site            order(24,43,46..47,71,74,76,80,83..84,87..88)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:239276"
     Site            order(64,67..70,73..75,77,80)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239276"
ORIGIN      
        1 mtrqsidgpa sngsdfsepr kpryvlrlyv sgltprstea iaklkavcee ylsgryelev
       61 idlfqeptla nveqiiatpt likklplplr rlvgdlsdte rvirglnlfe hmeh
//
LOCUS       WP_010583356             147 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Schlesneria paludicola].
ACCESSION   WP_010583356
VERSION     WP_010583356.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..147
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=16512
     Region          49..147
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mfvrtrrfnl pttdalttvq remenlfgrv lhdatenssn ygwrapiamw edadkvylel
       61 dvpgvakdtv dltvhdgvlr itgerktpeg drtywanern ygtfgrtval pkdvdadnid
      121 ahltdgvlqi vlskrpeaqp kkialkd
//
LOCUS       WP_010583413             321 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Schlesneria paludicola].
ACCESSION   WP_010583413
VERSION     WP_010583413.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..321
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35920
     Region          10..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msdenrsdai viehlskayg pkwavrdlnl ripsgcvygf lgrngagkst tikmltgmap
       61 pdagrvlllg editslspqt rsriaymaeg hplyswmtig qivqftrpfy enwdqslvdq
      121 ildhfelsrk qkcgrlsrgq qaqvslalam apdpellild dptlgldtvv rrdflealiq
      181 liqsrgrtif fsshvlgdve rvanrigimm ggvlrvdcpt etfresvrkv vlgfdtdppd
      241 fpecaglvnw rrvglelelv vvewgptqqa iadsleprwi dvttlnleda fieytrgnkr
      301 smplfnretn rvdstvvert a
//
LOCUS       WP_010583438             318 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Schlesneria paludicola].
ACCESSION   WP_010583438
VERSION     WP_010583438.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..318
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=35308
     Region          10..>46
                     /region_name="Trm112"
                     /note="RNA methyltransferase activator Trm112/YbaR
                     [Translation, ribosomal structure and biogenesis];
                     COG2835"
                     /db_xref="CDD:442083"
     Region          89..183
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 masinnlgnl lpmlrcpacg aalglvadsl ecsvchsrdp vvddiprftr dqhlasfgrq
       61 wnkyevahdd edratfqakt gtslsdligl rildagcggg ryskvcgeag atvigadhta
      121 avlkarelca hlpsvnfvqa dlkqlpfapa sfdfvfsigv mhhdadtksv fdavakmvkp
      181 ggrysvwlyr qnqwwqegin dalrqrttrm apeklerwce wgawlgglpv vnktlnkvvn
      241 fsahpnhenr vcdtfdwfap qyqyhhtvee lcswfdaagf vnlrvlppek sgrmyrwvye
      301 hnlligsgvn vtgeksan
//
LOCUS       WP_010583473             132 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Schlesneria paludicola].
ACCESSION   WP_010583473
VERSION     WP_010583473.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..132
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14762
     Region          9..122
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mssrfslqfe ihpssgvpiy rqlmdqlrtl iasgrlapge lipsvrqmae elqvnlmtvs
       61 kayarleadg vlerdrgigm rvkppqsggt kaerleqlrp laeqlsilaw qlkltdeqvl
      121 qlvkqelkdr pt
//
LOCUS       WP_010583491             258 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Schlesneria paludicola].
ACCESSION   WP_010583491
VERSION     WP_010583491.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..258
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27534
     Region          1..217
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mdvrekivvv tggangigra lclrftrega rkvvvadlne slarevaaei dgiaiktdvg
       61 qeadlqqlve hvtsslgpid lfcsnagiil nggpetldad wqriwnvnvm shvyaaravl
      121 pgmqargqgy llqtasaagl ltqigsapys vtkhaavgfa ewlsityasa gikvscvcpq
      181 gvrtdmldla eggiadhlre taldpaevad aviaglaset flilphpqva effrhkaddy
      241 erwlrgmrrl qtkfganp
//
LOCUS       WP_010583493             355 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Schlesneria paludicola].
ACCESSION   WP_010583493
VERSION     WP_010583493.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..355
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39470
     Region          39..293
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(42,45..47,50,61,63,95,114..117,216,218,220..221,223,
                     236..237,240,255..256,259)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(42,46,50,61,63,95,114..117,216,220..221,223,
                     236..237)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(45..47,216,218,221,237,240,255..256,259)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mtadlnnptp trageelple slegmlrrqw pdslgplive qfphghsnlt yllrlgsref
       61 vlrrppfgnq vatahdmgre yrilsklnsv yapaprpelf cddatvmgcp fyimerrhgl
      121 ilrktlppnl tihpelahrm scalidnlaa lhaidyqqag lgelgkpegy vhrqvagwtk
      181 rygqaqtaev pamdrlarwl aenlppemga tvihndykyd nvmldaadlt kvvavldwem
      241 atigdplmdl gtslgywvea gdpvalqhva fgptalpgsl trrqlvdryq ektgrsvdha
      301 lfylcfglfk lavivqqiya rfarghttds rfahldklvl ilgsqadhal esgsi
//
LOCUS       WP_010583503             402 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Schlesneria paludicola].
ACCESSION   WP_010583503
VERSION     WP_010583503.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..402
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=43872
     Region          2..401
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 maeyryiare lsgqqvagtv saaserealg slaaknlfpv sinladaaka hqankrrqvp
       61 arilavfysq iadllrsgvp llrsldllvk qtrhvtlklv vqevrdqvad gtrlaeamrq
      121 hptvfnelti smvrageegs fleeslqria tftehqeelk grvvgamiyp aflvvagtiv
      181 vigmlvffvp mfdsifdtmr kqgtlptatv illttsdflk kygllfllgl iaaiffgksy
      241 faneagrrry delrlkivgi gavvrslava rfcrvlgtll hngvpilsal niakdatgnr
      301 viseaiaqaa drvssgrsla eplaecgqfp vdvlemiavg eeannleqvl vgvadkmerq
      361 tnrqldlvvr lleplmlvam agvilfllma lmlpifnmss mt
//
LOCUS       WP_010583508             174 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Schlesneria paludicola].
ACCESSION   WP_010583508
VERSION     WP_010583508.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..174
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20005
     Region          17..173
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mpsgeqeslf lrwqsdhigl ilkivrayav sfvdqddllq evlsnlwssi prfqgaakes
       61 twiyrvalnt alawrrdetr rrqlhllmie cdvslnatvd ssmkpsrhel iekmyvairq
      121 lskidaalal mhldglnyhe msevlgisen yvgvklcrir kelfellkdd cdel
//
LOCUS       WP_010583509             193 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Schlesneria paludicola].
ACCESSION   WP_010583509
VERSION     WP_010583509.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..193
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20436
     Region          5..175
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mpstlkilaf agsvrrdsfn rkllrlavag aeeagaevtv vdlrdyplpi fdqdleaesg
       61 ppenakalkk lfiehhalli aspeynssvt plmkntidwv srpvagelal agfhgkvatl
      121 isaspgtlgg lrgliqlrsi lgnigvivlp eqiavplane afdahgalkn erqaakvkni
      181 gaglvfmarr fap
//
LOCUS       WP_010583510             452 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome-c peroxidase [Schlesneria paludicola].
ACCESSION   WP_010583510
VERSION     WP_010583510.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..452
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50067
     Region          59..401
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mitssvgssp vlnqtqnanr vlrptaeiir fseivaaiff vfliavsagh aqdlspieql
       61 gkelffdtnl svpagqacas chapetgftg pssdvnqqtg vypgaepsrf gnrkppsvay
      121 msfsqkreyk kddetwvggq fwdgraddli aqakgpflnp lemnnasaad vvnkvrrsny
      181 rdlfdrvfgk ksldtqasdt tfdqiaraia ayessrevnp fnskydafla krvkltpqeq
      241 rglrlfadka nctachphem gqdgspplft dftydnlgap rneknpfyra pksvnadgaa
      301 yrdlgigasv ndpahygkvk vptlrniakk pspdfvkcyl hngtfkslke vvhfynkrdq
      361 dpdhfppadv petvnhkelg nlgltdeeed dliaflgtls disipretpe pfqpmqplft
      421 kqayrgvldi qrvekfrmhv iqasgkkdaa rr
//
LOCUS       WP_010583549             143 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Schlesneria paludicola].
ACCESSION   WP_010583549
VERSION     WP_010583549.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..143
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14741
     Region          5..138
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mkitrkgsav wqgglkdgkg alttesgals sypygfssrf egvkgsnpee llgaahagcf
       61 tmalslilge akltaekmet saavtleqva dgfaitsvhl tlkakipgad katfekltgm
      121 akagcpvskl fkteitldat lld
//
LOCUS       WP_010583616             597 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp70 family protein [Schlesneria paludicola].
ACCESSION   WP_010583616
VERSION     WP_010583616.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Fernandez-Fernandez,M.R. and Valpuesta,J.M.
  TITLE     Hsp70 chaperone: a master player in protein homeostasis
  JOURNAL   F1000Res 7 (2018)
   PUBMED   30338057
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Mayer,M.P. and Bukau,B.
  TITLE     Hsp70 chaperones: cellular functions and molecular mechanism
  JOURNAL   Cell Mol Life Sci 62 (6), 670-684 (2005)
   PUBMED   15770419
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Bukau,B. and Horwich,A.L.
  TITLE     The Hsp70 and Hsp60 chaperone machines
  JOURNAL   Cell 92 (3), 351-366 (1998)
   PUBMED   9476895
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   5  (residues 1 to 597)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   6  (residues 1 to 597)
  AUTHORS   Rensing,S.A. and Maier,U.G.
  TITLE     Phylogenetic analysis of the stress-70 protein family
  JOURNAL   J Mol Evol 39 (1), 80-86 (1994)
   PUBMED   7545947
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..597
                     /product="Hsp70 family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
                     /calculated_mol_wt=64784
     Region          6..>468
                     /region_name="DnaK"
                     /note="Molecular chaperone DnaK (HSP70) [Posttranslational
                     modification, protein turnover, chaperones]; COG0443"
                     /db_xref="CDD:440212"
ORIGIN      
        1 mpakyvigid lgttnsalay aplgvdkpev qllpipqlva pgmvenrqll psflylaskh
       61 egstgaydip waqgrdfavg emalrqsael pdrtvsaaks wlchsrvdrh qailpwnagd
      121 dipkvspvta srrylehlia awetahpdal madqqviltv pasfdasare ltreaasaag
      181 lpdamillee pqsavyawlt tigerwrkvl kvndtllvcd vgggttdltl vrvteeegel
      241 tlkrvavgnh llvggdnmdl alahhvaglf akkgvnldpw qsvslwhscr qakevlltad
      301 gpkkhpisvl grgskliggt vtvdvakevt lqlladgffp ackvedkpar nrasgfqevg
      361 lpyeadaait khlasflqsh gsdegparpt hvlfnggvfk adpfrtrlld alkswfpeqp
      421 pqilegvhdl dhavargaay ygwakekggv rirggtarsy yigietagla ipgaprplra
      481 lcvvpfgmee gtevevpsda iglivgqpah frffssatrk ddspgvrlqr wtddeivetd
      541 sleatlakdd aiddhyvpvq fhtrltelgv lelwcvstrg sgrwklefsv redvegq
//
LOCUS       WP_010583565             449 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Schlesneria paludicola].
ACCESSION   WP_010583565
VERSION     WP_010583565.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..449
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48439
     Region          23..427
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(37..38,41..42,45,77,127..128,130..132,135,155,
                     158..159,162,249,252..253,256..258,261,289,293,349..350,
                     354,358,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mqepsserpt pastldappt ktrflvlavl cllsgvlyld ricisqalps isrdlklsht
       61 dksyilmaft lsyglfevpt grwgdliggr rvltrisiww saftaltgac tglysmitvr
      121 flfgageaga fpniarvlsr wfpdaergra qgillaasqa ggavapllas rliatigwrw
      181 tfatfgavgv vwavgfwrwf rddpaahqsv naaevahigr rvtagdvhga ipwaavvrnp
      241 svwmlsvlms fasfnsyiyf swfqtylieg rgvaeirtgs mtsmvlafsa vgtffggvvl
      301 dyvvhgagvs rrrmvgglaf flaaaslsta lmssdpwtat lftaiscflt qstqplwwsc
      361 aigisgrhvg alfglmnscg vigalssqyl vgavadwlgr hgysgrtqwd piffgnvgvl
      421 iaagilwscf rfvtvesddd eatlshvnh
//
LOCUS       WP_010583620             323 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Schlesneria paludicola].
ACCESSION   WP_010583620
VERSION     WP_010583620.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..323
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36524
     Region          11..295
                     /region_name="AKR_AKR11C1"
                     /note="AKR11C family of aldo-keto reductase (AKR);
                     cd19086"
                     /db_xref="CDD:381312"
     Site            order(19..21,50,55,81,128..129,159..160,181,209..215,263,
                     280..285,288,291..292)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381312"
     Site            order(50,55,81,128)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381312"
ORIGIN      
        1 mkyrrlgrtn wmvsevgygm wgmagwtgsd leevnralrr svalgcnffd tawgygagks
       61 egilgdlvrd fpdrklftat kippknfkwp slrefsledc fppghieqyv tdslknsgls
      121 sfdlmqfhtw edswlkddrw yhtmsdlksq glfssigisq nrwepwngve avksglidcv
      181 qviynifdqn pedelfpacq kydvgviarv pfdegtltgt ltksstwaeg dwrnsyfvpe
      241 nlhasvdrae alrpliptgm tmaemalrft lsepivgtvi pgmrsirnve anmaasdagp
      301 lsadlrknle thrwvrqpte wsq
//
LOCUS       WP_010583761             163 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Schlesneria paludicola].
ACCESSION   WP_010583761
VERSION     WP_010583761.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..163
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17988
     Region          6..146
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mkvevkrilf ptdfsppaqq alqyamslae rfqaelhvmh viaplpvtlp dattswtipd
       61 stqdilleqt rrrlseligq kwaeqhrtil vadvgfavde ivryakqedi dlivvgthgh
      121 sgfsrlllgs vaeklvrisd cpvltihptg hqfvdevgta tkg
//
LOCUS       WP_010583786             498 aa            linear   BCT 01-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Schlesneria
            paludicola].
ACCESSION   WP_010583786
VERSION     WP_010583786.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..498
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53048
     Region          41..298
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 midwkwtali vlagtvlpls aadlndlttv gstptkvvgd ckftegpafs pkgfllfsdi
       61 pnsrivrlda dgstseflsp sgkanglvfd aaghlyacqg gsrrvvkiai qdgkiealad
      121 rfdgqplnsp ndlaldgkgg lyftdpryga dmkidqscmg vyyvdasgkt trvidslkrp
      181 ngilvsidgk slyvaepner qlwqyqitap gklsagkiif tgdatkdggg pdgmcldqhg
      241 niyttyngiv vlspagelig ridvpehpan ctfggadgkt lyitartsly slpmkvagap
      301 laergpspap qvsrrqsfrg amhltqdkna gddakeveik gikllipanw kpekpsnnlr
      361 laqykppaad gdkptaelvv ssfggdgggv dqnlkrwndq ftsegrkikl ttgdcpqgky
      421 tlsdisgtyl qssggpfagg kktpmpeyrs lsvvllvpde gayflrftgp ektitacaea
      481 frksfgadaa keteyvlk
//
LOCUS       WP_010583773             589 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Schlesneria paludicola].
ACCESSION   WP_010583773
VERSION     WP_010583773.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..589
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=64348
     Region          17..195
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msiaelnael itaspapsdp elierfvgar dqfafaelvr rhspmvlgvc rrvlrdandi
       61 edafqatflv lirdarrvrk qtslaswlyg vayrislqvt rqkrrrrett lveednvidl
      121 gilagvadrh dhqlldaeln alperyrqpl vlrylagksp sdvatelglt vgavegllkr
      181 gkdelrqrll krgvtigaal taiqlaqgst savasealie atvqtglawd fsscrfaper
      241 issqhistra lelagkevfv mttgtkavlt igltlgclal atgtigyfde gsqgtaqaag
      301 ivstlsalqg ienaasiatl avdpiqaads kpanserpqs defkpgskna tfnssesett
      361 daftkakdvk lpfgsvqlpk pirkkwdtkk rsakaqqilt elevnseanf vdtplheaid
      421 vfksthgiav qfdnkalsde gistdvpvtl tvneiplknt lrlmldplal dyvlendqli
      481 ittqtraqnt fetrvyfdkp liaspannap llkqlvevip ksvhpdswap qkdgdrvage
      541 aegtisifeq kliirqtqri hdeineflde llgeqrvdet kptkanpgf
//
LOCUS       WP_010583824             133 aa            linear   BCT 01-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Schlesneria
            paludicola].
ACCESSION   WP_010583824
VERSION     WP_010583824.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..133
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14707
     Region          7..130
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 makpegtlta aqleileviw sgpqtgstvt eiwdaittqr evtrttvlnq vdrlekrgwl
       61 hrkkhddgfr yvaafareva trsvaeqfve affggsaadl vssllgskkl kpdevqrlrk
      121 lldsgssprk pkq
//
LOCUS       WP_010583828             716 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Schlesneria paludicola].
ACCESSION   WP_010583828
VERSION     WP_010583828.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..716
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=80063
     Region          23..201
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mnelkfqtgq advttgttdv tdsqllarfv tqrdqtafea lldrhgrmvf gicrrilkrh
       61 hesedafqat flslaqyaaq isqpallvsw lhrvarhaal kvrtaaskrp riepsgelem
      121 diavecspds ptlwadvspv ldeelarlsd plrcvvilcd iegktrkdaa rqlnwpeatv
      181 ssrlmkarsl ladrltrrgv alsavtlavl ltqnaaaaav pgplvaatlt tagvgatqtt
      241 matgtfskil smlgsikhsv vlatvaltvv astlivaagi glkpkpnane lrlalapipl
      301 vppfeeiaaa yrqnyatiqs irveyrirse tlmdpevlwk gwrrspipde ertaslvidh
      361 qkthysersr frslnfiade ikkkqpqrfv nlnapatsvl syreilewsp rarietreni
      421 qvydgsvvrn nnsglelkdd qhvarpnfvf qlpsqmdrem fnsrnyldli qfgitgaalp
      481 hdfkyrqrhr lsdllsqgvw hvvteheqld gsdcvviesa dtdrlwldrn agfalrrqtk
      541 qrpyridnef cdlrqvagqi wmprriietr yaenmvpkdy lgrpavrtey eltfielnqp
      601 vsdeyfqlvp pehstvfdlt lkpldangkp ietgtipgns lqardsqpsd ataapkvalq
      661 aqielgkqip sadsrpdvgq tpqlstaail irrfvilnlv vlliavgfiv yrrrsr
//
LOCUS       WP_010583950            1042 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Schlesneria paludicola].
ACCESSION   WP_010583950
VERSION     WP_010583950.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..1042
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=115756
     Region          1..1032
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mslfeshvee aslswfgelg ysighgpdma pdqasaeras fgdvvlvgrl rdaidrlnps
       61 ippeareeal qsvlhpdaai asrinrafhe tlrdgvevey krpdgsvagd hvrlvdfgdv
      121 tkndwlavnq ftvieshhnr rpdivvfvng lplailelkn aadeeatiwt aysqlqtyka
      181 eipsllnfne llvvsdglqa rigsltanqe wfkvwrtidg esdapkatle levlirgvfe
      241 rqrfldmlqh fivfeedpds gslnkivagy hqfhavnaal eetvrasgmg ksarqaggkp
      301 gdrragvvwh tqgsgksysm lfyaarvvrh ppmenptlvv ltdrndldeq lfgqfqrche
      361 ilgqtpvqaa nrehlrqlls vasggvvftt iqkflpekde rmpmlsdrqn ivviadeahr
      421 sqydvidgla rnlrdavpna sfigftgtpi ekkdantrav fgnyisiydi qqavadkatv
      481 piyyesriak lslneaqlpr idaefdeite geeesnrdkl kskwaaieal vgspnrialv
      541 akdlvahfek rveamdgkam vvcmsrrici elhnailalr pgwasakddd kevenrqdcv
      601 vkvimtggad dgpnwqphir nkekrkklat rfkdtkdpfr ivivrdmwlt gfdapclhtm
      661 yadkpmqghg lmqaiarvnr vfrdkpgglv vdylgladql kqalatytes ggkgdptydt
      721 qraieamlek ygiatamlhg vnwdkwttgt aperlslipa gqevilgqkd gkkrfvqvvt
      781 elsqafalca asdeaielrd dvsyfqaiqa alnkqstgsr ktpeqldaav rqlvskaitt
      841 dgqvidvfta aglpkpdisi lsdqflaevr glkhknvaae llekllkgei kirakrslvq
      901 sqlfseklkk tlnayhnrai atqevideli klakemeaag krgedlgltd deiafydala
      961 tnesavqamg ddklkviaae litqvrksvt idwtlregar akirvmvkri lnkygyppdl
     1021 qeeavkivlm qaellcadwa ev
//
LOCUS       WP_010583980             342 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Schlesneria paludicola].
ACCESSION   WP_010583980
VERSION     WP_010583980.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..342
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37457
     Region          18..249
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mklnvsqges vgtpilclen ltkrygsfta ldnlslslna gqilgligpn gagktttiki
       61 lvglirptsg satiagvdcv rnpmhikslv gympdkfgsy dnmrvreyld ffgsafkips
      121 sirtkrvnev memtgtaymk dryveslshg mqqrvglart ilhdpkvlil depvngldpq
      181 ariemrdlli elarqgktlv itshilpela ricqqvaivt ngklrafgtv eqigrqvsqk
      241 rtieaqflss dqvataadii rkslessaev veahaeatvr frtaqpetvl gallerliks
      301 nlnvtqfrel qtdleeafis ftrpqdsnke kkqattgaka da
//
LOCUS       WP_010584051             162 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Schlesneria paludicola].
ACCESSION   WP_010584051
VERSION     WP_010584051.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..162
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18007
     Region          5..146
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mnirisrilf ptdfseparq aqkyamelad rfqselhlih ivpevymplp dastswtmpv
       61 tnlqadveia skrlqnevnr pwadshqivr hvevgnpvna iityakthei dlivvgthgh
      121 tglshlllgs naekvvrlat cpvltihpkg hqfviddnpa nt
//
LOCUS       WP_010584114             463 aa            linear   BCT 01-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Schlesneria paludicola].
ACCESSION   WP_010584114
VERSION     WP_010584114.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..463
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=50604
     Region          13..451
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mthliefage tqsnavrrvi aetepvalrt ftpsqavfak sagvfhwtpe grtlydyssg
       61 vlvanlghnp krwmqsfgky mgwsadlfsg kpaqaddyvp altmtayngi tevetqavqr
      121 llanlhrspg snrlntivwa asgseaiqka lwaslardrt rdmivatrfg fhgkkglana
      181 vtgsekdaer dprvkfisfp meeildagyr tdsvnldryr neldelwrqf grkltclite
      241 pylggggsfh ppagyhqmlq qfcrehdmlf ifdevqanfg rtgamyafea ygvepdmvvl
      301 gkglgngvpv aavatrgdvf gvmkygeasd twsanplsca avlatldefe stevlkhtre
      361 ltpiflkgle rlkstglvnh vrgeglvfgf ecapfgsltp aevaakivea cyigrdnvgi
      421 hllgalagkv lrvsppltit taeanhslel lydlvsslak klk
//
LOCUS       WP_010584236             304 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Schlesneria paludicola].
ACCESSION   WP_010584236
VERSION     WP_010584236.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..304
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32633
     Region          45..258
                     /region_name="BD-FAE"
                     /note="pfam20434"
                     /db_xref="CDD:466583"
     Region          <235..300
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mpksicaavl cglillpwha skcddavrrt edvvygrkfg maltldlfqp akpngagllf
       61 lvnggwlssk stplmvtvrp ddyrvflerg ytvfaivtss qpkfvisdei ddvlraarfv
      121 rfnaakygvd perlgvmgss sgghltlsla trggpgnaea adpidrtssa vhaaacffpp
      181 tdflnygspg amgvgagpma plqvafgpsa ltsegreqlg raispiyyvt kslpptliih
      241 gdkdevvplq qaeifvakar seqapfvqli vrpgkghgwg dfwksaedie afanwfdqhl
      301 lpkk
//
LOCUS       WP_010584242             153 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Schlesneria
            paludicola].
ACCESSION   WP_010584242
VERSION     WP_010584242.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..153
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16853
     Region          1..137
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mislthspid yhaltesvrs pqsgavvlfl gtvremtgqr rtvalnyeay ptmaerklge
       61 letaararwp idqvgivhrl ghlelgeisv avavscphrk qafeagqfli delkvsvpiw
      121 kqenwddgst ewvdptadss qpppspdnsp rhc
//
LOCUS       WP_010584294             312 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Schlesneria paludicola].
ACCESSION   WP_010584294
VERSION     WP_010584294.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442503
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..312
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33931
     Region          12..281
                     /region_name="AKR_unchar"
                     /note="uncharacterized aldo-keto reductase (AKR)
                     superfamily protein; cd19097"
                     /db_xref="CDD:381323"
     Site            order(17..19,55,60,85,126..127,152..153,173,202..208,243,
                     260..265,268,271..272)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381323"
     Site            order(55,60,85,126)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381323"
ORIGIN      
        1 mltkawkefh lsrlmlgtvq fglpygvanr tgqpdfrhvv dmlsaaiegg vncfdtaaay
       61 gtsedvlgra ldelgaanrv tivtkvralt paeladpqaa riaieksvse srqrlrldcl
      121 pvvlfhread atyqnvlael kakgwlryyg vscdnrpgpa arfvadehfs alqipanild
      181 prhprsgvfq aagqrdvaif irsvylqgll vmpdedippa lcdvlparhr lallaadagm
      241 dlaelalrym lsfddvtcvl agvetvaqve hnlamvnrgp lptdllsria paipelpeti
      301 vnpglwpprk vd
//
LOCUS       WP_010584322             430 aa            linear   BCT 01-JAN-2025
DEFINITION  phenylacetate--CoA ligase family protein [Schlesneria paludicola].
ACCESSION   WP_010584322
VERSION     WP_010584322.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 430)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..430
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47408
     Region          8..429
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mirgaivdtl srselskwqs erlselltav ipanpfwtrk faeagvdpss irslenlrrl
       61 pfttkaelae dqqahppygt nltfpvanys rlhqtsgttt grplrwldtp sswnwmiecw
      121 stiyrlagll pedrfcfpfs fgpflgfwag fdgasrqgnl cltaggmsse arlkmifenq
      181 vtwlcctpty alrlaevaaa qdidvatssv ravlvagepg gaipsvreri tsawgarvfd
      241 hwgmtevgpl ateceddphv ltvnesacia eiidpqtlqp sadgrgelvi tnlgrtgspv
      301 fryrtgdlve adlsphpsgr twlrlrggil grtddmliir gnnvfpssie aivrgfttva
      361 efrivvtqhr emphvrlele phptadtstl vssvtvaike qlqfqaevll vpsgslprfe
      421 mkakrlvres
//
LOCUS       WP_010584326             132 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Schlesneria paludicola].
ACCESSION   WP_010584326
VERSION     WP_010584326.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..132
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14523
     Region          12..132
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 msdqppirvk sidhvtivvk dlnatrrfyv dvlgmeevar pnfsfqgqwf qagatlihti
       61 lefegsspag ftacanlrgh hfaflvddcr asakrieqmg vpfvsppkqr pdgaiqlfin
      121 dpdghlvelc sn
//
LOCUS       WP_010584342             345 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010584342
VERSION     WP_010584342.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..345
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37779
     Region          1..344
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mqtigvgmig sgfmgltyse vvakhaegcr lvaitggrra atlaadygvt aeasveslla
       61 rkdidavvla tpdldrlelt rqaaaagkhv laekpmaptv aecdemiavc kaagvnlgvv
      121 kteryrkitr kakefidnge mgpvrmlrtv safpqslakq lfderawmtd prggglfmgm
      181 ashntdflrw ltgrnalrvf aqattysdlp gpplsvmani vfedqimadm witselpdps
      241 lpssevrfqv fgrdamldle nfeyldvsrs gkweriytpe rfdylkepks pirlfphrgv
      301 iqdfidsire qrpphvggae graaveicea clisartgqa vnlpl
//
LOCUS       WP_010584362             411 aa            linear   BCT 01-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Schlesneria paludicola].
ACCESSION   WP_010584362
VERSION     WP_010584362.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..411
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44894
     Region          8..405
                     /region_name="ArgD"
                     /note="Acetylornithine/succinyldiaminopimelate/putrescine
                     aminotransferase [Amino acid transport and metabolism];
                     COG4992"
                     /db_xref="CDD:444016"
ORIGIN      
        1 mhpaatrtsq qtidqfgqyv ipnykrypvs lvhgegnyvw daegkryldl fpgwgcnilg
       61 hcpprvvkai qqqvehlihi pntwfteaqg dfaealvrhs fgkvffansg teanegaikl
      121 arlhyatkdg atkaggtsky rvisftngfh grtfgsvtat aqpkyheglg pllpgfryap
      181 yndfqavesl vddetcaill epvqgeggvn iatdhflrsl relcdqrdml lifdevqtgm
      241 grtgewfgyq qsqvqpdimt lakgvaagva cgaficqdhi apslrpgmha stfggnplam
      301 aagiatmkti eedgllencr smsdrfrqhf ealktklpii kevrtrgmmi gvelnipatp
      361 avakcmergv linathdtvv rllpalnitp aqvdegcqvi aetlelmase a
//
LOCUS       WP_010584389             179 aa            linear   BCT 01-JAN-2025
DEFINITION  shikimate kinase [Schlesneria paludicola].
ACCESSION   WP_010584389
VERSION     WP_010584389.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..179
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19647
     Region          3..171
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 mlitligyrg tgkttiaprl aqrlkfdwid adieleriag rsirdifatd gepefrrler
       61 enlvrllkrn rlvlatggga ilndatrldl rgagpvvwlk asveaiskri lvdggafanr
      121 pnlttgggid eirtlvaqre plyqecatis vptdslpids vveqilnqlp anyrqetna
//
LOCUS       WP_010584405            1168 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Schlesneria paludicola].
ACCESSION   WP_010584405
VERSION     WP_010584405.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 1168)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1168
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..1168
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=127625
     Region          1..1162
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mirnlirwal dnrlivillt ialigvggfs lvhlnveayp dpapaivevi sqypgasaee
       61 verevtiple ialagmpglh strskslfgl shvrnqfeyg tdffrarlev lnriytatlp
      121 psvtptlant tptgeiyryi vkgpkdaleh dlytsadlks mqdwvleref rrvpriadvv
      181 sfggamkrye vqpdperlkg ygisldqlqk aitdsnsnvg gdfvvqgptv qavrglglig
      241 ggldptqtyp agadpaaval hlrknedrrl reirsivlaa tnnvpirlgd vvsggryssd
      301 tvtgergvvv gahplqgrva vsrplvdddg edrldengar iwedrpdvvq givllrkgeq
      361 slpaltdvka kvkdlnsnss kmlpgtmiet iydrtrlvdl tthtvrenvv lgivlvsfil
      421 lvflnhfqsa mivavnipla llfamsvlyf rgksanllsl gavdfgiivd ssvimveaiy
      481 rslsagekad lslkdrilsa sgdverglfy stiimvfall plftmqgpeg qifgpmadty
      541 afalggalil altlspvlcr tffanvkpvk dnlivqalkg fyggqlklal rfrwislglf
      601 lvmcamtavi ipflgaefmp eleegniyvr gtfpvnvsld evsdkaavar rllqkhpetl
      661 lilnqmgrpd dgtdptgfyn cefsvplknh ddwprvfanq gwrrwiygpl rsrskdelie
      721 dmnqelnasi pgvdwnfsqy irdnvmetls gvkgenavki fgpdlnklee iaeqvkatli
      781 nvrgienvgi frikgqanle faidrnkcal wnvsvanvqd vlatavggks ltqvvegerk
      841 fdvtlrwper lryneetild ipvevvgnvl aadegsgsdg nsgkidyagg rrtnlavtgs
      901 renmtysnla hvprrrlrdl vtpigangea dpdgafvrsg astiyrekss rliavkfsvr
      961 grdlagavae aqtktqnffd spysaewsge fqemqeavhr lviasslalv liivllylal
     1021 rslldafvvl snvvvmsmgg vwalyatgeh fnisagvgfi svlgvgimng lllvswfnks
     1081 rshgvplqea lidgiekrir pltmtaltai fgllpaavst qigsetqrpl aivvvggmit
     1141 imlmvnlipv lysfyghrep pegggvgh
//
LOCUS       WP_010584409             277 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [Schlesneria paludicola].
ACCESSION   WP_010584409
VERSION     WP_010584409.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..277
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30211
     Region          18..156
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mtesnvrrpk pldtvimvat penvafefrl agpfprfval fvdlallgvt laifavllgl
       61 fgdagsglfl faafvgwwgy galmetllng qtlgkkalgi rvvadsglai nagqallrni
      121 lryadllppv fpgvasmflt rrfqrlgdla aetivvidga rlrphpprga qlarefreri
      181 ptrfrpdsal vdalaayvgr rndlstarrr elantlaehf irawslppnt dpdlllcaly
      241 dratmdhfrr dddelpasgv adypgraarv vsaakse
//
LOCUS       WP_010584406             427 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Schlesneria paludicola].
ACCESSION   WP_010584406
VERSION     WP_010584406.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..427
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46668
     Region          45..421
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrwialvvli glpglismas saetadpipp apdhseaaav saridldecv alalashprl
       61 teynarisea hgsavqagly pnprvdsgnp qvigptrtgv ysigltqevv rggklkldra
      121 aaleaahqae wdsvrkrfev ltsvrqeffs tlaaqrrktl lqklleiskq sektsmnlfd
      181 aeqvsetdvl llrverrkae tslqgadial lgqrrqlaas igvsvmmvge vdgqltakvp
      241 dfnddevlar vmttspviqi anldvnrtvl llrraevepi qnlsvqagtq yqestanyqa
      301 lvglyvdvpl wnrnqgnima ahaavqrsma grlasqqelt khladsvtrf rvaeqaveny
      361 engilpdamr tlelvqkayg rgqfeisrll qtqrtvfean ldyisalenr lnaaadiagl
      421 lqleqfp
//
LOCUS       WP_010584417             302 aa            linear   BCT 01-JAN-2025
DEFINITION  HDOD domain-containing protein [Schlesneria paludicola].
ACCESSION   WP_010584417
VERSION     WP_010584417.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..302
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=33454
     Region          22..253
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mvapltaevd dlflppqali sqlksratel qmlpsiaiea mqlakkpdcs issyssvver
       61 dvklmtdmlk lansamycpt tpivslhqav lrlglvecqn liltasatsm mkrislgqkv
      121 irevlarhgf ttallalqln htfrfgflge eftaglihdf grtllaiaep dlfikidple
      181 fdetpdllsq ervligtdhc rfgayyaihq qlpeslqevi lfhhqpelsr gnqkltalva
      241 vadhmanhlq rydgcenydp ssnpflptla kyadsrfpqk fiemagavmt rahndaegms
      301 ks
//
LOCUS       WP_010584481             206 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Schlesneria paludicola].
ACCESSION   WP_010584481
VERSION     WP_010584481.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..206
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23551
     Region          6..192
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtsipptqpt llvrirnsnd hdawnrfvdl ygplvygflr krglqdadav dlaqdvfrqv
       61 staihrldyd tqrgsfrgwl ftivknrmla hwrkqqeras gdtdalqrlh eipqpgtled
      121 ssewdadyer qlfhfasqiv kqdftpatws afwqtaiegr pgkvvaqele mtvaavylak
      181 grvmtrlkeq ikllvgeesl psrptp
//
LOCUS       WP_010584499             313 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Schlesneria
            paludicola].
ACCESSION   WP_010584499
VERSION     WP_010584499.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..313
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33800
     Region          7..304
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mslfqkplrg ivppmvtpll nrdeldlagl drlvehqvka gvaglfvlgt tgegpslsyr
       61 lryelvertc eivagrvpvl vgitdtsvee alelsqfskg aganavvaap pyyfglgqae
      121 vreflrdvad esvlpmfvyn mpscvklslt vetieqlsdh knicgvkdsg gdiewyrqll
      181 klrsvrpdwt fligpehlma esvlmggdgg vngggnlypr lfvslfqaad rkdqkeidrl
      241 qeellrlgel ynicgagpag ylrglksgle aagicsgrva ppfieidete rtrvaalikt
      301 lglaqagkaa nvk
//
LOCUS       WP_010584568             304 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Schlesneria paludicola].
ACCESSION   WP_010584568
VERSION     WP_010584568.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..304
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33897
     Region          38..297
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mkylafaivl sligrttfae igvistaean rlietsaadh kpividtrgg ykdyfrghip
       61 tahhlnfdtl rgtdrgipvq ylpdeltkal lvragvdrnr thliyatgdt lpndeilsas
      121 mvayvlekfg vddiriidgg lrgwhqaklp vtqeyfgnps gtlpvkgnhe iaigidella
      181 skvrpgvvlv darpyneyvg nddvwlrkgh ipgaisfhwa rlmdsenthq frpltqtkse
      241 lesagvtpdr qivvycgtsr egsllrfylk hvaryphvrl yegswkeyas lkqhpaetke
      301 nkap
//
LOCUS       WP_010584504             292 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Schlesneria paludicola].
ACCESSION   WP_010584504
VERSION     WP_010584504.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..292
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31692
     Region          3..269
                     /region_name="SDR_a4"
                     /note="atypical (a) SDRs, subgroup 4; cd05266"
                     /db_xref="CDD:187576"
     Site            order(7,9..11,30..32,69..71,105..107,131,135,159..162)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187576"
ORIGIN      
        1 mrilvlgcgy vgrraaatwv adghevfalt rseqnaksfl eaairpilgd vcdpgslrdl
       61 paidltlhsi gfdrssgktq edvtcgglrh vlnhlpnscg rfiqisstsv ygqsdgewvd
      121 enatcepiqp ggqlaltaen llhetfsarg hgrvvvlrla giygpdrlls rvnalreglv
      181 lsgrgdswln lihvddavta iravatqele sihnvynvvd depitrrdyf eclarlveap
      241 tprfdpaqps argsgglnkr csnrrlreef nwnpayptmg vglpaalkas ie
//
LOCUS       WP_010584569             318 aa            linear   BCT 01-JAN-2025
DEFINITION  inorganic phosphate transporter [Schlesneria paludicola].
ACCESSION   WP_010584569
VERSION     WP_010584569.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..318
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=32576
     Region          1..318
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mlttllflav cfvaftngan anfkgvasly gsgttslrga llwgtattfa gsiaaaflae
       61 gmlkkfsgrg ivsdvlvqsp efvcavaiga altsflatrf gfpvstthal vgalvgagla
      121 gsgsqvhlea lgknflyplf fspivaallg svtylflrav rlapdhrtpl ldalhylsag
      181 aasfarglnd tpkmvalllv apgfdlrwgf lavaatialg glldadrvae tlgkkvtsmn
      241 pgqgfaaslv taglvttasf hslpvstthv svgsllgmga ttrqakwrki geillawvst
      301 vpcgailaav ayaliswl
//
LOCUS       WP_010584573             222 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Schlesneria paludicola].
ACCESSION   WP_010584573
VERSION     WP_010584573.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..222
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24850
     Region          1..209
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msdlltadsl sksrqaflel rerildgrlp pgthltlrpi akslgvtvta vseavrelvh
       61 eqlvdfepny garvkrfdae tvrsqhvlri aieceairrc tqlvanrkld elqslaeevd
      121 rladveenla earrrdfefh lqiaehsgvp slaavlrsch lvrllavdav hdeamsapnr
      181 thvelvaair srdvdiaeka mrdhcersll lqlrrtfgti gi
//
LOCUS       WP_010584577             452 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Schlesneria paludicola].
ACCESSION   WP_010584577
VERSION     WP_010584577.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..452
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48721
     Region          13..423
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mnastattvg lkrtvpllml vvacghfnri sisvigneql ipkygispdr mglvysafll
       61 fytvamlpgg wlidrfgpra altllgfgsv vfvglsgcta ylskdveaiw isllivrsfm
      121 gvfnaplhpa aarmvsqcve prsrvlangf vtfsacvgma atysvmgyli dhcgwtwalg
      181 vssvmtlivt lawtsgtqrs pkepqssppn aqihdgqlsl whvlrqpsvi citlsyaamg
      241 yfqylffywi nfffetvqqq drsvarwyat iitlsmglgm vgggwlvgqi parlsprwrr
      301 slvpvlgmis sglifevgll asnphvtlvl laisaaliga cegsfwttsv elggryggtt
      361 aslmntgcni ggtlspsltp vmsqifaqyy gqdlgwrisl avaggivvag aflwwginps
      421 aqeddqasve srfqgplder sirdvltpqr gg
//
LOCUS       WP_010584610             147 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Schlesneria paludicola].
ACCESSION   WP_010584610
VERSION     WP_010584610.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..147
                     /product="VOC family protein"
                     /calculated_mol_wt=15953
     Region          12..141
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(12..16,32,68..69,72,89..94,96,100,129,139)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mpasqttnlq pipylsfngt caeamrfyek llggkikvmm sgaetpmadq ipkefanrim
       61 naqlelpggs llyagdcpah lpydgikgvs itlnfnhvde aeaifnklad ggqvtmpfsp
      121 tfwakkfgml idkfgvpwii ngellpi
//
LOCUS       WP_010584614             294 aa            linear   BCT 01-JAN-2025
DEFINITION  bestrophin family protein [Schlesneria paludicola].
ACCESSION   WP_010584614
VERSION     WP_010584614.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..294
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33066
     Region          1..293
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mpipessfwf dvfprdplsh kyvrhvlksl lpfvgvgiav yvldrftpvt mdigiapyem
       61 agavlgvflv lrtnsgydrw wearklwggi tnqcrsmata aaaygtdpvw kaeiicwitl
      121 fahatrrhlr gehelpeamr llrgplaaev prsphppqmi amhlarllre gsesgqlpda
      181 ilmqmerdrv slldymggce rivktpipra yntiirqflv lflvtlpfgi iqkvtwmtpf
      241 vtafvgfpll aldeigtelq npfalsqvnh lplgqicqti ednlrellpp akqd
//
LOCUS       WP_010584641             177 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Schlesneria paludicola].
ACCESSION   WP_010584641
VERSION     WP_010584641.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..177
                     /product="YceI family protein"
                     /calculated_mol_wt=19106
     Region          1..177
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mrqtfaalmv avgacglvqa eetkyslnge ntkiewtgtk adgkhdggfk qvkgtatlsd
       61 gsnlkfdvei dcgslysddp kltqhlkspd lfsvkdhpka kfkstkiekt sdgtqvtgdl
      121 tilgktkkvt fpaeiktgdt laikaafnin rqdfgmtygt gkinddvevr vdlkakr
//
LOCUS       WP_010584768             274 aa            linear   BCT 01-JAN-2025
DEFINITION  c-type cytochrome [Schlesneria paludicola].
ACCESSION   WP_010584768
VERSION     WP_010584768.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..274
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29891
     Region          45..258
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 mkrlfvvllc gvfvgfsrla wvgqaedqks lgthrtipeg plgeairlgk elvekttshe
       61 rtkpyvgnsl nctschlkng tdpqaasfig vaaaypawsp reksvitled rilncfmrsc
      121 ngirpplgsd vsisiaayit wlstdhplrm naerpagpha vpqlkvdvsq adferghqly
      181 ldrcatchae ngqgqkenpp vwgpqsfndg aglanisqla swlkvampld eadltqqeal
      241 dlaayinshe rpkfrlsehl ppsspseifs pkgk
//
LOCUS       WP_010584775             214 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Schlesneria
            paludicola].
ACCESSION   WP_010584775
VERSION     WP_010584775.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..214
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23477
     Region          7..176
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mndtdptska sathgvilta avnvfaaegf rntdvqviad ranvgkgtvy rhfgnkaqlf
       61 vataqfcieq lgefvshqlg khptieafie akgaaellhr iaracaqfyq qnppfleimi
      121 qervefreae nplqvvfrqn aragldrime igikrgefrk gdatsvsdaf sdllygclvk
      181 gcfegdaskl vervehaiel llngivrrsp rstg
//
LOCUS       WP_010584791             103 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Schlesneria paludicola].
ACCESSION   WP_010584791
VERSION     WP_010584791.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..103
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11378
     Region          7..89
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(25,28)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mseltreeld qrggatvvef gtswcphcqt iqskmasllt qypqiqhlki edgpgqrlgr
       61 sfqvklwptl vfmregrvig qvvrpsqkem edgfstlasa agd
//
LOCUS       WP_010584842             437 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Schlesneria paludicola].
ACCESSION   WP_010584842
VERSION     WP_010584842.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..437
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47713
     Region          1..392
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mprvlivggg faglnlakgl gdvpgvevlv vdrtnhhlfq pllyqvamag lspadiaapi
       61 rsllarfnni rvlqgevrsv dtdrnlvvtd fgelpfdylv lacgarhsyf ghdeweefap
      121 glktleqate irrrvlsaye saerttslee rkrlltfvvv gggptgvela gaigemsrft
      181 lakdfrnida tlarvillea gprilgmfse qlsaraardl eqlgvqiwtg savtkidang
      241 vdigneriis atvlwaagvk asslgkdsgf evdrsgrviv endlsvkghp nifvagdqsc
      301 ythqtgrplp gtapvamqqg cylanlirid vqggkrtpfr fadkgqmati grsravvevg
      361 kfkmtgfiaw mawllvhiyy ltgfpnrlrv vlnwgwsyit frrgarlivp kewrfgqaae
      421 erpkvatvpe apvkvsa
//
LOCUS       WP_010584852             303 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Schlesneria paludicola].
ACCESSION   WP_010584852
VERSION     WP_010584852.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..303
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32703
     Region          46..264
                     /region_name="BD-FAE"
                     /note="pfam20434"
                     /db_xref="CDD:466583"
     Region          <235..299
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mqgirvglpl iallacvgtn laaqdlpfiq hqnvvyaevh gialvmdvfv ptgdknglai
       61 idvvsgawhs drskirdhml tqtfhilckk gytvfgirpg siskfsaiem rqnvnqgihw
      121 vkshateygi dperigmmga sagghlaclt avtaedgspi dgkkpstgdt rvkavavffp
      181 ptdflqygdk vidpsaddql gkitrrlani dseenpsaee msqmlakisp arlvtskapp
      241 fllihgdadp lvplqqsetm vselkkagvp aelivkkgga hpwftiheev qvianwfdkq
      301 lan
//
LOCUS       WP_010584860             166 aa            linear   BCT 01-JAN-2025
DEFINITION  FHA domain-containing protein [Schlesneria paludicola].
ACCESSION   WP_010584860
VERSION     WP_010584860.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..166
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17681
     Region          15..96
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mpaflvpvda nqslipleka ivligrqsdc dvsltnsrki srkhcciaqv netliirdlg
       61 stngvflngn rvekeamitv gdeitigdih ftlrseipat akaggakngk gtekpnaspr
      121 gvppipppvp aasrkpllip ssaelnlkfd eessdeqptt prprrs
//
LOCUS       WP_010584862             172 aa            linear   BCT 01-JAN-2025
DEFINITION  MOSC domain-containing protein [Schlesneria paludicola].
ACCESSION   WP_010584862
VERSION     WP_010584862.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..172
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18479
     Region          16..168
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mpvetltsll ntlpqqgrlr wigvrparlt pvqsvekail fvgrgiegdh rfggrigskr
       61 qvtliqyehl qavasllhrd dvapelarrn lvisglnlla lkgkqfrige vcleysgpce
      121 pcsrmesvlg pggynamrgh ggitakvivg gtihvgdamr aipspqsqss pr
//
LOCUS       WP_010585000             162 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Schlesneria paludicola].
ACCESSION   WP_010585000
VERSION     WP_010585000.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..162
                     /product="VOC family protein"
                     /calculated_mol_wt=17641
     Region          15..140
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(15..18,20,35,50..51,58..59,61..63,85..87,89..94,100,
                     121,126,134..137)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 mssssqpipp ghecliphlv cspaseaief ykkafgaeev vrlpspdgkr lmhaslrvnn
       61 gfvyladdfp eycegkseta ialkgtpvtl hqytkdcdaa iqrakaagat vimpatdmfw
      121 gdrygvivdp yghkwsfath qkdlspkqie qamndaygqa pq
//
LOCUS       WP_010584960             211 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Schlesneria paludicola].
ACCESSION   WP_010584960
VERSION     WP_010584960.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..211
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21350
     Region          1..191
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mgkylaefig tfflvltigc tvaskepmap laigsalmvm iyagghvsga hfnpavtlav
       61 tmrgrcslad aipyvvaqvl aaiaaaitvg flipadklsa itaidlsktv pqallaeglf
      121 tfalayvvln tatakanann sfyglaigft vltgafavgg isggafnpav avgismlgft
      181 swsniwiyli gdlaggalaa iafkiinpsd k
//
LOCUS       WP_010585073             466 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Schlesneria paludicola].
ACCESSION   WP_010585073
VERSION     WP_010585073.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51404
     Region          1..446
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mndsvrlpfr plfcysignv tltaiygylg afllkyysdh vhldpawigw aflvrsvvda
       61 avdpligfws drsrfsqgrr rpffligsip aallfywmmt ppdgsqflif iyltvtstlm
      121 vcflslmgis hlalgfeltt dydertrlfg yknlvenltt lvatfsvpla lllsgyslag
      181 helsradcyc laaaalavls vvaalvayfg tserptpsdq qtfrfvdgvv aiiqnrafli
      241 llgvfvlmti adrvtsaelf ivlehfhglk eedslallvg lfagalisvw pwvwlaqryg
      301 kdiilrlaia lwpitciafv arqwtmvelc aitfgmgvfg tgmitilgai vpdvleydrh
      361 htsqrregmy vsignlvyqi amgvgfliag qtlhaigyrg esevspnlvl glrvtyaavp
      421 tvlamgasla lvyfpiskrs yqelvecres hvslapiast anpeir
//
LOCUS       WP_010585083            1171 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Schlesneria paludicola].
ACCESSION   WP_010585083
VERSION     WP_010585083.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 1171)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1171
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..1171
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=127950
     Region          1..1167
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mvallikwsv nnplivilgt ialtvlgiys fqnvnveayp dpapaivevi aqnrgrsaee
       61 merlvtaple vslsgmpglk slrskslfgl tyinlqfeyg tpylsarqev lnriasadip
      121 pdintgispr spigeilrys lncendangq plyslndmrs iqtwtlertf rripgivdvv
      181 smggttkrye iqpdpdrmkr ygitldqlqk avaasndnvs gdylsqgdsa avvrgiglig
      241 rgrdpvqrtl tlktpevavq hlrreddrrl meirkitlks tnnlpiridd vvdggplkpg
      301 qsaseakgvv ishltrlgka alsqpkldad gkpvldeqge rvwidedeii qglvllrkga
      361 eslpalqkik akieelnqsk gilppgvtiq vfydrttlik tttetveenl llgilfvtvi
      421 llmflsnvrs aliiainlpl allfaftvlf frgqsanlls igavdfgiii dstvimveni
      481 yrvlstgkya dlplsqrivr astevqralf fstmimvcam lplftmrgpe gqlfrpmaet
      541 yafaiggall lsltiapvlc lmlfknlkts gdnffvrflk rgylknlevc lnhrwlvvla
      601 fsamiagtaa tlphlgrefm paleeghiwa raifpvgvnl eenskksqia reimrsypev
      661 elvvnqlgrp dsgadptgfy sseffiplmk qeewpaivpt tgwrawlgsr rprtkpelvr
      721 elsdrltaal pgvnwnfsqv irdnvlevls gvqgensvki igpdldrlee lgqqavlams
      781 glpgiqdvgy ykingqsnva lpidrekcsl wnvsvadvhd viqtaiggkt vsqmiegeks
      841 fditirwpap lrrdlssild ipvvvtentv ttsvasgkds nptlattgaa apalpitgns
      901 rggalpetlt apierlrdlv tplgvdpdgp lspdghfvrs gvsmvsreeg qrlvaikfsv
      961 rdrdlasavk daqaavrkli ptgyrdewsg efknmeegeg rllvivpmsf vlvfillyla
     1021 frslldatvv llnvvslslg giwalfltgt nfsiaaavgf tsifgvaimd glllvssfnh
     1081 hraegmplre aimagaeqrv rpvmmtalta ilgllpaais tkigaqsqkp laivvvgsmi
     1141 ttlfltrylm pvlysfygsr epvegaadle h
//
LOCUS       WP_010585117             354 aa            linear   BCT 01-JAN-2025
DEFINITION  ADP-ribosylglycohydrolase family protein [Schlesneria paludicola].
ACCESSION   WP_010585117
VERSION     WP_010585117.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..354
                     /product="ADP-ribosylglycohydrolase family protein"
                     /calculated_mol_wt=38114
     Region          8..310
                     /region_name="DraG"
                     /note="ADP-ribosylglycohydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG1397"
                     /db_xref="CDD:441007"
ORIGIN      
        1 mtspqptdsi agailgcavg daiglpyegl srqratrlig vpnrhrflmg rgmvsddteh
       61 tcfvaeslcr eprdvdqfar elgirlrwwl vglpagigfa tlratvklwl gygashsgvf
      121 sagngpamrs pilgaaiddl dllrdyvhas trithtdpka fhgalavaia awcakrglst
      181 pgaffekyrs lvdtdtsdef qglmktmass laagdsteif adqlgcrrgv sgyvyhtvpv
      241 vlhcwlshpr dyqssiqtvi rcggdtdtta aivgaivgae vgrsgippaw lnglcewprs
      301 vdwmerlada tdkamqtgdi qstpryvpiv glgrnavfls avmvhiarrm lppy
//
LOCUS       WP_010585123             183 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Schlesneria paludicola].
ACCESSION   WP_010585123
VERSION     WP_010585123.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..183
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20002
     Region          28..181
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mapvrvggqi agstsftfvm kditvarqki ttflwfdnqa eeaanfyvsl fknskvnrvt
       61 rnaeggpgra gsamtvefal sgvefialng gphfkfteai slsvdcesqa eidelwekls
      121 eggqksrcgw lkdryglswq ivpsaiselm sgkeptktrr ameammtmtk ldiqklkaay
      181 eag
//
LOCUS       WP_010585128             195 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Schlesneria
            paludicola].
ACCESSION   WP_010585128
VERSION     WP_010585128.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..195
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22085
     Region          1..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkrtatpdri idsafqtfsq rgvlkssled vataagltrv tiyrhfsnke alvaavcqri
       61 lrpfahaaam gptvtmkqyd nwllellkel rdlpvsqflp claeiqnafp dihrefrrqr
      121 esaieqifqn amrvvreagy wreelnplvv qvifrssvig lgenpqivsa disyeelclt
      181 vidvfrygtl kadar
//
LOCUS       WP_010585252             409 aa            linear   BCT 01-JAN-2025
DEFINITION  RidA family protein [Schlesneria paludicola].
ACCESSION   WP_010585252
VERSION     WP_010585252.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..409
                     /product="RidA family protein"
                     /calculated_mol_wt=45544
     Region          1..134
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
     Region          153..271
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
     Region          288..405
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mhkdflapkn hcggasgsgt qavragnlil vggqmsldeq grvvgddiat qtrnaleslk
       61 rvlaeagatm rdvvkhniyf qcegddeavs tflneidrvr leyfsapgpt ttetrvgldr
      121 egamiqidaw avvgeakerl mppghwnwsk pmpfshgwkv gdmvfvggqr sldekgnvqg
      181 igdieiqtdh afrnldtllr aaggdrntlm rqntyfrfyg qgrevtdywe kmtnvrrrym
      241 svpsaagagl ritgfpnsse liqvegigvl gedkqrlqpe nhwdwsipnt qftqgwrigk
      301 wafiggqisa dnrakavgkd metqtrnvfq firnvmaegd ldesdvakly iyyhcdgdwn
      361 qiaqtkatie rvqrefypap gpavtairvs gfafedllie ieafaisrd
//
LOCUS       WP_010585367             633 aa            linear   BCT 01-JAN-2025
DEFINITION  CocE/NonD family hydrolase [Schlesneria paludicola].
ACCESSION   WP_010585367
VERSION     WP_010585367.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..633
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=71785
     Region          40..629
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mherlrhssq lnlavvvisa vwwglfsqaa saqgiefvka nytksefrip mrdgkqlfta
       61 vyapkdqskt ypilltrtpy gikpygvdqy rgdlgpsalf gksgylfvyq dvrgrflseg
      121 dfvnvrpqrd qqretrdtde stdtwdtiew lmkhcpghng kvgmtgvsyp gfytnagmid
      181 ahpalvacsp qapvvdwfig ddwhhngafh laeavgfins vglprgeptt ksppkfdpet
      241 pdgyefllal gtltrigerc eksqvpywke lmahgtydgy wktrdlrphl rgirpavmtv
      301 ggwfdaenlf galetyrqie ghspeaknil vmgpwshgaw srsdgdqlga vsfnsktgqf
      361 freqielpff eyhlkgqgtl ehpeawvfet gtnvwkkydt wppksaeprt fylhskgris
      421 gdmptenesk lafdeylsnp akpvpytdkt tmgmtadymt adqrhaarrp dvlvyqsdti
      481 erdtvlsgpv evefyvsttg tdsdwivkli dvypndypdp kenptgirmg gyqqlirgdi
      541 lrgkfrngfd rpepftpgka elvkfkladi chvfrpghrl miqiqstwfp lfdrnpqtfv
      601 diyaaspddf qaavqrvyrs ylmpscirvl qqp
//
LOCUS       WP_010585427             437 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010585427
VERSION     WP_010585427.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..437
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48774
     Region          40..411
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mmnqstrrqf lqfgaaatas lslpigtrst fadqavkspn erwrvgaigm ryqgsvitrq
       61 aqafgdinli cdvdrhvleq arasfnssak ivedyhdlis skdidvvlig apdhwhakma
      121 idacragkdv ylekpislti eegraisrva aetgrvvqvg twqrhdqrfr laaemiragr
      181 lgkvtkativ lgknlqggpf aqvpipkqln wdrwlgqapm tpyiperchy tfrfwydyag
      241 gemtdtgahh vdiamwalgl dntgptqiip qgklpnvvdg ynvakdfsvq mkfangvefa
      301 ildtgrngil fegelgrifv nrgiisgtpv delksnplpr esfqvyahdn lsrperagky
      361 dalinhmgnf ydcvqsrktp issvesqhrv attchlgnla lrlgrtlnwn pdterfinda
      421 eadtylrreq rkgyevv
//
LOCUS       WP_010585476             260 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Schlesneria paludicola].
ACCESSION   WP_010585476
VERSION     WP_010585476.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27879
     Region          3..250
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtlhaadvsf qygprrvlnq vslsfapgvt glvgpnaagk stllkclcgv lsptghislm
       61 grsireysrr eisqaigylp qagfhrgglt vfetvllgrl hdlswrisst daqcvhslle
      121 emaltsvanr miqelsggqa qlvaiaqali rhpsilllde ptsnldlrrq feicsriqqi
      181 tksrgvitvi slhdlnlaar fadhiavlrd gaiyaagtps dvltakmmad vyqvdtevth
      241 dssgnptvfv rgpslgvpsv
//
LOCUS       WP_010585551            1025 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Schlesneria paludicola].
ACCESSION   WP_010585551
VERSION     WP_010585551.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..1025
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=111676
     Region          26..1002
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mswlveialr lrvavlalav llivagirli phlpldvfpe fsppyvevqt eapglsaeev
       61 enlvtfplen vligtpglda lrsksvlgls qiklllhqga dlyrarqlvq erlaaetprl
      121 pavsrppvil qplsslsrmm kigvwsekls qrdltelavw tirprlmaip gvanvaiwgq
      181 rdkqlqvlvd pdrlrahhvt ldavvksaad avvldaggfv dtpnqrmavr qlppiygped
      241 laktvvsfre gavlrlgdva hvqigsppai gdaiindgpg lllivekqpa anmlevtrkv
      301 eqalealkpg lkdveldpti frpatfiers idnlthallt gcilvvivlv aflydwrtav
      361 isltaiplsl vativvlyww gltintmiia glvialgevv ddaiidveni vrrlrlnraa
      421 atprsafrvv ldaslevrsa vvyatliivl vflpvffldg lpgaffrpla igyvlailas
      481 lltalvvtpa lslmilpnsq qssheapfsr wlrrpyqkvl pwfvsrpkss lgflavafia
      541 taflvnslgq eflpnfqetd flmhfvekpg tsieamdrit iqasrelrsi pgvrnfgshi
      601 graevadevv gpnftelwis idpnvpygpt lnkiqeavdg ypglyrdvlt flrervkevl
      661 tgasssivvr iygadlavlr skakevseam akvdgvanlk veaqvlvpqv qvrlrqdaae
      721 rfgltpgqvr ravttllrgm kvgevyedqk kfdvvvwgme dsrtdlnalh dlridtptgg
      781 qvplkdvadv eivpapnevk reggsrridv tcdakgrdlg svardieavv gtlpfdrgyh
      841 peflgeytar qesqrrlfsl gaisligill ilyidfqsvq ltlmvaltip faliggvvaa
      901 wiaggvlslg sligfvtvlg iaarngimlv shyrhlqeve gepfglglvi rgaeerlipi
      961 lmtvlttala llplaisgnk pgheieypla vvivgglvts tvlnlfllpp lyllwgrnav
     1021 vppen
//
LOCUS       WP_010585628             305 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Schlesneria
            paludicola].
ACCESSION   WP_010585628
VERSION     WP_010585628.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..305
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32682
     Region          4..298
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 makpiqgvlp iahtpflddd sidvtslarq ldwafaagad gfatgmvsel irltfeerta
       61 ltktlaelah grgtfvagvg aestrqaiqy aqiaekagad gvmatppmtt rapaaavrdy
      121 fvalaesisi pvivqdasgy vgqpipldvs vgllkrfgrd kilfkpeasp igpnlsalrd
      181 atggearifd gsggvclvdc yrrgidgtmp gmefltgiva lwkalerkdd aaiyrlyfpi
      241 calvslqlqa gldgflavek yvlhkrglft tdrrrppyay sldnetrael drllkclddv
      301 vnsgs
//
LOCUS       WP_010585673             668 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Schlesneria paludicola].
ACCESSION   WP_010585673
VERSION     WP_010585673.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..668
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=74470
     Region          10..668
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mtlgvkdvlg degsiarrlk tyesrsqqie maeaveqaia hrqhlvveag tgtgksfayl
       61 vptilaatak qgeggkrkkv visthtislq eqligkdipf lnsvlpvefs avlvkgrsny
      121 islrrmkgav dhakslysrp deltqlqdvv ewsrttydgs ladldfkpls svwdevhsdh
      181 gnclgkkcpt heqclyykar rriwnadilv vnhalffadl slrregvsll pdydivvfde
      241 ahtveqvaad hlgisissgq ieymlsklhn ektqkgllar atssnssflg tqrnaiqlvd
      301 rvrfqardlf dsiheakrsf agkngrfrhp ldihnevsta lkelgshiaq lgnqlssdee
      361 rveytsaaer csgladslns wlqqsleeav ywletsgpnq qriklvsapi dvgpvlrdel
      421 fnkistvilt satlavggqs fdfvrgrlgl tksdekkvgs pfdyksqmql ilpegmpdpg
      481 espsdyesav ceqiqkyveq tkghafvlft syqmlrncar rltswfvskn yglysqgeem
      541 prtmllekfr ndpagvlfga esfwqgvdvp gdalqnviit klpfsvpdhp llearleair
      601 nsggnpfmdy qvpeaviklk qgfgrlirtk sdkgivvild prvktkrygk lfldslpece
      661 ivrdhglr
//
LOCUS       WP_010585718             310 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Schlesneria paludicola].
ACCESSION   WP_010585718
VERSION     WP_010585718.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..310
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34624
     Region          4..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mlavdvqnlt iqygkleavk gislqippge vfgfigpnga gksstirvla tlqpnyrgva
       61 rvmelnirsk pqlvreqigy vpdffgvyed ltvreylhff aaayrlspqk rkavvedvlq
      121 ltdltgkids qvdslsrgmk qrlslarvll hdpavlllde pasgldprar iemrellkal
      181 kemgktiiis shilhelaql ctrigiieag rmvaqgsvae iyqrlgvlki vhvqvafqtp
      241 dlieqlrqle gvtqvddqvd risirfqegs levedlhdfi hkqgarirmf qpevmdmeta
      301 fmkltegqta
//
LOCUS       WP_010585778             521 aa            linear   BCT 01-JAN-2025
DEFINITION  formylglycine-generating enzyme family protein [Schlesneria
            paludicola].
ACCESSION   WP_010585778
VERSION     WP_010585778.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..521
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=59549
     Region          251..517
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 msrscrlsir ieqlqtrlcr giflslciaa tllihvgala aaedianlte klldadenef
       61 rdlfpklker rnavinrlrt evdvtfpsvd wpsnqvreri vqrqanaava lvklesplqv
      121 wpllkhrsds slrtllihrl avlqadveti tvhlyeeddv siqqalllcl gefgeglprh
      181 eraslipklk qmyrdeldag lhaavewllr rwkeeewltr tngelasdrv errrkigeiq
      241 qrlgfpsdna paqwyinlqg qtmvvipgpv efqmgspene dgrqpneirh rvrighsfai
      301 astavtveqf lrfrrehhyd knqaavptcp inlvtwyqaa efcnwlskre giskdqwcyi
      361 pddsdnytkg mkvaenlgdr tgyrlpteae reyacragte taysfgrweg pldqyawskr
      421 nsdkrshsvg llkpndwgif dmhgntydwc qdrylndptd fdhatkdtae lvddadnrvl
      481 rggswtdpgw sirsasrsdf apnvplgnvg frvartvkva k
//
LOCUS       WP_010585893             568 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-keto acid decarboxylase family protein [Schlesneria
            paludicola].
ACCESSION   WP_010585893
VERSION     WP_010585893.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..568
                     /product="alpha-keto acid decarboxylase family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62360
     Region          25..562
                     /region_name="PDC1"
                     /note="TPP-dependent 2-oxoacid decarboxylase, includes
                     indolepyruvate decarboxylase [Carbohydrate transport and
                     metabolism, Coenzyme transport and metabolism, General
                     function prediction only]; COG3961"
                     /db_xref="CDD:443161"
ORIGIN      
        1 marksttlka vngktstaki atsvkselti gsyliqrlqd ygltdifgip gdfvlqfygm
       61 leespikvvg ctredcagya adgyarihgl gavcvtycvg glslcnsiag afaekspviv
      121 isgapgmder ranpllhhrv rdfntqrevf ekitvasaal edpltafrei drcleaavrf
      181 rrpvylelpr drvhtkcpyp hvaktesfts dkdslneala eardvinaak kpviiagvem
      241 hrfsladdvv klaeknsipm catllgksvv sekhplylgi yegamcrdsl rryvedsdcl
      301 imlgafltdi dmgiftanld prkcidatse hmrishhhfh dilitdfvkg lgkldlkvak
      361 rpmlarpkga dakfvlrpdd kvtnarlfar indlldetmv vvadvgdclf gaadltiykk
      421 teflspayyt smgfavpasi gvsvaapdrr pivlvgdgaf qmtcmelsta vrhgfnpivi
      481 vlnnkgytte rflqdgpfnd ilnwnyhrmp dllgggwgfe vhtegeldqa lnaaianqda
      541 fsilnvhlep ddisqalkrl aeglsqrl
//
LOCUS       WP_010585989             331 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010585989
VERSION     WP_010585989.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..331
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36281
     Region          1..254
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mpkikigqig tahghaagkl etyraspeye vvgiaepdpr lkklaetqaa yrdlpwltve
       61 qllaveglqa vaieteprdl lkyaeagiea glhvhldkpa gesliqfrri ldqaarkhlc
      121 vqmgymfryn pavvlmknlv rkgylgepfe mhcvmskvvd dasrvknaay pggmmfelgc
      181 hmidivvdll gtptgvsafh qhsgnqadgl qdnmlavmty praiasvkss alevdgsarr
      241 hlvvcgtegt ihiepidspk fvrltlaker gpykkgtqev pvepykryva daadfakvir
      301 aekmldwsmm hdlavqetvl rgsaspldva p
//
LOCUS       WP_010586000             452 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Schlesneria
            paludicola].
ACCESSION   WP_010586000
VERSION     WP_010586000.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..452
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47621
     Region          1..448
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mpfeitvprl gwsmeegtfv rwlkkhgelv nagdalfele gekaaqdiea vdsgllvips
       61 napqpgtiva vgavighlva egeaapavvt gasasvtssi pktsapanps paadtstlee
      121 paaapsvrrl aremgvklas legsgpagri tandvrttgs rpstvaanhv lssiasprar
      181 rvakelgidw kgvkgtgrdg rvrerdvrts qsqprpasts tpttissrrr tianrmiasr
      241 ertapvtltt ridatnlvgl rlqfkqageg spipsytdli iklvalalrk hptlatrdeg
      301 gqwivpasad diyigmavdt edglvvpvvs raatlglfdl akqtlsliek artgkisaad
      361 mqggvftitn lgsfgidaft piinlpetav lglgrirrep vviddqivar dqmslsltfd
      421 hrivdgapaa rflqtvsqai enpsawllrg di
//
LOCUS       WP_010586059             352 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010586059
VERSION     WP_010586059.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..352
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37804
     Region          6..350
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 maasssssir vgvvgagdnt rrhhipglra vpgvsvagvv nrtpestara atelgipkqf
       61 atwqalvtdp gidavvigtw pnmhcaitca aleagkhvlc earmarnvae arqmqavada
      121 hpdriamvvp spfglpcdae mlqlmrdrfi gelrelvvig addqfhdysr flhwrqdaei
      181 sgfnvlslgi mhetllrwvp apirvfaqtq tfepvrpnpn gpgnrqvtvp dsvqvltqlp
      241 ggargvyhfs gidlhgpgkq ihlygssgtv kvlfgaqeri ligrvgdaql relvapanki
      301 ggwrveaefi gairgeepvt rttfpsgvqy mefteavars aasglpvdlp ll
//
LOCUS       WP_010586233             255 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Schlesneria paludicola].
ACCESSION   WP_010586233
VERSION     WP_010586233.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..255
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27618
     Region          2..254
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mrdyvqtaee aarraghvlr awsskftvre ksrsnlvtea deaaqaaihd fihgryphhg
       61 fcgeeglsva gndstyrwvi dpldgttnyv hgfpyysvsi glecrgemiv gaifdpihde
      121 mflavrgega tlnrrplrcs ainqldqalv iaslpvntdr hdeavrrfls vlpvaqavqr
      181 tgsaalnlan iaagrvdgfw stslkpwdma agillveeag griskidgsa fqlevpnlla
      241 snglalheql vaalv
//
LOCUS       WP_010586209             256 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Schlesneria paludicola].
ACCESSION   WP_010586209
VERSION     WP_010586209.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27237
     Region          19..239
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtalqsltgp pthptetlav acrqiikefg vgdtktvalr gvdldvlagq mtllvgqsgc
       61 gkttlisiva gllnatsgsl tvlgndmmhl tgtqlvqfrq knigfvfqqy nllptlsave
      121 naavpliiag qsrraafeaa keilsavglg srmhlypnql sggqqqrvai aralvheprl
      181 lvcdeptaal daqsgqtvme llrrvalqpd ravivvthdn rvfrfgdrii hmddgvvtkv
      241 dipdrasggd pestmh
//
LOCUS       WP_010586264             253 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Schlesneria paludicola].
ACCESSION   WP_010586264
VERSION     WP_010586264.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27784
     Region          2..242
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 miivdeltrh fssggktlva vdrlslsvks gevygllgpn gagktttlrm ilgllqptsg
       61 davvdgfrvs qfpdevkrri glvsasagly qwltpremll ffadlygiep avarerlasl
      121 aelldlkrfi dqrcatlstg qkqrvtlara lmhdppimll deptrgldvv gthvifqyis
      181 hlrsqgksvv vsthrldeas qicdrmglly rgtlrhegtf pelqqetgcq tlfemflqlm
      241 nqpatasptv tkg
//
LOCUS       WP_010586356            1096 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Schlesneria paludicola].
ACCESSION   WP_010586356
VERSION     WP_010586356.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..1096
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=120119
     Region          1..1053
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mfsrffidrp ifasvlsili tlaggiavfe lpiaqyppva pptvqvdcny pgasaqvvaq
       61 tvaapieqqv ngvenmlyms sqstsdgsyt ltvtfkpgvn lnlaqvlvqn rvslaipllp
      121 dvvrqtgvtt kkrspdillt vsincpdery dqlylsnfal mrikdelsrl pgisevlvfg
      181 qrdysmrvwv dpdklstlgl avsdvvnalr qenldvasgy fgqsptpsse sggapthqmp
      241 ldilgrlstv eefeqvvvrs gadgellcik digrvemgar sqdvsnrfds kptvglaifq
      301 lpdanaleta dlvkekmhvl sqtfpdgvry digydttpfi resieevvka lrdsvilvai
      361 vvlvflqgwr aaiipliavp vaiigtfaam amtqfsinnl tlfglvlaig ivvddaivvv
      421 eavehyiekg lsprqaaisa mdevsgpvia vglvlsavfi pcafltgivg qffrqfalti
      481 aistiistfn sltlspalaa lllkpksqgr dpltwlidvl fgwffwlfnr tfrastrvyi
      541 sivgrmlrvp alvlivyvgl lgltywgfqr lptgfiptqd kgyfiasvql pdstaavrtr
      601 dviariekia letpgiknvn svagnsfvls aygsnfgsmf iilknfedrh dksmsadeil
      661 ktlrkryaae ipdavvnvfp ppavsglgra ggfklmiedr gdvrlqnlqq qtdnivnkgn
      721 lgesdkpqsl iglftvykan spqlfvdinr racltqginl ndvfgtlqay lgsryvnnfn
      781 rfgrtwqvvv qadaqfrdei rdvsrlrvrn rnqemvpigs vaavneissp lvltrynmyp
      841 aaaingnvva gfstgqaiaq veelcrrelp sdmayewtei tylerltgnt gllvfalsvv
      901 fvflvlaaly eswslplavi lvvpmcvlss itgvavaemd inlftqigfi vliglackna
      961 ilivefakfr rdegvnrrda tlqacelrlr pilmtsfafi lgvvplvvar gagaemrral
     1021 gtavfsgmlg vtffgifltp vffyvidrmt dwklfaalsp vrirqwlfnt itaaplrrrl
     1081 arsatrslvs seppsk
//
LOCUS       WP_010586471             429 aa            linear   BCT 01-JAN-2025
DEFINITION  GspE/PulE family protein [Schlesneria paludicola].
ACCESSION   WP_010586471
VERSION     WP_010586471.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..429
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=46581
     Region          <40..414
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 msqnspaarp qsldestprs ladqfardap qsdpssakyv telvasllrs asqagasdih
       61 fsvgeselqv lwridgvlqp iaaysrsltp nivarlkvma elltyrtdip qegrlrests
      121 dvemrlstfp tlygekavvr lfassgrfql pqelglpeel leellgllhe trgailitgp
      181 agsgktttay aclrelqref gvgkslvtle dpietvlggv sqspvnrtag fdyatglrsl
      241 mrqdpdvilv geirdretae tvfqacltgh lvlstyhagn aveavsrlgd mgiepyllrt
      301 glrailcqrl lrrlcdcaaw tteetaklgf nvarvripqg cdqcagtgyr grfviaellr
      361 pdssivgrai ldhreadeiq rlamqqgyqt vglravaait agttspvevr rvlglrrdpe
      421 ttksarsdg
//
LOCUS       WP_010586517             253 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Schlesneria paludicola].
ACCESSION   WP_010586517
VERSION     WP_010586517.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..253
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=29271
     Region          33..230
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mpfdfpvaqg rfprfattrw slvlqakerp lvganealad lcraywypiy alfrrrsrns
       61 heaqdltqsf fakllekafl dsvdpargrf rsfllaavnh ffanewdrkn tlkrgggqai
      121 lsldvrafdw esgeskyqme pghhltpere ferrwalavl drvlqrlrde yidlgklslf
      181 etlqpylstd reqaryadaa eklnatdsai rvathrlrkr yrdllrneia qtvaspseve
      241 delqqlfial sss
//
LOCUS       WP_010586518             544 aa            linear   BCT 01-JAN-2025
DEFINITION  arylsulfatase [Schlesneria paludicola].
ACCESSION   WP_010586518
VERSION     WP_010586518.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..544
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60689
     Region          29..508
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(39..40,77,133,135,215,342..343,387)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(39..40,77,133,135,215,343,387)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 mnssavfrls iglfvwssll givlaadktp pnvviiladd lgfsdlgcyg geietpnldq
       61 laarglkftq fyntarcwpt ragimtgyya qqvrrdslpq lpsaggganr pawarllpem
      121 lrnigyrnyh sgkwhidglp lkngfdhayt lddhnrffsp qfhteddkpl ppvelgsgyy
      181 attaiadhcl kclsehaleh askpffhylc ftsphfplha lpediakykd rytegwdvir
      241 arrfarqrel gllscelapr aektsppwnp peselrerig pgeigravaw tdlteeqkrf
      301 qadkmaihaa mvdrmdrevg rvidqlramd vlentliffl sdngasaeql irgdghdpav
      361 pagsaksflg lgpgwstvsn apfrmhkswv heggiatpli vhwpqglttt gelrgtashl
      421 idlvptilev tganrfetwn gdpvpappgk slvpalardv gvphdflwwy hsgnrairig
      481 dwklvswgeq gpwelfdlna drsethnlaa elpgkvrqme qawkskleef qelakrdlpk
      541 dakd
//
LOCUS       WP_010586602             746 aa            linear   BCT 01-JAN-2025
DEFINITION  PAS domain-containing sensor histidine kinase [Schlesneria
            paludicola].
ACCESSION   WP_010586602
VERSION     WP_010586602.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13889307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..746
                     /product="PAS domain-containing sensor histidine kinase"
                     /calculated_mol_wt=83194
     Region          232..300
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          289..737
                     /region_name="PRK13557"
                     /note="histidine kinase; Provisional"
                     /db_xref="CDD:237425"
ORIGIN      
        1 mceqadtmea tirsraqell shelesvrya tdirflsvli iqwcveiais lwlaphaans
       61 sasavhagvw qaivwggaii svpcllaars pgrlstriai aagqalsssl liqlmdgrle
      121 mhfhlfasla llafyrdikv lvlfsvlvas dhlirgfwwp qsvygvaand pwrfaehmaw
      181 viveagflfv fcrqsiaemt qaterqarfe fvnnrfesrv vqrteslrrs eerfelallg
      241 trvgicdwdl ksdqvywser ineilglqpg elqqtilala srlhrddfrr vvngvrhaiq
      301 nrlpfqeefr lrcenkgycw veasgacivd degqpyrftg gltdishrkq veselaerda
      361 qlrqahklea igslaggiah efnnllqair gytryamkgl apeetrhqdl qqvldaaera
      421 tvltrqllgf sryqsidrre lnplsvlegv tnmlrpliga pikiitntsg nlgtifadpg
      481 lmqqmllnlc lnardampdg ghimltlkrr yfgekvyklh slpkpgpyll msvtdngtgm
      541 tqdvqqrife pffttkdvgv gtglglsvvy givqqhegai evksqlgfgt tfnillpinq
      601 ssipdlipre qpgspggtet iliaeddasv relgtriltg agyrvlsann gvealslhqr
      661 hqneislvll dailprlsgh rvleelrtrs sslpvvlctg ydpdsaslgf tkeegvrlvq
      721 kpfeadtllr tiresldlqh lklemv
//
LOCUS       WP_010586604             211 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Schlesneria paludicola].
ACCESSION   WP_010586604
VERSION     WP_010586604.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..211
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23708
     Region          18..200
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mqtssivllh dnhdqfvdyl vkqlsldgft tefvetceel ipqlhasnfa svivrlgteq
       61 leglrileel hrkqvplaai avlensnisa iveaarhgtv tfllrenagp qeiqaavrta
      121 teqtarlrea aekratlral fsrlttgetq vlerlvkgqk lmmiaealdl srrtvelrra
      181 klmhklevat fpelvalvie ydrdrqdser v
//
LOCUS       WP_010586625             311 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Schlesneria paludicola].
ACCESSION   WP_010586625
VERSION     WP_010586625.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..311
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34358
     Region          6..221
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtalfefqqv tkqfgrqtal drvsltgerg evvallgeng agkttalkil lglikpdggs
       61 srvlgldsql hgaeirrrvg ympdrpalye wmtvaeigwf aagfyplgyq qryqhliqkf
      121 elpndkaikn lskgmqgkvs lalamshepe llvldeptsg ldplvrrefl esmidvaagg
      181 rtvllsshqm vevervadki aiirggklvl fesldvlknr vqeviitcdm metippdlpp
      241 gasllgaqrl arqwqmlvrd ldelgaaqlv deashldvei rtpsleqifv vcmksdvlie
      301 yesppdrvav r
//
LOCUS       WP_010586697             218 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Schlesneria
            paludicola].
ACCESSION   WP_010586697
VERSION     WP_010586697.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24626
     Region          10..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtlheehtrt rnaertkrlv ldaaerlfae rgfvgtsmrd iadasgvsqp liqyhfehkd
       61 glyaaalrra veayaarfpe aahvtdqpvd fscemhrlft flqenrlqir migwarlegk
      121 helvtgcenl rramvqrief aqqqghvrtd idarslgvml egllfswfen ralnemlfpe
      181 gmdddaflrs aiamlergaa pavheagmev aaisegqr
//
LOCUS       WP_010586707             295 aa            linear   BCT 01-JAN-2025
DEFINITION  bestrophin family protein [Schlesneria paludicola].
ACCESSION   WP_010586707
VERSION     WP_010586707.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..295
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33337
     Region          1..279
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mssydphrwt shlfdvegsm vreilcrvla svswsigvvl ayqfgpeslh risipptahs
       61 ligtalglll vyrtnssydr fwegrkmwgg ianecrnlar qtgvwlaadr plmqevirwt
      121 mafpystmqr irgaagigtv ldgidereiq rveasrhvpl avarnitsrl llarqrgvid
      181 glqlasldnn vqllmdycga cerirttplp fayavhlrrv livycftlpf alvkdygwtt
      241 vlatlfisyi lygieeigve iedpfgfhin dlpirsfces nefvlseird qidpi
//
LOCUS       WP_010586755             131 aa            linear   BCT 01-JAN-2025
DEFINITION  BON domain-containing protein [Schlesneria paludicola].
ACCESSION   WP_010586755
VERSION     WP_010586755.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..131
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=13972
     Region          63..>126
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mrrltisgll llcvsacset tnqtankppv skttptaees lvspsehrss sstqpldqek
       61 snsdeqvtad irkgmmdskm avsleqikvn tsdgkvtltg lvktleekqk ageiaesiag
      121 adhvdnwvev e
//
LOCUS       WP_010586724             368 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010586724
VERSION     WP_010586724.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..368
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40279
     Region          3..366
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 manekvriai igaglvsdfh hvpgirvddr celaavcdpn eqllnqrkne wgpakyttdy
       61 eqiandpdld aviiatpnft hkdialacia ggkhvmcekp lgvsyaeade myqaakakgv
      121 rhmtaftyrf apsmrylrhl lksgalgepr hfrsqrfldl petswgwrqy kklagagdly
      181 dmtthridfa qdlmgpiqsv cgavktfvpr dktadgtpca psevddwsal igtfrsgavg
      241 vwegstlmkg hhnggvgfew aevngsegsa vyqlvdpnyi lvgkhggtme kslvpaefmk
      301 pvksprnpad gkpstvfryd lvfelvsaiv egrdavpgfd dgasaqavad avlqsyaerr
      361 widvpsyr
//
LOCUS       WP_010586756             406 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Schlesneria paludicola].
ACCESSION   WP_010586756
VERSION     WP_010586756.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118302
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..406
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44610
     Region          18..397
                     /region_name="ABC2_membrane_3"
                     /note="ABC-2 family transporter protein; pfam12698"
                     /db_xref="CDD:463674"
     Region          211..401
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mgiwaltikd iriilqdrga lytllalpvv fiailgvstg qllstrdelk likiglvded
       61 ktelseqvyh dlsmigglkv dkistrddaa irlqdgrsgi vivlgkdfdd rveeldlsdv
      121 fdaqngklsq gvealdmqvl sgasyvgvsd lveyvvlsav lkvvspevvr rnpllrrlid
      181 rmkerhaeda lpkppviavv ksgssiiyqt lvpafivmfa fflvnimass fiserqlgtl
      241 krmqttritp sqllcgktlp fllisiaqss llflsgkimf gmswgtypfl lipviittav
      301 satglgllla tfvrtesqva systflvvvl agisgcympr dwlpelmktv slgtphawal
      361 iayqellthp hpslnvvgec clmllgfgvi afilgwirfr kleyhi
//
LOCUS       WP_010586766             285 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Schlesneria paludicola].
ACCESSION   WP_010586766
VERSION     WP_010586766.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..285
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31684
     Region          21..266
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mnepvptser rrnaptwyvt ltrivfylip vlllvmillp falmvlislg sgwafprllp
       61 drmdlaawrh flsdrdqmli aiatsavmsl tvgvfsvsgg lligravrrt gsrfahfliy
      121 lpfvispvvv giclydllir mrvignvvgv ilmqtvfals fssvffyelw spraerleql
      181 vsnfggsrwd vwrhavfpqi sglilvcflq talyswldyg ivsivgggyv psvttrlfgy
      241 ireasvnqaa qaslillapa llgflittsv yflrltlpgd trqss
//
LOCUS       WP_010586810             322 aa            linear   BCT 01-JAN-2025
DEFINITION  ion transporter [Schlesneria paludicola].
ACCESSION   WP_010586810
VERSION     WP_010586810.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..322
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35884
     Region          58..243
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mlscsipesd rftgafrets qrldlrfsll lcrfevffma svvqasevse defrpqqllm
       61 lllcvyslgs latetfapls aeyvaildvi dnlicgiflf dfvvglliaq dklrflawgw
      121 idlvssipvi difragrivr virilrvlrg irlawilary lqrdrangaf laviflsill
      181 lllssvailq veqveganih sasdalwwsv vtmttvgygd kypvttvgri iasvvmisgv
      241 glfgalsgsv tswilnpvev rqevdldaih lelaairtrl dhvpavglke ldpqltrimd
      301 swgnltenrr rqilrlmdst ae
//
LOCUS       WP_010586832             103 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Schlesneria paludicola].
ACCESSION   WP_010586832
VERSION     WP_010586832.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..103
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11468
     Region          2..95
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mihvlaliet tpghredflk efaqvtvpvr kengcieyga avdavtdlpv qqslganfvm
       61 ivekweslah lkahlvaphm adyririkpf vqsvrlqvle pra
//
LOCUS       WP_010586896             345 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010586896
VERSION     WP_010586896.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..345
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37304
     Region          11..343
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mpeftvavlt nqggahldgy ftglaqteqa trvvvadpsg aseslakkll gsklhrferd
       61 fqkclaehkp glavvtleav qgppaiqaal danchvlaek pacvtaadfe plaqlaemkh
      121 rhlmlamanr trnsvhaakr lirtgqigqi ygselhliad qtrlvspayh ktwfadrara
      181 ggghliwlgi hwidlimflt dsqiietagf tgivggqplk aedsaamalr fdngtfgtmt
      241 sgyyldrgkq msiriwgskg wlelsfdege glkwystaep spsikkydga addgtytpfi
      301 qacvraside aapppitptq slnvlktifa cyraaesgrs qsvfa
//
LOCUS       WP_010586939             461 aa            linear   BCT 01-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Schlesneria paludicola].
ACCESSION   WP_010586939
VERSION     WP_010586939.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..461
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=50130
     Region          5..240
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mriptgtllv ardvgaawgr qhveelaqgl esrlhqpvaa clpdideipl leriqslvep
       61 ttrrlvivpc gllpvpergf iarsitaaqr kwpsltvhva vpltwiewsg wlrlisldai
      121 helavppadt gvlvvgqids dpmvnanlar lahliyessp latvtyaflg ggqpgvsdai
      181 rtlarqglrn livipwlvsd nvslaklqae laqvtktcnl paqlvqptla hpalvnllva
      241 ncyaaltygg edqlidttak pnsddqpseg sstsdqlaed afelqelear inallpseyq
      301 gryedvssqs mgtaglkydt dgnvawdeiw tsfcdlalag gpphrgrlle avsaedvkke
      361 peqyqavvte igrgiqmvtg lpivasaslg wigvrcenee mavwlmraii venimvrreg
      421 nvlylpagpq ftvkreiknv itavaktvhy wtahlnarrq s
//
LOCUS       WP_010586970             118 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Schlesneria paludicola].
ACCESSION   WP_010586970
VERSION     WP_010586970.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..118
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13248
     Region          8..107
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(24,28..30,36,60,62..64,66..68,71..72,94,98..99,101)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            63
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mstsrrridi eevngvtiat fvdkkildea niqtigsqlf alidedgrkk iildfthvey
       61 lssaalgkli imdkkaktas tklrlcsirp eiyevfeitr lnkifdikgt qeealegf
//
LOCUS       WP_010586975             261 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Schlesneria paludicola].
ACCESSION   WP_010586975
VERSION     WP_010586975.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..261
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=29579
     Region          <43..155
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          60..90
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          95..119
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlrtntlttm lilmgtvwag davdqvpapp lseskraelt ksleksleds mrlvqetprs
       61 vaaysrrgda yfflgrfkea vadydtmvel ddslaashwr rgialfyaer yqdaaaqfes
      121 yhsfdqvdre ngiwrylsqh kahgrakare gllkyqkddr epfpavyklf agtispeqil
      181 adigaaelsk mereqrlfya qlyiglnsav egdddqarah laeatrntwg pvagygptym
      241 whvgrlheel lrtkkthesp k
//
LOCUS       WP_010586978             486 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010586978
VERSION     WP_010586978.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..486
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53293
     Region          42..405
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mthvsrrefl ersmfataal tlaksprlfa addngaanag qklrvavvgv kgrggshieg
       61 fgsredceia alvdvdetii nqradaieqk ygkrpavysd mrkcfedkti diasiatpnh
      121 whslaaiwai qagkdvyvek pvshnvsegr rvveaarkyn kivqtgtqsr snpgmreaia
      181 flhgggigdv klarglcykp rgsigpkgny dvpasvdydl wsgpaeikpl srkslhydwh
      241 wmwdygngdl gnqgihqmdi arwglnemnl gesivsyggr fgyedageta ntqvsihnfa
      301 ngkrlvfevr glktekymda gvgvifkgse gylvvpsyhg gvvldkdgkp tgktfeggsd
      361 kfhfanfina vrsrkytdln adildghlss alchvgnisy rlgtpsaise iitkfqgdae
      421 aldtldrfql hlrdnkvdpe ttkitlgpkl tlttseefag ahspeanrml treyrapfvv
      481 pqtkdl
//
LOCUS       WP_010587023             373 aa            linear   BCT 01-JAN-2025
DEFINITION  type III polyketide synthase [Schlesneria paludicola].
ACCESSION   WP_010587023
VERSION     WP_010587023.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..373
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39931
     Region          3..372
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 mhvaiagigt avpdhqceqe eagevaaqyc satpeqahml svlyrmsgvn trgsvvlesa
       61 dgiltdrqef fppctpespn gpttearlni yaekagplal taskraleqs etspqaithl
      121 itvtcsgfva pgfdftlikq lplrsdvart qigfmgchaa lnalrvaraf vaadptavvl
      181 vccvelctlh yqygwnpeqi vanslfadga aacviraeip avtgsvlesq qrpisrilas
      241 gstllpdsed amtwrvgdhg frmtlstrvp glleahlrpw ltswlkqydl rpeeistwaa
      301 hpggpkilna fadtmsipre qlsvsreimq thgnmssptv lfvldrlrsk qasgpcvaig
      361 fgpglvaeat lla
//
LOCUS       WP_010587156             165 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Schlesneria paludicola].
ACCESSION   WP_010587156
VERSION     WP_010587156.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..165
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18703
     Region          12..153
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 msdlatmnvt vapvdkfref lltkkmrltp ereavvtaiy ashehfdadq widslaghkg
       61 tmlasrstvy rtlnllqeag lirkvarand revyehdygy pqhdhlickk cgemiefpne
      121 misgfletia aehgfrmsgh rlevegicad csrppvrshr kldmi
//
LOCUS       WP_010587147             590 aa            linear   BCT 01-JAN-2025
DEFINITION  leucine-rich repeat domain-containing protein [Schlesneria
            paludicola].
ACCESSION   WP_010587147
VERSION     WP_010587147.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..590
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=65360
     Region          77..100
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          101..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          125..148
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..542
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          149..172
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          173..196
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          197..226
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          227..250
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          251..274
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          275..298
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          299..322
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          393..416
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          417..440
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          441..462
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          465..488
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          489..512
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          513..536
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          537..560
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          561..581
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 mrapllslit atvlagsrli aqdgpdvska vqklellgal ierdaeapdh pvigiafeea
       61 hkfsekhlhl lkpfsdlsdl dlhaipildr dlkeladlts lvnlnlsdtr itdrglfhlk
      121 rltnletvwl qntsitdagi kelasferla elnlsdtrit drglrelsdf qnlttlwlqn
      181 vemtddglqa lkrlktittl dlsnlnglnt iritdegleq lsdlpelrhl ylanipiads
      241 gltslrrlkh ltvldlrgtq itdeglnelr glheletfkl tktqisdagl talkglknlt
      301 tlligsnqit gtglqeltnl dqlktldlsd tqvtdvelnr lssirtltdl rlsdtpitdv
      361 glrslrelkr lrrltlggtq itdiselnhl rdlthldlrv tpitdtglhg lgdlkhltsl
      421 nldatqvtda slselkclvh lkelslsrta isglgfksle rleqltvlrc drcliadegl
      481 reictlkslk tlvisgtrvt ddglaelhql eglqelrien naltdagmse lmvlgklrtl
      541 gishnkitdt slsdikrlkn ltmlrirnte itdsglngfk darpnvsifr
//
LOCUS       WP_010587191             318 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Schlesneria
            paludicola].
ACCESSION   WP_010587191
VERSION     WP_010587191.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Grant Pearce,F., Hudson,A.O., Loomes,K. and Dobson,R.C.J.
  TITLE     Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and
            Evolution
  JOURNAL   Subcell Biochem 83, 271-289 (2017)
   PUBMED   28271480
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Laber,B., Gomis-Ruth,F.X., Romao,M.J. and Huber,R.
  TITLE     Escherichia coli dihydrodipicolinate synthase. Identification of
            the active site and crystallization
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 691-695 (1992)
   PUBMED   1463470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..318
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0009436 - glyoxylate catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=35622
     Region          19..308
                     /region_name="DHDPS-like"
                     /note="Dihydrodipicolinate synthase family; cd00408"
                     /db_xref="CDD:188630"
     Site            order(21,52,55..57,181)
                     /site_type="inhibition"
                     /note="inhibitor site"
                     /db_xref="CDD:188630"
     Site            order(52,55..57,181,224)
                     /site_type="active"
                     /db_xref="CDD:188630"
     Site            order(56,61..62,96..97,122..123,130,136,291..292)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188630"
     Site            181
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188630"
ORIGIN      
        1 msafdplsll kprrkvtgis aillpftqag dvdwpafhah vqrtlesglt pavnmdtgyv
       61 nlldratqda vlqqtrevag grpfvagafv sdgegdafrp deyarrievi qshggtpiif
      121 qsygltrqsg pkivasyekl artadrflaf eltqdlasfg aiydletfaa vmsipqcvgv
      181 khssfhrepe wqrlvlrnan rpefviftgn dfaidmimyg sdyllglstf apdlfaqrdh
      241 fwetgdprfy elndqlqylg yfafrrpspa ykhsaaqfln lrgwinssht hpqsrtrpds
      301 drdvlrelgq rlgvvspt
//
LOCUS       WP_010587259             426 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Schlesneria paludicola].
ACCESSION   WP_010587259
VERSION     WP_010587259.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..426
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=46506
     Region          4..179
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtktsddvli lavrdgdrta faelveryrd lvvgvaysqv gdfarsedia qqafitawkr
       61 nfdladpsri aawlcgiakn lvrnerrqia resseplddq tasrpaespe qqaiareeae
      121 llwsvldkip etyrepmily yrnesttdev aaaldispdv vrqrlsrgrk lleekvaefv
      181 ettlskrkvs hgfvgsilla lpasgaakta gvaattglts waglgallgp lvgiaggayg
      241 skrsldnats sierrflwrf iawislliaa llaaqsamrt wfpnaprgts eliwglygll
      301 lplsitlgnr rlkaikrehg tkeeqaviqr tdespfptrg aawnigiait gstawmfata
      361 avcrdwigli latallaill gtfvprtlra sttrqletsn fhavlailag tlvvaamrws
      421 awlpaf
//
LOCUS       WP_010587304             421 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010587304
VERSION     WP_010587304.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..421
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46950
     Region          8..286
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msvtaadrsl ragmvgmgmi fdetyrpffe rvhsellfdr rfgvldvpli avasktggra
       61 sayrkacgsk vhpfesfsgd davdrliaag ldfacvatpd drhfgvarkl lnaginvlie
      121 kpsvlrlqel eeltalakqq nlvakvvyhk lldpdhkklr tlvvdgvlkh vnhgycslle
      181 pkqisgsqfs ewitgrnpgt yvachyikli dftfggrlkt vtatgqrgiv gpkdgptwds
      241 tqlrliyeys dhreaafdih tswvtpdnfp gyveqevqfr fdngvwnghs rkrgvectve
      301 getpisrkit mnnhyngtfv epwgersqrg ygievlerfa relgyvkfgg paserskrlq
      361 eiqalayndl eadwqsvaav qaleailerh aagepdcvvr vtddrklaly rpgqaqpvll
      421 n
//
LOCUS       WP_010587336             567 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Schlesneria paludicola].
ACCESSION   WP_010587336
VERSION     WP_010587336.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..567
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=62214
     Region          80..321
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(80,104..105,134,139,144..147,159)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(87..88,90..93,95,108,110,142,158..161,165,167,203,
                     205,207..208,210,220..221,224,240..243)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(87..88,90..93,95,108,110,142,158..161,165,205,
                     207..208,210,220..221)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(91,165,167,203,205,207,224,240..243)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(220..228,236..243)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mktdcptdde llplaagepa ddglrahvdq cpiclarvdq lrremtelqs lavsmgstsk
       61 lrpaagpsve plpnstkigr yvvignlgsg gqadvyrvid pnlerqlvlk lsrqhadgpa
      121 engdavsaeg rllaeldhpg lirvfdvgif qkrpylvleh vpgrnleqlf sterpafrda
      181 aritaemarv layahrrgvv hgdvtpknil idahgrarli dfglsrmeda wgenarltgg
      241 tpeylppema langrlgrav pasdvfglga tlfwmltgra pfagttvnes laharrgevd
      301 ftplrtanvp rrlrdicrkc laadpaarpa pdavaaeier frargrvwvv vtaatlllas
      361 aiatawwltn drksdslesv nfvhsrpvin vlhrdgvrml snalplrtgd rifvychisq
      421 geeavmlwfn pagqlkiirp vrdvaenvdr lvvpaphrsl tleppegtem lffccgddfs
      481 eqelracfpe kptstnlpph nwltvqrsev kiegplatdi pddilavees lkeinrqlkq
      541 hfksvtgivf phhtsathda ptispnn
//
LOCUS       WP_010587413             596 aa            linear   BCT 01-JAN-2025
DEFINITION  fatty acyl-AMP ligase [Schlesneria paludicola].
ACCESSION   WP_010587413
VERSION     WP_010587413.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10148874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..596
                     /product="fatty acyl-AMP ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65004
     Region          19..563
                     /region_name="FAAL"
                     /note="Fatty acyl-AMP ligase (FAAL); cd05931"
                     /db_xref="CDD:341254"
     Site            order(167,170..175,177..178)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341254"
     Site            order(194,214..216,290,293..296,321..325,330,367,433,444,
                     447)
                     /site_type="active"
                     /db_xref="CDD:341254"
ORIGIN      
        1 mdarinnnvr etilsvlgdh vrrsgeriay tflksdsere sltyrqlddr arsiaaallr
       61 harpgdrall aypsglefiq vflgclyagi vavpsyppkr krnsvrvgai shdcgatlll
      121 gtretrgsll teilarspga vvlatdeitt tggkclrpve atdvaflqyt sgstaspkgv
      181 vvthgnivan lrliqacfqf sanstlvswl pmfhdmglig cvmaplflgf pavlmapstf
      241 lfspiqwlrt vsefratctg apnfaydlcv kaitpdqrrg ldlsslriaf ngaepirast
      301 ldqfselfsd cgfrrdaffp cyglaeatlm vsggpplapr pilrlgadal eqhrveesid
      361 grrivgcgrl tdhlevcivh pgtgvqcapd eigeiwvrga svtqgyfrrp eetistfkat
      421 ieqesggwlr tgdygfirdq vlfvtgrlkd livirgrniy pqdveravep hiknptancv
      481 aafsielege ervvvvcegt qeiqrlanda drsadlrsym damlsnlrad vlalcdvqvh
      541 yvaisaplaf prtssgkvqr raclnglihr tlpclelpgc issldglslk tessev
//
LOCUS       WP_010587416             437 aa            linear   BCT 01-JAN-2025
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Schlesneria paludicola].
ACCESSION   WP_010587416
VERSION     WP_010587416.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..437
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47715
     Region          35..428
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mndqthrvhd ekspslkgsl isylalngkt nekrlsdwte wlasrrndkl wpysrviegh
       61 pgvsatvcte krehprrlln fgsqdylsls khpqvieaav dtcrelgvhs agspilagrt
      121 apmyelenri sqlckkecca ifstgwaagf gvmaglvrsd dsvvidrlah nclcegtkha
      181 tdsmflfahn staelthalq karrandsgg vfvvveslys mdsdspdlqa vvsiarqfda
      241 itildvahdf gcmgasglgl ldvtpeefwp dvimgsfskt fasnggfvaa seqvidylrc
      301 ysspfafsna lspvqasivl tcldlvfset gsemrqrlaa nvdalrrgmt hhgfhvagkp
      361 spivpvfvgs eanarvvsre lgelglmanl vefpgvprgs arfrfqvmrd htmfeidaac
      421 evmrkaadta gllmdhw
//
LOCUS       WP_010587474             599 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [Schlesneria paludicola].
ACCESSION   WP_010587474
VERSION     WP_010587474.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..599
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=66613
     Region          439..590
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mschkrlyli glfliaaiss vpqtafiysa aieyfrsrsl pvhsipgfsr ipishkseli
       61 qaafsqnrfv lldnklidhk trtltlrtfd pesgttarql dvpatceyvv asfedrlwil
      121 prdpnaqsye lidgiaqksd ipmfknhvdq gtrflidgep ayvspdikrl avftprherh
      181 dwiptkpidl pdlscewsyg dtivhfrgdl pdfklircgd qshvflsmng yvlyrqgief
      241 npnasspdqr pgplrvtwpr svgsnevgvs agddaqlvkw slvcdrpaiv seitmhssrq
      301 lakgallieg qpavliieea qpkestgtih rfdgtdwspw etlsfpfavr dfctatrsdg
      361 qssyivvatp lgeafvyfvd asgihplqsk lphpslktqt elsilfsifv gssilcaigv
      421 wllmwryaap eyafgqetvq laslarrgla rmidigliat salilggilt wgldwpafle
      481 ainlrvahps ipivrravel taiwiafsvf vflliqgitg rtpgkrwcgi ktvrstlrpc
      541 giarsltrei ifyvdscsll cwtpgilsia ltplrqrlgd lvadtivida strkqrppe
//
LOCUS       WP_010587550             315 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010587550
VERSION     WP_010587550.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..315
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34627
     Region          5..314
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgdesktwrv givglnpigl flleqfrlip nvrvvgiydr dpsrchlane ldcrvwdhpa
       61 qafsatdvda vvladqvsse siamglqngk hlvvdrpwgv ssrewrelse tagrssaqlt
      121 fvclrrwssd fptvlvamrs grvgtlqsar yvshemclas elaaprflte iafslldqll
      181 lltasnpkdv fakrlgsaag gedtgliati efengcvaqi dlqsqsrlsq rtgwmlegaq
      241 gsyrddrlyt vttdgevide plsppnmpdn sfvrelvasw ngeasslpsl teavrtvqla
      301 emiersaerr dvvrs
//
LOCUS       WP_010587585             390 aa            linear   BCT 01-JAN-2025
DEFINITION  MlaD family protein [Schlesneria paludicola].
ACCESSION   WP_010587585
VERSION     WP_010587585.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..390
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42500
     Region          3..266
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 materqlqfr vgalvivats icvglairfg dtqslwkrhy pltihlenga glypsapvtl
       61 sgltigsvrr velnqtrggv nvqvevqesi rlpidsraii srslmgestv dfirgtdpdl
      121 lkpgghlvgi aaadplvmvq rleartletl safsetsqew gsvakninml ldterghldq
      181 vveraaeslh eftramqsan amisaanqiv adpasqqaik etlnslpklv nttrtaidet
      241 rqtvvasrqv ldsmnrnlvn lsqvtepvgk rgeemvakld ssltnidsll telnrfarvv
      301 nqkdgslqkl vqdpslydnl drssqsiavl mknlepilrd mrefsdkvar npellgvgga
      361 vrpstglkde eildakrtav pkvargkspr
//
LOCUS       WP_010587662             515 aa            linear   BCT 01-JAN-2025
DEFINITION  NADH-quinone oxidoreductase subunit N [Schlesneria paludicola].
ACCESSION   WP_010587662
VERSION     WP_010587662.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..515
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=54950
     Region          9..512
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mnvaiqqlns altliapdav llagvcliff aapflvnekg eapeglrhrw gflsllvlim
       61 aglvwwqstp vartfgpfal deltwyirgl tltsgfvlvl lqwnqaddsr saechaclla
      121 ilagvnliaa andliglfva lelvsiptyl flllprrdap aqeatlkyfl lsifssaivl
      181 fgmsylygat gttnlgaiha afagaqgqpa nplvavatvm liaglgfrlt avpfhfyapd
      241 vfqgaptsaa amlsfvpkia gfvallrlmv patgaeqamn swtmtpaatp llwwlavvtm
      301 fvgnlmalmq tdirrllays svshagymlv glivglehei tkdvlnrtgg havsgigaml
      361 fylavygamt lgafavliaa rrgdkpietl ddlsglaksr palalvfavf lfslsglppt
      421 agflgklnlf faawsqgyds srwlavvlai naalgawyyl kiigvmflrd piyrdespaa
      481 aeapsliagg iclaatlglf fmpgwlwvpi qsimp
//
LOCUS       WP_010587685             432 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010587685
VERSION     WP_010587685.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..432
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47178
     Region          42..407
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtqglsrref leaavkagta ataagvlawp tvaqakears aneklnlavi gvadrgaanl
       61 ngvshenivv lcdiddkrle aagekipqak rvfdfreale vpgldgvvcs tpdhvhafva
      121 aaalkkglpv ycekplthsv wearqirkln aaarvptqmg nqihagsnyr rvvetiragt
      181 igpvervhvw vgapvrsfpa vktseppsyv hydqwigpap yrpfseahfh fnwrfwwdfg
      241 ggtladlgch ymdlafwale lgaptsvsat gekghngdne cpnlmkvdyk fpargdqppv
      301 hltwyhggwm pegaesykkn savlfegpng rlisdygtnn lfmqegktaa pvkpwiaesv
      361 aghhaewlta irtkgstssh feyggtltea vllgnvsyra gkpilwdaqa lktdspeadq
      421 flkreyragw sl
//
LOCUS       WP_010587774              81 aa            linear   BCT 01-JAN-2025
DEFINITION  carbon storage regulator [Schlesneria paludicola].
ACCESSION   WP_010587774
VERSION     WP_010587774.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..81
                     /product="carbon storage regulator"
                     /calculated_mol_wt=9013
     Region          8..>46
                     /region_name="CsrA"
                     /note="sRNA-binding carbon storage regulator CsrA [Signal
                     transduction mechanisms]; COG1551"
                     /db_xref="CDD:441160"
ORIGIN      
        1 mqcllslnds lmvgeveisv levrydsvkl giidpnaspt yreevlflns ededlgyndd
       61 veaksipfef epfhsfaisv l
//
LOCUS       WP_010587826             536 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Schlesneria paludicola].
ACCESSION   WP_010587826
VERSION     WP_010587826.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..536
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57704
     Region          216..532
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mvphsrrial arigfvllll lpasgcrssk lsvatvrnik pdgvrsskpa atrsrddaat
       61 dpvnhtaged evsiqltaae etlpspvqgd pasvrsgvat vtdanpahed tqsidlttal
      121 lltsggnpqv gfaharieea raqvqkaevl wlpsirmgan ynqhegniqd vagniinttr
      181 gsfftgfgan avgagsptip gllaqfhlad avfqpriaqq tasarnagaq aatndallqt
      241 alayltllrs aqelavaidi eqkakelerv tgefahtgqg lasdhdrart elalrtndvr
      301 raeeavgvas arlaeqirwd ssrrlvples qliplelvhi gerpqalvam altqrpevae
      361 srhlvceave rlqreryapl ipsvllgvsy gglggglggn ltnfnsrvda daiayweirq
      421 lglgdqaarr eadsriqqsk freialldrv arevveahvq vtsraqqitt gqvaveaaed
      481 sfsrnweriq ngqglpvevl qsiqalavar reyvrvvady ntaqftlhrs lgwpiq
//
LOCUS       WP_010587858             506 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Schlesneria paludicola].
ACCESSION   WP_010587858
VERSION     WP_010587858.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 506)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..506
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55509
     Region          245..506
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 myklllcqry lrtryialas iisvtlgvat mivvnsvmag fgtemrsriq gilsdiiiit
       61 rsmngeidpe arkaevrelv gdyitgvtat veihailsyk yggdwvphpi nlvgidpesk
      121 sevgpivgyl qsynsqevdg vklpperskd eplgweltpa amaerverar wykdqelkre
      181 mmasgaapaa dpaaaggdsl ldlempdeap algklrkgrl fvgvglatyt qvdpdtqklk
      241 tydmikpgdd vkistiqaga pepvhfeati vdtfktgmse ydstlvycnl dhlqevrkmi
      301 htkedgstvg gftslqiklk dykdapkvmd llrthfsadr yivktweqqq gpllaavdve
      361 ssilnillfl iitvagfgil aiffmivvek trdigilkal gasssgvmsi fltyglllgm
      421 vgagagvvfg llfvhyinei eafvtlvtgr evfpekiyyf kdipthvepf tvvwvtvgai
      481 liavlasvlp arraarlrpv qalrye
//
LOCUS       WP_010587859             236 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Schlesneria paludicola].
ACCESSION   WP_010587859
VERSION     WP_010587859.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26347
     Region          11..231
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mpqthvaala vqksyrkgeh avpvlhgvdi svrkgeflsi igqsgsgkst lmhligllds
       61 pdlgevqleg eriddlpart rdelrnrvfg fvfqfyhllp emslienvlt plmirhsiws
      121 ywarrreyhd rakemidrvg lghrlthkps elsggemqra aiaralvarp eilladeptg
      181 nldaktgrei idliaqlnek drltiimvth dksiaaeahr tvklcegrie sltdaa
//
LOCUS       WP_010587986             407 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein, partial [Schlesneria
            paludicola].
ACCESSION   WP_010587986
VERSION     WP_010587986.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         <1..407
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <25..>134
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(29,33..34,37..39,41..42,46,49,58,60,62,66..67,
                     70..72,74..75,79,82,91,93,95,99..100,103..105,107..108,
                     112,115)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          29..58
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          60..91
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          93..126
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 cptfsqsgfg ylaqliqtka mkmcntfehs awlcaaiagd idkltlllss ganideqgqr
       61 gssaitlgaa ransdlvdwl iengasidla ddcgntalml atkaaamvcv qllldagadc
      121 lrvnrrgnta rsmapnesfa rlldeasstg tsltthvkrr ltglsdeamp eltpsqyysd
      181 rsrrfgslnp elmnvpfwhq mirsgitayk arqivsdddn ngpvwsfnrs gmsftrlpgr
      241 rfvqiggehe dcydrdfciy ndvivqshag efrvygypaa cfppisfhsa trvsnviyiv
      301 gglsypgsak vhmtnvyrln ckswaihevr trgeppgvif dhkarfdgst rlivwdgkis
      361 etidgkrevf dndaefclnl semiwtrisa yrrasddsdd hgdsayl
//
LOCUS       WP_010587891             139 aa            linear   BCT 01-JAN-2025
DEFINITION  SOS response-associated peptidase, partial [Schlesneria
            paludicola].
ACCESSION   WP_010587891
VERSION     WP_010587891.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         <1..139
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
     Region          <1..135
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 safksrrclv masgfyewrk ldaknkqpyy isltngapmp maglwevwkl pegetvesct
       61 iithtandmm eplhdrmpvi lthalvdpwl dpaindpaai qpmlehfpad emqawpvskd
      121 vgnvrnqger lieaitvga
//
LOCUS       WP_010588053             351 aa            linear   BCT 01-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Schlesneria paludicola].
ACCESSION   WP_010588053
VERSION     WP_010588053.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..351
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=40167
     Region          34..111
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(34,46..47,49..50,52..53,56..57,59,66..67,68..72,74)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          100..335
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 msdeepelep teevaqapge plksiveara hgwrvdhylv rlypnfsraa fqrvleddgv
       61 linglpvkms rrlrvndcie frlpeepdrt lppediplni lydddalivi nksanmivhp
      121 grgnylgtla galqfhfdrl sdvagkfrag ivhrldrdts gvlvvakdnt vhhhlsrqfe
      181 ertvekeyra itwgelsfdr dyiethvrvs nrnrermmvc pegnnsrhaa tfyevlerfn
      241 gfsfvrlcpq tgrthqlrvh mhhlghpiva drlyegnssl slselvegvs edddevlmsr
      301 qalhalklgf dhpvtgqrme feaplpddfq rtldairkyr tkparvapvr r
//
LOCUS       WP_010588055             183 aa            linear   BCT 01-JAN-2025
DEFINITION  DinB family protein [Schlesneria paludicola].
ACCESSION   WP_010588055
VERSION     WP_010588055.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..183
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20452
     Region          12..166
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 metipliarl nqhrawtnrn lraavallnd eqlhtslpig qgsvwkslth myaaeyvwlg
       61 alhgeeeplv qgdvrgklpg nqlgegkiad fvelrqkwee lelrwseyvn glqpseledt
      121 vfkvvstaga gvrfgtrrad illhvclhah yttaqtvnml rqlgveklpe smlislarhe
      181 lat
//
LOCUS       WP_010588084             129 aa            linear   BCT 01-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Schlesneria
            paludicola].
ACCESSION   WP_010588084
VERSION     WP_010588084.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..129
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14603
     Region          6..128
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mlkprdlppl seaqleimni vwlagecsva dvleqlstrr tvtrntvqtm lsrldekgwl
       61 ihrddggtfi yrtsvprerv qqqrleqvve tvfdgstagi lmallkdstl tsdeanrirk
      121 midhaekrp
//
LOCUS       WP_010588175             365 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Schlesneria paludicola].
ACCESSION   WP_010588175
VERSION     WP_010588175.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..365
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40360
     Region          14..357
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mfrriiasel tqltprricl ikpsalgdvv qtipllpvlk qcypeaeisw vvnrelrdli
       61 dghpalhesi pferrggwsa witllktlre rrfdlvfdlq gllrsavmta vtgarvrvgm
      121 etaregsryt lncmipnsgr dvpaharywr vadvlgfget prqtkivtsd adqawaitql
      181 qelprpifav hpgarwvtkr wpvekfadlm rradrqwsgs vlilgskaer pdadqltnll
      241 aekmgtigts riknlagqst lkqltsller vdfaisndsg pmhlaagldi ptlglftcts
      301 airsgppgsm helvstkvac aagyhktcph hgaehlsclr elgvsrawsa lqrlvdknat
      361 aqrva
//
LOCUS       WP_010588162             425 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Schlesneria
            paludicola].
ACCESSION   WP_010588162
VERSION     WP_010588162.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..425
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=47523
     Region          53..425
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mtrkpysppp rrfetnrrpa piqrdlleqr plcpedkrpl pkvevnmgga lwhpfvfrkr
       61 lgqisrdaqp gdlvelvsss ggtlghglfn peaeiavrvl rtgqhrpdea wwserlaeav
      121 alrretlrld evsqayrvih aeadglpglv idrfgdvlva ecyslgmyqr aeaiiaqlep
      181 llgtkhgvlr vapmsqeheg ftaapygsae vpikltiqeh gtkfrvhfag gnktgfycdq
      241 rdnrkqlaef crgktvldlc cytggfslqa krlgqasevt gveldedtva larenaqqnq
      301 vkinfvqaev fgymrdmlrn krrfdvvvld ppklirgrme teegrhkyfd lnrlamqlvn
      361 pggilltcsc sglldmaeft kivcaapevg rrcqifakgg aapdhpiatt cpeseylkti
      421 wcrle
//
LOCUS       WP_010588200             271 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Schlesneria paludicola].
ACCESSION   WP_010588200
VERSION     WP_010588200.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 271)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..271
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=29543
     Region          <36..256
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mkatisefde lptaarvael qqqiqslqqq llqaqkmssi gvlassithe fnnilmtvin
       61 yakmgvrhkd patrdkafdk ilaaghrask ittgmlsyar qqsdrreamd lvplvedvlv
      121 lvekdlqryr irlttqfdvh pyaavnsgqv qqvllnlvin arqamenggn ltvtvrsnqe
      181 qgqaeisird tgsgiapdkl rkifdpfftt ktvdeqgqgg tglglslard vmeshggrir
      241 vesavgsgtt ftlkfpqvas pvkpqakqav g
//
LOCUS       WP_010588362             620 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [Schlesneria paludicola].
ACCESSION   WP_010588362
VERSION     WP_010588362.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..620
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=69026
     Region          <530..603
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mndfgwsfrr iaasaafvlv slvlplgiig ltvaslvsgd atrtpegewk cydggvldqg
       61 slvfpvqrnl rgisnstmgf earirrldlk sgvesdtgvv vanqginlql vneellvwtr
      121 qgihrwddss lvkiadshsc lrvrnhpfly dehltqvvea edggfrlmhl iddawvkglk
      181 irlpetdcdw hedpktgkar lqsrapslpl ptggavpwih lmvaqhagkt hlllntipng
      241 lyayrhgfef edpecasaqa panasvdvsg wepvpllvsg drcagivcdr dgllvastks
      301 lepirmirrt dvghwqevva vegvklrctp qlfvdaatet ayvfdayrpw syaalypieq
      361 nsilpadpvw slevrkylar wlallaavlv gwlvhlitlt cgtellalrr pengyefgnq
      421 sailattwrr gfafsvdala valilsmvla islrdpnlrw hdgderdlcq tlydvedill
      481 krpresdqmn lanyprfeyf atifrgrpdl yssalatsli vcglkiyveg rfgvtpgkwf
      541 mgirsvgstl rpcgfaralv rrvlyvvdil cfitplpaai smmfsshrqr lgdrvsdtvv
      601 irrrsgspsr trleikhpqn
//
LOCUS       WP_010587398             328 aa            linear   BCT 01-JAN-2025
DEFINITION  energy-coupling factor ABC transporter permease [Schlesneria
            paludicola].
ACCESSION   WP_010587398
VERSION     WP_010587398.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Rempel,S., Stanek,W.K. and Slotboom,D.J.
  TITLE     ECF-Type ATP-Binding Cassette Transporters
  JOURNAL   Annu Rev Biochem 88, 551-576 (2019)
   PUBMED   30485755
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Rodionov,D.A., Hebbeln,P., Gelfand,M.S. and Eitinger,T.
  TITLE     Comparative and functional genomic analysis of prokaryotic nickel
            and cobalt uptake transporters: evidence for a novel group of
            ATP-binding cassette transporters
  JOURNAL   J Bacteriol 188 (1), 317-327 (2006)
   PUBMED   16352848
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001051
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..328
                     /product="energy-coupling factor ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0000041 - transition metal ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33504
     Region          1..206
                     /region_name="CbiM"
                     /note="ABC-type Co2+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG0310"
                     /db_xref="CDD:440079"
ORIGIN      
        1 mhirdgilsp evcaaaslls lgavgyslrq lrvdledrav pltgmlaavv fagqmvnfpl
       61 iglpvsghll ggvlaavilg pwagclaitl vllvqavlfn dgglmslgan ilnmavvgaw
      121 ggyavyalir rclgnapfta ipaaiaaawl svlsaaavfc lefacssnsk dfslsgiftl
      181 mvlyhaligi geafitgsvl gfvlarrpdl ittptsksat tsvgqavvag lvaalavaaf
      241 lapfkseepd gldkvaqmkg ldvlqverdg lilndyevpl paplewsaaa tslagilgtc
      301 vvfamaialg kaarwklpep vadgghaa
//
LOCUS       WP_010588370             318 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Schlesneria paludicola].
ACCESSION   WP_010588370
VERSION     WP_010588370.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..318
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=34342
     Region          138..313
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mpklelsrte rhlvdsilem qvgrpnffaw gylvcggvla vfaglndnta maftafglvc
       61 gfriweersn skyaphwlsl iqkyesmred lsrggsspdt wdavdryfng qlipsdgvle
      121 saliesaaag lpsqqvapnq gkllmllaki sharkileig tlggystiwl argmaeggtv
      181 isleadpkha evargnvsra glaevvdirv gdalealpkl aeencgpfdl vfidadkksn
      241 snyfawaikl ckpgsvivvd nvvrdgtvid rqssdpsvqg vrrftelfaa esrvsgtviq
      301 tvgskgydgf aialmldk
//
LOCUS       WP_010588374             158 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA (cytidine(34)-2'-O)-methyltransferase [Schlesneria
            paludicola].
ACCESSION   WP_010588374
VERSION     WP_010588374.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..158
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=17639
     Region          7..157
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 msrepllhiv lfqpeippnt gnigrtcvav gaklwlirpl gfsldeqqlr ragldywphl
       61 dyevveswse ivqrlpgrtv wcienpaart vweasftpgd illfgretng lpaslveqyr
      121 shtlqfpmha evrslnlant vcavayeavr qfggltan
//
LOCUS       WP_010588427             118 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Schlesneria paludicola].
ACCESSION   WP_010588427
VERSION     WP_010588427.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..118
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13089
     Region          6..105
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 makktnpdfl ngvpellilq lldrrsmhgy dlvqaireas drkldfgegc vypvlhrmee
       61 qkllaskrel vggrnrivyr ltklgqqkla dsratwqhvv tavnavlqgg vhgepgma
//
LOCUS       WP_010588451             490 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Schlesneria paludicola].
ACCESSION   WP_010588451
VERSION     WP_010588451.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18742127
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..490
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=55539
     Region          100..209
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          242..474
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(358,361..362,365..366,368,392,395..396,399..400,
                     402..403,432,435..436,439..440,443)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          358..385
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          390..420
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          427..459
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msdsgyspee irkrklasdc fkrateamak qnwdyaveml ltcakvqpen lvyrqsltgc
       61 lrkkykdnkt gasmtfmklp girsrlkkar saknwsemdi aaleghalnp wdgqfnadlg
      121 daarqrdfle isvfyyelav gpdgapknve fltaladvhe lrrnysaaia tlerigkldp
      181 lngsirskim glgadqtinr grydeakstq dvkevkneap kqgyeesvkg nvkttkevla
      241 pgeseeadll rmtrkepanv ahylkladfy rrngkledsa ntfklalnvs ndpnireqme
      301 dveldmvrrn lnfakesask dpsneqsrld vaelatellq qeieifsrrv drypndlrlk
      361 helakrymra kkfdkaipll qaaskdirie aqvlaslgsc flakkqnsla krqfekalek
      421 lnandnpipf kechyylgrl seeagdkada ekhyteilai dydyrdtvdr mtriqggdee
      481 snqidtgehe
//
LOCUS       WP_010588458             361 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Schlesneria paludicola].
ACCESSION   WP_010588458
VERSION     WP_010588458.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..361
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38887
     Region          4..327
                     /region_name="UDP-GlcNAcDh_Arch"
                     /note="UDP-N-acetylglucosamine 3-dehydrogenase; NF040723"
                     /db_xref="CDD:468687"
ORIGIN      
        1 mdrlrvavvg vgalgrhhar ilselegvdl vavadsqaer gqeiaakhqt qwvadyhell
       61 qdnridavsv vvptiahrkv agafleqgip vlvekplagn vaearelvel akrhqtllqv
      121 ghierfnpaf maaekviaep kylrcertst ytfrstdigv vldlmihdid lvlslvkspl
      181 rgceafgigv mgqhedaaqa rlyfangcia ditasrispv asrsmtawsa agcvtvdmhq
      241 revkcfapsh alrhgtpplq maaqpgadle tlkkgvfghf itndaipvdn tgpdaltqel
      301 aefvqcvktg crphvggdqa laamivadri lrqvkthqwd gtpagavgay phatvpqrkv
      361 a
//
LOCUS       WP_010588466             497 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Schlesneria paludicola].
ACCESSION   WP_010588466
VERSION     WP_010588466.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..497
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55160
     Region          10..366
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mwslkgakra iifagclaaa ytqlttspat iqyiralgan efhigilgam ptlmlfmqfv
       61 savvvnhlay rrrlwfwaam thrlmllpta lgpwlfpems dqfwvwtlli ttainqgllh
      121 fssplwlswm gdylphkgls sfwgqrqlwt qiaaagslca aaflvhqsgl pidisyavmt
      181 cigtlcgvid lllffkvaep pvqkapsprl mkvltepfhs sefrryigfm cfwnfaamag
      241 apfislylls evgmdlfhvl llwtiswvgg amfsrtlgrw adahgsqpvl vmcvalkssn
      301 mlalllipps psiafwvlap cfmldaalna gilianngfm iknspsenrt myiaatqava
      361 gvvggltsil aglvmqqlsg tqwnvlgwtl gqfqimflas ialrwvallm tryvnepsar
      421 htwdvvqema rdtlermevr rtrvfarvrv itkrrlrtgs vidgtsqglg adipggharv
      481 papkrarrlr prrsqpm
//
LOCUS       WP_010588535             189 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Schlesneria paludicola].
ACCESSION   WP_010588535
VERSION     WP_010588535.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..189
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=21001
     Region          15..>176
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnedilqnlq kvnlfrglsa eevrsmmsha elrtygssas vfetgadera iyflvegtve
       61 ialevpfste vildelnvgs vfgessffhs qphsvtarav sevtvarler adydrllesn
      121 nlaacrmgan aaeilaaklq htdhwiadll qaeeahrtre rwhqfrqslg hafdnpeggg
      181 fsthagwre
//
LOCUS       WP_010588711             166 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Acinetobacter ursingii].
ACCESSION   WP_010588711
VERSION     WP_010588711.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter ursingii
  ORGANISM  Acinetobacter ursingii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Acinetobacter ursingii"
                     /db_xref="taxon:108980"
     Protein         1..166
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=18995
     Region          1..>30
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mvviviiail aslillnisg vdqrkamqar effildlkki nkesvdqsri fallthnatd
       61 vapfsyelae yhdlraqtvi qedkkwqpys efpvrvlper vafniesvdq nyqnatqqdl
      121 inqqapkliw fgngevkpvr iqfyfeqnpv gdpievdhlg ninenq
//
LOCUS       WP_010588607             339 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Acinetobacter].
ACCESSION   WP_010588607
VERSION     WP_010588607.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..339
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=38080
     Region          3..332
                     /region_name="rsmC"
                     /note="16S rRNA (guanine(1207)-N(2))-methyltransferase
                     RsmC; PRK09489"
                     /db_xref="CDD:181902"
ORIGIN      
        1 mdprsevvlr qqqflsgkvl linapadela relpndlnis iwtwnfadhq yfeqqqfath
       61 fsvefpqkdi dqviifvpks kellsyilhv vashlkqgqs iflvgekkgg veraakqlqv
      121 lgknlkldsa rhcqlwqcil hktetlkple nwvktysiev nqtqlhical pgvfsqnhld
      181 vgtgillpyl nniksgklad fgcgagvisa ylaklncnne iyaldvdafa lrstemtfhr
      241 nglhleqlhi qavtgihdap leldaivsnp pfhqgihtdy aaseglckqa krhltvngel
      301 wivanrflny pllieqqfgr cntladqqgf kvlyahvsq
//
LOCUS       WP_010589192             270 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Acinetobacter parvus].
ACCESSION   WP_010589192
VERSION     WP_010589192.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter parvus
  ORGANISM  Acinetobacter parvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Acinetobacter parvus"
                     /db_xref="taxon:134533"
     Protein         1..270
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30421
     Region          3..269
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mqlfdththf dvadfdhdrq hlavqakqvg vealvligfi esrfdeliqt hqqlqhwenv
       61 pqsylapglh pfyieqhqqa hlqrleqvlk qhdcvalgei gldtflkqhk qpelfakqqh
      121 yfnaqlelat hyqkpvllhi rkahaealai lkaqkfklgg iahafsggve eakaliklgf
      181 kigvtgqitn pnakklhqvv qaigaeylvi etdcpdmtpl ccqtstehrt rntpvnlpyv
      241 ldslaqtlgh sqdqlaeqlw qnslaalrlq
//
LOCUS       WP_010589565             327 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Acinetobacter parvus].
ACCESSION   WP_010589565
VERSION     WP_010589565.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter parvus
  ORGANISM  Acinetobacter parvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Acinetobacter parvus"
                     /db_xref="taxon:134533"
     Protein         1..327
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=38601
     Region          12..316
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mqknkkisqf dddifsdfmd ylqdnphvrs nnqiitigyq iidflffvae lyninnfigi
       61 gknnrislsi knkklsrenn kkranpsyfh ysfpppspkr krypvslddy nrllnhinss
      121 eneplrlrnl cilqalentg grrtevcsis mnslrsalks esnsplleii nlknnrlikt
      181 reipvsrtfl lnlrfyvqyy rnpilqkkgi nhdyifisht sgqplqpdtl ttymnnwske
      241 anlssqvcah mfrhrfitek fkslilehel sngdefrkml lntyrlkqim lewtghksii
      301 sldtyinlaf delseidklk ermmwfr
//
LOCUS       WP_010589716             237 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [unclassified Acinetobacter].
ACCESSION   WP_010589716
VERSION     WP_010589716.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..237
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26986
     Region          1..223
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mllekilqsq gfgsrkycqq likngsvqid qqvcnnpkqn iatdqlcfqv fgeeyqyreh
       61 vyivlnkpqg yecshqathh ksvfsllpei lihrgiqcvg rldqdttgll lltddgqylq
      121 althprkhvp kvyhvstadp vtaeqqmrle rgvelrnekg iyaatdvqlf sthqlsmtih
      181 qgiyhqvkrm laavgnkvea lhrhqigsle lpellqgewm ylsdeqkqls qnisged
//
LOCUS       WP_010589833             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: patatin-like phospholipase family protein
            [Acinetobacter].
ACCESSION   WP_010589833
VERSION     WP_010589833.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..305
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31763
     Region          53..280
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mkiarlscla ilgfallgcd qtakkapstm aikarepvia lalggggakg fahigvikvl
       61 eshgikakiv tgtsagsfvg siyasgqtpy qmqnlalklq esdlrdltln sqgiilgqkl
      121 qnyvntqvgn kpieqfpirf aavatrldsg kkaefikgna gqavrascsi pnvfvpavig
      181 ntkyvdgglv spipvktakd mgadiviavd isarpvggkp lsmwglldqt inimgqqsin
      241 eelnqatvvi qpkvghlgal dlkssneail egekaaqaki taiqnaittf knspaalkpa
      301 pkskf
//
LOCUS       WP_010588565             261 aa            linear   BCT 01-JAN-2025
DEFINITION  NRDE family protein [Acinetobacter ursingii].
ACCESSION   WP_010588565
VERSION     WP_010588565.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter ursingii
  ORGANISM  Acinetobacter ursingii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Bard,F., Casano,L., Mallabiabarrena,A., Wallace,E., Saito,K.,
            Kitayama,H., Guizzunti,G., Hu,Y., Wendler,F., Dasgupta,R.,
            Perrimon,N. and Malhotra,V.
  TITLE     Functional genomics reveals genes involved in protein secretion and
            Golgi organization
  JOURNAL   Nature 439 (7076), 604-607 (2006)
   PUBMED   16452979
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Acinetobacter ursingii"
                     /db_xref="taxon:108980"
     Protein         1..261
                     /product="NRDE family protein"
                     /GO_process="GO:0007030 - Golgi organization [Evidence
                     IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=29754
     Region          1..241
                     /region_name="Tango2"
                     /note="Uncharacterized stress-responsive protein, TANGO2
                     (Transport and Golgi organisation 2) family, contains NRDE
                     motif [General function prediction only]; COG3332"
                     /db_xref="CDD:442561"
ORIGIN      
        1 mcivalawqv leqtpiclls nrdefyarpt tqlyqwsnlp ivagqdlqsg gtwmgvtasg
       61 rwaivtnfrd gqdkktydts rgalvedfll sdltpirfaq qleqkqqqya gfnlfmgvqt
      121 qavymsnrge apqvlakgvy vvsnglmseh wektahlrkr ftqeflpmlq dnanqddien
      181 aawdileder kvisellpat gisaemeqll sstfiqspvy gtrcsnflnm rnqqwnwlek
      241 tqwgdfkdqi idlniplnkq s
//
LOCUS       WP_010590103             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Acinetobacter].
ACCESSION   WP_010590103
VERSION     WP_010590103.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 182)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10632273
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..182
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20737
     Region          3..33
                     /region_name="Nudix_N_2"
                     /note="Nudix N-terminal; pfam14803"
                     /db_xref="CDD:464323"
     Region          37..159
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04511"
                     /db_xref="CDD:467545"
ORIGIN      
        1 msfcvvcghq teakiplgdh ksrlvcthcg nihyenpkvi cgalalwddk vllcrraiep
       61 ryglwtlpag ymelfetmeq gaaretreea eaeveieqly cmyniprigq iyvlfkahlk
      121 qglfgagees iecrlfeehe ipwtelafps veqtlrhyfa drktglfpph letlgtrldh
      181 tg
//
LOCUS       WP_010590117             318 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Acinetobacter sp. CIP 64.2].
ACCESSION   WP_010590117
VERSION     WP_010590117.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 64.2
  ORGANISM  Acinetobacter sp. CIP 64.2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acinetobacter sp. CIP 64.2"
                     /db_xref="taxon:1217694"
     Protein         1..318
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32484
     Region          26..318
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          209..316
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(214..215,248..249,252,256..257,260,306,310)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mqdiidpvag isvkpancaa dgallndagi tsmdaqgnls rngdegifhv nadgsgtany
       61 eggvivvnad gsgtingngd ggaddgiisv eadgsgtyng kygiivldgk gggtwngdhg
      121 virnqgdgsg swngpqgivt inadgsgtwn sphglvsndg kgngsigtpa rqvkmapipk
      181 vtpagkfppl kkfaplgapc gfiitlndqv lfdfdksdir pdaakvldtl avalqkvpak
      241 tieirghtda kgsdaynlnl serraksvsm alrqrgaatd asthgygesq pvapnevsgq
      301 dnpagrqlnr rveifvrt
//
LOCUS       WP_010591279             138 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Acinetobacter].
ACCESSION   WP_010591279
VERSION     WP_010591279.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..138
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14797
     Region          1..138
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mkstkteive flqqffspsl arceieevte kgaslvwhvs dqdirpggtv sgptmmalad
       61 falyvailge igliglavtt nmninflrkp tggvdirgvc klmkvgkalv vgevwiysld
      121 sddpvahvtg tysippqk
//
LOCUS       WP_010591459             199 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_010591459
VERSION     WP_010591459.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..199
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22580
     Region          23..69
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          88..199
                     /region_name="TetR_C_24"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17932"
                     /db_xref="CDD:465574"
ORIGIN      
        1 miansindiq piacfddspr grlllgaayl fhkqgyaktt vrelanfigi qsgslfhhfk
       61 skddilahvm qqtiiynhar lldaikisdd peqqlkhlik aelisisgdt gsamavlvye
      121 wfalskprqd ellklrnaye diwltviekl relnkvqhda fiwrrllgga iawtvtwykp
      181 ngkmtmdelt etvlsmalk
//
LOCUS       WP_010591536             193 aa            linear   BCT 01-JAN-2025
DEFINITION  TMEM165/GDT1 family protein [Acinetobacter bereziniae].
ACCESSION   WP_010591536
VERSION     WP_010591536.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bereziniae
  ORGANISM  Acinetobacter bereziniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Acinetobacter bereziniae"
                     /db_xref="taxon:106648"
     Protein         1..193
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20721
     Region          1..191
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 msaflislav valseigdkt qllalllsar frkpipilla iflatlvnhg vsailgqwit
       61 tvlsptvllw ivslgfigma iwmlipdelg desesinkwq kygvfgatfv lfflaeigdk
      121 tqiatvalaa rfdsigwvtv gttlgimlvn apavfignql aeklpislih kigalvflti
      181 gvaalvqhyf fkv
//
LOCUS       WP_010591918             548 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sigma-54-dependent Fis family transcriptional
            regulator [Rhodococcus].
ACCESSION   WP_010591918
VERSION     WP_010591918.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..548
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=58487
     Region          3..545
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mnglrpeial swkrsqlsgi dpgrlpeptl lgpsdaagrl ldaarpvlde lrtqlagtgc
       61 cillvdrdcr ivarlfdsap mqrameeigv vpgaalsedt ygtnalgtpf evrqslvvhg
      121 eehyleslkd fscyghplvh pvtrriegil ditaagktan plfapflara ardiearlle
      181 garesdrrvv dafqraaqqr gvavaamged imltnkaave lllpadhaal raiavdlpag
      241 esrtmdfals aggstrlrid ripgigsgal flldasgare pvprsdvaqd attrlrrrlg
      301 rlrdgaggva ivgepgsgrt waarelvrea gtfldaariv gegerewsar lltvaaaatd
      361 rgfvvvehvh lapdpvpall ssmlsdpaap rlvltadpvd girppvrell arcpgqvrvp
      421 alrqrirelg dlaaalaqel grpdlrlgps altalsersw pgnlaelrav laavpvresp
      481 lpvrredlpv dyratsrvsr lggreraere aiiealresg gnkvhaaaql gisrttlysr
      541 iralgiag
//
LOCUS       WP_010591971             271 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutamate racemase [Rhodococcus].
ACCESSION   WP_010591971
VERSION     WP_010591971.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..271
                     /product="glutamate racemase"
                     /EC_number="5.1.1.3"
                     /GO_function="GO:0008881 - glutamate racemase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=27826
     Region          3..236
                     /region_name="MurI"
                     /note="Glutamate racemase [Cell wall/membrane/envelope
                     biogenesis]; COG0796"
                     /db_xref="CDD:440559"
ORIGIN      
        1 mivalidsgl gllptsawlr rlrpeldlml smdpdgapwg pkpgdwvidr vvrtaeravt
       61 rgaevvvlpc ntasvtaleh vrealgdeip vigtvpaikp aaaacesvai wataattasr
      121 yqadlvarfa gdrtvvgvac hgladaidrg dttaaataia aaaqrtppdv ggvvlgcthy
      181 plvadviaah lppgvrlfds aeavaaqtlr ridalgrpwa gsgrvevfls grpgelppga
      241 lgypagrrlv dgigdptagl pgdeapraet r
//
LOCUS       WP_010591994             305 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Rhodococcus sp. P14].
ACCESSION   WP_010591994
VERSION     WP_010591994.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32188
     Region          <41..73
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          104..301
                     /region_name="PBP2_CysL_like"
                     /note="C-terminal substrate binding domain of LysR-type
                     transcriptional regulator CysL, which activates the
                     transcription of the cysJI operon encoding sulfite
                     reductase, contains the type 2 periplasmic binding fold;
                     cd08420"
                     /db_xref="CDD:176112"
     Site            order(119..120,122..123,126,130,132..138,230..235,
                     241..242,244..245)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176112"
ORIGIN      
        1 mtqpppsptv rwpdlaalel lvgiddhggl gaaaraagva qpnasravrr lekqlgavlv
       61 rrgragsalt pegtvvahwa rqtltdarrl ldaaaalrtd rqaeltvaas mtvaehlipr
      121 wlgrfrglhd dvhiqlqvhn srqvcdavaa archvgfvea pavppglhst pvaqdrlvvv
      181 vtpahpwarr rrpltvaela atplvvreeg sgtrhtldla lrefdrpapl lelgsgaavr
      241 taalggvgpa vlstlavadh lapgelravd vegldlartl ravwrpprkl agpagdlvrm
      301 ivrga
//
LOCUS       WP_010592111             418 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ROK family protein [Rhodococcus].
ACCESSION   WP_010592111
VERSION     WP_010592111.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..418
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=42897
     Region          105..397
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mypnvvrpkt garsrgaaar vqptarvqiv ppelkiadgt aaavfrtaaa rgpicrdqaa
       61 aatgasiatv nrqvsamlaa gllrerpeli esgavgrprv pfetdheryl tvgihvgaav
      121 tgivasdlrg rviggveipt prggqeaalg titgsarafa arwhrrmplw agvalggrvd
      181 satgtvdhpr lgwadapvga vvsrglglpv svaahveama asellltpdr dtadvegatl
      241 yfyaretvgi aiafdgrvht prggpgsvsh lptgssvpca cgargcleat vadravlara
      301 raaglldara tsvaalyala rngsreahei laeraqvlgr svamlrdlfn pdrvilggqa
      361 ftaypaaaph varalgstsg advrvtgfgd rvqahaasvv slsslysdpl gamrrals
//
LOCUS       WP_010592135             246 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010592135
VERSION     WP_010592135.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..246
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26965
     Region          35..190
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpnhrvpqpp sptdtpvpta aaptkqdgrk rrwhehkiar reelvdgtik airsrgrdvg
       61 mdeiaaeigv sktvlyryft dkndlttatm lryvetilap riyaavaedl deydltrvai
      121 atyvetvasd pevylyvmtn saaagrdvva dsermiaelv atvigerlrh lemdsggsvp
      181 wayaivgaiq lathwwisnk smsaedltdy ltmmtwggis giaavggspa rfksrphpll
      241 pdadtp
//
LOCUS       WP_010592147             152 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SRPBCC family protein [Rhodococcus].
ACCESSION   WP_010592147
VERSION     WP_010592147.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167397
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..152
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16450
     Region          4..132
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cd07812"
                     /db_xref="CDD:176854"
     Site            order(5,7,16..18,20..21,36,42,44,46,48,65,67,69,76,78,
                     92..93,95,97,103,105,107,109,123..127,129..130)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176854"
ORIGIN      
        1 msetaqrdtt atsqqvwdvl adgwsyaswv vgasriravd dtwpavgsri hhsvgvwpal
       61 lndhtevvas vpgkelklra rawpagqaei tmrlherpgg criemaekaa agpgqlvpda
      121 iqarlvlprn ieclrrlvlm aeratepkgv ge
//
LOCUS       WP_010592182             229 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Rhodococcus].
ACCESSION   WP_010592182
VERSION     WP_010592182.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..229
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25504
     Region          6..218
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msaggtrrdr vyralrsdlm tgvlppdtrl geerlaeqyg vsrtpvreal arlvsdglve
       61 rreqglfpyr prfddladly elrttlelrg irraladhsn rhdpdvlgge ldrwyalrrd
      121 lpepdagfvv ldeqfhlall aaagnpalcd alaavnakvr pvrmfdylth driaatvdeh
      181 igvaeavlag rledahdqll ahidtsravv vqraeqartm arlaravrd
//
LOCUS       WP_010592210             211 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Rhodococcus].
ACCESSION   WP_010592210
VERSION     WP_010592210.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..211
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=22719
     Region          44..119
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          126..197
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 madrpseapa rpheataarp leataarple ataarplnat aasllgflhe gpktgwdlvv
       61 taqerigkfw sittsqvyre laameraglv eagevgprdr kpfaltgagr aafaewiere
      121 pgpenirypl lltvafgrhl ppgrlaemla vhrvaherrl adyeraaaec gadpyssatl
      181 dfgivyerav lewfdrvegs lggglvnpda v
//
LOCUS       WP_010592232             116 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Rhodococcus].
ACCESSION   WP_010592232
VERSION     WP_010592232.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..116
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13002
     Region          9..105
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mlvnsprtev tdnkdqnrfe lrlngdlvgi lgyfdtdrps gvpgrnhpvv dflhtvived
       61 fghrglagvl vgrsldlare rgwrvrpvct yvqrfltahp eyrdvvlple paagrr
//
LOCUS       WP_010592256             439 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA cytosine methyltransferase [Rhodococcus].
ACCESSION   WP_010592256
VERSION     WP_010592256.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..439
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=47703
     Region          12..336
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 msgsvrdgel evieicagag gqslglerag fshrlaveld phaaatlthn lgksvsdpge
       61 ivkvgdaads svldpaehvg idlfaggvpc ppfsiagkql ganderdlfa wavemcgrmk
      121 pkalllenvr glsgnrfsay rqhvldqlre ygyigewrll hasdfgvaql rprfvlialq
      181 peyaeyfswp epiegpaptv gevlrdlmgv ngwedhhvda wvrkantiap tivggskkhg
      241 gadlgptrak rawaelgvda mgvadaapsk gwvvpegkpg pkltnemvar iqgwygeftg
      301 weflgkktsv yrqignafpp pvakalgvsi rdallktgtr rkliedvdvv hdpiytllrs
      361 cvqpltvdqi carlskneil iaapeverri anlsrdfeit tterstgtla frlgeffgfv
      421 gqeshmrhel falnrskis
//
LOCUS       WP_010592302             186 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aromatic-ring-hydroxylating dioxygenase subunit beta
            [Rhodococcus].
ACCESSION   WP_010592302
VERSION     WP_010592302.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..186
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=21773
     Region          18..186
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mttdtrsteg spasvrradv hlqhaveqfl yaeaehldnh ryhdwldffg edvhywaptr
       61 mtrtfrerda eisgpdegaf idddfhflrg rvrrltsgls wseeppsrtr rlltnvrvah
      121 redgdldvvc nfsvyrsrle rhedwfvger fdvlrhhgga lpfkirerri vleqttilap
      181 sisifl
//
LOCUS       WP_010592306             418 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Rhodococcus].
ACCESSION   WP_010592306
VERSION     WP_010592306.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..418
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44141
     Region          23..402
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtriehhvvv gagaaglaaa samrdngfag ritvvdadph tpyerpplsk eyladrrlre
       61 ivaeteyrrl dvelrlgvgv rrlrpadrri dtadgdalaa drvllatgvs arrldvpgad
      121 lgniltlrda ddaaalaarl saggplvvvg ggfvglevaa saadrgidvt vvelgdlpll
      181 aavgpdiarr icrlhtergv riltrrtvda fvgssaveav rlstgerlda atvvvgcgvv
      241 pndalarqag tacadgitvd dlgrssdwiw aagdvaahvn phlgrrgrie hwdvarrhga
      301 avgasmagta tvnreipyfw shqyahtlqm ygrgrpgdrv vvresttepg fvafwvrdgr
      361 iaaaaaldep rdvrsakila enrsavpdev lrsagtdlrr varqlgrsga praadvag
//
LOCUS       WP_010592308             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010592308
VERSION     WP_010592308.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22159
     Region          5..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mssaeatsqs sreylmnvae qlmaargyhr tsiadirras glpvgsiyhh fksksgllaa
       61 viergsrrff anlpravdis gsseetmray wsaaaatiae hisyfqlead ivwhgaadpe
      121 laavvatatd yardqlvavv epfaresgvg dpralavela ltsvtfvrga viesggdaay
      181 lerkigalyr mlradivvqg adrgarq
//
LOCUS       WP_010592345             356 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Rhodococcus].
ACCESSION   WP_010592345
VERSION     WP_010592345.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..356
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39286
     Region          33..354
                     /region_name="COG3435"
                     /note="Gentisate 1,2-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442661"
ORIGIN      
        1 mtatentdpe lqqlytdfea ehlnplwtql gdlmpmvpts kavpfvwkws tlyplaqrag
       61 dlvpvgrgge rraialanpg lggvpyvtpt lwaaiqylgp ketapehrhs qnafrfvveg
      121 egvwtvvngd pvamcrgdfl ltpgwnfhgh hnetdhpmaw idgldipfvn ytdtgffefg
      181 sdgvtdestp dvsrserlwv hpglrplvgl dakasspiac yrwkytdaal neqlaledeg
      241 yaatpepgha airytnpttg gdvmptirae fhrlragaht rtrrdvgstv fqvfegegrf
      301 hlggtdhdvt kgdmivvpsw vewsletdgg vdlfafsdap iverlhfnrt yisega
//
LOCUS       WP_010592365             395 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Rhodococcus].
ACCESSION   WP_010592365
VERSION     WP_010592365.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..395
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42760
     Region          13..393
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msatdalhpp vlfapeyeef aqwvrefaap haesylerah reefpwdlae kmaaqgllgl
       61 gvseenggqg rigevltkth lgiaheelay snfyltqlay tnnltgplle rflapevakd
      121 wvrgivegrh vvalgltepg sgsdamamra kaekvdggwk lngektsitf aphakamitf
      181 vkargatpee sgvtaflvpl daegvsmqkf pdagwkplgr agvflddvfv pdeyviggvg
      241 ngfrlvmsef dytrsviglm stgvarkald itidyvksrk afgrpvssfq gvsfpiaena
      301 tkleaarwlt yralsladag kpftkeaamt klyatevslq tirdcivahg hsgfaeelpl
      361 qamlrdvfgl eigegtpqiq kvvigrallg reata
//
LOCUS       WP_010592381             538 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease, partial [Rhodococcus sp. P14].
ACCESSION   WP_010592381
VERSION     WP_010592381.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 538)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         1..>538
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          31..>533
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 msanpirrva lrnlaahkvr llltvlsvvl gtafvtgsfv ftdtlqrtfd dlfadaakgv
       61 dvrvsseqqg ssgvpdsdva vvsavpgvrt vvpafegpvi vldsegaaiq tggapsegta
      121 ylppdqqlgd ptefvagrpp aadgqialns saaeraglsv gdptkilaas agivpvtvsg
      181 iydvetdtgg yvgamftenq aralftdgth vqyidvagdg vpadelrdri aaavpdqkvq
      241 tgaevseeik teieealsfl nyfllafgai allvgtfiiy ntfsmivaqr lrelallrai
      301 gasrsqvgrs vtlealvvgv vgsalgivgg valayglraa lnafdvglps gplqlaprtv
      361 lvalligivv tvvsayapar raskvapvaa mreestatve slrmrtvvga vaavvgaavv
      421 vvgaqgtggg aastvgigaf aliiavllaa palsrpfvag lgavvarpfg avgrlartna
      481 vrnprrtaat afaltlglml vsvigvfgas akasvnslvd tgvksdfmlt gpqmigvp
//
LOCUS       WP_010592436             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Rhodococcus].
ACCESSION   WP_010592436
VERSION     WP_010592436.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..389
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42284
     Region          1..387
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maeivldkvt klypdgarav sdvdmtiadg efiilvgpsg cgksttlnmi agledissge
       61 lriggervne kapkdrdiam vfqsyalyph mtvreniafp ltlakvpkde varkveeaak
      121 ildltghldr kpsnlsggqr qrvamgraiv rnpkaflmde plsnldaklr vqmrteiarl
      181 qkrlgtttvy vthdqteamt lgdrvvvlrg glvqqigapq elydrpknlf vagfigspsm
      241 nffagrldgd rvrtaigdft lpaerwaavq khdpgrdvvv girpehfeda alldpaqreq
      301 gtiftvdidv lesmgsdkya yftvespelh ssdlddlaad vgvadlaggs mvarlpaesd
      361 vakgrpvqlw fdpakvalfd qatgenvtl
//
LOCUS       WP_010592446             483 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S1C family serine protease [Rhodococcus].
ACCESSION   WP_010592446
VERSION     WP_010592446.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..483
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49446
     Region          211..480
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mscradtprl qprpvyrpav ddaanrvfgr pagttgpfgr saeeraaepp vrhgaptdpv
       61 laeafgrpad tseilqrppv dpdaeadadg pepdpwrdpa tnvrlgapaq shdeqplppa
      121 pkltlrevlf ggrietrala tlaavaltig mvgglvvalv tsdtgsltsr svtlaqvdqd
      181 gdlpsgqvar vadavlpavv siqvtlgeea gtgsgvvidg agyivtnnhv vsmaatapda
      241 kiqvtfndgt kvpaeivgrd iktdlavlsv dadnltvael grsedvqvge dviavgsplg
      301 lsktvtrgiv salnrpmrlg gqgtdtdavi davqtdasin pgnsggplvd aegrvigins
      361 aiktetggsv glgfaipidd vtavaqelir tgemrhpeig vntrsvandv asgaevanvq
      421 qgspaqqagi vegdvivkvg drevtsadel vvavhaqeig kpvtvqlvra grlvdvqvtp
      481 msd
//
LOCUS       WP_010592517              65 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tautomerase family protein [Rhodococcus].
ACCESSION   WP_010592517
VERSION     WP_010592517.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..65
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=7119
     Region          2..59
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mplidvtiae grspdelrrl iheltqaahr aldaplpnir vvlretpkth faagdvtiae
       61 retra
//
LOCUS       WP_010592521             437 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Rhodococcus sp. P14].
ACCESSION   WP_010592521
VERSION     WP_010592521.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         1..437
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46194
     Region          21..411
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,262,265..266,269..271,274,301,305,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mttrterfae lpltrrhgrl llgsgvgwal damdvglisf vmaalavqwn lsatqlswig
       61 sigfvgmavg aavgglladr igrrqvfavt llvyglatga aalagsvavl ivlrfvvglg
      121 lgaelpvast lvseyaprrq rgrmvvalea fwaagwilaa ligyfviplg ddgwrwalav
      181 givptlyavv vrfglpesvr ylerrgryae aekavrsfem sagvaaptda eetsrpvlte
      241 tsaesiwspr lrrrtaalwt vwfcinlsyy gafiwlpsll vnqgfdlvks fqytliitla
      301 qlpgyavaaw lievwgrrat lasflvgsaa aaglfgladt pteivaagma lsffnlgawg
      361 alyaigpely ptsvraagtg aaaafgrias ivapllvpwl ltgggnalvf gvfaaafvla
      421 avaaftlper kghvlea
//
LOCUS       WP_010592548             551 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkaline phosphatase D family protein [Rhodococcus].
ACCESSION   WP_010592548
VERSION     WP_010592548.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..551
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=61684
     Region          94..458
                     /region_name="MPP_PhoD"
                     /note="Bacillus subtilis PhoD and related proteins,
                     metallophosphatase domain; cd07389"
                     /db_xref="CDD:277335"
     Site            order(99,142,145,204..206,210..211,429,431)
                     /site_type="active"
                     /db_xref="CDD:277335"
     Site            order(99,142,145,204..205,210..211,429,431)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277335"
ORIGIN      
        1 maelvlgpvl rhvgrrdatv wvetsdpctv eilghrehtw tvaghhyalv viddlesgst
       61 tpyevrldgh pvwpppdfpa svvrtlgtgr plelifgscr fattaatend dklgadalda
      121 yaqrmttrap drwpdallll gdqvyadels aqtlervrer hdldeppgpq vrnyeeytwl
      181 yaeswsdphv rwllstvpts mifddhdvhd dwntsqswrd eveatswwee rivgalasyw
      241 vyqhlgnldp aelagnelyq rvrkcdgdae pllrefasaa deeadgakgt lwsfrrdlgn
      301 vrllvidsrc grilaggrre mvsdpefswi erqtegdydh llvgtslpwl lpralhdles
      361 wderlaagvr gkrvagwaei vrrgadlehw aafrdsfdrl arlfaeigrg rctgpsgrpp
      421 aticvlsgdv hhayvaqarf pdpmstrvfq ltcsplhnyv paavravfrv swsramerav
      481 rfvlgrvsev ppvpiewtra tgpffgnqia tlrlagraah lllerservp rgpvgfttta
      541 dlvlsapega p
//
LOCUS       WP_010592577             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Rhodococcus].
ACCESSION   WP_010592577
VERSION     WP_010592577.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..279
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29934
     Region          82..278
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtstadrrag tpaavvdvlh vagprptpas afaaslsfgw rallrikhvp eqlfdvtvfp
       61 lmftllftfl fggalagstd ayvqflipgi lvqtvctitm ytgmtlnrdi ekgvfdrfrs
      121 mpvwrpaplv galfgdlary tlasvivltl givlgfrpag gpvgaaaava lvllfafsls
      181 wvwtmlamll rteqavmgvs mtilfpltfa snvfvdpatm pswlqgfvtv npisrlvtav
      241 rdltagtpda ahlamvfgwc aalvvlfgpa tmwlynrrs
//
LOCUS       WP_010592614             480 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amidohydrolase [Rhodococcus].
ACCESSION   WP_010592614
VERSION     WP_010592614.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..480
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50516
     Region          5..>58
                     /region_name="metallo-dependent_hydrolases"
                     /note="Superfamily of metallo-dependent hydrolases (also
                     called amidohydrolase superfamily) is a large group of
                     proteins that show conservation in their 3-dimensional
                     fold (TIM barrel) and in details of their active site. The
                     vast majority of the members have a...; cl00281"
                     /db_xref="CDD:469705"
     Region          35..476
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mpphlvlrsa rtapgadpvd lpitgdrvvs dpaggaetvd vggrlvlpgl wdahvhfdqw
       61 althaaldls gatsaahava lvaarlvvdp apvvvargfr dglwpdapta avldaiapar
      121 pvvalsadlh cawfntsalq hfslhphptg llresefmpl mndiqrvdae vrdrlvdaaa
      181 raaaargvvg vvdfeiadnl aawsrrigag trylrvrcgi wprwlgaaia agmrtgdpvp
      241 gtaglatvgp vkvivdgslg trtaychepy pdgehgvltv ppeqleplmr hahdhgfesa
      301 vhaigdhaca hvldafaatg ahgsvehaql vaerdvprfa rsgiaasiqp ahvyddvdla
      361 erywpgrthr sfpyatlhaa garlvlgsda pvapldpwrt laaaidrtlp dgrvwhreqe
      421 ldlqvalaas tggrtrvtag dvadlvvlda dtlprsgael aatavwgtml ggrwthgpla
//
LOCUS       WP_010592636              85 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HPr family phosphocarrier protein [Rhodococcus].
ACCESSION   WP_010592636
VERSION     WP_010592636.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..85
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=8080
     Region          1..84
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 mpsttvtvgs siglharpag iiaeavvaag vpvtlavdgg epvdagsall vmtlgatqgt
       61 evtvtsddad vlariaelva adlda
//
LOCUS       WP_010592653             511 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: serine/threonine-protein kinase [Rhodococcus].
ACCESSION   WP_010592653
VERSION     WP_010592653.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..511
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=53475
     Region          16..271
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(16,40..41,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(23..24,26..29,31,44,46,78,94..97,101,103,139,141,
                     143..144,146,161..162,165,182..185)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(23..24,26..29,31,44,46,78,94..97,101,141,143..144,
                     146,161..162)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(27,101,103,139,141,143,165,182..185)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(161..169,178..185)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mddtvgelqp gsvfagyrie rrlatggmgs vylarhpnlp rfvalklldl sananpgnrs
       61 rflreadhva rlehpnivtv ydrgnvgdql wiamqyvdgt davgalregp mrparavriv
      121 setaraldha hahgvlhrdv kpanillaps sgsepervll adfgiakslg stavtetgil
      181 vaslqyaspe qiegrppgpr tdvyalgctl yqlltarppf pgteaahlvh ahlhlapprp
      241 taarpelppa ldaviarama krpedrfptc galaaaaraa ldepvteptr tvsaastatp
      301 vspgppaasg hpgarsprpl lvllgvvaav tlagaltgil lardgsqdad vragisatgr
      361 vdtpgpatlp svsvpataei tdittsalap tttaapqsrp dripvaqagi rgfdddigpr
      421 cnaadeavav artsesrvlv crngfdglyy kglrlgdgad ieladavpda agftvvsgpv
      481 rytfdrnell iiengtvttr eqvlqfwsay p
//
LOCUS       WP_010592656             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010592656
VERSION     WP_010592656.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22182
     Region          20..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msirneefrs sgapattved qildatrscl ldfglrrttl aevarragvs rptvyrrwpd
       61 tralvadllt reiravlpdl dgegpvrpri vravvtavde igahplfeki lrsdpdllmt
      121 yivdrlgtsq navlevltga ltrgqrdgtv rsgdvralaa fvlltaqsvv qsagmiaevv
      181 drealltela havdtylapa gedrp
//
LOCUS       WP_010592674             509 aa            linear   BCT 01-JAN-2025
DEFINITION  ribonuclease J, partial [Rhodococcus sp. P14].
ACCESSION   WP_010592674
VERSION     WP_010592674.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         <1..509
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
     Region          2..505
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 rpgvalilpd frhiedrmdd veavvlthgh edhigavpfl lrlrpdipvv gskftlalva
       61 akcrehrlrp nlvevvegdr tthgpfecey favnhsipda lavavrteag lvlhtgdikl
      121 dqlpldgrlt dlagfsrlgd egvdlflvds tnaevpgfvm pereiggvld nvigkatqrv
      181 ivasfashvh riqqvvdvae rynrriafvg rsmvrnmqia qdlgylrvpd glvvdldtaa
      241 tlpdnrlvli stgsqgepls alsrmargeh rqiniraddl vvlasslipg nensvfavvn
      301 glakrgatvv tqqnakvhvs ghasagelly lynavrptna mpvhgewrhl ranaalaeat
      361 gvprerivla edgvvvdlvd glaeivgqvp vghvyvdgls vgdvgestls drlilgeggf
      421 isisvavden gravstpgvs grgfsddpga lseaaqlvdk vlnelaaegi ddahriaqai
      481 rrvvgrwvsd tyrrrpmivp tvitvpgpa
//
LOCUS       WP_010592743             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tyrosine recombinase XerC [Rhodococcus].
ACCESSION   WP_010592743
VERSION     WP_010592743.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..308
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=32880
     Region          4..308
                     /region_name="xerC"
                     /note="site-specific tyrosine recombinase XerC; Reviewed;
                     PRK00236"
                     /db_xref="CDD:234698"
     Site            order(159,254,257..258,289)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 mdtalpppla vhleefvehl dlqggrsaht irayttdirt llahletghp dariddltle
       61 vlrswladqv aggaarttla rrtssartfc awlartgrld hdpaarlvsa rthrtlppvl
      121 radqacevma aaeagareld pvalrdrlvl ellyatgirv gelcgldvdd vdadrralrv
      181 lgkgnrertv pygapaatal dawlhsgrpa larpdsgpal llgarggrlg prqvrsvvhe
      241 nvaavpgapd laphglrhsa athlleggad lrvvqellgh aslattqlyt hvsvarlraa
      301 heqahpra
//
LOCUS       WP_010592745             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: siderophore-interacting protein [Rhodococcus].
ACCESSION   WP_010592745
VERSION     WP_010592745.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..264
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=27871
     Region          6..249
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mevgvapksp rsttltvtgs erltphlvrv ylggpgfdef epgphtdsyv kleleadget
       61 vlrtytvrav dreagqiaid fvvhgdqgva gpwaasvrpg qtvvvrgpgg ayrpdpdadw
      121 hllagddtai pavaaaleal apdargrvfl evagpddeia laapagvevt wlhrgsaagn
      181 agpdlsgasa plvsavtgae wlpgdphvfi hgeaetvmqy lrpyvrktrg vpaarasisg
      241 ywrrgrseeg frewkrelat aear
//
LOCUS       WP_010592778             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010592778
VERSION     WP_010592778.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20714
     Region          1..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msksartrqr iqatavhlft edgydavtvd riasaagvsh mtffrhfpsk davllddpyd
       61 pviaeavaaq padrsplera crgileawaq ipesdlgdvr trlrivathp rlrarmwent
      121 lrtqeavaaa laepgtrrle aavaagacmg almaaltdwa etgdgtlgnr iasalrqlvp
      181 qarpsrqsre ts
//
LOCUS       WP_010592828             450 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ammonium transporter [Rhodococcus].
ACCESSION   WP_010592828
VERSION     WP_010592828.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..450
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45433
     Region          1..416
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 meeaiaaadt awilaaftav slmvpglalf yggmvsvrst lnmimmtfag falvgvlwvl
       61 fgysavlgds lggagllgnp leylglgqll aapaepglpp aliagfqllf agitvalvcg
      121 aladrmkfsa wmvfaglwav lvyfpvahwv fafdsedgsv vggwiantlg avdfaggtav
      181 hinagiaala vilvlgkrrs flnpprphsl pltvlgagil ffgwfgfngg salaannsas
      241 vvvlntlaaa cagicgwliv erlreghatt lgaasgliaa lvaitpacga vspigalvvg
      301 alagalccfa islkfrlgyd daldvvgihl vggvlgtili gflavpaaps gatglfyggg
      361 fgllgtqtva vlavlaysfa vtwiiakgld lvmglrvdpe teyegldvvv hgetayvlda
      421 vgftgtsrte aasvaeaata ltskaaaekl
//
LOCUS       WP_010592853             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Rhodococcus].
ACCESSION   WP_010592853
VERSION     WP_010592853.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..389
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40264
     Region          33..341
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mqsterkppa pkpdrttlia sgglalakws aalvviaaga lvigwiiekm wvivlpvala
       61 ivvatmlwpp trgmmkrgvp paasagltlf lffaivggii agivpsvvaq apelankttd
      121 ginkvldwvq gppfnlkdeq lenatqvvid kvqesgatia sgvftgvsta gsllvtiglv
      181 lvlvfffikd gprfipwvha vgggragrhl eevlirmwnt lggfirtqal vsfidaffig
      241 lglvilgvpl apvlailtfi ggfipivgaf vagalavlva lvanglttai ivlviiiavq
      301 qlegnvlqpv lqsrsmhlha vvvllavtag sslfgiigaf lavpvaavaa vvlryvgeqi
      361 dersaatdel etteetpalp papaepgpa
//
LOCUS       WP_010592892             320 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SGNH/GDSL hydrolase family protein [Rhodococcus].
ACCESSION   WP_010592892
VERSION     WP_010592892.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..320
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=32451
     Region          76..271
                     /region_name="FeeA_FeeB_like"
                     /note="SGNH_hydrolase subfamily, FeeA, FeeB and similar
                     esterases/lipases. FeeA and FeeB are part of a
                     biosynthetic gene cluster and may participate in the
                     biosynthesis of long-chain N-acyltyrosines by providing
                     saturated and unsaturated fatty acids, which it...;
                     cd01836"
                     /db_xref="CDD:238874"
     Site            order(85,124,154,249,252)
                     /site_type="active"
                     /db_xref="CDD:238874"
     Site            order(85,249,252)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238874"
     Site            order(85,106,154)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238874"
ORIGIN      
        1 mprtswraaa lagatavaag sgaggaswlt ytylmrqata argvigrtwa rppeadgvyp
       61 pgaqspvpwr rgvpfdlhlm ifgdstaagl gcvsaaevpg vllaralade sgrsvrldtk
      121 aiagatsrgl agqvdamfva gpppdaavil vgandvtakl slhrsaqrlg savrrlrtsg
      181 aavvvgtcpd lgvvgaipqp lrtvvrtwgr qlaraqaaat raaggypvpl adlltpefls
      241 apdrlfsadg fhpsaagyel aaghllpvla aalglwaggp vpappqtsaa arlwlprtrr
      301 gprervfpgp avgtvagelg
//
LOCUS       WP_010592925             386 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Rhodococcus].
ACCESSION   WP_010592925
VERSION     WP_010592925.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11177873
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..386
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=41542
     Region          4..63
                     /region_name="Methyltransf_13"
                     /note="Putative zinc binding domain; pfam08421"
                     /db_xref="CDD:429987"
     Region          92..200
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
     Region          207..358
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
ORIGIN      
        1 mttcrgcgga gveqvldlga mpaadhfpla gtpvtpaets hplamalcrd cglaqladdd
       61 tvpdeprgve pqalrdqaaa avrdvadagw ltgrtvaefg sphggtwlpl ltdrgyeivp
      121 trrpaslvld cfgimhepdq htafrqrtra ltadgvlllq fhslativrq rqwtalrhgh
      181 fayysltalr hlladvglhv adawtfdlyg gtvlvaatra rrplslaarr iltdekavgv
      241 tepvavhalq raadeqaval rtclktmarq grrvyaygaa sravalfara gldqhlvagv
      301 adaspakqgr rmpgtdvpii speqllrlrp drvlltlpdl lpevrrrype ldgrwmipad
      361 haaprrgthg lraarvttga gsevqs
//
LOCUS       WP_010592967             345 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Rhodococcus].
ACCESSION   WP_010592967
VERSION     WP_010592967.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..345
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36789
     Region          14..343
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mtdtfirtrv ahgvgevvld rpmalnaldr tmirdmyepl lawrddpeit avlvtsasdr
       61 afcaggdiks vrdaavagdt ttvrdyfane yrldelvaty pkpylalldg vtmggglgis
      121 vhgavrvvte navlampeta igfvpdvgas hflprlrgtt arcdavglyl gltgaradag
      181 daiavglath fvpsdrieal adrireghwq laldefaeaa pqspiadrya didavfgdgt
      241 vvdaverlsg dhgfdeewat ttraalgaas ptslwatael lhrgaestls ecfareleva
      301 vritavpdfa egvravlvdk drnpswrprg vgevdpalia glfrd
//
LOCUS       WP_010592993             120 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Rhodococcus].
ACCESSION   WP_010592993
VERSION     WP_010592993.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..120
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12958
     Region          4..111
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mldividpgs pvppyeqlrq riatmvrrde liagtklptv rglaehlgia pntvaktyre
       61 leqlgiietr gragtfvads gdltrtlaqr aatgyvrelr tlgmsddevl efvvaalrga
//
LOCUS       WP_010592999             356 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Rhodococcus].
ACCESSION   WP_010592999
VERSION     WP_010592999.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..356
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35195
     Region          109..352
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflalrdlrf atgrfavmta vlvlisflvv mlsgltaglg nqsiaairgi gaehfaldgg
       61 gtdpsdvsfg estvtdsqra alaaqpgvad tavlgvapgr vgsggrevaa alfgvapgsf
      121 aapaglrpat aavdaqlaad ngwspgtilt vggrevtvaa lvedsyyshq pvvwldlgtw
      181 rdlpatagad gtvialrtgp gfdaptvata tgtsvldtsa tldtigsyts ergslllmqa
      241 mllvvgalvv gafftvwtvq rsrdiavlra igastsyllr dalgqaavvl vlgtglgtva
      301 ataagaaaat vvpftlsaat tvlpfvalvg igllgaaaav arigsvdplt alaaah
//
LOCUS       WP_010593048             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010593048
VERSION     WP_010593048.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20811
     Region          10..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mayrrtpavq qrldaqreai adaavsllse rgyqglsiaa vaeragvatg svyrhyadks
       61 elmvrifrsl cgrevdavva aadaarpdga aaqvaavvet farralrnpt layallaepv
      121 daavdaerlv lrrafaaafe dalrrgvdsg dltsrnpals aaalvgavge vltgplqsgv
      181 aatdtvpelv afalralgar p
//
LOCUS       WP_010593082             104 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Rhodococcus].
ACCESSION   WP_010593082
VERSION     WP_010593082.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..104
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=10818
     Region          1..101
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mreiditafa dawksgatvv dvredyeyeq ahvpgaqwip lgelgsrlae ipgadlvyvv
       61 casgnrslrg adivsasgrp avsvaggtkg wlraghpveq ggtr
//
LOCUS       WP_010593109             208 aa            linear   BCT 01-JAN-2025
DEFINITION  ZIP family metal transporter, partial [Rhodococcus sp. P14].
ACCESSION   WP_010593109
VERSION     WP_010593109.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         1..>208
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          1..>203
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mifgivassa lvlgalvggw veipkrvlaa mlafaagali talsfelfed syekggiwra
       61 aiglavgaiv ftalsawldr vaegrrekdh gsekldvdaa aegtapssss vsgaaglall
      121 aavtldgvpe nvalgvslge gtgglallva ifvsnfpesl vgsasmraqg rsrryivgmw
      181 vacaalltva vvvgagplav tppetisl
//
LOCUS       WP_010593114             354 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S1C family serine protease [Rhodococcus].
ACCESSION   WP_010593114
VERSION     WP_010593114.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..354
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35383
     Region          69..353
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mirrlgavla mvaaglvlta patveiavpp pppaapalpi vpptaeevse riapavvtlt
       61 anrgwrgisg tgivltadgt vltnhhvvtg atdisavsph tgasydvavl gydstldiav
      121 lqlgsaaglp vaavtetplp qpgspvtafg nadgggvvvp apgtivavdk tvsvrdsmdg
      181 slrrlrgmlq vsaairpgds ggplvdafgt vvgvntagav epdpaavpdp peayavpigt
      241 aldvvdqvrt gtsagtvhvg ptpllgvsvt tdrtgneetg aevlwvgygt paagtgleig
      301 dvivafdgrp vsttvdledm lmarrpgdsv eigwldvtgr hrtarvvldv gppr
//
LOCUS       WP_010593115             168 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pyridoxamine 5'-phosphate oxidase family protein
            [Rhodococcus].
ACCESSION   WP_010593115
VERSION     WP_010593115.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Leiros,H.K., Tedesco,C. and McSweeney,S.M.
  TITLE     High-resolution structure of the antibiotic resistance protein NimA
            from Deinococcus radiodurans
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 64 (Pt 6), 442-447
            (2008)
   PUBMED   18540048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..168
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18177
     Region          27..152
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 mstpvtttvd arfgddgepp lpwsdteell esaqlywlst vrrdgvphvt pliglwhagg
       61 fvfctgpgeq kthnlrhnda vavttgvatw aagtdvvveg rahrvtdgda lhavaeayyv
      121 kygqqwrfev hgdavgpvdd pgwvfrvvps kvlvfakgpf gqtthrfa
//
LOCUS       WP_010593117             545 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Rhodococcus].
ACCESSION   WP_010593117
VERSION     WP_010593117.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..545
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58676
     Region          7..542
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mtatlrisgl sasrgertlf tdlnltvapg dviglvgang agkstllatl agvgtadvtg
       61 tvafgppdat vgylaqeper vpgetilgfl grrtgvtaae hamnaaaeal gstdvddytp
      121 alerwlalgg adlaeraekv vadlgldvgl dapmtglsgg qaaraglaal llsrydvlll
      181 deptndldla gldqlerfva etrtalmvis hdreflartv tgiveldpvq qqiavydggy
      241 eaylvereva rrharetyee yadtkqeled rarmqrnwle hgvrnarrks kdndkvgrkf
      301 raeatekqaa karqtqrrie rldvveeprk ewelrmsiaa aprsgtvvat ldgacvdrgd
      361 fvlgpvttqv qwgdrivltg pngagkttll rtllgrirpd agtatlgsgv kigevdqara
      421 lfegdeplvd afaaqvpdwp dadvrtllak fglrghhvlr sasslspger traglallqa
      481 rgvnllvlde ptnhldlpai eqleqavdsf egtlmlvthd rrmlattrst rrwhldggrl
      541 teepa
//
LOCUS       WP_010593132             195 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase family protein [Rhodococcus].
ACCESSION   WP_010593132
VERSION     WP_010593132.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..195
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21363
     Region          2..186
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkltyyvat tldgfiadpa ggydffpleg dhahyqvqef petiptparg slgiegppkh
       61 fdavvmgrrt wepardagwt sgyrhlqqyv ftttmtqapd etvtlvatdp leyvrdlkqq
      121 dglgiwlcgg gslagallpa idelvlkvhp ivagdgiplf rhgfephrfd rletrtfdsg
      181 vtvcrfaagv pfgrs
//
LOCUS       WP_010593144             422 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Rhodococcus].
ACCESSION   WP_010593144
VERSION     WP_010593144.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..422
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43898
     Region          16..383
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(26..27,30..31,34,66,121..122,124..126,129,149,
                     152..153,156,229,232..233,236..238,241,268,272,335..336,
                     340,344,360,363..364,367..368,371)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mrrlladttp lenrdyrrlw tagivtvvga qlsvvavpqq iyeitrssay vgltgvfalv
       61 plvvfglwgg aladvmdrrr lltfttlgmg vtslllwaqa aaglanvwlv lvllslqqac
      121 favnqptrga viprlipngq laaanslnmt vmqfgaiagp llagalipvl glptlylidt
      181 vallatlwav lalppipptg qarraglrev ldgfrylstq killasfvvd ivamvfgmpr
      241 alfpqiahds fgdpaeggfa lgllfaamsa gavlggvfsg wlprvrrqgl avivcivawg
      301 lamvgfgvav glaepggtav wlwialafla fggavdmvsa afrstmlqsv atdemrgrlq
      361 gvfivvvagg prigdvlhgg aaalvgtava aagggvlvva gvlvcvlafp afvryrvdrt
      421 ih
//
LOCUS       WP_010593214             310 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Rhodococcus].
ACCESSION   WP_010593214
VERSION     WP_010593214.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..310
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32165
     Region          28..297
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mgvghghshg hagagapgea gpsrgrlrrm aialailvaf llleagvalw idslallada
       61 ghmltdvvgm smgmaalila rrgstaaart fgwhraevla amanaalllv vavwvfyeai
      121 hrigdapdip gtalvltata glaanlvvml llradakdsl avrgaylevl adavgsvgvl
      181 vagalvllfd wtladvvvgv lislwvvpra vrlaaaslri ltqaspahld vdgvradlst
      241 lpgvtgvhdl hvwtlttgmd vatvhlisdh dpqwvlesar avltshgleh atvqvettvn
      301 grrceenvtw
//
LOCUS       WP_010593249             179 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Rhodococcus].
ACCESSION   WP_010593249
VERSION     WP_010593249.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..179
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=19038
     Region          17..158
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 maaehtvldp rtmrdvlgnf ctgvtvvtgh dgreplgfac qsfasvsldp plvsfcpart
       61 sqtwprirei gtlainvlah dqrdtcmafa vsggdkftgv dwtrgdngap altgalarie
      121 avveaehdag dhtivvarvt gltalhddgp llfyrggfgr yttetildee tatdvnplr
//
LOCUS       WP_010593251             383 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Rhodococcus sp. P14].
ACCESSION   WP_010593251
VERSION     WP_010593251.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         1..383
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40716
     Region          128..360
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlrlplialm alvgpvivva hwlpvlfltv ltgyalaalg wlvlvlrgpv rhswwaptlv
       61 divallglca asggatsvll pvffllpvtv tflhrpwwta avgvatatgf llvwlfyavr
      121 ddgvdlpavv ylyfgfmvwl aaamtglsvv lahradavaa llatrrrlvt ealdaesrer
      181 qllaeqlhdg plqnvlaarl dveeagerrp ddallaadta lreaarqlrs tvttlhpqvl
      241 sqlglatalr elaeqsarrg gfavdvvvdg sfpreeallf svarellgnv vkhakatsvr
      301 vrlvrrgpdm vlevaddgcg fdpatlpdrv gqghiglash vlrvesvggt avvrsapgdg
      361 ttvtvtvpat epdgaalrpg rar
//
LOCUS       WP_010593296             203 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar transferase [Rhodococcus].
ACCESSION   WP_010593296
VERSION     WP_010593296.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..203
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22501
     Region          <5..177
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mallvfaiva svirldskgp vfyraerigv drepfgmikf rslmanadtl vatsmaqndg
       61 aglllkvkeg pratrvghil rrlsidelpq linvirgdmr mvdphppmrr eveaydaraq
      121 rrllvrpgtt glshlsrqsd lsgdesvrln lfhvenrsri sdvlmtgktv kavlvrdayk
      181 yrhincgral gsslregaad ser
//
LOCUS       WP_010593333             195 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010593333
VERSION     WP_010593333.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..195
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22198
     Region          1..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdpherrrqi ldrsahlfas kgiaattire iadevgvysg alyhyfpske aivtelirey
       61 iddlsgrcre itaqsqtpvd riealallal stsedyrgat tiwqregeym rdrlveadla
      121 etadeveraw raaiadgvae gtfrddidpd vfyqlirdav wqaprwhrpt sersnadlar
      181 eitrifvdgf rprae
//
LOCUS       WP_010593332             257 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Rhodococcus].
ACCESSION   WP_010593332
VERSION     WP_010593332.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..257
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27490
     Region          8..238
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtthndvpva vidraarlle afrdserltl aeltrltgmp rssthrllnq lveigwvrrd
       61 apayslgtkm lelgslvqhn dalhraalpv mhelhgrtgl vvhlavltgt evlylekvgg
      121 pysmripsrv ggrqpahcta lgkallaqgq ydvealfadh plpartphsv tdpgrlrsel
      181 armreqhvah erdeaapgvs cvaapigpag kcvgalslsg psasiratal aapvrvaalt
      241 awrrfthlra gnartav
//
LOCUS       WP_010593345             183 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010593345
VERSION     WP_010593345.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..183
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20651
     Region          1..143
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdrsrkildi aaelfyekgf hgtsvdelga ragltgpaiy rhfsgkdeil atlfdeamde
       61 liraaepmde dadsdferlv rhhvefairh rhlvnvtqre drslvdpwrr kvnrrrklyv
      121 gcwetavarc lpratpaeva vatqtclgti fsiaywptkv srtpgladli vrltneglda
      181 frg
//
LOCUS       WP_010593348             378 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Rhodococcus].
ACCESSION   WP_010593348
VERSION     WP_010593348.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..378
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41071
     Region          1..377
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mrfsreqqef alavrefcda ecktlqqrda ltadgtvans qvildkfagl gwlavslpee
       61 fggggagmie ecifleetsr glapitgyst gltaaqtylr ygteeqkrti vsnmaagkle
      121 aialsepgag sdlggvrika elvddhyvin gqktwisaah vaehvlllar tdssgskheg
      181 ltlfmvptdt pgleihgiat meartcndly ftdvavpvta vvgtpnqawr hlmrglsver
      241 liiatmslga aeralddvia fvtereqfgr kvgsfqairh riadlateia faksfvyeva
      301 eridageedn lnregsmakl kcteiakktt leamqmmggy gytreygmee qvrrslapti
      361 yggtneiqre iiskslgl
//
LOCUS       WP_010593380             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thiolase family protein [Rhodococcus].
ACCESSION   WP_010593380
VERSION     WP_010593380.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 397)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..397
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42533
     Region          13..396
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mtnatnpfqr sareviiaea artpmgrsha ergwfrdthp nemlgavytd lirrsglapa
       61 avedlvvgct apfgeqsrni grnawlqagy ppevpavvld rrcgsaqtav emgaalvgsg
      121 thdlviaggv ehmghvpins pakiselygd pwpaelreky dfvhqgesae liadrwgitr
      181 qemdefavrs hrlateaiea grfdeemipl eldgevrrtd qtvrpgtsld tlaglrtafr
      241 engritagss spisdgaagv llasrdavdt hglrararil dqttvgvdpi imltgpipat
      301 qklldrngmt iddidlfein eafgsvvlaw erelkpdldr vnvnggaial ghpvgatgar
      361 liativaele rrdaeiglvt mccggglgta tliqrid
//
LOCUS       WP_010593403             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Rhodococcus].
ACCESSION   WP_010593403
VERSION     WP_010593403.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..412
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43114
     Region          10..409
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtttlsaadr nvvvvgagha aaslvgllrq eghtgritml geeldypyhr pplskkfaeg
       61 eleqwlrppe fyreqdvevr lgeqvteidr kagrivtasg erigydvlvl atgsrprplp
      121 vagaglagvg alrnlgdara lrkwvgegrk laiigggyig levaavaraa gaeavvlere
      181 drvlarvasp qlsailtarh teqgtvvrtr vgvtglegaa gqvqsvvleg getidctaal
      241 vgigalpcde laaacdlerg paggivvdef artsdpaila igdvtcrrvp gldgigrles
      301 ipsateqarq avaailgtps pqpetpwfws dqfdlklkia gvvrpgadvv rrgdpetgrf
      361 alfhlrdgvp vavesanasp dfmagkkwig agtsvdpvrl adpgialrda vr
//
LOCUS       WP_010593408             186 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aromatic-ring-hydroxylating dioxygenase subunit beta
            [Rhodococcus].
ACCESSION   WP_010593408
VERSION     WP_010593408.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..186
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=21040
     Region          26..171
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mtttapetpk aapapspqvg dlrqvtrsrv edllyleael lddwdldtwi tlytddcryv
       61 vpcndtpdad pardlvlvdd dhlrlscrve rlnsrrahre yphsatshqv snvrlrpvvd
      121 gtggaaelpv vaefvvwrfr gersytyagr yhyrlrvvdg hlriaskrcv lrmgslrqvs
      181 dvaiil
//
LOCUS       WP_010593424             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010593424
VERSION     WP_010593424.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..187
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20762
     Region          3..146
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mhaarevfee qgfhetkiad iprranvshg tfytyfdskh sifrevvnaa mgdlfqatrs
       61 glgssgspve rirtanrryf aayarnagvl raieeasfrd pyfhdllaqi ravfvdriai
      121 gvqrlqdqgl adpkldskra atilggmaeq aarhaflfge tfeedvtvdt ltrlwargig
      181 ldpdade
//
LOCUS       WP_010593432             175 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Rhodococcus].
ACCESSION   WP_010593432
VERSION     WP_010593432.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..175
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=19276
     Region          25..166
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mpletttlar stvaapdpee mrrvmgqfat gvtvvtgldd agpvgfacqs fasvsleppl
       61 ilicadhrgr awpriraagr fcvnvlredq sdlcarfgss rgrryeeldw evsrwgtptl
      121 pdvlmrvhae vhevhvagdh dviigrvlel dtvceerpmv ffrgrfgidh pvpva
//
LOCUS       WP_010593458             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thiamine pyrophosphate-dependent dehydrogenase E1
            component subunit alpha [Rhodococcus].
ACCESSION   WP_010593458
VERSION     WP_010593458.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..321
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33856
     Region          1..319
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 malnksalls ayrkmseire fedrlheena tgdipgfihl ysgqeaiavg vcenlhdtdy
       61 igsthrghgh ciakgcdldg mmaeifgknd glchgkggsm hiadlsvgml ganaivggap
      121 slaigaalsa ktlgnggvaa sftgdggsnq gtvfeamnma vvlelpivfv ienngfgeat
      181 grdyavgtps iaaraasfgm pattvdgtdf fevheaarea verarrgggp stieavahrw
      241 hghfegdaql yrtadqvael rrthdplvkf rakvdgkkvt akeldaidae arervevavt
      301 karaaeyppl tnlltdvyvs y
//
LOCUS       WP_010593490             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pentapeptide repeat-containing protein [Rhodococcus].
ACCESSION   WP_010593490
VERSION     WP_010593490.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..248
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=26920
     Region          <162..219
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 malpfaassd faidkdagrp cpnlqddfrc gihrdlrsrg ftgctvydcf gagqkvsqlt
       61 fggedwrrsp qlarqmfdvf pvvrqlhell wyldeaaalp tsgpirtdlr aaraatdrls
      121 ngdagalarl dvaahrqqin tlllhasela ratvpgrrkd rrgadlvgak lrqanlrgas
      181 lrgallvaad lreadlrrad ligadlrdad lrgadltgsl flvqsqldsa rgdgrtrlpa
      241 tvttpkhw
//
LOCUS       WP_010593498             354 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TerC family protein [Rhodococcus].
ACCESSION   WP_010593498
VERSION     WP_010593498.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..354
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=39438
     Region          4..303
                     /region_name="R_switched_Alx"
                     /note="integral membrane protein, TerC family; TIGR03718"
                     /db_xref="CDD:274743"
ORIGIN      
        1 mtvplwlwaa vlaaivamla vdlfahrrah vigvreaagw svfwvatgvg fgaliwwqyg
       61 sefgqqyfsg yliekslavd nvfvwaiilt yfavpreyqh rvlflgvlga lvfrglfiaa
      121 gsvliasfgw ilylfaafll ytgyrmirqr dehldpeksr alrlfrrhvp mtdayhgqkf
      181 lvrrggalla tpllavlvli eitdivfavd sipaifavtd epflvftana favlglramy
      241 flladlihrf vylkiglalv lvwvgikmll kidvfyiptp islavvatil tvsivaslra
      301 trgqgrrgle apttppfrva taeetaalep vwrlpgarrr aerterddsl sger
//
LOCUS       WP_010593516             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Rhodococcus].
ACCESSION   WP_010593516
VERSION     WP_010593516.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..412
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43196
     Region          2..402
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtetivvvgt gvagataaqt lrnegfagrv vligeeaalp yrrpvlskdl lagritdeka
       61 qlepagywtd hdielrtetr vveldperhr lrlwdneive ydavilatga rarhlehdag
      121 drvlslrtae nvaplraaia shrallvvga gligcevast arelgaevtv lesapsplar
      181 ivppavarmy vglhaehdvp vhtgvalrsl tgsddgvhav aedgrswtag talvavgsvp
      241 dtalaraagl tvgdgivvde ayrtsaagvy aagdvieqpd pvlggrhrte nwnsaraqgl
      301 aaaksvlgqp lgaaevpwgw snqyghnlqf agwsrhdddy vvrgsiedrd ftalalrgdr
      361 lvgaialgrp kdirivrrlv aagapidraa ladesvalgd vagrgaavpa sl
//
LOCUS       WP_010593519             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Rhodococcus].
ACCESSION   WP_010593519
VERSION     WP_010593519.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..155
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16426
     Region          6..151
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mpadliliay dgsenakrav eyagrflasc ravvvtawep mvrqaarmsg lsgvmqpewv
       61 pdeetedval tdakvinaeg ldlarsagla aegrtlevvs avwtaiveaa delnvdiivt
      121 gtrgttglrs llqssvadhv lrhshrpvli vppgr
//
LOCUS       WP_010593528             277 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein, partial [Rhodococcus sp. P14].
ACCESSION   WP_010593528
VERSION     WP_010593528.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         1..>277
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          1..>228
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mvalaldvgg tkmaaarvra dgtldpprtv ptpvhgvwaa caqllrqvaa gdevtavgia
       61 sagpvdtgag svapinidew argfdladav rglfpragvr lavdgaaaal aehrlgagrg
      121 tadlvgvvvs tgiggglvlg griaggrtgn aghighmvsg agteacacgg agcvetvasg
      181 paavrwargh gwsgadgaal ardagagdpv avaalgragt algeviasaa alvdvdlvvv
      241 gggfaqagap lwrpmraaaa rharlpflsg lrlppar
//
LOCUS       WP_010593562             408 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Rhodococcus].
ACCESSION   WP_010593562
VERSION     WP_010593562.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..408
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44421
     Region          2..406
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 myewsdtdlm frdalrgfid keirphvdrl esgelppydi irkmfatfgi delardglnk
       61 alareeagev psaksgggmg sggmaallns eiagvslglv asmgvslglt agtirsrgtl
      121 aqkkrwlpel vtfekvgawa itepdsgsda fggmkstvrr dgedyilngq ktfitngpya
      181 dvvvvyakld egdpsvdrrd rkvlafvlek gmegltqspp fkkmgmnssp tgelffdnvr
      241 ltrdrllget eeggrsdgke saresfaaer igiaylalgi ieeclrlckd yarsrtlwgr
      301 eiaqfqliql klaemeiari nvrnmvfsai eraeagkpva laeasamkly ssraatevam
      361 eavqlfggng ymaeyrveql ardakslmiy agsneiqvth iakgllsg
//
LOCUS       WP_010593570             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pyridoxamine 5'-phosphate oxidase family protein
            [Rhodococcus].
ACCESSION   WP_010593570
VERSION     WP_010593570.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..231
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23976
     Region          15..151
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 menirryper artrradlda vldaavtctf atvvdglpwv vpmlyardgd rillhgstga
       61 galrlaasga pvavcvslld gvvvaqdlfh ssanfrsavv rgevtalpae esaaaldals
      121 dglipgrste trahtrkela atatlvlpir agqwtvkird appsapdvsd gswagvvplr
      181 tvadrpvaap wvaddvpvpe svrrlvdrya tstamvsats agfsapsast a
//
LOCUS       WP_010593621             447 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Rhodococcus].
ACCESSION   WP_010593621
VERSION     WP_010593621.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..447
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46592
     Region          6..399
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mervpseteq kkklsltgsv algtgvmiga gifalvgqva elagswipwa fvagavvvaf
       61 saysyvryss tnpssggiam ilkaaygpgv vagsfslfmy vsmilaesll artfgtyllr
      121 pfgmqgsavw vpvlavvaia aatvvnlvgn rwvegsatvt aaikivgiaa lavagiaatg
      181 vsafsrlvtg gadatppdsg llgflagial cilaykgftt itnqgddlrd pqrniarsiv
      241 iaiavctvly llltvavtgs lsvpeivaar dyalaeaaep lfgswgvwlt vavavvatls
      301 glvaslfsvs rlydmlremg qvpglpgsvn rqsllitaal alvtatvfdl sqiaslgaml
      361 ylsmdiaihw gmvrrlrdev efatwvpava ialdvlvlvp fvimkvrtdl ftvvvtavva
      421 aavfasqwli vrrhvahrrr stgrsaq
//
LOCUS       WP_010593634             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PDR/VanB family oxidoreductase [Rhodococcus].
ACCESSION   WP_010593634
VERSION     WP_010593634.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..316
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34036
     Region          9..218
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(50..51,53,67..69,75,77..78,118,218)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(50,52..53)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(75,78,81,87)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(110,114..117,119)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(115..116,139..141,192..193)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          233..315
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 malidvtvae ivqesptvrs ftltktdgsp lgtyrpgahi dvvgptsitr qyslfstpda
       61 qdsfafavkr eensrggsaa lhelrvgdal rispprnlls iaadathhvl vaagigitpm
      121 lsmarymdvh gisfelhyfa rseteaaflp llrercpdkl hahlgvgrde qdeilgtifa
      181 gtdpgthvyt cgpdgfmtkv valasrhvpa gsihlenfha teqpdasens afeveleget
      241 yrvpadrsiv evlqengcdv dtscqegicg tcimqvvagt pvhrdnvltr sekesgevma
      301 vcvsraager lvldyy
//
LOCUS       WP_010593668             336 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Rhodococcus].
ACCESSION   WP_010593668
VERSION     WP_010593668.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..336
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33408
     Region          143..326
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mhrthsgrwa alilgastag ltvplltapt agathlspep vaasvadalt itgadpagqv
       61 vdparwqtva niaaagvraa rdngalddtv atlqslagca arwsaqgtga sllsvcrtel
      121 agldysiapr llaalaadpg tptapgrhgp papepgtppe eddapaagap dtapgnegat
      181 rledpgaapa sptpprpaeg grwggtgrpv aptagvitst fgdgrghggi diantmvapi
      241 vavadgevvs agpaqgyglw vrirhddgtv ttyghnnanl vkvgqrveag qkiatigdrg
      301 nstgphlhfe vedpsgaktd paqwladrgt pliaad
//
LOCUS       WP_010593699             381 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Rhodococcus].
ACCESSION   WP_010593699
VERSION     WP_010593699.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10893456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..381
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41007
     Region          5..103
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Site            71
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238089"
     Region          119..294
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(171,175,232,250,253,257..259)
                     /site_type="active"
                     /db_xref="CDD:293810"
ORIGIN      
        1 madtvtasel flelragtvp eildirsted fragriegpr pvptrhvpvy rvmeeleeqa
       61 aatrsgavvv cgqgngselv aeefetlglr trsleggtda wnrllvpvei tglpgdvriw
      121 qfqrpakacl sylvgvpggr givvdparst eaylelarkq dvsivhvvdt hvhadhvsgg
      181 palaarldae yhlppedagg ivpfpnrplk egdeldlgsa avramtmhlp ghtpgttall
      241 vsesvllvgd tvfvrglgrp dltgraeela rdlfrsvhdr lrpldprtti apahwssnee
      301 inadglvvtt leeiftatll nehalerfve qivnslpaap dtyetirrvn agqlapadde
      361 idvldvgrnq caastslkaa h
//
LOCUS       WP_010593711             170 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Rhodococcus].
ACCESSION   WP_010593711
VERSION     WP_010593711.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..170
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=18216
     Region          35..168
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mttapsthlr avvdtnreai agdptrahav fraeahghda vastvalgrf svevdeppal
       61 ggentapnpv eyylasllsc qvvtyrvwae qlgirvddis araegdldvr gffgfgdvrp
      121 gfgevrvavt lsgpeprery lelqeavdah cpvldltrnp tpvrtvveia
//
LOCUS       WP_010593752             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010593752
VERSION     WP_010593752.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22069
     Region          4..201
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 msiaatpkge rrrqalvaaa adlileggid avrhravahr aglplastty yfhslddlva
       61 savqhngrre ldvmrsrvqc vppsdrgpes tadlivdllv gpggvgeier erliaryerc
      121 vatarhpelr dvqkelraqi eqlltdllqr cgrsvhepql rrlvavvdga vlgalgdldp
      181 dpralarcil pgvlegvapp aeqea
//
LOCUS       WP_010593755             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010593755
VERSION     WP_010593755.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20944
     Region          1..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrtraallda atevflrdgy aaaateeiva vagvtrgaly hhfankrdlf rgvvermqve
       61 teetlaaieg sdpwesftaa vlasldvvyd pairrlllie apavlgwaev reghrkntim
      121 iteralraia rrsgepapqs salahmivaa veeamlylah sddpirerpe vqaqllqlle
      181 gvrrpapvqe sa
//
LOCUS       WP_010593772             294 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Rhodococcus].
ACCESSION   WP_010593772
VERSION     WP_010593772.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..294
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31799
     Region          4..292
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mttisgivay pvtpfdsrdp etidvdilhl lldrmidagv daiaplgstg esayldhnew
       61 itvatetieh tdgrvptvvg vsdlttagti rraqiaerlg atavmalpts ywrlteeevr
      121 lhfttlaesi gipvmvynnp attgidmtae flfdlvatve nitmvkestg diarmhrlne
      181 lsgntlaffn gsnplaqraf qagaagwcta apcliphriv efhraittgr edeaaelfdr
      241 lrplldmivs rglpatikag lrsvgveagt prrpllplde petarleeli aacr
//
LOCUS       WP_010593829             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Rhodococcus].
ACCESSION   WP_010593829
VERSION     WP_010593829.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..214
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22883
     Region          1..179
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mrlthfghsc llvehlgati lfdpgnfshg fegitgldai lvthqhpdha dparlpalve
       61 anpgaalyad pqtaaqlggg wqavhpgdaf tvgdvrvrgt ggrhavihpe lpvidntayl
      121 lgddenparl lhpgdslyip hervdvlalp aaapwlkiwe svdylravnp rvavpihqgi
      181 ladqatgify grysemapeg tefrvlpaed svea
//
LOCUS       WP_010593855             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MOSC domain-containing protein [Rhodococcus].
ACCESSION   WP_010593855
VERSION     WP_010593855.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..224
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24238
     Region          8..182
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mshrnpptgr veavctvhsv rasgtrrvah taidkrpvtg pvqvrrlgla gdrqcdtahh
       61 ggrhkavyay aedearrwad elgrelpagw fgenlrvsgi aasdaviger wrigalglll
      121 evtgprtpcg tfgvwaqepg wvrrfaargd tgaylkvlae gpveagdgif vvhvpehgvt
      181 vrdlftgrdp ariaemlaqq ddlspsvadk arrrvagrev qvey
//
LOCUS       WP_010593847             203 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Uma2 family endonuclease [Rhodococcus].
ACCESSION   WP_010593847
VERSION     WP_010593847.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..203
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21989
     Region          1..158
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mtgpsfpdhl ltlaewaelp eyeqfhvevc egvlsasprp gylhqhvafg lvaqladqlp
       61 kelavlgdve vlltetpltv rcpdgivvdr alvdadpdra tgtdvrlvve vmaegsvrtd
      121 rvtkfseyae aripvywmid lvepatlgvf vlddgwyrye geytgkvtlp vaghrvsvdl
      181 daltavrppq rsapvdgagr apg
//
LOCUS       WP_010593869             278 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfurtransferase [Rhodococcus].
ACCESSION   WP_010593869
VERSION     WP_010593869.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..278
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31338
     Region          14..274
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 marsdvlvsa dwaeqnlhap ntvfievded taaydgghie gaikldwrkd lqdgvrrdfl
       61 nreqfsalls akgvadddtv vlyggnnnwf aayaywyfkf yghrdvklld ggrkkweldg
      121 rplskdevtr pateykaqep dysirafrde vidaigtkni idvrspdefs grilapahlp
      181 qeqaqqrghv pgainipwst tanedgtfks dddlealyra kgfddsreti aycrigerss
      241 htwfvlqeil gknnvknydg swveygslvg apielevr
//
LOCUS       WP_010593958             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Rhodococcus].
ACCESSION   WP_010593958
VERSION     WP_010593958.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..272
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30203
     Region          1..259
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msttpklrle hvtkrfpvrg tdtaftaldd vsldvadgef lvlvgpsgcg kstlldllgg
       61 lssptsgril ldgqpisgpg ldrgivfqqy allpwrtarh niefgleakg lprrqrrera
      121 ehylelvglr gfgdryphel sggmkqrvai arslafdpev llmdepfaal daqtreslqd
      181 ellrirhetg ktilfithgi deavylgqrv avltsrpgrv eavvdididr tvddvrsgea
      241 frhyrhriws llhsdveraq nhgaaiqevh hv
//
LOCUS       WP_010594038             391 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thiolase family protein [Rhodococcus].
ACCESSION   WP_010594038
VERSION     WP_010594038.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 391)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..391
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=39945
     Region          1..391
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mtravivdav rspvgrgraq galagvhpsd llgqvlaglv arndldpgli ddvvigcvnq
       61 sgeqsatpgr qallaagfpt hvpsvtverk cgsgqqaidf avqgiaagay divvaggves
      121 msrvpmgsaa mgkdphgpav rgrfpdlvpq giaaelvaqk walsraelde ysarsheraa
      181 haraagwfdg eivpvttptg vvtadetire gttaerlagl paafgtdtrr erfpdldwkv
      241 tagnssqisd gasallimse akaaalglrp raaivasavv gddptlmltg pipatekvla
      301 raglsvadia afevneafas vplawqreig asddvlnpvg gavalghplg asgarlattl
      361 ishlertggr yglqtmceag gmanativer l
//
LOCUS       WP_010594045             296 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Rhodococcus].
ACCESSION   WP_010594045
VERSION     WP_010594045.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..296
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30646
     Region          3..296
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 msqlvidalv lgsiyllfcl gmsiswgtid ilnfahggif mfsafvasqi vsnvglglvt
       61 vclisvvvga alsaaidvfa fqpilrrakn qrtaelqili ggigigtipv aivqfrtlse
      121 pfgflgssye tsvytlgglr ltstglivlg caliltlais fwlkntshgl alraigvdse
      181 taelmgvkrr qlslltmavs gglaglagal ltynlgaita esgetllika faiiilggvg
      241 stggaalgam vlafsevlvl rytgggwvda vgfglilvvl llrpqgifgr kevrrv
//
LOCUS       WP_010594057             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HdeD family acid-resistance protein [Rhodococcus].
ACCESSION   WP_010594057
VERSION     WP_010594057.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..197
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=21131
     Region          17..193
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mavserafta ndqfsplfkq mwwlvlirgi lavlfgvval vwpgitvwal vvvfgiyaiv
       61 dgvvlvyhai rdrarldgwg wwlamglvsi aagivalvwp aatalvvlyi iafyailfgv
      121 tgiigalsfr kvpnsgwgws lvagilavll gvvllifpgs giisliwllg iyailfgvll
      181 ivvafqvrkv akeaglv
//
LOCUS       WP_010594066             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Rhodococcus].
ACCESSION   WP_010594066
VERSION     WP_010594066.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..201
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21762
     Region          82..200
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtrtvdvpad lreataelva atralmlaaa tttadadtvr aaraaiaela etlgsrprpr
       61 vlrppfdgps rsrdtggrep walfthnpmg ipleihfgad eararlvana lhegppdsvh
      121 ggfsahlldc mlgtlmqarg srsltasldl rylrrtplde pldlysrive tegrktvaeg
      181 wiecrgertv eargvfvrve t
//
LOCUS       WP_010594074             136 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Zn-ribbon domain-containing OB-fold protein
            [Rhodococcus].
ACCESSION   WP_010594074
VERSION     WP_010594074.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..136
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14962
     Region          16..129
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mtavprltit qdnefwfaaa regrleiqrc sdcgalrhpp gpacpkcrsf kwdtvessrr
       61 gtlhswtvih hpkdpsfyyp lavglidlee girivadiag vehdrlrigm elevgfaeha
      121 hgeilpqlrl pgggaa
//
LOCUS       WP_010594078             411 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acetyl-CoA C-acetyltransferase [Rhodococcus].
ACCESSION   WP_010594078
VERSION     WP_010594078.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 411)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..411
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43034
     Region          10..411
                     /region_name="PRK06205"
                     /note="acetyl-CoA C-acetyltransferase"
                     /db_xref="CDD:235741"
ORIGIN      
        1 mtttdatand vviceplrtp vgryggvfvd vpatdlaagv isellsrtgv dpesvddvif
       61 gqcypngeap aigrvvalda glpvtvpglq ldrrcgsglq avldaamrvq tgvadvviag
      121 gvesmsraey ytesmrwgak gapaalhdrl argrvtaggr nhpvpggmle taenlrrryg
      181 igrreqdela veshrravaa idsgvfaeei vpvsvpqrkg ddrvvdrdeh pradttvdtl
      241 arlrpimaaq dpeatvtagn asgqndgaaa clvttrahae rlglrplgrl vtwavagvap
      301 aemgigpvps tekalkragl tladidliel neafaaqala vtrewgftaa dfertnvngs
      361 gislghpvga tgvrilatll reldrrgary gletmciggg qgltaiferv a
//
LOCUS       WP_010594088             176 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DinB family protein [Rhodococcus].
ACCESSION   WP_010594088
VERSION     WP_010594088.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Newton,G.L., Leung,S.S., Wakabayashi,J.I., Rawat,M. and Fahey,R.C.
  TITLE     The DinB superfamily includes novel mycothiol, bacillithiol, and
            glutathione S-transferases
  JOURNAL   Biochemistry 50 (49), 10751-10760 (2011)
   PUBMED   22059487
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Cheo,D.L., Bayles,K.W. and Yasbin,R.E.
  TITLE     Cloning and characterization of DNA damage-inducible promoter
            regions from Bacillus subtilis
  JOURNAL   J Bacteriol 173 (5), 1696-1703 (1991)
   PUBMED   1847907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..176
                     /product="DinB family protein"
                     /calculated_mol_wt=19802
     Region          10..160
                     /region_name="DUF664"
                     /note="Protein of unknown function (DUF664); pfam04978"
                     /db_xref="CDD:428232"
ORIGIN      
        1 mteptgerad ildilaeqrk tflitlrdld deqartrstv seltlggllr hvatteqhwi
       61 dtirtlddta efdmesameq yfmrdddtva glleryeaia keteafvagl edldlpvplp
      121 tapwaperqw wsarkvllhi iretahhsgh adiiresldg anttrqqgad agmtfe
//
LOCUS       WP_010594112             557 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [Rhodococcus].
ACCESSION   WP_010594112
VERSION     WP_010594112.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..557
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=58625
     Region          25..557
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mstdvpalsl typdvtmavw apsmaalygd rpaivdgdrm ctyrelders aqfasalqga
       61 gvapcdvvlm hvgncieflv ayygalraga tvtlvnplqp epglrkqiee tgavaavtqt
      121 qqlgvllgaa agttvativv asgdpvsapp tsaavvrfdd flagqptaft pahvagtdva
      181 hlaytggttg iskgvrvlhr nvvanvtqmc gwraahqvva tgdglvalrp iegldvhgvi
      241 pgegatvvvs plfhahalin tsflllcglt qvlagrfdpa rmlelverhr vsyitgspam
      301 whalathpdv arrdttsvrv vssgaapidh vtlealgvaf pnarvaegyg ltegtcvvta
      361 mplvvgsayr lgsvglplfd teleiraqgd psvvlgeger gelwirgpqv tdgylghpei
      421 taqqyvdgwl dtgdiayrda dgyvyicdra kdmliykgyn vypreleeil vshpavstaa
      481 vvgreagsvg qepvafvvpv pgtqpdpael mafvaeqvlp ykkireivlv dalptsaagk
      541 vlktdlrtrl eqsaatr
//
LOCUS       WP_010594114             376 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thiolase family protein [Rhodococcus].
ACCESSION   WP_010594114
VERSION     WP_010594114.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 376)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..376
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=38576
     Region          1..376
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mrdavivdav rtpvgrrgga lseihpvnls ahvltalaer vgldpgtvdd viwgcvsqvg
       61 eqagivsrsa vlaagwpvtv pattltracg ssqqavsfaa atvlsgqndv viaggvevms
      121 rvpmgtaakn gehfptevld rfgvdgfsqg vgaemmaekw clsrtlldef slrshersaa
      181 atdagaftgq lapiagltad egirrggsve slaklktvfk edgvihagns sqisdgagal
      241 lvttseyaaa qgwtpmarih tavvaaddpv imltgpipat qkaldrsgls lddigafein
      301 eafapvplaw qaetgvddar lnpvggaiav ghplggsgai lmtrlahhmr dngiryglqs
      361 mceaggmana tilell
//
LOCUS       WP_010594121             364 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Rhodococcus].
ACCESSION   WP_010594121
VERSION     WP_010594121.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..364
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38217
     Region          1..352
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 malragivgc gkiagnhaha lqqvpgvevv accdpdlera rafaarhgia havgsvdelf
       61 glgldactvc tphpvheqiv vaaaeagihv lcekpiavdv aaadrmiaaa dragitfgvl
      121 fqrrfwpaar rikaaiedgr lgvpvlgevs vllhrpsryy sadawrgrwd tdgggvlmtq
      181 avhqidmlqw fmgepvrvgg fvgtrfhgeh ietedtasav vsfasggtat itattgaghn
      241 lgnrvtviga tgalasvlef pegregvnel wtvpgevelr spyspavdan ldvrdinagl
      301 tdfhtlqvqd faeavltgrr pavtgrdara slavvaaiye ssrtgrvvel spaptpvpsg
      361 kepr
//
LOCUS       WP_010594125             454 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Rhodococcus].
ACCESSION   WP_010594125
VERSION     WP_010594125.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48725
     Region          18..422
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(31..32,35..36,39,77,135..136,138..140,143,163,
                     166..167,170,251,254..255,258..260,263,291,295,348..349,
                     353,357,373,376..377,380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 manthaagpd grpnenarra aisgflgstl eyydffiygs aaalvfgkif fpgdgatstl
       61 lsigtlgvay iarplgavlw ghwgdkfgrr nallaclllm giatfvigcl ptyeqigiaa
      121 pvilvllrll qglsaggesp gsssltleha panrrsffts ftmsgimfgi visslvfipv
      181 aslpdealys wgwrvpfwls ivvtviavwl rrkldepevf eelqengeta alpvvemfrs
      241 hwrtvvrisl satfaminti vnvfalayav qvegferstm lwaiatanfv avlsqpvagl
      301 ladrigrkpv fvfgalgsga mvfvffhaig tgstpmvfas givligffya mpngvypayf
      361 peqfparvry tgmavslmlg llvagftpav aqmlsagdts nwtpvawmcl gfavlssiaa
      421 ltgpetyrtr tedlgerrpa svarpaqelv rsdv
//
LOCUS       WP_010594147             394 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ROK family protein [Rhodococcus].
ACCESSION   WP_010594147
VERSION     WP_010594147.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..394
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=40274
     Region          74..377
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 msrsssapat agevfalvra gaattrseig hhtglsrtav aarvaalqdl glvveteegp
       61 stggrppltl tfgagagivl vvaigrsrtq lavcdlagdl lrtedleqei gaspgelmpk
      121 vaahladlra algpgaprtv gigvslpgtv dtargcslds pmmagwdgve lqpfladlgg
      181 apvfvdndan vmvlaerlge rrkfddmlli kastglgagi vsggvlqrga vgaageight
      241 ktaaaqgvlc rcgdvgcvea iaggwalvrd lqeqgrdvth irdvvalavg gdaearrmir
      301 dsgrrigevi agavnlldpa vlvvggdmae aydvfvaglr etlyrdavsv atralqilpw
      361 shgdrsgmig casmaldqvl svravdrmva ergr
//
LOCUS       WP_010594160             795 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: xanthine dehydrogenase family protein
            molybdopterin-binding subunit [Rhodococcus].
ACCESSION   WP_010594160
VERSION     WP_010594160.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..795
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=85514
     Region          9..784
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtstvepeig qarrrkedeh lvtgrtrwtd nlvlpgmlhm ailrspfaha ritsidtsea
       61 rqrpgvvavl tgadaspeqg slpcawvitp dmkippapsl avdtvnfage avavvvarsa
      121 yeahdaleai dvdyddlpvv ldladaardg adlvhpdlgt nvsatwtfds aeagtggdve
      181 qairdaevvv ertfrqqrli pafmeprsvv vdptgpqitv wsatqvphil kimlamtlgi
      241 pehklrviap dvgggfggkl qvtpeellal lvarrlgkpv kytetrsesm vaahhgrdqi
      301 qkltlaarrd gtvvglkvel ladmgaylrl vtpgvpilga fmfngiykfg ayhfsctnvf
      361 tnkvptdayr gagrpeatfg ierimdelaa elsmdplelr aknwirheef pfdtvaglty
      421 dsgnyeaata kardlfhyde lrreqeerrr rndpvqlgig vstftemcgl apsrvlgsln
      481 ygaggwehaa irmlptgrve vvtgssshgq ghetawsqiv adrlgvpfed vevlhgdtqt
      541 sprgldtygs rslavggvav vkaaekviak arpiaahmme cseddlefae grfrvrgtek
      601 avgmsdiala vftaadlpeg iepnldseat ydpdnfsfph gthlcatevd tetgqvrirs
      661 yvcvddvghv vnplivegqv hgglaqgiaq alyeeavhde sgtllsgsfa eyllpsaadl
      721 ptfttdrtet patgnplgvk gvgesgtias tpavvnavld avrhlgvrdi empctpmrvw
      781 havesarnsa qggvr
//
LOCUS       WP_010594168             608 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 15 protein [Rhodococcus].
ACCESSION   WP_010594168
VERSION     WP_010594168.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..608
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=66634
     Region          18..594
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mtftastfer irddaavpsr iedygllgdt rtaalvsedg sldwlcvprf dadpvfgrlv
       61 ggaqagrfrl gpdgpapvvr rryrthtatl ettwdlgnar ltlreamiae vagrllpatv
      121 lvrqlsaegg svraavdfdp rfgerhrapk vrrrgpdlvc ewgslalsla cdpgtsitpg
      181 rptsihvspg hpvtvvlava hreplihltp gaawelvaed earwrtwtad iahdlpyrea
      241 vvrslltlrl ltyspsgapv aapttslper pggirnwdyr yawprdagig vaaflgagkv
      301 deargflgwl lhasrlqrpr lpvlftldgr pgpaertlag wpgfagsapv rfgndaadqh
      361 qldgygwvvd aawafvrtgr slnsetwrmv rgftdhvcer wrdpdagiwe iradaahhvh
      421 skmmawlald ralriaethr lsarrrrrwr avrdavaaev rdrgfdrlgd rytrtygsrd
      481 vdaallvlpv lgiddpdshr vrgtidairr elsaggplly ryppgqdglp ggegaflpcs
      541 fwlaqalalt grraeaeelf etllrhtgal gllpeevdpa tgaflgnypq althaavvqa
      601 alalrtvr
//
LOCUS       WP_010594182             570 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Rhodococcus].
ACCESSION   WP_010594182
VERSION     WP_010594182.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..570
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58458
     Region          69..263
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
     Region          363..540
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msfpgtaart grpaaaglla eqlrhtvvdl wrvrvvfvft flfpltwlvv igflagnatv
       61 dedsgvrvmq fvtptavvmg vlyaawptva talatareqg vlkrvrgtpl pawiylagrv
      121 ggavvfalcs vltmlivgal aydvqilwrt apatvvtiav giacfaalgl avaalspsaa
      181 vaeavsiaga valgflsglf ivgdlpgwad siaavfplkp fnealqgqfd pfasgggwdp
      241 galavmaawt laaslvavra fgwdparggt grapapavas rrdravdada pgrpstarlv
      301 lgqvgwatra aardpgwvff avalpvglya fimavlpdga aadgvppels saagmaawga
      361 avtafvnmpe avvrardrgv lkrlrgtplg pvgfmaghtv stlwialvta vlvvavgvvf
      421 fglvltwpgv flaaavvvlg tatlaacgfa laavlpsska vsavglaill plaffsdiff
      481 lgdtpgwmqt vgsafplkhf snslaaaldp sgprilwgai avmaawlvaa alvatrtfrw
      541 gpraehgaps aaplglrrrg sgyarnsarr
//
LOCUS       WP_010594187             555 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [Rhodococcus].
ACCESSION   WP_010594187
VERSION     WP_010594187.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..555
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=59683
     Region          27..548
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtsqmrpwta lypngldpep vvpfvslvda wrarvdadpd gkaiayfdgv ltaretdels
       61 dalavafaar gvrrgdrvgi ylqnipqyal tllalwklga aalvlnpmyr raelrrlvdd
      121 aeivgmvcad tavaetadtv rdssvrwivs tsdldfqsrd darvfpttdr avaapdgdlv
      181 elieqhrgrr pspveitgdd vallaytsgt tgppkgamnt hanvlavatt fgsfvgltag
      241 davfavaplf hitgavinat lalvhpttlv fanrfnaeva lealvehgvt ftigsitvfn
      301 alyetpgaea rhfasvktly sggapippat vekfeakfgk yihnaygmte tssgviavpp
      361 grrapvdpas gtlaigvplp lidarvvdad gaavepgtqg elelagpqvi sgywrkpeas
      421 astlpggrlr tgdgaiidrh gwvylvdrlk dqinvsgykv wprevedaly ehpavheaav
      481 vgqpddyqge svvayvsler dahaterelv dfvrdrlaay krprrvhive nlpktqtgki
      541 rrsdlrdrti ptpta
//
LOCUS       WP_010594190             348 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Rhodococcus].
ACCESSION   WP_010594190
VERSION     WP_010594190.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..348
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36949
     Region          25..344
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mwdpcpsdtp rpapaaatvd gvderrvvvv gydraelldi acvtttfaaa nrfgaapayr
       61 velatpggaa itcdtglvla gqrrlerlvg aldtlvvsgg fghvdvadda rfvghvrrla
      121 rdsrrvasvc tgasvlaaag lldgrratth wafaarlaar ypqvqvdplp ifvrdghvat
      181 aagvtsaldl tlafveedhg pdlarhvsra lvtylqrpgn qaqmslfttv pepedrgmrr
      241 lvdhitthlg gdlsatalaa ragmserhlt rvflhhlhet paryvrrvrl eaaavllttt
      301 slpitaiaar cgfgttetlr qaftrrygas paafraghsh aaarhtgg
//
LOCUS       WP_010594201             167 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Rhodococcus].
ACCESSION   WP_010594201
VERSION     WP_010594201.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..167
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18677
     Region          <57..161
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mttarhiqvc tvrqddplaa pllaelavey stryerplde qihtltthpa defagpdgtl
       61 lvlveddepv aggafrryda ttaelkriwt skkhrrrglg rlvleeleae aarrgyariy
      121 lttgwrqpea valylaagyt alfdpgrpae eigphpfekv lirlrtd
//
LOCUS       WP_010594222             332 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
            [Rhodococcus].
ACCESSION   WP_010594222
VERSION     WP_010594222.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..332
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=34214
     Region          3..330
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
ORIGIN      
        1 mskaavlgag swgtafakvl aeagtdvtiw arraevaeai atrhenpdyl pgvelpatvr
       61 atadhrvald gvdflvlavp sqtlranlga wrddigpdat llslakgies gtlmrmsqvi
      121 aqvtgaehdr iavlsgpnla reiadrqpaa tviacsdstr aleiqracat gyfrpytntd
      181 vigceiggac knvialacgm aagvglgdnt vasiitrgla eitrlgtalg akpatlagla
      241 gvgdlvatct splsrnrsfg erlgrggtle saqeathgqv aegvksctsv ralaasydve
      301 mpltdavhrv cyegmsvpea iglllgrrvk pe
//
LOCUS       WP_010594240             652 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 15 protein [Rhodococcus].
ACCESSION   WP_010594240
VERSION     WP_010594240.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 652)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..652
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=73106
     Region          25..638
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mahtfegsgl ssahshpphr spyppiddya flsdcettcl iarngavewm clprpdspsv
       61 fgaildrsag yfrigphdrt vpaarrylpg glilettwqt etgwivvrda lvmapwhavq
      121 ersrthtrtp tdwdaehmll rtvrcvsgtv elevscapaf dyhraparwe ytgkvyeeat
      181 ayctagepge hpelrlttdl rlgledgear artrmrkgdk afvalswsdv pcpgtyeeaa
      241 akmaetadfw rewittgrfp dhpwrsylqr saltlkglty aptgallaaa ttslpetpgg
      301 ernwdyryaw vrdstfalwg lytlgldrea daffafisda srsedgtlqp lqvmygvgge
      361 rvltesqleh lcgydgarpv rigndayhqv qhdiwgamld svylhartrr hmpqsfwpav
      421 krlvgqaeqh wrlpdrgiwe vrgepqhfts skvmcwvald rgarlarthg rpdyavrwea
      481 vadeikadil ahgvdergvf tqryghpsld asallvvllr flpaddprvr atvlaiedel
      541 tedglvlryr vdstddgltg eegtfticsf wlvsalveig everarilce rllgyasplk
      601 lyaeeidprs grhlgnfpqa fthlaqinav vhviraeeqi aagefqparr ap
//
LOCUS       WP_010594244             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sirohydrochlorin chelatase [Rhodococcus].
ACCESSION   WP_010594244
VERSION     WP_010594244.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..251
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26110
     Region          1..237
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 miplvavahg srdprsaram aaalaalrdr hpdrevrlaf ldlntpsvgq vvdavaaegh
       61 rrvvvvplll gsafharvdl pallaearvr hprldvvqad vlgaddrlvs avretigaag
      121 vsrtdpsvgv alcavgsrrr danaataait prllrgtawa wgrtcfataa aptvvdalad
      181 lraagastlv lapwmlapgl lwdravaaar aefpevvcsg tladspavgf vvderyrqsl
      241 vhagvasrrt a
//
LOCUS       WP_010594318             169 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010594318
VERSION     WP_010594318.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..169
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18419
     Region          5..131
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mlsfdrldaa llaelthnpr agivdlaakl gvarntvqsr irkleesgav tgyrpvvdlp
       61 klglplqafi gaelvqarmg hviaelerfp evlevhattg redllirmaa qsqedlllql
      121 erihaiegva httttlaltt pvayrtqpll ehltrdsghg rsvptsdrr
//
LOCUS       WP_010594447              61 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ferredoxin [Rhodococcus].
ACCESSION   WP_010594447
VERSION     WP_010594447.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 61)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..61
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=6525
     Region          1..59
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mevkvdfdrc eangvcvgia pevfdlnddd elivthpiap eqeedvrtai aqcpraalse
       61 a
//
LOCUS       WP_010594504             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase family protein [Rhodococcus].
ACCESSION   WP_010594504
VERSION     WP_010594504.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..214
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22720
     Region          9..191
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mglidielft tldlvgqapg gpdedpegfp fggwqaplld evtgaqigaa ydgtdalllg
       61 rrtydifaay wphqhsgedh diatlfnsvp kyvasrgrpd lswsgstqlg pdlagavrei
      121 rdrhehikvv gsldlvqtll reklfdrldl wvhpivlgvg kkvfdagavp tnltllappv
      181 agptgtvylr yaladgipgt gdmsapdrga grdg
//
LOCUS       WP_010594460             205 aa            linear   BCT 01-JAN-2025
DEFINITION  Zn-ribbon domain-containing OB-fold protein, partial [Rhodococcus
            sp. P14].
ACCESSION   WP_010594460
VERSION     WP_010594460.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         <1..205
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
     Region          70..182
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 dpadmrtgmr vrvrwaddrv ghirdiagfe pgeagtvtvr pedsgepvtm mitpldlhyt
       61 hsasseesyy lrglaegrli ggrtgpggkv yipprganpt dgiptreqve vsdkgivttf
      121 civnvpflgq qitppyvaay vlldgadipf lhlilecdas evrmgmrvea kwrpreewdy
      181 tlrnieyfrp tgepdaayet fehhl
//
LOCUS       WP_010594508             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor
            [Rhodococcus].
ACCESSION   WP_010594508
VERSION     WP_010594508.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..228
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24403
     Region          14..132
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
     Region          163..220
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mnpgasgpda pikvllvdde hlvrsgfril levedgitvv geaatgaeav eqaravrpdv
       61 vlmdirmpkm dgieatrqit ttpglqhvri lilttydtda yvfeglqaga sgfllkdagp
      121 aellhgirvi aageallapr itrrliaqft aqrtadkaad rrlevltdre revltlvgmg
      181 msnkeigael clspatarth vshamvklga rdraqlvvia yrtglvkp
//
LOCUS       WP_010594548             352 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Rhodococcus].
ACCESSION   WP_010594548
VERSION     WP_010594548.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..352
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35813
     Region          1..324
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfarddtqe avaevavgll arglgpdelw raladadlls lalparlggd dlgvaevaal
       61 lteigrgaap vpalatlgfg vlpvrtlata aqqdelladv gdgavltaal aeagrafpas
      121 ptatavpdge rhavtghfvg vpyaatarri lvptaagvia veptapgvtl iespssarap
      181 efsvrldsap glrlgdgaep aadvaalyrl alaavgayad gllsgatqlt aqhvstrhqf
      241 grplatfqav aqqiadvyvt srtlhvaala aawrvaqdar saaadddldv aaywiaaelp
      301 pamgvlhhlh gglgvdetyp lhrysstakd larllggasy rldlvgarcs st
//
LOCUS       WP_010594562             596 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Rhodococcus].
ACCESSION   WP_010594562
VERSION     WP_010594562.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..596
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=67066
     Region          29..385
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mleisrpeva ddtrtfdvai igggiggtal aailarngvr vvmieagghp rfaigestvp
       61 etivglrvla rrydvpelgy laghntlrrk vsaasgvkrn fgfayhrege pfaaeectqh
      121 ptwsppigpd shffrqdvda ymfqvalsyg atgltytpvt avdfdsdgat irtassgdfr
      181 agfvvdaggm rsllgeqldl ridppyrtrs rtifnhfvgv epfdrvappr kqhlmpspfs
      241 qgtlhhlfeg gwawvipfdn hvgttsqlcs vginldidvy pkrdgetpee efwahvdrfp
      301 tiqrqmraar avrpytssnr sqfaskrivg drwvllphas dfidplfssg lavtmmilna
      361 lghrlisavr eddfsverfe yvqtwtkrsf ryyddlvsfs ytswdhfdlw nawhrvwcla
      421 tmyganaqmq tvmeyektrd kavfdrleqp pyrglqavdn prfaamfdaa caamqayrdk
      481 eidateaghr ihvalkesel vpsarwtgwr aldpdnrlpt geftlwdmtr lllwgkyasp
      541 phirgtyftn gfagvakeag klylselrhg sglsmqvard mvsyrnrdwr rvggld
//
LOCUS       WP_010594563             306 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Rhodococcus].
ACCESSION   WP_010594563
VERSION     WP_010594563.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12000796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..306
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33273
     Region          16..292
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          156..>211
                     /region_name="PRK15340"
                     /note="AraC family transcriptional regulator InvF"
                     /db_xref="CDD:185240"
ORIGIN      
        1 mtddrrawwr hrslgtrrel tlstgrlayf eagagepivl lhgpltnanv wrkvvaalsg
       61 rfrcialdlp fgahsvpmpd adlsfaglaa ivtealeald lrevtlvgnd ggtpvaqlva
      121 ttrpdlvrrl vltaggaydn cpprryraim kaiayapaar elilgplrir alrrlpmsyg
      181 wlarrpvepa tsdswvlpal esdavyadlr rmlrslepsa vlaaaesfgd fpgpvlvvws
      241 redrvfppeh aerlagdfad aglewiadsc sllpedkpfe vaqlladfvq rtssvpaaai
      301 stnqes
//
LOCUS       WP_010594594             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Rhodococcus].
ACCESSION   WP_010594594
VERSION     WP_010594594.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..146
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14624
     Region          4..141
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mptrtsrtaw ngglqdgagq veltssgrat fdvsfpkraa ddadgttspe eliaaahssc
       61 yamqlsalia eaggtpqsld vtadvslgpd pnggfrltgi kltvrgevdg ldadgfakaa
      121 qgakegcpvs kaltgvditl daales
//
LOCUS       WP_010594599             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PIG-L deacetylase family protein [Rhodococcus].
ACCESSION   WP_010594599
VERSION     WP_010594599.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..262
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28502
     Region          10..229
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mnattsrlgt ilsiwahpdd etylaagima aardagrrvv casasagehg tadprswppe
       61 rlgrvrrwea aaamavlgve ehhvlglpdg altdhddagl swagrllddl rpdtiltfga
      121 dgmtyhpdhn avhrwvtraw rdrggrsrll yatptvehld rfrdlyeewg mymsderptg
      181 ipeeqlavhv rlqgpeldrk ltalramatq tgdlvaridp aiyaaqiaee afvdalrvpd
      241 hdeattgtar tgtartgtaa av
//
LOCUS       WP_010594652             476 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Rhodococcus sp. P14].
ACCESSION   WP_010594652
VERSION     WP_010594652.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         1..476
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50354
     Region          2..423
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtvsfsdlgv prtlvaslnd ngitspfpiq vdtlpdtlag rdvlgrgrtg sgktlafsip
       61 ltarlaggat raagrprglv laptrelatq iaavveplar vaglrvttif ggvsqnrqvd
      121 alrrgvdivi acpgrledlm rqkfvtldav eitvldeadh madlgflpgv trilnatpkd
      181 gqrllfsatl dngvdklvtr flrnevlhsv deahspvaam thhvfdvdna dtkkdlvrtl
      241 asgtgrrilf mrtkhqarkl arqltesgip avdlhgnlsq nardrnlaaf ssgearvlva
      301 tdvaargvhv ddvelvvhvd ppaehkaylh rsgrtarags tgdvvtvvlp eqrkdlavim
      361 rkaaikvtpv rvtaksehvl dlvgeiaphv apsakqaaap sggasrrpar rggsgataqr
      421 garqhgggaa rqhgggaarq qsssrqeqpa arqergaqpg srrrrpnrts atvarg
//
LOCUS       WP_010594702             136 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Rhodococcus].
ACCESSION   WP_010594702
VERSION     WP_010594702.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..136
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14099
     Region          10..133
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mdttgtdlps dsaflqaagl vldevsgtrv tghidlgrdh htpwgvvhgg vyttavesaa
       61 svgasaavqd rgqfavgvhn stdflrsstg ervdvvaepl qqgrvqqlwl vtvtgtesgr
      121 tlargqvrlq nvplpg
//
LOCUS       WP_010594759             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Rhodococcus].
ACCESSION   WP_010594759
VERSION     WP_010594759.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 187)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..187
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20188
     Region          50..166
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 msastlhasa vdrlrawrtd sadaeslrht mlafldaape gclrrhvpgh vtasslvlda
       61 drrhvlltlh prvgrwiqlg ghceesdetv vdaalreate esgiedltid pellsahthp
      121 itcslgrptr hldlrflvva ppgavpvrst estdlrwwpv dalppeaehd tlghllglag
      181 arvraag
//
LOCUS       WP_010594769             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GtrA family protein [Rhodococcus].
ACCESSION   WP_010594769
VERSION     WP_010594769.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..182
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20395
     Region          16..160
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 msfvdaavnr vpeplrglll rhhelikfai vggttfvvds vifytlkltv leekpvtakv
       61 iagviavics yvlnrewsfk nrggrerhhe allffavsgi gvvlsfiplw issyvfdlrv
      121 pdvsltveni adfvsayiig nllqmvfrfw cfrrfvfpee mnpdgdevpg heelaeeglg
      181 hs
//
LOCUS       WP_010594777             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Rhodococcus].
ACCESSION   WP_010594777
VERSION     WP_010594777.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13841068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..265
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28098
     Region          53..145
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
     Region          <108..205
                     /region_name="arsM"
                     /note="arsenite methyltransferase; PRK11873"
                     /db_xref="CDD:237007"
ORIGIN      
        1 msdphalpms erdsahlpgh wllarlgkrv lrpggagmtt rlladagieg sdvvelapgl
       61 grtareilas aplsytgveh detaaaltrd aigdrgrcvv adaaatglpd adadvvvgea
      121 mltmqtdaak arivaeavrt lrpggryaih elalvpdeld davkteirqg larsikvnar
      181 pltvaewrsl ltdaglrvdv vrlapmallr parfvadegv lgtlrfvrnv lrdgdarkrv
      241 lgmratftty rksiaavaiv aakpr
//
LOCUS       WP_010594787             113 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VanZ family protein [Rhodococcus].
ACCESSION   WP_010594787
VERSION     WP_010594787.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF037970.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..113
                     /product="VanZ family protein"
                     /calculated_mol_wt=11965
     Region          <30..102
                     /region_name="VanZ"
                     /note="VanZ-like family protein (function unknown)
                     [Function unknown]; cl42358"
                     /db_xref="CDD:478153"
ORIGIN      
        1 mtarfapvtl tlvvvtvllm lpgdttpsgf phadkithal mfavlayasr farippattv
       61 awlavyaalt evlqaavavr rsgsvwdwca dlagallgia lyaavrrrsr art
//
LOCUS       WP_010594807             271 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Rhodococcus].
ACCESSION   WP_010594807
VERSION     WP_010594807.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..271
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29318
     Region          8..106
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(9..11,25,43..45)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            46
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(57,60,64..65,74,85,89,95,99,102..103)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          124..260
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mspadgwlsi gefarmsrls vrtlrhydre rllapgrvdp rtgyryysre qlasalriav
       61 lrraevsvpa irlllqdpgh teavlaaere riereadrkr ralalvasla eaeagglsvr
      121 rhrvedrtvl wrsgestaes ldsdvtnlvt allteassag lptdapvvgq ypatldgvvq
      181 fgvglelrsp pgraetattt lpggafagvd fvgpvallpv ayhalfgwld erglaaegpf
      241 reyyladprd vapdamrtrv lhpvpgdhvp g
//
LOCUS       WP_010594850             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleoside deaminase [Rhodococcus].
ACCESSION   WP_010594850
VERSION     WP_010594850.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..157
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16425
     Region          23..150
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mglrddeali raaleaaaaa pagdvpvgav lfaadgtela raansreatg dptahaeila
       61 lraaakvhgd gwrlegttla vtlepctmca galvlarvhr vvfgawepkt gavgslwdvv
      121 rdrrlthrpq vrggvlekec aavledffra qrlpeps
//
LOCUS       WP_010594867             907 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation-translocating P-type ATPase [Rhodococcus].
ACCESSION   WP_010594867
VERSION     WP_010594867.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..907
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95504
     Region          26..896
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mtlattwhtr dadavaaald vdpavglstg eveerrlehg pnalveaaav pgwrkvlall
       61 adrmtlvlva aavvsavvsr ewetpvvila vitlntvlny vqerraensl qalrqmavdt
      121 arvrrdgreq hlprtelvpg dvvlleagds vpadgrvvta arlqvaesal tgeshpvdkt
      181 vepvddeqap lgdradmlfm nteitrgrga mvvtatgmqt eigaiatllg tagvektplq
      241 rridqlaktl tivaltvvav vfvlgllrgq swsdllitav slavatipeg ltavvaftla
      301 mgasrlaarg aivkrlaave tlgstthiat dktgtltlne mtvqrllarg rsfrvtgtgy
      361 etdgkilvgd glpppdltap llgmalcnda vvrdgvlvgd ptegalvvla ekggidvega
      421 rlavprlaev pfdsaykyma tfhalpdggs rcfakgapga lldratamld gdgpvplddr
      481 rrerlrsavq slaaeglrtl miagrdlhav prgdaealqr avsdltlyav vgivdpprte
      541 aeraievaha agievhmitg dhlvtasaia grlgiggaaa tgadldalnd delrsraadf
      601 gvlarvapeh kirvvkalqa ngevvamtgd gvndapaleq adigvamgit gtdvsksaad
      661 miltddnfat ivaaveegrg iyanivkfvk fqlttawgfv liflvsgalg laggapftal
      721 qilwvniimd gppalalgvd ptepgtmsrp prpaherlls rdrlrrilgl givmtagtva
      781 vlhyapqwfp esagdplfat tlafttfvff qvfnllnvrs elgsvfslqt ltnhsiwial
      841 vvvvvlqvcv vqtaflqgff dttaltsqqw alavgvgssv lwvdelvkat grslrrrrgd
      901 aharsga
//
LOCUS       WP_010594878             461 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Rhodococcus].
ACCESSION   WP_010594878
VERSION     WP_010594878.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..461
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49352
     Region          22..431
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,83,141..142,144..146,149,169,
                     172..173,176,262,265..266,269..271,274,302,306,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msveqsrpgg rapdetptsg lrkvvgasma gtvvewyeff lygtaatlvf skvffpdngn
       61 eldaiiaafv tyavgfvarp lggvvfghfg dkfgrkkllq tslvlvgvat flmgclptfg
      121 aigywapall vtlrfvqgfa vggewggavl lvaehspdrs rgfwaswpqa gvpmgnlvat
      181 vvllvltttl sdaaflswgw riafwlsavi vlvgyyirtk vtdapiflea qreaeqlkss
      241 sysvvevvkr yprgvftamg lrfaenvmyy lvvtfsityl kvvvgadtat ilwwmlaaha
      301 vhfaiipvvg rlsdtfgrrp vymvgavtag twgffafpmm dsghnalvms aiviglvfha
      361 fmyagqpaim aemfptrmry agvslgyqvt sivagslapi iatallsryg savpiavyla
      421 vasvvtiiav vaaretkgis lrdvdaadvr avdaektavp a
//
LOCUS       WP_010594880             194 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010594880
VERSION     WP_010594880.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20635
     Region          26..191
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mrarpyatts ptrlaaalle vaarigldga svrevashag vsigavqhhf ptkdemlays
       61 frslaervlt rlstvdpdid partlfaals qllpldeqrs aeahvmaaft vraatspsls
      121 rirhttlftm rtavsavlir mgtaeaetra alllaavngl aldaiaspel yppeylthal
      181 htqiqlsldg adar
//
LOCUS       WP_010594887             216 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YoaK family protein [Rhodococcus].
ACCESSION   WP_010594887
VERSION     WP_010594887.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..216
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21949
     Region          6..197
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mvgygrqlta lavalsglag fvdalgfitl ggvfvsfmsg nstrlsvgla egtwgpaalt
       61 agviglflvg vvlggvvaql sdrsrrarkt avlatvsall llgalahtag wtpvavvamt
      121 lamgaensvf qrdgevsval tymtgalvki gqrlaaamfg gprwtwlpyl glwlglvtga
      181 vggaaahrml glhalwiata aavaltlavr hlpyrp
//
LOCUS       WP_010594924             477 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [Rhodococcus].
ACCESSION   WP_010594924
VERSION     WP_010594924.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..477
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=53548
     Region          57..466
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mqkpksvvvp sgesahragv erllrsyrai padapvrlak ktsnlfrara rvnapgldvs
       61 glggvvsvdp vartadvagm ctyedlvdat lphglaplvv pqlktitlgg avtglgiest
      121 sfrnglphes vlemdiltga geivtatpdg ehadlfhgfp nsygtlgyat rlrielepvk
      181 pyvalrhlrf dsldemqsal driatervha gvpvdyldgv mfsaaesylt lgtqtdapgp
      241 vsdytgeniy yrsiqhasvn hprtdrltvr dylwrwdtdw fwcsrafgaq dprirrlwpk
      301 rllrssfywk lialdhrygv adrierrkgn lprervvqdi evpiertaef lrwfldeipi
      361 epvwlcplrl reggpvarda qrpwplyple pkrtyvnvgf wssvpavage iegaanrrie
      421 hkvaeldghk slysdsyytr aefeelyygg gdypalkkry dpesrlldlf skavhnr
//
LOCUS       WP_010594962             185 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010594962
VERSION     WP_010594962.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..185
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20097
     Region          12..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrqgegtatp eeriadavle llrrkgpkav tieavaahtg marttiyrry rdrdemltav
       61 mepiaqpspp dpdatahevl mwlaeqslrs vdggvgfggl aalvtdadpa ftglirsvlv
      121 rhrstltevv rhhisrgivr adldvetfld civgaycaer arsgdidadw nervaltllp
      181 afvqp
//
LOCUS       WP_010594969             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010594969
VERSION     WP_010594969.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..187
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20881
     Region          3..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mverivtagr evllthgyeg astnriaaaa gispgslyqy fpgkdaivae vvdrwteevq
       61 arishvftda ldaptwtesv rtnmrvllea lgenprllrv lveqlprtpd srlvafehri
      121 dallamwlrf npgrrriehp daiawmlvrt venvavgyvl dqppiepevv adqltamita
      181 ylkeild
//
LOCUS       WP_010594995             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Dps family protein [Rhodococcus].
ACCESSION   WP_010594995
VERSION     WP_010594995.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 157)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..157
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=16749
     Region          4..157
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mtgpitstln pdqqkiagda lqdtlvdmid lsliakqahw nvvgpqfrsl hlaldeivta
       61 artytdevae rltaigvspd grattvaqds gtkgfgagwt kdeqvvasit dnlsavigrl
      121 reriaatdea dpvtqdllia qtagleqthw mwqaqla
//
LOCUS       WP_010594788             131 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MmcQ/YjbR family DNA-binding protein [Rhodococcus].
ACCESSION   WP_010594788
VERSION     WP_010594788.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Singarapu,K.K., Liu,G., Xiao,R., Bertonati,C., Honig,B.,
            Montelione,G.T. and Szyperski,T.
  TITLE     NMR structure of protein yjbR from Escherichia coli reveals
            'double-wing' DNA binding motif
  JOURNAL   Proteins 67 (2), 501-504 (2007)
   PUBMED   17266124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10515191
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..131
                     /product="MmcQ/YjbR family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14401
     Region          22..115
                     /region_name="YjbR"
                     /note="pfam04237"
                     /db_xref="CDD:461233"
ORIGIN      
        1 mphpvmfdea dplltrirgl altfpgaaek ishgrpffyt rtafavyggs vkatgvqfpr
       61 slivkpdaae reallgqpht ydpaylgpsg wigfdlerad vdwdeiaell dmsfrvtapa
      121 rlvrewdgrv g
//
LOCUS       WP_010594999             248 aa            linear   BCT 01-JAN-2025
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Rhodococcus sp. P14].
ACCESSION   WP_010594999
VERSION     WP_010594999.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         1..248
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26575
     Region          21..224
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mdrasypkll radterlgap gegrldrpvp tcprwsverl lghvgrvhrn aaawlrtgrr
       61 teippapaga avlpwvrdgl eelteavqsa dphadeqtfa gpqpasfwvr rmavetalhr
      121 tdaelatgeg ttpvdtalav egidelfgvl lpfralagtg sagspswsgk tmhlhatdpa
      181 laagegewsi tfdadepsvv hthaegdvav cgpasdllll lwnrasldrf evfgdaallt
      241 rwrdevti
//
LOCUS       WP_010595004             317 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metallophosphoesterase [Rhodococcus].
ACCESSION   WP_010595004
VERSION     WP_010595004.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..317
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=34259
     Region          24..297
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mpdvptlrra aigaagaavl glgyatlver nafalrevtl pvlapdastl rvlhlsdihm
       61 tpgqrlkqnw lreldrlepd lvintgdnla hpkavpavvq alggllarpg lfvfgsndyf
      121 gprvknplky fdrnhervhg aplpwsdlra afsergwldv thvrreleia gvrisaagvd
      181 dphidrdryd tvagpanpaa dlrlglthsp eprvldrfad dgydlvmagh thggqlclpl
      241 vgalvtncgl drsrvkgpsr wgshmrlhvs agigtsptap arfwcrpeat lltlvpapre
      301 qarstadagt rstfspr
//
LOCUS       WP_010595115             309 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: 1-phosphofructokinase family hexose kinase
            [Rhodococcus].
ACCESSION   WP_010595115
VERSION     WP_010595115.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..309
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32120
     Region          4..302
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mpdivtvtmn paldmttyte qvrptsklrc eaprleaggg ginvakvagv lgvsaaavyp
       61 aggptgdmls allsgggvds rrididgmtr esftaierst gqeyrfvlpg pelsvrdqer
      121 cldmlvetat garyvvasgs lppgvpgefv qrvadaatda garfvldssg dalrriksgv
      181 hlvkpslrel rewvgrelrt pheqaaaahe lvdagiaevv vvslgpdgal lvsadttarv
      241 kaldvpvrsa vgagdsmvag lvvgllrgrs lrdamalgia agsaalltpg sqvcrredve
      301 rfdvlarer
//
LOCUS       WP_010595137             406 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: patatin-like phospholipase family protein
            [Rhodococcus].
ACCESSION   WP_010595137
VERSION     WP_010595137.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..406
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42894
     Region          9..312
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 magrgtsgth grrrtalvva gagargayqa gaittllprm trhhgapril vgtsagainv
       61 vglaafadeg lptaaerlvd lwtgvvssdv yssvhsvlgt gaaflgqaig fprtrlvsll
      121 dttpirgtlq rlvpwdrlhe niraglvdav avattsvatg gtvvfvekna svplpeydir
      181 rnisyvettl tvdhllassa vpilfrpihv tdrcapqrsg wyidggllln tpikpalvlg
      241 andvgvvatq prmwpppvsa rtgrrrpapp dvagvaalal ramlgyrmie dlhtlefrna
      301 riaqtravsp tdrpigidfa gpppgqagri aeiaegvvrr rpavrrflrn papsvvarli
      361 ggddedrgdl lsfllfdpef tcaiaelgre hgaepstaqp aaelra
//
LOCUS       WP_010595153             452 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Rhodococcus].
ACCESSION   WP_010595153
VERSION     WP_010595153.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..452
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46779
     Region          22..432
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mgsstsslen htatstpagp rtrsrkypwl vfaltfglll sdymsrqvls avfpflkaew
       61 altdsqlasl tsivalmvgl ltlplsllad rwgrvkslvl mavlwsvatl mcavatnfeq
      121 mlgarflvgv geaaygsvgi avvlsvfapr vhaslsgafm aggsfgsvlg valggviavh
      181 lswrwsfaam avfglilval fralvterrl aahaaddrpa avderpagaa ttppdgfrap
      241 vsslftnpav lcayaggglq mftaavllsw tpsffnryyg lapdkagvaa sivvllvgsg
      301 mvvcgivtdr vgrhditrkw ttaiafcais laclalafrl dtgtaqlvll gigaffsags
      361 sgptaamvan lthssvrasa mgtltvannl lglalgpfvv giladrlglr ealqlsplvy
      421 vlaigalvag krlyplglrk fttlgtgpgt aa
//
LOCUS       WP_010595167             576 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endolytic transglycosylase MltG [Rhodococcus].
ACCESSION   WP_010595167
VERSION     WP_010595167.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..576
                     /product="endolytic transglycosylase MltG"
                     /EC_number="4.2.2.-"
                     /GO_function="GO:0008932 - lytic endotransglycosylase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=61957
     Region          220..568
                     /region_name="MltG"
                     /note="Endolytic transglycosylase MltG, terminates
                     peptidoglycan polymerization [Cell wall/membrane/envelope
                     biogenesis]; COG1559"
                     /db_xref="CDD:441167"
ORIGIN      
        1 msrhgrpdde stganhvsgd rpgfepaqqd ewyrprhgte asqppphpag ghpyddaptt
       61 ehvyrldeyd pgapsqperr pygghpadep gsetqvfear tyetqgyepr dydprdhdgy
      121 dpapgayrhd dyeqrpayde sgydqfgyaa adddprghte tsaagrdwtd sadraapepv
      181 gmsparraha rsargrrtrg rivgmlavaa vlvlllgggf fayqkftgpd lppdytgagg
      241 pavvvqvhpg dtaeqigaaf keadivassd afynaavqnp gmnslqpgfy siasklpare
      301 avaalvdpan rvgalviseg rqlhdirdvn tgavrkgiyt liaeascler dgqrtcltye
      361 eldaagastd laalgvpewa raavanvpdr srqlegliaa grwdfdpgag aadilrylvs
      421 tsaerydetg itqaaakvgl tpyemlvaas lverealpdd fskvarviln rleigqplqf
      481 dstvnyalde telattdadr aqvtpwntya spglpatpis spsiealqav enpeagnwty
      541 fvtidaqgtt lfadnydehl tntqqalesg ildsgr
//
LOCUS       WP_010595198             221 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HEAT repeat domain-containing protein [Rhodococcus].
ACCESSION   WP_010595198
VERSION     WP_010595198.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..221
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23225
     Region          11..125
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mntasygepd arlvdaltgd dpatrlraal eagtvaderl ttilvdrcgv epdffvrdml
       61 twalcrlpad vtvprlleel dsgtaqarsq alhtlskigd rkawpavstm lhdgdddvar
      121 sawraavalv pagsegrlaa algialgrgd hdlqlslsra lamldeaavp vleaatassd
      181 pgirahaeat erlrldpdsg ftlslelakr vaatapdrag r
//
LOCUS       WP_010595211             469 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Rhodococcus].
ACCESSION   WP_010595211
VERSION     WP_010595211.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..469
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49530
     Region          2..450
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 msnsaepglr htlqkrhlsm iaiagvigag lfvgsgaair etgpgvlvay alagvvvvlv
       61 mrmlgemaaa npqtgsfsay adraigrwag fsigwlyawf wiivlgieat agavimnrwm
      121 pgvpqwtwal almivltltn iasvksfgef efwfaaikvt aivaflvlgv laicgllpgv
      181 dapgmsnltg hggffpngtg avlagvlvvv fsffgaeiat iaagesanpa eavrkavrsv
      241 vwrilifyig siavvvtllp wddasvalsp yvavidsygi paaatimdvi vltsvlscln
      301 sglytasrmi fslsrrgdap psmarigrsg vprnavlvst vvgfltvgln ylypetvflf
      361 lvnssgaial fvwlviaasq lrmrrsleaq grelspkmwl fpyltwvtia aivalcvgmv
      421 alestrsqml tssalaavvv gvgiyrqrrr papsveandd vavrvpett
//
LOCUS       WP_010595266             275 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: inositol monophosphatase family protein
            [Rhodococcus].
ACCESSION   WP_010595266
VERSION     WP_010595266.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..275
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28418
     Region          8..263
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mttpadlssl lavagevldv aserfvagrg aprsvdkgpn dfatdldlel ersisseler
       61 rtgisvhgee fggpeadsgt vwlldpidgt vnysaglpta gillalvrdg dpvlgltwlp
      121 fvgdrfaata ggpllrngrp qpplqpaalg evmvgvgsfd idsrgripgr rrldvitels
      181 rrvsrlrmhg stgvdlayta agvlgaavvf ghhpwdnaag valvraaggr atdfagepwr
      241 igsgsvvaga pgvheeildi vgslagpvpe edrit
//
LOCUS       WP_010595316             172 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: 2'-5' RNA ligase family protein [Rhodococcus].
ACCESSION   WP_010595316
VERSION     WP_010595316.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..172
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=18712
     Region          1..>136
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 mvqsvellld drldqavree warlldvglv sqarnrsesn rphitlavaa sippgvegam
       61 reritgeplp vrlggmvlfg srtatvarlv vptaellelq rvvfelidgc pgvpphirpg
      121 ewtphvtlar rvppgrlgsa ltatragtre ltgvsagirr wdgearrewr vv
//
LOCUS       WP_010595399             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Rhodococcus].
ACCESSION   WP_010595399
VERSION     WP_010595399.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..272
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29279
     Region          24..251
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mnetttfplp ghagtlaarc wvhdhpryvv llchgygeha gryeyvatrl vadgavvyav
       61 dhtghglseg ervliedfer vvddfrllda tarsdhpglp vvlvghsmgg miaaryaqry
      121 gselaavvls gpvlgrwpal eamlaaeqip dapidpatls rdpevgrayv ddplvwhgpf
      181 krptvealqh cldtitaagt vgdvpvlwlh geddglvplg gsregwatfa gpqstskvyp
      241 garheifnet nrdevlddvv dfvhsriaag gr
//
LOCUS       WP_010594246             314 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfate adenylyltransferase subunit CysD
            [Rhodococcus].
ACCESSION   WP_010594246
VERSION     WP_010594246.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Mougous,J.D., Lee,D.H., Hubbard,S.C., Schelle,M.W., Vocadlo,D.J.,
            Berger,J.M. and Bertozzi,C.R.
  TITLE     Molecular basis for G protein control of the prokaryotic ATP
            sulfurylase
  JOURNAL   Mol Cell 21 (1), 109-122 (2006)
   PUBMED   16387658
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Snoeck,C., Verreth,C., Hernandez-Lucas,I., Martinez-Romero,E. and
            Vanderleyden,J.
  TITLE     Identification of a third sulfate activation system in
            Sinorhizobium sp. strain BR816: the CysDN sulfate activation
            complex
  JOURNAL   Appl Environ Microbiol 69 (4), 2006-2014 (2003)
   PUBMED   12676676
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Malo,M.S. and Loughlin,R.E.
  TITLE     Promoter elements and regulation of expression of the cysD gene of
            Escherichia coli K-12
  JOURNAL   Gene 87 (1), 127-131 (1990)
   PUBMED   2185135
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Leyh,T.S., Taylor,J.C. and Markham,G.D.
  TITLE     The sulfate activation locus of Escherichia coli K12: cloning,
            genetic, and enzymatic characterization
  JOURNAL   J Biol Chem 263 (5), 2409-2416 (1988)
   PUBMED   2828368
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     gene            1..314
                     /gene="cysD"
     Protein         1..314
                     /product="sulfate adenylyltransferase subunit CysD"
                     /EC_number="2.7.7.4"
                     /GO_component="GO:0009336 - sulfate adenylyltransferase
                     complex (ATP) [Evidence IEA]"
                     /GO_function="GO:0004781 - sulfate adenylyltransferase
                     (ATP) activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0070814 - hydrogen sulfide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=35596
     Region          18..314
                     /region_name="PRK05253"
                     /note="sulfate adenylyltransferase subunit CysD"
                     /db_xref="CDD:235375"
ORIGIN      
        1 mtlidtkfte srntsdgtrf dtldalesea ihvfrevage ferpvilfsg gkdstvllhl
       61 alkafwpapl pfallhvdtg hnlpevlefr dhvvekyglr lhvakvedyl adgrlterpd
      121 girnplqtvp lldaiadnrf davfgggrrd eersrakeri fslrnafgqw dpkrqrpelw
      181 nlyngrhapg ehvrvfplsn fteldiwryi aredielasi yyahqrpvyr rdgmwmtpgv
      241 wggpaegeel evrsvryrtv gdgsttgail seaadneail devaasrlte rgatrgddrv
      301 seaamedrkr egyf
//
LOCUS       WP_010595422             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Rhodococcus].
ACCESSION   WP_010595422
VERSION     WP_010595422.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 197)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..197
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21450
     Region          69..174
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
ORIGIN      
        1 mspaeranrn rrtsrrrgag aksggrstsd tskphlrtvr etsagglvvd glggppeklc
       61 aaligrtdrr grllwslpkg hiekgetaeq tamrevheet gihgtvlatl gsidywfvte
      121 grrvhktvhh yllryldgel sdadvevtev awvplpelrs rlayaderrl advadqliae
      181 mdpsmllgpg gpearlg
//
LOCUS       WP_010595445             315 aa            linear   BCT 01-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase, partial [Rhodococcus sp. P14].
ACCESSION   WP_010595445
VERSION     WP_010595445.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         <1..315
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
     Region          14..222
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(57..58,60,74..76,82,84..85,124,221)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(57,59..60)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(82,85,88,94)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(116,120..123,125)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(121..122,145..147,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          234..315
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 gaadadrqvd llvaerapvt adgdvvrltl rapdgaelpa whpgahldfh lpsgrrrqys
       61 lcgdhedrgr ytvavrripg ggggslemha lepgdlvavr gprngfpfva egpalfvagg
      121 igitpvlama raahragmdw rlvytgrtrs ampfldeigt wdpsrvfvrp ddefgtptga
      181 ellagapagg avyccgptpm ldavragida tpasalhfer fgappvvagr pfevqlastg
      241 evldvpades aleiirrrlp gigyscrqgf cgtcrvrvls gtpdhrenrl tpeerreeml
      301 vcvsradggr lvldl
//
LOCUS       WP_010595483             183 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010595483
VERSION     WP_010595483.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..183
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19623
     Region          1..182
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mtdkraavld aaiellgreg lrglthrgvd aaagvpagst snyfrtrral legvldrlve
       61 rdrsdiavlg ggnlprtede lvdvlagyvm fatgpdalrt rarfalfvea saspalrrsv
      121 qrrrdelqgt gltvlaalgs adpvggarml adhldgmilh rltsedadsd predlrrlvr
      181 alr
//
LOCUS       WP_010595491              97 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [Rhodococcus].
ACCESSION   WP_010595491
VERSION     WP_010595491.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..97
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9810
     Region          4..94
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mtelrvvati pakpgsedav rgalvalaaa srdedgcvsy elfesgsapg tfvtvevwsg
       61 qealdahmts rhvtsalatv gehlaaapvi hpltava
//
LOCUS       WP_010595536             511 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: multicopper oxidase family protein [Rhodococcus].
ACCESSION   WP_010595536
VERSION     WP_010595536.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..511
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=54722
     Region          59..494
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mcrparrssi dlvkrvllql sgalvavivv ltaiagglva hawnsavvdt tgrvtfdral
       61 ripplatsti apdgvrvfdl tmqrgttdlg hgpgtrtwgv ngsylgptlr agrgeqvrvn
      121 vtneldeast lhwhgmhlpa avdggphqpi apgatwspqw tvdqpaatlw yhphphgtta
      181 dhvyrgiagl fllddpaggp plpdrygidd iplvvqdkrf drdqlatdga mfaavgllgd
      241 eivvngtprp yldvtaerir lrllnasnar vynfsfdtgl pfllvgtdgg pltnpapmrr
      301 iqlspgerae ivvalpagat tvlrstppdl gadfwqtrfs ggddefdile lraartltps
      361 tqvqgepvth edpgppavtr hldltgsgti dgretdmsri dqtvaagate vwevrnssgt
      421 ihnfhvhgts frvlgdghpa lsgpkdtvyi apgrtvrllm rftghpdpaa pymyhchllr
      481 heddgmmgqf vvvdpgagpp peppahtavh e
//
LOCUS       WP_010595633             342 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Rhodococcus].
ACCESSION   WP_010595633
VERSION     WP_010595633.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..342
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35951
     Region          25..342
                     /region_name="CeuB"
                     /note="ABC-type enterochelin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4606"
                     /db_xref="CDD:443656"
ORIGIN      
        1 msapvttgra gdrtpraaag pavrlrpvll gavllavaaf aslfvgvadv tpadllrgdt
       61 atlevffvsr vprliailla gaalsvsgli mqhltrnrfv apdtagtvew allgilvatl
      121 flggqsvlgk mlvavafslv gtflflrllr rvrftdmivv plvglmfggv vmavttffay
      181 rlelmqalnt wtsgdfsgil rgryeiiwvv vavmavayly adrftvaglg egfaknlgvp
      241 yqlvinigmv vvavttavvt vvvgaipflg lvvpnlvtma lgdnlrrvlp italagagfv
      301 lacdvvgrvi rypyeipvgt vasvvgavvf ialilrtrrg ar
//
LOCUS       WP_010595694             246 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein, partial [Rhodococcus sp.
            P14].
ACCESSION   WP_010595694
VERSION     WP_010595694.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         1..>246
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          4..>246
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mavdlsypeh vqalvaktee fvrehvlpve dahngditaa ggddlrvklq qaakeagvfa
       61 phapveyggh glgmvdrapv feaagyslfg pialniaapd egnvhmlahi asaeqkeqfl
      121 aplahgdvrs gfamtepapg agsdpnaltt raekapggwk ingrkyfitg adgagffiim
      181 artsgepgqr ggatmflapa dtpgltvgrh idtidramig ghcevffedl fvpdsavlge
      241 vdqgfa
//
LOCUS       WP_010595702             169 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010595702
VERSION     WP_010595702.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..169
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18309
     Region          5..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mrdtvqldel dfalletlht dpkigalels rrlrvaratv sarvrrlees gviagyeprl
       61 nlaaagfevq afvtmeivqg aleaitdvle aipgvleafa ttgagdilcr iaadshlglq
      121 qtlielnrss ivarstsvmv lsevvryram pllrtlqpgr takapayrr
//
LOCUS       WP_010595704             469 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Rhodococcus].
ACCESSION   WP_010595704
VERSION     WP_010595704.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..469
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48442
     Region          21..465
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtdtlatppa ttaapapram lhqamrprql vmmslggaig aglfvgsgag iavagpailv
       61 sflaaaalvv limrmmgema aanpasgafs vhaenalgsv agrtigwlyw iqvviviaae
      121 atgaaaitaa sipgipqwaa alffmvvltg vnlvgvrrfg evefwfaalk ivaivaflai
      181 gvamiagwvp afdstgfanl tahggfaptg iagiaaglli vvfafggtei iaiaaaetsd
      241 prrnvgravr tliwrilvfy igsvlimvtv lpwtsedlvt gpfvavlnag svpgaaavmt
      301 vivvvallss lnamlfsasr miyslsqrgs aypvfgrvaa ngvprnavla svafgfvtva
      361 lnyvrpdkvl plllnavgst ilvlwtfvav shlvlrkrar regtedalpl kmwgfpylsy
      421 atlgllagia vlalfdsaar tqlvatgalt atiagacwll hrrqavrqp
//
LOCUS       WP_010595708             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010595708
VERSION     WP_010595708.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22054
     Region          18..64
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          83..196
                     /region_name="TetR_C_24"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17932"
                     /db_xref="CDD:465574"
ORIGIN      
        1 mstsrdavis gskaaarlre aavevfaeng yggtttrqia arldmspaam yphykskeel
       61 lyaisyeghd lalevvrtad lpdedattrl stviarfaew qaehhrrarv vqyeltaltp
      121 ehyrvitglr rrttqvvrti vdagvasgef tvpdtegvtl almslcvdic rwypsgryne
      181 phaianlysd lalrlvgavr
//
LOCUS       WP_010595756             278 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Rhodococcus].
ACCESSION   WP_010595756
VERSION     WP_010595756.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..278
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29758
     Region          25..261
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mqrtetsfts adgtrvvydv wspdgdpagv lvlchgfgeh arrydhvver lgelglvvya
       61 ldhrghgrsg grrvfvrdmd qftgdvhrlv giaafdqpgl prvllghsmg gaialayale
      121 hpdeltalal sgpavdvtsg tprpvvalgk vigrvlpqlp vqkldsagis rdpdvvaaye
      181 adplvhhglv pagiaralvt tgeslparlp aldlpillqh gtedrltaps gsrlvadlvg
      241 sqdvtlklye glyhevfnep ekkqvlddlv ewlrprlg
//
LOCUS       WP_010595783             226 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Rhodococcus].
ACCESSION   WP_010595783
VERSION     WP_010595783.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..226
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23867
     Region          24..225
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mvdqvtaall aaipadagap tdglagwals lmdrlggvga giaialenff pplpsevilp
       61 lagfaaslgs ftlfgalfwt tlgslvgalg lyaagrgigp drirrivdrl plvdvadldr
      121 ttawferhgg kavffgrmvp lfrslisipa gvtrmpawrf vlfttagsli wnsifvfagy
      181 glganwsrve pyasvfqnvv iggvvlfagy avvkrvrkrr aqtdan
//
LOCUS       WP_010595811             513 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carboxylesterase/lipase family protein [Rhodococcus].
ACCESSION   WP_010595811
VERSION     WP_010595811.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..513
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=55816
     Region          3..509
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mdaetlivgc kygdvrgyrd gsvytwkgvp yaapasgdlr frapeppepw tdvldarrfg
       61 piapqgrnnp ipidpgltig edclslniwa pepdgeprpv mvwihggayv lgysgqriyd
      121 grllaergdv vvvtvnyrlg algfldfssf stagttfesn vglrdqiaal ewvrdcisaf
      181 ggdpdrvtvf gessgggslt tlmtvpraeg lfhraiaqsp patsaygser aarvaeryle
      241 ildltparvw alrdmpheal tdagdvlvge iptkfpgtla mapvvdrdlv pkypvaafqk
      301 glahriplii gsnkdepsif rfmksplmpv sdasvqamld alaedhpelp pdriaeiisa
      361 ypdvtktsga malsrdagfr mpvvwiadah sahsptwvyr fdhatpmlka arigaghate
      421 lpyvfgnfgt ldrdptfwlg grkaattisg riqrrwlafa hhgvpaaldg srhwapydtd
      481 krmtllidnt dtlvpdpdki lrevwgdqvm gfs
//
LOCUS       WP_010595825             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: maleylpyruvate isomerase family mycothiol-dependent
            enzyme [Rhodococcus].
ACCESSION   WP_010595825
VERSION     WP_010595825.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..290
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31002
     Region          30..260
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mthgntpapg stapdtketp efpvepirtl lleqfdaidg lladvhgdtw ytptslpgwt
       61 vkditahlig tesmlagvet phvaidvhal ghvrneigaf nerwieslrg tpgdevlary
      121 reivarrreq laamtqadfe apattpvgqa tygrfmriri fdcwmheldl rdalgvpgde
      181 ggaraelasa eifgalafav gklgkapags ritfelsgpl artvhvevdg raavvpalsg
      241 patstvamds rlfvrlaggr vhafehldei alggdttvgr rivdnlafvi
//
LOCUS       WP_010595833             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [Rhodococcus].
ACCESSION   WP_010595833
VERSION     WP_010595833.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..207
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22508
     Region          24..185
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtehpateps gteqprtgtd rtykvgyfvg slsstsinri laktlirlap sdldfveipi
       61 rdlplyspdy danyppegaa lkdaigavda vlfvspeynr sipgalknai dwasrpwgqn
      121 sfdhipaavi gasigaigta vgqqslravl sfcnarqmts peayihytpe vfgddgsvhn
      181 agtedflrny mrefrdhvvr vltvlpr
//
LOCUS       WP_010595927             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Rhodococcus].
ACCESSION   WP_010595927
VERSION     WP_010595927.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..247
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26098
     Region          24..231
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mvmtqvgsrp ertadsdivr vqpdsgmskt lhhgleilel laahprgltv seiadgigvh
       61 rtvahrlirt leahrlcrrd drkrislgtg lvtladsveq dlrtlarpil eeladtveat
      121 ahlvvreses dvrammvvep rrsrmhiafr pgqvdpidrg saglailasm pptdgerpev
      181 gaarhlgyal sqgeiipaai gisaavpsrp ggtqaavgis vfeltageeq laaavmaaag
      241 algnllh
//
LOCUS       WP_010595963             406 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Rhodococcus].
ACCESSION   WP_010595963
VERSION     WP_010595963.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..406
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41399
     Region          20..399
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(30..31,34..35,38,70,125..126,128..130,133,153,
                     156..157,160,235,238..239,242..244,247,271,275,326..327,
                     331,335,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtvltdlrgq tfaafrganf rrylsgqais ligtwmqtva qswlvleltg sgtaiglvla
       61 lqtvpmlllg pyggvvadrv dkrrlmiglq samgvqalvl glltvtgavq lwhvyvlavv
      121 lglnqcfenp arqsfmlelv gpedlrnavs lqsvlasvar ligpavagli iavgglgvcf
      181 llnalsfvav vaslasldls llrpsppaar argqlregfa hvrqtpalav plltmalvgc
      241 layefqvvlp vvarqtfgag aetygfltaa mgagavvggl avatwgrtgt tavvvtsavf
      301 gvvllaaaaa ptlelmlaam vlvgvlsvaf tattnsslql aaapgmrgrv malfavaflg
      361 stavggpvag wvseqwggra glllgaaacl vaagigatrl grddpr
//
LOCUS       WP_010595983             215 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010595983
VERSION     WP_010595983.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23522
     Region          29..75
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          95..207
                     /region_name="TetR_C_24"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17932"
                     /db_xref="CDD:465574"
ORIGIN      
        1 mgtstdgtva dgvagpdwrr lepmeltpil saaldafyet gfhgtsvrei arrvgvtvpa
       61 lyyhhenkeg lliallelst sdvmarayaa dadggddpvq rlanaveaiv lrmtnrprla
      121 alegevryls penrqryrav rkeieklvle ivedgtrrgv fdvedpaett rallgmcqsi
      181 prwyhregsl tpeevarkyv aialktvgat pasts
//
LOCUS       WP_010595985             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADPH:quinone oxidoreductase family protein
            [Rhodococcus].
ACCESSION   WP_010595985
VERSION     WP_010595985.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..322
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33273
     Region          1..318
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(39..40,120,124,145,148..150,169..170,174,211,
                     233..234,236..237,258..260,310,312,314)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mqavqlidrt gpegvrlvdv pepdphgsvl vdlhaagvsf pdllqttagy qvvrplpcvl
       61 gvegagvvrs apadsgltpg rrvavlaaag awqqtvavtp esvfplpdsv sltagagflm
      121 nyltvhfald eraryragdt vlvhgaaggv gvaalhvaaa lgletvavvs taekaavaka
      181 nrathtvlad gfkdrvlelt ggrgvdivld pvggdrftds lrslapngrl vvlgftggei
      241 ptvkvnrlll nnisvlgagw geyvrtfpgy tarqwaqlep llrsgalqvp eptvhpmaha
      301 atalrsladr tatgkvalnl rp
//
LOCUS       WP_010596006             784 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: arylsulfatase [Rhodococcus].
ACCESSION   WP_010596006
VERSION     WP_010596006.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..784
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=86160
     Region          31..548
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(41..42,79,137,139,232,356..357,417)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(41..42,79,137,139,232,357,417)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 marthhgkia vdirdsvpdw apylpaqape napnvliiaw ddvgygsmdi fggpietptm
       61 rriadrgvky snfhttalcs ptraslltgr nattngmati aelssgfpgi sthipfengf
      121 vsevlaergw ntycvgkwhl tpgeemnmsa vksrwplgrg ferfygflgg essswypdlv
      181 ydnhpidapg tpedgyhlsk dladkaigfi rdaktidpdk pffmylapqa ghaphhvfte
      241 wadrykgrfd qgyeairvei lqrqkdlgll pentelspin phgepattgp dgqpwplldt
      301 vrpwdsltad eqrlfvrmae vfagyisytd dqlgrvidml dasgeldntl vvvvsdngas
      361 geggpngsfn ewrffngipd ttettlphld elgtpvsynh yntgwawafd tpfpywkrwa
      421 gyeggvadmc vvswpariea saeprsqyvh avdvvptiye llgitppavl kgytqspleg
      481 esfaasltdp tapgkdvqfy tmlgqrslyh egwlvcsvhp plsgwghfdk dvwelyhlae
      541 draqlhnlad aeperlealk slwfyyagrh hglplddrsa leqvlaerph pgkkrdhyvy
      601 ypdcadvpea agvaitgrsy tivagvhvds aaaegvlyah gglagghsly vkdgrlryaf
      661 nwvgthlqtv vadrdltlga hvctaefavs gkntdpampg fagtltlyvd dqqvasdeiv
      721 tqpgafclvg dgicvgrdsa spvtpdyvsp frftggtidk vvvdvsgery vdheaqvraw
      781 fsid
//
LOCUS       WP_010596018             210 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Rhodococcus].
ACCESSION   WP_010596018
VERSION     WP_010596018.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19424215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..210
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22875
     Region          4..>67
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
     Region          37..142
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mpehlqdeel wderyrsrpa lwsgepnrhl vgevaglspg laldvgcgeg adaiwlaqrg
       61 wrvdgvdvsg valqraaeha dragaevagr iswlhenlta wdpgrgrydl vsaqymhlps
      121 perdvlfrrl geavapggtl livghhpsdl qttvprpprp elfftgadvv alldpdgwdv
      181 vtdaavarev tdpdgrvvtv hdtvvrarrr
//
LOCUS       WP_010596024             438 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Rhodococcus].
ACCESSION   WP_010596024
VERSION     WP_010596024.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..438
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45939
     Region          46..419
                     /region_name="MFS_MdtG_SLC18_like"
                     /note="bacterial MdtG-like and eukaryotic solute carrier
                     18 (SLC18) family of the Major Facilitator Superfamily of
                     transporters; cd17325"
                     /db_xref="CDD:340883"
     Site            order(78,128..129,131..133,136,156,159..160,163,254,
                     257..258,261..263,266,293,297,346..347,351,355,371,
                     374..375,378..379,382)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340883"
ORIGIN      
        1 mntstpptap pdkqiglglr rnlaqftllv vvnalvggml gqertvlpll aeeefgiray
       61 taglsfilvf glskaitnyf agtfsdrygr kpvlvagwlv alpvpllliw apswgwvifa
      121 nvllgisqgl twsttvvmki dlvgparrgf amglneaagy aavaatalat gylaeayglr
      181 papfllgiaf aalglglstl avketreyar leavghvara dgrhdhlhdk ltdrqvlvqt
      241 sfkepalssa sqaglvnnln dglawglfpi lfaaaglsvg rigilaalyp avwgvgqlvt
      301 galsdrwgrk wmivagmwlq alalaviavs dsflpwaiaa aalgagtalv yptllasigd
      361 vahpawrara vgvyrlwrdg gfaagallag vvadafgiha avwvvaalta lsglvvavrm
      421 yethprptra pqegptrg
//
LOCUS       WP_010596063             370 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Rhodococcus].
ACCESSION   WP_010596063
VERSION     WP_010596063.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..370
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38662
     Region          1..338
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfnfseeqe airglahevf tgkagidrvk qvelgdervd relwrelatt gllgvalpee
       61 lgggglglse lyvlleqqgr hvapvpiwqs vlaalavvef gtdaqrtalv pgvadgsrfl
      121 tigleefgpy vdgapattat etgggwhltg akaavpvthv aeraivsatt pagaalfvvd
      181 lagdgvaveq tqsttweicg nvtfdaapae llgpadgtav qwlldrvela laalqlgvga
      241 gaveqavtyl ngrmqfgrpl atfqavghql adcyidleam rvtlwqaawl ltegadpgts
      301 vlvakwwatd ggqrvvhrtt hvhggmgvdt dypvhrhllw gkqigatlgg sasdlarlga
      361 qlaagvevva
//
LOCUS       WP_010596089             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010596089
VERSION     WP_010596089.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24464
     Region          26..72
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          94..207
                     /region_name="TetR_C_24"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17932"
                     /db_xref="CDD:465574"
ORIGIN      
        1 makasadras ttvetlsksd rtrerilnaa advlsrngya gtrlsdiadv aelqapaiyy
       61 yfrsredvie evirvgqrlt idhvvaaldp lppetpavdr ilaavaahle vvltrskyas
      121 asirnmsqlp admrerqlel rreygtiwre lfeqgaaage fdprldphaa rmlvigalnw
      181 vpewwnpdrg tadsiienaq qfvrfgltkr sstrfaptls
//
LOCUS       WP_010596175             139 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Rhodococcus].
ACCESSION   WP_010596175
VERSION     WP_010596175.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..139
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15050
     Region          23..122
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 mistttrpae rptdrkfria glvitglvvl fllfdaaihv lnvdqarqam idlgfdpnln
       61 yvigvvmlvc lalylvpats ilgavlltgy lggavatnml nemplfstil fpvyvgvfvw
      121 aglylrdpvv rsvmplrrg
//
LOCUS       WP_010596129             532 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [Rhodococcus].
ACCESSION   WP_010596129
VERSION     WP_010596129.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..532
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=57218
     Region          19..528
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mnndtepars itpqsatlsa llhnaspdsp fllcpdrdwt ygdfsravde faagllsmgi
       61 skggrvaiaa pnsaqwlitw faaakigail vtlnvayrer efdymlnqsa asmlicssrd
      121 gdfdfvdfvq glrpriptvc hyifldddgf agshrwdeip tapdtetlrh reslvqphdp
      181 avvlytsgtt gdpkgatlth asilasaaat aehlhltadd vaighmplnh vggmtctvga
      241 tmaaggkval lprysprtal eaidgrkvti figvptmytm mmdlpefpaa dtssvrtcvt
      301 ggsnvepalg rrildtfngv rmanlyglse tsgaciisap dddletlvat lgvpigdfei
      361 ritdddhhql pidsegelhi rgrcvadgyw nkpaeskhtf lpdgwlvtgd marqrpdgri
      421 alcgrkkemy vrsgynvypv eienvlaadp tvamsavvgv pddlygevgh ayivptpgtt
      481 vdidalfdrc reqlakykip arihvvdtlp ltpsgkikkv alrasapaes sp
//
LOCUS       WP_010596199             336 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PDR/VanB family oxidoreductase [Rhodococcus].
ACCESSION   WP_010596199
VERSION     WP_010596199.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..336
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35661
     Region          15..230
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(53..54,56,79..81,87,89..90,130,229)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(53,55..56)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(87,90,93,99)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(122,126..129,131)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(127..128,151..153,202..203)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          242..319
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msafnqpswq rgrvvstdpa adaiarivla ldtpvraepg shvdvrldtg evrsysvvst
       61 gtagtvvsag adgrtvtlgv hlsptsrggs rfmhalrpgd eldvtaplqn fplrigarry
      121 vllaggigit aisamgtalk rvgadyrlvy vartrsaaaf lselaalhgd rlelhlddeg
      181 tgldvgtlvd gvdahtelym cgpirlmdav rrawtdrelp lpnlryetfg nsgwfdaeef
      241 vvkvpdlgve ttvgtdesll daleragvdm mfdcrkgecg lcqvgiaavd gavdhrdvfy
      301 seeqkaaatk lcacvsrvvr rpgapavpgt vtlavr
//
LOCUS       WP_010596235             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Rhodococcus].
ACCESSION   WP_010596235
VERSION     WP_010596235.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..187
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=19984
     Region          32..179
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mslsmsnale ysataaseha pgvrgdeyrs alrrhpagvt ivtlesgsgp vgftatsfas
       61 lsldpplvsf nitdtsssid avrsaeslvi hllgdhqqhl aqrfarsaae rfsdeslwtr
      121 iesgepvlhg tpvwlrvvvd rliplgdstl vvgvvvrahe dpnpaegksi pllyhegayh
      181 rpvalee
//
LOCUS       WP_010596271             357 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Rhodococcus].
ACCESSION   WP_010596271
VERSION     WP_010596271.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..357
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39188
     Region          1..356
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mapvtfdhat clfpgsttpa vdalnleied geflvlvgps gcgkstslrm lagleqvhsg
       61 riliggrdvt aqepkdrdia mvfqnyalyp hmsvaenmgf alklaktpka eirarveeva
      121 kmldleqyld rkpkalsggq rqrvamgrai vrqpqvflmd eplsnldakl rvqtrtqiaq
      181 lqrrlgtttv yvthdqveam tmgdrvavld kgilqqcasp rvlynkpanv fvagfmgspa
      241 mnlftlpvfd rgvmlgdtav qvprdvvgrv tesevvvgir pehfeiapdg lemdvdvvee
      301 lgsdayvygr aqvagrpqqi vargdwrnpp qkgervhlrf dpdqvhvftt sdgrrlg
//
LOCUS       WP_010596276             411 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SRPBCC family protein [Rhodococcus].
ACCESSION   WP_010596276
VERSION     WP_010596276.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..411
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=44941
     Region          161..295
                     /region_name="SRPBCC_8"
                     /note="Ligand-binding SRPBCC domain of an uncharacterized
                     subfamily of proteins; cd07817"
                     /db_xref="CDD:176859"
     Site            order(162,164,166,175..177,179..180,195,201,203,205,207,
                     218,220,223,229,231,241..242,244,246,256,258,260,262,
                     274..278,280..282,284..286,289)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176859"
ORIGIN      
        1 mtrsledatr rlgktaketa gkagktaagt agqagktasg aagsagkaaq dlsptkhlqk
       61 slqglagtfa eralstvsdk vtgtagrlnd yaeggggnll gaitgvqksa egkspitaal
      121 sggfenvkqt akdkfddvke slgggegkgk gggnkklklt niveqidvgv pidlaydlwt
      181 qfadwpkfmk kveqveqasd eklqwtgkvf wsrrnwesti leqvpfdriv wrskgakgyi
      241 dgavtfhela dnltriimvl eyhprglfek tanlwravgr rarlelkhfe rhvmteavlh
      301 pddvvgwhge irdsevvkdd etarreeeeq eqeedvgdeg sedelpeden edelpeeqde
      361 edeglqdded eglqdeteee peepeedeea parrrrggag trrgarrgar t
//
LOCUS       WP_010596287             212 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010596287
VERSION     WP_010596287.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23494
     Region          5..126
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          76..201
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 marprtplls rpliretalr lvdehgldel smrkiaaelg vrapslyshy ankdellddi
       61 adrigesvdv ggfdtddwld alrrwarsyr aalaehpnlv pflarspgrr elaldhanav
      121 hggltrcgwp prtatligas ikylvvgsai asfsggfldd ltiyreryph lsqahrlreh
      181 adeidrdgfe lalesflqgl aqrfasltga dr
//
LOCUS       WP_010596308             519 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [Rhodococcus].
ACCESSION   WP_010596308
VERSION     WP_010596308.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..519
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=56823
     Region          34..133
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          259..513
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msgmlpdrfr lvdlllepdl glrlvtdadp nvgitgahpi eienptrwlr pgsmmlttgs
       61 rfpslehpqq acrelirelv gsgitalgyg vgvitgdipr slldeaerhr favvaippel
      121 pfmevvgrvn aavqaqdsml lrrtlqmqnh lleamtaesp eadlvarltg llrssvvlyn
      181 evgdvvasag gapvhlirnq lrgrdgrllf rvgrwsvsah sispgdqhyw lalasksnel
      241 adpltapave vslrllntie rtrqratven rarhaalvra lasgdpsdtd tvldqlemlr
      301 fgpepdmrml vlsaapdydn rrwvfransl ldavesdvsg lardigltll largdgglig
      361 vvparaeafe swshnlpqgl tcgssepftd pargpgklre arwarrsaer lgrtaqrfed
      421 vsladwllag rdpeqalgra tavlgplldg hddlvdflvl hlardldvgr tarelnlhpn
      481 tvrhrvkrve dllgrslrsp rdvtdlhlal evlaerpts
//
LOCUS       WP_010596309             516 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [Rhodococcus].
ACCESSION   WP_010596309
VERSION     WP_010596309.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..516
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=54513
     Region          11..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          223..511
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mavtvrrltt lpdlgltlva grdgadrvie wahpielpdp tpwlsggelv mttgleigad
       61 adaqfaylqg lvgagcvala fdtgtrfdrv pdglraagda lgfpvlavpa stpfiaitra
      121 videltadqv ravqrvvdqq erlaratlrg gvpavvtalg qalagvvavv dpddrvlaey
      181 gsdtsrairh aravsesasr sprrrqlskv laddgghytv qsiaaaqdly gylavgtaep
      241 lppadrllla havslisiel gkpakvqsae qrlravvtrt lfdapermda gllryfgfep
      301 tdtvavavlt dvgpllpaer qvgaalaveg iphltasvga dvavvlpadr areiatrvqd
      361 rvraqlgrpv rcglgspgav tdantsvhqa lsaahaardg srepvvftel gtfsvllgmq
      421 dpdalhaiah sglealddyd ekhgasgrlv etlaaylehn gqaestaval gihrhtlrnr
      481 lariteltgr dldsihtrve wwlavkarem ldgrdg
//
LOCUS       WP_010595842             395 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: benzoate/H(+) symporter BenE family transporter
            [Rhodococcus].
ACCESSION   WP_010595842
VERSION     WP_010595842.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..395
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39295
     Region          9..395
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 msdapapsrp dslirplgas vvtalvgfts sfavvltglq avgaspsqaa sglsalcltq
       61 glgilwlarr frtpitlaws tpgaallagt gvvaggwpaa vgafvvvgaa ivltglwprl
      121 galiaaipas laqamlagil vplclapveg vmdapaailp vvatwlvlqr lrprwavpga
      181 fgaaavvvai hlvrsgtapa arelvpalel tapawtwqal lgialplyiv tmasqnipgt
      241 avldsfgyat pwraamtvtg lgtvagatag ghainlaais aalaaapeae pdparrwvva
      301 wcagwsylal avcstglatv vatapdgvve avaglallat lggalasalr dapereaavv
      361 tflvaasgws mfgigsafwa lmvglavrvg lssgr
//
LOCUS       WP_010596344             216 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010596344
VERSION     WP_010596344.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22146
     Region          12..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marrsdpttg praamirsai rlirergvaa tsfadvlahs gaprgsvyhh fpggkaqlve
       61 eatrsaadhl gdgvtrvlea sdtpgalral adlwrrgled gdyavgcpiv aaalgterga
      121 rdvagvafet wcdlladalv adgvgperar slavlvvgal egalvlaqaq rssapldavv
      181 deltvlcrsa idpavgpcfg svespgrsgg eacrer
//
LOCUS       WP_010596410             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Fpg/Nei family DNA glycosylase [Rhodococcus].
ACCESSION   WP_010596410
VERSION     WP_010596410.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..265
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=29223
     Region          2..263
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpegpslhrl arlhqrrfsg aplrvsspqg rfagdaalvd grvllraeal gkhlwhhydn
       61 gltvhvhlgl ygsfteapvp mpdpvgqvrm rmvgaeygtd lrgptacevl tpdevaaiaa
      121 rigpdplrkd adperawari cksrsaigsl lmdqsvisgv gniyraevlf rhgihpqrpg
      181 rdltraefdg iwddlvvlmr tgvrrgaihv vrrehdrgap ayakgrprty vyrragepcr
      241 lcttpvlhsi mqgrnlfwcp acqtg
//
LOCUS       WP_010596509             140 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Rhodococcus].
ACCESSION   WP_010596509
VERSION     WP_010596509.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..140
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=15111
     Region          1..103
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 maalgelera vmdhlwsste pqtvrqvhea laarrslayt tvmtvlqrla kknlviqqrd
       61 drahryvpvh greelvaslm vdaldqades agrvaalvhf igrvnpdeaa alrealaale
      121 aqqdgptrpt vadpgtgras
//
LOCUS       WP_010596515             361 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [Rhodococcus].
ACCESSION   WP_010596515
VERSION     WP_010596515.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..361
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=38410
     Region          17..>347
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mndwlavllt vlllagnaff vgaefalita rrdrlealvg qgkkrartvi aagehlslml
       61 agsqlgitic sillgrvgep aiahlietpm halgvpdsll hpigfalalt ivvvlhillg
      121 emvpkniaia gpersamllv pthllfmkva rpliafynlc anlslrllrv epkdeldvtv
      181 telelsemig esrsegllde eehrrltqal qtsgrtvadv tiplsgvrtv plgpagttlg
      241 aveqavtetg ysrypaetah gelagylhlk dvldlvrdes agpdtliata eirplppvpv
      301 daplddalsl lrrtsahlgg vvdehgtvig ivaledlveq fvgtvrdtth rmadpgpgpr
      361 p
//
LOCUS       WP_010596539             343 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [Rhodococcus].
ACCESSION   WP_010596539
VERSION     WP_010596539.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..343
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=36851
     Region          <20..>121
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          101..329
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mhkparrdgt pdrrktnsra gnpprvrrge paaraatskp aagaatpkka hrkgdtplnk
       61 rgrpaapkpq aqrpaalpki snarparhqh aaerpqlpag egvrlqkvla qagvasrraa
      121 eeliaagrve vdgaivteqg lrvdpenavi rvdgirvvvd kdlvhlvlnk prgwqstmsd
      181 dlgrpcvgdi vservaagqr lfhvgrldad teglllltnd gelahrlmhp syevtktyla
      241 tvkgvlprgi gkqlragvel ddgpakvdsf allqvnegqs lvrlelhegr khivrrllda
      301 vghpvirlvr tdigpvalgd qrpgtlrvlg rkevgslyqa vgl
//
LOCUS       WP_010596552             329 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HAD-IIA family hydrolase [Rhodococcus].
ACCESSION   WP_010596552
VERSION     WP_010596552.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..329
                     /product="HAD-IIA family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33848
     Region          6..261
                     /region_name="NagD"
                     /note="Ribonucleotide monophosphatase NagD, HAD
                     superfamily [Nucleotide transport and metabolism];
                     COG0647"
                     /db_xref="CDD:440412"
ORIGIN      
        1 mtgtgaslrt hydvllldld gtvyrgaeav pgarealseg aerlfyvtnn asrrpgevak
       61 hlrelgfaad esnvvtssqs aarllaervp agapvlvvgt ealvdevagv glvpvrsada
      121 dpvavvqghs petgwailae atlalrsgal wvatnidstl pterglvlgn gsmvaalrsa
      181 tgreplvagk paapliedav vrsgasrplv vgdrldtdia ganavgvdsl lvltgvstva
      241 dllrapaeqr ptyvadslas ldgeaaelrp gtrephavsf dgrdvhlapq paadpmaalr
      301 avldvawshp gfgrvvatdd llarwgmpr
//
LOCUS       WP_010596630             318 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PDR/VanB family oxidoreductase [Rhodococcus].
ACCESSION   WP_010596630
VERSION     WP_010596630.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..318
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34670
     Region          12..220
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(54..55,57,71..73,79,81..82,122,219)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(54,56..57)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(79,82,85,92)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(114,118..121,123)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(119..120,143..145,194..195)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          235..318
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mntidtpltl nvarrqeats dvvilelatp dgtelpkwsa gahidlhlkd gltrqyslcg
       61 dpddrsrwri avlrepnsrg gseyvhtsvl eqtdltvshp rnhfellpaa ryifiaggig
      121 itpilamlqs dtarnaewel hyggrsresm aftdelatty adrvqlhpqd evglldldti
      181 lgepradtli yccgpgplld aveercktwp egalrlerfa pkesanltqd gsfevelrss
      241 gvsvqvhagq sildavrgvg asvafsceeg tcgtcevsvl egevdhrdsi lspeeqadnd
      301 tmficvsraa cprlvldl
//
LOCUS       WP_010596557             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Rhodococcus].
ACCESSION   WP_010596557
VERSION     WP_010596557.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..233
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24353
     Region          5..218
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mrqhsgigvl dkamavlhav arqpcnltel cartglprat ahrlavglev hrllardgdg
       61 qwrpgpglae lsagagdplv daaslvlprl reitgesvql yrregthrvc vaalepptgl
      121 rdtvlvgarl pmtagsgarv llawadaatq railpeaafg ervlaevrrr gwaqsvaere
      181 pgvasvaapv rdasgsvvaa isvsgpvdrm grrpgarwaa dllaaadalh krl
//
LOCUS       WP_010596632             156 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein, partial [Rhodococcus sp. P14].
ACCESSION   WP_010596632
VERSION     WP_010596632.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         1..>156
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          12..106
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
ORIGIN      
        1 mqfirpfddt qafdtgfpgy raqfvsrles allihsviqe dgcgpglhyh lsdqlyflid
       61 ghmqvqlgde vhaigpktlv fipaglphrn wnegpgaenh femiiptpmp gsslalmvda
      121 vdavpaehrt tskgyvravd teqlrealpg frlqpl
//
LOCUS       WP_010596683             337 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Rhodococcus sp. P14].
ACCESSION   WP_010596683
VERSION     WP_010596683.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P14
  ORGANISM  Rhodococcus sp. P14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rhodococcus sp. P14"
                     /db_xref="taxon:450821"
     Protein         1..337
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37039
     Region          <215..271
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 msfysveptp rtswrqavlm gvnsrtykfa lgtallelak pgrdavtlae laeryawall
       61 areggfpqap aavelrdtdf lailereraa ssaagrptea lveaavrsmp gmvmqkfhnl
      121 rgigevahaf yrvqgrgsna mvrltpelhr vaaaddvlgr eldsrwsive asfdasigrt
      181 lidrgveidp rgavvvspar rvpltsvrga iagfqhgrcf ychqeldqld adihvdhvfp
      241 fswmntgswc gpdlnhvwnl vlacapcnla ksnrlptaee verllernda iagsphplrr
      301 tleitmgttg ptaearrrqr rdfvgavwnh ateglvr
//
LOCUS       WP_010596748             152 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Rhodococcus].
ACCESSION   WP_010596748
VERSION     WP_010596748.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..152
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16472
     Region          20..142
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mhsrhasqaf tstgmfyrgv raepgqvtml rqaldrwldr lhleaelgqd vllasyeala
       61 nvvehayadg pgdhrgavdl eavyrpdehs vevvvtdhgr wrtpasgdsc rghglalirt
      121 ltshtdvvsv pdgtsvsmrw dvadhpalva ap
//
LOCUS       WP_010596742             680 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha-1,4-glucan--maltose-1-phosphate
            maltosyltransferase [Rhodococcus].
ACCESSION   WP_010596742
VERSION     WP_010596742.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 680)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 680)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10571012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..680
                     /product="alpha-1,4-glucan--maltose-1-phosphate
                     maltosyltransferase"
                     /EC_number="2.4.99.16"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009313 - oligosaccharide catabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0030979 - alpha-glucan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=75489
     Region          11..203
                     /region_name="GlgE_dom_N_S"
                     /note="Alpha-1,4-glucan:maltose-1-phosphate
                     maltosyltransferase, domain N/S; pfam11896"
                     /db_xref="CDD:463388"
     Region          208..567
                     /region_name="AmyAc_GlgE_like"
                     /note="Alpha amylase catalytic domain found in GlgE-like
                     proteins; cd11344"
                     /db_xref="CDD:200482"
     Site            order(265,269,280,282,325,357..358,360..361,393,395..396,
                     424,480,534..535)
                     /site_type="active"
                     /db_xref="CDD:200482"
     Site            order(343..345,352..354,367,398..401,403,406,428,430..431,
                     434,438)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200482"
     Site            order(395,424,480)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200482"
     Site            order(427..429,446,449..450)
                     /site_type="other"
                     /note="acceptor binding site [chemical binding]"
                     /db_xref="CDD:200482"
     Region          <555..607
                     /region_name="GlgB"
                     /note="1,4-alpha-glucan branching enzyme [Carbohydrate
                     transport and metabolism]; COG0296"
                     /db_xref="CDD:440065"
ORIGIN      
        1 mtgrigasat grlgiddvrp disggrhpvk avvgevlpvs avvwreghda vaatlavrgp
       61 gsdpesegkl iripmvpgea pdtfhavftp tspglwtyrv eawsdpvttw rhavdakvaa
      121 gqgpedland ieigarlfek aaktaprpnr pallavaaal rserpladri apafaadite
      181 ilranplrel vtrgkaytav vdreralfgs wyeffprstg gwnedgtprh gtfataaael
      241 prvaamgfdv vylppihpig kinrkgpnnt ltagpddvgs pwaigsdegg hdaihpqlgt
      301 eddfrafvar areldleval dlalqcapdh pwakehpewf tvlpdgtiay aenppkkyqd
      361 iypvnfdndp dgiyaevlrv vrhwisfgvk ifrvdnphtk ppnfwewlia evkrtdpdvl
      421 flseaftrpa rmyglarrgf tqsytyftwr vakweltefg qeiaakadea rpnlfvntpd
      481 ilhetlqhgg pgmfalraal aatlapswgv ysgyelyehi plrpgseeyl dsekyqlrpr
      541 rfdearrrge slepwiatln rirrahpalq qlrnihfhhi dndaliaysk fdprtgdsvl
      601 avinlnpfga eqgtiwldmp alghewhdql tvfdevsgaq yswgqanfvr lepwravahi
      661 lalppigvpt rttlayrrns
//
LOCUS       WP_010597024             106 aa            linear   BCT 01-JAN-2025
DEFINITION  BON domain-containing protein [Rickettsiella massiliensis].
ACCESSION   WP_010597024
VERSION     WP_010597024.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..106
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11564
     Region          22..>105
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mktklwiilg lmifpitstf amsshkamqs dsvgqyvdns vitlkikskl ltdpeirglg
       61 isvmsdrgri klsgtveteg qkqkaenltk qvegvtnvdn eivvkk
//
LOCUS       WP_010596863             343 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Rhodococcus].
ACCESSION   WP_010596863
VERSION     WP_010596863.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..343
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35301
     Region          18..330
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msvtldkttt tkrpapvads trprvalgpl vekyalvlal vavvlvfsal rpeiyptann
       61 lqnilgsqav llilalgliv pltagefdls avstmslaam tiavlnvqqg wsllpaiava
      121 vlvalfvgiv navlvvrlhi dsfiatlgsg tvvlgvvqwi sdstsvtgid aalvdatigt
      181 rvfgvslqfy yalalvllta vifqytpigr rllfvgrgpq varlsglhvd rirggalvts
      241 alvaalagiv yagmlggadp ssgqsfmlpa faaaflgata ivpgrfnafg tlvavyflva
      301 gvvglqmlgv asfvqqlfyg galvvavals gavrrrtasr sar
//
LOCUS       WP_010597060             360 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Rickettsiella
            massiliensis].
ACCESSION   WP_010597060
VERSION     WP_010597060.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..360
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39585
     Region          14..354
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mltsgksltn sptminliav ekiypsrpis lpvlqdinlh vnqgeifgil gqsgagkstl
       61 lrcinllekp trgavwvdgq allslnkqql rqlrqkigmi fqhfnllnak tvyenialtl
      121 qlskcskkei egkvrsllel tglqdkpqhy ptelsggqkq rvaiaralac epkillcdea
      181 tsaldpqttq tiiqllktin trlnltivli themevvkgl chrvalldkg qiieqapvad
      241 ffmtpqtpia kkwvhfdlek alppllqarl vaearpgyha vlriffrgsa asepliahlm
      301 chiglilnil qanieslnel pvgifvaevi gsqqalqrgi dyllekglfv eiigyvaasv
//
LOCUS       WP_010597453             248 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Rickettsiella massiliensis].
ACCESSION   WP_010597453
VERSION     WP_010597453.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142575
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..248
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27491
     Region          6..>166
                     /region_name="SDR_c"
                     /note="classical (c) SDRs; cd05233"
                     /db_xref="CDD:212491"
     Site            order(113,139,157,161)
                     /site_type="active"
                     /db_xref="CDD:212491"
ORIGIN      
        1 msqkialvtg gssgigrata ielvnqgyqv fitarkevel lntknsaknp eniisivvdf
       61 nksgfekeip sfikksvgey vkidrlihca aiigpidklk nlesrlaesm hvnayaplil
      121 thellplcnp ntrgsfmssn fmkpakitpf idifgayiss kivlltciil sypffkgkis
      181 ieiptlapvk dtiiynyfli krlqilvnns qkikssldqe kstklkdetl kqapvnkkst
      241 evvtfikn
//
LOCUS       WP_010597465             113 aa            linear   BCT 01-JAN-2025
DEFINITION  CinA family protein [Rickettsiella massiliensis].
ACCESSION   WP_010597465
VERSION     WP_010597465.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..113
                     /product="CinA family protein"
                     /calculated_mol_wt=11646
     Region          8..>101
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 myptlyrlad qlgrlvksrh qylataesct ggqlatllts vpgasqwftg gvilalspsq
       61 lthdgvasqe talamaegvl tkleaniama itgiagpsga tvtpgfnhlf fvk
//
LOCUS       WP_010597477             265 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Rickettsiella
            massiliensis].
ACCESSION   WP_010597477
VERSION     WP_010597477.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..265
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29119
     Region          19..260
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 msqkkmtdsq tapikngeal rfvalslayg srvifsnfna ticqgefiai lgangagkst
       61 llrailglvp sqsgqirvfg kkpvrkgssl vgympqtrqp wmdsalsaya wlsaqlngfk
      121 wgipwldraq kqeidrvval vnaepilhka yallsggerq rlllaqalln rpqlllldep
      181 lmnldpyyqe tlvtlvnrir lelgitillt shdinpllss vsrvlylakg naalgsvaev
      241 itsqklsely nrdiqviehe knvll
//
LOCUS       WP_010597729             399 aa            linear   BCT 01-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Rickettsiella
            massiliensis].
ACCESSION   WP_010597729
VERSION     WP_010597729.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..399
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43875
     Region          36..385
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mskprlflss flamvfvvms pltqadpiip itapsaaspt ltpvapnvda kayllmdtys
       61 ghilashnid erlapasltk mmtsyvisqa lkegrihldd pvmisesawk tggskmfvkv
      121 gdkvpvrdlm qgiivdsgnd acvamaeyia gsqesfvslm nqeaahlgmt qthfvdvdgl
      181 pdpnhyssar dmailarali ldfpedykwy sqkwftyngi rqanrnrllw rdpnvdgikt
      241 ghtseagycl aasghkdnmr lisivmgaps demraqdsqk lltygfrffq svklynantp
      301 lttariwfgd rsrvsvgvar glyatvpvgr nsgmknkltf tpnlsapikk gekvgeiqvv
      361 lndktiaqap lialeevskg gvwrklidht srwfektna
//
LOCUS       WP_010597815              64 aa            linear   BCT 01-JAN-2025
DEFINITION  dephospho-CoA kinase [Rickettsiella massiliensis].
ACCESSION   WP_010597815
VERSION     WP_010597815.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..64
                     /product="dephospho-CoA kinase"
                     /EC_number="2.7.1.24"
                     /GO_function="GO:0004140 - dephospho-CoA kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015937 - coenzyme A biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=6722
     Region          1..>56
                     /region_name="CoaE"
                     /note="Dephospho-CoA kinase [Coenzyme transport and
                     metabolism]; COG0237"
                     /db_xref="CDD:440007"
ORIGIN      
        1 mfvvaltgni asgkstaagy faeygvpvid adaiartllt enkvlqgkis rlfgsgysdr
       61 rrid
//
LOCUS       WP_010598046             132 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Rickettsiella
            massiliensis].
ACCESSION   WP_010598046
VERSION     WP_010598046.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..132
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15316
     Region          <43..100
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mlydelardy llylgnrkps nnqlvvfkkl itdvisnclf tfpdkltlqe mkclylsfkg
       61 ksiahaaeil eihpdtvkyy rkrsirklgc knmveaafkc tgthfqndlc dklitqnirh
      121 ikvyiqrkvn sl
//
LOCUS       WP_010598091             268 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Rickettsiella massiliensis].
ACCESSION   WP_010598091
VERSION     WP_010598091.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..268
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30513
     Region          94..267
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mtigsdrlci syksnknipa clakkniclg nninllinll kkncqnnvyy fdfglgrtnn
       61 yfgseinqik ktptvegpdg ftpistekgs lflisggyiw rfnsllfpta svgleysymp
      121 eisirgniyd lndrdqppgf iyqynvshts lrligkmnly cwksfmpyve igvggswnym
      181 neykektmef prmipttfqd skkfafsysa tigidyrsnq nfilsvgyry dnfglnetgl
      241 aigqyknnhl netlnsntll ltgrylfs
//
LOCUS       WP_010598148             268 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Rickettsiella massiliensis].
ACCESSION   WP_010598148
VERSION     WP_010598148.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..268
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30008
     Region          2..264
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mlklriltal vlipivilgl fglsqpyfgg vtafitliaa wewarlggwt rhpmrgiyvg
       61 lqavilmgis ffsvyehivv llglllwfli sgylvwartq itlpwispnv rltlgffilt
      121 scwvalqqlq qqpiyllvlf liiwladsaa ylggrlwgkh ylapllspkk tweglifsfs
      181 vtflmvmafi ymlhgpkphf wqvlilvllt iiasvagdlf esqlkrleki kdsgqllpgh
      241 gglldrvdsl lsaapvfagt fwllglfl
//
LOCUS       WP_010598159             196 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Rickettsiella
            massiliensis].
ACCESSION   WP_010598159
VERSION     WP_010598159.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..196
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22661
     Region          2..180
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 miqlqlrylp nlvtcirfil igpilwallk kyyplafylf lvaglsdgld gflarffgwt
       61 sqfgalidpl adklllmssf mvlaylkqip fwlmilvigr dtwimggali yrycvgplny
      121 kpvwisklnt flqlvlvtll liklafyplp erlidrliea vfitsllsfi qytwvwarqa
      181 lfyskilkke pprslp
//
LOCUS       WP_010598189             297 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rickettsiella massiliensis].
ACCESSION   WP_010598189
VERSION     WP_010598189.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..297
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33656
     Region          4..202
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mqalsienlc kvypphtval qgidlqveqg dffallgpng agksttigit akaclglvpq
       61 efnfsifekv mdvliyqagy ygiplrtakq raerylkalq lwdqrhqism rlsggmkrrl
      121 miaralvhqp kllildepta gvdieirrsm weflqtinre gttiiltthy leeaehlckn
      181 iaiidkgril kntsmknlls eldretfvcd lkkplteapq atseftlrlq dpwtievdvk
      241 kaqslnsvfh yldtqqieva slrnksnrle alflsiisrq aqaeftlktn lerknad
//
LOCUS       WP_010598300             107 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Rickettsiella massiliensis].
ACCESSION   WP_010598300
VERSION     WP_010598300.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..107
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=12096
     Region          16..>96
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 meqqneirdk kivkeillve dcaiqvkalc rflylleyqv eiardaktai qfiqnksytl
       61 ivtdlglpdd sgelvieetr ksefnqltpl ivctghansk kkknaks
//
LOCUS       WP_010598470             181 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Rickettsiella massiliensis].
ACCESSION   WP_010598470
VERSION     WP_010598470.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..181
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=20637
     Region          9..>117
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mntsnipfkk qlqedmktal raqekerlgv irlilavlkk aeideglete tllandpril
       61 rildkmrkqr qdsiqqyeqa qradlaeqer feesvicsyl paplsieevd qlikqvircy
      121 lkshrlsfhe nvcplidgvc llvgieanki vfrgfnakak cpnstrfysg aacplryciv
      181 n
//
LOCUS       WP_010598343             336 aa            linear   BCT 01-JAN-2025
DEFINITION  inorganic phosphate transporter [Rickettsiella massiliensis].
ACCESSION   WP_010598343
VERSION     WP_010598343.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..336
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36034
     Region          3..331
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mtstyafiff viflaftfdf ingfhdaans vailiatkvl kpftavlwaa ffnfiaflff
       61 hlnvattigs gliephivtp ylifaalmga itwnlltwyf glpsssshgl igglvgaalv
      121 aggggilnwh gllpvliaiv lspllgllms wmlinasnrf lkgvhsekte rwakrvqlla
      181 gallslghgg ndaqktmgii aillfstgll ngqfyvpfwv viscnfvmgl gtlmggwrii
      241 ntmgtkltrl tlvsgscaat gaaltlfaat dmgipvstth tvtgailgag ttnkwlgtqw
      301 qivrrivwaw fltipaaalv aaavmwlihy fqnipl
//
LOCUS       WP_010598563             287 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Rickettsiella massiliensis].
ACCESSION   WP_010598563
VERSION     WP_010598563.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..287
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=32567
     Region          <166..249
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mrqrfgyhhi flfslllsnp lwakvilsnn fisccdtpky pkpyielgis qashqqfshd
       61 nhqftlfsdg tiektlsirp thhstlpnff tlgvgsqwtr nhslspfpaw svglryqygs
      121 tnrakqwlnf sldsqqegei qpliktflpv sliqhtvtsd vklnlyrldt fspyvnvglg
      181 vswkripgqa fwlnppthlp aqentsnwqn sslsyhlgag ldflisrvwt ltlgyqydnf
      241 gsievgapvl spqtqssffp kgiklsnfyl gklmthslql sgryffg
//
LOCUS       WP_010598722             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Rickettsiella massiliensis].
ACCESSION   WP_010598722
VERSION     WP_010598722.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45122
     Region          3..362
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mpkervrlfp wlvcglgalf ycyeyflril psvmsedllk ifsisgvafg hlvafyyyay
       61 tpmqlpvgim mdrfgprkll vfascvcaig tylfahhhlp taqagrflvg lgsafafvgv
      121 lklaslwfpp srfafiagma tslgmfgami gditlsklvh vlgssatldw aatvglvltl
      181 lmwliipetk tiktkaaaas sqlnyrefsl avfklcknpq mwivgligsl lylslsgfae
      241 vwgipylira yglsnqaaaw disfvflgwa igsplvgwis dkignrrcpi iigalfgavl
      301 ftiiiycpqi vraqlpfllf ifgvcssaqi ivfpiarein vpalagtaia vinslvmfsg
      361 vfisafdrqg tgclnrnpce rqfngilgrk lsirvechss rlyfccnins vc
//
LOCUS       WP_010598846             187 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Rickettsiella
            massiliensis].
ACCESSION   WP_010598846
VERSION     WP_010598846.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..187
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=20402
     Region          1..181
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; cl46157"
                     /db_xref="CDD:480497"
ORIGIN      
        1 mhlatstala siifsaliav fyqqrrgaih wpifgqlmpg mllgllggaf lslrlstetl
       61 kilfslflwa malklfmykk deklhknehp llivqwvmga figlisgllg igggavavpi
      121 llrlgftflf tltslhlsgl pegihsfvyw pavfglvlgs llcvplgvrl gqrlsgsklr
      181 kcslfff
//
LOCUS       WP_010599046             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: uroporphyrinogen-III synthase [Pedobacter].
ACCESSION   WP_010599046
VERSION     WP_010599046.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schubert,H.L., Raux,E., Matthews,M.A., Phillips,J.D., Wilson,K.S.,
            Hill,C.P. and Warren,M.J.
  TITLE     Structural diversity in metal ion chelation and the structure of
            uroporphyrinogen III synthase
  JOURNAL   Biochem Soc Trans 30 (4), 595-600 (2002)
   PUBMED   12196144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..256
                     /product="uroporphyrinogen-III synthase"
                     /EC_number="4.2.1.75"
                     /GO_function="GO:0004852 - uroporphyrinogen-III synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006780 - uroporphyrinogen III
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0033014 - tetrapyrrole biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29263
     Region          13..233
                     /region_name="HemD"
                     /note="Uroporphyrinogen-III synthase [Coenzyme transport
                     and metabolism]; COG1587"
                     /db_xref="CDD:441195"
ORIGIN      
        1 mqekndsrir kvksilvtlp kpetekspyy dlakkhnlkv dfrsfihveg vpardfrkdk
       61 inladftavi ftsrnaadhf friceemryd vpaelkyfcl setialylqk yiqyrkrkif
      121 fgkqtaadla evlkkhanek flypcsdvat edtmkfleks gydftpavlf rtvvsdlsdl
      181 aevfydviaf fspssiqslf knfpdfkqnn triaafgvnt skactdmdli vdiaaptpgv
      241 psmtmaieny iktsnk
//
LOCUS       WP_010598937             254 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Rickettsiella massiliensis].
ACCESSION   WP_010598937
VERSION     WP_010598937.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..254
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=29503
     Region          1..225
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdsihmdslk ryikerkleg vknrtincgl qvvrhilkla eqewkdeynl swlhkaakik
       61 llreidkrep yplqiteqar llnelplhlk gmalfavntg crdheicclk wkweikipeg
      121 svfiipasev knreqrlvvl nrnalrviee vrgehseyvc tfrvqpvsrm lnsawkkarv
      181 rvglpqvrvh dlkhtfgyrl rsaevsfedr qvlmghktks vtthysvael gnliraanev
      241 cetgrhlmil rkaa
//
LOCUS       WP_010599005             146 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Rickettsiella massiliensis].
ACCESSION   WP_010599005
VERSION     WP_010599005.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella massiliensis (Diplorickettsia massiliensis)
  ORGANISM  Rickettsiella massiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Rickettsiella massiliensis"
                     /db_xref="taxon:676517"
     Protein         1..146
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=16761
     Region          17..132
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 melqqqeiky kkivkeillv enctvqvktl crflwfleyq ieiatdakta iqliqnkpya
       61 liitnlglsd nsdelvvqei rkselnqltp livctnnlds kkaekckelr aqeilikpid
      121 ietlknsiek clinkesdvc idrelv
//
LOCUS       WP_010599079             219 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Pedobacter agri].
ACCESSION   WP_010599079
VERSION     WP_010599079.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..219
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=24438
     Region          19..219
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mktlirtsil lsfcliafts mtlkpkriif fgdsitqqgv skngyvtlik ksldstkyev
       61 lgagiggnkv ydlylrledd vlnkkpdlvv iyvgindvwh kqsshtgtdy dkylkfyqal
      121 inkiqgvgsk vilvtpsvvg ekkdgtneld adlnkyaagi relakknnlp lcdlrkifae
      181 yeaknnpedk ekdilttdrv hlnetgnklv aeqllplvk
//
LOCUS       WP_010599091             374 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 18 protein [Pedobacter agri].
ACCESSION   WP_010599091
VERSION     WP_010599091.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Funkhouser,J.D. and Aronson,N.N. Jr.
  TITLE     Chitinase family GH18: evolutionary insights from the genomic
            history of a diverse protein family
  JOURNAL   BMC Evol Biol 7, 96 (2007)
   PUBMED   17594485
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Fukamizo,T.
  TITLE     Chitinolytic enzymes: catalysis, substrate binding, and their
            application
  JOURNAL   Curr Protein Pept Sci 1 (1), 105-124 (2000)
   PUBMED   12369923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..374
                     /product="glycoside hydrolase family 18 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004568 - chitinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008061 - chitin binding [Evidence IEA]"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41639
     Region          30..372
                     /region_name="ChiA"
                     /note="Chitinase, GH18 family [Carbohydrate transport and
                     metabolism]; COG3325"
                     /db_xref="CDD:442554"
ORIGIN      
        1 mnhqtnslsq lssrililta alllfgfnlk aqkttkpnvi ayytggggte iesypiekls
       61 hliysfghlk gdslninsak dsaliakmva lksrnkdlkv miamggwsac gpcsevfsrk
      121 ngretfaktt kelldyfhad gididweypa vagypghryt eddkqnftll iqelrkklgk
      181 kaeisfaagg tkncidscfe wkkvmplvdr vnlmsydlvs gyatqsghht alfstpqlml
      241 sadygikemi kkgvpankia lgaafyarif qnttdanqgl yqptkflsgv sykhfsdqft
      301 eekgfkyywd dsakapyyyn aatkqlatfd dpksialktk yvvdhqlngi mfweltdday
      361 sngllsvihe tlak
//
LOCUS       WP_010599123             215 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Pedobacter agri].
ACCESSION   WP_010599123
VERSION     WP_010599123.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..215
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24237
     Region          74..153
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 mknnsnsrrd aiqqlgllsa gmfmlslnsc tddkiandnl ketkaplpfl ipaqkpletg
       61 pmgnnmrtli rstqtnnqfs cveavlapkk iagsphkhdk ldelmyvleg tasilmgdev
      121 vevkagcwhl rprgivhvvw nsgsenlrli dmyfnqnfed yleevyfkii peviqnklsf
      181 edpiiakrma eldkkfglty ypekqqalid kygls
//
LOCUS       WP_010599165             397 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Pedobacter agri].
ACCESSION   WP_010599165
VERSION     WP_010599165.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..397
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44491
     Region          33..295
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mhrrsfvkhs avlgssllvg ddvfaafqtd rviniamigc gdrgkgvlsv iksmpskfni
       61 itycdvldfr lketekyvpt gakpvkdyhk vlddqkidav fiatplsehf kiakdavlag
      121 khvyvektmt yniaqalelk klvkkypkqv fqvgyqyrys plyfkvkdmi qsgylgkvsq
      181 idcrwdrnwn wrravadpal erqinwrmyk eysgglaael lshqidfinw afetqpdeit
      241 gtggidvfkd gretydniqa tlrynekgmi gnfgatcgna rdgylfkikg tkgsvsllts
      301 tglfypeest rkelgivdgv tgatkivvnq dggipildka tqdgttyald efyksimnqi
      361 lpasnintgt qasicvamcn eaiytgnkql wkkeyni
//
LOCUS       WP_010599174             160 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pedobacter agri].
ACCESSION   WP_010599174
VERSION     WP_010599174.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..160
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17750
     Region          4..153
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 msdlklirth sahtdfmqlv alldqelavr dgdehsfyaq fnkvdaikev ivayqneipv
       61 acgaikafsk taaevkrmfv hpdyrnqgia ikilaeleqw akelgysecv letgkkqpea
      121 ialyqkvgyq vtpnygqyvg vdnsvcmakp lsnllpdnns
//
LOCUS       WP_010599218             336 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: inorganic phosphate transporter [Pedobacter].
ACCESSION   WP_010599218
VERSION     WP_010599218.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..336
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35514
     Region          16..335
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mvttllvvvv ilaiafdyin gfhdaansia tvvstkvltp fqavlwaalf nfaayfyftd
       61 hkvantvakt vienyitlev ilaglvaaii wnlltwwygi psssshtlig gfagagmtha
      121 lltgaspmda vnmgyvvkiv sfivlapiig lvisvvltli iinicryakp ataekwfkrl
      181 qllssaalsf fhggndaqkv mgiiatalia akvipdfdsm pswvpiacys aislgtmsgg
      241 wkivktmgsk itkvtalegv aaegagaitl gitehfgipv stthtitgsi vgvgvvksvs
      301 avrwgvtinl iwawiltipv satlaaiiyg aiyyfk
//
LOCUS       WP_010599293             323 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Pedobacter agri].
ACCESSION   WP_010599293
VERSION     WP_010599293.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..323
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34730
     Region          1..320
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,123,127,130,148,151..153,172..173,177,192,
                     212..213,234..235,237,259..261,309,314)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkavqitrpg npgvlklvdy pdpspsdqqv riavkaagln radiaqrqgk ypppagvpeq
       61 ipgleiagvv iesgknvsqw klgdkvcall agggyaeqvv veegqclsip ahlsfaeaas
      121 lpeaiftvws nvfqrgaltk gehflvhggs sgigitaiql akafgakvfv tvgsaekakt
      181 cislgadlai nyktqdfqkl lapegvdvil dmiggsylpr niaimrpegr lvyinamegn
      241 speisigevm kkrltitgst lrgreytfkk qlakeieeqv wplldtgqlk pliyktfsfe
      301 dviqahelme ssehigkivl vre
//
LOCUS       WP_010599327             189 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Pedobacter agri].
ACCESSION   WP_010599327
VERSION     WP_010599327.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..189
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=21580
     Region          11..189
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mkalidlilq fgvlnkqqtd filskaktld mkkdeyfsea gkvprhvgfv legvfrfcyy
       61 nnkgdevtny fvdegnfvvd nekfesqiva seyiqavtdc kilafskkdw ddisntivgf
      121 emiksnvvkk cltlamerrs plvsedastr ylsfiqnfps lvnriplsfv asylgitqqs
      181 lsrirrnir
//
LOCUS       WP_010599355             411 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Pedobacter agri].
ACCESSION   WP_010599355
VERSION     WP_010599355.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..411
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43982
     Region          7..398
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mknsilknys gllwllagit agsivglifg krvesikplg diflnllfta viplvffavs
       61 saianidrtk klgrlltimv lvflstvlis avltlvatwl fpihqalgnn piptetekiq
      121 sfgeqmtqll tvgeffeigs rknmlaliif svlvgfstly snkegdgfkn flvsgnevmk
      181 kliilimklg piglgayfay qvgvfgpqlf gtyakalgly ygvgafyfiv fftlyafiag
      241 gfkaikvfwk nnivpsltsi gtcssiatip anlegtlkmg vpayitnvti plgstlhkdg
      301 ssissiikia vvfaifgkdl vhvdtiilal gitvlvsive ggipnggyig ellmisayql
      361 ppealppami igtlvdpmat llnatgdnva amliarfteg knwmeskils s
//
LOCUS       WP_010599318             643 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein [Pedobacter
            agri].
ACCESSION   WP_010599318
VERSION     WP_010599318.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..643
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=73578
     Region          76..217
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          300..619
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkanniyqsl lllsiitsvs lftgckrefl kpdplsfyep eltfssrsgl datlalsdrh
       61 lraywshltt rdisvpigte ymlsdigvsa ktddgnifad vatrltpldg mfdndvnmis
      121 yfwgetyngi kyantitsfi drvpgldeat kqeylgrayf hrsfrylalc fqygdiplvt
      181 kiltvpkqny kttsrqaile mitgdmenav kwvpeqskma yigmvnkaac rqllikcyla
      241 igqwdkaidq anilinqsgy almtsnfgtf dnpnpntwpv nrnviwdlhr pvnkaiaank
      301 eallvmpnre gtdatiryks mrnwgpmwnq aalkspsgkv llsvaktdsr yraqydinsa
      361 igrgiamirp thfaqfglwk vnglddvtdl rhssatgnwa kmemlkyndp tdsfygqnlr
      421 lyngntllct dtirswfnwp hykiyiddpv fqatptsnrn dggaadwycy rlaetyllra
      481 eayyykgnaa laaddvnavr rraqcsqlyt tvnigdivne rarelymeew rhmelsrisy
      541 slalsnkpde wgntyqvanl asnnywfqri qhyndyynkn kvsvrnrnyt iaphniywpi
      601 pqnainanlf gklrqnpgyn gydasvqiwn dwhdavaded nvn
//
LOCUS       WP_010599386             150 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Pedobacter].
ACCESSION   WP_010599386
VERSION     WP_010599386.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..150
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16691
     Region          42..146
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(49..50,82..83,86,90..91,94,136,140)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mkkkffgtli mlflfvsvna dgdiskaknk nkydaktlae ltrnleydfd kpavrsayfk
       61 klddlasavk senyvvslrg hadgigayky nwvlsdkral svkdylvskg vksdrivttp
      121 fgstvpiasn ktesgrqknr rveislkkvs
//
LOCUS       WP_010599405             334 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Pedobacter].
ACCESSION   WP_010599405
VERSION     WP_010599405.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..334
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37403
     Region          1..255
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mikvalvgag kmgvshlsil gahpdveivg vcdtskivtn fleryskldc ysdfgkmldq
       61 vkpdavfiav ptkfhyqlik mameknihvf aekpfclntt egrelislaa knklvnqvgy
      121 hnkfvgtfke vkriiklgmi gevfhfvaes ygpvvtkpkq sswrskpeeg ggclmdyash
      181 vidlvndiva pitevkgatl ksiysntved avysvmstts nvsgilsvnw seetyrkmst
      241 tvtilgskgk iisdanelkl ylkdenkedy tkgwnvkyit dlteqvnfnl rgeeysaqid
      301 yfvdavmnrk pntintfqqa wetdkviell krhk
//
LOCUS       WP_010599435             146 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Pedobacter agri].
ACCESSION   WP_010599435
VERSION     WP_010599435.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..146
                     /product="VOC family protein"
                     /calculated_mol_wt=16063
     Region          5..137
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(5..9,25,63..64,67,85..90,92,96,125,135)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mattntylnf ngnceeafnf yksvfggeft yigrfgdvpe sdeykvpegd knkvmhvslp
       61 tgasvlmgsd nseqyessfv kgnnfsvsid aeskeeadkl fsglsaggqv tmpladtfwg
      121 ayfgmftdkf ginwmvnydd pakmqh
//
LOCUS       WP_010599509              65 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Pedobacter agri].
ACCESSION   WP_010599509
VERSION     WP_010599509.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..65
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6947
     Region          1..>36
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mrlgtvkyyd dekglglitp snggkdlivs akglidkiqt qnivlfdlnf aannvevvkv
       61 ivlks
//
LOCUS       WP_010599540             651 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Pedobacter agri].
ACCESSION   WP_010599540
VERSION     WP_010599540.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..651
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=70120
     Region          442..646
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 meennenqpi deiplaqsia gakilgiaqn gstnlfsisn irgdykgvan adtspglava
       61 gteyeatvgv typnflsvsn qpitipsein gkkvlsaklr aidpahweav ftpvdvslpi
      121 fsedgntyis knifnktted vghfidtdgt ykvysgtdvs csalidvsel dvitvsgvip
      181 kpvepianpy qfldangnvv sfgpmssfpk tiavpanavk frftlrwfqt disllnavqv
      241 esgnvatdfe sfgtytaita ingkkveapa eytksgsisk nlydksarvs gwyvdidgsy
      301 kqalvdspqn fsaspaitvf glahvtvsgl sgsfnpyqfl dmngsiigfg klsnpnttlp
      361 ipsnavklrf tdkfdtssna vfdtiqvesg esasqyvafa anktiskvng reieasylak
      421 gvkidgvdva tvaminanin tkdktilydg dsiskddrii qyvslklsst rinqavagtg
      481 wvdsngqtvg snpnnmyyrs qliashnpdl ivlwggtndf arsiplgspg tktnvltfyg
      541 gvwqtierir fqnpgvqili itpvqrnnpf efpgrdsmnn vnatlydyvk ilkevaaqla
      601 cpvldmyges gitseniird fandglhiym tpkgvqragd misskinqla l
//
LOCUS       WP_010599556             178 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Pedobacter agri].
ACCESSION   WP_010599556
VERSION     WP_010599556.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..178
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20219
     Region          2..155
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkitvlsmi tldgvmqapg gpeedlsggf eyggwsapfn deesgkimqk lmqpsdlllg
       61 rktfkiwedy wpkhtnywps intvtkyvls ttvtksdwqn tvfingiedi kqiknsdgsd
      121 lqvwgsseli qlllkndlid elwlfihplt lgkgknyllm vpfqplspfk rvllrqka
//
LOCUS       WP_010599564             175 aa            linear   BCT 01-JAN-2025
DEFINITION  DinB family protein [Pedobacter agri].
ACCESSION   WP_010599564
VERSION     WP_010599564.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..175
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20624
     Region          <89..157
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 mdhsikeilw nqlgasidml lnvisscpdd yfltnkrfyf iafhstifld yystispqdf
       61 spllsftqke lserpkeaig dlipdeiysk eeilkylkqi rekckriifs ltadelnkrf
      121 kegdqpddmd ypileillyn mrhtqhhaaq lnmllrqdld khiewsfrag diide
//
LOCUS       WP_010599567             683 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pedobacter agri].
ACCESSION   WP_010599567
VERSION     WP_010599567.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..683
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76510
     Region          29..667
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkstfttlll lccgisfaqi tkvdstrklk dvviqgyynt qpllrsvsav tlldsnqlkn
       61 qqntslvssf ntitgvrmee rspgsyrlsl rgsllrspfg irnikiyide lpltdaggnt
      121 ylnaldptai qsaevykgpe anifgantgg avlirsagld qnkieaslta gsyglfhqta
      181 niersfknys fsivegyqrs dgyrqnsgme rkylqtshrw nynnkgslkl fafysdlsyk
      241 tpggltltqm qqdpkagrpa tptlpgavtq qagiynqttf agitntyqls enfkhvvsif
      301 ttytdfknpf itnyekryes tlglrtfley ihskenlkvn aqlgiesagt ktqvrnfnnn
      361 ageatamqas dwlkanqdfa flrlnfdigq kllielassi nffnykyesi fpipvakqkr
      421 tfteqwmpkl aasyllnnsl slrasiskgy spptiaevrs sdnninnnlq aelgwnyeag
      481 lrfnsrnnrf yananvfqfe lrdaivrrln andteffina ggtrqkgiel etsfwiikne
      541 esfltgiqlr ssysyshfrf sdfqngntdf tgnkltgvpa nvivsnllfe skigvylfaq
      601 hnytsmipln dantafadky hlielkagir dlkmgktkie ffaginnlln ekyslgndln
      661 avgnryynpa aglnfysgla vkl
//
LOCUS       WP_010599578             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pedobacter].
ACCESSION   WP_010599578
VERSION     WP_010599578.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32960
     Region          35..98
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <197..286
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mktlkpsfei vepsfgssfy yskyvenenn kahlwhyhpe iemvfvnggt gkrqigshvs
       61 yytdgdlili gsnlphcgft dtntgnknet viqfkadflg aeflnlqesk wikalfnkak
      121 ggiafgeatk kavgnkiegm adqppfkrlm tllsvlksld sskdftilna tgfsmemqiq
      181 dndrinmifn yvkdhfqqqi sledvaemsa mtvpsfcryf kkitkktftr fvneyrvvha
      241 skllaekris itaislesgf nnfshfnkif heftgksase yrnelkliik
//
LOCUS       WP_010599638              63 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Pedobacter].
ACCESSION   WP_010599638
VERSION     WP_010599638.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..63
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6772
     Region          1..63
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mqqgtvkffn etkgfgfitp sngdaeifvh asglidnire ndtvnydvee grkglnavnv
       61 kva
//
LOCUS       WP_010599642             143 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Pedobacter agri].
ACCESSION   WP_010599642
VERSION     WP_010599642.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..143
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15972
     Region          68..141
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mikisitliv siacitsafa qdevkkqkss fhidslakek fdffsiekqp eypgglknfy
       61 qylgnsiryp kqaykdkvgg qvvlsfvvek dgsltnakvv rgvrddidte airvimqspk
      121 wnpgiqngkp vrvkyninvn fap
//
LOCUS       WP_010599673             125 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Pedobacter agri].
ACCESSION   WP_010599673
VERSION     WP_010599673.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..125
                     /product="VOC family protein"
                     /calculated_mol_wt=13731
     Region          11..124
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mlqtskafss fsvknieeak afyesiglkt kvgemgilel vidgaeniml ypkddhepat
       61 ftvlnfpvas ieqtvddlia kgvkfeqyhs eyiktdekgi srgsegpqia wfkdpsgnil
      121 svlev
//
LOCUS       WP_010599728             196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Pedobacter].
ACCESSION   WP_010599728
VERSION     WP_010599728.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..196
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22782
     Region          15..191
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 midqfknylk ekiqitdeqf dsistdlkik kfdkneiiqy tgditkhgff vckgllrays
       61 idskgkehil qfapenwlis drnsmnneas vffidaieat eviimpndfm eqaaiqvpcl
      121 qpmhtrllnn sirfmqkrin mllsataeer yldfiklypn ltlrvpqwmi asylgitpes
      181 lsrvrkelan khfrps
//
LOCUS       WP_010599764             450 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Pedobacter agri].
ACCESSION   WP_010599764
VERSION     WP_010599764.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..450
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47941
     Region          175..446
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          348..446
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(352..353,385..386,389,393..394,397,439,443)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mnystlkksv alslvaltgv atlavaqdap attsstkvfg grgqyrtwsi gvnagvlapv
       61 iaiggtndfd kwdvnlgygl nirkqlghsf alelagvrgk vsgtnnsvls ptstvrefet
      121 elqyavdlrg vvnlgsidfl rrensvgffl tagagylaya pkvtytngnv vdwkgraigp
      181 addrhdspkd yvkgfyipvg agvkfkvser vnfnlgytmn fvdadnfdgv yakgttkdkf
      241 sygyaglefs lgssakpsle wsnplatmyd elkdptlrqe vealknrvsn veksvedlkk
      301 dtdgdgvadq fdkcpgtpag tavdgsgcpl pkftaaadss nvtgfekigf dfnssvlkte
      361 syptldklss vlrenggkvt vngyassegt aaynlklskd ransvktylv nsgvnasqva
      421 tkglgeanpi asndteegri qnrrvetarn
//
LOCUS       WP_010599775             465 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: anthranilate synthase component I family protein
            [Pedobacter].
ACCESSION   WP_010599775
VERSION     WP_010599775.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Kerbarh,O., Bulloch,E.M., Payne,R.J., Sahr,T., Rebeille,F. and
            Abell,C.
  TITLE     Mechanistic and inhibition studies of chorismate-utilizing enzymes
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 763-766 (2005)
   PUBMED   16042594
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Dosselaere,F. and Vanderleyden,J.
  TITLE     A metabolic node in action: chorismate-utilizing enzymes in
            microorganisms
  JOURNAL   Crit Rev Microbiol 27 (2), 75-131 (2001)
   PUBMED   11450855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..465
                     /product="anthranilate synthase component I family
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53190
     Region          6..461
                     /region_name="TrpE"
                     /note="Anthranilate/para-aminobenzoate synthases component
                     I [Amino acid transport and metabolism, Coenzyme transport
                     and metabolism]; COG0147"
                     /db_xref="CDD:439917"
ORIGIN      
        1 myrinttykk lladtttpvs iylrlrdvyp nsillessdy hsrensmsfv cadpvagiil
       61 kgkrletyfp dgtvgitesk nlmqeiadfk dkfketelpe ikfissglfg yftwnavqhf
      121 ediqftsetp egeeipemqy hlyryiiaid hfkneitlfk ntfegeeegg lekmeyliqn
      181 knypeykfql rgeetsnltd qgfmdlvekl qkhiyrgdvf qivpsrafkq afsgdefnvy
      241 rclrsinpsp ylfyfdygnf klfgsspeaq itiknntani fpiagtfkrs gndiedaeqa
      301 kkleqdpkes aehvmlvdla rndlsrhcnr vevksfkevq yyshlihlvs kvsghlqenv
      361 safnvvadty pagtlsgapk ykamqliden eklgrnfyag aigfmgfned fnhaimirtf
      421 msknnelhyr agagivadsv petemqevnn kiaalrkale maegi
//
LOCUS       WP_010599778             359 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Pedobacter agri].
ACCESSION   WP_010599778
VERSION     WP_010599778.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..359
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41205
     Region          88..340
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mqyldhffgy pipifiknli igiaaillgl likfiihkif imlsrwwdsv iikstikhlr
       61 rpvavfipll llnssldimv mpasvrlhld kmleialtai falilirlin vledffylky
      121 dlnkennlke rkirtqlqfv rkfivsliil itaaiillsf esmrkigagl ltgvgiggii
      181 igfaaqkslg nllagfqiaf tqpiriddvl ivegewgrve eitltyvvvs iwdqrrlilp
      241 ityfiekpfq nwtrvsadll gtvflymdyt ipieplrqel trllttnplw dkrvnvvqvt
      301 dtnkdgsiei rflmsasnss rafdlrcnvr eamitfiqnn ypeslpktrl ehkdkfanl
//
LOCUS       WP_010599814             273 aa            linear   BCT 01-JAN-2025
DEFINITION  SOS response-associated peptidase [Pedobacter agri].
ACCESSION   WP_010599814
VERSION     WP_010599814.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..273
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=31513
     Region          1..232
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcyyngqrvt raefiqlkql ekavknydfl dtgvhngfny apcailvstd drrdfeiqqa
       61 ewgfipgyak dreeakkfrg myttlnfkae nlfkneagkk smwaeaarqr rclvlstgii
      121 esmhvptygk kgqllkatdk vpyqigivgk eyfwfagvyn dwfdkevgqw vrtvafgtta
      181 angimqqihn skkrmptilt ddlawewlme qpseerltei altqipsklm eactidkdyr
      241 fageatplny pdhpaldlsf vdqeqldfdh wrn
//
LOCUS       WP_010599943             158 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA thioesterase [Pedobacter agri].
ACCESSION   WP_010599943
VERSION     WP_010599943.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..158
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17665
     Region          7..147
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 martknhiel qflsepsdvn yggkvhggmm mkwidqaafa calqwsdsyc vtvyvggirf
       61 frpvhighlv kmeariiytg ktsmhiavda yskpvgksdf vknthciivf vavgddgqpk
      121 pipsfkpktd keiamhgyai klmelrksid kemepyiv
//
LOCUS       WP_010599960             360 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Pedobacter agri].
ACCESSION   WP_010599960
VERSION     WP_010599960.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..360
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39680
     Region          16..340
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mniktnegif rtvtsiilyt agliillwfl ykilsvvllg ifaivlgvii napvsrleqk
       61 gmkrwlasli vfliifgitf llgwmvvphl snqldvlign lpkyyasvsg yldnllskfp
      121 elrkevregg ssitsampsv gntvmgignf sfsviggifv fivficmvvf fvgnpkpive
      181 lyltvfpikq rekaenamkh tsvmlvgwmk snliggaiea vlvygfltlm nvpgalvwaa
      241 laffselipk igfyimaipp tlvalsvspa talwclvffl llnelvsdfl mpklrsstmn
      301 ihpmsslfll lamgtafglt gallatplaa iikayyeefy iskfpddpql ekrthdiiyp
//
LOCUS       WP_010599973             192 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Pedobacter agri].
ACCESSION   WP_010599973
VERSION     WP_010599973.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..192
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22802
     Region          16..187
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtaqdilkth lgqtidlsek dfdyvfshfk pisfkkgesi inigdvvnye yfvldgcikt
       61 fylndeqkmf ilqfamtnww asdynalyld vkatlmldci tdtqvlclsn qdreklcref
      121 ypmeyffrwr snkgyiaaqk rllsfmnnda kyryeelmqm ypqlynivpk qliaaylgvs
      181 retlsrmyek kq
//
LOCUS       WP_010600019             390 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Pedobacter agri].
ACCESSION   WP_010600019
VERSION     WP_010600019.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..390
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43907
     Region          104..370
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mfdsaffdqe fwgntvkdyc lfggillfgl ifkrifskll skllfklfks fsqqshdeaf
       61 vallvkpiet fillatlyls inqlkhplev aifhysklvg ktkeaipvsi gdcidriflf
      121 miilsvfwii lriidfishv llfkaslthn ksddqlvpfl kelfktivvf igfftllgfv
      181 fevnvltlit glgiggiaia laakeslenl igsftifldk pfvvgdlvkv dgvegtiekv
      241 gfrstrirts ektmatipnr gmidgvlenl slrnlrkvaf iigltyetna esvkkivsei
      301 edyinqrdgt adgnahfksf gdsglnieis yfvtildnaq flkirqeinl eimdiivrnk
      361 sdfayptqrl isdrplnddh dkevgndatd
//
LOCUS       WP_010600069             171 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Pedobacter agri].
ACCESSION   WP_010600069
VERSION     WP_010600069.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..171
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19544
     Region          6..166
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkkrlfgemi vnhsdtlssf alkftrdeqd akdllqntfl kaldnyemyr edgnlggwly
       61 wimrntyind frkltasrsl aglvanicsa elldvaefnl iegafikddi qkaierispi
      121 yavafvrhfe gykyeeiaas lsvpigtvkr rihsarmqlq kalnqysccd n
//
LOCUS       WP_010600081             185 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Pedobacter agri].
ACCESSION   WP_010600081
VERSION     WP_010600081.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..185
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20140
     Region          6..168
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 meknrkivgl cgslrkgsyn amllkfagtl vpegiefeiv pfddipvyna dddtpevaer
       61 pasvvkfraa laqadafiia speynysipg glknaidwas rgkdaplmhk pvamlgatqg
      121 mwgtvrmqta flpvftflnm npvlqpevli aqaqtkfdea gnltdektis likrkienli
      181 vaskv
//
LOCUS       WP_010600071             466 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Pedobacter agri].
ACCESSION   WP_010600071
VERSION     WP_010600071.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..466
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51107
     Region          149..439
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mnklgrdikn ieelatqqlv lkkeieagkn riknavqeaa weipvtitqn ltktpfernl
       61 eslsdpagkl lpelssllvn kiiprkvgff krimltsatk flirkalkpy atvtapkpep
      121 ikqlrvprlq mtspalkiqa kentenptak enkrislkgl wqvlktsftg fgdhkvtkis
      181 gslayytvfs mgpllvviis lcgifmkkea aqgkvfeqlk gflgsetalq lqeiiksagl
      241 gdkgtiafii glitlllgat tvfgdiqdsi ntiwgikpkp krgwlkmlqn rflsfsvivs
      301 lgflllvslg vtavldgfsn rlqnrfadvs vvffyilntv itlgvvsaif avifkvlpda
      361 nikwrdvaag alvtgvlfli gklgislyis ksdvgstyga agslvvlllw tyyssiilyf
      421 gaeftksyav aygseilpnh yavtikeiev eqgsksvqdt hveddk
//
LOCUS       WP_010600092             403 aa            linear   BCT 01-JAN-2025
DEFINITION  dipeptidase [Pedobacter agri].
ACCESSION   WP_010600092
VERSION     WP_010600092.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..403
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44543
     Region          43..402
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mdeikrectr rrflvtmsaa saalivdpfs swawlsddek kvaktfgidt hnhidvplls
       61 selpgpeidl igqmknsgls aivmtfavdy qklteqgqay drflngltam dsalehnkmk
      121 rslnlsdlks ahqkktptvi qsvegahfle gkidrlkvay drglrhltll hdndasvplg
      181 diftnspkwg gltafgaqvi kecerlgilv dlshcdnnti ngalkvmtkp fiishtglnt
      241 rlgdkefmak mmkprliskd qakivadagg vigiwthlad tptafadnik amvdivgidh
      301 vaigtdtkmt payrspndkw eqpkerpgqn kddnnfnkdd kpkgnenkkq cgdttnnvwg
      361 gekqcfyftv veallkagyt ekeigkiggg nylrifdevt kgy
//
LOCUS       WP_010600114             292 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Pedobacter agri].
ACCESSION   WP_010600114
VERSION     WP_010600114.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..292
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32918
     Region          130..277
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(136..137,194,198,234..236)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mkyklltiia agiilftscq snsqtgntdg tdstgqvtkt aentsapvdi skikvadakt
       61 ilarkqvpil cyhqvrnwkp tdgkvgkdyi veiqnfkdqm kmladsgyht ilpdqlyayl
      121 ntgaalpskp imltfddtdl dqftivnptl kklgykavyf imtvsigkkg kfvdymssdq
      181 ikqlsdegnv igshtydhkn fkkytgkdwe eqldkptkrl eeitgkkmte faypfglwna
      241 egipelkkrg frmayqlstk rdekdplfti rriiasgyws pktlsnsikn sf
//
LOCUS       WP_010600144             376 aa            linear   BCT 01-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Pedobacter agri].
ACCESSION   WP_010600144
VERSION     WP_010600144.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..376
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41107
     Region          3..376
                     /region_name="ArgD"
                     /note="Acetylornithine/succinyldiaminopimelate/putrescine
                     aminotransferase [Amino acid transport and metabolism];
                     COG4992"
                     /db_xref="CDD:444016"
ORIGIN      
        1 mqlfdvypln nieitkasgs nvwdaneqky ldlygghavi sightnphyv srltnqlnkv
       61 gfysnsvkip lqvqlaeklg qvsgkkdfql flvnsgaean enalklasfy ngrkkviaft
      121 gafhgrtsla vavtdnpkiv apvnqtenvi flpfnneval eetfksqgde isaviiegiq
      181 gvggikeask sflqkirslc deynavyiad svqcgygrtg lfyshdysgv eadvytmakg
      241 mgngfpvagi siapkfkpwh gelgttfggn hlacaaalav levmekdnlm knaeeignyl
      301 itelkkfeqv kevrgrglmi gielpeelah vkkellfkhf iftgeakpnv irllpalnlt
      361 kahadeflaa fselvk
//
LOCUS       WP_010600197             419 aa            linear   BCT 01-JAN-2025
DEFINITION  anthranilate synthase component I family protein [Pedobacter agri].
ACCESSION   WP_010600197
VERSION     WP_010600197.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Kerbarh,O., Bulloch,E.M., Payne,R.J., Sahr,T., Rebeille,F. and
            Abell,C.
  TITLE     Mechanistic and inhibition studies of chorismate-utilizing enzymes
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 763-766 (2005)
   PUBMED   16042594
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Dosselaere,F. and Vanderleyden,J.
  TITLE     A metabolic node in action: chorismate-utilizing enzymes in
            microorganisms
  JOURNAL   Crit Rev Microbiol 27 (2), 75-131 (2001)
   PUBMED   11450855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..419
                     /product="anthranilate synthase component I family
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=47339
     Region          24..416
                     /region_name="TrpE"
                     /note="Anthranilate/para-aminobenzoate synthases component
                     I [Amino acid transport and metabolism, Coenzyme transport
                     and metabolism]; COG0147"
                     /db_xref="CDD:439917"
ORIGIN      
        1 mkntdhtsaf kqkalhwanq fdvcclldsn qypdvysayd filaadvqae iqcnsgnafe
       61 qlkafqeank qwlfgffsyd lkneiedlvs nntdhlnfpe lyfftpkyli avkngmakvl
      121 igddavlnei nnftieeses tshlnierrl sktaylnkii klkehiirgd iyevnfcqef
      181 faenakinpv etfgllndis ptpfagflkv nehyilsstp erflakrgsk lisqpikgta
      241 rrsadskede qikiqlrndv keqsenvmiv dlvrhdltks avkgsvkvee lfgiysfpqv
      301 hqmistitce ldsaihfida iknafpmgsm tgapkvkamk lieqyeetkr giysgsfgci
      361 spdgnfdfnv virsilyhsa nqylsfqvgg aityhsdaek eyeecllkas ailkvlnae
//
LOCUS       WP_010600261             400 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Pedobacter agri].
ACCESSION   WP_010600261
VERSION     WP_010600261.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..400
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45161
     Region          53..400
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mentftvnsl qgsivalvgf sqdtslfala ecsfsgmqvt lfdngmklvq ewaakrlpia
       61 aiisngeils nnglalletl kknqlaevpf flvvrhfnan lrilalgsgv advfrlpidt
      121 erlekrlvfl vqnwvllkkg fsvqaktvyr vgaakrafdi lfagvalill lplfiiiafl
      181 iqlesagpvf yyslrsgtgf rifkfykfrs myvnadqrih elkhlnqyds ereikdtqtg
      241 hselcssckq igkcqypmya dgaqwcekny dyiiaqksgs affkiandpr vtkignfirn
      301 tsidelpqlw nvlkgdmsiv gnrplpiyea erlttdryvl rfaapagitg lwqvekrgkg
      361 emseeerlml dnayamnqsf wndiklilkt ipalfqkenv
//
LOCUS       WP_010600279             207 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Pedobacter agri].
ACCESSION   WP_010600279
VERSION     WP_010600279.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..207
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23699
     Region          4..196
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mkqiyiirhg etelnrqgiv qgrginsdln dtgraqaeaf yqkykdisfd kiytsdlkrt
       61 wqtvqkfids glpwerlsgl delawgvweg kpnseaarea fremletwqt gdytahfdgg
      121 esvqdvyerl kqpmevlstr pdeetvllcm hgramrvflc lllnkplsem tefphqntvl
      181 yklgfedgkf tvlefnsavh ldglvig
//
LOCUS       WP_010600284             155 aa            linear   BCT 01-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Pedobacter agri].
ACCESSION   WP_010600284
VERSION     WP_010600284.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..155
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17985
     Region          19..138
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(49,52)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mriffiicls lvtysvnaqv rlltlddldk rvakgkdtty vinfwatscs pcvaelphfe
       61 klrtenekkp lkvllvsldf ksklqrevip fvnnnnikae vyllnepdqq kyieridkkw
      121 sgaipatlfv nkkvrrfyek eftaeelkst llnlk
//
LOCUS       WP_010600330             352 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar kinase [Pedobacter].
ACCESSION   WP_010600330
VERSION     WP_010600330.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..352
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39164
     Region          <7..345
                     /region_name="trifunc_aldol"
                     /note="KHG/KDPG aldolase/sugar kinase fusion protein;
                     NF041633"
                     /db_xref="CDD:469516"
ORIGIN      
        1 msdqisslak qgekvlsfge illricpdmd gqwlkesklp fyvggaelnv atalalwnvp
       61 saylsampdn svtreiedyl kvrnidtspm vfhgdrlgly ylpkgkdlkn agviydrans
      121 syadlkvgqi nwdevfngvt wfhfsaicpa inqsiadvcl ealkaasern itisldlnyr
      181 aklwkygkdp idilpelaky ctlimgnvwa ankmlgtalh edllptegya ketllqqatd
      241 takeilslfp ackavantfr fdhgkgiryy taiytedqlt vseeyvseei ldkvgsgdcf
      301 magliygfyn hlpveetlnf ataaaydkly ipsdattstv adiekriirh dk
//
LOCUS       WP_010600285             201 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Pedobacter agri].
ACCESSION   WP_010600285
VERSION     WP_010600285.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..201
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21732
     Region          26..198
                     /region_name="PRX_like1"
                     /note="Peroxiredoxin (PRX)-like 1 family; hypothetical
                     proteins that show sequence similarity to PRXs. Members of
                     this group contain a conserved cysteine that aligns to the
                     first cysteine in the CXXC motif of TRX. This does not
                     correspond to the peroxidatic...; cd02969"
                     /db_xref="CDD:239267"
     Site            62
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239267"
ORIGIN      
        1 mknlfligll lvssvafaqt ngykvgdvvk dfslknvnnk tvsladyqna kgyivvftcn
       61 tcpvakayqe rvsnlnntfa atgypviain pndagavpge sfekmqvlak eknfsfpyll
      121 dpehvvtkqf galktphvfv lsktgngnvv eyigaidnda egdnpdkvny venaikelsa
      181 grnptvsftk avgcsikwkk e
//
LOCUS       WP_010600365             298 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pedobacter agri].
ACCESSION   WP_010600365
VERSION     WP_010600365.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..298
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32374
     Region          3..291
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdfdviiigg syaglsaala lgrakrnili vdagkpcnrq tphahnflth dgdrpaeisa
       61 qakvevlqyp tvkfidgtvn aakkitggfs vvvnelisys srklliatgl kdvfpnikgl
      121 aecwgisvih cpychgyevs gekigllmng diayemaknv nhwnkdltll tngkseltae
      181 qtnklksksi kiietgiael ihhdgelerv vfadgtilkl kaiyaktdve qhidfhqqlg
      241 fdltefktik vdeqqqttak gvyaagdctt lmrslsvita agtiaavmin kemiaedf
//
LOCUS       WP_010600369             111 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Pedobacter agri].
ACCESSION   WP_010600369
VERSION     WP_010600369.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..111
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12283
     Region          9..102
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 miaentqiqm rkgileycvl siisrgeiya sdiiaelrsa kllvvegtly plltrlknng
       61 llsynwvest sgpprkyytl tevgkdilsq ldqtwqelay avgvsqegak s
//
LOCUS       WP_010600393             527 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Pedobacter agri].
ACCESSION   WP_010600393
VERSION     WP_010600393.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..527
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=59417
     Region          <47..>161
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(68,70,74,76,89..91,93..94,98,101,110,112,114,
                     118..119,122..124,126..127,131,134,143,145,147,151..152,
                     155..157,159..160,164)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          68..110
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          112..143
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          244..523
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          270..297
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          304..335
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(403..404,406..407,411,414,427,429,431,435..436,
                     439..441,443,447,451,454,463,465,467,471..472,478..480,
                     482..483,487,490,501)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          429..463
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          465..501
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mnlyqieqay iqgrdlaein elykteiadi teeqqvevwr qvcgfvnvem vdyliakgwr
       61 tagvedsngd tllhflatpl rsydyfiaek rvyectkkll eakvsplrkn sqgetalmla
      121 akigytemle ayaetgakid fndrngntil hilasnsssa isdyeksler lmihqrdeny
      181 dennqrhlqe rrqlewrhhv dkarfnqfit faivgrefgi dplqrnnekr tavevaigqk
      241 sksigailkg vdfndqekvs lyfnaggmdl hqacaekdle aidaliklge nvneiydkeg
      301 drfngmtpla iamqkhsvei tdlllkngad attvdskgwh pfrhlydins tiavhidlfh
      361 nkvfqkilka yldagfdins llddeentll tlsakyadrl mmhnsytisk vlldeatyag
      421 advnktnrdg isalmylcat glergeksll tlleqgaste lidkngktal iyavnndrks
      481 daqtycelma efgdllidak dntqqsaldy vvakdnealv awlvgkm
//
LOCUS       WP_010600395             354 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Pedobacter agri].
ACCESSION   WP_010600395
VERSION     WP_010600395.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..354
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=39716
     Region          <33..208
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          71..101
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          103..135
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 makkkktlpk dfreildakd fesfkkvfdt ceidarggyg kttalsfyri pndfvrwlva
       61 qgadleavdn yqrtalheqa sirggdvsvf lelganvnav dtygatplhf atghgfnvda
      121 vkklieygan vkavddyeqt plesalsnar nmdlqalaki ssillsadnn itqkmkdavv
      181 kkgedfefhr enfnkdylqe teqaldqlyk ifhvppvkrr lmhdgvspik vngttwqeqy
      241 ealwellips sgsaktlqge vvriagkvrd eihrngggnw nadfkkmlda fglhlktens
      301 latadlekad liikdirkng dgdddelhfl celatkwvlk npnpvrlekp aykr
//
LOCUS       WP_010600456             251 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Pedobacter agri].
ACCESSION   WP_010600456
VERSION     WP_010600456.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..251
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28338
     Region          2..125
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mmqhidvlia ednlidqkll sayleeydit hiivdsgeea ikilqsvtfk lllfdislpg
       61 idgyqltkvv keemkittpv vaitayside akdkcfasgm nacfskpisk ielvgmltqf
      121 lpkekltsah srdfevidls ylkeislgdv dyemeitnkf vetiesdlle lensfhskna
      181 eqlsvvahrt lstiyimglk sklestlcai eqddltysel ktnlehvyet craakieakl
      241 fiedlrncks y
//
LOCUS       WP_010600405             544 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Pedobacter agri].
ACCESSION   WP_010600405
VERSION     WP_010600405.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..544
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61868
     Region          4..532
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 minvnnisvs fggttlfsdv tfsinendki almgkngagk stilkiiadv akptsgsvtg
       61 pkdaviaylp qhlltedklt vfeetmkafq evnqmqkeld elneqltvrt dydsddymkl
      121 iervselsek fysieevnyd aevekvlkgl gferkdftrq tsefsggwrm rielakillq
      181 kpdlilldep tnhmdiesiq wledflinsa kavmvishdr afvdnitnrt ievtmgriyd
      241 ykakyshylq lradrrihql kayeeqqrfi adnqefidrf rgtysktlqv qsrvkmlekl
      301 evieidevdt salrlkfpps prsgqypvmv eeltktygdh vvfqkanlvi ergekvafvg
      361 kngegkstmi kaimgeidfe gslkvghnak igyfaqnqaa lldenltvfd tidqipmgeg
      421 tvkikdllga fmfsgddttk kvkvlsggek trlamiklll epvnvlilde ptnhldmktk
      481 diikdalkdf dgtlilvshd rdfldglvek vfefgnkrvr ehfedikgfl aykkmdslke
      541 iekn
//
LOCUS       WP_010600461             223 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Pedobacter agri].
ACCESSION   WP_010600461
VERSION     WP_010600461.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..223
                     /product="YceI family protein"
                     /calculated_mol_wt=23646
     Region          1..222
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mrklifalpa lfllascggs sndnakttse qtaaeqkget ltldtvgtkv dwkathkggl
       61 aprwgkisvt sgtvsvnkds lsggeftinl aslyvdpasv tekdkkstdl aghlkspdff
      121 dvakfptakf vitkvepftg aqpsslltdp nylisgnltl kdstlnitfp skvaiagsdv
      181 tatakfiidr sawginykae gspenwmisk dveigltlka kkn
//
LOCUS       WP_010600483             492 aa            linear   BCT 01-JAN-2025
DEFINITION  xylulokinase [Pedobacter agri].
ACCESSION   WP_010600483
VERSION     WP_010600483.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..492
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53736
     Region          2..436
                     /region_name="ASKHA_NBD_FGGY_BaXK-like"
                     /note="nucleotide-binding domain (NBD) of Bifidobacterium
                     adolescentis xylulose kinase (XK) and similar proteins;
                     cd07809"
                     /db_xref="CDD:466809"
ORIGIN      
        1 myllgidigt ssikvavvdv etqksiatvq ypeaeteiks vrpgwaeqsp adwwentkla
       61 ilklnatnlf npkniaaigi ayqmhglvvv denqdvlrds iiwcdsrave igekafdqig
      121 hqnalsslln spgnftaskl awikenephi yrkidkimlp gdfismkltg nittsisals
      181 egifwdfqqd kiskavmdyy gldynfipei nelfashgvl teeialflgl tagipvayks
      241 gdqpnnalsl nvmkpgevaa tagtsgviyg vsnsltydpq srvntfahvt yspeekntgv
      301 llcingtgsm frwakntfap hlnyqelntl aakapigskg lnvlpfgnga ermlnnqytg
      361 aqflgidlni hsqaeifrav qegiafsfry gidimreigm epkviragra nlflsevfaq
      421 tfvdvtgvrv elyendgsvg aalgagigag ifntaedaft hhevvatldp knsaayepiy
      481 qewksllmkt lk
//
LOCUS       WP_010600554             259 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Pedobacter agri].
ACCESSION   WP_010600554
VERSION     WP_010600554.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..259
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27639
     Region          6..253
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mayqnllsev kdnilyivin rekalnalnk etlqeladvi afaekneevr gviltgagek
       61 afvagadike fsnyngtqge elarkgqenv fnaiensskl fiaaingfal ggglelamac
      121 hiriaadnak lglpevtlgl ipgyggtqrl tqlvgkgkai elittanais aveaekiglv
      181 nytvpqadli nkareildiv kqraplaisa aiqavnasin tdhgfeteik afgkcfetdd
      241 fkegvtafve krpakfsgk
//
LOCUS       WP_010600585             436 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Pedobacter agri].
ACCESSION   WP_010600585
VERSION     WP_010600585.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..436
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48419
     Region          25..431
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mskkfkiaif lfslsisgfa qeklslreai sialqnnydi kiskneidia knnanignag
       61 mlptidgtyt nggsiqntrq tpvtgedrvi rgarstnnsy gadlnwtifd gftmfanydr
      121 lkelqkqgev narltilttv sdviaayydv vrqqqlliaa dsaidvsvwr tniaktklel
      181 grgskldvlt aqvdyntdts nfiqvknflq iakvrlnqlm vrdigtgftv adsidvdrgi
      241 lfskqaeiae qqnpnvqnaf inqkiaalnl ksikgarypa iilnsgysra kstsptgfnq
      301 rfaangftyg vtaslnlfng flqrqqerna kidienstln lsktkldvns qlltayqnya
      361 tyldlikleq rnvdiakenl ditmakyrlg siaplelrea qrnaidaqnr fiemqfqaki
      421 aettlkeisg nidlsn
//
LOCUS       WP_010600614             230 aa            linear   BCT 01-JAN-2025
DEFINITION  CAP domain-containing protein [Pedobacter agri].
ACCESSION   WP_010600614
VERSION     WP_010600614.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..230
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=26627
     Region          <106..221
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
ORIGIN      
        1 mtklvlpflf limlsaglsa qtwtdaefrs antaanvpyl sneeknivmy mnliridgek
       61 fyytfledyi nnynakvkky rnyhqlkiar nntyyvsllk hlqavknlpl yypdekltll
      121 sknhaqdlnk nnidthessd gtkfakrlar yfpnknmsen idfgysnsid ivchllldcg
      181 vpslghrlni ldqknkfntv gvgiqrhpty twcavidfvs qpiyytnnqr
//
LOCUS       WP_010600690             111 aa            linear   BCT 01-JAN-2025
DEFINITION  Rieske (2Fe-2S) protein [Pedobacter agri].
ACCESSION   WP_010600690
VERSION     WP_010600690.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..111
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=12349
     Region          1..103
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mkwfkalnkv qiptvgdskt ielggkqlci innddeiiat qsfcphaggh fsggwckngh
       61 licpihryay dlktgrgaeg qgdyiniyat elredglyig feeswwsklw g
//
LOCUS       WP_010600813             215 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Pedobacter agri].
ACCESSION   WP_010600813
VERSION     WP_010600813.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..215
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25135
     Region          28..207
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnlenefger kwdefggisp lialfksyhp lnpeiekiin eqtfpvrfdk nkhiasplkr
       61 nryiylilqg svhgyikmgi ekvttwiaie helagtirnl wteeaseeyi esidpvlaia
      121 iphamsrqly qqfpianyvg rkmteiyfks aserafisrl ptakkryery litysylvdr
      181 vplkyiasfl nmrletlsri ratiaketek ilter
//
LOCUS       WP_010600842             212 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Pedobacter agri].
ACCESSION   WP_010600842
VERSION     WP_010600842.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..212
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23953
     Region          43..212
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mslinddlqq lllnycepes ellqhidret nlkvlmprml sghyqgrvls mlskmvtpkr
       61 ileigtftgy atlclaegls adgliytldi naeledmvra nfeksplnsk ikyilgdane
      121 tlnqldevfd ivfidadkkn ngtyydlvfd rvrpggiliv dnvlwsgkvl qekqdkdtrn
      181 itsfndkiaa derveklilp vrdglfvirk ig
//
LOCUS       WP_010600849             144 aa            linear   BCT 01-JAN-2025
DEFINITION  ester cyclase [Pedobacter agri].
ACCESSION   WP_010600849
VERSION     WP_010600849.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..144
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16389
     Region          15..135
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mdnqveknka ickvffdelf nnanldaidq fvdsgvkvhk tfpwqregak afydtievfk
       61 lgfndlkirf ddvlgdgdkv vakftvsgth ketflnipat gkkveyeevn ivrfrdekii
      121 ehwvvadtys lmqtltggev hqli
//
LOCUS       WP_010600862             105 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Pedobacter].
ACCESSION   WP_010600862
VERSION     WP_010600862.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..105
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11795
     Region          1..105
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mkeisvqelk ekidnkedfq lidvretfey evsnlngeni plggiliead kvskdkpviv
       61 qcrsgkrsaa avmqleaqyg yenlynlkgg ilawqeafdp nmpvy
//
LOCUS       WP_010600781             111 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Pedobacter].
ACCESSION   WP_010600781
VERSION     WP_010600781.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..111
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12990
     Region          13..111
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(14..16,30,47..49)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mpykerdink myytmgevte mfnvnasqir fyekefdilq pkknkkgnrl ftpedienlk
       61 iifnlvdekg ftlkgakehl knnkgdvken qkiidslekl kgflmnlaqe l
//
LOCUS       WP_010600901             329 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YihY/virulence factor BrkB family protein
            [Pedobacter].
ACCESSION   WP_010600901
VERSION     WP_010600901.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..329
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=37316
     Region          32..312
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mewlhrqllh lkiyskfiew tkgcvlpgfs plplytvatf ffreigkdtl vnkssslays
       61 fmlaifpgii flftlipfip ikgfqdqlln lielvlphna ynafestlkd iiknqntgll
      121 sfgflsaiff atngvknlmk afnkssliie trgwlkqrli afiltsvicl siivcisama
      181 igevalnyik gelhikdsla vyaiqftrws llailyfiti silyrygpsh akkwklfsag
      241 swlatilafi tiwgfsfyin hfasynkvyg sigtlivvmi wlylnslill igfelnasvd
      301 vskrsvkiir ptfnlfkksd piegniqkk
//
LOCUS       WP_010600343             296 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: bestrophin family protein [Pedobacter].
ACCESSION   WP_010600343
VERSION     WP_010600343.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..296
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33959
     Region          7..296
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mlliqnirls rilrntwhvd limiasctaa yfireyliah hfviptiipt vlgtaiaffi
       61 gfnnnqaydr wwegrkiwga ivndsrsfar allnyidedp vsakrmiyrh iaflyalkas
      121 lrgavdeiyi kylseedlke vakhtnvhna ilniqsrdlq klskanqidg frfieineml
      181 vrfsdsmgms erikntifpt tytyltkvfi wlfvvtftlv isqdagpasi flgwligfvf
      241 vstqingmsl vnpfennsag vplnqitrti einllqmlee tdipepikpi neeyil
//
LOCUS       WP_010600925             343 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Pedobacter agri].
ACCESSION   WP_010600925
VERSION     WP_010600925.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..343
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=37592
     Region          39..331
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mkityiitpt lkikftifll ltyfassaqv lkkrttllmg skfeitivak dsetasrnid
       61 sviaeitrie ylisdwkpet qisevnrnag ikpvkvdqev feltkralhl stitngafdi
      121 sfaamdriwk fdgsmtempt aeaikksvek vgyqniilds lnntiflklp gmkigfgalg
      181 egyaadrcrd mmlakgikag ivngsgdmss wgkppkgknw vigitnpfqk dslyaivplk
      241 ngavvtsgsy ekfvvfngkr yahiinpttg ypatgltsvt vfgpdaalan gfstsmmvlg
      301 kkaalefirs fpayscilfg ddgkvyhsen itekmlakwk kgi
//
LOCUS       WP_010600931             406 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Pedobacter agri].
ACCESSION   WP_010600931
VERSION     WP_010600931.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..406
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47939
     Region          81..235
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mglnylafai paffifvyie ykiaqnqkrt tifkyestva nfsigiaerl lnlfiaasfy
       61 qlydwvyrny alfdissawy vwvlillatd fvwywyhrlg heinflwaah ivhhqseefn
      121 lsaaarittf qalfrnifwc vlpfvgfhpt miitillvhg aysffthtql vgklgwlehv
      181 fitpslhgvh hasdekyldk nygdvfvfwd klfgtfqtee eppkfglthp lksysflwqh
      241 fhyyleigea ykrangfkak wnalfgspal mdqnirpile rkfrqdkikq qskprfkfyl
      301 ntqliivvam ltgltlyfnl mnitdqlail ffiiitlini galleqrkwi yylecfrlil
      361 vlaylfysfn ifglvvfpia aliflertis lskiyikyvf ayqsik
//
LOCUS       WP_010600945             708 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Pedobacter agri].
ACCESSION   WP_010600945
VERSION     WP_010600945.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..708
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=76427
     Region          12..708
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mekrvlkdan drvdgiykvt gkakyfaeye lpgltygvlv tstitkgkit sldtkaaeka
       61 pgvvsvishl nkpsapayeq eggspfkify tdkiffngqp iaivvantfe ratyaaslvk
      121 vtyakedfnt dfekavtdvk akklqgqpey krgvenaykt aevkieakyh lpiethnpme
      181 lhgiiadwrp nnqvtvyakt qgvkatqgti anvfkipien iqvnsefvgg gfgmalrtwp
      241 leiatvmask hiakpvklvi trmqmftmvg nrpaavqtig lgankdgtlt githrafget
      301 sayenftegv vnmakfmyqc dnvntqytvv pvdlgvpiwm rgpgeatgaf alesaidema
      361 haldmdplef rikndpekdq qrnkpfsdkn ikeayrvgaq kigwnerknk pgslidgqwk
      421 ygfgvsigvf nanrgrasvk gilkadgtlv lqsatsdigp gtgtgmtlia skllgipgdk
      481 ikfelgdssl ppapsqggsa tlstvgsavn dvcvslksti aelaansnmd atsnfvdvlk
      541 knnlpqievt kqsqagkere dysmysfsih fvkvkvhslt gvvkvdkivs vgdsgsivsp
      601 ktarsqmvgg avggvgmalh eesiidhryg ryinnnfady hvpvnadipe ievhfinkpd
      661 pyinpmgakg mgeialigfs aavanavfna tgkrirtlpi tpdkvlag
//
LOCUS       WP_010601057             330 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pedobacter agri].
ACCESSION   WP_010601057
VERSION     WP_010601057.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..330
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36730
     Region          1..324
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msdtiisvkn ltkqyqseqa ggiknisfni nsgdvvaiig esgsgkstll ksifgllktd
       61 egdvffedkr vlgpdeqlip ghkqmkmvtq dfslniyakv ydniasqlsn tdlktkaekt
      121 laimehlril plqnkkiiel sggeqqrvai akamvadtkv llldepfsqv dallknqlra
      181 dikrvaaetg vtvilvshdp adglfladql lilrngellq tgkpseiyqh pkhiytaqil
      241 gnavvlsrgd aekiglktfs gnvvfypewa eissnwssrr fevkdvyykg fydelllern
      301 gvtvralqln rgehkkndhv qlnisrflef
//
LOCUS       WP_010601077             605 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Pedobacter agri].
ACCESSION   WP_010601077
VERSION     WP_010601077.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..605
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=69888
     Region          9..596
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mnhsrrpfqp ienygiignl ktvalvslqg sidfmcapkf dsptvfatml dsqrggffav
       61 epdlknftsk qlylpgtail ltryfsdsgi aeltdfmpiq kgnktltsai vrqiktvrgs
      121 ikfkvscvpr fgysesdhev eclekeirft saeeklqikm lsdkpltvrk kngyaeftlh
      181 etevativle flpedhqgqe lefyqqdayh qtkdfwvkwi nktsydgrys elirrsaitl
      241 klltsaefgs avaaptfglp eaiggnrnwd yrftwirdaa ftmyaflklg ffdeatafid
      301 wifnlcqkid lqlvyqidgn pklhekelkh megyraskpv rigneaatql qidiygelid
      361 tiyiynksyk pityefwtli ekqivqvikn wkkpdhgiwe irsekkeflh trlmcwvamd
      421 raikiaehrs fpypenewhq vrsdiyndiy hnfwnekrga wvqykgaehv dasvllmplt
      481 hfispieprw lstlkaidee llvdvlvyry nngmtkidgl dgeegtfnmc sfwfiealak
      541 sgeveraven fekmigysnh lllfseelgk kgehlgnfpq afthlalisa avelnkqigr
      601 rtskl
//
LOCUS       WP_010601078             750 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Pedobacter agri].
ACCESSION   WP_010601078
VERSION     WP_010601078.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..750
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=84731
     Region          1..750
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mssfvasaqq nlvqyvkpii gtskmghtyp gatvpfgavq lspetdtlsy evngkyngdv
       61 ykycagykye dktitgfsht hfsgtghsdl gdflimptqg klqlnpgtad npkagyrsay
      121 shanekveag yykvkldddn itaeltatnr vgmhqytfpk sdqshiildl magiynyedk
      181 tvwtyvrvvn dtlvtgyrqt ngwartrtvy famsfskpfk nygrksydak qayrgfwgkf
      241 nqdqnfpeia gkklkmyfdf dtqegekvki kfalspvsqe nalqnmrtei sgwdfekvkt
      301 qaqttwnkel nkiqvntsnn nkinfytaly hsfinpttyt dvngeykgld qgihkaegfi
      361 nyttfslwdt yralhpffni mqpgrsndmv ksmmahydqs slkmlpiwsh yandnwcmsg
      421 yhsvsvlada iikgtyngda nkaldacvtt akhrdyegig yymdkgyipa ersgvsvsnt
      481 leyayddwai aqlakklnrm dvynefikrs nnwrnnfdsa sgfmrprlad gsfkkafdpk
      541 dtegqgfieg nswnysffvp hdpaslvevm ggkkkfaarl dslfsmhlpd effahtedit
      601 regiiggyvh gnepahhvay lynwtdevyk gqaqirhiln mqykptadgl ggnddcgqms
      661 awymfsamgf ypvapgsdvy slgsplvnna vinlengktf tveaikqsdk nvyvqkvlln
      721 gkeitnhqik haditnggkl tfymsakpkk
//
LOCUS       WP_010601100             408 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpP1/FadL family transporter [Pedobacter].
ACCESSION   WP_010601100
VERSION     WP_010601100.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..408
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43985
     Region          17..408
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mmkklllsal laaplwvlgq gfqvnlqgqk qigmagagsa laldeasvff npgavsflek
       61 nsisagvnpl lfksafqqng snitehvknk iappfeayav wgpksnkwkl glgvytpfgg
      121 lvdwgnewsg ryaltslnlk aiyfqptlsv kitdrigiga gfvynhgdvn lqralpvnya
      181 dgrsghatle gtgsgygwna glyintlsni tfavvhkskv vtklndgtat fdvpeslrss
      241 fpagntfnae lplpstttlg igiplsqstt lafdaswvqw rvyeelafdy avntpvladt
      301 rsarnyrdgs sfklgvnhka seklalragi gyafspvqdg yvtpeapdad ryilsagvgy
      361 aptsrfevna sfffedvksr kqknietgld gtfktlvyap glsltykw
//
LOCUS       WP_010601116            1005 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Pedobacter agri].
ACCESSION   WP_010601116
VERSION     WP_010601116.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..1005
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=114354
     Region          4..>351
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mqdkegrila vnqlklwdhq kdalkdiidy inafdiksfl vkmptgtgkt gvfsalsrva
       61 ypdlnfliit pstalkfqil kevqekfwnk iakpiselpd qvvepllpkd aveviskieg
      121 kksiivttiq alqyisands vsfeaikknt dciifdeghk epaytwgetv rsfrkptvlf
      181 satpyrndyk ifnvdkekff sldhskceqa kilraleiqq ldlstlnpst fvnavlakll
      241 vviqilngqg iaqprtiirc enqsdiekiv aslkklkkra vgihqnfkdk ndllsevpdt
      301 agqqkydffv hqfklvegid npefsivaly apfkssrlli qqigrvlrnp elqpdrsayl
      361 fgldaqglkk ewksyldydk mvdkrkklyd itdvlkvnke astlyfdgsf relvnvseis
      421 lsksilfqkk vnayfhdgsl ifnelsenll eewgrrdysi lkheltspnc liilyikyen
      481 splvkdgvfi eqklaatmlr mdkshifyyd seqnnpmrqi edlapvsren lvklfknkrn
      541 iskvflintd igsrnirske iqsnsieata pglsdhsyfp ariegkvrek getkrrylgf
      601 qngritdatg kripfdelql widevdqelr tvipsssint fmarfaervd ppatvegici
      661 lldidgedld nfrfgedskp vyfddlcani ennaftliin dqafdfvisy asdtkrfnlf
      721 sagidefvss ryeneegila ffntnqsfri vlkgneyvya gkfffrpgan liskkkdldl
      781 nqifsphpci skiisekgni atlpitsnlw hkdtlfglia rqasgygdnp lenafdfehl
      841 lcddlqgeig dfialdtqkk rvvfihakag dsglsatafq evcgqatknl dyltpyfdkk
      901 ptaniakwtn pwayskvgtv ssriikgglt pkafyatyek lvsdpstsre vwiivgnmfd
      961 yrsfskeink rkisevkpqv iqlvyllrst wnnvasvgaq lkifc
//
LOCUS       WP_010601130             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: single-stranded DNA-binding protein [Pedobacter].
ACCESSION   WP_010601130
VERSION     WP_010601130.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..145
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=16122
     Region          4..116
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 msginkvilv ghlgkdpevr hldggvtvas fplatsetyn kdgkrveqte whnivlwrgl
       61 aevaskylqk gklvyiegkl rtrsfedkek vkkyvteiva enftmlgrks dfeqtpaasv
      121 pqstepkiqd eftigpsden gdlpf
//
LOCUS       WP_010601222             418 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydroorotase [Pedobacter agri].
ACCESSION   WP_010601222
VERSION     WP_010601222.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gojkovic,Z., Rislund,L., Andersen,B., Sandrini,M.P., Cook,P.F.,
            Schnackerz,K.D. and Piskur,J.
  TITLE     Dihydropyrimidine amidohydrolases and dihydroorotases share the
            same origin and several enzymatic properties
  JOURNAL   Nucleic Acids Res 31 (6), 1683-1692 (2003)
   PUBMED   12626710
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..418
                     /product="dihydroorotase"
                     /EC_number="3.5.2.3"
                     /GO_function="GO:0004151 - dihydroorotase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006221 - pyrimidine nucleotide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=45275
     Region          1..418
                     /region_name="pyrC"
                     /note="dihydroorotase; Validated; PRK09357"
                     /db_xref="CDD:236479"
     Site            order(61,63,179,232,305)
                     /site_type="active"
                     /db_xref="CDD:238642"
ORIGIN      
        1 mnllvknvti adpqsnfnkq qcdvrvvdgk iqnigklsae kdetvfdgqg sflspgffdl
       61 ncvagdpgfe tkediqtlta takaggftgl allpqtspvv qsksqveyii nkaknnlvdv
      121 ypvgaisqnr eakelaelfd mqqagavafs dgdkslqddg fmsralqyak gfdallmvyp
      181 enksiagksq inesknsvll gmkglpalae emhiardifl aqynetkihi snistagsva
      241 lirkakrdgv qvscdvtahh lvfteellad fdsnykvkpp lrskadvkal iaglkdgtid
      301 aitsqhrpee iefknvefei ahygiialqt vlplllkagl dasliaekva inprkllnln
      361 vpviaagaea nftvynpnek wlynlasnks ksanspllgt eltgkvtlvy nnsqifqd
//
LOCUS       WP_010601247             117 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Pedobacter agri].
ACCESSION   WP_010601247
VERSION     WP_010601247.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..117
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=13431
     Region          1..114
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mrkvliiedd idilnvmtti lkdsyhvlpi ssprhwkndv eefqpdiaii dvhlgdedgi
       61 nicrelksns ktshiklvvt salviqperl keycdaylek pfeidnftei iedvqlk
//
LOCUS       WP_010601298             197 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Pedobacter agri].
ACCESSION   WP_010601298
VERSION     WP_010601298.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..197
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23179
     Region          20..196
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mvdhlpasdy enlfslfnnl yplkeeiqta iiansevikv tkkvkllnag ersntiyfil
       61 kgaarifyld kdgketntwf lfenellisv ysfytgkpsf eyietledct liavkrdrld
      121 elylkymefn fsgrkltefy hmrneiqane lrmfsakery hkllertpql fqrvslghia
      181 sylgisqetl srirkqk
//
LOCUS       WP_010600499             101 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YbaB/EbfC family nucleoid-associated protein
            [Pedobacter].
ACCESSION   WP_010600499
VERSION     WP_010600499.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Cordeiro,T.F.V.B., Gontijo,M.T.P., Jorge,G.P. and Brocchi,M.
  TITLE     EbfC/YbaB: A Widely Distributed Nucleoid-Associated Protein in
            Prokaryotes
  JOURNAL   Microorganisms 10 (10), 1945 (2022)
   PUBMED   36296221
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Cooley,A.E., Riley,S.P., Kral,K., Miller,M.C., DeMoll,E.,
            Fried,M.G. and Stevenson,B.
  TITLE     DNA-binding by Haemophilus influenzae and Escherichia coli YbaB,
            members of a widely-distributed bacterial protein family
  JOURNAL   BMC Microbiol 9, 137 (2009)
   PUBMED   19594923
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..101
                     /product="YbaB/EbfC family nucleoid-associated protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10785
     Region          1..86
                     /region_name="YbaB"
                     /note="DNA-binding nucleoid-associated protein YbaB/EfbC
                     [Transcription]; COG0718"
                     /db_xref="CDD:440482"
ORIGIN      
        1 mfdklfaaqq kaeeikkrld tisvfgeven gaikitatan kaitgvside effknadkee
       61 leellqtain kalanaeevs stemqasakd mlgglggmfg q
//
LOCUS       WP_010601320             379 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Pedobacter agri].
ACCESSION   WP_010601320
VERSION     WP_010601320.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..379
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43958
     Region          196..353
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mspnkrlvvg qgqisgyisi flavlallgi lcfhypeklt tpefreiytk dsmealmlgg
       61 vitsfffaal svilskklkw gwpgfalaal avilgalsve grdvaksswh fgldwmildl
      121 llmvaifvpl elffpknneq tkfheewrtd ltyfvishlf iqffgivtqk pavlffgwmg
      181 ldklhtwvqg lpfivalfla ffttdffqyw ahrffhtrvs lwrfhsihhs tqnmdwlags
      241 rthfidifft ramtfiplyv lgfsstvfnv yiifiaihav lihantrinf gflkyifttp
      301 qyhhwhhced pkyygnnfas ifpfidmmfg tyylpgkewp agtgvheaey pkgfvkqtiy
      361 pftkspfdtd lkmeersdr
//
LOCUS       WP_010601302             544 aa            linear   BCT 01-JAN-2025
DEFINITION  amidohydrolase [Pedobacter agri].
ACCESSION   WP_010601302
VERSION     WP_010601302.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..544
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60383
     Region          20..544
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mksllyiplf valftscvkk eqadlivyna vvytvnnsfd tveafavkng kilatgsskd
       61 iqtkyqakde inaegksvyp gfidahahff gygqslqaad lrdtksweei lerlavfakt
      121 npdgwligng wdqndwenka fptnekltel fpnrpvllnr idghaavvnq kafdaagikg
      181 eqeliggdml tqngkltgvl idnavglvds kipspdgkla ekiftdaqtn cfaaglttid
      241 dcglpfqavd fieklqkenk lkmrlyvmls dapqnydylf krgaiktdrl nvrsfkvyad
      301 galgsrgacl lhpysdmpnk sgfllstqkh feevaekiaa hhfqmcthai gdsanrvmln
      361 iynkvlkgkn dkrwriehaq vvnsndfnlf gkanvipsvq pthatsdmyw agqrlgasrv
      421 kdayaykqll kqngwiplgt dfpveninpl ltfyaatvra dakgfpkggf qienaltpqe
      481 alrgmtiwaa kanfeenekg sleigkfadf vildhdilka tpqnilktkv lktylngekv
      541 ydak
//
LOCUS       WP_010601349             807 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pedobacter agri].
ACCESSION   WP_010601349
VERSION     WP_010601349.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 807)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 807)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 807)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 807)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13543845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..807
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=90615
     Region          5..807
                     /region_name="ADOP"
                     /note="Acidobacterial duplicated orphan permease;
                     TIGR03434"
                     /db_xref="CDD:274576"
     Region          440..807
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mfklnlkiaw rnlwknkvya ainigglalg ltafvlmlly inheesydsw tpdlenvfqi
       61 rekhdfftpd nkehwqeatd srmaslvren ipqavavtkv dqdwewsagy svkvdgadpi
      121 lvkqikdads sffsvfnyqf lhgsaeaals tpksivvkes ialklfgtdk vlgktvklli
      181 wrsdpgqmft itgvvkepkt pqsvsfnaii rtgeqdhdpe nisnrhfcqv yakmngpmds
      241 talnktlqsv yvnfkkaafa kekrnykdiy kngntpglsa lkisdvhanp tlklswkdkl
      301 kpivgisifl llvsvinfvn lataqsvqra kevgvkkilg sykgqlltqf llesamqsmv
      361 slflcvvlve mvlpafnqnf nvslsfwynp qlfimivqll tlfvlvtlla gfypswilsn
      421 ynpvsvlkgn yenglkgial rnilvvfqfv isvtfiiaig vmyqqtkyvs nkdlgfekgn
      481 lvniksnyee kfaerlrtvp gvkyiatstq vmgnvfntpe vitykenkip vnsvtvtmda
      541 lqalgvqvmq grlfskdykq dtansvvina saaklidknp vgktydllrd drkytfqivg
      601 vikdyhnegf dkavmptiyk vthlggmstt nnmlvrldaa nsgeiikkie aewrflypdy
      661 pmtytsmnda fdkilednnr fvnmivlfsl vsvslsllgl falstfvakr rtreiavrkv
      721 lgasniqivn llnksflilv vvanliswpi ayilikkwld gfayridmpv ipfllatlvs
      781 iviavltvsi qarkaavtdp vnalkye
//
LOCUS       WP_010601370             224 aa            linear   BCT 01-JAN-2025
DEFINITION  carotenoid biosynthesis protein [Pedobacter agri].
ACCESSION   WP_010601370
VERSION     WP_010601370.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..224
                     /product="carotenoid biosynthesis protein"
                     /calculated_mol_wt=25228
     Region          14..216
                     /region_name="COG2324"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:441898"
ORIGIN      
        1 megqndqsdl kvkkiavavi iifhlvglig fllpvtqpyf iklvpfhlll mfaiilftyn
       61 anikrlllfv sgvflcgflv evlgvhtgki fgsyyygdtl gykiaavpil mgvnwvilif
      121 svgqmmkslk ignsilasvl gaitlvifdy flepvamkfd ywewdlheip gqnfvawfiv
      181 slilfkfyya lglkqqkyig tamfvsqlif fvvlymttgs nifa
//
LOCUS       WP_010601388             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Pedobacter].
ACCESSION   WP_010601388
VERSION     WP_010601388.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..193
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21010
     Region          1..193
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mkrlvfgiia aviavstlss cgynsmvsld envkskwgtv qtqyqrradl ipnlvatvkg
       61 aakfeqgtlt avtearakat qmtvnaddlt peniqkyqaa qgqlsqalgk llsitenype
      121 lratqqfsdl saqlestenr itvarkdfnd avqqyngkir sfptnltagm fgfkpkgyfe
      181 adatakdapk vef
//
LOCUS       WP_010601440             292 aa            linear   BCT 01-JAN-2025
DEFINITION  polyphosphate kinase 2 family protein [Pedobacter agri].
ACCESSION   WP_010601440
VERSION     WP_010601440.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Motomura,K., Hirota,R., Okada,M., Ikeda,T., Ishida,T. and Kuroda,A.
  TITLE     A new subfamily of polyphosphate kinase 2 (class III PPK2)
            catalyzes both nucleoside monophosphate phosphorylation and
            nucleoside diphosphate phosphorylation
  JOURNAL   Appl Environ Microbiol 80 (8), 2602-2608 (2014)
   PUBMED   24532069
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Sureka,K., Sanyal,S., Basu,J. and Kundu,M.
  TITLE     Polyphosphate kinase 2: a modulator of nucleoside diphosphate
            kinase activity in mycobacteria
  JOURNAL   Mol Microbiol 74 (5), 1187-1197 (2009)
   PUBMED   19843229
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Nocek,B., Kochinyan,S., Proudfoot,M., Brown,G., Evdokimova,E.,
            Osipiuk,J., Edwards,A.M., Savchenko,A., Joachimiak,A. and
            Yakunin,A.F.
  TITLE     Polyphosphate-dependent synthesis of ATP and ADP by the family-2
            polyphosphate kinases in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 105 (46), 17730-17735 (2008)
   PUBMED   19001261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..292
                     /product="polyphosphate kinase 2 family protein"
                     /EC_number="2.7.4.-"
                     /GO_function="GO:0008976 - polyphosphate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006797 - polyphosphate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33619
     Region          6..282
                     /region_name="PPK2_rel_1"
                     /note="polyphosphate:nucleotide phosphotransferase, PPK2
                     family; TIGR03709"
                     /db_xref="CDD:274737"
ORIGIN      
        1 mknefkaliv qgdkkfsiks aktdftgdyn kekakdalik skievshlqe klyasathsl
       61 liifqamdaa gkdsaiehvm sglnpqgcqv fsfkvptsee ykhdflwrhi kalpergrig
      121 ihnrshyenv lvckvhpeyi lsesipgfde vkkvnknfwk qryqsirnfe nhlaangtvv
      181 lkfflnvgkd eqkqrfldri edptknwkfs sgdikeralw deymkayeda inetstkesp
      241 whiipadkkw farlaiseii adklkslnik fpvldeteqg klletktall ne
//
LOCUS       WP_010601467             398 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent aminotransferase
            [Pedobacter].
ACCESSION   WP_010601467
VERSION     WP_010601467.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..398
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43733
     Region          1..397
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,207,234,236..237,245)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,200,243..245,274,277)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            237
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mstlskrins lsesatlkmt klgrelaskg iniislsvge pdfntpdhvk daakkalddn
       61 ytryspvpgy pdlrqaivnk lktennldyd vsqivvstga kqslsnvilt lidpddevii
      121 ptpywvsyse mvvlaegksv fidtdiesnf kitpaqleaa itpksklfmf sspcnptgsv
      181 yskeelaalv kvfekypdiy ilsdeiyehi nfvdqhesia qfdsikdrvi ivngfskafa
      241 mtgwrlgyia ankeiaaand klqgqttsgt csiaqragiv ayeqglesvl kmkeaflrrr
      301 elvynllnei pgvktnlpdg afyffpeiss ffgkkdadgn vikdssdlal yllnvghvat
      361 vggdsfgnnn yirlsyaasd eslvealrri kealgkla
//
LOCUS       WP_010601364             258 aa            linear   BCT 01-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Pedobacter agri].
ACCESSION   WP_010601364
VERSION     WP_010601364.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..258
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30110
     Region          71..168
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(83,86,132,162,165)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mqthsslywk kyftrnasvk ridwqlepql tkfekgkiik slqawqlget segehllqaa
       61 kkyalktndn eypeavklfi keeqkhgnnl gkyldlidep ritkdwgdtm frkiryyntn
      121 melwtiavit vesaaqifyq alkdasnctl lkqictdili deaahitfqk erlyiifsgk
      181 nsiskfiayh aytcfficts lviwfahqkl fkagrlnffk yfqkmmrkln kvagtailyh
      241 tenktssvyd sseivqsi
//
LOCUS       WP_010601463             138 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Pedobacter agri].
ACCESSION   WP_010601463
VERSION     WP_010601463.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..138
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15322
     Region          1..129
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 mikslwvnlp vknvknskdf ftkigfqlnl khgvrddsac fmvgddnfii mffekplfed
       61 fvatsvadsr sgsevlfsfd aesaeevddf akkvveaggt lyaapgykdg wmygcgfidl
      121 dgqrwnilhm dlgkmplg
//
LOCUS       WP_010601483             176 aa            linear   BCT 01-JAN-2025
DEFINITION  DinB family protein [Pedobacter agri].
ACCESSION   WP_010601483
VERSION     WP_010601483.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..176
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19747
     Region          30..172
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 mktiklltsl lvlmavfnta raqttsadvv kewerakayt keyldampek dyglkptpem
       61 rsfaeqmlhl gadnyvftaa algakspagm dqlektsekt kvvvtknvld sydfviaalk
      121 klntaqlnek vklfdrfels reaafekgfe hqthhrgqtt vylrlagtkp pqeklf
//
LOCUS       WP_010601498             239 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Pedobacter agri].
ACCESSION   WP_010601498
VERSION     WP_010601498.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..239
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27068
     Region          98..234
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhpavaiaif qsfqvkkkks sngckglpgl qldrikkdaf fdtknnmdke kyltqlgnrt
       61 alsiglsayi sfvitsetfs akqtlplnql svnpttmlak gsariyivde aqrehtlffy
      121 qyhdflsias gitlqhdatl fiefledsel llvpgthipn lyklfpefhq vqaghhqtfq
      181 qnlfnhqlnl svlngaeryn rflskykqia mvceqkkias flgidaktls rlranpkrk
//
LOCUS       WP_010601512             204 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Pedobacter agri].
ACCESSION   WP_010601512
VERSION     WP_010601512.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..204
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23660
     Region          10..181
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mnasrnsehd kilfdllkqg deaafgeiyk lywvelynaa ykrlpekekc qdviqnvftd
       61 lwnrrteldl ekpvaylhta vrfqvlkhia rtpknnyfat sfenqlispl dadgalldre
      121 akllielfik alpekrrkif lmhyfeglst arisvklnis qktvqnqltt athalkfrlt
      181 hlffacccil plileiiyps klnl
//
LOCUS       WP_010601612             176 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Pedobacter].
ACCESSION   WP_010601612
VERSION     WP_010601612.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..176
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20209
     Region          5..167
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtkfefnhlv nhhsvslrsy alnftkdaed andlvqdtml kaityynkfk egtnlkgwlf
       61 timkntfinn yrrlvktntl itqsedissa nlsysatknq aeskfvlgdi dkalaqlpee
      121 yyvpfiryfe gykyheiadm lqipigtvkt rihvargilk kylktyakdt alseva
//
LOCUS       WP_010601562             610 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein [Pedobacter
            agri].
ACCESSION   WP_010601562
VERSION     WP_010601562.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..610
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=67526
     Region          75..546
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          319..610
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkkifiytag allvignysc kkflnqvpdd rltfeqqyqr kstvdqalan vystlpdqnq
       61 drspsalgns gpwtaasdea dytlpnften intgawdats gqvnyhwqny yrgiqaastf
      121 manvtrctdc niggvdivnr yfnearalra iyyyhlirqy gpvvllgndp iqsdaplevi
      181 skprnsmdec vdyvvaelta aaaglpatpq anedfghita svadaykikt lltaarplfn
      241 gntdyaalrn qdgkqlisqt asaakwtrla taakaflenp nyssyalysi sttpsglpnt
      301 afnrafiatr dvflngwnse vifgrggdvt lyqyslapnh ngasggdkgg sflspsqqlv
      361 dafftanglp iesdptytan gmssfqapdp ndqnaarsis nmfvnreprf yanitysgrk
      421 winpqsniit dftnsgnagk gaianndytk tgytsrkhlt vagwttgrpi ftvirlaeiy
      481 ldyiealqet npsdpdiliy lnrirtragi apygsgtgai avpanmreai rrerrvelaf
      541 ewdryfytre wkiaettdtq irglnitqna pgfftpivve nrvfqkkhyl wpipngeiqk
      601 vpvivqntgw
//
LOCUS       WP_010601616             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pedobacter].
ACCESSION   WP_010601616
VERSION     WP_010601616.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22990
     Region          4..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mivadkkreq iiegaikrfs hfgigkttmn diaedlsvsk pslyyyfpdk khlilgviek
       61 ifneffeaiq kkynpelele tilfntidvr ntffqkyyml kiaegvpdll ndeaiktkln
      121 glkdierdff akvfgsakek geiahedmsh laelyleslm glttmcvmet akdilpdkka
      181 lnkmtqkqkd lssiftkglk c
//
LOCUS       WP_010601619            1058 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pedobacter agri].
ACCESSION   WP_010601619
VERSION     WP_010601619.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..1058
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115398
     Region          1..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mkitdisikr pslvivvfta ltlmgllsyf slgyellpkf ssnvvsisti ypgaspneve
       61 stvtkkieda vssmenikki nansyeslsv viitltdkae idialndaqr kvnailadlp
      121 ddvkqpslsk fslddfpvit msasgnmddi sfydlmdkri apiisrvpgv aqvnliggse
      181 revkvaldak kmqgyglsvp avqqailssn ldfptgsvkt kaqdilvrls gkyanvedmr
      241 nlvvstskdg aqirlgdiad vqdtqketek iarinransi avqiikqsda navtvsegtk
      301 qtieqlkady knvgldikiv ndssvytles adavihdlml avvlvaivml fflhslrnav
      361 ivmisipasl iatfigialf gytlnlmsll glslvvgilv ddaivvleni qrhmemgknk
      421 vraasdatre igftvvsitf vivvvffpia vstgmvanil rqfcvvviis tllslvasft
      481 ivplifsrfg kleriegkni fgkfilwfek qlrkftqwit nllewtlkhk altlvmmvvl
      541 ffsscgllag gyigfeffpk sdkgefllqi empkdvsleq tnfytqkaed ylskqkdviq
      601 tiatvgqsse gmgasqstay kseinvklke keergnlssd iisttytrel ekvlvgakik
      661 tvpigilgta ddapiqlvvm gseldsvlaf aqkaqnvlak ipgatqtkls vekgtpeinv
      721 kvdrdkmsal gltlqtvgat mqtafagntd gkfrqgeyey diniqyqdfd rkdiddvrnl
      781 iftnqagaqi klsqfadike gsgpsllerl nkstsvtvka qtvgvptgtv vtnfqteldk
      841 lkkpagisfy wagdqenqse gfgtlgiall aaivlvylim valydsfvyp lvvmfslpla
      901 ligallalal tnnalgifti lgfimlmglv aknaiilvdf tnqmkaqgks thealilanh
      961 arlrpilmtt iamvigmlpi alasgagadw knglawviig gltsslfltl vvvpvmyqif
     1021 dnmlhkfgfd kkgktiddlm vepykhkdvn eydldhgh
//
LOCUS       WP_010601625             310 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Pedobacter agri].
ACCESSION   WP_010601625
VERSION     WP_010601625.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..310
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=34550
     Region          6..300
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mehaqkgfip vmltpflsng nidypaltql teiylqagas glfanclsse mfelsdeeri
       61 qaikhvikit ngavpvvatg tfggaiskqa dfvkkisdlg veaviaitsl ladenetddv
      121 fnervfdlld qtpdipigfy ecpvpykrll kpqqladfvv tgrviyhkdt cldlgqikdk
      181 lslteghafg lydaymahav eslkagssgl sciqgnyfpe livwlcdhyd nellkhevai
      241 vqqfiidnmd vmhhvypivs kyflqkrgld istftrrnvg aftpgivkdi eklyddytll
      301 rsdlniqvyi
//
LOCUS       WP_010601626             289 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pedobacter agri].
ACCESSION   WP_010601626
VERSION     WP_010601626.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18991537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33595
     Region          14..99
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
     Region          <115..280
                     /region_name="PRK15185"
                     /note="transcriptional regulator HilD; Provisional"
                     /db_xref="CDD:185107"
     Region          <202..287
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkphfhkvpv tlqssfsirh dinpdfgniw hyhpelelhy vikgegvrfi gdnisnfepg
       61 emillgenlp htwrckdeyf qnnrdlntea mvihflpdcl gkyllnlpea yllpklfeka
      121 ksgmvingdt kdklvtlmqs aidatnldri iillfilktl aetdeyativ tskntfyqsn
      181 esetlrinki cnytlsnykk ditleevasl snlsitsfcr yfklmtkktf ydflieirvs
      241 hacrllienk lptemicfdc gfnnvsnfyr hfkkvtgmtp ldykrkyln
//
LOCUS       WP_010601684             140 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Pedobacter agri].
ACCESSION   WP_010601684
VERSION     WP_010601684.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..140
                     /product="VOC family protein"
                     /calculated_mol_wt=15817
     Region          4..136
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(4..9,25,61,63,66,84..89,91,95,124,134)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mrtmhpylnf dgqaeeafnf yksvlggefa ffkkmsdape sdklpenern rvmhvalpin
       61 ehtilmasdc vpsaghvlre gnnmyvhlaa esredadklf nglsaggtve mpmedmfwgd
      121 yfgsfkdkfg iqwminfgny
//
LOCUS       WP_010601715             444 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Pedobacter agri].
ACCESSION   WP_010601715
VERSION     WP_010601715.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..444
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48534
     Region          2..439
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mqqkkqlslf dlsmivvslv igmgifrtpv nvaakaqipe lfylawfigg fvafcgalty
       61 aeigsrypvt ggyykifska yhpsiafain civlissaas vaaisiigae ylskiilpve
      121 mqnetyrvai aiatillfyl inllglkass ktqnvltiik iglililica iffaettqii
      181 tpvfktannt lpswadygka lglcliavsf syagyaqtin fggevteakk viprsiiigl
      241 tiivilymal nyvyvqvigf eelktaesia ailaskifgp agfkmlsvii fvsvmgyvnv
      301 nllsnpramf amgeegalpk vfarmnkkev isvsltvfsl vavviiffak tfdkilnyti
      361 flesismass aatifilrkr tanldnktiy tvplypilpv ifiaaytfva fsiyaddpna
      421 alnglyifig fliiyfiskv ftrk
//
LOCUS       WP_010601780             201 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pedobacter agri].
ACCESSION   WP_010601780
VERSION     WP_010601780.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23184
     Region          9..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgskerilrl keetrtsild aalnivqteg wqalsmrkia dqieytapii yeyfpnkegi
       61 lleltrrgyq ilgkdirear dkhenpedkm eamwvaywnf afshkefyql mygvdmvcct
      121 vknsmqeaeq vsamlgdvie slfikkpvse ndicmkyyty wsiihglisi nlvrpngrtt
      181 delnqqilkd aikgitlsin s
//
LOCUS       WP_010601863             188 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Pedobacter agri].
ACCESSION   WP_010601863
VERSION     WP_010601863.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..188
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21849
     Region          10..183
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mnnslkssvp tdrevilgil nnsedtlnkl ykayyamvlq filnnngded dakdvyqeai
       61 ivlynkikeg nfelssklkt yiysvcrriw lkklshnskk agnitdyedv liveedveeh
      121 eqkdlqfvkm qsaldhlgep cktiiqdfyi hnlsmqdice kfgytntdna ktqkykclqr
      181 lkkiffqp
//
LOCUS       WP_010601890             356 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Pedobacter agri].
ACCESSION   WP_010601890
VERSION     WP_010601890.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..356
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=40726
     Region          4..308
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mifevlkafn ldgpetqysl fggglinntw kvstkngdfi lqqintdift speeiieniv
       61 nlksylhqta peylfvgpiq tnsgqsvlni ggytfrifpf vpesitidkv vhpnqayqaa
      121 kqfgqfsrll kdfdvskinf plrdfhnlcl rvaqyrqalk ladesrlsaa awaiqqlakh
      181 mdiaqkydei iasnrlkvri fhhdtkisnv llhrdtglgi cvidldtvmp gyfisdvgdm
      241 mrtylspvte eetdfslidi rveifeaiyr gymsemdtvl tsserelfiy agqfiifmqa
      301 lrfltdflng diyygatype qnlnraknqi hllnkyteki aafekfiati eikqvd
//
LOCUS       WP_010601944             262 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Pedobacter agri].
ACCESSION   WP_010601944
VERSION     WP_010601944.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..262
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=29580
     Region          6..260
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mnyellcnkv isivkltgnf irkesmqfda skieykglnd mvsyvdktae qklvqnlekl
       61 ipdagfitee ktisregknf iwiidpldgt tnfihgipay gisvalyeng lpvigvvyel
      121 nrgemfysyr ggkaflnkke iqvsvnpdlk ssllatgfpy yqfdkqaqyl klleemmqks
      181 hgvrrigaaa idlvytacgr fdaffeynlq qwdfaagcfi vqqaggevfd fsggndyftk
      241 reilatngkl taetleaikr yf
//
LOCUS       WP_010601992             165 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Pedobacter].
ACCESSION   WP_010601992
VERSION     WP_010601992.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..165
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19360
     Region          8..163
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 meqkdklfke ifdsnskkif hlcygytgdt daandllqet flkvwqnldk frnkslistw
       61 iyriavntcl tylrsekrqa kdelteniie nkieefsekn eqvallykci skleendrli
      121 itmvldelpy heiadisgis egnlrvkihr ikqkltelyn qyasv
//
LOCUS       WP_010601973             136 aa            linear   BCT 01-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Pedobacter agri].
ACCESSION   WP_010601973
VERSION     WP_010601973.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..136
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=14640
     Region          3..106
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 meitgrltad avvrtvsedr kvvgfsiain dtfrsggeqk kittfidcsy wlntgiaeyl
       61 kkggwvqlyg rigvnaymsg nneakasltf htseikllgg tarsgelpnv vakevemiaa
      121 aqanstfegi dedlpf
//
LOCUS       WP_010601993             457 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dicarboxylate/amino acid:cation symporter
            [Pedobacter].
ACCESSION   WP_010601993
VERSION     WP_010601993.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..457
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=49533
     Region          81..455
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkknkltlfi flaliagval gyilnvnsid tynqkilnad akvksievsi kktadttsav
       61 yaqlkaerkv naqikkened irekkleyft llsdiflrli kmivaplvft tlvvgvakvg
      121 dikavgrigg ktlgwfmams lmslvlglvl vnlfepgkhm qltlpdqmvn tgiqkaamsv
      181 kdfiahvfpk siaesmatne ilqivvfslf fgvataaigd lgqvvikafd aiahvilkmt
      241 gyvmnfapla vfgamtaiva kqglnvlnty aifigefylg lgilwavlif lgflilkkrv
      301 frlvndmkep ailafstass eaaypktmml lerfgckdki vsfvlplgys fnldgsmmym
      361 tfaslfiaqa ygihlgfeqq ismllilmlt skgiagvpra slvviagtia sfnipeagla
      421 lligidplld mgrsatnvvg nsiatavvsk wegelkd
//
LOCUS       WP_010601995             120 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Pedobacter].
ACCESSION   WP_010601995
VERSION     WP_010601995.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..120
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=13822
     Region          1..120
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mekltiqeee amlavwqvgk gfikdfmdvl pepkppyttl astiknlekk gyliserfan
       61 anrygakvke veykkrfmsg fvnnyfqssy kelvaffakd kkisaeelke iinlienpek
//
LOCUS       WP_010602081             244 aa            linear   BCT 01-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Pedobacter agri].
ACCESSION   WP_010602081
VERSION     WP_010602081.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..244
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27577
     Region          106..207
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(125,128)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mekpiiiavm ampcllllnc fdlnlknndr pgtlmllllq vmykfrlfil knlartflfi
       61 nlffflalds sgqiaqkqvl sigdtvpesl wnsnhtvyke gkivnhsleq ykgqllildf
      121 wstwcgpcir slpeldsigk mfrdkvqvvl vtkntneils kflknsdyak gvklpfilnd
      181 silnshfphq sishqifids kgivraitgi ngatikniqq ivngnpidfp lkddfaprsn
      241 pnke
//
LOCUS       WP_010602109             200 aa            linear   BCT 01-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Pedobacter agri].
ACCESSION   WP_010602109
VERSION     WP_010602109.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..200
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21380
     Region          1..197
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mkkilhiiss prggasvsiq lgnavvskiq etypesivke knlaqhpfph leevhlnaff
       61 tpaesrsaen laaiqhsdea iaelqeadii vigvpfynfg vpstlkawvd hiaragvtfq
      121 yteqgpqgli tgkkvylava sggiysdgpm qaydfatpyl kgvlgflgmt dvtvfraega
      181 sipvvkdtal ekgiesilia
//
LOCUS       WP_010602112             130 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Pedobacter agri].
ACCESSION   WP_010602112
VERSION     WP_010602112.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14755
     Region          3..127
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 mntkmiwanl avkdlkrtak fytslgfkpn gkfnddlvsf ffgqdnfiih ffvekqfkta
       61 aklenselyt gseiifslsa esreevdawm ekvkeagasi yadaadfdkg ytfgfsdpdg
      121 hkfnllywps
//
LOCUS       WP_010602192             239 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Pedobacter agri].
ACCESSION   WP_010602192
VERSION     WP_010602192.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..239
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26248
     Region          1..>125
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
     Region          1..58
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mthtyqltgm tcggcenkvk nnllilpevt avevskdtns atismdkhig iaalqqalgg
       61 aeskyqitan nhselaeetk swaetykpil lifgyvttis llvswqdgni nlmtfmrifm
      121 agffltfsff kmlnlkafae syamydivak kfnawgyiya fielclglsf alnlspvvvn
      181 wvtlvvmlvs iigvlesvln kkkiqcaclg avfnlpmstv tivedaimia msaamlilm
//
LOCUS       WP_010602234             358 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Pedobacter agri].
ACCESSION   WP_010602234
VERSION     WP_010602234.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..358
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=40982
     Region          8..314
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 melnldsevl lafgytketa titqigsgli nrtyllspls edqkyilqni ntsvfkkped
       61 iannlkaiad ylsknypdyl fikpvstidg kemamiesey wrmlpfvpnt vsldvlsepq
      121 qayeaakqfg klsallnnfd aslleptipg fhdlglrfeq ftaalttttk elkgkakpqi
      181 ddalkhkyil dyyesyshre dfpdrvmhhd tkisnvllka etfagicvid ldtimpgkfi
      241 sdlgdmmrty lcafsenekd lskikirlpy feamvkgyls emkniltete kelilfsgky
      301 iiymqalrfl tdflngdiyy ptayptqnld raknqfkllh eltvnekelq diieehla
//
LOCUS       WP_010602204             278 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pedobacter agri].
ACCESSION   WP_010602204
VERSION     WP_010602204.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..278
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31310
     Region          41..277
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mlekllpiml lfqtilssaq vktakninya gntevkntln ifykndgian kpvlvfihgg
       61 swssgkkety wwlgrnfark givtviinyp laptaqyekm agdcalavkw vrenienyqa
      121 sgdkifvmgh sagahlgeli nsdpkyfqla giknpikgmi lndpfgldif eyltsaekdn
      181 yyydflrtft dqpavwkras pldyvnnikn phllfyggkt ydaikiqtpr lyekltankv
      241 aveinevkgk shvpmisqmi fgsnalykai vefvnkft
//
LOCUS       WP_010602257             319 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PhoH family protein [Pedobacter].
ACCESSION   WP_010602257
VERSION     WP_010602257.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..319
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=35084
     Region          1..315
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 mnelkltldt vnpahfwgan nenyemikga faklklvarg sdvkvlgdeq elkafedkfn
       61 qlvahlekys sltnndvesi lgakangvak kdvdqptggg gevivfgtng llvkartanq
      121 rrmvssiakn dilfaigpag tgktytaval avralknkei kriiltrpav eagenlgflp
      181 gdlkekidpy lrplydaldd mipaeklkfy ienrtieiap lafmrgrtld ncfvildeaq
      241 natdmqlkmf ltrmgptakf ivtgdvtqvd lpkkqmsglf nglriledik gidiiylsge
      301 dvvrhklvkd ilkaygdiq
//
LOCUS       WP_010602294             426 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Pedobacter agri].
ACCESSION   WP_010602294
VERSION     WP_010602294.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..426
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=46934
     Region          6..418
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mnedkiiavi glgyvglpla iefakkykvi gydikatrva alnnlrdgtn eanlddlkiv
       61 lhskglnglk lssdlsdikn aqvfivtvpt pidhlkrpdl eplleasrml gkvikkgdiv
      121 iyestvypgc teedcvpvle kysglkynid ffcgysperi npgdkvntlt kikkvtsgsn
      181 pqismeidql yasiitagth lapsikvaea skaienaqrd vnisfvnela lifdkmgidt
      241 sdvlaaastk wnflnykpgl vgghcigvdp yylahkseal gykpevilsg rrvndnmgmf
      301 vankvikmiv aksgilnear vlilgfafke ncpdtrntrv vdiidelkaf nievdvhdpw
      361 asaeevkley gieliaegdf tsyhavilav shqkflaldy grfkeqgaii fdtksfinre
      421 fvdarl
//
LOCUS       WP_010602328              80 aa            linear   BCT 01-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Pedobacter agri].
ACCESSION   WP_010602328
VERSION     WP_010602328.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..80
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=9085
     Region          17..>76
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 maiqtqnlde hnskvvvrnf inalnaenfa aareqladdm ifkgvmgerr gadvymedmk
       61 kmkfkyeikk lfvdgndisl
//
LOCUS       WP_010602353             123 aa            linear   BCT 01-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Pedobacter agri].
ACCESSION   WP_010602353
VERSION     WP_010602353.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..123
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=13885
     Region          4..123
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mtinnikpte gemeilqvlw kkglatvrev healnkkdsg ytttlklmqi mhekgmverd
       61 tnqkthiyka ivnrdktekq lvtkmidnvf ngsaarlvmq algnhsasad eldeikkyld
      121 slk
//
LOCUS       WP_010602383             215 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Pedobacter agri].
ACCESSION   WP_010602383
VERSION     WP_010602383.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..215
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=24678
     Region          23..207
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(103,110,129..131,175,181,185)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mhikrntlli iltlliiaft slsvfiaghp ilqfdirasl fvqqyqadwl dklmlaisff
       61 gelpwsllsv lvvaaifywq kfkreglfma sillsgliil giknminrpr pttfyvrlve
      121 vnrfqsypsg hvlsyvlffg fliilmdrle tipkitrniv tylsaflmis iapsriylga
      181 hwftdtlggf llgliclfpl cyfyfkkdss rsenn
//
LOCUS       WP_010602397             144 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Pedobacter
            agri].
ACCESSION   WP_010602397
VERSION     WP_010602397.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..144
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15957
     Region          11..143
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 menriniqka dpaayqamyg lekylsassv dpillelikm rasqingcaf clnmhsadar
       61 kigeteqrly llnawrettl ftkeeeavla lteevtlign hvsdetyaka agffdkktls
      121 qiimaivtin awnriaitsk ltvg
//
LOCUS       WP_010602407             191 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Pedobacter agri].
ACCESSION   WP_010602407
VERSION     WP_010602407.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..191
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=21601
     Region          1..181
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 msenyiaeqt fdredfsira lpkaeyenck fincnfansd lsgvkfldce fnacnlsmas
       61 ltktalndih fsdckmlglr fencndfgla ftfnnckldh ssfyklklkk tsfkntqlqe
      121 vdfsesdlsn ssfencdlsg atfdrtilek vdfrsasnfs idpdknrikk arfsqaglgg
      181 llhkydivis q
//
LOCUS       WP_010602468             159 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Pedobacter agri].
ACCESSION   WP_010602468
VERSION     WP_010602468.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..159
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17400
     Region          5..151
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 mpkdhlystt vtwtgnkgsg tmdyrsydrd yvisvkgkad isgssdsafl gdkskynped
       61 lllasissch mlwylhlcsk neivvidykd eavgtmeesa dgsgkfkevt lhpqvliadk
      121 ahfelaeslh aeankmcfia nslnfpvkhe aackaensa
//
LOCUS       WP_010602481             168 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Pedobacter agri].
ACCESSION   WP_010602481
VERSION     WP_010602481.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..168
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19422
     Region          9..164
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mnnvkftsei yahsdhlmsh alkftrdedd akdllqetli kglrfahsfd qgtnlrgwly
       61 vimrntyind yrkdtkrkaf vtveeeitng qlaisatkna gestfaledi nkamasikde
      121 yripfkkyfe gykydeiaae lnlpigtvkt hihqarqglk kylkmyrs
//
LOCUS       WP_010602482             143 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Pedobacter agri].
ACCESSION   WP_010602482
VERSION     WP_010602482.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..143
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=15935
     Region          1..119
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 meqkkifive ddlvlletiq dilldqgfdc qgcfhpenai rmiekyrpdl vlldymlpew
       61 nggelcsair aidgfeytpi iitsayakil lsisdygcda viekpfrisd ligvinsqlc
      121 trrsdsgllp kikkvvksal plg
//
LOCUS       WP_010602506             233 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Pedobacter agri].
ACCESSION   WP_010602506
VERSION     WP_010602506.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..>233
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          1..229
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mievkdiyks fsgnevlkgi sgkfeegvtn liiggsgsgk ttllkcmvgl hqpdsgsvly
       61 dgrdftpmty eqrievrkei gmlfqgsalf dsmtvednim fplnmftdqt raekiervnf
      121 clervnlagk nklfpaelsg gmkkrvgiar aismnpkylf cdepnsgldp ktsivideli
      181 qeiteefktt tivvthdmns vmgigdyilf lhegkkfweg snkeiahtdi qel
//
LOCUS       WP_010602530             159 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase [Pedobacter
            agri].
ACCESSION   WP_010602530
VERSION     WP_010602530.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..159
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17542
     Region          1..152
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mkyasniesp igkitiladd dcvyaitfsd edtdglsese ltknvaqqla ayfrgdlkhf
       61 sfpmkqkgte fqqdvwqnll nipfgettsy akfsahhpla iraiaaangk nniaivvpch
      121 rvigsngklv gyagglwrkq wllqheqeis kqgqtalkf
//
LOCUS       WP_010602559             313 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Pedobacter agri].
ACCESSION   WP_010602559
VERSION     WP_010602559.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..313
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34546
     Region          4..294
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 maranksiys alaanlliai tkfvagaftn sssmiaegih stvdtsnqll llyglkrsvk
       61 padkyrpfgy gkelyfwsfi vsimifglgg vvsitqgieh irhpetlvnp gwnyvvlvls
      121 fvfegasliv aikefnktrn glpwwkaiik skdpsgflvl fedgaavmgl iivfvlmvls
      181 hnlnmpfldg lasvlvglll ifvsfilare srsllmgegl spetqqklke lieadkdvit
      241 vksilstyqs pkevilvlii tfqsdldtee ltaaidrlrs evkqkytiir fviiqpqsan
      301 ieegnqskdi fla
//
LOCUS       WP_010602579             389 aa            linear   BCT 01-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Pedobacter agri].
ACCESSION   WP_010602579
VERSION     WP_010602579.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..389
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=44510
     Region          157..287
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          231..349
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mqnnfdlsgk lclsilkinl fnyplliqia vivsilavia ifltltyiiy nrtkrqsdqr
       61 ktyeaenqil eelndhllmy dsieempene lqetvkklne fknrsvifqn vlvrlliyfk
      121 hnltgnitrl itatyfnlkl neitlsklks vfwftkaqgl kelqdindyn sadtiqpllv
      181 nknldvrvea yaallklqtn ssfnflknee eelsnwhqil lfdaitkseh avvpnfadfl
      241 ssenktivil siklllhykq feaipdlirl lsnkneqlrs eaicalgvld aedaeqklis
      301 iypternpnk tqillalgei asgsalhflk dkflkadhyt ilksaaaaim shpavlkeki
      361 laslkdldee qkaiikhfed plirlhgvr
//
LOCUS       WP_010602662             131 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Pedobacter agri].
ACCESSION   WP_010602662
VERSION     WP_010602662.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..131
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14494
     Region          4..131
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mdknwaylis rlaiglsffg hglvrlpkla gfsnwmvsqf sksllpeflv vpfsyilpfa
       61 efiaglliii glftrqglll aglislalif gttmienwea lpsqlihvaf lsvllaylph
      121 ntyavdqiik k
//
LOCUS       WP_010602722             500 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Pedobacter agri].
ACCESSION   WP_010602722
VERSION     WP_010602722.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..500
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55596
     Region          23..500
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mqiatektps ietleaiqnf egkypkqlwy lslvemwerf cfygmrgvla ffmvdqlgls
       61 dqksnlqyga iqafvyaftf iggifadkil gfrkslfwgg slmiignlil afspqdlfyv
      121 gitlsiigtg ffkpnissmv gelyhekdnr rdagfglfya ginvggllgg amciylgkyv
      181 swhlcflsaa lvmafglgtf iftkkflgpi gnspllnlek tkrttyeiav yvgsllcipl
      241 ifimvkntay tdyfmytigi iamiyfiyet amikdikaqy kliaafvfif cyfifmaise
      301 qsggslslfa kdnldhnllf fnidpnvvnn svnsffvivf splvgllwig mykrkiepnt
      361 vvkfgigfll lalsfyvfya trffandqgi sslniftlay llltlgelcl gpigmsiitk
      421 lspkkmfgmm mglwflssaf gqlaagklga emssidnasl maklvayteg ykalalysli
      481 agvaliafsq lvkklmgevr
//
LOCUS       WP_010602753             237 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Pedobacter agri].
ACCESSION   WP_010602753
VERSION     WP_010602753.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..237
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26821
     Region          158..234
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mmiklsltla iflgittlsf sqgkrsdftf klenttyfvn lskgstkaey dtvfynfyry
       61 gkpellakei khivnrntgd tiksgsyrvv nnrvffdrne kneatilkvy sfqdalkpap
      121 ieptppyhny gqpkqeqlet vaefpggink arqfiannlk ypkkaiehgv nstvqakfti
      181 evdgsltnid ivkklgygcd eevirvlksm pkwkpatlkg ksvksyftmp isfktte
//
LOCUS       WP_010602673             379 aa            linear   BCT 01-JAN-2025
DEFINITION  FecR family protein [Pedobacter agri].
ACCESSION   WP_010602673
VERSION     WP_010602673.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..379
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=41569
     Region          <167..378
                     /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"
ORIGIN      
        1 meentskpel fgkflaekss aaqlnqlfdy fgnadqeele rliraefekd tqdlsetdqp
       61 rldliysnlt kqlfakpesn llrvlrseiv kiaaailvff siglmifkfl npthnvvpga
      121 aiatlsfnga kaklgavqkg viyaqggiqi ikkadgsivy mavnadaata sklntletpn
      181 ggeyritlgd gsvvmlnags klifpmdfrg perkvyvege affnvtknpe kpfivaiggs
      241 eikvlgtqfn vssypenegt eatllegsiq fsntsgkvvl kpnqqviagy stlnvrnvsa
      301 edfsawtkge flfndtplav vmqklarwyn vevdltvlpk knlymkisrr adidevlgni
      361 skatglefnl kankivlee
//
LOCUS       WP_010602836             148 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pedobacter agri].
ACCESSION   WP_010602836
VERSION     WP_010602836.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..148
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16778
     Region          15..148
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 meytssiksf tqlspeelyq imklrievfi ieqecfyqda ddkdqychhl mlwneenlva
       61 yarlvpagls ftevsigrvi tnadvrgtgt gkilmksaia ecktlfgdvp irigaqtyak
      121 afysglgfed tkiefmedgi phlemlyr
//
LOCUS       WP_010602841             327 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Pedobacter agri].
ACCESSION   WP_010602841
VERSION     WP_010602841.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..327
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35956
     Region          10..307
                     /region_name="AKR_AKR13C1_2"
                     /note="AKR13C family of aldo-keto reductase (AKR);
                     cd19078"
                     /db_xref="CDD:381304"
     Site            order(19..21,52,57,82,123..124,153..154,173,201..207,258,
                     275..280,283,286..287)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381304"
     Site            order(52,57,82,123)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381304"
ORIGIN      
        1 mekrilgnqg lavsalglgc mgltfgygpa tdeteavsli rnafdlgitf fdtaeaysqg
       61 gneivlgkav qpfrnqvvia tkfgfqdgda tkgldsrper irqvvenslk hlqtdyidll
      121 yqhrvdpnip ieevagtiqe linegkikhw glseagaeti rkahavqpva alqseysmff
      181 rdaekdiipt leelgigfvp fsplgkgflt gtinettqfd kddfrnivpr fseenrkanq
      241 tlvnllkkla nekeatpaqi alawllakks fiapipgttk lhrlkenvgg atvqlsendl
      301 akikqsltei eivgerypqh lqnrvgk
//
LOCUS       WP_010603001             257 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pedobacter agri].
ACCESSION   WP_010603001
VERSION     WP_010603001.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..257
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29003
     Region          2..255
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mqellvsnyt anrlklktgd dfimyfvqnq lrprkfkivg iydigvedid ksfvlgnlni
       61 ikrlnnwnan qiggveirik nfkdlnkvsl eifeslpqnl rsfsivenfp nifnwmslld
      121 vntnvllilm livgvinmvt allimilekt nmigmlksfg asnwsimkif lynaayligi
      181 glllgnilgl glgffqqath ifklnqssyf ltyapieihf idvlglnvlt vvvclivlii
      241 pslliskvsp lkairfk
//
LOCUS       WP_010603032             167 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Pedobacter agri].
ACCESSION   WP_010603032
VERSION     WP_010603032.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..167
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19619
     Region          8..164
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mnetenifls linqhkaiih kvskmymida eqqrdlfqei vmqlwkaypt fkgnskfstw
       61 myrvalntal vyfkkdhrkv dktplnenid vidtddseak eerlaylyka vqelnaveka
      121 liflflenqs hreialnlgi sevnarvkln rtkeklqfii kkngyef
//
LOCUS       WP_010603046             127 aa            linear   BCT 01-JAN-2025
DEFINITION  c-type cytochrome [Pedobacter agri].
ACCESSION   WP_010603046
VERSION     WP_010603046.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..127
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13816
     Region          44..126
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mkktflglga ivifmasfsk adlekekmvv atatlthhef qmsageklin ksdcigchnk
       61 vnkiigpsyt eiakkypate kninyladki ikggtgvwgt mpmtahatlk padaklmvky
      121 ilslkkk
//
LOCUS       WP_010603064             265 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pedobacter agri].
ACCESSION   WP_010603064
VERSION     WP_010603064.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..265
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29957
     Region          3..265
                     /region_name="EfiE"
                     /note="Predicted lantabiotic-exporting membrane pepmease,
                     EfiE/EfiG/ABC2 family [Defense mechanisms]; COG4200"
                     /db_xref="CDD:443354"
ORIGIN      
        1 mrsifislvs efyksrktla fwaaillpva icslvsfgfy sgsekvlkln apgmmlwvry
       61 agatlnvmgm lvmpfyvmfm afsvnniehk ndtwktlfaq plnkfsiyta kylfsvllif
      121 iclflfaalt fafghllqal vpqytfnqyn psnflinsys klflsslgil siqfilsliw
      181 gdflkpigig fvgtimgivt gmlnwtyayl ipyslpslal qftqlkkgkd plnfeiftre
      241 iwtslayaaa lfiagyfivt rksik
//
LOCUS       WP_010603053             323 aa            linear   BCT 01-JAN-2025
DEFINITION  MlaD family protein [Pedobacter agri].
ACCESSION   WP_010603053
VERSION     WP_010603053.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..323
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34960
     Region          1..254
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mndnkkkitv gifiaigili fvfaiftlgs qkktfvksft lsvvfndiqg lkkgnnvwfs
       61 gvkigtikki effgtsqvrv flsieedmhk yihkdagasi gadglignki vvltggnpkf
      121 pfvedgdvlk vnsslstddi mktlqvnnkn lvdvtgdfki larnlvdgkg aagallsdeq
      181 lamnfktmvs nlnritlsta qtaqdlntfg ktlnsknglv nkmmtdtavf akleksaasl
      241 qqtsqsaslm aanlekasgk lnttdnaagl llndaktaeq vkaimtnlek gskkldedle
      301 alqsnflfrg ffkkrardsi knq
//
LOCUS       WP_010603068             132 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SRPBCC family protein [Pedobacter].
ACCESSION   WP_010603068
VERSION     WP_010603068.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167397
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..132
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=14832
     Region          4..131
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cd07812"
                     /db_xref="CDD:176854"
     Site            order(4,6,8,17..19,21..22,38,44,45,61,63,65,84..85,87,89,
                     96,98,100,102,116..120,122..123,126..128,131)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176854"
ORIGIN      
        1 mtiienavev nkpvsevytf lsdmnnhqql mpeniynwes tedearftiq nmaklaikis
       61 nrvenqelta iptekapfev elkwtvadng ngtttakhii sadlnmmmkm lasgplqklv
      121 dhqteklkei lg
//
LOCUS       WP_010603118             361 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Pedobacter].
ACCESSION   WP_010603118
VERSION     WP_010603118.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..361
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40951
     Region          1..347
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mlrlgilglg egrstisasl askkfkliqi cdankklcee ralefdfqnw ttnyedmlts
       61 dkidmiaiyt pdhmhfehik qallhgkhvv ctkpfiddls qanellelak ksrkkifvgq
      121 ssrffepamr qkkdfdkgli gelitiesyy hadhrwflek gwslkqsfkw lygglshpvd
      181 firwympdie evmgygmlsa nglkagiknq dtmhfifkak dgriarvsga ytgptqpasr
      241 dsgmscilrg tegasqadyh elrysvttkt geekiitwgd atlkhyfrfe gqshhageyq
      301 nyldyfadsi nnkftaypdl kegigtvall qamdksmeig lpvkiddilk annitresig
      361 l
//
LOCUS       WP_010603167             296 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Pedobacter agri].
ACCESSION   WP_010603167
VERSION     WP_010603167.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..296
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=33716
     Region          1..296
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mnhlslfsgm ggfdlaaewm gweniahcew npfcqqilky ywpkaisyad itktdfsihr
       61 gsidiitggf pcqpystagk rkgkdderhl wphmlraire ikprwvvgen vlglvgwngg
      121 lvfeevqadl eaegyevqpy ilpaasvsap hkrdrvwfva ysksfrrgag irekvdrcew
      181 npkeyfyera girnkseaig ragispdany erleveqrig ghndskcktt krnnngwedw
      241 ptqspicdgd dgfparldgi tfskwrresi kgggnaivpq vaiqifktie eyekri
//
LOCUS       WP_010603154             353 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Pedobacter agri].
ACCESSION   WP_010603154
VERSION     WP_010603154.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..353
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38450
     Region          1..327
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mdklqrsvyi lllialifgi lyfassflip lalaavfsml firlsnfles kkinravasl
       61 icilifvaai glivgllywq mgsltenide mksrltnmiq dvrswlnqsv gidknqqkei
      121 ikqgnsqtga viagfavnla sigvstilvl vymylclyyr ahiknfilkl vpdnqedkta
      181 hivhesglia qkylsglgam igvlwvmygi gfsivgvesa iffavlcgil eiipfvgnlt
      241 gtsltvlaav aqggdskmii gvlvvyavvq lvqtyilepl ivgeqvninp lftimaivgg
      301 efvwgvagmi laipllgivk iicdrvpvlq pygfligpak pvvrkrnifk rka
//
LOCUS       WP_010603210             483 aa            linear   BCT 01-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Pedobacter agri].
ACCESSION   WP_010603210
VERSION     WP_010603210.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..483
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=53025
     Region          4..430
                     /region_name="ASKHA_NBD_FGGY_SePSK_AtXK1-like"
                     /note="nucleotide-binding domain (NBD) of Synechococcus
                     elongatus putative sugar kinase (SePSK), Arabidopsis
                     thaliana xylulose kinase-1 (AtXK-1) and similar proteins;
                     cd07783"
                     /db_xref="CDD:466801"
ORIGIN      
        1 meayflgidi gtqgarvvll saqgeligee eevfpinegs reeqspeaww qsclsslekl
       61 llsvqidrtk ilslsvtsts gtvipldenh qplhqaimys dkrsaaqgei ctaaalryhn
      121 kgftgfnsss glakmlwfiq sypekakkih kwvhaadyit gklsgefgit dytnafksgy
      181 dvgdyywpdy istelgikke wlakvvpsgt vigtidvala gqlglplkva vtagitdgca
      241 sqiasgamkp gdwnttigtt mvikgvtkke iidregriys hrhpagywmp ggasntgadw
      301 vsakfgndlq klneaaakri ptgiisypli qkgerfpmma pnaygfeden lsseekftss
      361 megvaylery afelishlsk ekinviytag ggsksdvwlr iranvmrcpi ikmkhvsgav
      421 gaailaasav yfddiiqaan altivekefl pettlanqyd iyyqeflrel vkrgfikqee
      481 iya
//
LOCUS       WP_010603254             354 aa            linear   BCT 01-JAN-2025
DEFINITION  FecR family protein [Pedobacter agri].
ACCESSION   WP_010603254
VERSION     WP_010603254.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..354
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=40439
     Region          71..353
                     /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"
ORIGIN      
        1 mvdrsefnae dflvdstfqq ycagtdklci eywekyinah peqavviaea qklyvilsgn
       61 krqlnhqvnd fknqlspkei kvlktnrflw lkiaaaivvv igsfllylsy nnfkknepvq
      121 evftwatksg erkkirlqdg tsvllnakss lsiikgfnkk trevnligea ffdvvhckdv
      181 pfkvhtndfn idvlgtafnv kaypdeltse atlirglitm eavggkggii tlkpsqkvtf
      241 ykninepkks klakpslsrp eiainhytli kdstivetaw tknrieiydq dfdeikdife
      301 kwynveikft ntavekyrft atfsketieq alsalqdved fkyeikgnqv iisk
//
LOCUS       WP_010603261             169 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Pedobacter agri].
ACCESSION   WP_010603261
VERSION     WP_010603261.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..169
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=19379
     Region          5..158
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mpemliings arlngdtqkf isrltegmdy tlislvehyi lpyhyessyp pedqfellak
       61 eisyhkhivf atpvywyams grmknlfdrl tdwvtlnkea grnlkgktlk viavgtdgdl
      121 pdgfitpfsr tagylemdfk gyqyfnsant iteeelteir ksffsfisv
//
LOCUS       WP_010603260             202 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Pedobacter agri].
ACCESSION   WP_010603260
VERSION     WP_010603260.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..202
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23154
     Region          25..189
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mlrtnptfls fierfyehnq dtgitlktfr kgfrfveqge iikniyivkd gitkcfisee
       61 ngkdfiiefl gkgeivgele aikkinclcn vaaisevtay aipnhvflsl tetnqeftri
      121 llqelstrii qtssrasfqq lytleygllk llrlqadehf siskedmaay lgisvrsfnr
      181 tlqqvkskne dekftkflen lg
//
LOCUS       WP_010603302             282 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Pedobacter agri].
ACCESSION   WP_010603302
VERSION     WP_010603302.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..282
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30165
     Region          3..279
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mkaflgmgll gsnfvkamlr kgdqvqvwnr tatkakalet dgaiafddvf davrgvdyih
       61 ltlkdddtvn qvlelastgf ktgviiidht ttsvngaier taywknkgft ylhapvfmgp
      121 pnalestgnm lvsgdqevik kvedelskmt gkllnfgsee graaaiklsg nhflisltag
      181 lsdtlalaks lgvpttdisd lfaawnpgag vparlnkilt gdfgkpswel dmarkdaglm
      241 isaaqekgvk lnvlpavvae mdqwienghg sddwsviakn ni
//
LOCUS       WP_010603316             216 aa            linear   BCT 01-JAN-2025
DEFINITION  SCO family protein [Pedobacter agri].
ACCESSION   WP_010603316
VERSION     WP_010603316.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..216
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24423
     Region          58..213
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mnkiissiai gmlsvtilss cqqekklpfy geryaetikd aagvekidtv yqtipnwafl
       61 nqdsvlttnk atdgkvyvad ffftscstic ptmhrnlmtv yndfktnpdv mfvshtidfk
      121 ydkpsvlkky aqklgvdnak wqflygskds vytlaeknyl vavgedstak dgyihqgylv
      181 lidkdrrirg aydgtkedqv eqlkkdipvl laeykk
//
LOCUS       WP_010603377             484 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein [Pedobacter
            agri].
ACCESSION   WP_010603377
VERSION     WP_010603377.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   5  (residues 1 to 484)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 484)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..484
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53031
     Region          44..439
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkklynifya tliallitsc gkefleidpe qqaavnmvvv dlpttkaavm gtysllqsaa
       61 yygrsavilp dlmadnmyis rrnssrytsy dqyitntndg tasgswnimy rtivnanvii
      121 akgevlsvpq seqaevshlv geaytlrala hfdllrfyaa pynstpnash igvpvlaksg
      181 tskedivnpk rntvkegydq ivsdlkkais lmpatpvgft asnkghisqf aakallarvy
      241 lymedwanae amatdvissn kftllsnany vggstnfriq nnseaifevv ynatnnlgtd
      301 rlaaflfqgs sygdglatdd lynlytntdv rkgfmtrgsr tsaenpanvi tkynnvttfe
      361 egvkvirlse lyliraeara kqigkealai adldliakra dasaptttat gvalqnlill
      421 enrkefafeg hrlfdltrnk laftkyrtgg ltiaipntsl ktvlpiplae mnantnmeqn
      481 egyk
//
LOCUS       WP_010603394             261 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase, partial [Pedobacter agri].
ACCESSION   WP_010603394
VERSION     WP_010603394.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         <1..261
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          21..259
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 tytlkeenle nrlnisnkqr wliiliasls vfisssiyfy fyiqnkyksq navqrfleek
       61 nkavailete enerrrisgd lhdgvgqtla aaslqlkkak ndiaqlqkld dlidqaanev
      121 rmlshemtpe mvlhfglvka meqvidrlnd vqnftvfkff khvefddvnq vravvvyrsf
      181 qeltnnilkh akaknvgvhl nmsddeillm ieddgigydk neiklglglq nlesririfn
      241 ghlevdstig kgtttilrfs y
//
LOCUS       WP_010603428             153 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Pedobacter agri].
ACCESSION   WP_010603428
VERSION     WP_010603428.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..>153
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          1..>153
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mekplitike igrkyvigse vihalksvsl dinkgefval mgpsgsgkst lmnilgcldt
       61 pssgtyilng tnvsqmsdda laevrnkeig fvfqtfnllp rstaldnval pliyagnskk
      121 drearaakal envnlgnrmd hkpnelsggq rqr
//
LOCUS       WP_010603462             295 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Pedobacter agri].
ACCESSION   WP_010603462
VERSION     WP_010603462.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..295
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32601
     Region          22..191
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mltlktedlt pvqlqdylqy aiaprpicfa stvdaegnin lspfsffnmf stkppicifs
       61 parrvrdntt khtlenvlev kecvinivny dmvqqmslas teyakgvnef ekagftmlqs
      121 elvapprvae apvqfecvvn qviplgdnhg agnlilaeik lihinenvld engkidqqki
      181 dlvarlggdw ycrvtesnlf kvakplaklg igvdalpksv rlskvltgnd lgmlgniehl
      241 pnedeidlvs nhpevkevld atigdvtnre relhelarnf lkngdvdlal kvvll
//
LOCUS       WP_010603459              92 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase, partial [Pedobacter agri].
ACCESSION   WP_010603459
VERSION     WP_010603459.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 92)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142575
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         <1..92
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          <1..87
                     /region_name="SDR_c"
                     /note="classical (c) SDRs; cd05233"
                     /db_xref="CDD:212491"
ORIGIN      
        1 gsvkfpglsa ysaskaalht lteclafela etgikvncla lgsaqtemle aafpgyqspv
       61 mafemgkyva dfaktgqkff ngkilpvavt tp
//
LOCUS       WP_010603478             606 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein [Pedobacter
            agri].
ACCESSION   WP_010603478
VERSION     WP_010603478.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..606
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=67883
     Region          42..546
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          312..606
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkkyifiafv acltlatsck kgfldqvpnd rltleetftn rataekflan vyslipdefg
       61 qrnpntgrsa gvwtgasdea efvwgfnqan nvnigswdan sgfvndywnn fyrgirsasf
      121 fmanidkvtq ditpqlitqy knearalram yyfylvriyg pviilgenvi epdaptesvr
      181 lprnsfdeci nyiaselqaa adnlpvtpln drnyaritkg qalayrlqay llaasplyng
      241 ntdlanlknk dgkqlvsqty datkwkrasd aykayitqfv pstysllrkt nsdgsingyl
      301 scrdvfldkf nseiimsrld adiegrqyem tpyhsgkase vrgsaglgat qnqvdaffma
      361 nglsindags gyvttgftdy rapgspiatn tfnqwvnrep rfyvnityhn svwlntafgn
      421 vitefnnngn sgkatggndy tvtgyavrka mglgnwresn racilyrvgn lfldyvealn
      481 estpgdpdil nylnqirqra gipqygsgag qiaapadqaa mrtairkerr selafenvry
      541 fdtrrwkiae ttdngpiygl nitqnapnff nvvpfetrtf nkrhylfpip akdvnsddlm
      601 vqnpgw
//
LOCUS       WP_010603484             309 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Pedobacter
            agri].
ACCESSION   WP_010603484
VERSION     WP_010603484.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..309
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34581
     Region          43..306
                     /region_name="EEP-1"
                     /note="Exonuclease-Endonuclease-Phosphatase domain;
                     uncharacterized family 1; cd09083"
                     /db_xref="CDD:197317"
     Site            order(48,86,184,218,220,271,298..299)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197317"
     Site            order(86,298)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197317"
     Site            order(184,220,299)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197317"
ORIGIN      
        1 msefsrrnfv kglgialsas fignqagain qyasnqkfed shrilgcnir valpeddalg
       61 rgwearkdic ikiikaqkpd iiglqevlri qaediqkamp dyfafgfdgp emdinkdtyn
      121 giaknlvifs rkrysmisag cywlsetpei ggslawgtar arhanwvrll dkksgkefrv
      181 isthldhksq earnkqgeli vkesnqyqrd fpqlligdfn vdaknpvfki itdggwnety
      241 lsvhgnaepg ltahnfigee yaktkntgki dfiftrgkmk tlsakiikdq ingvfpsdhf
      301 fvnaevslt
//
LOCUS       WP_010603566             170 aa            linear   BCT 01-JAN-2025
DEFINITION  SH3 domain-containing protein [Pedobacter agri].
ACCESSION   WP_010603566
VERSION     WP_010603566.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..170
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18053
     Region          107..>163
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 mkvftflial mlchflgncq kissvgavne skmgrctgsa ycsackncsr cahcrsggtc
       61 gvcspvesqp lvrasprrka sthkasapsk qytqslsvnn sslgsytaea isvvklkeis
      121 lrsgpglsyp vietlngnqk vkriakkgew invkvlssgk igyckltein
//
LOCUS       WP_010603628             234 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein
            [Pseudoalteromonas maricaloris].
ACCESSION   WP_010603628
VERSION     WP_010603628.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..234
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26252
     Region          13..>93
                     /region_name="DUF6697"
                     /note="Domain of unknown function (DUF6697); pfam20411"
                     /db_xref="CDD:466560"
     Region          154..234
                     /region_name="COG3183"
                     /note="Predicted restriction endonuclease, HNH family
                     [Defense mechanisms]"
                     /db_xref="CDD:442416"
ORIGIN      
        1 mfkqgqeysr keissliggq iqgymgtrnk kvigvyleln snpnapreil cgtgidiakh
       61 glwlsqqdep vpifvkrkan ewvyqglfsv estivdgstl ekirkqagrk yqlsraiyls
      121 evseqlefeq qvtwsraltr aqrverlska eatpkaikvk ttvyirnpdv vaealiradg
      181 icencnkpap firksdntpy levhhvlpla qggddtienv lalcpnchre ehfg
//
LOCUS       WP_010603661             701 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010603661
VERSION     WP_010603661.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78072
     Region          5..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mkintlyaav clsllsqtts anenqkdele rievqgsqyk stgtksslap inapfsishi
       61 dqdtlqlrqa dsvnaalryv sgitpesrst vtifdqytir gfesyrnyyd glelqsnnlw
      121 nlypqvdafa tdtievlkgp asvlygsapp ggmvnqiakl angteqtqvr lrvgsralke
      181 igvdhggvit delsyraial srtsdgqqkt teeertvfap slrwqpshdt altaqlyyqd
      241 dpkaipstpl hsvgtltras ygyldadafa gdinwsnfdr ttlmaglkle hnlsdnwalf
      301 anwrytdaeg lqqntynqnl iadsdtilar aayktdetqh gyvldnqlst hftvgnsshh
      361 lllgfeyktl sstvgywdtl gtgtpninla apnyaafdvg alplnfytea hdieqsnraf
      421 yvqdevtisa ltllaglryd sftsdvtadk nyagtewqte sniddtqltg riaalyqlds
      481 gwrpyvsysq sfepvageds vtqqafkpte aeqwelgvky qsrdtqltfa lfdltkqnei
      541 inskdfvtkt qageiqskgi eleashtfne qvdvqfnath ldqkvtknel dqdlvgkrlv
      601 wvadntaslw lnyypsllsa lkvsvgaryv gesyvgkyns dtvpsytlfd iafdyelseq
      661 arltfsisnl sdkryvgacy desncwmgae rkadvglhyr f
//
LOCUS       WP_010603701             130 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pseudoalteromonas maricaloris].
ACCESSION   WP_010603701
VERSION     WP_010603701.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..130
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14678
     Region          11..121
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mveaerpynp tiksqdakyy dfeklltcsn tlvvvgevse qivatgyvqm raskqqlqht
       61 qhgylgfmyv apehrgkgln qaimehliaw cktqnvndfy ldvyssnaaa irayekagft
      121 pcllemklhl
//
LOCUS       WP_010603712             370 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Pseudoalteromonas].
ACCESSION   WP_010603712
VERSION     WP_010603712.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..370
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41614
     Region          136..365
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msaffrypta wlvttiftwl avaipslvya qqkaqwlpwv qhigvlilvl lcinesekyy
       61 gykvrysmlf vlalliqsin ltspaaihli ynvklvgila fyvplsfalg yilvtsclyv
      121 asqyffwghg feylnavlfa cfqlfayvvc krmqkeqeak ealqlahsql satqsllsqs
      181 iakqerlqla relhddvghq itslivnldv arrtaaaplt elldscylqa kdtlkcirdl
      241 vsdkrsnehi dlhdallrlt esiprlniel dyehhpllek lsyancilkc cqeaitntlk
      301 hakadkmqvr vycqqglkvq isdngitlns irfgnglagm qeriqelggs ldvsthqgvt
      361 ltihfgatng
//
LOCUS       WP_010603750             634 aa            linear   BCT 01-JAN-2025
DEFINITION  S9 family peptidase [Pseudoalteromonas maricaloris].
ACCESSION   WP_010603750
VERSION     WP_010603750.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..634
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=71622
     Region          202..355
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          380..634
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mlrillcasl glapsfglva kevmtpdklw qvkrvsalgl skdkthviyr vttpsvennd
       61 fdskvyqvpl kggvsqllsa yqgilsddni spdgskklfh dtvnveavla tdrhkaltqa
      121 dayvfddlny rhwdtwkdgs vkhvfyqdlt teekvdimkg mpfdsptspf ggssdyvwgp
      181 kgeniyyvsk kltgaeyass tntdiyrynl askkttnlte qnlgydkspe fsstgllafl
      241 rmdeagnead kndiivklgd revnltahwd gtvssfewsh dgkhiyfiap vdgtiqlfqv
      301 avnsktkanp kikqltkgmf dvnsivaald dqlvvtrnsm nqakeifrfd lnskklvalt
      361 nvneafyadl dlpnvekrmv ktkdgedmlt wviyppnfdk rkqyptllyl qggpqsplsq
      421 fysfrwnfqv masqgyivva pnrrgmpghg vkwnkdisqd wggkvmqdyl daiddvakes
      481 yvdnkriaav gasfggysaf ylagnhdgrf ktfiahcgif dlrsmygtte emffvnnelg
      541 gayweqnnaa iskaynqfnp isyvdkwdap mfvihggkdy rvplsqgmqa fqaaklrglk
      601 srflyfpeen hwvltpqngi vwqreffkwl eetl
//
LOCUS       WP_010603754            1009 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010603754
VERSION     WP_010603754.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..1009
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=109825
     Region          1..1008
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msiaavainn rvvtlvltvv mlisglyifn gmsrledpef tikdaliitp ysgasaleve
       61 qevtelleka vqqlgeldkv tskserglst itvtikenyn ketlpqvwnk lrqkiddvkp
      121 ylppgagpsl vmddygdvys ifmvvtgdgy sfkelktyvd nlqqqlllvd nvgkittfge
      181 kreaiyiefn rarmaqlgms pdvitaqlss kglvvdagka hvgsanlais itgaftqvsd
      241 fekllithet kqfylgdiaq vsrgyespss qliyydgkag iglgistvsg gnvvemgeav
      301 laklsaleve rpagielgyv slqsegvkea isgftsslae avvivivvll ffmglrsgll
      361 igfvliltia gsfiflapmg valerislga liialgmlvd naivivdgvl irmqkgesak
      421 saspkvvnqs alpllgatli ailafaaigt sndatgeycr slfqvvmvsl llswviavtv
      481 tpllcvmflk apeindpanp yqgtfytkyr nflaycirrr ylssasvigv fvlslwgfsf
      541 vqqnffpsst raqfmvdlwl pqgthiedtq knaqsvekyl sqlaniehvt ttvgegalrf
      601 lltyqpqqpn ssyaqflvdv ndyntiktli pkietdllqq fpnalvyasp felgtgtigk
      661 iqarisgpnt dvlretsdkv fevfskesna kgvrtdwrnk qlyieavlae eqananginr
      721 amvaeaikea fegvttgvyr ennlllpiiv raeaiersdi tnidnlqiws pnaqkmiplr
      781 qvllgfetkl edglilrrnr ertitifadp itgtaselfa mlkpkveaip lpsgytlewg
      841 geyedaskae qglassipvf ilamilitiv ifnslkqtlv iwlcvplali gvtagmlatn
      901 qpfgfmallg flsligmlik naivlveein leqsegkpli dsilnsgvsr lrpvamaalt
      961 talgmiplif daffvsmavt iiaglifata ltmivlpily alifkaknp
//
LOCUS       WP_010603799             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Pseudoalteromonas].
ACCESSION   WP_010603799
VERSION     WP_010603799.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..238
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25599
     Region          1..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnsviqlnni kkrfqtdeia tqaldginlv vepgefvait gpsgcgkstl lsilglidep
       61 sngeyfisgn qafnlssder ahiranhigf ifqafnlisd lnvlenvmlp ltyiggisqk
      121 emeqkakdal amvglenrvn hfpsqlsggq qqraavaral inspdlilad eptgnldsnn
      181 aqqvlgllse lhaagkticm vthdiestty asrvismldg nilrdkkqld rvskvvga
//
LOCUS       WP_010603832             472 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Pseudoalteromonas maricaloris].
ACCESSION   WP_010603832
VERSION     WP_010603832.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..472
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49962
     Region          25..466
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,281,284..285,288..290,293,321,325,377..378,
                     382,386,402,405..406,409..410,413)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mledtvnted qtalgagqkr vlfslavvli lptlgmssin vllptlaeef gvgqalvnwv
       61 vvayllslta filgagavgd svgrkralri gisvfcvgsi vaglsvnlwm liaarlfqgi
      121 gaalllsqvf alasvampkr kvglamgllg ttaaigtalg pllsgamlew lswqftfwlm
      181 illggaayfl iarflpddva nppepqrfdi igsvwlsasc lfyvlampss ssfslvlhsv
      241 ffffsvafiy cfvksqkraq fplvslaflk hklrntsliv sfivdaiams tlvvgpfylt
      301 yalglspvtv glivsigpci aavagypsge vvdhfgiafa mflgllmili gtisfailps
      361 lfglygyvva lfvltpgrql flaahhtfvm ttvaekekgm gsglinlckn lglmtgasll
      421 ggvfsvllqv ksatlaspaq lnmafsltfl laalfilvsl vavfvisrkq af
//
LOCUS       WP_010603862             890 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas maricaloris].
ACCESSION   WP_010603862
VERSION     WP_010603862.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 890)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 890)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..890
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..890
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=100020
     Region          108..852
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mlfkllipll awliwfggva fattdhqfnl pkatlqqrll diaaqsgwql saaeipdnis
       61 veqitgrytl eqvlltsfqq aaydfsldpe qqrifvtpkk lesaqhferi ivtgvsgknr
      121 silnssisit qlaslqlekq tpyssaealk nitgfwveds ggetnnnvap rglrggegfr
      181 fislmedglp vtydgiwgdf flrpdlthqa ieavrggssg iftvngpaam vnyigrrgse
      241 npfnlvkvsq glsydytrfd gvfsgalnde wfytvggfyr tsdgirepgy qsdlggqvsa
      301 rmswltdafe ldfsykhlnd ktsfyaplvm qnsgeirelv slpyddgtll sddlrsltff
      361 tpegrvqrdl kdaqqtrlns ytllfntplf ehinlsnrtr fsslnndlyt lmnlgnqtiv
      421 datsrlqhad itefkrhfan salrprylry sdntlvanpa tlngnglvta syplysryrq
      481 qqlvnhfsvd yldaqwsltl ghiyarsdfd elpldkwlga lltdvkhqpe rldivlvdgq
      541 envianfteq gflsyagpvy lsgsglsqsh slyanidwql tenlrvdlal rnehlnltst
      601 lleggksytd sskatyshyl pattlrdsft qnalsigany qigdamaifa rysdafempr
      661 linygngrgw akseeervqq dfgqpirlal gevglryqta dwqfsgalfe tkfdplpltv
      721 yrgaattqqa vsintqtrgl efefdyqysp alqfraigvw qdagfygipk qlpqsefngn
      781 qitrtpelql rltpeykagp itaaitwsyv gkrysdianr falpayqtwd lftelaineq
      841 lsaqlevknl tnalgltegn prddlshqea ifyarpifgr tiklslsylf
//
LOCUS       WP_010603867             840 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas maricaloris].
ACCESSION   WP_010603867
VERSION     WP_010603867.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..840
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=93002
     Region          46..816
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msnntsrynk hlialaisga llgshtavaq akemqettek kklldleriv vtgsggrgqt
       61 klessvsvtt lnaeqlarea plgtadlles vpgfwvedsg getnnnvapr glrggegfry
      121 igveedglpv vydgvwvdfy qrqditiehm eavrggtsgl lttngpaalv nfitrkpddi
      181 eeatirltaa dygmyrgeff ygtpisdnwk msiggsyrrs dgvrdtefta dhggqlrlnl
      241 vrefdkgqlt lsakhlndht tffvpiplrd qsdpkgiagv dpqhgtlign gqrflhylqp
      301 dgsyktrdlk dgqhtkfstl gyhldwelsd rwllntagry sqfendmyil lnfdnstlvn
      361 antrlgqqdv qnmldqfasd gavaaryryv dsgeiltdvs nlngnglvtt syplysryda
      421 eqfvnklnft yegdqhtlti gwlfayvdad slpvdkwesq fltevkdnar lldivavnsn
      481 qqvvgqltdh gstgyapgwg qatafgtsts nslfineqyq atdnlridgg vriewlelds
      541 tasattfaqp vagafdsagn didnnlanny vdmpsnkfls ktrsetetaw tvgfnytfsd
      601 dvsvfgryad afemprlmsf gqnihsgvda dfndsvnltf selgaryagd sigasltlfr
      661 tkfndlvern ftgsngevan qtidtvtdgl efetvwqahd nlqleltgvl qdpkmegftg
      721 afahwegkqv krtpkvqlrl tptyyfddgd iyltihhlge rysdgenkfe lpayttidmg
      781 vnyrftdava lhvkatnisd elgltegnpr aindvqagyd yyyarpilgr tisasltlnf
//
LOCUS       WP_010603864             191 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Pseudoalteromonas].
ACCESSION   WP_010603864
VERSION     WP_010603864.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..191
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21959
     Region          26..191
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mppllsfkrk avdtttaaan ddlarrqqve elflkqqqkl irhimgkgld kreaedvaqe
       61 afvkllgleq dnvsnyiaay lykiatnlai dklrrkarsp fddrehdsdq mpqpcasanp
      121 eqnhhnqell kemekslasl pdkcrlafll ykirgqsyee ialtlqisps mvrkyvlrav
      181 rhcyqqlqhe l
//
LOCUS       WP_010603868             298 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010603868
VERSION     WP_010603868.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..298
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33204
     Region          33..180
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <184..289
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mvedyrelvk plaqrvllcc kksgdhesqv qklsmhirsa pteplhciyt lslavvlqgt
       61 kqisidneil fcsagqamlt tfdlplishv teasrhhpfv gmlvkldynl ilqtaaelnl
      121 skpakqsvsk sisihhidag ltdalsrlfs leydanlrds lapliekeiv irllqgphae
      181 tltrlafegs assqivkavs wlktnfmrpi einelaervh msassfrqhf ksttgtsplq
      241 ylktlrlqea reqmlingld anqasgvvgy espsqfsrey srlfglppqk diqrlkls
//
LOCUS       WP_010603873             598 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 3 protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010603873
VERSION     WP_010603873.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 598)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..598
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64318
     Region          48..>435
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 msfitsahat aaqvplttsq mlgqklmldf ryycgeskkp sgdcraamtt lppelsklis
       61 kydiggailf aenvqntaqi vsltnalqsa aqqsksqlpl fvaidqeggr varinreqat
      121 sftgnmsiga typkqgdtya tkvasaigke lnslginvnf aptvdvnsnp nnpvinvrsf
      181 senpkvvakl glaqvkafea agvlsalkhf pghgdthvds htglprvdhd rdkinqqdll
      241 pfaeiikasp pgmimtahiq ypaldnskvv nsqgesmirp atmsyqimtq llrhelgyqg
      301 vtvtdaldma gisdffnpvd atietfnagv dialmpiair nradikrfeq ymaqlakaln
      361 tnklnqeqls ssmariaklk tklpqssasl aianstlgnp shrrleaela laaitevknd
      421 gvlplrdnaq vvhlimpdrq kcfaleqalq thsknsltls ctslqaydpn iahdaikqad
      481 viiaahaspp qsaveiggmd dvkklrehgv arnvqpealk allqygqklg kkqlfislra
      541 pyeistfgpl snavlasyay nvdvnhdkkv agpaytalak vilgiakaeg slpvtvnh
//
LOCUS       WP_010603878             672 aa            linear   BCT 01-JAN-2025
DEFINITION  S9 family peptidase [Pseudoalteromonas maricaloris].
ACCESSION   WP_010603878
VERSION     WP_010603878.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..672
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=74189
     Region          62..236
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          187..352
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          423..668
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkyflagvai assactvqaa sleptdifnl eyanqiditn dgdkvffvrn rmdiksdrkv
       61 gniwsvdlat namqpvtsgl hmdyspvlsp sndriafvst rdgssqiyvk wlatgaiaki
      121 snlahgpsgl hwspdgksly fsqfvpsqka ppvsvagkpk gaewakppvf idevyyradg
      181 agytepgfnh ifkidanggn akqltsgnfd hggelsfadd akalyfsanr hkdnqlnptn
      241 sevykldlns leitavtdrv gpdnhpevsp ngrylaylgy ddkktnyens llyvkdlksg
      301 etktyaadld rslasvtwaa nsrgvyvsyd segkttlgyq plkgrfeqit daigsvsfgr
      361 pysggdyais drglvaftla dtqrpadvai vkrgeprpit klnedalgdk tlakveevwl
      421 ksthdqlpiq awvayppgfd kskkyplvle ihggpvanyg phfsaevqlf aaqgsvvlym
      481 nprgsdsygk efaqtihhny pshdfddlmt gvdhligegy idkdrlfvtg gsgggvltaw
      541 tvghtdrfaa avvakpvinw ysfvltadfy pffadywfpg kpwehmehym krspisyvgn
      601 vktptmlltg eadyrtpise teqyyqalkl qgvetamvri pdashgitkr psnllnkvay
      661 iqwwfdkhdp kk
//
LOCUS       WP_010603940             229 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Pseudoalteromonas].
ACCESSION   WP_010603940
VERSION     WP_010603940.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..229
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25484
     Region          1..220
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mlsmrhlska yytdtiktqa lqpfdlrieq gefvsvvgps gsgkttflni tglledfcdg
       61 syeldginve klsdkakskl rnekigfifq sfnllpdlnl ydnvdmplry rklsskerhe
      121 rimdalnkvg lasrkehyps qlsggqqqrv aiaraiagkp sflladeptg nldskmadsi
      181 mellmdintq gtsvvmvthd thqaakaqri ieirdgviie rkhcnkaia
//
LOCUS       WP_010604067             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase
            [Pseudoalteromonas].
ACCESSION   WP_010604067
VERSION     WP_010604067.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..412
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=45777
     Region          13..340
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 makenvdvli igagpagtmt aakliqaglt vkivershfp ryvigesllp qsmqhledag
       61 fmdalvarny qkkiganfkq ddfqeffdfs knytdgwtwt wqvprddfdn vlaeevqkmg
      121 apiefgtsvv danmdleepi ikvvneagdv qeiqakfvvd ssgygrvlan lldlnepssa
      181 ptratlfaqf kpadgietga ennkvtilvh eedvwvwlip fsdgrvsvgf vgnpeylesa
      241 egdaktrflt ylardqhasa mlegmalcme pkeikgyskg ikqlfgknfv ltgnasefid
      301 pvfsagvmfa iesgaraadl ivaqlngeea dwqqdyeahm lkgiavmrty iegwydgrlr
      361 rlffsdnkpe kiksqitsvl agyvwdetnp fvnrsektln llselhnnpe ma
//
LOCUS       WP_010604080             674 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein
            [Pseudoalteromonas].
ACCESSION   WP_010604080
VERSION     WP_010604080.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..674
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=74419
     Region          146..674
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mlskltikqk itlgfsalgv llllacvlay lalaqiksan qnmgqitlpi qrsadalqle
       61 qlklsklvsq aytleseqdi nrarqqfttq qqlyverqrh ltsltqampe fvtplkqtla
      121 lgeqlsraae qmlqakadvv qaqqriqsqy qalkqdkeqa snamldleli etdktrqlee
      181 mvgtgvridd mlftlennsq risgltleqv dqhqqdmlfl ldniennltf lkrqaygmda
      241 ddllnqfseg mtklreklge pghlyvavqe klrqqqqaam lykqseqhaf ailtelekmq
      301 qsanaafnrs qnnaetlier aqntaillvi vfialgafis vstsramlgp laavnkmlky
      361 laagdfskqm skrsddefgq lidninqvkd nlrallesin nqvhelegls esslseskqi
      421 annateqmrr mdnanrlaqs isasalavse rssdslasih tanqhktevs kytqdnkehi
      481 lslstrmsea vesmtkltth senigsildt ivsiaeqtnl lalnaaieaa rageqgrgfa
      541 vvadevrtla srtqestnei nqmiaalrqd thsaseains gqrdvascvk qsealasamd
      601 eianailqvt qlseevsqaa dhqatdcqqi eqvmldaqst anenaqamqs lakgseslss
      661 fshrlatlve rfkl
//
LOCUS       WP_010604119             373 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Pseudoalteromonas maricaloris].
ACCESSION   WP_010604119
VERSION     WP_010604119.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..373
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41050
     Region          6..346
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msdpllftqk klgnlilpnr ilmapmtrsr ttqpgdipnq lmakyyaqra sagliiseat
       61 qiscqgkgys ftpgiytasq vagwkeitha vqqkggrifc qlwhvgrmsh stfhedgqpv
      121 apsalapdaq vwvvnekgvg emvdcptpra latqeiqsiv edyvhaaena mmagfngvei
      181 hagngylidq flrrssnqrh dqyggskenr irfavevita isqaigpekv girlapfitq
      241 rgmqdeeaid tillaaehfn rlgiayvhla eadwddapvv mesfrqalrr kfhgaiivag
      301 nyepeqaeal ieqglvdfva fgrkfisnpd lvyrlthqlp lspinpdapl fggseqgytd
      361 yadfqqlrak gai
//
LOCUS       WP_010604146             312 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010604146
VERSION     WP_010604146.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..312
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34198
     Region          49..305
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 msvkkrglgr gldallssak pkpsaaapvp nqqeavatvs eapaesaveq elqrlpiewl
       61 kpgkyqprkd mseqaleela ssirsqgilq pivvrkvttq sfeiiagerr wraaqlakqd
      121 tvpclikdvp deaavaiali eniqredlna meeaialdrl lnefelthqq vadavgksrt
      181 tvtnllrlnn lnddvkille hgdiemghar cllaltgeaq seaartavak gltvretekl
      241 vrtilepvek keakqkdpdv klleqqlqen lgakveinyn qkgkgklvis yasldeldgi
      301 lgrinsemne ae
//
LOCUS       WP_010604124             317 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010604124
VERSION     WP_010604124.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..317
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=36551
     Region          3..310
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mqsinqlsqq fislckdkrk lsdhtlkayq idlkqfmqal denksikdis kvdlsqfhqf
       61 lvdselsnts ikrkmacvra mfqwlereef ielnpfhkfq ldiklpkrlp rnvslsdlkr
      121 llkqarknck nlwvessnty svsqkrmlne ftslialelm istgirvsel agicltdiyi
      181 nekkikilgk garerfvylt dqeiakllkn yiesraicap hcdhllinsr gepastqflr
      241 klikklsqqa ytqlkvtphm lrhsaacell esgldirfvq rllghssist teiythvtdn
      301 alqkkitkan vrkrias
//
LOCUS       WP_010604214             356 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010604214
VERSION     WP_010604214.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 356)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..356
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40334
     Region          79..346
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mtkyhpyskp dqvealkfal lrrvaaycmw lhagligvfw hlevnilawv nvgsvlmwyv
       61 giklidaskp sialrvfcle vavhatlvca ylgmslgfqy ylwtvsclml ldyqlrlrna
      121 viysvvlitl favlellfgd vayqyryqql ipyvhfanvl icgipmiyti shirkmtvqq
      181 rdkleelaah dpltqmfnrr yarelithak encisthspl clvmadidhf kkindtfghd
      241 kgdqilksva etikahihpa diavrwggee flivlapcss geamqrmekl rraveatsfe
      301 neilkvtmsf gvanwdpsqt fevviqhada alydskhsgr nritaapilr vsegvs
//
LOCUS       WP_010604231             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Pseudoalteromonas].
ACCESSION   WP_010604231
VERSION     WP_010604231.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..218
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23852
     Region          11..217
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mlefvdypak gqhkasiiwl hglgdsgngf lpiaselnlp delgahfifp hapeqpvtin
       61 ggmvmrawyd iksfdldkra deqgvrdssa qvealiqaql dkgipanrii lagfsqggvi
      121 alhlaprltv klagvmalst ymcvpeklsa eaqqseltif mahgsadpvv pmfagehafn
      181 tlqqqgyevs wqdypmehqv cleelkaira wlitrlsd
//
LOCUS       WP_010604264             684 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S9 family peptidase [Pseudoalteromonas].
ACCESSION   WP_010604264
VERSION     WP_010604264.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..684
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=75791
     Region          <36..>287
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          <40..149
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          406..658
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkllksalal amgftsaasl asdtitiedi pkiqsvssts vspdgelvaf trsvprelyv
       61 dqngsnysel yvvddegver pfitgkvsis siswsadgqf iyfltkkked kqralyriav
      121 nggeaqkvls lkgtgisays lspdgkqvai lampaadkse kelkklgfma evyelglknk
      181 qlhiidlaas ekpltpaaln iegyvseinw addaskllvk tqptaliddk ymksqwhvld
      241 aktqqittsf ktegklgtae fshdgkyiai lgaedkhdpa tgrlyladaq sgkveewipn
      301 fmghigdfew snrknqltfv anvgaesfvg qikvgsnkyk klikegkfia snlsisdsdk
      361 tialrantak hpnevfvirs skatrlsnsn pwldnkrfak qeainfkard gveiggvliy
      421 pldyqegtry plimsvhggp eshdkngwlt sysdpgqmga argyavfypn yrgstgkgvd
      481 ysklgqgdya gkefddlvdm keylvntglv dtkrvgitgg syggyasawg atkltehfaa
      541 svmfvgvtnq lskfgttdis nemylvhars ypwdkwqwyl erspiywagq sktpllimhg
      601 kddprvhpaq smelyrymkv qgkdvrlvyy pgeghgnrka aaqydyslrl mrwmdnylie
      661 gkkdmpdyei dhaaklkavk dank
//
LOCUS       WP_010604268             204 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010604268
VERSION     WP_010604268.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..204
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22282
     Region          1..200
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mytlyylpga calatqvilr elkqpfelvd krgvdnflai nptgkipaln dgenclvega
       61 aillyllnkh ennllpqadi lqkqqaieni lfanatmhpa ynrlffatga iadeharqpf
      121 leaaavaine lwvlvekkla qqsflggdqv stadimlavy arwgtyfpvd iiipekvskm
      181 laavearpsf iasiaaeqah stda
//
LOCUS       WP_010604316             170 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Pseudoalteromonas].
ACCESSION   WP_010604316
VERSION     WP_010604316.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..170
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19425
     Region          17..149
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mskfaikwan visdnkgkvl aylnsilkcp ylaedalqdt firlssmsht qnaqinntts
       61 fcfqvarnia idmlrkqsre slvaleathv eymsdtdsdi enkvesaqld rrmdstiqkl
      121 strhqniisf yrtgrfkqke iaklykispt lvnfmikeav hscqkeflah
//
LOCUS       WP_010604320             349 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Pseudoalteromonas].
ACCESSION   WP_010604320
VERSION     WP_010604320.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..349
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37895
     Region          52..342
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          237..339
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(241..242,275..276,279,283..284,287,329,333)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mkiktlsllv amavtanana ntteptegvy lgvfgdyyda dwqnhrdmag ldveestgwg
       61 aeigyrfdky wsgrleyadm dfdlggisng sldaerygid glyhfdggpf yglvgikkmn
      121 ldvisdntfa nvgagvrhyf tdhlfvnaea avyqgleagf tdvggkigln ysfgsagkse
      181 evapapapvv aeapqdsdkd gvvdsedkca ntpmtdavda sgctlyetne dkvnllvrfp
      241 hddasfsqqy vddinavakf lkehknadvv ieghasavgd adynqklser raknvaeklv
      301 dmgidsmrit tvgygeerlk npantleaha enrrveahvs skekvkvkr
//
LOCUS       WP_010604332            1045 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: non-ribosomal peptide synthetase [Pseudoalteromonas].
ACCESSION   WP_010604332
VERSION     WP_010604332.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1045)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..1045
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=117101
     Region          6..1036
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mrfdfslaqk dvyfdqlhci gnakyniggy vdissanvts lleasdqvia snpmfsltie
       61 hehdgpkarf dnalhikstv vdyrdaiepi ksaqelvkei fsqpfdlkgr clyktyiiql
      121 tdqriwfvgv ahhllidgwg falwaealsk ayeskeyqvn ehaqqnyfeq dsvylesery
      181 qkdkefwksy lhcskrnili pnrkleskss servvfsvar dkyeslfsnk gflakspgtv
      241 flslvfimfs rlyrernfnv glpahnrksa kqkndialyt svspislayt sdtsfdqfls
      301 yvaseqkkiy rhqkypighi vsdmgpears glydvcvnfl klnnscrfak ahasyhyien
      361 pfqttpfnlt iwdngevqpv elqvdyhmgy fskeeiaqll eilfslleqv snnpevklse
      421 lmltseknks lslsdtglde eiqpfitlfl eqvrkspntv avscqnrelt yealdlsstr
      481 lalrfkeigv kagdlvglml hrsermveai valskigagf vpmdpsypvs rlkhmahdsn
      541 isllvidsdf selafeltdk iyiveslcen taveigsttv akndstayvi ytsgstgtpk
      601 gveisnlsla nfllsmrkkp gisrgdrlla vtpfsfdisi lelllplisg atvkvfpsri
      661 thdlqglvde inkpdtsivq mtpsawklvl asgwqgkpsl kalvggealp qhlateltsk
      721 vdalwnmygp tettiwssci rveeswsvns ighpiantqm aildsqhsfm pvgwtgelyi
      781 sgkglakgyf nqpeltasrf iscngerwyn tgdlakiqad gsvefvgrid tqvkfqgyri
      841 elgeiesilk klpnisdavv liktsdsghq clcayyisen delssehlra aaseylplhm
      901 lpshwqalka fpltpsgkld skslslpssf aqvsttened rliqelaavi chhlqiphld
      961 aetnffdaga rsqemvelvp klnealslsl tvvdmfsyps lnalaqvida satrnseaks
     1021 rteqlqsgks rlqrrlntrk qvney
//
LOCUS       WP_010604343             242 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SURF1 family protein [Pseudoalteromonas].
ACCESSION   WP_010604343
VERSION     WP_010604343.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..242
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=26617
     Region          5..241
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mdlgalfkgr skppilaali vvllcgslsy wqwqraqqkh vlqhkveiek slgvaneqqv
       61 tsqqltqyvn aevsitgnfv gdavwyldnq vvkgrvgfdv igiikisetd eylavnlgfv
      121 pqqasrvptv fslpsgtvsl pvyikssask rftlaksaae eatkqsviqy idvdylsaes
      181 gkpllpliay mtknrfagte phyqpvvmsp qkheayalqw llialaavvi gwklskkenk
      241 nv
//
LOCUS       WP_010604420             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010604420
VERSION     WP_010604420.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..135
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14528
     Region          1..58
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 minnlqaerk rlglspteva dkisvglaty yrweagkaip sdkladlakl gfdvnfivlg
       61 thsassnstv gltreqlsrs lttflfntgq lgllnksest dvsslvdmai ytieqeigen
      121 lesdrtvktt skats
//
LOCUS       WP_010604468            1068 aa            linear   BCT 01-JAN-2025
DEFINITION  non-ribosomal peptide synthetase, partial [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010604468
VERSION     WP_010604468.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1068)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         <1..>1068
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
     Region          <1..127
                     /region_name="entF"
                     /note="enterobactin non-ribosomal peptide synthetase EntF;
                     PRK10252"
                     /db_xref="CDD:236668"
     Region          130..>1068
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 eylrallpey mlpsryigvs qwplspngki dknalkakvn qpiaeqimqp qsetevklls
       61 iwssilntpv teidlnssff sqgghslrav kmqaaiqaef akslslqtif kaqsirniah
      121 cldeqadyil gatiqakadk sqlhplsyaq krlwfidnln qgsseyhits avqlsgkfdl
      181 asaqqsftll ierhetlrtv fiksadgvvm qkvnhtkpfq ikhlslthlt gdaqklaler
      241 liheqnsqpf dlsldqmlrv savslaedel aiiftvhhia sdawsmgvlv nefcsiyqaq
      301 vtqqpqdlpp lsiqysdyah wqqqsdtqar issqlhywqq qlqglpsvhq ipldharpsa
      361 klsngkrlqr klpsalaekl qrlataanit pfmlyhgals lliskysyeh dvvigtpvan
      421 rcqtelepli gffvntlvlr sdtqertlsa ffqhirdvnl aaqehqevpf eqvvdaccns
      481 rttqytplfq imlnmnntes ssftlsgvea nlipvaadrc kydlefavql ssscpvlmlq
      541 ydtslflpss melmladfaa lltslsectf ettmlseltl sssergyigr eapqelrlqe
      601 sfqqqvnrkp kqaalqfsns tmtyadlaaq vqdlacylvt hfppharigi clgrcesllv
      661 svlailradm tyvpmdpshp eqrllriaeh aelaaiitkp ewqsklqgvs iatvvdinty
      721 ektaktklae vysnpvayvi ytsgstgtpk gievlhkgls nyldyaakhy lcagilrsvv
      781 sstlsfdatl tsllaplisa ktitilpeed tladlyqclr rgpaslfklt pshlkalcai
      841 hhgesittph tivvggeqft gqllgqcqrw lngatfvney gpsetvvgcc dyvvlpgqke
      901 pasaavsigr aiantqlyvl dpylqvapkg gvgelciagf gvakgylqqp qltaekflnw
      961 qgeriyrsgd lvrqrkdgnl vyvgrideqv kirgyriela eiealavaft gveqavahvi
     1021 egknnsaqll lyitlkptlc gneqtsllkr ylaeqlpeym vpsqfvvl
//
LOCUS       WP_010604504             224 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010604504
VERSION     WP_010604504.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..224
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24407
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnsviqlecv ckhfytnkik ttalnkvslq vdkgefiait gksgsgkstl lnaiglfsni
       61 dsgslhlngf dvsaisqknk lkyrrehlgy vfqsfnlipd lsvldnimlp lkfrgvphkd
      121 rlglaeqele rmeliarkdh ypsqlsggqq qrvaiartma ckpsiilade ptgnldektg
      181 qrvldillev ndtsastiim vthsaaaasv agrrvsmvdg elvn
//
LOCUS       WP_010604522             894 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF349 domain-containing protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010604522
VERSION     WP_010604522.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13280064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..894
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..894
                     /product="DUF349 domain-containing protein"
                     /calculated_mol_wt=101134
     Region          <235..790
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          550..623
                     /region_name="DUF349"
                     /note="Domain of Unknown Function (DUF349); pfam03993"
                     /db_xref="CDD:427636"
     Region          627..692
                     /region_name="DUF349"
                     /note="Domain of Unknown Function (DUF349); pfam03993"
                     /db_xref="CDD:427636"
ORIGIN      
        1 mifkhlftpk wkhpkvdvrs qavdkldlsk datllhtlal edesaqirkk vltkvndlgl
       61 wwkvykqdse lkelaeqkis savinqdtal qsnireeyie ryapaktlek valietdltn
      121 kvkllkrlan atlieksfke gdealqiaml eliaqhslek svlkaakgea ltsltgsleq
      181 qrlakemptq vaeqtrvvla klnalrdkqn yeivngqaqq lfaqwqsiel kwldaetvsa
      241 ldakyqqvad klnrhlnelq vkhqaqqael mqkqnealev aeltaeleai eksveiackt
      301 ldlashdalv krsevlkgkv sapqyvtvea lgeftrklqn ierdladlpa liaasetfnn
      361 alaelkavev ptsleslytq vqaqkgryva arkaldslpk vlhksakael sdvsqvfmta
      421 ieplkneqek alkiakkkar dvqrlidqgr fnvafgvfng fieqfelltp sykkqlenqh
      481 eslsqalkdl kdwqkyaatp kreellaeld nklaeeavdp vkraeevkll rvrwnelghv
      541 eteqekaqaa qfdekiellf vpcrtyfaeq evqreqakia reavieevka llgtldnegi
      601 dwreveaqfn rlakawknag nvdakvyqkl nsiyrehhqa vyeklkafhq anavektklv
      661 etaqqqleae dlaaacdllk slqkqwqqig fagakqehtl wkafrahnda vfekrsaqya
      721 eqkaqeksqe aeqrqllaef dnkvieavtq nelvairnel nmfivvpglk qeknrllsqv
      781 ksklddlfss qrrekfnelv eavdtdgdip sswqgsnkts lnaaqlllrl eiltnqsspe
      841 alqsermseq vamldaklqg eessletyli sylaeaekad ivtskgrlla vlna
//
LOCUS       WP_010604550             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [Pseudoalteromonas].
ACCESSION   WP_010604550
VERSION     WP_010604550.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..251
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=27305
     Region          5..249
                     /region_name="THN_reductase-like_SDR_c"
                     /note="tetrahydroxynaphthalene/trihydroxynaphthalene
                     reductase-like, classical (c) SDRs; cd05362"
                     /db_xref="CDD:187620"
     Site            order(14,17..19,37..40,43,66..68,94..96,117,142..144,157,
                     161,187..190,192..194)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187620"
     Site            order(26,29..30,169,172,212..213,215..218,220..221,
                     224..225,228,232,235..238,240,242..248)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187620"
     Site            order(118,144,157,161)
                     /site_type="active"
                     /db_xref="CDD:187620"
     Site            order(144..145,157,189,194..195,199,202)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187620"
ORIGIN      
        1 mskqltgkva fitgsaknmg kdfaialakq gadlvihyhs ahsklqafet qkevealgvr
       61 ttlvhgdvsn kaqvmnifeh iisefggvdi vinnagtisk kpfveyseed fdrlfginck
      121 gaffvmqeaa khirdngrii nmgtsllaaf tgnyalyags kaplehftra lakeighrgv
      181 tvntiapgpi dtdffrgeen eqtvnylqsa svmnrlgqvd ditpavlyla seqsrwttgq
      241 tlfvnggfvt r
//
LOCUS       WP_010604571             182 aa            linear   BCT 01-JAN-2025
DEFINITION  HPP family protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010604571
VERSION     WP_010604571.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..182
                     /product="HPP family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=19651
     Region          54..178
                     /region_name="HPP"
                     /note="HPP family; pfam04982"
                     /db_xref="CDD:461506"
ORIGIN      
        1 mkvyfkrmas kgvcpprkpl kkilwswvga mvrillitvi snlalpygvg salligsfga
       61 tavllygapm aefsqprnll gghffsallg vsifillgee slfaaplavs lsivvmhftr
      121 tlhppggata liaiiggesv hnlgymyafy pvlmgallml lvalsvnnms rnpkrhypvy
      181 wf
//
LOCUS       WP_010604583             380 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudoalteromonas maricaloris].
ACCESSION   WP_010604583
VERSION     WP_010604583.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12810515
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..380
                     /product="ABC transporter permease"
                     /calculated_mol_wt=42267
     Region          4..321
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          187..380
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mlrlrrlnai vskefmqlar dritfamivm lplaqlllfg yaintdvrhv sagivdfsqt
       61 yqsrqliqta antqvvdfig yydsiaaaeq aitrgkvntv lvipadfvrr qlnrdyqlsg
      121 ykvgnstaqh svaqwlidgs dpllsgavag lsklpisikr lpmpalpdsa falqnyfnpe
      181 krssvniipg liaiiltmtm ilftssalvr ereqgnmefl ittpvrptel mlgkilpyil
      241 vgfiqmaiil flghwlfdvp lnfdmpslli vtllfitasl tlgllistka knqlqamqmt
      301 vfvllpaill sgfmfpfaam praaqylaei lpathyvrsi ravvlrgahf sdlyfdllcl
      361 vafsvigfmi atmrfkkrld
//
LOCUS       WP_010604582             310 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010604582
VERSION     WP_010604582.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..310
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33920
     Region          7..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtkeiviqsk glgkqfndyw avsdldltvk qgeiygflgp ngcgksttir mltglltptt
       61 ghisimgkdv qahgeslrnr lgymtqkfsl yeslsvlenl efvakiygls rndvkrrvae
      121 llqeyqledk ksvqsgalsg gqkqrlalaa avihkpellf ldeptsavdp enrrafweql
      181 fslsaqgtti lvsthymdea erchrlaile qgvkraddsp ialmeqlkvs vcevvgddva
      241 alktrlaslp svisvsqiga rlrvlinkke sqplallrae sgggyevdft ranledvfvt
      301 stgrgyaala
//
LOCUS       WP_010604649             403 aa            linear   BCT 01-JAN-2025
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme
            [Pseudoalteromonas maricaloris].
ACCESSION   WP_010604649
VERSION     WP_010604649.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 403)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..403
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=44192
     Region          3..401
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mtdiqslrnd fpilnkqldg qplcyldsaa taqkpnkvid viktfyqnen snvhrglhml
       61 senatvryes aretianfln vetreivwts gateslnlla hglsarftsd sviaispfeh
      121 hanivpwqea cqrtgatllv lpmldgvlde qgaiamlkqh kpdvlamghv snalgnihpv
      181 eslisvckal gtitvidgaq sllhlrpdlk aldcdfyvfs ahkalgptgv gglygkyqql
      241 nalpvyktgg emikevsfer ssyreapgkf epgtpnisgv igfaaaidyv neidpsalqr
      301 yeqalyhsll aklrqiegit vygdtqnnvg vvsfnykneh hydlatllnt ygvavrsghh
      361 ctqplmkmlk vngtvrasla fynnqddieh finalsatie lld
//
LOCUS       WP_010604608             142 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pseudoalteromonas maricaloris].
ACCESSION   WP_010604608
VERSION     WP_010604608.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..142
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15184
     Region          45..119
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 mtfkieekvp cpeeycdlri aaglsaksle aatrglpnsl ygvairhneq lvamgrvvgd
       61 ggcnfeivdv avnplyqgqg lgrtvmeyid gylasnvlpg syvsmiadep afyeklgyrl
      121 vapasqgmtk kftvgsikss ki
//
LOCUS       WP_010604674             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Pseudoalteromonas].
ACCESSION   WP_010604674
VERSION     WP_010604674.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..264
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29482
     Region          2..255
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mivdshchld rldfeklgls leevlsnarq kqvehflcvs vtldqfpsml ekiahfddvs
       61 ascgvhpldq kdkldverlv qlasndkvva igetgldyyy skdthqvqqe sfaghidvan
      121 qlqkpliiht rdakadtidi mrahnaqncg gvlhcftedw pmakqaldlg fyisisgivt
      181 fknatalqev vkqipmdrll ietdspylap vphrgktnqp ayvqdvayyi adlkgvsyka
      241 laeqttnnfy slfnlvkrqd gstt
//
LOCUS       WP_010604695             402 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudoalteromonas maricaloris].
ACCESSION   WP_010604695
VERSION     WP_010604695.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..402
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44140
     Region          4..>402
                     /region_name="ABC_perm_CPBP"
                     /note="ABC transporter permease subunit/CPBP intramembrane
                     protease; NF041647"
                     /db_xref="CDD:469529"
ORIGIN      
        1 mfevflkeir ellrdrktlf fvialpmlvf pvimalvgfm asqaameakq evhtyyivne
       61 ayaekfseqv fyhksfkkya gelkldsvea lsdavrrgvi dvgvfipsdp venlesgvks
      121 ewkivfndaq sinfiydrls klakkfsdel raakltslgl sqaeqaavlq pisitkvdta
      181 dkrenlgekl gafisymlip lvlmgasypa idlgageker gtletllltp isrtelvlgk
      241 fltvlsssif calitvssma lwigiassfv eldviknafs svalldfvli falllpvavm
      301 lssltlaisi yartfkeaqn ymgplsmgif ipivmslmpn meltaktali pitnvalaik
      361 eiikgtvdyg yvalifgasa vlaagllvcc vkwfnketvl fr
//
LOCUS       WP_010604819             679 aa            linear   BCT 01-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010604819
VERSION     WP_010604819.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..679
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=74025
     Region          15..677
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 memfasladk lpkaneshfa ieiaglsgsl fkvlsfesqn dslcsdyrfd ievlseelie
       61 pdlvigkdvt fsitwamsdr tvsgiiteyv chgrshqgyv ytlsfqsllv llkhqrsnrv
      121 ftdmsadaiv ksvldkagfp sgklqlkass pslamtvqyd esdfdfvtrl mrrygfvygs
      181 testgsqanl svfgsssdfs aemeeitlpy asptgqvrps esvfafskka sllnsgfrly
      241 dedyekccal svnsnnqtev ggfgedsifa enfmtegdgd altkvhqqsi dcqrnlfvid
      301 tdcralrpgv altitdhpny sgrylvvsva hkgcqggsve ygskvkglty knqatiipid
      361 vqfkapvikr kkvfasfnat ieqevdnkgr ykvklpfnqd gegeeskptr lmqhyggpgg
      421 ygmhfplnkg tevmvageng dldrpiilga lfneealspv tfenssenkl vtrasntllm
      481 ddkegeekiq lftksqenil efnategsef ikletkkgyi dikskeamtl qsqanivaqa
      541 dkeisiraed avyiqsiesn ieinakeaiq ltadtdikiq sadsniqfea qqsinleaaq
      601 disyfsvdgn velaaqngnl tinadrnisi vgqgsgsiql sqgggkieid aagnitidan
      661 nlnlsasnis vsgsaishn
//
LOCUS       WP_010604933             379 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010604933
VERSION     WP_010604933.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..379
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41526
     Region          27..365
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 miefelinhe eapvifeqat chngmkiala tlnapkalna lnldmirlla pqldawandp
       61 qiamvmlkga gekafcaggd vvslyremss dtsnalietf fseeyrldyq ihnydkpill
      121 wgngiimggg lgltagashk vmtetsriam peitiglypd vggsyflnkm pkgvglflgl
      181 taaninaada klvgladhfm dseklslllq nlvevnwgkt nvlnhekltq lllsldeash
      241 appkseikpl ikvfealdek dtlseqvefi laldstdnkw lskaqaalkh gsplsaalvk
      301 aqltrsagkt lrdcfkqelg msvtagefge fqegvralli dkdgkpnwrf ksvaevtdda
      361 verffaprwd endhplrdl
//
LOCUS       WP_010604936             496 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [Pseudoalteromonas].
ACCESSION   WP_010604936
VERSION     WP_010604936.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..496
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54389
     Region          4..480
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(61,63,67,70,74,107,110..111,120..127,132,135,138,
                     231,235,238,241,243,416,418..419,421..422,425,428..429,
                     431,433..436,445,449,451,465,472..477,479..480)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(147..150,158,173,176,206,223..226,229,247..249,281,
                     381,383,409)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(150,247,278,281)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mhqvplying efsqsqsdkw ldvvnpanqe vlakvpcatn eevqaaihsa qeafktwrnv
       61 pvterarimm ryaallkehq eeiatiiche lgktfedakg dvwrgievve qacnapsmmm
      121 getvenvarn idtysytqpl gvcagitpfn fpamiplwmf pmaivcgntf vlkpseqdpl
      181 tpmrlvelfe eagapkgvlq vvhgskdqvd qileapeira isfvgscgvg qyiyskgtqn
      241 lkrvqacvga knhmvimpda kkeqvinnlv gssvgaggqr cmgisvavfv gqsqqwveel
      301 kdamakvrpg vwddpeaayg pqttpqakar ilslidsgkq qgatclldgs dftvegyesg
      361 nwvgptlfsn vttemdiyke eifgpvlccv fvdsldeait linnnpygng tslftasgga
      421 arkfqreiev gqvginipip vplpffsftg wknsfygdqh tygkqgvrfy tetktitsrw
      481 fddeavsgpn msinlr
//
LOCUS       WP_010604973             213 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010604973
VERSION     WP_010604973.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..213
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24482
     Region          106..194
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mnasqyrwce lvfvffvlpi vayqfrdhln nwlfpaliil mavcthlllt dphfkrfrlt
       61 glgefssvkk rlfttffaga mfsamlyglv sqgnwfslpl nspsdwllll vaypilsvlp
      121 qelifrsyff hrykrilpnk nnrvllsalv falahciydn wiavalsfvg gllfsytyah
      181 srslavcvle hslwglwmft igigqyldsg vkf
//
LOCUS       WP_010605009             330 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010605009
VERSION     WP_010605009.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..330
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36732
     Region          6..330
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mksytkvaiv lykhmlvtsv tlplemlkag qafakvhlke ayvplevllc ssqgeavnad
       61 nyltleaqsd fsslplydyi ivpsiwrnpr pivrqnqals esladawgag stligvgtgv
      121 cflassglld ghsatthwhf akqfsqlypn velkpdyfit qseriytvas lnaladvivh
      181 iiellygida ahhvqqnfsh eirkpyeeqr ylegavdrha deqiaailfw lknnaaseis
      241 lpavaaqfdl syrtfnrrfk qatgqtavay lqqvriemck ellassnlsi qdialasgfn
      301 sqgqlsrvfr qlmgkspsty raivrkklfs
//
LOCUS       WP_010605014             791 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010605014
VERSION     WP_010605014.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 791)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..791
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86625
     Region          4..88
                     /region_name="ATPase-cat_bd"
                     /note="Putative metal-binding domain of cation transport
                     ATPase; pfam12156"
                     /db_xref="CDD:463475"
     Region          91..790
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 manscfhcle pipkgfvgsv tfegsaqpvc cigcqavaet iisqgmsdyy tyrtesagkv
       61 eelvpeqlkm llsydndeiq edfveisgeh kevllsvegi scaacawlie kqllalggiv
      121 rvdvntsthr amivwqdkhv klsdiikslm eigykaypfq adeeaaqkqa vakayirrlg
      181 vaglmtmqvm mfafamyfgm fsgmeenfeq yfrwislvla spvilysamp fltnavkglk
      241 akqlnmdlpv slaifgayga styatfmevg evyfesicmf tfllllgkyl efrarlkase
      301 ftanlqkllp ltarkvdesn neqhiaakkl klndlilvka getipadglv ikghttvdes
      361 mmtgehlpvk kyqghqvyag tvnhdgiitl einkigqntl lnqiirlqhn altkrpklve
      421 itdkvaqwfv acllvfasit aigwypispd kafwvtisvl vatcpcalsl aiptaltcav
      481 asltkkgili keahvletat kltrvafdkt gtltegrfsi khiellqtdy neqqvldfaa
      541 alerfsehpi arafahitpt enlvqdvevv agsgirghwq gitialgksh wfdnhasfaq
      601 atlfidnnav adfyfndkvk snaetvveql qqagltchml tgdssnagke lsqqlaldsy
      661 qsactpeikq qaveawskqg eivamvgdgi ndspvfnsah lsvamdtgad iskntadvvl
      721 lnsdlnaila lqqvakqtrr ivkqnltisl lyngsilpla alglippwia vigmsassii
      781 vignslrllk l
//
LOCUS       WP_010605111             341 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010605111
VERSION     WP_010605111.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..341
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39146
     Region          150..318
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(201,244)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(206,209..210,214,218,240,242..245)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(236,264)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mqedllnsvi kitktrdvds leyslvstiq efigckevav ykdllvpgei aierslllrk
       61 lsdkefdwee rslvkepdke lisclqsaci itvqakdgte hrwvpislqe kpvgaiavis
      121 tglssadqvl lnafcrifen yltilhener dkltgllnrq tfekrlkqli ekqvikqhkt
      181 vwhgdvrsvh kgatswlaim didhfkkvnd nyghvcgdev llllaqrmrq ffrstdllfr
      241 fggeefvlvf eptdydsika kmdefmelvr nthfpfvkkl tvsvgmsris pydfpitvle
      301 nadkalyyak dngrdmlcfy eallsehkie apeessdidl f
//
LOCUS       WP_010605146             193 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Pseudoalteromonas maricaloris].
ACCESSION   WP_010605146
VERSION     WP_010605146.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Ko,T.P., Lin,J.J., Hu,C.Y., Hsu,Y.H., Wang,A.H. and Liaw,S.H.
  TITLE     Crystal structure of yeast cytosine deaminase. Insights into enzyme
            mechanism and evolution
  JOURNAL   J Biol Chem 278 (21), 19111-19117 (2003)
   PUBMED   12637534
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Carter,C.W. Jr.
  TITLE     The nucleoside deaminases for cytidine and adenosine: structure,
            transition state stabilization, mechanism, and evolution
  JOURNAL   Biochimie 77 (1-2), 92-98 (1995)
   PUBMED   7599282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..193
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0001882 - nucleoside binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21075
     Region          45..136
                     /region_name="nucleoside_deaminase"
                     /note="Nucleoside deaminases include adenosine, guanine
                     and cytosine deaminases. These enzymes are Zn dependent
                     and catalyze the deamination of nucleosides. The zinc ion
                     in the active site plays a central role in the proposed
                     catalytic mechanism, activating a...; cd01285"
                     /db_xref="CDD:238612"
     Site            order(63,81,92..94,118,121)
                     /site_type="active"
                     /note="nucleoside/Zn binding site [active]"
                     /db_xref="CDD:238612"
     Site            order(90,95,99,119..120,123..124,127..128)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238612"
     Site            order(92..94,117..118,121)
                     /site_type="active"
                     /note="catalytic motif [active]"
                     /db_xref="CDD:238612"
ORIGIN      
        1 mtvllnaetq vnsealnaia hmptkslgvl ldsdftrklc dqdfmriavl lakkgyeegg
       61 cpigavivdn etnqivgkgh ntlvqeshpy nhgetsaird agridfsrtt lytslspcdv
      121 catllymrgf qrvvvgditn asgneplles kgvqvdiled eqgialyqqf raekpeqdle
      181 dwqglaavna rhk
//
LOCUS       WP_010605167             195 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010605167
VERSION     WP_010605167.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..195
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21289
     Region          1..63
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 memqinkqli kskrveraws qselaqvsgl slrtiqriek sgtaslesik alaavyevkv
       61 ieiqhqpklk gakltrkaaa ffagsavmaa svftltasak pvmvdlmlts qgqtladvqv
      121 lndegafsei vfsdklkirl tskieqenqv kivteiysls segqvliasp svtvqhqkqa
      181 evhfddyqls lspnl
//
LOCUS       WP_010605194             766 aa            linear   BCT 01-JAN-2025
DEFINITION  CHAT domain-containing protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010605194
VERSION     WP_010605194.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Classification of the caspase-hemoglobinase fold: detection of new
            families and implications for the origin of the eukaryotic separins
  JOURNAL   Proteins 46 (4), 355-367 (2002)
   PUBMED   11835511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10579557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..766
                     /product="CHAT domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=86095
     Region          488..746
                     /region_name="CHAT"
                     /note="CHAT domain; pfam12770"
                     /db_xref="CDD:432771"
ORIGIN      
        1 mkliiyfkvl flsftsisce ldaldyqnsv lttfmlsevs hsglqllkna kndidvsctd
       61 mldtlplalk iveaqvklgv evleaerkli tlkntlfpik kfykneysqv laqmillymn
      121 igrehlalfy snlllqekdi askeirlfah aisnhfsnyv pegdlkklla vkvgffqner
      181 qalylpaerl layvnsrlrs gkmrevvsqf kelsidklid snttyvsnnl leivlgieva
      241 klslfgkkyk fpsglksytg kygtrisien tivinllkaa ntkkkirkhs lekvkknyay
      301 lyniydlgrs vksevyirtl lnslitmysy ditvqssvye lsqyistlnt lvpvsmsssq
      361 ekltykdlvi kqqmlkdild dglapsddli qeilslkell skskkgevqs isvtqnqlld
      421 detllytadl sgktviyklt knsftlkvnr tqdlrtqiee hrhlltsrgd srasgqklrv
      481 tvglkdmykt livassgile tlpfstlynd etdkwliqem niyrlngler lltrrgssnt
      541 aasriaianp tyytppptgv kwqelstsrd tlinlaplke stteakails nlvnqnrlll
      601 tmgnavesnv keklnqrnwg lvsfsthtvf psydtpisyp glalsidyqd landslllad
      661 eiaemnfsds vvllaacnta nasevggsfn slitsfhfag aygvvasqwr vnseetvefm
      721 stfaellnse qfilntaiam tqskladklg tkadsashwg awevyf
//
LOCUS       WP_010605228             287 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HDOD domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010605228
VERSION     WP_010605228.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..287
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=32017
     Region          17..261
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 midlddkvla dvkhgfnlpp kpaliselqa alatadpdln diasiiahdv stsaavlkii
       61 nsplyglart vtdvkqavvf lgldsisklv tgfllkqtfd qrkccisler fwdnasdiad
      121 simvignklk srvpienlhl lglfhdagia amavnypdym etliaankdy dkllveheee
      181 kyetnhaiig yflaaswnlp qsicqmilch hdpeflgnck deeqklafsa lkmaenfvhi
      241 nkrfvaapdw hlmkadvlkv lnldeddyqd ikedldeyfl eqdgvsn
//
LOCUS       WP_010605234             309 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010605234
VERSION     WP_010605234.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34085
     Region          10..69
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..301
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(108,112,151,165,167,233,250,280)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(109..110,114..115,117..118,121,125,127..133,194,
                     227..231,238..239,242)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 matskhiell qemsifvsvv ntgsfsesar qlgvspssvs raikqleqql gvcllqrttr
       61 slrlsetgra vyerctqleq aakdvislce shhqtaqgtv kiaapkavah tlihpsvmaf
      121 lgefpnidvh lvlddnaldl irdeidilfk itneppqgli grsvmtiehi vaaspkylat
      181 hsipthpkel iqhscialge tdadakwrfr kgtqkhtqkh ttpvngryka nhtrvrldaa
      241 lqglgitslp mfvakdalas geliqvlpew qfetnysgel wmlypatrhi pakvsvfadf
      301 ivqrltkgc
//
LOCUS       WP_010605332             370 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: arginase family protein [Pseudoalteromonas].
ACCESSION   WP_010605332
VERSION     WP_010605332.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..370
                     /product="arginase family protein"
                     /calculated_mol_wt=40631
     Region          55..367
                     /region_name="SpeB"
                     /note="Arginase/agmatinase family enzyme [Amino acid
                     transport and metabolism]; COG0010"
                     /db_xref="CDD:439781"
ORIGIN      
        1 mseskkqfhk klehclcppg dgvftvntak erkdalrqkl ygqtegvdtl wkasleklge
       61 sehkaailgi ssdcgggilr ganwgplflr stlieqqpqt safdlgdvrv iphllhdkyl
      121 nestisncqk alyadpesey yvsplsited vcdgfyenyp nkgvfgiggd hsisypltka
      181 ylkakrargv ktaiihfdah tdllverlgi dlcfgswcth ileflpaphh lvqfgirssg
      241 kpkshwestf gvkqhwahei rergaqvivd eviaqlkadd veelyvsfdi daldeefasa
      301 tgtpeaggmt pdeamlilqa lrgefkitga dmmeiapftd sslvgqtsse ttlkegakls
      361 aflidainns
//
LOCUS       WP_010605244             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phytanoyl-CoA dioxygenase family protein
            [Pseudoalteromonas].
ACCESSION   WP_010605244
VERSION     WP_010605244.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..300
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33931
     Region          9..217
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mtivskskld fyknngfvlf eqtlpdklle klkrlsnale skakqaqqdg kiatqyhlsn
       61 esgepklfry ndllfeapel iiellatpam laisehlcgv gsvplqcdlv ckyphphphi
      121 awhqdaphsr hfaylnvgiy lddaniddgc lrylpnsqhq ildiyslsse ygwnipgvvq
      181 qpakagdilv qdmmvlhgse pkrtegprrt iyvelrplag vnenqssewa elrkqwmahv
      241 iqaadpedvp enwlavygep nydlntlver ikqkreavip avwapkiveh pdyptpadlr
//
LOCUS       WP_010605501             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Pseudoalteromonas].
ACCESSION   WP_010605501
VERSION     WP_010605501.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..201
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21696
     Region          120..197
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mrylialvia givtfflflg mqaliqggeg amtdpvkgqv ldfvrlkkee tvekkerkpq
       61 kpptpkeppp pmdapqtqnn nldatggnfd fsanvdadvd lasglaless dgeylpivkv
      121 apvyprrals rgiegyvive fivtkqgtvr npvvvsaepe sifdqaalda alkfkykprv
      181 vngepvevag vqnkisfqin g
//
LOCUS       WP_010605502             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Pseudoalteromonas].
ACCESSION   WP_010605502
VERSION     WP_010605502.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..455
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49498
     Region          271..448
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mkfvqkftkh aifattlalt asahaeqald ldsllktleq gqtaqtaqnk qreaefkaqq
       61 nnqiqmlnal tgernqalak serletnfee neiklanlsd tlskrmgtlk elfgvlqqva
      121 gdssnkfats vvsaeikgrd dymtelakkm gstsrlasie diekvwfemq remteqgkvs
      181 rfntevivag gakqnkevlr vgafnliadg kyltynndtq tlseltrqpa srftstagel
      241 qnaktgsvdf aldptggsil gllvqapnte eqvhqggavg yvilgvglla lliaierfvs
      301 lmlmgskinr qlkdsvardd nplgrvmkvk eqypdvaydt lelklseail rempkitrnl
      361 tlikiisvva pllgllgtvt gmintfqait lfgtgdpklm aggisqalvt tvlglvvaip
      421 tvflytllnt rsrnlllilq eqsagiiaer sekga
//
LOCUS       WP_010605545              70 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010605545
VERSION     WP_010605545.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..70
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7912
     Region          6..70
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 madlpiknki rmlrfmsgem tqkelaervg vtrqtimaie aakyspslev afkiahvfnv
       61 pieevfeyqp
//
LOCUS       WP_010605574             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Pseudoalteromonas].
ACCESSION   WP_010605574
VERSION     WP_010605574.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27892
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mllaerhqfi ldqlnlqgri tsvslaqtld vsedtirrdl nklaelkllr rvhggalalq
       61 dntpdyierl dkpdtskiry iepalamlvp gqtividsge tcrylaqhlp knmpltvvtg
      121 cpliakelay hslvdvivlg gpmfkpamrv vgmtaiemvk rirfdivfmg icsfhihhgf
      181 sasyieeaei lsatirqsdh tvimgpshkl dkvatyqivt aneidtiitd eeinpslkkq
      241 iesleialtl v
//
LOCUS       WP_010605586             833 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pseudoalteromonas maricaloris].
ACCESSION   WP_010605586
VERSION     WP_010605586.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 833)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 833)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 833)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 833)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..833
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91889
     Region          1..832
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mwfklaltlf srefrrgelt iilaaialav ltvfslssit erirlnleqk sadfiaadrr
       61 lssnhdfddr vlatarefgl ntakqvyfds mlfandelil galkavtdty plrgkltlrd
      121 slngenyqvq aapkkgnvwl seglfyslgl kigdvveiga gqftvskvli sepdapffsl
      181 agnkrvlinh ddiavtkaiq pgsrvfyrll fsgseqqlge yytwlkpqlk snqswqgikd
      241 rqsplgenla rsesflllag lfgimlaava mavsakryce rqydpvammk tlggsrktir
      301 riyllhlslv tffsvvvgla igyglqsvga aylinfmdta lpeagfrpwl lsiavgvvca
      361 mmfslkplld lfdipplrvl rrnlgdtiai srihmalsvl tifglmwlfs rdikitailf
      421 gatlllmavl yvisrllfsa grklglspgs swslaiatlq krananavql isfalaiklm
      481 lflvvlkndm isdwqmqvpe dapnaffini meqeiqpmqs kldesgikhe hfypvflgrv
      541 nalngeefar rvslqegeek dedardgvgr elnltwldel pagnevvdge wfddsdalqv
      601 svaqglaerv gikvgdtlsf linsqtieak vtslrsvnwg slkpnfvmif ndkiagqfpv
      661 tyftaaklei adtkvisqfl kayptismid iqsqlkqaqs misqvslais fvlsivlisg
      721 slvlisqvqa slaermqeiv ilrtlgakgr liklatlyef lllgglaglv aavvsdiall
      781 viqvqtfdvd grlhpyiwll gpatgatfva vigyfmvant mkqntqgllr kla
//
LOCUS       WP_010605623             177 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DinB family protein [Pseudoalteromonas].
ACCESSION   WP_010605623
VERSION     WP_010605623.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..177
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19934
     Region          8..162
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 mkanfelmad yncwmnerly eavsglsate lhqdrgaffg simgslnhil vadiiwlkry
       61 tehshhaeal navatmplpt kldamlyedf aalrqaraem dkviiefane vteealaadl
      121 hykntqgktf srkfgflvhh lfnhqthhrg qittllsqig idmgetdlla riptsfg
//
LOCUS       WP_010605630             165 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RDD family protein [Pseudoalteromonas].
ACCESSION   WP_010605630
VERSION     WP_010605630.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..165
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18220
     Region          3..150
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mshfapanfs rrlasliyds lvvvafamlt tvlflltina lisfnvltlg nhedvsaliq
       61 adpilytlra tllvlvsvlf fayfwtksgq tigmrawrlk vqtpdgallt wpkaiarslc
      121 allglgnliv lldfkkkrsl qdmlcgtevv vlskeenkkv ynsld
//
LOCUS       WP_010605676             386 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Pseudoalteromonas maricaloris].
ACCESSION   WP_010605676
VERSION     WP_010605676.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..386
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42002
     Region          148..343
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mkrhylsacl iallshqata agqhdsvaip eftaehisal pissvmavnp elflfsnalq
       61 qvdwqqvlds taphlsdkle vllhyagyas inpklllalm elesgvisnp dkqslsapfg
      121 klsheqgfda qvkdvalnls aryyafqklr degkakklpa vneatvalad lthtsankll
      181 dtyqtlfnge slalkadssi afserastqa vsaasfsmsf pwpsgyawys ggahsntgsg
      241 ypyssldfnn gsggwgsntp wvqaahggtv trysacnirv thssgystqy yhmeslqynt
      301 gdvisagawl gryaddkata lcqggqstgp hvhfsllyng ghislhnwyi sgyridvgns
      361 nyddncnrff fekngyrtca wralyk
//
LOCUS       WP_010605783             396 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [Pseudoalteromonas].
ACCESSION   WP_010605783
VERSION     WP_010605783.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..396
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=43339
     Region          3..394
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 msksfkykvv nesgmveqge vhatslasaq akleedfklv lsvkenstlf ernrvslkel
       61 eeatsqlatl lhnglridka iavlaqasss saiggvwrqv lsdlkhggsl sdsladkpnv
      121 fpklfvemtk igestgtlpl vferlsqnlr fqyelkskvm qaatypifil ivcilaiwgi
      181 ftfvvpsmsa mfegvdqvpe ytqlllnmss wviqyqgvif valigipigv alalqkhqlr
      241 tkllnflsgf piakslitfs drirfstalq ltlesgvsls sslelasetv inpqlsdklk
      301 ktkvevssge sisgavaklk lfdeislsli tvgeesgnle msfseisrrs rqsfeqwlmk
      361 ftalleplli limggivgsv vivmllsivs mndvsf
//
LOCUS       WP_010605850             275 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Pseudoalteromonas maricaloris].
ACCESSION   WP_010605850
VERSION     WP_010605850.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..275
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30020
     Region          10..273
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mkhvvdrewl fanlgkvkvl dagivkpgqs gpynapaiiq galrfdisga lanphatspn
       61 mccspaqfqa emrqlginqh dvlvayddkg mfsaarawym lkmmghkqvy vldgglpawc
      121 ekqyplsqay aqvqqagnfv aaydetafvd kaavlsnida elsylfdarg akrftgeeqe
      181 pradmrsghv pksknlpyms llnadgcfkp ltelevlysd lskdktkpli fscgsgvtac
      241 ilalvadelg yehltvydgs wsewgadpdv pvetn
//
LOCUS       WP_010605982             170 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Pseudoalteromonas].
ACCESSION   WP_010605982
VERSION     WP_010605982.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 170)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..170
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19097
     Region          22..118
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cd02883"
                     /db_xref="CDD:467528"
ORIGIN      
        1 mqslnntpvi plqgscftre ttraivlrgn dilmlytkry ddytlpgggv negesleaal
       61 erelkeetga vsitgltpfg ryeeyrpwyk pdhdnvhiis ycyvceicgk fdlptmenye
      121 langmkplwi ninqaiahne akladannkg msilreltll khisaqlite
//
LOCUS       WP_010605991             797 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas maricaloris].
ACCESSION   WP_010605991
VERSION     WP_010605991.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12149321
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..797
                     /product="TonB-dependent receptor"
                     /calculated_mol_wt=87143
     Region          23..94
                     /region_name="CarboxypepD_reg"
                     /note="Carboxypeptidase regulatory-like domain; pfam13620"
                     /db_xref="CDD:433354"
     Region          103..777
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msklstisll vaallppslv aksiegtvvn kagkgianas ievegtdirv ltdnnghfqi
       61 sgvglgnkqi hvrapgfahl hkaltldqgg vknamlmlnr spievidiva tpvhmsames
      121 avpvsvlage tlrrqqtatl gdsleklpgv ntnfhakvas tpiirglsgp rvlvtqngld
      181 vsdvsrvgpd hsvaseasta qqievlrgpa tlfygsgaig gvvnvvdtrv ptdnatrgew
      241 nlesnsvddq ntasfnatsg igsvalyvda fwresndyei pvpaeihehs ernnsgehhy
      301 kvansaeesd gftvgssylf dqgyvgvave kfnrkygipg hthgdeeahh eaeeqvfadl
      361 aqtkvqllse ykfnkgwldk vnvragftey ehaevehgmv gttfkndtne lkvdllhqpl
      421 sawtggvslh ykhsdveaqg seaftppsdt qtlaigvmee rrfgdflvql ggrieqveit
      481 asnvplpsid ahshdtemyd highdseatk vyavehqftp vslssglvwd faqnynlgls
      541 vshserapss selfsfgphi gtgtyevgal fkmdehghfe ldeqgialek shniditlrk
      601 tqgdigfifn afynqvdnyh yqietglyae sgdshdhnhe hehdhaselp iylfktddvv
      661 lhgfeaqvaw qltdelkvdv fsdfvrarle eggdlprtpp lrfgsqlsyq tdnlsahihi
      721 tryqeqdria peetatdgyt lvdasisydl svlnqdlsiy lrgsnltdte arvhssflkd
      781 igprpgrsfa lgirgyf
//
LOCUS       WP_010605993             323 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010605993
VERSION     WP_010605993.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..323
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35504
     Region          10..298
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 maahkhgfna drpsdipalg wwdvskrlyh slsqdnlslv aagvafyall aifpalaavv
       61 siyayfsspa emvdqllpli ellppssqei mlqqlkaltq ksqaslslga iftlfltiws
      121 sskgcqalit acnityhehn krqflqalvv rflfsvgaif vaivalsiig ilpivlnlvg
      181 fttaldsiiq litwsilaal fhfslafvyr yaphrraakw rwitlgsfta tglwilaslg
      241 fsyyvaqfas ynetygslgg vvimmmwlyl sayiiifgaa lnastelqtl kdstvgpakt
      301 rgqrgafvad nlttrqrkek eph
//
LOCUS       WP_010606022             767 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas maricaloris].
ACCESSION   WP_010606022
VERSION     WP_010606022.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..767
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84599
     Region          40..749
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkamkrstla tlinatlfsa vagtsfsala eeeqakknql eviqitarkr venaqevpvs
       61 vsalqgdnln ayssagmdir fmnakipsls vessfgrtfp rfyvrglgnt dfdlnasqpv
      121 slvvdevvqe npilkgfpvf diarievlrg pqgtlfgrnt paglvkfdtv rpsqefdgya
      181 avsygsrgav dfegavggsv tdristrisa lwqeqedyid vkapgfeked slggyseqav
      241 rvqflyegdd fngllnyhyr dldgrpiafr anlieagtnn inplydndvv yhdaasrstq
      301 qvetqglslk lewdlpehtv tsitawesae iysradvdgg ygpnnagvsg pgliiftset
      361 advipehnqy tqelrlssnf sgdynyqvgl flfeedlmie sysfdtngyd aayaqygvqn
      421 gyayqdqdts awavfgsfdy tvsddlkvta glrysddeke fyakrtknpt pwngspdvld
      481 gtanpsdshv swdlsatykl tddvnlfgrl angfrapsvq grilfgdevt vaksettnsi
      541 eagiksdvld gqgrvnatvf yyqmddqqlt avgggsnfnr lvnadkttgy gfeldtewvl
      601 tdelnatfnl synkteledk nlavavcaqc tvtdptymve gangpearai ldgnslphap
      661 ewianatlry tkeleggeff vygdmsyrse vdfflyksve fegealfetg lragymwseg
      721 dneyevsafv rnlfdeqvvi ggvdfnnntg mlnearfiga efkvkff
//
LOCUS       WP_010606070             221 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA-uridine aminocarboxypropyltransferase [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010606070
VERSION     WP_010606070.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Funk,H.M., Zhao,R., Thomas,M., Spigelmyer,S.M., Sebree,N.J.,
            Bales,R.O., Burchett,J.B., Mamaril,J.B., Limbach,P.A. and Guy,M.P.
  TITLE     Identification of the enzymes responsible for m2,2G and acp3U
            formation on cytosolic tRNA from insects and plants
  JOURNAL   PLoS One 15 (11), e0242737 (2020)
   PUBMED   33253256
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Meyer,B., Immer,C., Kaiser,S., Sharma,S., Yang,J., Watzinger,P.,
            Weiss,L., Kotter,A., Helm,M., Seitz,H.M., Kotter,P., Kellner,S.,
            Entian,K.D. and Wohnert,J.
  TITLE     Identification of the 3-amino-3-carboxypropyl (acp) transferase
            enzyme responsible for acp3U formation at position 47 in
            Escherichia coli tRNAs
  JOURNAL   Nucleic Acids Res 48 (3), 1435-1450 (2020)
   PUBMED   31863583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..221
                     /product="tRNA-uridine aminocarboxypropyltransferase"
                     /EC_number="2.5.1.25"
                     /GO_function="GO:0016432 - tRNA-uridine
                     aminocarboxypropyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=24788
     Region          22..220
                     /region_name="TapT"
                     /note="tRNA U47 aminocarboxypropyltransferaseTapT/TuaA/
                     YfiP, DTW domain [Translation, ribosomal structure and
                     biogenesis]; COG3148"
                     /db_xref="CDD:442382"
ORIGIN      
        1 mnnsvlalrq rqiaaaqrey kargsklarc eccllattlc icdkvemaka dcavcllmyh
       61 nesfkpsntg rliadvipdn hafrwdrtep daallallsd eqyapivvfp eqgvepervi
      121 tkvtrteskt plfifldgtw reakkmfrks pyldnlpvls iapeklsdyk lrvaphehql
      181 gtaevacvlf aecgeqdaad kltahfinfr daylkgkrsk l
//
LOCUS       WP_010606103             265 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010606103
VERSION     WP_010606103.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..265
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28592
     Region          7..248
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mavtpqfqvd klsvqlggka ilkalsfain sgefigllgp ngagkstllr tlyqytapss
       61 gsllfngkpl asygrkayar hvavvlqeip aeftlplfdm vlmgltpnks llatttaaek
      121 qailhaikqv glshkleqcf sslsggekqr amiaramvqa pqvlimdept shldikyqiq
      181 imelakqlgv tiiasfhdln lasalcdrll vlnngelvtd gsplevinet llsqvfgvca
      241 evstvrhppn nseiphirfh ygyql
//
LOCUS       WP_010606124             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HDOD domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010606124
VERSION     WP_010606124.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..279
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=31139
     Region          13..230
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mstenallti ltdrinndtl vlptlpeiav rvrqaaddpe inlmqmadvi shdpalaarm
       61 ikvansafmg rsvkvntlnq avtriglrqi kniatamame qlfvsnnkli ktymdkawqk
      121 tlkvacqait tmdfylrvnk htslnkdtit laslvfnigv lpilteaerh pevfanpsfl
      181 ahaiqklggk iggaimrewe ftdefvevae swanpnyrpe hvcyvdfirv gaivegilqv
      241 sdksaalkqy eekgvirevn mfaddtylhv ledvktmfa
//
LOCUS       WP_010606197             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010606197
VERSION     WP_010606197.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..282
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30592
     Region          1..281
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mstfvkikal rpslsnseak ladftlnsgd kiralssvel areagvsqss vvkfaqklgy
       61 kgfpafklav vdalneqtdt saaideliss ndsieliadk lqlkqqnvis etrklnsakq
      121 fenaiqlvkn arkvivcalg stftmaqdlt wklqklgipa iaqvdeisas sfiatmgkdd
      181 lfivisntgt skslltltnq aldngckcla isrygshsla emadailyci negeplkhsg
      241 mlsrtsqayl idvlftalaq snlhwqkrvd kanenmqvlr se
//
LOCUS       WP_010606207             208 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GTP cyclohydrolase II [Pseudoalteromonas].
ACCESSION   WP_010606207
VERSION     WP_010606207.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Ren,J., Kotaka,M., Lockyer,M., Lamb,H.K., Hawkins,A.R. and
            Stammers,D.K.
  TITLE     GTP cyclohydrolase II structure and mechanism
  JOURNAL   J Biol Chem 280 (44), 36912-36919 (2005)
   PUBMED   16115872
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Ritz,H., Schramek,N., Bracher,A., Herz,S., Eisenreich,W.,
            Richter,G. and Bacher,A.
  TITLE     Biosynthesis of riboflavin: studies on the mechanism of GTP
            cyclohydrolase II
  JOURNAL   J Biol Chem 276 (25), 22273-22277 (2001)
   PUBMED   11301327
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..208
                     /product="GTP cyclohydrolase II"
                     /EC_number="3.5.4.25"
                     /GO_function="GO:0003935 - GTP cyclohydrolase II activity
                     [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009231 - riboflavin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22791
     Region          10..202
                     /region_name="ribA"
                     /note="GTP cyclohydrolase II RibA; PRK00393"
                     /db_xref="CDD:234745"
     Site            order(22,24..26,33,35,37,56,58..59,61..65,67,74..75,78,90,
                     92,100..101,104..105,107..108,111)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238348"
     Site            order(52..57,59,68,70,73,93..96,103,107,110,116,128,130,
                     151..153,156)
                     /site_type="active"
                     /db_xref="CDD:238348"
ORIGIN      
        1 maevrarvgl nvgqhsnipa eivsfsglkd gqehvalvfn sadsqqqipl irmhsecltg
       61 dvfhssrcdc geqlneciea mhkqggilly lrqegrgigl ynkidayvlq sqgmntyean
      121 nhlgfeddlr dfsdavlmlq alglnhvklm tnnprklkal rnagitvdev vgtqahvkag
      181 vsgneqylkt kiqhgahmld ikkiskad
//
LOCUS       WP_010606240             815 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas maricaloris].
ACCESSION   WP_010606240
VERSION     WP_010606240.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 815)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..815
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..815
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89933
     Region          35..769
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msklhpslva lavsssffvv tqsqaeeska qeksieriqv tatrragtvq eaplnitavd
       61 sdvmsdqnig dfedvarwvp gltiteqggr egspiivrgl ntnsserasd sgtvatylge
      121 ipinvdlrlt diervevlig pqgtlygagt lggairtmlk apvldviegk lsgdlfsind
      181 sdshghevga vfnmpvvmde lavrasinry hnpgfmdyry vvkqagvsnp dpdwsnaedv
      241 kaninavada ndetitttrv slrwlvseni dttlnyfhqk qengansisq yqslaaqhpl
      301 adtikpyesa yrvlepneqe ddllsleina dlefadlvsa sgwsskeqqg qrdqtdllyd
      361 iwpgyadfps ftaltkdttd qdtftqeirl vskgddalnw iagvyyskqe issddreytp
      421 gltefwgdei dnieqdleyi altnatskes alfgeigyaf sddfnitvga rfyrydvkte
      481 saaetplysg glpsleqisf eqvsakdngs lfkfnanytw qdglltyftv segfrldggn
      541 glescpetlp eqqiicalph elsykpdttt nyelglkstw lnnklhfnaa lfsvdwedaq
      601 issvtvngqe iitsnagsan ssgielstra mlndqwtvya tysyakaqlt ddapalfavf
      661 kegdysaeei alyqpyydgt dgdrlpgape qqfsfglsye qevfddkmln vnygvtaqsd
      721 vytkvglkad gevlpgfals nlsaklsseq wavtfyvdnl fdkfaftsvr rdkswageak
      781 faalnkalpe qqrvyghyvt tprtvgvkln yqfel
//
LOCUS       WP_010606323             353 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010606323
VERSION     WP_010606323.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..353
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39500
     Region          5..>224
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mqtssakikl gfigagfigq vahienyaql tdcelhgiad lrpellaqva skfgfnhtya
       61 dhhalleddd idavvvvtar ahtfevvkdc llagkhvfse kpmagnskna celvelakar
      121 glvycvgymk rfdagvikak avfsqlidtk elgellqvna hcymgdsyck aggyihsqqa
      181 rplmpdeanf apdwltnehr plfaryvnvh shllnllryf ldcdldveyf nfvsakahvc
      241 vmrtdhqlvt lhtgevdqkd wqeqctfvfe hgqlqltlpp allrnvparv elerngeise
      301 ktqyqvpwsw afkeqaqafl dalqqqnlss piaasealsd iqlaeaiwqk inn
//
LOCUS       WP_010606336             306 aa            linear   BCT 01-JAN-2025
DEFINITION  transketolase family protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010606336
VERSION     WP_010606336.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..306
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33668
     Region          1..275
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mrnafarvlt elakndesll lfyadignrl fnplkefaed rainagiaea nmasmaagsa
       61 mmghkpfiyt itpfttsrnf eqikidiayq nqpviivgtg sglsyanlgp thhsfedial
      121 mralpnmhvi cpadayeleq lmpqlielna pcyfrigkkn epavhegspa ltfgkvhvmr
      181 pgeriavlst gtimplaqel vseltkrgls pelvsfhtvk pldeaylnda itrfdhvitl
      241 eehnvsggfg savleyfseq tnwprvhrfg ipdrfidqvh stsdaranag livpdimstl
      301 sergvv
//
LOCUS       WP_010606346             502 aa            linear   BCT 01-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010606346
VERSION     WP_010606346.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..502
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54397
     Region          5..500
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtksiyelfe envkqtpkka avvyldqqvs yeelnrqvlk lsahfvrsgl apgqrvgvfa
       61 pngiefvvtl laiaklgiaa vplpislkgn alitalkktp vamvvawpti skilldanli
      121 epsnlvtlgk avseelswea vqsceklddl qhgvdldapf iltmtsgstg qpkpivlsqa
      181 ckinramdat iqyygltkqd vilvatpmyh slaqrgvlmp lmlgattvvm pkfnlsqwls
      241 aieqykvsfl favaaqlesl iakgtsgadl sslkcivsss avlegttkkr llgmlscrfh
      301 ecygasevgv vtdfavsenp eqsgsvgkal pfvslkitdd qgcevaagqv geiccntsti
      361 fggylkmpeq traafyvggf fktgdlgyvd eqgylyyvgr kkevissggi nvfpqdietv
      421 vksiegvedc vafgikdaql geivkvvieq sqdtdlipvi rkaclqeltd yqqprfierv
      481 ealprnqmgk vlrndvktqf sq
//
LOCUS       WP_010606347             377 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010606347
VERSION     WP_010606347.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..377
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42068
     Region          3..272
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnnrplqlaf igggnnsavg yvhfsaahld nkfqvvagaf srdakvnqht aeqwnister
       61 tyncwkqlil aeqnavdafv vltptphhte vltallekdl aviseksltc glaeakeiea
      121 cydpkkhfla vtfnysgyam vrelkhiisn galgeiqkih lempqegfkr ppdiagkpsq
      181 pqswrlkdyd vpticldlgv hlhhlssyll evepeatcaq fanhsefkgl vddvnmllky
      241 pngivgsmwm sktaighrng lsvrvygtkg sarwfqlnpd elelnyndgr revldragqc
      301 qyanqfrynr mkpghptgfv eafanlysdi agalqlhlsk qpsrseyvfg feqakqglal
      361 feaakrsaes gtwqqvk
//
LOCUS       WP_010606419             191 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010606419
VERSION     WP_010606419.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..191
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=20491
     Region          19..191
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mskralvfpp nfklvlyama vmclvqllgg ifglpvyrfg ivphnvhhls gvltapfvhg
       61 swghllsnll glsisgylaa rlprfkratl fivvatgllv wlfaghanhi gasgivmgyf
      121 glllgaalfn rdvlgivsfi allvltyyan isflatltdf saqtsssshi fgflsglgga
      181 yltkqkriar r
//
LOCUS       WP_010606373             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Pseudoalteromonas].
ACCESSION   WP_010606373
VERSION     WP_010606373.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..256
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28320
     Region          1..255
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkiwtvanqk ggvgkttttv slggilaeqg hrvllidtdp hasltyyfgi dseelevsvy
       61 difargssmt seeilqslcp stienldilp atmaiatldr smgnktgmgl ilkkslekia
      121 dqydyaildc ppvlgvlmvn alaaserilv pvqteflalk gldrmmrtme lmqssqqkqy
      181 qytiiptmyd krtkasleay ktlletykda vwpgvvpvdt kfrdaslaqq vpvqfcpksr
      241 gvfayralld ylkqls
//
LOCUS       WP_010606484             544 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010606484
VERSION     WP_010606484.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..544
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60017
     Region          27..544
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkqlnkllgl mkvpnklrls lllsvviial vqlssalvlr dsltqerrin aknlmettva
       61 qlnmvateas ltpqqrqeki kklidaaryg dagyfflfdl dgnmvthpik pllngtsmth
      121 hherfireaf sqfvvianqn qqgfaqyqwp kpgtkelegk lsyianlghy nwaigtgiyl
      181 qdveeqfydr lmlmtaetlg yailliflss lisknitkpl dkltrtmgli saqkdltial
      241 kshgkdelaq maiafnkmns hfrdvlhdin enthslasqa eelsciteqi qagigqqnse
      301 teslqnrmqs lnqvaqavnn eskraldkvt etttlttqgl thvdenvavi ahasrsvdsa
      361 qqavlelqrs steigavldv ikkvadqtnl lalnaaieaa rageqgrgfa vvadevrtla
      421 qrtqqstddi qaiidklhng vattveemes craaseqslk vsqeckhale qinlsiatvh
      481 dinvniatws ekqsedlndm tdnisgiatv anqtalgaeh tkassqqlse msqrlsqmvn
      541 efkv
//
LOCUS       WP_010606493             176 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010606493
VERSION     WP_010606493.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..176
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19803
     Region          4..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstkrqqlid camdlfyqhg ihaiginevl kssgiakktl ynhfeskeal vlatleqrhh
       61 lfiswlsrcl enartneqlt eqlfsaldqw innkvavlgd frgcyfinta aefgeltnpi
      121 nqlcrrhkla vkallkqaln naddaaverl fllsegiist aytchdtdva kralkn
//
LOCUS       WP_010606501             444 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010606501
VERSION     WP_010606501.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..444
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49762
     Region          <235..338
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          248..278
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          280..311
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 meqvliwpaq ypmllkglie qngayildai eawpncqqmk deqgvtttvl pplfylawlr
       61 plepfeacyf qhiddyddkq rqyvnsviqh ieendtdqde liktliqrlg qysniqaqvq
      121 eqslsfvell cdkhyektli wlmekglkfs akeivslwcn sseathaall thidtclldr
      181 aataklatds lldgqqtfel lctmcdkdev tglleqallf qltqqqvkqs aiitlvtqga
      241 tgtardssgr laimlaveng fvsavetmlp hhkvneldes grnlmhyaaa snsaamiemi
      301 fehgddptla dihgdtpyrv amknqaltsk qtfeqhgiie lsneakyqki ktvhilyafa
      361 aillplqlfl fftdevdekt iatlfttaas iaifvfarrk rsnplypnss tpwsligvna
      421 lawlsigvqv lfsvlvliav lslq
//
LOCUS       WP_010606507             355 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Pseudoalteromonas].
ACCESSION   WP_010606507
VERSION     WP_010606507.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..355
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39047
     Region          17..348
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mfelvkawyi kkfsdphsvt lllmlvatva llyffgsyvm pvlvaiviay llewpvnklt
       61 rvtgsrmlsa vvvmavfvgv alglvfgivp vlwqqlsnll qesptmveeg kdfllhlpey
      121 yptlisttqv qaivssvesk llelgevivs asltslkdvv awmiylvlvp llaffmlkdk
      181 seltsgvski ipkdrklisq vwhemdqqim nyirgkvfei vivgvvsfvt fsildlryaa
      241 llgtlvglsv lipfigaalv tlpvaavalf qfglapefwt iliaygiiqa ldgnvlvpll
      301 fseavdlnpv yiivavlffg glwgfwgvff aiplaslvka linawsskse ellvk
//
LOCUS       WP_010606519              96 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010606519
VERSION     WP_010606519.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..96
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10462
     Region          5..93
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 minedkrrfm rmsvdavakl telesgkvhq gvchdlsatg lsvtvsepie anstvdifid
       61 ssgdmiqpls ahatvircsq eqdeqwvvgl eitkfn
//
LOCUS       WP_010606529             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Pseudoalteromonas].
ACCESSION   WP_010606529
VERSION     WP_010606529.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..429
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45308
     Region          1..429
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mlerlfslqa mhtnvrtevi aglttfvtmv yivfvnpaml aeagmdhgaa fvatciaaai
       61 gcfimglwan yplalapgmg lnafftygvv lgmgytwqsa lgavfmsgcl flflsvfkvr
      121 ewviqaipiv lkraiaagig aflalialkn akiviasdat lvqlgditsp gpllaiasff
      181 viaalmyrev ksgvlisilm vtgiawglgl vdyhgvvdip psiaptymql dlsgifelsm
      241 lsvvfaflfv dlfdtsgtlv avtqkaglsd ehgrmprlgr alsadstati agsvlgtstt
      301 tsyiesvsgv svggrtglta vvvgicfllm mffaplaqmv payatagail yvsvlmlqnl
      361 klinwdemsd aipvsvvllm tpltfsiahg ialgfisyta vklacnkane isisvwvltl
      421 lfilkfafg
//
LOCUS       WP_010606559             542 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein
            [Pseudoalteromonas].
ACCESSION   WP_010606559
VERSION     WP_010606559.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..542
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58701
     Region          10..542
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mqlkklsisn qitlsftllf vifisvglms yqgmkevnan lnyivrtsip smetikdiki
       61 dlatirkdef stalnpedpe vhnwlailrd lkkslndkia fyqslpvske ekalfnafit
      121 awqryvnaty hyeslilsgn akeanriild sypvfanams elseletlnd ssvensersa
      181 isavnstlft laisgllvav tiviicills kaiktplals vdlaskiarg elnhaialed
      241 tgknelgllt qslekmrsql halitminds aiqltaavee vnaisyqnaq gmnvqqnelq
      301 svasamtqmq aaisevakst emgaesanqa sekaregsda lksninhisd vaqtvtsage
      361 lannleknsh ninvvvdvir eiaeqtnlla lnaaieaara gaqgrgfavv adevrslaqr
      421 tqdsttqive ivndlqtksk etgvatksce qgialcveqs evagnmihqi esqidsiaam
      481 stqiasachq qsvvseelnk nietinysav emteganqta tacnemskla hdlksqvdkf
      541 tl
//
LOCUS       WP_010606562             124 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010606562
VERSION     WP_010606562.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..124
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=13918
     Region          18..124
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mrkliisfmw fvssicyaqs etitqqalmv nqmsadayti vdvrspeefa aghikgaini
       61 pfneiethqe eltkltdtpl vvycrsgrra gifiealapk gytlkhlegd mnkwlekslp
      121 vvkk
//
LOCUS       WP_010606608             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YdcF family protein [Pseudoalteromonas].
ACCESSION   WP_010606608
VERSION     WP_010606608.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..254
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28021
     Region          25..249
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mfevkkvigq llmplplslv almglmffia ktrkgpyiav wlvllttwsi stpyvaqhii
       61 ewdkgtltaf npsrhknidr ivvlgcnlyp ddslpsnaql gscglarlve girlaniypk
      121 aqlyvsgygy gnatsaglma ktaqslgisa trikqnhnak dtadeakmla pvlvdydval
      181 vtsashmkra knlfeaqgve vfpaptefyn fkslplsrqf iandkaldiv triwheqvgs
      241 mwitirriid peal
//
LOCUS       WP_010606647             288 aa            linear   BCT 01-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010606647
VERSION     WP_010606647.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..288
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32664
     Region          10..235
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mfdkyydmsa hqkqlndtgl vkfegllneq mldkleacyd rimageyvsg nppprrthpp
       61 kdsekyltrv syptvadpal vglfmeagig vlssrlmnsd faqaffihlv nkvpgegley
      121 niswhqdgqy gkhlfsghwi tahialedvn sddapilyve nshrleplnk revsgfsfrk
      181 pldelgqqfa qktgikwnvv eylskrgdvt fhdsrlihat dnllsgrtrk tfvlhlrfeh
      241 nkllfsdpih vtneppqpnf yvdiadsimc pvlhgvatdl perrlkag
//
LOCUS       WP_010606799             392 aa            linear   BCT 01-JAN-2025
DEFINITION  TniQ family protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010606799
VERSION     WP_010606799.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Li,Z., Zhang,H., Xiao,R. and Chang,L.
  TITLE     Cryo-EM structure of a type I-F CRISPR RNA guided surveillance
            complex bound to transposition protein TniQ
  JOURNAL   Cell Res 30 (2), 179-181 (2020)
   PUBMED   31900425
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Kholodii,G.Y., Mindlin,S.Z., Bass,I.A., Yurieva,O.V.,
            Minakhina,S.V. and Nikiforov,V.G.
  TITLE     Four genes, two ends, and a res region are involved in
            transposition of Tn5053: a paradigm for a novel family of
            transposons carrying either a mer operon or an integron
  JOURNAL   Mol Microbiol 17 (6), 1189-1200 (1995)
   PUBMED   8594337
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10534787
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..392
                     /product="TniQ family protein"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=43680
     Region          9..157
                     /region_name="TniQ"
                     /note="pfam06527"
                     /db_xref="CDD:461938"
ORIGIN      
        1 mqflsqttpy pdetiesylf rlsqdngylg fadmadilwd wlvtqdhele gafpnelqsv
       61 dvykasqssn frvralrlva qlagveasel fnlcwlhsnt qfgaltavsr ggllvprqll
      121 rksgipvcie clkqdahipy lwhlraykac hkhnqlltri cghcaaeidy raseaflece
      181 cgaaikpaak anqadlklan alagnavakl vglmawfsqc qsisydedef selfvsyfsn
      241 wpcgfegeli staelakvkq lrpfnhtpfn dvfgsllkds klacagsqgy ntvqlaiiaf
      301 ltklveqnpk kkhpnlgdll lsmldaavil gtsaeqvfrl yeegflaavq ppkkntflkp
      361 sdsvfylrqv ielqqsfapn mpnnqqqfvp pw
//
LOCUS       WP_010606834             409 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010606834
VERSION     WP_010606834.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..409
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45991
     Region          93..383
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mkfdhlhdvv qpwlkelpqg tvisalftng vavvglllly wvirrlvlpn venlarhisp
       61 rkighlapql skfsgrfafv lcllvfsayh erlfvapawv fivmetlvyv mlvvssgflf
      121 sslvnlgngv ynlfpfakev piqgiiqvik llifivcsil vvsilvdksp tyilsgfgai
      181 aaviilvfkd tilglvasiq iaanrlvttg dwiqvdafga dgevidlgln tvrvrnwdnt
      241 vttiptymli sdsfknwram qesagrrikr aihidftsie plpeqkrasl teqypllekl
      301 ddvpsditnl glfrryaeay lkqhdainqe clcmvrelap tqhglplefy cfsrdkrwvf
      361 yehlqadild ymlsvmpafg lrpyqsvsdy fgahrvkvra gskpdatse
//
LOCUS       WP_010606798             590 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010606798
VERSION     WP_010606798.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 590)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 590)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 590)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 590)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418077
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..590
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67511
     Region          100..589
                     /region_name="HerA"
                     /note="Archaeal DNA helicase HerA or a related bacterial
                     ATPase, contains HAS-barrel and ATPase domains
                     [Replication, recombination and repair]; COG0433"
                     /db_xref="CDD:440202"
ORIGIN      
        1 msiaigevis ikgtniviel yeesnketlf yngvkfngvs iqefllirrg fkdivarvqg
       61 eylderykde esnqyirkve lipigyfqsd tffegikhlp mirdiaylms dtqvkeifgk
      121 pddnfivget lteelpvslp weklfnthlg ifgntgsgks ntltnlyttl fnnklgkiig
      181 kshfvvidfn geytnnqlvs drnykqvyql dtrsddgdkf pltsdafwde elfgilfkat
      241 entqkpflkr lvsgrkkyig qpnslenyvk stiyfaltst aqkkefvdli seiskitesq
      301 glmfvvsqig whssqqklyf pgtsdylsgg dndvayntrc rpyvdaislt tlspfnelrl
      361 rinvqlladl vsgyvqfehi qpllkrveas lvaldrvfni devlpsekll svislrktnq
      421 evkkvlplll akfyygfhkq qvinqsppqq tlhmiideah nilsmqstre seswkdyrle
      481 lfeeiikegr kfgffltlss qrpadispti msqlhnffih rlvndrdlkl lentisslde
      541 lsrqmipnla kgcavltgts fdipmvvqfn evadghrpds ddvnirelws
//
LOCUS       WP_010606871             351 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010606871
VERSION     WP_010606871.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..351
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40456
     Region          103..351
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <284..346
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mfsqtvqlqp vnilqivftv vsvlgvilvw kmdryrgvlf lfiyysilmi fnlyeetrgq
       61 dgyivtpift likgpivyfl vrwiinekpi asklkflhva pailalpftq hvqliiliat
      121 fsqitylias lklikryhsi smavrsdals lkldwvnkii yvffifalvd llrlnlqpfn
      181 aieikagwyf idvlvalllm cflvvktahq pelfddmvpy edlkvkvlec eqqsnlklaq
      241 qlceditkvv lekelykkpr lslievanet gfklkdvsws infatgynfc efinnmrvne
      301 vkkqivlpqe shksileiaf dsgfnsksvf ystfkstvgm tpskyrssqk q
//
LOCUS       WP_010606876             333 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010606876
VERSION     WP_010606876.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 333)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..333
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37786
     Region          <152..330
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mmfhdpmava qekmtqvclf leqhhlpptp lnyqvaythi satnkdldra inkaikahtk
       61 idcvfieqly yqfldqgqkt qsellegvds lvtelhenae tsqkqvirfa qqvsqcvhnl
      121 dehniqkskr alstltkqte lllkqhkqfk qaliksrldy ernqkllldl rkqhlldpqt
      181 glykrhylhq kvslwqsqqk svcalsiqvd nldefstrfg dvvgevvlnr iannikryvv
      241 esglpgrtgk keftviladv dldtasviae kvrkgverlk fvsakgkipl pnvslalgia
      301 qlapeqdfnm lakragyaaq kahslgqhcy ish
//
LOCUS       WP_010606882             258 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Pseudoalteromonas maricaloris].
ACCESSION   WP_010606882
VERSION     WP_010606882.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..258
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28809
     Region          4..256
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mdkmidagvn ltssqfssdl aevitrakea giesmlaigc dltsseqsis laeqyqlyct
       61 agvhphdakd apdtlyddll tllkssnkai avgecgldfn rdfsprpiqq nvcltqlqla
      121 eainypvylh erdahdalfa llqevkvqgv lhcftgdrta lrhyldyglm igitgwvcde
      181 rrgttlqeli qyipldrlll etdapyllpr tinpkpksrr nepmylsyva eqiahlkqcp
      241 vsevistttt nfkqlfvr
//
LOCUS       WP_010606908             386 aa            linear   BCT 01-JAN-2025
DEFINITION  porin [Pseudoalteromonas maricaloris].
ACCESSION   WP_010606908
VERSION     WP_010606908.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..386
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=43494
     Region          85..340
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mnftlsnsta liglacllts saalatdrpv tmadienler qlaelkarfm tqnselkaaa
       61 pmakstpqsd pvkpptepst tlktyatirp tfgvinqdda snwdvrdals hagikvthef
      121 mpgwqaelhg ewgidlaneg nfgksrrayt algtpygrfg igkqrpaqyl fiaeyvdifn
      181 hasspfaydp esiffidnlv tyryelgpmt fiaagqfngd kgdnqtdlfn tglsydnagl
      241 haaityqqnd vydneqhige nqlwsgalay qftsrfyaam ayqdkdyqrv ealdsrqght
      301 fdlslayqla khyklktgyf efddgygshd plnqsfdgyn vtlewlptpp lrvhleylnk
      361 sfdnqidmds isigfrydyk qewqfd
//
LOCUS       WP_010606952              99 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [Pseudoalteromonas].
ACCESSION   WP_010606952
VERSION     WP_010606952.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..99
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11327
     Region          11..94
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 manshnnvnf iahitpkteh yqncinaiqe ilpatraevg clrfelyese drtqltlver
       61 fvdhaafdfh hqqaytkqvf tlyqgwlaka vdiiaikpl
//
LOCUS       WP_010607096             183 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Pseudoalteromonas].
ACCESSION   WP_010607096
VERSION     WP_010607096.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..183
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21114
     Region          16..178
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 miinakeaft qeqtdalvar cqqgdqsafr elfeqhhrrv yalclrllae pahaedacqe
       61 vfvqlwqkid qfkgqsqftt wlhsvtsnia isylrkqknw lqkvvsfeqs gldeqgaeql
      121 gelngldkli vrlperarlv fvlhavegyr heeianmlnm avgssksqyh rarnllqewy
      181 nnd
//
LOCUS       WP_010607114             371 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010607114
VERSION     WP_010607114.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..371
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42358
     Region          17..362
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mwiweqvrwp nftwdkdkie pqlrsvrlhq gvllgkvlsq tanhkqsmld tllanivhss
       61 aiegeklnaf slrsslankl glseerpfpt sartdglaei mldavdnlev plsierllhw
      121 hkrlfveddt lfnsvvggql rgdepmhvvs grldrptvhf eapgrelldr elgvficwfn
      181 esriqpsldp llragiahlw fvtlhpfddg ngrltrlltd lalaqaerqs vrfyamsvsi
      241 larrksyydi leqtqkgsld itdwlvwfld tldetfaqvl qeidkttikt nfwrninqtq
      301 ltaeqvkvln kmldgefeqg intsqyhkva kvskptatrh ltwlvelgcl vkseaggrst
      361 rytlaqmevd k
//
LOCUS       WP_010607225             357 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphotransferase enzyme family protein
            [Pseudoalteromonas].
ACCESSION   WP_010607225
VERSION     WP_010607225.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..357
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39740
     Region          5..315
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 meyqavaqql adeyglisee akmkpigsgh inttmllqdn hktmvvqkln ttvfpnplhl
       61 venaraieqh ltakalngey slaiikhlat ssgqylvdin devwralafi grsysedvva
      121 neqqaltaan afgqfahaln dfdaaqlhhv ipnfhnlamr idafnqvlak dehgradkcs
      181 dviaafqqqf alaeelqqaq kqvplrachn dtkinnmlfs tqsdaaravi dldtcmpgnw
      241 lfdfgdmvrt fcspeaedst nlsnvqvren ifaalaqgyi eplqdsvtea ekdsfilgak
      301 vmpfmiglrf ltdhldgdny fathranhnl draknqfaly ssvlekedcl nniirai
//
LOCUS       WP_010607270             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010607270
VERSION     WP_010607270.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33670
     Region          7..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,228,245,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 melhkqlenl ylfrlvasig sfqgaadkvq lprssvskri sqleqqlnvr llerstrkla
       61 ltqsgsqllk steklqevls qteqlseqqr stpsgkvkis cstlmaeryl laklhdiskq
      121 fpdirfelnl tddivdlidn qiniairigh lpdssllakk igeksfawfa speylavagt
      181 pdspdallsh rclvfknkgt tmdkwpfvhq ngqvfnikph avaycddara mvqlavlgqg
      241 ivmgdpyyvq qelnqgqlvp ilteyahpdr qpihlvclgk qgrskavqcv wealshslnr
      301 m
//
LOCUS       WP_010607335             833 aa            linear   BCT 01-JAN-2025
DEFINITION  PilZ domain-containing protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010607335
VERSION     WP_010607335.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..833
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95753
     Region          149..>232
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
     Region          494..583
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mpedrlqkyq sliedlkldl gdpafdrifk qrtadlskpd qfllkmemsr lsqpvarfid
       61 lrgqvagqvk pyeyegkqhf mddlaievfe revakhggyt lavyesvmst dnnykvmqkq
      121 akareeevek davnhnytkl vrfasyesrs eermnysiki tvelaknrpk vsattsdisl
      181 sgakiklptn qqvdpgqiis irlvgleqdf elglkegiqy evvavepgti eynqvrlkrt
      241 fieknqgfdd flnsfihgnk rrykinldnt ldavvckgye qyyfprvcsl fvfisekqkq
      301 lypsmvltne nnahinyyfe derkqsglys vfnqkrmqrl lalcgavkea vchvfthssq
      361 gkmyfysafd feleemqqln dlffafgsqk dswrtfkvql mpshhedafi plslpasagk
      421 nveklnkrpt prvqgfiqdv kylmlltdig npsiterfqr lsyeqslvnq lkkfghgksa
      481 tppplevval eyvnlrahrr ylyktnvvvh idgqgtfncv trdfsvmglq iecgqempln
      541 kgdsihldlv dlqkltkqhn ltnlryevmm vnktktiinl kvqkigqldh samgffkali
      601 esnkdklvac deapkvpgls lalrnmvtks vcqfplylhk etshnavgai gqglyptslh
      661 hllhsfsdnd dntldakaif perfveeklt eilkaksrqd kplkylvfik fnpsqanqhe
      721 avgaqviahd esidslylya kkalrndllf vyqlyvsktg rpdmdylane lryvshyaih
      781 kakdleealw svtgvcdlid vteyvvrnmg fdaplvtkme eqkkrwletn fkh
//
LOCUS       WP_010607418             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010607418
VERSION     WP_010607418.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 259)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..259
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29930
     Region          2..249
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 myyighyeye syeelfwfgi sftlfnlitr eiansflria llvycaglll diidnftdgf
       61 sipllnfdts lknigfllis fgfycmitnk rasitelkke verrrlleer mryeadhdam
      121 tgvgsrracf eglqthrfdd qwllyldldn fkqvndnygh higdevlikf tqnmkdyfgl
      181 dysfriggde fiayinavlp dtdevraall kglhdykinv sigmvkvdpa kqadliihea
      241 dehmygdkrg kslrssarg
//
LOCUS       WP_010607494              52 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF2256 domain-containing protein
            [Pseudoalteromonas].
ACCESSION   WP_010607494
VERSION     WP_010607494.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..52
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..52
                     /product="DUF2256 domain-containing protein"
                     /calculated_mol_wt=6332
     Region          2..45
                     /region_name="COG4338"
                     /note="Uncharacterized conserved protein, DUF2256 family
                     [Function unknown]"
                     /db_xref="CDD:443479"
ORIGIN      
        1 mahkkvnlpy kvcpickrpf ywrkkwqrdw envkycskrc aaerrlsigy nn
//
LOCUS       WP_010607497             300 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010607497
VERSION     WP_010607497.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..300
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=32088
     Region          65..283
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlqritkptm wplfftlgvy atliwvqgfy qalgqiises hialtmalgs fvaggtalgg
       61 gavafpvmtk lldidpatak vfslaiqsfg mtaatitifc rripvyknvi lmalpmaalg
      121 vtlsllyiap laprllvksi fsflllcfal tlilrwwrka hhqpssefiq pkmlrfmava
      181 liggiasglv gsgadialfa llviaynadv kkatatsvvv mtftsligss inawhlntis
      241 neingyllaa ipivvvgapl gayvcskvkv ghlvsfllvl iglevsftcy elyptllglf
//
LOCUS       WP_010607522             437 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudoalteromonas].
ACCESSION   WP_010607522
VERSION     WP_010607522.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..437
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49032
     Region          5..435
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mfahyldlaw rslkatplat slmtlaiaig igvtmvslsv yhmmsadpip sksgklyavq
       61 lqvmdegqty hsaddipfql tfldaknlyq tlnvdkkvam fksgfavhvs npevrpmlqt
      121 trlitreffa mfelsflygg vwsqsqadna apvvvideti aqklfgrsdv vgesiylaqr
      181 ryqvvgvtke wqpnvkmydl nngafadaer ifipfshaaa yeidtwgntn gwkreeinnf
      241 tdkmnsemlw tqfwvelene keqqalatql dnyiqtqqdl grfnrktref slrnvtewle
      301 ynnvvsednk vmiglsfmfl avclanilgl llakflkrap dvgvrralga sktqvfyqhl
      361 vevallgfmg gvigivfaql glwgirktsh vyeslatmdv smllaapsia ivtcilagly
      421 pawivcktsp atylkvq
//
LOCUS       WP_010607577             403 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S41 family peptidase [Pseudoalteromonas].
ACCESSION   WP_010607577
VERSION     WP_010607577.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..403
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43639
     Region          40..387
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mnrqtrfyal aaryvallsf llllsfsafs hastqkfsaq eideilyhih tyyvedlpls
       61 rynagnlssl fdnldpysky lneedlesif saangrytgl gieveeqdny viildtlpns
      121 paaqagiesg dklhaingan vagksieevs allkaanknl inlvvlrqde lvalelkrqe
      181 iviesvaskl lndgtgflsv nsfnhhtyhd varhisrlqv qlgsplkklv idlrdnpggt
      241 lnsavaisdl fldsgtivtt kgrfydanqa yiakrgdiln gapilvlinn nsasaaeila
      301 aalkdnkral vvglrsygkg svqslipign gttalkltta ryytpagtsi egkgiepdvy
      361 ftkqalslld ksaiitgees ikttgieqla shwpkalalv qsq
//
LOCUS       WP_010607681             210 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pseudoalteromonas maricaloris].
ACCESSION   WP_010607681
VERSION     WP_010607681.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..210
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24867
     Region          44..186
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mysihplwqq fpcadktalq gtelasyhnp qinktvrfkl iskadlplfc qwmndprvah
       61 fwqqawseek qwqylserla dnfslpllmy fdeqpfgyve vywaeldkla gyyewqpkdr
      121 gvhllvgeqs crgpenfraw mtslshliyl ghedtqrivl eprhdntrll triaelgyhs
      181 qfefdfphkr aalvmaekas fyrdvfpqfa
//
LOCUS       WP_010607602             495 aa            linear   BCT 01-JAN-2025
DEFINITION  sialidase family protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010607602
VERSION     WP_010607602.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..495
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54004
     Region          188..474
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          291..346
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          355..395
                     /region_name="Sialidase propeller 4"
                     /note="Sialidase propeller 4 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mfsnvytsmr laylgvalsl lsacggssnd dvddinnagk ekppaevkyn vtgvveglka
       61 kystnelvdi dvnllgddkp lsskdgwlvk yklyqtsstg aeqlldergg mfdqqtqrwk
      121 isfsasesam nvklklqagc svasglcadk agsnkdkqwe qtfeysvnav vehrvnvtnt
      181 teysgatsli slengdlval ynhglsdths rvsissdngq swvqtfslnv etlgdfaiet
      241 gklfedksgn llavgncnes slcilksdse slwskvseid fsnydscdgg vdfpcsnarl
      301 vpgsliqlkn gkymlsylfa pgansaeldv yirisddlvn wseekrvagn gfdrsesnvn
      361 aialpdgrvl lsytpfdsel itilisndge nfetlqklnt asiprsvsli nhngstrlfy
      421 sadygnfyss slgeaelftk pqlikefdys dirtsdeplv tdlidgtlgv iytkklneqh
      481 dvffenlgaa regvh
//
LOCUS       WP_010607787             188 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [Pseudoalteromonas].
ACCESSION   WP_010607787
VERSION     WP_010607787.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..188
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19744
     Region          5..171
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mttakiiala gslrkdsynq lliqaaanfa lesgaevevi klqdldipmf dedleaqgtp
       61 kgaqllkdkl rdadgillas peyngsftav lknaidwasr teqgavpafr nkvvalyaas
      121 pgglgglrgl nhvrdvlsgi gslvladqla vpsafnvfdd qgkikdpela ekvsslalql
      181 vsvasklk
//
LOCUS       WP_010607744             760 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas maricaloris].
ACCESSION   WP_010607744
VERSION     WP_010607744.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 760)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..760
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83679
     Region          36..724
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mnsyqprysa ialaitlatq vspaaaeqat qsegklerie vtarktvenl qtvpvavtsi
       61 getdllengi svlsevqqfs pnttlqasrg tnstltafir gvgqqdplwg yepgvgiyvd
      121 diylarpqga vldlldvqqi evlrgpqgtl ygkntiggai kyvtkemsgd atfnvegtvg
      181 synqrdlkit gqlplledtl ylgygfatln rdgfgefkvs tlpsqdkeny nkeiqaarlt
      241 leyrpsddlf frlawdktdd dsnskggyrl lpslltdapv pdsvfdsyts mptwnkvele
      301 gysltarwdl sdattikyig asrdsysptn idfdntplri fdvpaiydde qttheiqlsh
      361 agngykfvsg lyyydgescg qfqailevlg qslgapgltr evsgcnnsns kaayiqgtid
      421 laaqwsltlg arytkdskea qvsnglvfdv vypesnwipg ytrpagelvp svlddeedws
      481 rftprvgvey qynrdimffa syaqgfksgt fnprastaep aadpeivdsf eigmksewnd
      541 nlranitlft ldhkdrqyis vlpgatsadl nqrlgnigks tangieaels yvatealsfd
      601 aaigyidsdf eevldtnpdt gatfdksdrf sisntpdltf nlgatyklys digdwvfnas
      661 yyhrgdyvlf eedslltqds yglvnlsinw ystdgnwrvg lhgknltdke ymiggyqfvt
      721 pdpsdpsnvs kytpglggdn tligyfgdpr tvsltvgyrf
//
LOCUS       WP_010607770             350 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010607770
VERSION     WP_010607770.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..350
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40522
     Region          6..293
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mfryyvalll lflstqiaal ekvtlqlkwt hqfqfagyym akekgfyhre gldvhilpad
       61 pnnpnidfrv lygqaqfgvf hsgllkqrln gkpfvalaav lqsspycwmv radsdiyvpr
      121 dfqgkrlshl ghtengellm mlqragvntq nmrlysgnep lkdfiagkfd amqvystnep
      181 yavqqsglst reicpkqfgl nvyadvlftt esvlenrpel vkrfrraslk gwryamlhle
      241 etlaitkqqy atqksleqla feaeklrefi kvanipigtm stakwqwiaq lyhldvsqfh
      301 ehkarfiyse vkneqpklsw vliiaailtl vcipmyihli fsrkyhqqlr
//
LOCUS       WP_010607839             449 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudoalteromonas].
ACCESSION   WP_010607839
VERSION     WP_010607839.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..449
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48860
     Region          7..366
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(14..15,18..19,22,54,104..105,107..109,112,132,
                     135..136,139,206,209..210,213..215,218,242,246,296..297,
                     301,305,321,324..325,328..329,332)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mksfpslylt nlflvggtgl lttylalylg qhgvstfwig lltsfyylgl llgaklgyhl
       61 iksvghiraf aastaavtac vaihgvsdni ylwlglrlvv glgmmcnfmv leswlneqaa
      121 peqrgrvfsf ymltsylgmv tgqfalsnfp elgyaplfli vvalsfgiip isttrrihpk
      181 plkpiqvslf tyfkkvpqsl tavcfagvin gsfyglaptf asqsgfnaee iamymsvtif
      241 agllaqwpmg iisdrvrrsi llrsnavfig lislcifllp lspsyslwlt fgfglfaftm
      301 yplssalans rvddedrvgv ssallvafgg gacvgsaaia qimshfghqa lyaslsaltv
      361 vmflllhfin arqkaeqpep sdyvaatsdi tssplaatmd prieektahe qllvvdedtp
      421 rdnddelddn eqnsepteel deitnkpqp
//
LOCUS       WP_010607913             394 aa            linear   BCT 01-JAN-2025
DEFINITION  dipeptidase [Pseudoalteromonas maricaloris].
ACCESSION   WP_010607913
VERSION     WP_010607913.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..394
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43543
     Region          33..388
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mklgtalcal alavstayat eykaseravk lahdnilidt hidvpyriqs kwddvsqate
       61 ggdfdyprav kgglnapfms iyipanlefe gkgksyqlan qlidgmeala hrapdkfama
      121 yntddiyaqf dsgimsiamg mengspiege mknlkhfydr gvryitlahs qsnhisdssy
      181 dvrrkwkgls pfgkelvvem nkigmlidvs hisddafyqv mdiskvpvva shsslrkytp
      241 gfernmddkm lkalaknggv iqinfgssfv takagawydk rdeaqkeakd kdrtdfraaf
      301 raknpfpfat ldqvldhidh vvkligidhv gigsdydgvg dslpvglkdv stypnlvqgl
      361 ldrgysdadi kkilggntlr vwkqaeayak kfak
//
LOCUS       WP_010607893             359 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: potassium channel family protein [Pseudoalteromonas].
ACCESSION   WP_010607893
VERSION     WP_010607893.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..359
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40201
     Region          23..104
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mpiifkrlvv lmrahvdkas wqllfmatli hmsvtwgllw lsnesallpl stffyyyvvt
       61 tstvgygdfs attdfgrlvv aiiqipfgla lfgvllgkag qfvtywvrrg mtgekdfahl
      121 qnhivifgwh dvrtkkmvdy ilgdnkredr kivlavteam ehpllsypev afarltsftd
      181 deqlsrinie radkiiidgd ddnqtfttal klsrvvkpea hisahfldds kalllrehck
      241 nvecsasmsa eilvramqdp gssrvqeell stlhgdtqfs lalpaevscl tfgdifgyfk
      301 qhhdatllgv ahdinalnmd lnppldynit ggdilhyiap qrvlasevdw sslcsknsf
//
LOCUS       WP_010612964             511 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase, partial [Actinomyces oris].
ACCESSION   WP_010612964
VERSION     WP_010612964.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         <1..511
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          189..>290
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
     Region          406..501
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 asttaaatas aqtaapssdg atgtagssee etdtatfsca vitvpldyan ptgetisiav
       61 kkraatggha qgalfinpgg pgdsgvsfae ragnafspdl leaydiigfd prgvgsstai
      121 tcssdddssg staepsatas ssasgtpsag tepspessae aasggesyee waestrqsfq
      181 elteqcasht epaalldhvd tvsaardldi lralagqekl nylgfsygty lasvyaetfp
      241 gntgrmvldg aidpslslae qglgqakgfe qalrtyvdyc qnstgcplsg gtdagvqqir
      301 dlitsanstp latgdpnrtv tgsdivaals eylytteqnw eplnkaldqa inhrdgsafv
      361 aseeqdtssk ddgggafqav tcldypvegd kttwaaqyeq akreapvfad savgmdlvcs
      421 vwghngtrkp aqihargaap ilvvgttgdp atpyawsksl aeqldsgqll twegnghtay
      481 ggdascvnda vdaylisgtm pkkgltchgn e
//
LOCUS       WP_010612894             238 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Actinomyces
            oris].
ACCESSION   WP_010612894
VERSION     WP_010612894.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..238
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=25866
     Region          126..225
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mtsmpditrt grgvvalllm rtvllfagtg ivlpfvgwiy nrallwanvt vvivdvitll
       61 vlsrllarqd rrlrdllaps wsgtawglla fiilqigfsa stfigilvay qgdppasgvl
      121 hgvpmwmgww vllvmpvtia laeeglyrgy aaealesrfh kaaaliviaf ffalqhaalt
      181 plspraqlar fittflggll lggmrwrcrr glwplvvahw gldvlglglp illasqas
//
LOCUS       WP_010612985             267 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Actinomyces oris].
ACCESSION   WP_010612985
VERSION     WP_010612985.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27745
     Region          19..253
                     /region_name="EfiE"
                     /note="Predicted lantabiotic-exporting membrane pepmease,
                     EfiE/EfiG/ABC2 family [Defense mechanisms]; COG4200"
                     /db_xref="CDD:443354"
ORIGIN      
        1 mstsalipvt trragntgfp sllaaevikl krssvwvvav llpllavitg tfnfyrnqgv
       61 fsaewgslts qislfysmff cslgvallas sawrmehrgt swnamrtsph spvsvvlakt
      121 lvivlpvltm qvalivlawi sgafvmglgl ampstviasn llavvsiipl ialqsllsml
      181 mrsfaapval gfvgcvlgfg lgaaqnplay aipqglvsmt lslgstalta geldaasmlp
      241 lllsivgvga vmwgllvlaa rrtggvr
//
LOCUS       WP_010612988             402 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase, partial [Actinomyces oris].
ACCESSION   WP_010612988
VERSION     WP_010612988.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         <1..402
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          72..401
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 giclsahlvl ftgfsvffvv tgliavettq srleapwrwv alvleivgve latarvfhli
       61 ggyvhagear svvvvniwlv tivaafvgaa rrrsrdrynr alerasvlea qqaterrlav
      121 ietqqriard vhdllghslt viamqaegar ailatdpaaa dealaviget srrsvdevha
      181 lvdmlrsdag aagvggsgag grpaggaggg asgtveagae agtgtgeats gqhvellrep
      241 vrqaqraglp vtleadpagr vppavaqvlh rvvqesltnv lrhapgaatr vslrtgagrv
      301 ilvvenapvp eslagdadpm prtfdphred rgeqvdavpg rtphasaams rpavsvsegl
      361 rrggfgligm rdrvaqvggt ftagptvegg wrvttelpcv pq
//
LOCUS       WP_010613168             440 aa            linear   BCT 01-JAN-2025
DEFINITION  uracil-xanthine permease family protein, partial [Actinomyces
            oris].
ACCESSION   WP_010613168
VERSION     WP_010613168.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..>440
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          15..424
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mssspsrgwr lhgdgrsiap gevvapgerl twprtigigv qhvvamfgat flvplltgfd
       61 pattlfftgv gtllflgits grlpsylgss fallapigav taytrdsgaa ldphkaalaq
      121 ggiisvglcl lvvgvvvhlv gsawidrlmp pivtgaivsl igfnlapaaw gnvtkgpvta
      181 vvtivsilvi tvlfkgiigr lailigvlig yatavlrgev nfdavakapv lglpdfhapa
      241 fdvrylglfi pvvlvliaen ighvksvsam tgedldditg ralfadglst mlagsgggsg
      301 tttyaenigv maatrvysta ayvvaalsal glsllpkfgq iiatipagvl ggaatvlygm
      361 igmlgvriwv qnrvdfsdpv nlntaavsmv vaiadytlvw gdmtfkgial gsaaaigvyh
      421 amrwisklrg tnleqaspas
//
LOCUS       WP_010613351             384 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Actinomyces oris].
ACCESSION   WP_010613351
VERSION     WP_010613351.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..384
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38885
     Region          1..381
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mlrlggtgir arptraflsa lgiaigiaam isvvgisass raqlsaqlds lgtnlltata
       61 gqdlfgnsss lpqdsvgkvr lidnvqsass tglvknslvy rtplidknas ggittlaadk
      121 slldvvagqv dkgtwlneat skypatvlgq taaqrlgvvs pgtkvwlggn wftvvgilkp
      181 vvlapelnna aligqgvasd llghdakptt vytrsqdaav ptvrkllaps ispqapnevk
      241 vsrpsdalea knaadkaftg lllgvgsial lvggigvant miisvlerrr eiglrrslga
      301 mrghilvqfm tealllaslg galgciigig vtagmsaang wpfslpviav vgglgvtiai
      361 galagvypav rasrtpptaa lnaq
//
LOCUS       WP_010613502             727 aa            linear   BCT 01-JAN-2025
DEFINITION  M13 family metallopeptidase [Actinomyces oris].
ACCESSION   WP_010613502
VERSION     WP_010613502.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..727
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=79621
     Region          27..727
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mtdacatsst ptgpasdspa hhsqptasps ptaeavlagv letahtdtsv rpqddlfrfv
       61 ngqwlataei padrpssgaf ttlrdeaeaa crqiveelae qfssvapega sevlatnrgr
      121 vgalyeafmd eahleelgae plaeelapvl dasskeelar algemtpigf mgvvgadvev
      181 dindperyts wvgqsglglp desyyreeaq apmrqayvah varmlslagl tdsfgasgee
      241 laervmavet alakghwdrv tcrdvekmnn pmswrqivds apdlpwdewr egiraaarsa
      301 gieqtaflee aivtqpdylp haagvwqets lvdlkvwaaw havhgratll sgafveenfd
      361 fygrtlqgtd elrprwkrgv glvesclgea lgeiyverhf ppshksamea lvgrlieayh
      421 qsisslewms patreralek lalftpkigy pvrwrdysdv evvpgdvlas vrsveradma
      481 yslnkltkpv drdewhmtpq tvnayynptm neivfpaail qppffdpqad davnyagiga
      541 vigheighgf ddqgstfdgt gkvsdwwtqe dreaftertr alisqydayt pevvvakhqd
      601 agteqaeiph vngaltigen igdlgglgia lkayslalad vgipsvdeap vidgltglqr
      661 ffyswariwr sksrpdyael lltvdphspa efrcngivrn vdafykafav dsddalwlpp
      721 nervsiw
//
LOCUS       WP_010613557             313 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide pyruvyl transferase family protein [Actinomyces
            oris].
ACCESSION   WP_010613557
VERSION     WP_010613557.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10514996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..313
                     /product="polysaccharide pyruvyl transferase family
                     protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35327
     Region          2..286
                     /region_name="WcaK"
                     /note="Polysaccharide pyruvyl transferase family protein
                     WcaK (colanic acid biosynthesis) [Cell
                     wall/membrane/envelope biogenesis]; COG2327"
                     /db_xref="CDD:441900"
ORIGIN      
        1 mgdeiigrsi emnwrelfss nyvmrlasht pmytpaqyll skrklsifkg adikllcgtn
       61 alytnmlrpl ptwninylnc gmatgtvclg vgagansssv nlytralyrk vlshdlvhsv
      121 rdehtkhllq rvglrawntg cptlwgltpe hcetiartkg devvftltsy hpnprkdram
      181 vdvlrrsysr lhfwpqsidd ldylqslgaa dgveivtpsl agfrevldrg vdyvgnrlhg
      241 gifalqrkrr aiivaidyra remakdyslp lverdsietd ladliesswp taihgldfdr
      301 iekwkaqfdv gkp
//
LOCUS       WP_010613758             323 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter, partial [Actinomyces oris].
ACCESSION   WP_010613758
VERSION     WP_010613758.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         <1..>323
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          <4..269
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 angiaiatam tstaigtilp ilrdrgllpt avgasilnhg avgevgpviv malllgsrst
       61 wasmvilgvf liitllivrf tsrvkrvgrr lveaihlgas ttaqttirat vlllvglcai
      121 aaifdldvil gafaagfvlr halpegdaef eekldglayg ffvpiffvts gmgieaglna
      181 gdlvnllaff vllvlvrgvp vwlasraerr rdgsraysir qslqiavyst talpiivavt
      241 qvavsagams tsfastlvla gvlsvlvlpa aglalghrsd hvpanevmrv vqgpaapdgr
      301 tpeeatvpvg eevseprrpa spp
//
LOCUS       WP_010613847             488 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Actinomyces oris].
ACCESSION   WP_010613847
VERSION     WP_010613847.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..488
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=52297
     Region          17..271
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,74,91..94,98,100,136,138,
                     140..141,143,153..154,157,172..175)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,74,91..94,98,138,140..141,
                     143,153..154)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(24,98,100,136,138,140,157,172..175)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(37..38,65,71,76..79,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(153..161,168..175)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mldhkgpppv isgftylerl gaggystvyl feqhmprrev avkvmnadve dktasrfese
       61 anlmarvssh pailsiygag vsadghpflv meycpppqlg ailrqgplnv aetlstaiqi
      121 agavetahra givhrdikpa nilfttyrrp vlsdfgisam sgpegteelr gmsvpwappe
      181 qlvgmrsanp asdiyslgat tfamltgrsp fetdgipdvy elsrrivkdp lpplgrqdap
      241 pslhrvlsva mdknpdsryp talafaralq qvqaeldlpi ttvdlfqepd kaaksarrps
      301 hdetdtatkm gvfnqvdvts ehiamrvepd gedkgsssds eagetgrpnr mrgvltgllv
      361 vamvaavvaa ivvsqnqdkq kkpnnpiati apqpdanplq asvpmvgdiv geaqgdgtvk
      421 fswgepetnw sgsylyrvkl pdeeteldsv rtnevvvdaq partclevta vradgkaspa
      481 ktacvdtp
//
LOCUS       WP_010613881             225 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Actinomyces oris].
ACCESSION   WP_010613881
VERSION     WP_010613881.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..225
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23474
     Region          1..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtgaleliev svdyhrggqp vhaldsvsla igrsesvavm gpsgcgkstl lgvlaltipp
       61 tsgsvlvggv papsspdgra rtrnrllgli pqsgavidhl svlanvslpl eysrprtrrr
      121 vrherarqal advgigwaea ttpprlsgge rqrvavaral vnrprcilad eptasldsat
      181 alevtsllis qstrhggsli iathdprvae acdrvltmqd gritg
//
LOCUS       WP_010613959             148 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Actinomyces oris].
ACCESSION   WP_010613959
VERSION     WP_010613959.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..148
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15526
     Region          2..146
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mtyntivaav gnleenthvi dracemarlc datlllvagy dpvsprdkar inefapvadv
       61 rvgltedqay avvekardta vergvglaqg vvvegtavda vtlvtletea dlvivgskgv
      121 dslfgrifga vsvqvlrksk cdvlvvvp
//
LOCUS       WP_010613990             341 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Actinomyces oris].
ACCESSION   WP_010613990
VERSION     WP_010613990.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..341
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36280
     Region          57..322
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mqtsltrlta ddgtrlvvhi wlpdwlidgs llvadapetd spaptsavtr pqvpgaarpr
       61 giiviahgma ehasryarfa asaveegyav lagdhrghga taapggfgfi aerdgwdrvv
      121 admgtvldaa rrawpdvpvf lmghswgsfl ardlaarrgg elaglillgt gsgtgaltrp
      181 aaavcagesr lrgprhpsrl lnalafgpyq rhfapnrtea dwisrdvhev dryvadpwcg
      241 fvctasffrd lvtggravnt aahaaavpaq lpmllasgdr dpvgamgrgv qrsatlyrra
      301 gvrevcvily pggrhellne tnrdqvtgdi ltwidghlpe l
//
LOCUS       WP_010614100             305 aa            linear   BCT 01-JAN-2025
DEFINITION  biotin--[acetyl-CoA-carboxylase] ligase [Actinomyces oris].
ACCESSION   WP_010614100
VERSION     WP_010614100.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Chapman-Smith,A. and Cronan,J.E. Jr.
  TITLE     The enzymatic biotinylation of proteins: a post-translational
            modification of exceptional specificity
  JOURNAL   Trends Biochem Sci 24 (9), 359-363 (1999)
   PUBMED   10470036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..305
                     /product="biotin--[acetyl-CoA-carboxylase] ligase"
                     /EC_number="6.3.4.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009374 - biotin binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=31076
     Region          10..300
                     /region_name="BirA2"
                     /note="Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme
                     transport and metabolism]; COG0340"
                     /db_xref="CDD:440109"
ORIGIN      
        1 mtsggspfsr ldtvpvtgst qddlraaltg aeqeswphls alralaqtag rgrsgrawvt
       61 pddggallvs vvlrplvpve rlawlpllgg lavrdalapl vedlpwrvgt kwpndvvalp
      121 ddpaavpavp gwagtrkiag vlselvtpea aqgtaahgla sdvvpadrde apmvilgigv
      181 nigqaaeelp vpwagslrtl gavgagrgpa ltdaaesvlm aighqlarlv gqwedvggdv
      241 daadgalgrr lraalttlge rvsvqapdge igglavdvtp alvlrtqagd tevragdvtl
      301 vrves
//
LOCUS       WP_010614119             238 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Actinomyces oris].
ACCESSION   WP_010614119
VERSION     WP_010614119.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..238
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25669
     Region          23..195
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(26,28,105)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(53,104..105)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            103..105
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mttstatqtg eptpvspvtd twlviplyne atvvrevisq artifpyvvv vddgskdasa
       61 reaaaagavv vrhpinlgqg aalqtgfsyv lektnadyvv tfdadgqhsp tdaaamvaaa
      121 rdedlavvlg srflegpspv gwlkrlvlrt aaavsshtsg mrltdahngl rvirrdvleq
      181 ldlkqnrmah aseiirkiga tgmpwrefpv hivyteysrs kgqslwnsvn ilvdllfs
//
LOCUS       WP_010614389             418 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein, partial [Actinomyces
            oris].
ACCESSION   WP_010614389
VERSION     WP_010614389.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..>418
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          126..390
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mlvavttppa tpsadpsasa sttptptgvp evnvdetvkv vtkttndlva iawqagvgvv
       61 iglviafvvv ailtfmgrrr llyreivdfg rrpivavgam tgaflgtqla ltalrhtksd
      121 sttmvvierg vtialifsvt wlvvafakai estvvkgaqa ggdqgranrv ttqsqiirrv
      181 aqviiviagl vsaimtfpsv qfamgsllas aglasviagm aarsmlgnvf aglqlattda
      241 irvddvvvvd neqgtieeit ltyvvmrtwd drrlilpsth ftenpfanwt rggsqatgyf
      301 tldldwrvpi aslraelarl vaassvwdgr qaslevfdav gghvtvrivl tgndpgdvga
      361 lksyvreelv twlqreapya lprtrveveq vevtqdlgpe evaraaeqiv akqkagpa
//
LOCUS       WP_010614449             557 aa            linear   BCT 01-JAN-2025
DEFINITION  lysine--tRNA ligase [Actinomyces oris].
ACCESSION   WP_010614449
VERSION     WP_010614449.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Francklyn,C., Perona,J.J., Puetz,J. and Hou,Y.M.
  TITLE     Aminoacyl-tRNA synthetases: versatile players in the changing
            theater of translation
  JOURNAL   RNA 8 (11), 1363-1372 (2002)
   PUBMED   12458790
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Desogus,G., Todone,F., Brick,P. and Onesti,S.
  TITLE     Active site of lysyl-tRNA synthetase: structural studies of the
            adenylation reaction
  JOURNAL   Biochemistry 39 (29), 8418-8425 (2000)
   PUBMED   10913247
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Woese,C.R., Olsen,G.J., Ibba,M. and Soll,D.
  TITLE     Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary
            process
  JOURNAL   Microbiol Mol Biol Rev 64 (1), 202-236 (2000)
   PUBMED   10704480
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Delarue,M. and Moras,D.
  TITLE     The aminoacyl-tRNA synthetase family: modules at work
  JOURNAL   Bioessays 15 (10), 675-687 (1993)
   PUBMED   8274143
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..557
                     /product="lysine--tRNA ligase"
                     /EC_number="6.1.1.6"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004824 - lysine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006430 - lysyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=61177
     Region          38..556
                     /region_name="LysU"
                     /note="Lysyl-tRNA synthetase (class II) [Translation,
                     ribosomal structure and biogenesis]; COG1190"
                     /db_xref="CDD:440803"
ORIGIN      
        1 mtdestpspd ptatdaagtq sqkpdqpkqp kadpgpgeqf evragkrerl rgegwdpypv
       61 svpvtttiaa vregyahlea gqetddvvgv agrvvflrnt grlcfvtlqd gagttlqaml
      121 sakalpaegh talaafkadv dlgdhlfvhg rvissrrgel svmaepvlre gveaasagdd
      181 dvevpawria skalrplpkt wtneageavt lseeqrvrrr eldlltrpaa rdmvrtraav
      241 vrsirenffr rdyleletpm lqvihggaaa rpfithmnaf dmdlylriat eiylkravvg
      301 gvdrvfeinr nfrnegadss hspeftalea yeaysdydgm aeltrnlvqq aardafdlpe
      361 ggevvtladg teydlsgewd kidlytsvse algeeitvet preqlvahae kigleiddya
      421 vagkvvedif eelvgnklwa ptfvydfped tspltryhrs kpgltekwdl yvrgfetata
      481 yseladpvvq rerfeaqala aakgdpeami ldedflvame qgfppsggmg mgidrllmvl
      541 tgqgiretit fplvkrg
//
LOCUS       WP_010614450             313 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Actinomyces oris].
ACCESSION   WP_010614450
VERSION     WP_010614450.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..313
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33463
     Region          3..312
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mthavvalal pgvvafdlst aaqvfghpee deysfevvts dgrqvpsstg fqiagvgdps
       61 slrqadtivi pgysphttps ddvlealrsa hsrgtrvvsi ctgafalapt glldglsatt
      121 hwqdaqelrm aypavdvtpd vlyidhghva ssagvaagid lclhlvrrdh gaatanriar
      181 rmvvpphrag gqaqyvapaa rprhpenrla elttwvvahl drpvgvadla rhahlserql
      241 arrfvaetgq splqwllhqr vlaamdllet tglpleaiat rtglgtastl rrhflrhvgt
      301 tpsayrktfr gpe
//
LOCUS       WP_010614463             526 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Actinomyces oris].
ACCESSION   WP_010614463
VERSION     WP_010614463.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..526
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=55809
     Region          27..124
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          <394..524
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mvlvsdlidg adlgvravll paphaavtwv vatellqpas yleggelvlt tglvmadaea
       61 atwreyvasl veagvaalgl gtgiafdtvp edlreacrag rlnlievple vsfasisrev
      121 gamlqatepd igaegagdee tlvlqqltra aakdnqsaim ralasilrge vslrdatgrt
      181 vvgpfgpeat giddevaeci drirpggmrg agavglgdmr lvvrpvgitg eperylatvq
      241 retltraqtl gvdlawsfln liaesskaft gwllqlvgas trhllagdia qglaladqvq
      301 elvltrlpsp errsvpatgg ghqwrvvcle ggsadvagls tvlarllves rgapvgeqll
      361 wrtdrggtrl milgevervp slledgsvtp wtermrigvs gpvgvtdlpr gaqqalsvct
      421 gtrqlgqavc wetsglpsvt dlldeeraqa fararlggva dqpellellr iylseagavq
      481 riaerlgvhr nsvparlvrl rralgvdied aeqranlwfa lhfwae
//
LOCUS       WP_010613862            1017 aa            linear   BCT 01-JAN-2025
DEFINITION  LamG domain-containing protein [Actinomyces oris].
ACCESSION   WP_010613862
VERSION     WP_010613862.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hohenester,E.
  TITLE     Structural biology of laminins
  JOURNAL   Essays Biochem 63 (3), 285-295 (2019)
   PUBMED   31092689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Sasaki,T., Fassler,R. and Hohenester,E.
  TITLE     Laminin: the crux of basement membrane assembly
  JOURNAL   J Cell Biol 164 (7), 959-963 (2004)
   PUBMED   15037599
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10597119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..1017
                     /product="LamG domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=106259
     Region          <101..186
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          615..774
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
ORIGIN      
        1 mklprrllsg llaaalvplg avtlapaspa aadpapapag aagtpstvsa dalptaqing
       61 ivwdqvvvgd ivyavgkfsa vrpagspagq nesprsnama ynintgeivd wapttngtin
      121 aiaasadgqt lylggdfttl nnqaawrvga vrasdgqrap lgasangsvk alsvspdgqt
      181 lyiggaftqi nssarqrvaa lnlgsqrltn fapkidnyyv rsiveavdgs avaiggafes
      241 vegsdkpghg iaifekdgsl rknnassvvh gagaeasvms vkadehglya ssysrlgtfe
      301 gvmrlnwvtg didymaechg dtydvlpagd vvyaashshd csniggfpdv syhyhnamay
      361 tnaatgtvge nkvagyknya gqnattnlnf ypdftpgkis gaiqatwtve gndkyvvygg
      421 eflavngtaq qglvrfarrd iapnkqgpmd kggafkvsgt spragvvsls fkanwdrddk
      481 tltynvyrdd mnaqpvtsqt atagfwerpd lsatdvvepg sthryrvqvt dqwgastvsd
      541 wvtvkaaegq glskygarvl adgaahywsf detsgdkaed fvaqrnltir gkaykrgsgs
      601 vlgsgaslgl tsdatnksha atrvasqapt tfsmeawvrt tstsggeimg ygssaanqsw
      661 nrdrmvymrn dgtlsfmlyp gklttittpk syndgqwhhi vaslsptaga mlyvdgnlaa
      721 fdaamtages ysgywriggd alggvngqps ntniqadide aavystplsa rqiaehytaa
      781 tgkqvepdkg ddkgkdnagk dkgkqpegka llddsfersv nggwgkaqag gawkttwnaa
      841 afsvdgtsgr iamagprssa siisdpikst stdavvdfsl davptgngaf isyaarttka
      901 gqyqatvrig sagnpvvtvs rvvkgketsl gsyvmkqpyt agqplhlrmv vdgaestniq
      961 tklwagdtep aewgieavdn dktlneagtv glttymsgsa gpetvtlsvd kvtikqh
//
LOCUS       WP_010614466             526 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Actinomyces oris].
ACCESSION   WP_010614466
VERSION     WP_010614466.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..526
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56221
     Region          13..493
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msaattnsgg glskkglaeg svgllgaiii gvsciappyt ltgalgptas evgeqvpaif
       61 lvgfvpmllv afgyrelnaa mpdsgtsftw gtrafgpwig wmngwgliva tvvvlsnlaa
      121 iavdffylll aqvtrrpaia dlsdnvwvnt ltclvfitla twiayrdmqt tqklqywlvg
      181 fqltvflgfg avaiyryftg tavnptplkl ewfnpfavds lgtfvagvsl slfiywgwdv
      241 sltvneeadd asstpgraav ltvmtivsvy mfvtigsmmf aglgkdgigl gnpaiqdnvf
      301 falarpvlgp faillstavl vssaaslqst fvspartlls mgyygampek lgeisprflt
      361 pgratvvsai aastfytllr fvstsvlwdt vqtlgamiaf yygltafaav wyfrgqwfrs
      421 vrnfffmlvs pglgglilfs llgltlkdsl dpeygsgsqv fgvglvfvlt lalillgvvl
      481 mlvqyvrapa ffrgeviars davteemkva tvyedgdday plraas
//
LOCUS       WP_010614458             329 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Actinomyces oris].
ACCESSION   WP_010614458
VERSION     WP_010614458.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34521
     Region          21..273
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtdlpstesn agtgpaapga rlaargatia yerhvvsrnl dvdipagvft aivgpnacgk
       61 stllralarl hrpargavll dgadivrlgt kevarrvgll pqsatvpggm lvrdlvargr
      121 fphqglfrqw sqqdrqavee amemvgvtel aarpvdelsg gqrqrvwial alaqgtetil
      181 ldepttfldl ahqvdilqlc rrlnadgrtv vavlhdlnqa arcaehmivm hegrirttgs
      241 preiltedli eevfglaavi apdpvagtpm vvprhlgavv pagpapaatr saptdstggp
      301 apqpsadpas agtsptarsq qdgqerntd
//
LOCUS       WP_010614482             294 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator, partial [Actinomyces
            oris].
ACCESSION   WP_010614482
VERSION     WP_010614482.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..>294
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          27..>294
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mtgrtvadva gsaasaadpg gllrayeaas myyvqgetme viahhlgvsr stvsrllara
       61 rqegvvrvsl vqpggagsle grmaqvfgvr thivpvregt teihrlqqva svaaahmvdl
      121 iealaesgrg rgvgaresgg pegdepagsg rdadagsvvv gvawgttmse vsaalpsrsv
      181 pgltvvqlng asdpvregps agevlsrmrl slgartisfp vpaffdhvat reamwsersv
      241 krvlsvvrra slavfgvgal dalngalpsq vyegghltar dqavlrrqnv vgdv
//
LOCUS       WP_010614506             509 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein, partial [Actinomyces oris].
ACCESSION   WP_010614506
VERSION     WP_010614506.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         <1..509
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
     Region          76..493
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 qagrrrqahw haplvgvvgh awkrhkkppn skegadllee psplpqlpgt eptgirrllr
       61 hieplgqiar aarfyparla vivfaaiivv vtgllslpia ttsgehadfl dalftatsav
      121 cvtglstvdt aaywstfghv viilaaavgg lgvmtlasll slavsrhvgl tqrmlaasen
      181 qsrlgevgrl lraviytatg cellltlmll ppflshgldv ghalwyavfm alsifnnagf
      241 vimpegleay stdwwiglpi ilgtfmgavg fpvildimgr rrrprtwslh tkltlttyla
      301 ltlastiaia tfewnnplty gslptsgkim talvngvnar ssglstippe hmheatwflq
      361 dalmfvgggs astaggikvt tfavlllail aeargdqdie afgrritpst vrlsvavafi
      421 gssiiglatl lllqmtnlsl drilfevisa fatvglstgi tpslpdgaky vivalmfvgr
      481 vgtmtaasal alrerrrvir mpeaspmig
//
LOCUS       WP_010614525             139 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Actinomyces oris].
ACCESSION   WP_010614525
VERSION     WP_010614525.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..139
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14358
     Region          30..137
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(35..36,69..70,73,77..78,81,128,132)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mvpvsrsgss dsavtyssdg qttvaslsgd vtfdvdssal tdrakqvlde ivkrwngkpp
       61 atvtvvghtd svaddahnqt lseqrakava dyltskvpsl nvqssgkges epvasetnad
      121 gsvneagkaa nrhvdvrwg
//
LOCUS       WP_010614551             277 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Actinomyces oris].
ACCESSION   WP_010614551
VERSION     WP_010614551.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..277
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29619
     Region          78..275
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtvpttatap tssslspgvr rfsearlvpd tltmawrsli tmmrnpgefy diliqpvmft
       61 vlfgelfgga iagdvkaylp tivpgliimn alttsqsvgv dlredmdkgv fdrfrtmpms
      121 riapvlgpmv sdvlrylict sltvltgyil gyrpangwsg aigaialaag cawaiawifl
      181 flgtvfssaq avtsftvivl fpltflsnam vptstlpgwl kafvhhnpvs hivdgdryll
      241 dgtagsagdv raaiigslli lavmapltvv ryqrrna
//
LOCUS       WP_010614713             134 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase, partial [Actinomyces oris].
ACCESSION   WP_010614713
VERSION     WP_010614713.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..>134
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          41..>133
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 msadktlsws ytedftaede ataqarirgl elgitpvssg tgaalrmlaa svgaksvaev
       61 gtgtgvsglw llggmgtdgv lttidvepel qrearrafdg agypssrtri iqgrasdvmp
      121 rmaarsydmv vldv
//
LOCUS       WP_010614652             416 aa            linear   BCT 01-JAN-2025
DEFINITION  MraY family glycosyltransferase [Actinomyces oris].
ACCESSION   WP_010614652
VERSION     WP_010614652.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..416
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43823
     Region          38..306
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            95..96
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            220..223
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133463"
     Site            order(282,296..299)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 mkvyllvmai aaattyvavp iirhialvgn altpvrardv hstpiprlgg vamffglfsa
       61 isvastipyl sdvidssawa vvlgaglvcl lgvvddlwel dwmtklagqi laagvmawqg
      121 vqlltfpvag ltigssrlsl istvivvvaa inavnfvdgl dglaagiigi gstafflyty
      181 vltratspgs ysslaativa aligvcvgfl phnfnpatif mgdsgamqlg lvsaastiiv
      241 tgqidpgsfd gsralpafmp illplavlll pltdmmmaiv rrtrkglspt hpdrmhmhhr
      301 llaaghshrr avlvmylwaa vasfpvaama ffplpwvlag lalavlfafv vtvdlmpgvr
      361 hglrsalrrr qdrpeqrivi srnvsgtgev trpaegqapq gnalqashgs pertrq
//
LOCUS       WP_010614744             207 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Actinomyces oris].
ACCESSION   WP_010614744
VERSION     WP_010614744.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..207
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20301
     Region          6..193
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 msvpsisiig agnigsavag lavkagvstq vvvrdaskat dlsgvdvaei gspltgdivv
       61 lalpyaaide viatygaqaf agkvvvdptn pldfttldsl vpagssasae laaklpdaqv
      121 vkafntvfaa vlasgtigar pgtvlaasds aeakaglrsf veaaglawad agelkraerm
      181 ealgalnial gvteqvawtg glavvse
//
LOCUS       WP_010614806             345 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Actinomyces oris].
ACCESSION   WP_010614806
VERSION     WP_010614806.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..345
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36387
     Region          55..299
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mssaetgark dsatlqadgp geatspspiv mmtsdgdssa avmtaaeghe agigtatvvv
       61 deigvsyrap stdaedlraa svaqkivmgm tghrpkvrve alknisfvar agesigilgr
      121 ngagkstllr vmggletpts gtvsarstpv llgvnaalvp dlsgernvrl gclamgltpq
      181 qieaiipevi elagigkaiy rpmktyssgm asrlrfaiaa aanpdillid ealstgdaaf
      241 kerseikmte lrraagtvfi vnhaaqviee mctralwlmd geligdgpgp qiahdyrwws
      301 wniaknkpdk aatilaecre kwkpagvriq rsesrtlpyr hargv
//
LOCUS       WP_010614821             533 aa            linear   BCT 01-JAN-2025
DEFINITION  GTPase domain-containing protein [Actinomyces oris].
ACCESSION   WP_010614821
VERSION     WP_010614821.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Wennerberg,K., Rossman,K.L. and Der,C.J.
  TITLE     The Ras superfamily at a glance
  JOURNAL   J Cell Sci 118 (Pt 5), 843-846 (2005)
   PUBMED   15731001
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Paduch,M., Jelen,F. and Otlewski,J.
  TITLE     Structure of small G proteins and their regulators
  JOURNAL   Acta Biochim Pol 48 (4), 829-850 (2001)
   PUBMED   11995995
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Fenwick,C., Na,S.Y., Voll,R.E., Zhong,H., Im,S.Y., Lee,J.W. and
            Ghosh,S.
  TITLE     A subclass of Ras proteins that regulate the degradation of IkappaB
  JOURNAL   Science 287 (5454), 869-873 (2000)
   PUBMED   10657303
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Valencia,A., Chardin,P., Wittinghofer,A. and Sander,C.
  TITLE     The ras protein family: evolutionary tree and role of conserved
            amino acids
  JOURNAL   Biochemistry 30 (19), 4637-4648 (1991)
   PUBMED   2029511
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Bourne,H.R., Sanders,D.A. and McCormick,F.
  TITLE     The GTPase superfamily: conserved structure and molecular mechanism
  JOURNAL   Nature 349 (6305), 117-127 (1991)
   PUBMED   1898771
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Bourne,H.R., Sanders,D.A. and McCormick,F.
  TITLE     The GTPase superfamily: a conserved switch for diverse cell
            functions
  JOURNAL   Nature 348 (6297), 125-132 (1990)
   PUBMED   2122258
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096372
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..533
                     /product="GTPase domain-containing protein"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=55764
     Region          <16..>111
                     /region_name="MnmE"
                     /note="tRNA U34 5-carboxymethylaminomethyl modifying
                     GTPase MnmE/TrmE [Translation, ribosomal structure and
                     biogenesis]; COG0486"
                     /db_xref="CDD:440253"
     Region          78..261
                     /region_name="Ras_like_GTPase"
                     /note="Rat sarcoma (Ras)-like superfamily of small
                     guanosine triphosphatases (GTPases); cd00882"
                     /db_xref="CDD:206648"
     Site            order(81,83..89)
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206648"
     Site            order(84..90,153,208..209,211,241..242,249)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206648"
     Site            110
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206648"
     Site            114..116
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206648"
     Site            150..153
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206648"
     Site            order(152..153,173..174)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206648"
     Site            208..211
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     Site            order(241..242,249)
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206648"
ORIGIN      
        1 mpapvpsrhs qddapvssls raqlldvlsd lvrdlerldl alsadgveaa rtlrdgligq
       61 vrdqvvprlq dadipsivvi ggstgagkst lvnsvlgqev svagvlrptt rtpvlvanpe
      121 dvdslsehpl tqvcrqevsa aipaglalid asdldsvhea nralagrlle aadlwlfvtt
      181 aarygdqtpw ttleeaarre tpigvvlnrv parilpevrr dlitrlqglg lseapffvvp
      241 dagpheglls gdgvselrdw lqllagrhra aglvrrtgrg vwstlradle rladdvdaqn
      301 avaeelertc qelrqtaiea lsadiragsa gqgatatrwi tlassggpla slaqggklrr
      361 gflgradkar aeglsqland arqalanqlq aaivalsaea rrawaevgae erahkilgqg
      421 ddavatieaw vgyleanies pqdirrlspg svidllisaa agvdgavsaa rrlgleeqta
      481 qagallveav tealtatvpk gaatslapap gfaaalrlrs gelkpftrpg ata
//
LOCUS       WP_010614823             240 aa            linear   BCT 01-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Actinomyces oris].
ACCESSION   WP_010614823
VERSION     WP_010614823.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..240
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=25347
     Region          8..113
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 mtrqldltvq gvvgtnpvls rvgdnarpyc rfrvavtpty rteqgwnnae tiwftakawg
       61 qlaanlshsl rkgdavlltg rfsqeswesn grkhetnvit lqaaghdltr gesrfarvra
      121 aesapsassg agtgdaelep ggedrvpsdh weveavasga saspapgpgd presaestel
      181 sestestept glgqssatha qspesfvidp acarsedqtg epwpvyelad dlveqavgvs
//
LOCUS       WP_010614827             438 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Actinomyces oris].
ACCESSION   WP_010614827
VERSION     WP_010614827.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..438
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45569
     Region          41..434
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          <292..435
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mlsrlflrrs rrraavcala aaslvffysg disladerdd avakqneaer kqqqvmssle
       61 gvsadlgqay islqnaqasl staetqltta ettlaakere qqiasdrlst aqssletvkk
      121 eseaskktae etsdsvaeiv vstyqgdnsv tswsyvlasq dveelsqras aveigsgvqe
      181 avlsaaever aqnanrearq naattrvstl kteadtaean aksardaakt krdevaklta
      241 qkksaaeale srksdlqsql nqanadaaaa aarvaqidaa nraaasagtm psvpassiga
      301 dslgsgyigh pitgplevts pfgyrvhpvt gvatghqgvd faasegtpqy aavsgvatyw
      361 dsescgigid inggiidghs yvitlchlss rsiadgqqvk rgdvvgatgs tgyatgahvh
      421 fqvaqdgayi dpmslpgf
//
LOCUS       WP_010614832             541 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Actinomyces oris].
ACCESSION   WP_010614832
VERSION     WP_010614832.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 541)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..541
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58018
     Region          76..525
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 maittpagss rrdfirltgt lgmaaglavs laacggkgka sggakasgma adqevthkdg
       61 vitagisyel gtngydpmtt ssaltvaanw htlegltelh patrevyaal aaempkkvdd
      121 ttyevalrkd akfsdgsavt addvvfsftr vldpanksly sqflpfidkv eakdagtvti
      181 klkyafslva erlsvvkivp kaiveadakk fdmsptgsgp ykmtdngags qkvvferndk
      241 yngprpalak smtwqilpdd ttrtnamsss svqaidavpa anlktlkdpv kvaaqqgfgl
      301 lfamfnhttf snakarqavl yaldyakicn tgmaglatpa tcfvqdghpa ykkaktvysk
      361 daakakslla eagittinll ctdhgwfsav rpiirenlea lgvtvkydek ksadtysfid
      421 sgqgtwdvli apgdpsvfgn dadllmrwwy ggdvwtetrm hwkgsesqva vqklleeavk
      481 legdkqvakw qeifdklsee vplypifhrk aptaydsttl enfkpialtg lsfvgtgssk
      541 s
//
LOCUS       WP_010614844             247 aa            linear   ENV 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [uncultured Actinomyces sp.].
ACCESSION   WP_010614844
VERSION     WP_010614844.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Actinomyces sp.
  ORGANISM  uncultured Actinomyces sp.
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces; environmental
            samples.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="uncultured Actinomyces sp."
                     /db_xref="taxon:249061"
                     /environmental_sample
     Protein         1..247
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26128
     Region          2..235
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mrglvkafdr kvavdrlsld ipvssfygiv gpngagktts lsmatgllrp dagqvlvhgv
       61 dvwtqpqrak tllgvlpdgl rtfdrlngle lvtysgllrg lerdvvvpra telvkvlglw
      121 dagttlvady sagmrkkihl acamvhspsi lvldepfeav dpisaqtiqa ilrdyaaagg
      181 tvvisshvma tvqrlcdhva iinagrvvaa gtteqvaaga dleqrftelv gghvrtegls
      241 wlrpsss
//
LOCUS       WP_010614901             165 aa            linear   BCT 01-JAN-2025
DEFINITION  regulatory protein RecX [Actinomyces oris].
ACCESSION   WP_010614901
VERSION     WP_010614901.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Ragone,S., Maman,J.D., Furnham,N. and Pellegrini,L.
  TITLE     Structural basis for inhibition of homologous recombination by the
            RecX protein
  JOURNAL   EMBO J 27 (16), 2259-2269 (2008)
   PUBMED   18650935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..165
                     /product="regulatory protein RecX"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /calculated_mol_wt=17968
     Region          13..162
                     /region_name="RecX"
                     /note="SOS response regulatory protein OraA/RecX,
                     interacts with RecA [Posttranslational modification,
                     protein turnover, chaperones]; COG2137"
                     /db_xref="CDD:441740"
ORIGIN      
        1 mpwlipdaht qaveaareiv lrrldrsaap raalaeller kevdprvase vldrleaagv
       61 iddtayaarl artrfaekga arraiaeelr rkglgesdva qaldqisaed edsaalalar
      121 kklsatghlp wevrrrrtaa vlgrkgysre vtmraiaaah aeese
//
LOCUS       WP_010614937             752 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase RecG [Actinomyces oris].
ACCESSION   WP_010614937
VERSION     WP_010614937.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Singleton,M.R., Scaife,S. and Wigley,D.B.
  TITLE     Structural analysis of DNA replication fork reversal by RecG
  JOURNAL   Cell 107 (1), 79-89 (2001)
   PUBMED   11595187
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..752
                     /product="ATP-dependent DNA helicase RecG"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=80639
     Region          5..744
                     /region_name="RecG"
                     /note="RecG-like helicase [Replication, recombination and
                     repair]; COG1200"
                     /db_xref="CDD:440813"
ORIGIN      
        1 mtrlvgkrta aqlakqgvet gadllrllpr rydtwgeltd mrtlvegeqa tiqaqvvras
       61 srrtrsgrvp almeatvtdg astmdlvqfg aagqmrtraa qlapgttvll sgkvglhrgr
      121 kqlsnprlyv ldeldegere allarpmpiy pgtealpswl vakavrsvld qlesgdvadp
      181 lpeelrreag lvdaytayrw vhrpedsgqw kaarkrlrhe ealilqvala qrrahheatr
      241 tavawpvpet egslradlda rlpydltagq krvgeeisad lartvpmqrl lqgdvgsgkt
      301 lvalramlqv vggggqaall aptevlaaqh hsslevvlgp marlgmlgga ehatrvhllt
      361 gstpaaqrrr iltelaagep aivvgthall sdtvqipflg lvvvdeqhrf gvaqrdalre
      421 rggltdpatg qshtphllvm tatpiprtia mtvfgdlats vldelpagrs avpthlvpws
      481 rtswvegiwr raakevasgg rvyvvcprie vddeprqtpm dgattvetdd gpkqealaee
      541 gdgshpdrpl aaveewrrrl egepalegig vgvltgrmss ddkaasmadf asgatpvlvs
      601 ttvievgvdv peasmmvild aerfglsqlh qlrgrvgrgs rpslcvavtg aevgstafhr
      661 lkafasttdg falaeadlel rsegdvlgas qsghasgldl lrvtrdarli atarrqaeri
      721 vaadpqlseh ralaaaiver ldeesqafle ra
//
LOCUS       WP_010614996             291 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Actinomyces oris].
ACCESSION   WP_010614996
VERSION     WP_010614996.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..291
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=30295
     Region          1..285
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mslavvtdsa acltepllre raievvplha ipadngeaat tsrpsvqelv dayrraasra
       61 eevlaihiss alsgtmdnar vaatqleaey rdqpngpgps agrrrpqwlr vvdsgtssga
      121 lglavlaasg ahdarrgaal aqastarscq lfvvddlgrl arsgridrtt arldgvlgir
      181 pvlaltrdgi rtletvrgaa rsrrhliaqa vrvaggtals gprhpadpvr lviqgddadk
      241 lalletdlrq ameeagakvs evltlpvdea tsthvgpgal giavapdlrt h
//
LOCUS       WP_010615064             155 aa            linear   BCT 01-JAN-2025
DEFINITION  NfeD family protein [Actinomyces oris].
ACCESSION   WP_010615064
VERSION     WP_010615064.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..155
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15759
     Region          3..138
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mewlfwvaga lllvvietmt adltflmiag galgggltsf lggpvwaqvv vfacvstlll
       61 favrpwakrr laaatpqmkt nvealigrsa vtitpvdreg grvrlggeew sarlaavgqg
      121 gtsrleagvs vtvaqidgav avvapvtast aapas
//
LOCUS       WP_010615070             552 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Actinomyces].
ACCESSION   WP_010615070
VERSION     WP_010615070.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces
  ORGANISM  Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Actinomyces"
                     /db_xref="taxon:1654"
     Protein         1..552
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59341
     Region          4..547
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 minvqdltmr igarqlvaha gfrvdkgmri glvgrngagk ttmtkllaaa svaqgagrav
       61 ndaderhgle avehegtitc tssvgylpqd tkvgdlseia rdrilsargi dallarirka
      121 eeriavtege aqakaldryt rldheftmag gyaaaseaar isaalglpdr ildqpigtls
      181 ggqrrrvels rvlfqqpdtl lldeptnhld hdsilwlrdh lrtyaggfiv ishdvellrd
      241 tvnqvmylda grgvldvyhl gwdaylkqra ddehrrrrer anaekkaaal raqgekmrak
      301 atkavaaqqm lkraerlmad ledeaavekv ahlrfpdpap cgktplrasg lskaygslev
      361 fagvdlaidr gsrvvvlgln gagkttllrl lggveepdsg evipghglki gyyaqeheti
      421 dtaasvvenl rraapgmddt qvrsvlgsfl fsgadadkpa rvlsggektr lalamlvvss
      481 anvllldept nnldpasree ilgalgtfag avvlvthdeg avealnpdrv lllpdgdedl
      541 wgpeylelva la
//
LOCUS       WP_010615129             189 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Actinomyces oris].
ACCESSION   WP_010615129
VERSION     WP_010615129.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..189
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20940
     Region          1..132
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrtskrdrii tgalelahrd gfdtltfdal aehvgltrgg viyhfrtkte llegiaaafq
       61 erwraealea lgrpldeasr teriealtrs vldgeilpge vsfmlsttsq aetikkawdv
      121 lrdewigevd eltamqrval lavdgwwanr avdsrsrnpd epaiaelivs laagnppdek
      181 lfkpsdkdq
//
LOCUS       WP_010615185             319 aa            linear   BCT 01-JAN-2025
DEFINITION  CAP domain-containing protein [Actinomyces oris].
ACCESSION   WP_010615185
VERSION     WP_010615185.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..319
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=32474
     Region          46..170
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
ORIGIN      
        1 mnikrviaaa altvvpltas saalaapvap egapaaaaav paqvtsegaq yantvlnkvn
       61 elrssmglqp vtryqeldav aqdwseqqaa annmshrpdf tsvypqgwtt gsenvawrts
      121 ggdtgalife qwrnspghyk nmtdpnvnsi gigfaptsdg kwyatqnfaa ynvsnstltp
      181 ttttttnttt tksntppstt dtpptgttvp sptptpettp stpttsttpp tpvapptaqt
      241 ttpsatptps apattvttet vtttgtpakp satpvvaapr ttptkpalat tgpsiavavv
      301 aagllgsgaf lvmrrrqas
//
LOCUS       WP_010615204             207 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Actinomyces oris].
ACCESSION   WP_010615204
VERSION     WP_010615204.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..207
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=22702
     Region          11..196
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mstiphsdhf ptavflgdsi ttgwralshp rnrwtslvce hqrwrevnla adglgffarr
       61 gghlpggqrs pscrdttwle avlrcepdiv tislglndaa flpsqrelve qaidhdlsfi
      121 strlrgapvi iapyfpslev gprfqairrl vhekatslgl tstdalstai ngdedrlaid
      181 qihpddagha rmaramisfy aeilpgs
//
LOCUS       WP_010614992             993 aa            linear   BCT 01-JAN-2025
DEFINITION  leucine--tRNA ligase [Actinomyces oris].
ACCESSION   WP_010614992
VERSION     WP_010614992.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   ALLEN,E.H., GLASSMAN,E. and SCHWEET,R.S.
  TITLE     Incorporation of amino acids into ribonucleic acid. I. The role of
            activating enzymes
  JOURNAL   J Biol Chem 235, 1061-1067 (1960)
   PUBMED   13792726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..993
                     /product="leucine--tRNA ligase"
                     /EC_number="6.1.1.4"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0004823 - leucine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006429 - leucyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=109595
     Region          15..991
                     /region_name="LeuS"
                     /note="Leucyl-tRNA synthetase [Translation, ribosomal
                     structure and biogenesis]; COG0495"
                     /db_xref="CDD:440261"
ORIGIN      
        1 msertapves dtpfrytael adsietawqd rweaegtfna dnpvgalagp gadkekffll
       61 dmfpypsgkg lhvghplgyi atdvvarftr mtgrnvlytm gydafglpae qyavttgqhp
      121 risteanian mrrqlrrlgl shdprrslat idvdyvrwtq wiflqvfnsw fdpeaprrdg
      181 rgkgaarpvt elrdklasgq vpvpdgrdwd alsaaeqaev idsfrlayvs sapvnwcpgl
      241 gtvlaneevt segrsergny pvfkrnlrqw mmritaygdr laedldtvdw pekvklmqrn
      301 wigrsegaev tfavpgagqg dqqdaslsvy ttrpdtlfga tfmvvapehp mlgglqasgs
      361 vrteaqiadd aaaltvpaaw pegtkdawtg gyatpaeava ayraqaaats dadrtdegra
      421 ktgvftgffg inpvngakvp vfvadyvlmg ygtgaimavp ahderdyafa tkydidiiqt
      481 igpaddphgv dlsaqaytgd gvvvnsaqgd ldingmgkde akatmigwle akgagrgavt
      541 yrlrdwlfsr qrywgepfpi vwdedggvha lpesmlpvel pevtdysprs ydpddadssp
      601 epplgkatew veveldlgdg prryyretnt mpqwagscwy emryidptdd kalvdpanea
      661 ywmgprpqag nisggtdlyv ggvehavlhl lyarfwhkvl fdlghvssse pyhrlfnqgy
      721 vqayaytdar gqyvpadeve evtaedgtts yqwqgqpvrr eygkmgkslk nivtpddmye
      781 aygadtfrvy emsmgpldad rpwdtravag sqrflqrlwr nvidettgel tvteqsadee
      841 trrlvaktiv gvredyegmr lntaiakliv lnnhltglge vpreavealv lmtapvaphi
      901 aeeiwkrlgh ehslahedfp vvtdeallaa ekvtcviqvk gkvrdrlevd pdiseaelek
      961 laleapgvir tldgrgvrkv ivrapklvsi vpe
//
LOCUS       WP_010615206             370 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Actinomyces oris].
ACCESSION   WP_010615206
VERSION     WP_010615206.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..370
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38740
     Region          141..369
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflalreirh epvrftliis vitlvayltf flaslavgla hryragidgw ntasvavtda
       61 snenlsasrl sdkqleaata lakdngttas almstaavaq apdvkdedge alredvfafg
      121 idldgqlspp vadgqtisap dsevlvddsl kskglavgdt irllgsdhdw tvvgfthdtt
      181 fqaapvvtmd sqalrqhgpt slspavsavv ftsdlttdsk atqsakdagl tiltteelvr
      241 tlpgysaqvl tfslmigsli iiastvlgif iyvltlqkrp vlgilkargv ptgylirsgc
      301 aqtlvlsvag igigllltma tslvlphavp frisapldll ivtafiaisv iggfisvrvi
      361 sridpveais
//
LOCUS       WP_010615384             176 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Actinomyces oris].
ACCESSION   WP_010615384
VERSION     WP_010615384.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..176
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19819
     Region          2..173
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkvklfiam svdgyiadkn ggvaflqghe dclenestys efiknidivl mgwntynqii
       61 telspdnwvy gnlltyvfth reqqdsdkii ftsdsleeli kklkgvegkd iwicggadlv
      121 qqaissdvid eylisiipti lgngiklfsq ndaehklkli ntitnngive lnyirr
//
LOCUS       WP_010615433             194 aa            linear   BCT 01-JAN-2025
DEFINITION  TlyA family RNA methyltransferase, partial [Actinomyces oris].
ACCESSION   WP_010615433
VERSION     WP_010615433.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         <1..194
                     /product="TlyA family RNA methyltransferase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          <1..162
                     /region_name="YqxC"
                     /note="Predicted rRNA methylase YqxC, contains S4 and FtsJ
                     domains [Translation, ribosomal structure and biogenesis];
                     COG1189"
                     /db_xref="CDD:440802"
ORIGIN      
        1 stggftdvll rrgaehvvav dvgygqlaws lrsdprvtal drtnirtldp evvapapelv
       61 vgdlsfislt lvlepllraa addadlllmv kpqfevgkdr vghggvvrdp elhvdtvmtv
      121 aerahalgvg veavtasplp gpagnveyfl smhasragcp gdlsgdelrs siedavaagp
      181 aaggtrrrrt rtrp
//
LOCUS       WP_010615443             259 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase, partial [Actinomyces oris].
ACCESSION   WP_010615443
VERSION     WP_010615443.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         <1..259
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          1..252
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 dgtildmdgh vservlasva rlrahevpvv istgrgiaaa mpvvrhlgls agwmvcanga
       61 mtlrldpdap ggyevvdsrt fdpraaietl haavpdgila vedpgvgfkv srlfpdgeli
      121 edqrvvtfde lvsqpvtrvv lrapgmpver fsqivadsgl hsveyaigwt awldvapegv
      181 tkasaleali arlgtdsahv lavgdgsndv emiewagagv vmgsapqwvr drgdiltepv
      241 wrdgcaavld aliervrhp
//
LOCUS       WP_010615446             201 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase, partial [Actinomyces oris].
ACCESSION   WP_010615446
VERSION     WP_010615446.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..>201
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
     Region          4..>201
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mtartirvld lfagagglta gfhtassrfr siaavemdpe aaasyratfp ktevyagaiq
       61 dwlaegkipt gvdvvvggpp cqgfstlgkr daedarnrlw eqyaqviqra rpkyfvvenv
      121 pafgkspqyr dflaatgpge fledysfdfr vlnaadygap qarrravlig hrydmavpgf
      181 pepthspdgg gdlppyrtvr q
//
LOCUS       WP_010615490             559 aa            linear   BCT 01-JAN-2025
DEFINITION  catalase, partial [Actinomyces oris].
ACCESSION   WP_010615490
VERSION     WP_010615490.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         1..>559
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          31..521
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mndtnlpetp qdgapagcpm sraglgehlp srnnaagqgr mtmangspvy nnqdsmtagp
       61 rgpvalqdaw llekhahfnr eviperrmha kgsgawgtft vtraipeltr aaifstegnq
      121 celfmrfstv agergaadae rdirgfamrf ftsegnwdvv gnntpvfffr dgkkfidlnh
      181 avkrdprtnl rspntnwdfw tslpesllqv titmsdrgip lsyrymhgfs shaysfinae
      241 gvrtwvkfhf rsqqglanlt dqeaatviae dresnqrdly esiekgqypr wtmyvqtmtv
      301 eqaealtdfn pfdltkmwpk adfpfqevgv lelnrnpdny fqdveqagft pqnivpgigy
      361 spdrmlqarl fsygdaqryr lgvnhhqipv nsprgvacph gfhrdgamrv dgnagsqnay
      421 epnsygnwqd srelsepvqa ggdvamydfr eddhnyytqp gmlwramtpe qqlvlcenta
      481 ramgdstlqi khrhifncyh adpdygrgva qalgididsv dldgatadsy elwlarnran
      541 aeldvptspa apasaanlg
//
LOCUS       WP_010615513             142 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Actinomyces oris].
ACCESSION   WP_010615513
VERSION     WP_010615513.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 142)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         <1..142
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          <1..136
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 awnaldelgv aeladrplgq lsggqrqlva laqtlvrepg lilldeptsa ldlrrqvsvl
       61 shvrrichrd tgrlavvalh dlnlaarfcd rlailaggti raegppaevl qpdilaevyg
      121 lrvrivpdgd hvmvapeaeq ga
//
LOCUS       WP_010615565              99 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein [Pantoea].
ACCESSION   WP_010615565
VERSION     WP_010615565.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..99
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10791
     Region          <32..>85
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 mpkledliaq rspesqarir nkaaekilei rlrqlreela lsqvqlaekm gvsqpaiaai
       61 eargdelkls slkkyvealg gklsvtvelp agdgrifql
//
LOCUS       WP_010618799             136 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Pantoea].
ACCESSION   WP_010618799
VERSION     WP_010618799.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..136
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14601
     Region          1..130
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mkkfedsgll larvlmtilf itagwgkita yagtaqymqa mgvpgfllpl villelgggl
       61 ailfgfltrf talftagftl ltaflfhsnf aegvnqlmfm knlsiaggfl vlglvgpgay
      121 sidrlirqrf mpatar
//
LOCUS       WP_010619009             166 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA thioesterase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619009
VERSION     WP_010619009.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..166
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18123
     Region          7..151
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 msakqltcne tfasashrif lsdlnehetv fggrilswvd dsasiscera srqvtvtasl
       61 dhinfihpvv lqdgldlqsy vtgaghrsle vfvkgvgehl ltgekflafs cfstfvtlsk
      121 spnpalpeiv pvtdeqkfic agydernaar kagravqkdl mdhlel
//
LOCUS       WP_010619178             179 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010619178
VERSION     WP_010619178.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..179
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20597
     Region          3..124
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msdkrtnqtq qliyeallty mqngasfqgl tvtdiaeaah isrqtfynhy anlesiilip
       61 vqgyvdnffe qfakapdfng erlvttlyqg wlghmdlfrl liwakldnef mtilrdfnir
      121 imqlshtski naplisstla gatfsflkft lideykkwpe keaistflti tnygrdlfn
//
LOCUS       WP_010619093             149 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010619093
VERSION     WP_010619093.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..149
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17309
     Region          3..115
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(51,54,58..59,68,86,90,96,100,103..104)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mtysikevse kvglsiytlr fydkqgllpf varnqvgyre ftdgdlniih ticclkdtgm
       61 kindireyvn dimagpttia hrqqllsehr aevltkqqki adnlreidyk lemyeaddsf
      121 eqvsreiqfa srekeqnhle npykitnks
//
LOCUS       WP_010619205              95 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010619205
VERSION     WP_010619205.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 95)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 95)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..95
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10573
     Region          <4..92
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 maykdalvyr vggeefnmll pnvdileadr varrlknkie ttpietnkgs invtaslgva
       61 tlnendktpn dfyeradqll yrskgqgrnq itsel
//
LOCUS       WP_010619224             189 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010619224
VERSION     WP_010619224.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..189
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20833
     Region          3..165
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mrpkligivg snadfsfnri llqymkrhfa etvdieiqei ngvplfcene mktppaivne
       61 madkiedadg viiaapeydh aipaalksvi ewlssarhpf ndqhvmivga sygiqgtvrs
      121 qmnlrqvldp pgvnanvlpg nefmlsnvkd kfnengeitd egtikfldsc mnnfltyski
      181 gndanavlh
//
LOCUS       WP_010619214             102 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin
            [Secundilactobacillus malefermentans].
ACCESSION   WP_010619214
VERSION     WP_010619214.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..102
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11896
     Region          4..102
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mriykvqisd ealqeiesta nyirvtvknp ilanrfrikv fqtisslsmn pnrftildak
       61 ydspktdklr kliidhyvav ywvdepsnsv hilafynqlq ny
//
LOCUS       WP_010619211             432 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619211
VERSION     WP_010619211.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 432)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..432
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49337
     Region          <212..421
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mfkqtrfimh eryqriliaa tcialasqvn fqtytpgfil tlsvfllpvf lyfnadlnpi
       61 qltlaialas pifrgillfi gqdasttkil qfiatdmvfy lsygiiyyll ywrrgqrnns
      121 sflltiiicd yvsnllevsl ltgfsnysyr lfqilfvaal vrslcsclla flyhyftlml
      181 rdenheqryy hfiwvassvk sevyfmqkni teienimkna yllnqdlqkl dvgqkqktma
      241 ldiardvhev kkdyqnvirg lgdsfsdeqn epmqladilk vttnyiresi ktkhqsvvid
      301 vhnhvdliip nhyyvvsvis nlifngvdal enipngkiri titddgsnvl idisdngsgm
      361 deqtlamifq pgfttkfnet tgnvyrgigl shvkiiveeq fgghisvese lkkgtvfhli
      421 lskqkllqev as
//
LOCUS       WP_010619262             449 aa            linear   BCT 01-JAN-2025
DEFINITION  SLC45 family MFS transporter [Secundilactobacillus malefermentans].
ACCESSION   WP_010619262
VERSION     WP_010619262.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..449
                     /product="SLC45 family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49017
     Region          16..433
                     /region_name="MFS_SLC45_SUC"
                     /note="Solute carrier family 45 and similar sugar
                     transporters of the Major Facilitator Superfamily of
                     transporters; cd17313"
                     /db_xref="CDD:340871"
     Site            order(26..27,30..31,34,66,131..132,134..136,139,159,
                     162..163,166,259,262..263,266..268,271,310,314,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340871"
ORIGIN      
        1 measndslpk lplltlfamt fgyfgvnmaf slqssqmgri fqtigadptk lgfffilppl
       61 agmvvqplig kysdktwnhf grrmpyliig apvaalvmvl lpnagsfgfg yasvaallfg
      121 aiailfmdls snvcmqpfkm vigdmvnedq kdlawswqqs fanlggvlat llpflltsig
      181 ianvapkgsv plsvklafyi gaalllgtai ytiasvheyd pdtyaeyhhl kkqpkkkses
      241 lwklllkapr sfweialvql fawfaiqylw tygtgaiaan vwntsnpasa gyqdagnwfg
      301 imtcveslaa viwgflvqsh tspthrkfwy rlglviggfg figvffvhsq llliipfsmi
      361 giaylamqtq pfsifteeln gqnegaylgl fncaiclpqi iaslcsffif pligksmpgm
      421 ifvggvvmli galsvgiihe nknvievki
//
LOCUS       WP_010619271             454 aa            linear   BCT 01-JAN-2025
DEFINITION  SLC45 family MFS transporter [Secundilactobacillus malefermentans].
ACCESSION   WP_010619271
VERSION     WP_010619271.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..454
                     /product="SLC45 family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48965
     Region          27..444
                     /region_name="MFS_SLC45_SUC"
                     /note="Solute carrier family 45 and similar sugar
                     transporters of the Major Facilitator Superfamily of
                     transporters; cd17313"
                     /db_xref="CDD:340871"
     Site            order(37..38,41..42,45,77,143..144,146..148,151,171,
                     174..175,178,271,274..275,278..280,283,322,326,374..375,
                     379,383,399,402..403,406..407,410)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340871"
ORIGIN      
        1 mendsaqgnt attpktkpmp klsiatiwmi sfgffgvqma fslqssqmgr ifqtlgadpt
       61 klgfffilpp laglvvqplv gyysdktwmp kigrrlpyll mgslvavivm fllpnsgslg
      121 fgygslaalw fgaitilfmd lssnvamqpf kmmvgdmvnd eqkgfaysiq sflsnsgsvl
      181 aaifpylltg lgvaniapkg vipnsvifsf ytgavilvic saftilrvke ytpaeynayh
      241 giteadvqek vglftllkra pkvfwtltlv qffcwmafqy lwtygagava knvwratdpa
      301 sagyqaganw fgvlsaiyal aavvwslvla kmpndkhkpm yatslvlgav gfasifvvhn
      361 qwvlilsfcl igiswaamtm fpftiltnal sganmgsylg lfngsiclpq ivasvlsfal
      421 fplmgssmpg mvllagilml vgafsvssik evfa
//
LOCUS       WP_010619285             320 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Secundilactobacillus malefermentans].
ACCESSION   WP_010619285
VERSION     WP_010619285.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..320
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34053
     Region          6..320
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mnnalwvyvq lngqkvepts lqlitkarqi aegrpvvall aedlttnaee tvkeygpdei
       61 ivlkddhftq ptdgeladal fqvvsantpn gllfpatvqg rsvaprlqak lrtgltadcl
      121 dvyydgedli qvkptygddi mceilcpdhr pqmatvrpnt fnaekvtgan vkittatftf
      181 hseanievvs ekpiisssan iadakivval grgadndkti alaekaaakl ggmvgvsrpl
      241 tdnpkfshes qigqsgntia pdllinlgvs gavqytvgie nagkvvsvnt ddkapifavs
      301 dfgyvgtane flealvndik
//
LOCUS       WP_010619327             143 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010619327
VERSION     WP_010619327.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..143
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15775
     Region          14..143
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 melivgnqkw nrgaalfirq svfvtergia redefdakdt detiyvvaye dashpaatar
       61 yekmdaetvr pgrvatlpay rhqglaakvl naleefarkq gltrslihge ldavgfyekm
      121 gyqvasapfe edgapvvtlt kql
//
LOCUS       WP_010619343             279 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619343
VERSION     WP_010619343.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..279
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31041
     Region          12..268
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mskltetyel sngvkipkig fgtwqvpngq vaydavteal sqgyrhidta wqygneesvg
       61 rairdsglnr edvfvtskla aaaksydaam ktfdetmdri gldyldlyli hapwpwdemg
      121 adystqniev wqamediykt gkvraigisn fnvadqknil khatimpmvn qiqyyigyte
      181 pditvyaqdh nmlveafspl atgyllnnea vkdiaahydv svaqlairyv lqhgllplpk
      241 atnsahienn kqvefeisva dmavldklkd tapgedhng
//
LOCUS       WP_010619354             343 aa            linear   BCT 01-JAN-2025
DEFINITION  lipoate--protein ligase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619354
VERSION     WP_010619354.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000589
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..343
                     /product="lipoate--protein ligase"
                     /calculated_mol_wt=38392
     Region          3..255
                     /region_name="LplA"
                     /note="Lipoate-protein ligase A [Coenzyme transport and
                     metabolism]; COG0095"
                     /db_xref="CDD:439865"
     Region          257..341
                     /region_name="Lip_prot_lig_C"
                     /note="Bacterial lipoate protein ligase C-terminus;
                     pfam10437"
                     /db_xref="CDD:431286"
ORIGIN      
        1 mflidtsrng kpvydpivnq sldnylindl klpghglimy indpavivgv nqnvfaevnv
       61 pylienkikl vrrssgggav yhdrgnlife nivvgetddn akwgdygvfa qpvldalhel
      121 gasqavlrgk sdlvindhkf tgmtmvkagd gyaaggtlmf dmnidaasna lhpveekihg
      181 kwvksnrshi tnvkpflaad yqkltpeefr eqlllklfkv dsldqietyh lnekdwqiid
      241 erlaekynqd nwnfgsnpgf sqyrrqafdd kaivfnfate nnqiskmavy gdvlsrkhad
      301 klqdlltgvs ldetaitrai dkrfvkhaig engpdqlakl ilq
//
LOCUS       WP_010619381             173 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Secundilactobacillus malefermentans].
ACCESSION   WP_010619381
VERSION     WP_010619381.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..173
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19050
     Region          14..161
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mqislnqltl pnfklwigvs krglvfvgap ngakdeinnf ydpatidtte isnldvfkkw
       61 fvsyfagrks amppidrtig tdfqkrvwrt leqvtygttv sygelaekmg qktaaravah
      121 avshnpvmyl vpchrviksd gkigqysagp elkaallkme sqggelewps ttp
//
LOCUS       WP_010619401             643 aa            linear   BCT 01-JAN-2025
DEFINITION  M13 family metallopeptidase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619401
VERSION     WP_010619401.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..643
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72788
     Region          16..643
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mtqtnndqln tsllkddfyd ainggwiena eipadhsstg gfmdladnie kilmtdfakl
       61 rdgkmapenp qmaefkkfyq mtsnferrdk agaaplkpyl qriedltsya dlnaqlvdwi
      121 itglplpfdi dvdsdmknst iyalfaggpr lflpdktyye dgneaakklm plfsemtesl
      181 lrmadypead ahqiveqakd fdrqiaphvk saeesadysk mynpkdidtf gkytdkldlv
      241 aavkelvnge pkqiilpepa yfealssllt ddnfekiksw mlvktvdgla sylsedfrqt
      301 gsqygralsg rkearskeka ayylasgiyd qvvgdyyghk yfgekakqdv hdmvvkmvnv
      361 yknrlqnndw lsastrekav lkldklgiqv gypdkidsly dkfkvtepad ggtllgnimt
      421 ftqiqtkdqf skwnkpvdrt rwemsantvn ayyhpfhnii vfpaailqap fysleqsssq
      481 nfggigavia heishafdnn gslfdefgnm nnwwtdedhe hfkglaenmv nefegipfsg
      541 qkvngrltvs eniadaggls caleaaksed dvdleaffin wgtiwrmkat teymqlllsi
      601 dvhapaklra nvqvqnlddf fktfnvtend qmykkpvdrv kiw
//
LOCUS       WP_010619408             144 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Secundilactobacillus malefermentans].
ACCESSION   WP_010619408
VERSION     WP_010619408.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15164
     Region          1..140
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myekllvpld gsenasaals eaidlakhfs stlvlvsvan dqsytqygai fgqdiiehmr
       61 edaekilsaa etkvksagvn vethfvvgip kqaiadslpe tygttltvig ksgvhglnra
      121 imgsttayvi shsstnvmvv nepn
//
LOCUS       WP_010619443             334 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010619443
VERSION     WP_010619443.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..334
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37057
     Region          7..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maaterydit iigggpagmf agfysglrta ktqlieslse lggqvqalyp ekeildvagf
       61 ptikgsqlia qqnnqfkdfp idifknqtvt dikreadgfe ivtpqritht keillaigng
      121 aftprklave nidsfegkqv fysvsdlehf rnhevliagg gdsaidqalm leplakhvtl
      181 vhrrdqfrgl eymveklrns svtiktpflv kdieqtptkq lnislkrvkt edqfeqllvd
      241 dvivsygfis dnkavagwhv qfdedhrmlk vdskmqtsep gifaigdgvl ypgkqqliat
      301 aygeaptain ammqqiypdk rgpvhstslk ikkd
//
LOCUS       WP_010619447             160 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619447
VERSION     WP_010619447.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..160
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=17214
     Region          <44..156
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkkiilhsiv laslvalfii gfggksaqad ttdstdsstt yssiykvaks klgssyswga
       61 vgpnrfdcsg ftsyvykkgi gktisrtaqa qynkythvsy snikkgdlvf fgyskssish
      121 vglyvgdgkm idaqnrgvvk eavkapwwha vgyarvttls
//
LOCUS       WP_010619476             188 aa            linear   BCT 01-JAN-2025
DEFINITION  guanylate kinase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619476
VERSION     WP_010619476.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..188
                     /product="guanylate kinase"
                     /EC_number="2.7.4.8"
                     /GO_function="GO:0004385 - guanylate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006163 - purine nucleotide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21413
     Region          2..184
                     /region_name="Gmk"
                     /note="Guanylate kinase [Nucleotide transport and
                     metabolism]; COG0194"
                     /db_xref="CDD:439964"
ORIGIN      
        1 mrdriivitg atgsgkttvg kylkdkyaip kvithttrvp rpgeqnevdy yfesdetfnq
       61 rhflesvkyd ghrygssyea lergwekspl lsvvldtkga vtyseklgee aviifltvsk
      121 dnalqqrike rgddpnaidh rlesdeyqrd malpkelqgi ahvivndkld ktklmldeii
      181 kelrndln
//
LOCUS       WP_010619507             242 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619507
VERSION     WP_010619507.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..242
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25938
     Region          5..235
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mekltgkval itgassgfgr gtamafaeag cnlvltarre eklqqvveac kqfgvdaiyf
       61 agdaqleeta ieavklainh fgkidilinn agigrtlslt etsmadydli mnsnvrsaya
      121 ftkyavpeml krkdgqiilt ssvtgikghp detaytcskf alrgfgqald kellgkgirt
      181 cvfcphagat efevgygrtp eevaesgflt pedvgqalls vctqpkhsri velrlasnnv
      241 ty
//
LOCUS       WP_010619516             848 aa            linear   BCT 01-JAN-2025
DEFINITION  M1 family metallopeptidase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619516
VERSION     WP_010619516.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Evnouchidou,I., Koumantou,D., Nugue,M. and Saveanu,L.
  TITLE     M1-aminopeptidase family - beyond antigen-trimming activities
  JOURNAL   Curr Opin Immunol 83, 102337 (2023)
   PUBMED   37216842
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Peer,W.A.
  TITLE     The role of multifunctional M1 metallopeptidases in cell cycle
            progression
  JOURNAL   Ann Bot 107 (7), 1171-1181 (2011)
   PUBMED   21258033
REFERENCE   3  (residues 1 to 848)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   4  (residues 1 to 848)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..848
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=95035
     Region          14..437
                     /region_name="M1_APN-Q_like"
                     /note="Peptidase M1 aminopeptidase N catalytic domain
                     family which includes aminopeptidase N (APN),
                     aminopeptidase Q (APQ), tricorn interacting factor F3, and
                     endoplasmic reticulum aminopeptidase 1 (ERAP1); cd09601"
                     /db_xref="CDD:341064"
     Site            order(119,121,253..256,289..290,293,312,316,370,376)
                     /site_type="active"
                     /db_xref="CDD:341064"
     Region          508..823
                     /region_name="ERAP1_C"
                     /note="ERAP1-like C-terminal domain; pfam11838"
                     /db_xref="CDD:463368"
ORIGIN      
        1 madtthfyql fepehynvyl dinretkkit gkttiageak aekisihqky mniesiladg
       61 qkvafttdds adairidlgk tgnvtftidy tapltdsmmg iypsyyevng ekkqligtqf
      121 ettfarqafp sidepeakat fdlaikfdek pgetiianmp evrqeagvhy fdttvkmsty
      181 lvafafgdmq skltttksgv kvgvfgtkah dakeldfald iakrsiefye dfyqtpyplp
      241 hswqlalpdf sagamenwgl vtyreaylll dpdntaldtk qlvatviahe lahqwfgdlv
      301 tmkwwddlwl nesfanmmey vaidaiepdw hvwemfqtsd vpaalqrdat dgvqsvhvkv
      361 enpaeidslf dsaivyakga rmlvmvrall gddalraglk kyfelhqygn atgadlwsal
      421 gtasdldvga imnswleqpg ypvvsasvvd gqltlsqqqf fvgegqdtgr qwqiplngny
      481 detptimtek tiklgnyedl rqsngkpfrl nvgnnshfiv kydetllkdi faysemldai
      541 sqlqllqdfr llaesgkisy asvvpiltrf anhpssvvna alyqvagnlk kfvtpgsdee
      601 tqlqalfnkl strqvtrlgw tpkagesndd qltrpyvlna alyakneeav asahklftan
      661 kaslatlpad irvfvlrnev knfgndqlfd qlvadyrqtp dasykadira altsttddnq
      721 iakivdnyen adlikpqdlr awyrgvland kgqqaawdwi rndwqwledt vggdmefatf
      781 itvttavfht perlaefkaf fepklntpgl treikmdikt iesrvalvek ekaavneavk
      841 kivstcnk
//
LOCUS       WP_010619005             444 aa            linear   BCT 01-JAN-2025
DEFINITION  C1 family peptidase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619005
VERSION     WP_010619005.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Nagler,D.K. and Menard,R.
  TITLE     Family C1 cysteine proteases: biological diversity or redundancy?
  JOURNAL   Biol Chem 384 (6), 837-843 (2003)
   PUBMED   12887050
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of cysteine peptidases
  JOURNAL   Methods Enzymol 244, 461-486 (1994)
   PUBMED   7845226
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..444
                     /product="C1 family peptidase"
                     /EC_number="3.4.22.-"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=50776
     Region          11..443
                     /region_name="Peptidase_C1B"
                     /note="Peptidase C1B subfamily (MEROPS database
                     nomenclature); composed of eukaryotic bleomycin hydrolases
                     (BH) and bacterial aminopeptidases C (pepC). The proteins
                     of this subfamily contain a large insert relative to the
                     C1A peptidase (papain) subfamily. BH is...; cd00585"
                     /db_xref="CDD:238328"
     Site            order(48,55,57..59,168..169,233,235,237,243,384)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238328"
     Site            order(70,76,368,389)
                     /site_type="active"
                     /db_xref="CDD:238328"
ORIGIN      
        1 msekllnrtp lsdekraalh edlhkrpeaa visravmkng ikqasedtaa ltrlhrtfsv
       61 eletgrvtnq rhsgrcwefa tlntlrhamg akykvkdfel sqnylffwdk veranifydn
      121 ilntaelpad dravaaflar pgedggqwdm aaslvqkygv vpdyvmpeta ntndsssfge
      181 aldlklrkda mvlrqlvhdg kdeteiaaqr qeflsevyrm aaysfgeppv sfdleyrdde
      241 kkyhrdenlt pqafydkyfd infddyvvls napdrdfnkl yrlpsqeniv ggrpirllnv
      301 tldkmkkati dqlqdgetvw fgndvleqmn rseglldsql yreselfdvd lsmtkaqrle
      361 ygqanvsham tftgvnlvng vpnrwkvens wgekngdkgy fvmadswmnd yvyevvvnkk
      421 yldaetlavl dqeptilpsw dsla
//
LOCUS       WP_010619539             367 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Secundilactobacillus malefermentans].
ACCESSION   WP_010619539
VERSION     WP_010619539.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..367
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39596
     Region          128..367
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mylawkemry aklryaliig vmvlvayvvf mltgladgla dgnkqavvdw kassvilsnd
       61 snkiasassm kqsdlkrvsv sdknkagvgy fptavqhqkk sekqnvsvlg akkssfvvpn
      121 vtkgrlyqnk heiiisqnla nlgyhlnqkv klgsdsklyk ivgfskatkf sevpviylnl
      181 nafatlkygd qvfknngekp lsliaikkqs ankltvsqss ddtkldklsv ntfiqnipgy
      241 saqnvtlgam igflfvvvaa iigifmyvmt lqktslfgvm kaqgiktsyl aksivgqali
      301 vgvvgvaiaf vlgyltgfgl petmpystdl gqwlldgivl ilvaiigglf sirtvtkvdp
      361 inaigge
//
LOCUS       WP_010619561             232 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010619561
VERSION     WP_010619561.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 232)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 232)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..232
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25373
     Region          7..232
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mnseltfkag vkdvvptlfg yigvgiafgi ightshlsil miafmsfwvy agsaqfiian
       61 milvhdpisa iaistflvns rmilmattla qyfrkdsiln nigigilttd etfalamnkl
      121 nrtkqhltar wqhaanllay liwilativg awigslissp ekfgldfalv amfiglvylq
      181 litdktkgfr tqllvmlfvv iclyfsmavm saniavlfst ilgcafgmvi dk
//
LOCUS       WP_010619623             244 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619623
VERSION     WP_010619623.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..244
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=26809
     Region          27..240
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mmhhisklkl siiailsvlf fmvsmtvkad aattevsess mtatayvrrs stgwmydlsv
       61 kdkqvtfgak thylsnypnt twmvtkkmyv kksdgvtyly yyvtnvsgsv hgwiwhgylk
      121 agasyetlyg vakaqlgkpy syggngpsaf dcsgltsyvf kkamnktlvr taqsqyntyq
      181 hvsssnikkg dlvffgssks svthtgiyig sgkmldaqnn gvitekiaap wwnlvgyarp
      241 atis
//
LOCUS       WP_010619660             438 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619660
VERSION     WP_010619660.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..438
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49417
     Region          10..343
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mleqfkeqfe krgyekptai qeavfepmsq hksvlglapt gsgktvafil pilgevvpgd
       61 gsqililsps qelamqttsv irdwaksydv kvlaltggan vkrqmeqlrk rpeiiigtpg
      121 rvlnlvedrk lklhlmqtii ideaddllag etletvrntv eqapadvqlg ffsatetpil
      181 helpkwfgqe vetfdvrlid dtqgqvahdl lqispkkrve slkklstmen fralvffnqm
      241 stlkyvvsrf rhehvafael tsdarqvqre kalkdfrlgr vklllttdva argldipklp
      301 avvnfdlpst pntyvhragr tgrmgepglv vsmgddhdlr dfrhqmaksd yeykrvyffk
      361 kalveripdq pkarveastt nststptgre thkgaerakr epyssakvve tpikkkghkk
      421 hqknkgmrkk rreqsdkv
//
LOCUS       WP_010619673             381 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Secundilactobacillus malefermentans].
ACCESSION   WP_010619673
VERSION     WP_010619673.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..381
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42035
     Region          12..373
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mtlysrikns pmmfwsleil ivvaviwact kisflfapig tffqvvfipi llagilyyll
       61 spvvrlleki kirgkhisht wsvtvvflvl lavlilglvw llprliqqva nmisnipala
      121 sttqdlvekm anqpwlknvd lsqymnevek sassyassfl nkltesigtv istitsfavv
      181 aitvpvmlfy mlkdghkflp sikkiiptrh adqtidllsk msktiskyig gqiieclfvg
      241 tftaigyvlv gqgyalllgv fagicniipy vgpyigilpa livafgdstl qilyvvivvl
      301 vvqqvdgnvv ypniigktlk ihpltiivil laagniaglm gmilaiplya vvkvmvqyfy
      361 niwqlqsesr ksepekpkek a
//
LOCUS       WP_010619682             886 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010619682
VERSION     WP_010619682.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 886)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 886)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 886)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 886)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..886
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..886
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95326
     Region          7..875
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mkmtntqlpi eeivqnystn qtsglndaev vrrqeengkn vlteakkpni fqqigrhisd
       61 iaslvllfav vlsiylaltt dsgwtkpivi gsilvlnvmi gmyqehsaeq alsalkklsv
      121 hevqvlrngq kimldatelv vgdvillepg sqvpadarli tasnlsidea iltgeslpvd
      181 kiseplreep eeigdyqniv fsgtavtqgn atavvteigm qtelgsiagm lnqtkvkqtp
      241 lqnrlnrlvs slsgvaiagg iiifllgmfl hgdplasslm igvslavaav petlpiivti
      301 slahgvkkma krnaimrrvs avetignvnv iasdktgtlt qnkmtitklw vneggltavn
      361 evdvlddhqa kllkmfglat naqitkdend laleigdste laivrllhkf gmsrnslend
      421 sprlaedpfd stkktmatlq klpnnkslli vkgafdrlpi nrdtaeyaea lknhdafgre
      481 alrvlavgyk vfdgvptesi enlqdevdll glvgmidppr eeviaaisea hgagiktvmi
      541 tgdhletaka iakkigilna gdsvltgtel rklsdeqlmd qiegttvfar vspedkiriv
      601 tawqeqgavv amtgdgvnda palkaanvgi amgitgtevs kgaadmvltd dnfativaav
      661 segrtvyqni lkavefligv nfaqlflmif svaigwgapl iaeqlllinv ladgipgfyl
      721 srepgeksvm kqkpitqlts ifanglgtrv airavtftil tlsiyafgrf gmsnggaaig
      781 mtmlflvlal gsmidiyaik treslrvasf ksnptlnmgm tiavvlvlav ailpplqnlf
      841 elvslppmaw livvvtmfip tivleinkrl qnrnrvdney qaited
//
LOCUS       WP_010619703             252 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010619703
VERSION     WP_010619703.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..252
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28497
     Region          10..249
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mdqqylktge ridqlysrdv kiiqsnnvfs fsldavllah fanvpqkass tivdlcagng
       61 avglfmasht pshiyeveiq drladmatrs vslnrlddqm tilnmdlakv tskikkdsva
      121 vvtcnppyfa nyenskknpn kyyaiarhel ettltavmka tsdllkmngk syfvyrpdrl
      181 ddlfremalh rlapkrirfv hpkanseanm vlveaikdgk pngvriqkpi ivynseneye
      241 kevrgmlygr ed
//
LOCUS       WP_010619748             147 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010619748
VERSION     WP_010619748.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..147
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16166
     Region          1..146
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mglqdqltad lkvamkardk mslnvirsik taltndrvkl ehdlteeeet avvsremkqr
       61 keslvefena grddlseplk eeikivakya peqmsqdeve kivkqaisdt gassmgdfgk
      121 vmgkvmgqvk gkadgnvvnq tvksllk
//
LOCUS       WP_010619779              91 aa            linear   BCT 01-JAN-2025
DEFINITION  HU family DNA-binding protein [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010619779
VERSION     WP_010619779.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..91
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9390
     Region          3..91
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mankaqlvnd vasatgltkk dataavdavf gsvqatlakg ekvqligfgn fevreraark
       61 grnpqtgqei qipaskvpaf kpgkalkdav k
//
LOCUS       WP_010619871             247 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Secundilactobacillus malefermentans].
ACCESSION   WP_010619871
VERSION     WP_010619871.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..247
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26069
     Region          1..245
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mtvknkvivi tgassgigea sakllasnga kvvlgarres rlqeidndik ldggqatylk
       61 tdvtkpeevq alvdlaksef ggidvifnna gimpsspisa lhikewnqmi dinlkgvlng
      121 vaavmpdfvt qkggqivtts svagiksfag agvygatkfa vrnlmevirm esaqegtnir
      181 taslypaain tellgtitdd atktgmedfy kqvgftpdav arvvnfavnq padvnvneft
      241 iyptkqa
//
LOCUS       WP_010619872             442 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A
            [Secundilactobacillus malefermentans].
ACCESSION   WP_010619872
VERSION     WP_010619872.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..442
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=49315
     Region          1..441
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mkqgslfntd dtqnsplanr vrpltldefa gqqsligagk vlreiidsdq lpsiifwgpp
       61 gvgkttlaei iatqtkanfv tfsavtsgin dirkimkaae enrdlgeqti vfvdeihrfn
      121 kaqqdaflpf vergsitlig attenpsfei naallsrckv fvlhslapqe ilavlknaik
      181 hpkgfpnlei kisdetlmti ahfangdarv alntlemavl nanqqdksvt iseddlgqli
      241 ntrslrydkh geehyniisa lhksmrnsdv naaiywlsrm ldggedplyi arrlvrfase
      301 digvadtsal eltinvfqac qflgmpecdv hlteavvyls lapksnsvyl arenakddvk
      361 ktgnepvplq irnaptklmk dldygkdyiy ahstddklts mktmppeleg heyyfpseqg
      421 hedrfkkrla fiqkwhqqhd ae
//
LOCUS       WP_010619976             107 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Secundilactobacillus malefermentans].
ACCESSION   WP_010619976
VERSION     WP_010619976.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..107
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12061
     Region          10..103
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(30,33)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mealakmtsd elskkiskgk ymlffsatwc sdcsfikpsm peiekeytey hflavdrden
       61 idlaadlsvf gipsfiafdd gkevgrfvnk drktkkqvee fidglas
//
LOCUS       WP_010620025             218 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620025
VERSION     WP_010620025.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..218
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=24706
     Region          33..212
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(115,122,138..140,183,189,193)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mqsnslttew kvsgirwlfa iislllfcii avavskhqyw isvfdswiin hvrapefnsy
       61 kqlgifvtkt gnqtpagilt faivviasif knyryatfll vnvlllgglg nsiikeivkr
      121 prpdenpflh ltsysfpsgh sitamltfgt lillirhlir skkiqiplif vlciwiliig
      181 msriyvgvhy psdvlagfll gyffltlsqt ffygikwk
//
LOCUS       WP_010620084             148 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620084
VERSION     WP_010620084.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..148
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16512
     Region          1..132
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdktdviimn elqknarcsl keleakcfit spaiairinr lekngiikky qaivdlpkld
       61 yhvkafirlq ldpnlepdfy qfvshsahvl qcdcvtgdys qllqvafsnt galdsfvnev
      121 skfgktstqi vfstsvdnrg pkisseni
//
LOCUS       WP_010620125             170 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA (cytidine(34)-2'-O)-methyltransferase [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620125
VERSION     WP_010620125.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..170
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=19445
     Region          3..159
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 mtnhivlfep lmpantgnia rtcagtdtvl dlikplgfsl ddkhmkragl dywekvqint
       61 hknlpefmnq lpsngklflv skfanqtyvd pdytdsnsey yflfgkettg lpepfmrqyp
      121 ekairipqdd sniralnlsn saaiviyeam rqqnfnhleq shlykndklk
//
LOCUS       WP_010620127             386 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Secundilactobacillus malefermentans].
ACCESSION   WP_010620127
VERSION     WP_010620127.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..386
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43338
     Region          43..372
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mtnkegakhs wfynwvvnnr lvssltvill illilfvlsk vqwlfypikt lfgiigtpii
       61 iagvfyylln pivdrvenrf kikrvwsisa ifivvlgliv wgivaiipii qqqimsllan
      121 wpdywnkvve estkfsnsph fdsfrdqldn fnkqaseqys kamssffnqt lnsvggfvsr
      181 vttiavsiit apfilfyllk dghklpaylv hffptkarks isevikemns qvsnyvrgql
      241 ivafcvgvmf ligywiiglk falllaisag vlnlvpyigs flalvpalvv gafisplmli
      301 kviivfgieq tlegrfispl vlgnslkihp vtiifvllas gklfgvlgvi lgipgyavir
      361 vfvtqiflwy krysglylee idsesh
//
LOCUS       WP_010620152             276 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Secundilactobacillus malefermentans].
ACCESSION   WP_010620152
VERSION     WP_010620152.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..276
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30128
     Region          1..272
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkkwiaglt sivavslllv gcgkssstke ttitvgasni phseilkhvq pelkkegvnl
       61 kikvfqdyvl pnkdlankdl danyfqhipf lknwnkqnng tlvsagnvhl epigayskky
      121 kslkaipsgs tilvsnnvad ygrvltilrd aglvtlksgt dittatfkdi kdnkknlkfk
      181 tdlepklmpq fynnkegaav finanyavqa gldptkdsia leknsspyvn ivavrkgdtk
      241 kpaikklmka lqskgtqqwi tkkykgavvp aypngk
//
LOCUS       WP_010620169             154 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620169
VERSION     WP_010620169.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..154
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17249
     Region          24..111
                     /region_name="HTH_GlnR-like"
                     /note="Helix-Turn-Helix DNA binding domain of GlnR-like
                     transcription regulators; cd01105"
                     /db_xref="CDD:133380"
     Site            order(25..27,41,59..61)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133380"
     Site            order(73,76,80..81,90,93,97,103,107,110..111)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133380"
ORIGIN      
        1 mndindndfi rrvksilkhs gfslgigdia natgvsqrkl ryweekeyiq pssgseegkh
       61 rkysyftlak vsliesyles gytlvkavek aeqhskvaqa trkiisdrls gikrvddqye
      121 vdlgevegae skhivailke dsptrliltn vygn
//
LOCUS       WP_010620172             107 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF1048 domain-containing protein [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620172
VERSION     WP_010620172.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..107
                     /product="DUF1048 domain-containing protein"
                     /calculated_mol_wt=12347
     Region          8..100
                     /region_name="GINS"
                     /note="DNA-binding ferritin-like protein (Dps family)
                     [Replication, recombination and repair]; COG4817"
                     /db_xref="CDD:443845"
ORIGIN      
        1 mfnkfkqqkr eyrdykaris alpndyqatm kalekyfwnw akgdgmmail isvlemfena
       61 vadgspvefv vgediaefad ailadnpeet wlnkqrnqlr tsyknrg
//
LOCUS       WP_010620174             252 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Secundilactobacillus malefermentans].
ACCESSION   WP_010620174
VERSION     WP_010620174.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..252
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27412
     Region          57..218
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtylsdtftl agrlikhnlr svdtiitvii mpvmmlllmv flfggaiqid glshaeyvny
       61 vlpgillmti atgsaytalr inmdktsgmf drfkslpisk savlngqsva svifmmtstl
      121 vvlgvgflvg frshallvdw llvllillgs avaitwisvp falmassidg asafsyiilf
      181 llfvssafvp vtgmpkfirv faenqpmthi iqsirgllss qpignhgwia liwilaiiil
      241 frflgtliak rv
//
LOCUS       WP_010620211             183 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Secundilactobacillus malefermentans].
ACCESSION   WP_010620211
VERSION     WP_010620211.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..183
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19274
     Region          <22..73
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          125..181
                     /region_name="Lyz-like"
                     /note="lysozyme-like domains; cl00222"
                     /db_xref="CDD:469668"
ORIGIN      
        1 mkklvtsiia ttaaalglfi agttsasadt tytvkagdsv waisqkydtt inhlekinsi
       61 enhmihpgek lsidgkatak ktttakttts stktttssss tsytgsnlks yvlsqmesrt
      121 gvssstwnti itresnwqpt vrnsssgayg lfqnmhissg svetqvdaav alynaqgmsa
      181 wal
//
LOCUS       WP_010620168             500 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Secundilactobacillus malefermentans].
ACCESSION   WP_010620168
VERSION     WP_010620168.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..500
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53610
     Region          21..475
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,146,
                     149..150,153,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 mnqaidtngk sysrtwlvvl llvgtfctvl nqtilttafp tlmksfdvtt stvqwlttgf
       61 mlvngimipi sawltsrlns kvlyesamii fligtitcym apnfgvlltg rliqalgvgv
      121 tmpllqtlml sifpaasrgt amglaglvig vapaigptls gwvidnyqwr dlfgmiipiv
      181 aiviiagfwl mksvlptkks vldwlsaals tigfgsllyg fsevgtkgwd dpivitglvv
      241 gvifillfgw rqltmkepfl dlrvlknref svsallssvs mmamvgveml lplylqivrg
      301 dsafesgltl lpgalmmgvl spftgrifdr igakrlaitg mflllagtip fafitkttpv
      361 pylitlyavr magiamammp tttagmnalp lrmmsngtav nntlrqvass vgtailisis
      421 tnvsksntpg ksllksdpls yksgifngil dgyhaafwaa ilfcivgfiv affisgrspr
      481 smkvsvdega dksttargea
//
LOCUS       WP_010620237             436 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Secundilactobacillus malefermentans].
ACCESSION   WP_010620237
VERSION     WP_010620237.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..436
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46474
     Region          25..435
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 meskqngtsa dnmsflevlk hkdilrteii agitgffais yiiivnpmil kdagipadls
       61 vfatifssii gclimgfyan spviltpgmg vnafftytvv vnmglswqta vaisavsgvi
      121 ymaiaftkmn dilsksipqs lkhgitagig lflveiglek aglivagkts livlgdltkp
      181 aallaifgla islilylrrv kgsffigiil ttivgvifhi rdadtpnvil skltnyhqit
      241 fkgdfshils tpfilatfsm tmilvfesmg lvqgllpdqr kfkktfqgss vttflssflg
      301 tsptvaaaes asgiesggrt gwmavtaavm fglslifipl layvpqaaia pviiitgalm
      361 mesiggikig dftewfpafl iivlipltns istglafgfv cypilklagg qrrqltlpvy
      421 ilgvlflldl ifsall
//
LOCUS       WP_010620274             351 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620274
VERSION     WP_010620274.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..351
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38830
     Region          2..340
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mqvtlkgiql aydrhnkifd qlsfhvqdge llallgpsgs gkstilnlia glltpnagqi
       61 lfdetdvtkl darnrnigmv fqdyalypql nvmdniafpl kmahvkkatr reqaqklakl
      121 vhieslltkf pnelsggqqq rvaiaralak kpkillldep lsnldaglrv elrdeirhiq
      181 qvtgvttifv thdqndalri adkiivlang viqqvstgad lyrhprnlfv aqfigspkin
      241 tipvanlipy iskeipasil tqavtaafrs esitndpvan almtnlpvtm thqvqigrds
      301 qtqlqfennr listaisdny tqkiqtinva prgfflfndd dvciwegdah d
//
LOCUS       WP_010620354             288 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Secundilactobacillus malefermentans].
ACCESSION   WP_010620354
VERSION     WP_010620354.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..288
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32620
     Region          12..271
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mhndipqvpl angttipqlg lgvfqvtdpn evkdaikwal aagyrhidta tyyqneeavg
       61 eaikesgisr hdlfvtsklw nnvrgyeetk qafqtsldkl gldylnlyli hwpadgyves
      121 wkaledlykd gkikaigvsn feqnhlenlm sqteikpmvd qiethpffqq kelhaylekn
      181 giqheswspl gggrnnalsh plikrlaenh dvtpaqiilr whvqrdevii pksvhqerie
      241 qnrdifafgl dedemqsiad idagkrvgad pqdkewlaks ttyggpkk
//
LOCUS       WP_010620365             489 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Secundilactobacillus malefermentans].
ACCESSION   WP_010620365
VERSION     WP_010620365.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..489
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53181
     Region          28..482
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,153,
                     156..157,160,284,287..288,291..293,296,324,328,380..381,
                     385,389,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 mtnrpttadq pvdqngrpyn rlalvftllv gtfstfitst mlttafptlm ksfnisattv
       61 qwlttgfmlm mgivipitgf flqrfdtkrl ylsaiviffi gsilcyfats fwgilvgrlv
      121 qaagvgitap vyqtimtsif ppskrgaamg taglvvglap aigptfagwi lmhyswrmlf
      181 laimpvsllv lvmgfftlrk vlptkkapvd wmsvvmsvig fgsmlfgfss vgdhswtspi
      241 vyvtlivgvi vvalfilrsl kiknpllqfk vfessdytls ailvsvsfma mneftlvlpl
      301 ylqtihgesa fasgltllpg aitigimnpi tgrifdqlga rnmaiagmfl ltlttgsfip
      361 vtpttpvfyl vclytvrmfs ismvmmpvtt tgmnalplnl igdgtvvnnt arqmfasmgt
      421 ailvsimase ttkhlpsqgv ahatpilfgk lslhanvvgf rwaffiatlf slvgfvltff
      481 lkrdsrrlg
//
LOCUS       WP_010620407             125 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin
            [Secundilactobacillus malefermentans].
ACCESSION   WP_010620407
VERSION     WP_010620407.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..125
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=14444
     Region          9..117
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mtgtkenyip eqldiiyinf dptkgreikk rrpalvmsst vynrrtgfvv vcpitsthrd
       61 lpmyvelhsh kihgqvnaiq lrsldylksn rqiefvesap iqdfertaki ikdifnfddl
      121 isnfs
//
LOCUS       WP_010620415             148 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Secundilactobacillus malefermentans].
ACCESSION   WP_010620415
VERSION     WP_010620415.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..148
                     /product="VOC family protein"
                     /calculated_mol_wt=16556
     Region          7..143
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(7..12,27,66..67,85..90,92,101,132,142)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 msntsalypy ltfdntkaal ayyqavfgae dverlpvtka aaeamhipss vnyedltmha
       61 vftilgnwvy ssdnfnhddq ltnstrllid vdsgdaemlk kaealyhsfe tddsvtilmp
      121 ladqgwgakm gmvtdkynvt wmlqirkw
//
LOCUS       WP_010620441             173 aa            linear   BCT 01-JAN-2025
DEFINITION  shikimate kinase [Secundilactobacillus malefermentans].
ACCESSION   WP_010620441
VERSION     WP_010620441.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..173
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=18716
     Region          3..164
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 mslilvgfmg agkttigqqi splihlpqqd lddliikkag kpipqifdev geagfrqlet
       61 qvlestidda avistgggvi mqtinrhllq galapvvylk tsfetilari qnddnrplat
      121 nitamarlfn qrqslyeeva divvdtdaks pafisteimn qlasvselrh sam
//
LOCUS       WP_010620449             408 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Secundilactobacillus malefermentans].
ACCESSION   WP_010620449
VERSION     WP_010620449.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..408
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45188
     Region          16..396
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(24..25,28..29,32,64,119..120,122..124,127,147,
                     150..151,154,230,233..234,237..239,242,266,270,323..324,
                     328,332,348,351..352,355..356,359)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 metapqstnw ksnvgyflaa qnfflfgsss vyfailwyia lkassgtwim latmattlpq
       61 ilislwagiw adqynrrkli ilsssfvtif tiglallyff evrslwllll iaairslgsg
      121 vqtpagnall peitpkvels rmnglnqfis smlllispil sglilgklgi mfvfvvdlvt
      181 attgiilmal vrlhnqdrkv vghsavlpgi wdgikytfsr qylrnfmlft vvafalveps
      241 sqlstlfvkr tfgsavwrlt lnellwtiga llgslyitah kklpnkirli tigfigsgis
      301 favmgipepf wvyllfmffs gicmpiiqas sniliqenvp ndrlgrvfsi lqilstgiyp
      361 iamllygpla dqiaikyili atglilivvg fmfykrlsgl adkldelk
//
LOCUS       WP_010620609             361 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620609
VERSION     WP_010620609.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..361
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40338
     Region          7..242
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 maeeykikvq nitkeydlfk tqseklksff alnrkevphf wslmgvsltv kagetlglig
       61 vngsgkstls niisgiipqt tgtvdvkgdt siiaigaglr gnltglenir lkalmqgltn
      121 peidalmddi vsfadigdfl yqpvksyssg mksrlgfsia vhvnpdilii dealsvgddt
      181 fyqkcldkin efkaekktiv fvshslkqve mmcdrvawih ygtlhqiget devvgdyrkf
      241 tkwfkgltkk ekqqfqlkmk qdqknfdvea fqneitearq kaepdnphva sdvkrdlygs
      301 visekmskpn iiltwavlil vlffcavnvs ghslteiikn pirivqptht lhvpdqvnqi
      361 k
//
LOCUS       WP_010620627             285 aa            linear   BCT 01-JAN-2025
DEFINITION  GRP family sugar transporter [Secundilactobacillus malefermentans].
ACCESSION   WP_010620627
VERSION     WP_010620627.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..285
                     /product="GRP family sugar transporter"
                     /calculated_mol_wt=29906
     Region          1..282
                     /region_name="GlcU"
                     /note="Glucose uptake protein GlcU [Carbohydrate transport
                     and metabolism]; COG4975"
                     /db_xref="CDD:444000"
ORIGIN      
        1 mttlialipa lawgsiglis gkmggspsqq tlgmtigavi fgvlslvifq ptlttkvwvi
       61 gflsgifwff gqlgqfqsmk aigisktvpm stglqlagna lagvvifhew ktgamitsgt
      121 iaviiliiga tltalrdtkt naitkkseni gagafalafs tvgyvlytvi vtwgsvdska
      181 ivfpqsigml lgalvyslnk dpwnkgtykn iltgvvwgvg nffmflsipa vglaisysis
      241 qmgivistfg sifllgekkt sremvyvtig silvivggvi lssmr
//
LOCUS       WP_010620659             126 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620659
VERSION     WP_010620659.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..126
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14595
     Region          3..117
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mqfdfnfssn eplylqvakq ieeaifmngf segdqvpstt eisrqfhinp atvlkgmnil
       61 vseeiiekhr glgmfvkkna qerirmkrqn effddyvsgm vveaqklklt ekqliemier
      121 gyekne
//
LOCUS       WP_010620660             286 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620660
VERSION     WP_010620660.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..286
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31669
     Region          4..220
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mssieiknvt kqfgkkevla glnfklepnk iygllgrnga gkstllsimt nripltsgtv
       61 tvdgesiqnn dkilqkmylm sevslynsrl rvfqvfnetd kmygkfdfdl anrlagefgl
      121 dlnarigkls tgyrtifkvl vamgvsaeyi fldeptlgld anhrdlfyke lmesyanrpr
      181 tfvisthlie evanlvehvl iikngkilid sgvdetlaka htvtgpeadv dsytaglnvi
      241 ghdslgkika nyvfgdmddk ilpdtvsies mdlqklfinl tnegen
//
LOCUS       WP_010620667             157 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Secundilactobacillus malefermentans].
ACCESSION   WP_010620667
VERSION     WP_010620667.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..157
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17232
     Region          5..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlqqyknilv pvdgsyeael afkkavavan rndaslhlvh vvdtrafqni ssfdttmveq
       61 vtdtakktld kyieeakang idnvdysiey gapksiiand ipkyldidli migatglnav
      121 erlligsvte yvtrtaicdv lvvrtdlenk pakkpee
//
LOCUS       WP_010620705             451 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Secundilactobacillus malefermentans].
ACCESSION   WP_010620705
VERSION     WP_010620705.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..451
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51068
     Region          1..386
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfnefnlqp flveaieelg fteptavqkr lipviksgks vvgksqtgsg kthtfllpif
       61 dkidpeldev qslittpsre layqiyeaak qlashsekpi rvvnyvggtd karqqsklhh
      121 eqpqivigtp grlldlvkgg dldihtsrsf vvdeadmtld mgflsvvdqi asrlpnklqm
      181 mvfsatipqk lqpflkkyms npvmeeipvt svisptidnw listkgqnkn diiynlltmg
      241 epylalifan tksrvkeitk flkqnglkva miegdlppre rkrvmrevqn ldyqfvvatd
      301 lasrgididg vshvindgip edldffihrv grtgrkgmag iaitlytpde eskiteiesm
      361 gikfqpkaiq ngevvdsydr nrrkqrshgh eeldgalkak inktkkkvkp gykkkikkei
      421 nkdllfkrrl eqrqkgrter krkkqdsnry q
//
LOCUS       WP_010620719             293 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620719
VERSION     WP_010620719.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..293
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32580
     Region          54..287
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mkleflefhl lssslqhlws kfiehydwek llntvtsrlf qfillsilfl iirwvgkaii
       61 qkafnkyrds klatvsanrt dtihslvlni ftyiilffwi yalltlmgvp vgtliagagi
      121 fslalglgaq gfvsdivtgf filleqqldv gdavkinaie gtvtaiglrt tqitsydgtl
      181 nfipnrniqi vsnlsrnamr alieikvnpn tpidditkii kevneqltpk fpeitkgpty
      241 lgtsisadgh lalqvivytt pgeqftvqra flsaylrair eagislptiy pgk
//
LOCUS       WP_010620776             454 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Secundilactobacillus malefermentans].
ACCESSION   WP_010620776
VERSION     WP_010620776.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..454
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52696
     Region          11..422
                     /region_name="YdhJ"
                     /note="HD superfamily phosphohydrolase [General function
                     prediction only]; COG1078"
                     /db_xref="CDD:440696"
ORIGIN      
        1 msyqdeilpr ekvfrdpvhn yiyvqyqvil dlintsefqr lrrikqlgtt sltfhgaeht
       61 rfghclgvye itrricdnfq rnyptkvpgd glwddserlv alcaallhdi ghgpyshtfe
      121 hifhtnheai tvaiitspmt qvnqvlrrvs pdfpqkvasv iqktypnkqv vqmissqida
      181 drmdyllrda yntgtkygtf dltrilrvmr pysggitfei dgmhavedyi msrfqmyvqi
      241 yfhpvsrsme vildhllqra keiytpdnqq dtalsptlll pffngefdlk dylllddgtm
      301 ttyfaqwrgs hdtvlsdlaa rfldrkplks aefdekskdl iprlrdliqk agfdttyyta
      361 indsydlpyd aydphlkkpr tqielmqkdg slvelstiss lvsaitgkfs gdqryffpre
      421 mllpsssele lfepiyrefn ryilndhiiq pken
//
LOCUS       WP_010620778             466 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Secundilactobacillus malefermentans].
ACCESSION   WP_010620778
VERSION     WP_010620778.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..466
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50150
     Region          22..466
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mssggigryf kkesldryll kdaqlektmd gkdlvmlgvg avigtgifil pgtvaalysg
       61 pgivlsfila tivcafaamc yaefsssipv agsaysygni vfgevigwil gwalileyml
      121 avaavstgws ayflsflrgf gisipkaltg pfdpahgtyf nlfaivivlf vsfiiskgak
      181 tsiavnnmiv iikiliiflf iivglfyvrp snwspflpyg thgvlkgasl vfyaylgfdv
      241 vsasaaevkn pkknmpfgii gtliictily iavagvltgm tsytklnvsd pvsfalqlvh
      301 qnwaagiisi galagmftmm vsmifsssrl iysigrdgll pkalgkiekk hrtpqvslaa
      361 vtiviaimgg lvsldrltql vnigtliaft fisigiiplr krkdidntgg fkvpfypvlp
      421 ivsaglcifm lsqlpldtwi vssiwflfgl viyftygsrh stlnkk
//
LOCUS       WP_010620790             259 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Secundilactobacillus malefermentans].
ACCESSION   WP_010620790
VERSION     WP_010620790.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..259
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29220
     Region          3..255
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mqifdshthl nsdefyddvp tflahakelg vekianvgsn tilnsraiel aneydnlyai
       61 vgwhpedskn ytpetekvle eqlsqekvva vgeigldyhw dsspvdvqkk vfarqieiak
      121 efhlpisvhn rdafadcydi lkaaniseig gvmhsfngds ewlkkfldlg mnisysgvas
      181 fknahevhds vratpldrml vetdapyltp epfrgkqnep gftrytveai akerettpee
      241 iaaatwhnah qlfrleesk
//
LOCUS       WP_010620834             247 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620834
VERSION     WP_010620834.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..247
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26937
     Region          8..235
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mvtdyviakq vskhfghqqv lnqidltlpa gmiygligps gagkttliks ilgmeavdsg
       61 tvkvmdtvmp nravmaqigy maqsdalyet ltarenltlf gqlmsvpkik laqmidyaag
      121 lvdltsqldk rvsgysggmk rrlslaiali qdpqllilde ptvgidpelr qqiwtelnki
      181 kdtgksmlvt thvmdeaerc dylmlirhgi alaegtpaal kqqyavdtie qvflkagrmq
      241 dandgnr
//
LOCUS       WP_010620836             223 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Lactobacillaceae].
ACCESSION   WP_010620836
VERSION     WP_010620836.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillaceae
  ORGANISM  Lactobacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Lactobacillaceae"
                     /db_xref="taxon:33958"
     Protein         1..223
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25123
     Region          23..>145
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 merprirdyf qqdlsqneti tpkqrailqa sldlfaekgf dqtstsdiaq ragvaegtvy
       61 rryktkaalr dailapitah ivpilasdfs edelrqryps lqafvtaift drvafakanv
      121 kelkvifema afdterreqi lsqiapkmvk pmgsvinqlk adhlivdwpn dlilqsllsq
      181 lfgylaqlml elpgteiere qaylitvmtk iltpgehdqi tgq
//
LOCUS       WP_010620898             169 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein, partial [Secundilactobacillus malefermentans].
ACCESSION   WP_010620898
VERSION     WP_010620898.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         <1..>169
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          <18..165
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 ekylnetfad dytqdtylak llsplkekyd yiildvppql nkftdsalva sdfviiilqt
       61 qersltgaet yaehlinlkd dyklgldllg vlpvlqqngn nldldvldda idsfgkanmf
      121 kqrirqmarl krfdrtgitd rskdindirv msvyenvvne ikeritkfn
//
LOCUS       WP_010620924             245 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Paucilactobacillus
            suebicus].
ACCESSION   WP_010620924
VERSION     WP_010620924.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..245
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27631
     Region          5..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 maeklltvsh lvknygrqev lhdinftvek gsvtvllgps gsgksttirc lngledfhsg
       61 eiqfkdqvik pgfkkwqsvr qdigmvfqsy dlfpnrtvid nillgplkvq krskdealaq
      121 arhllkevql sdyenayprq lsggqkqria ivralalnpe fmlfdevtas ldpemvrgvl
      181 evieglarqk mtmlvvthem nfakqiadkv lflengkive esagheffdh pktqraqefl
      241 nsmdf
//
LOCUS       WP_010620946             450 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Paucilactobacillus suebicus].
ACCESSION   WP_010620946
VERSION     WP_010620946.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..450
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47726
     Region          3..436
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mkqpevelkr slglwsalal vvgtvigsgi ffkqasvlds agssttalla wvvgglitlt
       61 agltiaeiga qlpytgglyv ymekiygriw gflsgwmqii vygpaiiasl agylavllvs
      121 ffglsnawhv slalaamili gglnmfenry gaafaiittc ckllpvaaii ifglfyghqg
      181 algqtvagah asagnfgvav latlfaydgw ilianlggei knpqkilpka ivmgllfvlv
      241 vysvvsfgvf kglpaalihk lgdnttpyla tqafgtiggr llnigviisi igcmngkimt
      301 fprimyamak rndlpfskkl syvnpkthep mvatvviiai aslmvgffna dylsdlcift
      361 vycfyvaafi gvfllrkrmp gprpfstplf pltpiiaivg alfviiself sdpvgacasl
      421 givaiglpif yvvkkhaaae dmdalnqsvk
//
LOCUS       WP_010620955             369 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010620955
VERSION     WP_010620955.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..369
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=41647
     Region          73..338
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 meqetrqqry nhrppkqnrg iilfiiiivl fgvikiayst ysslnntvqn sykganiknr
       61 rnvskliknk kpisilllgt dtgsldrsyk grtdtimlvt vnpkekktsl fsiprdtmva
      121 ipgyendfpe kinsvytytn isdtvntisk ymnvpidfya lvnmgglekl vnevggvtik
      181 spltftfsnd tahetgkhry kfykgsstfk yakdgvhfkt yhkmngqaal afsrmrymdp
      241 egdygrtkrq rmvitailkq saspkmlfnk afmksissnv rtnltfkqmm siaasyyqak
      301 nnvstksate ntvmhngvsy qvfsksekqk atnqlrsdle lshaktgpil agdkskvtvp
      361 ydieevldq
//
LOCUS       WP_010620961             312 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Paucilactobacillus suebicus].
ACCESSION   WP_010620961
VERSION     WP_010620961.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..312
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34356
     Region          4..311
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mdiflhavsg vfvilgmivv gyflsragwf dehsktliak lvtqlalpcy mlstimsdft
       61 tkelkallpd lkfpiismsv lfvvavivsr ilkikqnhrg lfesmffisn tvfvglavnv
      121 alfgerslpy vlvyymantt ffwtlgvyli grdggktghl dvrqtlkqif sppllgfmla
      181 vvlvlfhvkl ptflmsdfry iggltiplsm ifigiavqsa gishvkfnrd nlgvlfgrfl
      241 lapalmsllv ipssmpilmk qvfilqsamp amtnapvvak lygadsdyaa imvaettils
      301 livipvlmli mn
//
LOCUS       WP_010621005             178 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paucilactobacillus
            suebicus].
ACCESSION   WP_010621005
VERSION     WP_010621005.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..178
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20438
     Region          2..123
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdkrivktqr klwtalftil atknidditv telcsmadit rrtfyrtfsn vpavfdsysd
       61 ylneqarqtl saqyadvnel lsafdrlvte nytglrlift dqrhlrlvdn fvdafyqslc
      121 qvvlnnqhnv hnrlvmkyva sgilgmmaew fksmpevkyg elakvvkpmv ksamgmlt
//
LOCUS       WP_010621017             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Paucilactobacillus suebicus].
ACCESSION   WP_010621017
VERSION     WP_010621017.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..269
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29979
     Region          11..198
                     /region_name="YycJ-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Bacillus
                     subtilis YycJ and related proteins; MBL-fold metallo
                     hydrolase domain; cd07733"
                     /db_xref="CDD:293819"
     Site            order(63,65,67..68,128..129,150,198)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293819"
ORIGIN      
        1 mqtiddqlhy silasgstgn vtyletpehk ilidaglsgk kiqglmekig rsltdvdalf
       61 vthehtdhik gvgvlarkyg mnvyanhgtw damsskigkv pveqqhilep gktlsmgdmd
      121 vesfavshda aepqfyqvhh dgktfcdltd tgyvsdrveq tikdadayli ecnhdmemlr
      181 mgpyawplkq rilgdeghls nedgantmms vignqtkqif lghrsqennm rslahltvtt
      241 mmeqhdfgvd hdfhlhdtep daptklytl
//
LOCUS       WP_010621042             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Paucilactobacillus
            suebicus].
ACCESSION   WP_010621042
VERSION     WP_010621042.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..144
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16104
     Region          22..108
                     /region_name="HTH_GlnR-like"
                     /note="Helix-Turn-Helix DNA binding domain of GlnR-like
                     transcription regulators; cd01105"
                     /db_xref="CDD:133380"
     Site            order(24..26,40,56..58)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133380"
     Site            order(70,73,77..78,87,90,94,100,104,107..108)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133380"
ORIGIN      
        1 mdnlteelqk vkeillnrna ilvsmtdisk itgvsarqlr yweqkgyies vhdqsenrky
       61 nitamvkigm iknfidegft vakasekaqe adqittalhr vdsekfnqas vndtglefdl
      121 gsvagldegk klflnvptdk dsff
//
LOCUS       WP_010621031             473 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Paucilactobacillus suebicus].
ACCESSION   WP_010621031
VERSION     WP_010621031.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..473
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51931
     Region          19..466
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mdtnskaqan gqttisnipf ttkdkvgymf gdignnftfa tvtsflmify tnvlgisaai
       61 vgilflvari idafadltvg rlvdngplle egrfrpwirr mkypllllsi llflpwikdl
      121 pmgvktvyif ltyivwgily stvnipygsm asaissspse ktslstfrsi gaglggatvs
      181 llvpmfmysk gshqisamrm fiivaicata gfvayiilyr lsvervrtnk aekvplstvv
      241 kklgqdkali alalvdllmc iglfsnnafi pylfndyfqn ktamsialic gtivililap
      301 fskklyerfg rkevtvafls fgfvmfailf flhtrnvvlf livtflanlg lgmfnmmvwa
      361 fitdvidneq vqtgiredgv vygvnsfvrk vsqaiaggma gfiltfigyq asttggavqs
      421 etvinhiyqv avgvpavsyg lalaclfffy plnkkkvldn aaylkkvane qae
//
LOCUS       WP_010621064             315 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Paucilactobacillus suebicus].
ACCESSION   WP_010621064
VERSION     WP_010621064.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..315
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35562
     Region          49..311
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mttyknqqaw rdvqnflpkk yhftnsyhpt eeswnwkgng vhldtfrnpk akakiilfhg
       61 vgtngrqism iiggplaldg yetitvdmpt ygvtdvnpns iisyddwiqc gsdlidaela
      121 kddrpiflyg lsaggmetyh vaarnkkvkg iigmtfldqr skdvqmtttn nwfwgtfgip
      181 mtkmatnmgl sgfkmkmsip skmsalvndp dclkvlfkdk tsagnkvsmk fmntymtytp
      241 diepenfdvc pvlltqpedd rwtpqwlsdp fldkitkvpv trtvlrngsh ypieataldd
      301 lhkyilgflk dnlkg
//
LOCUS       WP_010621068             228 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Paucilactobacillus suebicus].
ACCESSION   WP_010621068
VERSION     WP_010621068.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..228
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25184
     Region          6..195
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mteptigivg agklgstlar lgiqaqlpil igsrhkvedl kwvidtlapg titlttdevi
       61 eradviilai plghyldldp vklagkivld asnywvevdg thnnisdfkr sssevvqdhl
      121 nnslvakafn hmgyhdleie vdrhpdvrra mayatdhdei rptvehvita fgfdplflgp
      181 lryglllepg splfgeaipr defqdkinti ydspygqkii tergekik
//
LOCUS       WP_010621073             433 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Paucilactobacillus suebicus].
ACCESSION   WP_010621073
VERSION     WP_010621073.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46634
     Region          8..407
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtndslgtkw takqflviag iwfaflisfi trlswstimp saidslhftv qqgntyltaf
       61 yigyaitvlp ggmladkfgy rkllmaavlg nfivmaamif mhgywdglal rfilglvsgp
      121 dlsaclgiit ewfdgkkrat atgifntcts fgltviniya ptvlvhygwr aafgvtamfp
      181 laalifcyfa lkgnppfpqq fgikeangnv atesvwsrlg gaisnrsvwm laitglfatg
      241 akwgvtnwan lfmvknlhfs litagtamsi ygitsvismv vagwisdhsk wsrhtwaaif
      301 maiftptiig falvpkgnlg llyfwtgamg vgafmfstit nnlsvevapa dqrgtvsgfi
      361 nvfnqsgsfl apillgalla gtgsyvtsfl visvfpliav valmfvresd adkgakkvvv
      421 ndeeadtvak gel
//
LOCUS       WP_010621099             252 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621099
VERSION     WP_010621099.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..252
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=28449
     Region          2..>118
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mkivalyggq dangmtatlv kdildgakda ecefinlndy rivpdqphqi npvmdelesk
       61 laaadvwvlg tptyfgtvag qfkqffdyfr hrmvkmthkg dtlpgkykdk hyvsvtscfa
      121 spwdntfthq tdatltmidk amtaaglhkv kelvlpgtwn lhgklpdakr dtaralgtkl
      181 ttkkrkddet lkryillfcm iavmalatmg iqalfpiltt nfwmryasfv iiffvllaci
      241 lhyatfvrht rr
//
LOCUS       WP_010621112             296 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Paucilactobacillus suebicus].
ACCESSION   WP_010621112
VERSION     WP_010621112.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..296
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33369
     Region          13..273
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mtelqipkik fndgleipqv glgvfqmddf eetkqsvlna lkvgyrhidt asfydneeav
       61 gaalaetdvp reqifvttkl wsnvrgydnv kaqfktslkk lgldyldlyl ihwpapgyee
      121 vwrafedlhd egliksigvs nftdaqldnl lkgaritpvi dqiethpylq qdnmhqylad
      181 hnivheawsp lgggsnnvls ndkvneiaek ygksaaqvvl rwhlqrgevi ipksthleqi
      241 eqnidlfdfa ltdddmatik tlnknlrvgp vpddpawlke smkfgnqaeq aalhdn
//
LOCUS       WP_010621142             370 aa            linear   BCT 01-JAN-2025
DEFINITION  CapA family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621142
VERSION     WP_010621142.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..370
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=40394
     Region          53..362
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 miglrskrfk allgvtaval igvtlagcss sgskkstdks snttssktts srartvhltf
       61 mgddtlgtdp nlnsatslpt vwaqhgdnph yffqnvqkyf ksddltianl ettfattaqm
      121 apkagnvvfh fkgnpklanv lkvsgidavt vsnnhiydyg kqgfkqtika veaagvgyfg
      181 egykyvktvk gvkfgflgyt gwtatasdka kiardikslr kqgcqvvipy fhwgierqak
      241 pnatqvtlah yainhgadmv igshphviet melykgklia ysmgnfcfgg npnpvdkrsf
      301 llqtnltvkn kkitnstfrv iptristtda qndyvptpyt gsekqavlky mnqlsptfkg
      361 riadrfnkie
//
LOCUS       WP_010621164             401 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Paucilactobacillus suebicus].
ACCESSION   WP_010621164
VERSION     WP_010621164.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..401
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=44512
     Region          1..377
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mkevvilgag yaglralkel qrhrtdchvt lidkhdyhye atdlhevatg mqhrsrisyd
       61 indvvdrert tfvqetvdkv dcenqkvict ngkevtydyl ivalgfeset fgtpgvdeya
      121 lsmtnvddae kiyhhiceqm qlykqtqded flkivvcgag ftgvelmgal veakpeyaki
      181 advnpaqiei ycveastrll pmfneklasy gidhlkewgv klytgmrvke ikpnlvmyra
      241 gdddpmkeis artiiwttgv rgskviaasg fsekrgrvmv kddlsapdhd nvyivgdvaa
      301 vmdtstqrpy pttaqislkm ghhaakniir qiagqstepf sfkslgsvas ignthafglv
      361 gttpikgypa sfvkkaimdk slletggvke tmskgrfdfy h
//
LOCUS       WP_010621174             857 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paucilactobacillus suebicus].
ACCESSION   WP_010621174
VERSION     WP_010621174.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 857)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 857)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 857)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11905783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..857
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94718
     Region          6..855
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
     Region          613..855
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mkpltknlwr girgsmgrfi aiiliimlgv ltyvgvkatg palkdsvnqt vtnlhlsdvq
       61 imsttgftkq dvktaekvag akaeavkfky vtggkdsyai alygyqhnlt enklslrsgh
      121 lpknnhqivl dyrahskysy klgqkikfdk saelkhrtyt vvgfvdspsy vdntergsan
      181 vgdgsvkffa evpasqmnls aatllnvrfs klqsrdtysh sykeavsakv kslkkvfktr
      241 gaersktlyn knageltasq dkltaaknql mamgmtskqa taqlkseqsq ldtakakikk
      301 atkttytwqt rsdlpgftal gqsadriaai anvfpvfffl vaalitftti trmveearaq
      361 igtfkalgys kmaiarnyls yafiagmigt iigafvgnis lprlvlslyq ncipliavdk
      421 fqwslfvisi iialittvga aaivvrselk ekpselmrpr spksakrilm erikplwrrm
      481 nfnqkvsyrn lfryksrmfm tilgiaggta liltgfgiqn sigasgsrqy seiakyqavv
      541 rlngsnssqa vkvlkqdkqy ksqtaidanv gnvsahghkv ddiniyapss knqlknfvkl
      601 istdngknls lkksgvvlse kmasqlkvkv gdtirvkttd nhtgtakvtg itenfvghym
      661 ylsqsayqkm fgtraktntl lvrlshqnqh qreklanqlm khgdtmgtsy tvdqqqtitt
      721 mssslstvvl ifillsgvls fvvlynltni nvserirels tikvlgfydk evtmyivren
      781 imltvigiiv gygvgnalta yilrqaatdq iifpltihwv gyvvatalmv lftvivmlvt
      841 hrrlkhvdmv ealksne
//
LOCUS       WP_010621178             507 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease/substrate-binding protein
            [Paucilactobacillus suebicus].
ACCESSION   WP_010621178
VERSION     WP_010621178.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 507)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..507
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55137
     Region          <47..204
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          235..500
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(241,243,292..293,296,339,341,420,444)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mnsftsyiak ngsalidslg qhifisliaa iiaiiiavpl aialinhrrw gefvlqvtsv
       61 iqtipslavl glliplvgig tvpaiialvl yavmpifqnt yagltnidpl lieaadafgm
      121 srrfklfrvq iplampmils giriavvmii gtatlaalig ggglgtyiit giqtnnnnal
      181 iagavlsall ailaswlikv lakvsfkkla vgvailaalv aggtiyheat qpketitiag
      241 kmggepevli nmykdliead nskvnvvlkp nfggtsflfk glqsgkidiy peftgtvlqs
      301 lvktpknvsh npktsyklak kllnkqygld ylkpmkyqnd yalavrksda kkydlhnltd
      361 lsrvstefta afdtdfaqqk dgypglkkdy gldfksvkim eptlryaala nkkvnvtday
      421 ttdpqvreyh lvtlkdnksf fptyqgaplm tnqfarshkg ivkslnklsg kittkqmrem
      481 nyqvtvkhkk asvvarqflv keglltk
//
LOCUS       WP_010621210              76 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein
            [Paucilactobacillus suebicus].
ACCESSION   WP_010621210
VERSION     WP_010621210.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..76
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=8015
     Region          2..72
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mskkavlqld tltcpscmtk iekavsgqps venvkvlfna gkvkadfdds tvsadqlatv
       61 vtklgyevkn vkvkea
//
LOCUS       WP_010621212             203 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paucilactobacillus
            suebicus].
ACCESSION   WP_010621212
VERSION     WP_010621212.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23886
     Region          8..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpktqdlrvv rtrkmifdaf vrlvneygid ritvqqiade aminratfya hfrdkqdlyd
       61 qifdtvmqsf eiftkadifv gdnelhlatl ektltevfen leqqkelfyl icdgskrvel
      121 mqrlqqmlsd ttsefltnlk ieqngkvvpn efifsyitst lmgtlnwwlk edkefrpdhl
      181 ahfmiqlien shltvlgiql mde
//
LOCUS       WP_010621218             486 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Paucilactobacillus suebicus].
ACCESSION   WP_010621218
VERSION     WP_010621218.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..486
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51403
     Region          18..470
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 maslkekifr kedpsvydtk dahlvrslrv rdflalgvgt ivstsiftlp gvvaaqhagp
       61 avalsflvaa ivaglvafay aemsaampfa gsayswinvi fgeffgwiag wallaeyfia
      121 vafvgsglss nfrgliaplg lslpkqlsna vgvnggvidl vaaiaiviva lllsrgvssa
      181 arvenvlvvl kvlavllfla vgvtaikahn yvpfipkyra tadgafggwq giyagvseif
      241 layigfdsia ansaeakdpq ktmprgilgs lviavvlfvg valvlvgmfk ysdyannaep
      301 vgwalresgh avvasvvqai avigmftali gmtlagsrli ysfgrdgllp kwlgkldskk
      361 rpnralavit vvgvvvgslf pfaflaqlis agtliafmfv slgvyglrrr egkdiqnpsf
      421 kmpfypvlpa lgfigslivf wglgtdakiy agvwfllglv iyfvygsrhs ylndngkqqa
      481 kdskeg
//
LOCUS       WP_010621325             199 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphoribosylanthranilate isomerase [Paucilactobacillus suebicus].
ACCESSION   WP_010621325
VERSION     WP_010621325.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..199
                     /product="phosphoribosylanthranilate isomerase"
                     /EC_number="5.3.1.24"
                     /GO_function="GO:0004640 - phosphoribosylanthranilate
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22037
     Region          1..190
                     /region_name="TrpF"
                     /note="Phosphoribosylanthranilate isomerase [Amino acid
                     transport and metabolism]; COG0135"
                     /db_xref="CDD:439905"
ORIGIN      
        1 mtkvkicgls tmdavqavnq vhadlagfvf aksrrqvsid qarhlrqsld gqiptvgvfi
       61 epdleliqql adqhiinivq ihgeqnqsti nsihemhlkv tqvlhpgqtl ltepdyvmyd
      121 ginpgsghqi dwdniaqvrq pfflaggldp anvenainqv hpdfvdvssg vetdghkdpa
      181 kiieftrrah yarnearnk
//
LOCUS       WP_010621371             147 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621371
VERSION     WP_010621371.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..147
                     /product="VOC family protein"
                     /calculated_mol_wt=16471
     Region          5..140
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(5..10,25,63..64,67,82..87,89,93,129,139)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mtaklypyit finakeamay ykevfgatni srlpvsedqa eyygmmpsnl edttyhgefe
       61 vagtkilcsd afmaepqpss lisilldfds ndtddtkiae dlfnkvtesd tvrvilpysp
      121 qangdrmgqf vdhygitwvi rvgerie
//
LOCUS       WP_010621408             535 aa            linear   BCT 01-JAN-2025
DEFINITION  xylulokinase [Paucilactobacillus suebicus].
ACCESSION   WP_010621408
VERSION     WP_010621408.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..535
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57762
     Region          15..475
                     /region_name="ASKHA_NBD_FGGY_BaXK-like"
                     /note="nucleotide-binding domain (NBD) of Bifidobacterium
                     adolescentis xylulose kinase (XK) and similar proteins;
                     cd07809"
                     /db_xref="CDD:466809"
ORIGIN      
        1 mdadqiknei vsgntalgie lgstrikavl vstdfqtvas gdyvweneln qgiwsyplnk
       61 vwegiqtsya nlaaevedky gvgltkigsi gisammhgym afdkggeilv pfrtwrnnit
      121 gqaaseltel fnfniperws iahlyqailn keehvknvdf ittldgyvhw klsgekvvgi
      181 gdasgifpid egtkdfdagm ldkfralqav kqyqwdikdi lpsikvages agtlssegaa
      241 lldpsgqlqa gslmapsegd agtgmvstna vrkrtgnisa gtsafsmvvl dsplkkvhrd
      301 idmvttpdga pvamvhtnnc ssdinawasi fsefaraigk plkgnelyga lfdnslkgdq
      361 daggvvnfay lsgenitrlp egrpmfvrkp danfnlanff ksqlysafap lkigmdillr
      421 eehiktdvli aqgglfktpv vaqqvladal ntpitvmgna geggpwgmav lalyakshkd
      481 gqslsdyldd evftdpdsst ldpepvsvrg yekfidnyka alpveskave smkmn
//
LOCUS       WP_010621412             283 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Paucilactobacillus suebicus].
ACCESSION   WP_010621412
VERSION     WP_010621412.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..283
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32632
     Region          13..272
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mtdisdnfit ladgnkmpqq gfgvykitdq sefeqavtaa wqqgyrlfdt aqmyeneqyl
       61 gkilhdlqvp reqifittki seanqgydat irsmkeslkk lqmdyvdlll ihwpinthff
      121 dtwrafedlk aqgltksigv snygmvhlqy latqarempv lnqievspym sqkpllqfdr
      181 enniatqaws plgrgkvfne pviakiaeqk hrsaaqiilr whlqngvafi pksthperia
      241 qnasiydfsl tdeemqlmds vnknhrvske pelvyefgeq ypy
//
LOCUS       WP_010621442             242 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paucilactobacillus
            suebicus].
ACCESSION   WP_010621442
VERSION     WP_010621442.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..242
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27609
     Region          6..233
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 madlvyrevm hdlknrifnn qfdnkklpde rslsesygvs rssikralnv laqqgiifkk
       61 rgsgtfinpl ylknqslfqy egtnlgvtds fnldgqhpsv klldyqvvpa nsdlqqdlfl
      121 nendfvyqik rlrllddkpi iietgyipik vapeltpsiv qgsifnyled segksvtksf
      181 msimaepsnd edhqllglsd repvgimegi fflddgtpfe fsnmrvhyky lkyntfvsld
      241 ee
//
LOCUS       WP_010621468             169 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621468
VERSION     WP_010621468.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..169
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=19037
     Region          5..150
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mqwgfingsp naqghtyqla qylldgqskv dwnlvnyqia qlgqqrhakt defmdvvsev
       61 shadalligt piywsdmtgl lktfldrctm varqfdftdi pvyllvngtq tpdqtaqgia
      121 pavsqlcefl kmdyqdtiyv dtskvvqpsd ytsalhkqqe qlhtfvnvr
//
LOCUS       WP_010621560             396 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621560
VERSION     WP_010621560.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..396
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=44304
     Region          81..369
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 malnkqsird lneksvlrqi fvegpisriq isrnlklnks tvsaifndls drqlvmemgq
       61 gqstqvggrk pvmikvnqky gytlnfdigf rhldmmanyl dgtafqytrf etagyninqv
      121 ldliiesvnn fknpdtvngl lgisvavhgi vyqnqvtysp fidmedvsiy erltatftvp
      181 ivvdneanlv avfqrdfshd eehnmnnivv isihkgigag iiinhqiyrg ekgeageigr
      241 aiyptvfaep grvekienya sqdaiidlik nekkldeldf ddvaqmysdg dkvvvkaidd
      301 frdyitmivy naavsynpdt iylssnliet idqllpminn qynllpengn tdirmlrgak
      361 yasllggcss vthlalkmsg qqlkfnfdln aagiie
//
LOCUS       WP_010621531             360 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621531
VERSION     WP_010621531.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40304
     Region          1..344
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 magkviefrh viksfdetqv lkqidfeiea gkfytllgps gcgkttilrl iagflhptsg
       61 eilfngqtin evpanqrqvn tvfqdyalfp hlnveqnvaf gleikkvdkk iiknkisdal
      121 klvqlsgygq rnidelsggq kqrvaiarai vnepkvllld eplsaldhkl rkemqgelra
      181 lqqrlgitfi fvthdqeeal amsdqifvmn agkilqsgtp vdiydepinh fvadfigesn
      241 iipgkmkddy ivtfdghdfe cvdagmktne aveivirped ldiapantgk mnvtvdtqlf
      301 rgvdyqitah dvndnewkin sihkttvgqm vglnfdpedi hvmrfgedea tfdarleqye
//
LOCUS       WP_010621550             453 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar porter family MFS transporter [Paucilactobacillus suebicus].
ACCESSION   WP_010621550
VERSION     WP_010621550.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..453
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48209
     Region          8..427
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(20,138,141,145,252..253,257..258,261..262,351,
                     355..356,360,383..384,387)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 mhkvsrgfiy ffgalggilf gydtgvisga ilfiqkqlnl gtwqqgwvvs gvlagalvga
       61 iiigplgdkf grrkmvmasa viffigalgc glalgfwsli lfrfvlgiav ggastmvpmy
      121 lsevapadmr gslsslnqlm imtgiflayv tnyawsgyti gwrlmvgaat vpaailfigg
      181 iflpesprfl vrigkidear gvlgqlrnqd evqaeltdie ekakikmggw gdlfskvarp
      241 alvigiglai fqqimgcntv lyyaptiftd igfgvsaall ahigigifnv ivtavavvim
      301 dkvnrktmli vgalgmaasl ftlgiamhys hnsmtaayia aialtvyiaf fsatwgpvmw
      361 vmigevfpln irglgvglsg tfnwganmiv sltfptllaa lgtetlfvgy gvlcvlaiwf
      421 vhsgvfetrg ksleqiegyl dkragvtsta knd
//
LOCUS       WP_010621569             217 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621569
VERSION     WP_010621569.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..217
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24845
     Region          19..213
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mdqvtyvfsh lnevilpmvn wlgpwsylil fvlifmetgl vifpwlpges lifltsalaa
       61 vsgsklnifa lilvffsaaf mgdtvnfrig nyllrwkffr rhikntslhr terffkkygl
      121 ltvvfgrfvp lirtfvplia gtskfkwarf tlanflgval wvtvgstlgy ffgtisfvqe
      181 hlaliilgia liaitpaslf wlirqirrhi isrnftr
//
LOCUS       WP_010621571             698 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621571
VERSION     WP_010621571.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..698
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78737
     Region          18..630
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mktvlqkvrs glntklgffi ltvvlfaikt ywayqnkftl gaegsiqqfl lffnvfpgai
       61 iligialyfr grlsywlmml idfllsfwlf anilyyrefs dfisfslitg agstsnnlgk
      121 siagifrgsd lfafadvail ilfllfkvir idphyfkiry agvitllgfl lfganlgmae
      181 gnrsqlltri fdnnyivkyl glnfytayda vkthhnsevk skasssdlkp vlkflkknqt
      241 sknvtyagka kgknvfiihl eslqqwvidy kvdgeevtpn lnkiyhasdt iafdnffnqv
      301 gqgktadael mlenslfglp egsamttngt tntfqsapai leqqqgytta sfhgdvpsfw
      361 nrdnayksfg yeyffsksyy psvkdddvgy gikdkiflkg aanyvqqlpq pfyaklitit
      421 nhypyildkk nksidalktg dntvdpyvqt ahyldqsige fmsyldksgl rknsmivlyg
      481 dhygisnnhk paiadilgkk svdnydlamf qkvpfmiqmp glkgginhty ggeidvlpti
      541 enllgvyhkn yiqfgqdlla tdrkqivafr dgdfvssqft kyggdlyytk tgkkvthetk
      601 aqkavvakdq kyvttelsls ddvvngdllr fyhpkhftkv nkkdynynln aslkrlkeaq
      661 vkkktsvete nggkstlddy ttdapelkds sfvfpsik
//
LOCUS       WP_010621597             303 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621597
VERSION     WP_010621597.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..303
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35028
     Region          4..179
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mtaisiiipv sncaqelael lsdlkhqtft dfdvifvdng sfdqspqrir sfkrlsgfpc
       61 eiienhlnqd myssfnqgld catgryvlfl kpgqilhsky leqlvnaqsq itafsyqqrh
      121 itdsrnvmqm fmtglisldl igalierdlv adlrfepqlk kmaeklflyn lllkvtelnl
      181 isditkhtni tkqgekvphy setlayldqi eshikmsmpe lasiawihhy qelsnvylqi
      241 ralsfntrrl yleeqrhlkl llkeiekqkl dlstnkrlks wlnrtfghhv mtinqpqias
      301 vse
//
LOCUS       WP_010621598             152 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621598
VERSION     WP_010621598.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..152
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16554
     Region          10..150
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 maieitvphf dkilvgvdda vdakmafdya vdkakrdese lgivsiletg dinvyqalsk
       61 dyvhgtrdel darmneyvea ainygvdpkk itkiidegsk paeriinhvl paykpdllvi
      121 gsigsddsrk lfgsqaayma knagisvtii rk
//
LOCUS       WP_010621599             304 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Paucilactobacillus
            suebicus].
ACCESSION   WP_010621599
VERSION     WP_010621599.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..304
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34001
     Region          2..283
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mhshsvngar ffwvtflnil itvveilggv fsgslallsd afhnlgdsaa illgyfaqli
       61 grhpeterrt ygyrraeiif allnsifliv isvflifeaa krfshpqpin gelmlivavv
      121 gllanlasaf llqggskdsl nikatylhil sdalssvgvi igalfiwftd iswidpviti
      181 lvaiyicyet wpiihqtlsi lmqsspeldy acikkdikqi dgitgvhhvh awmidehrii
      241 fsvhinlkdm klsevepiyq rietllknky hichitiqae vergieetmf ntpadkatts
      301 deve
//
LOCUS       WP_010621601              66 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621601
VERSION     WP_010621601.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7225
     Region          1..63
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 meqgtvkwfn adkgfgfitr edgndvfvhf saiqgdgfkt leegqsvtfd veesdrgpqa
       61 vnvnkq
//
LOCUS       WP_010621610             447 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621610
VERSION     WP_010621610.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..447
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49172
     Region          11..427
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mqkhsyklsl pklltigfvt iiligsillk lpiasrpgvt thyidalfta tsatcvtgmt
       61 tvntiahwsl fgqlvimvlv eigglgfmtf tvllfsmlrr qptlttralv keslslesla
      121 dvktvtryvi glsltiqmig vvllsfdlvp rygwikgiyy sifhsvmgfc nagfdlfgns
      181 lenfgndpyv ifilsiliva gglgflvwrd illwphrhrv slhtkisltt satlttgati
      241 ifwftehgma kmpghadtwa rmvdtfllav sprtaglqvm pytsvsmaei iitmmlmfig
      301 gtpgstaggv ktttigilwl qswaalrgre dvefahrrft raniyrasml vfvstivvvi
      361 avvllsifet ipkgqgleyi mfealsafgt agmtmgltsd ltipgkviim almfigrvgl
      421 ftvmytilna drnkkhyryv eesvmig
//
LOCUS       WP_010621670             323 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621670
VERSION     WP_010621670.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..323
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36419
     Region          1..292
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mksynwaivg pgriaedfcs efpseqtlyg vasshdpnka kqfakkfnik htyqdyedll
       61 ndpqvdivyv attnnfhfdn ikhaltagkh vfsekpvtln tsqlqeliti skekhlilme
      121 aqtiyhmply dkltefirdq qlgqlksiqv sfgmhidktq tkdrllnpnl aggalldmgi
      181 yaisfarrfm taapklvatq mvptstgvdd vstylltndn nelctmnfnm ladmptigyv
      241 iyengyfiie nylrpenavf inadtggkql iiagktdiam gyealdmaka vetgdndtld
      301 wtvqtmnvmt qarkdwdfky pne
//
LOCUS       WP_010621699             332 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621699
VERSION     WP_010621699.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..332
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37222
     Region          1..254
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mlklgiigth witdqfidat vknghwqlts vysrnlqrar dygepkhate ffddldnffn
       61 dgsfdvvyia spnvlhyqqv rlaiendkhv iiekpaftnp defsqieall qahptvrlie
      121 aarhvhtplf aavkdqlnem ntvqgatftf mkyssrydqv lagetpnvfs pefaggalqd
      181 lgvypiyaaa alfgepdtvv yfptmidtga dgkggavlky pdfevtlnfg kianshmpse
      241 iyglkdtlvm dniadmteat yfdenqkahk ldavvpdnsm spevdeftkv leqpndlnnl
      301 ksyetwfkls rlvnsltysl resagikfpn eq
//
LOCUS       WP_010621690             260 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Paucilactobacillus suebicus].
ACCESSION   WP_010621690
VERSION     WP_010621690.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..260
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29092
     Region          20..260
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkiikqidvt ydpnhdlkad iylpdeefks mvidihgggw frgdkqkdad waqriaehgy
       61 avivpnyrit pagyypaplq dmdnliqwik eqdfavdkfa avggsaggnm avelaikygm
      121 paislsgiid ienwlsqhqn vvakegdtsh fnqqasaqin qngaddgfyk wfvvnyfngk
      181 tdqyheaspv frvsdqtgpm ylansldefv ptsgvlqmaq altdhnvpft vrmitgqqha
      241 kgyleevfdd tinfldryla
//
LOCUS       WP_010621715             310 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621715
VERSION     WP_010621715.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..310
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35377
     Region          6..190
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(9,11,97)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(43,96..97)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            95..97
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mekisvivpc fneqetvpif yptvekvfnq mnkidrdywf iddgssdgtl delkklhsen
       61 enkvhyisfs rnfgkeaall aglnsstgdf vvvmdvdlqd ppellptmln tiknedydcv
      121 gtrrtsrnge pvirsffanm fyklinriss tnivngardy rmmtrqmvds iislkeynrf
      181 skgifswvgf ktkyieyknv ervagntsws fwkllkysid gitdfsefpl siaswtgfls
      241 flfsicflvf ivvraivvpn ssvsgwaslv ciilmiggle llclgivgky igkiylqskd
      301 rpiyvvrekk
//
LOCUS       WP_010621724             335 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621724
VERSION     WP_010621724.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..335
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37904
     Region          4..186
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msysplvsii mpvynsedtl iytinsvlhq kfkdwqllci ddgstdnssg iisdfvkkdd
       61 rinyfykkns gvsdtrnfgl nlsqgefiff ldsddicktn llseavsaie kfncdtvifg
      121 ydsivkgnvi kssvpggsig tlvagndmar llrdglisvv ynklyrksll khnsfentsl
      181 gedflfnldv ilknpsical keslymynld svgslykkfs sdrsqvlrle ydkivevanv
      241 ykwssnvtnd tlnyfkihnl sgvimndfrd nspystgqkk sliskefnfy kvsvndilac
      301 rflskielvk lvcaklglir ilnilyflkk rkvkv
//
LOCUS       WP_010621726             474 aa            linear   BCT 01-JAN-2025
DEFINITION  flippase [Paucilactobacillus suebicus].
ACCESSION   WP_010621726
VERSION     WP_010621726.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..474
                     /product="flippase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53295
     Region          3..400
                     /region_name="MATE_Wzx_like"
                     /note="Wzx, a subfamily of the multidrug and toxic
                     compound extrusion (MATE)-like proteins; cd13128"
                     /db_xref="CDD:240533"
ORIGIN      
        1 mkvvknyiyn mgyqvlvlla plitvpyvar vlgahgvgin sytnswvtff lllgqmgial
       61 ygnreiaynr ddkkkrskif weieilqait iafayviflf fmfelshayr hyfliqslfi
      121 iaggldvswy fmgmedfkkt vlrnmmiklv sialiftlvk gqddlgkyif llgisqvlgn
      181 ltlwpylkes vnlvkisilr pfkhfypsll lfiptittqv ylvvnrimlg rfsttvsvge
      241 fdyadkitkl vlaivtatgs vmlphiahkf adgdvkgirq slynsfdfvt slsvpmmfgl
      301 aaistkfapw flgdqfagsa kimfieapvi vfiawsnvtg tqylmpvnrv seytasvsig
      361 avvnvitnlf lietyganga alstviseft vtavqiycir ntirrrqlft giwkyvvagf
      421 imfivvdrln smmkasivnf gvqialgfvi yaaglimlka pilhqmnnll krki
//
LOCUS       WP_010621742             293 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paucilactobacillus
            suebicus].
ACCESSION   WP_010621742
VERSION     WP_010621742.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..293
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32752
     Region          7..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..276
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(105..106,108..109,112,116..122,217..222,228..229,
                     231..232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mldkryqaly itsktqsytk taqqlfitqp avsqqissle teldlklvdn irgkihltdv
       61 glklakyahq vqlesdkvld svqastsqrs islgctlsls sfllpeligt lkqtntriss
      121 mivntgkvln alqegkidfg lvegnfnkee fsaikirdee figvvnsknp laaqtkldia
      181 dlintplivr ekgsgtrdif anwlatqnyh iddfhqviei gnpspiiell qrdvgvsfmy
      241 rslvddslnn ghlsilqvig fpiqhpinlv ylkdsyfanq yrqiatslqf nrh
//
LOCUS       WP_010621768             171 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA thioesterase [Paucilactobacillus suebicus].
ACCESSION   WP_010621768
VERSION     WP_010621768.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..171
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19070
     Region          8..152
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mdnnnvitcg qtltvvahri mpedlnehgt lfgggtlslv dreaslaalr vskapivtak
       61 idhinfirpm dlsvslnles yvsgfghrsi evftkiiged lrtgkrflaf tcfvtfvven
      121 ptgkigfdhl ipendeqnsi cdgyqkrvir rkqdrqdlnn lsnhininra y
//
LOCUS       WP_010621842             140 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621842
VERSION     WP_010621842.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..140
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15122
     Region          26..127
                     /region_name="cupin_HNL-like"
                     /note="Granulicella tundricola hydroxynitrile lyase
                     (GtHNL) and related proteins, cupin domain; cd02233"
                     /db_xref="CDD:380361"
     Site            order(35..36,67,69,90,92,94..95,114,116,118)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380361"
ORIGIN      
        1 mskneavkqg iifpagpknd ayakyfkgqs ylqglvadpa vnvgvgnvtf epgcrnnwhi
       61 hhdgyqillv tggeglyqee gkparhlvpg dvvvthdgvk hwhgatkdsw fshiaitagt
      121 pewleevsda qykaaeegak
//
LOCUS       WP_010621881             372 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Paucilactobacillus suebicus].
ACCESSION   WP_010621881
VERSION     WP_010621881.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..372
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42407
     Region          156..359
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtndyqkqqi iknlkavrgp liawmlmvgc laafvldtmh gsqlsyriai arqtrsvapl
       61 famfsigsvm lsiwfsprly ihakwmvvgl pliltwiysi vlvngtpviy igtypvfmvy
      121 liiiydhphk iftcitfvyf lvwgaytaiv gwmqglivll afvfvmvfvl yfwriyyiql
      181 rerqhfedly nelklayaqv eesavhaerq rvarelhdtl tqglaglvmq leaansfmhk
      241 gqndrakeiv ekaidiarda lrdsrttltd lrstteeslp arlqlvaeai dknyglnvtv
      301 hadevpdysp sqlteitriv sealtnvakh aqtdqavirt fisgnvfklq vidygsgfdn
      361 hdrkikkrti mg
//
LOCUS       WP_010621893             175 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621893
VERSION     WP_010621893.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..175
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=19134
     Region          2..172
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mkilvitgss hhpgtseila dnfimgaqes gneitrfdag dtpispltvd aknntangne
       61 tdrqiltmln dadmvvlvtp lyyfgmtaql kavidrmyqn nqnlignkya mllataygdg
      121 dsfdalvmhy hsitrymkwt dqgmllaggc sgvndvnrtn ypsqayqlgk qikld
//
LOCUS       WP_010621895             193 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Paucilactobacillus suebicus].
ACCESSION   WP_010621895
VERSION     WP_010621895.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 193)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..193
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21588
     Region          43..>154
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 menktgeiis ekllaqspif tvydrqvkss fdgvvvhrqv vdhgnsiavl pferinddyk
       61 lylseefrag mntttkgiva gmvngdeapd haakrelree mglllnsssd lvlvdrints
      121 egftneqtyi ylvelttnnh nftdkrdfdk dedvgkweyi astlelnklp svldihsaqg
      181 vvalqglfiy lns
//
LOCUS       WP_010621901             442 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A [Paucilactobacillus
            suebicus].
ACCESSION   WP_010621901
VERSION     WP_010621901.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..442
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=49951
     Region          1..435
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mkqeslfeqq sqqnsplanr vrpqsidefv gqghllehgk ilreiidsdq lssmifwgpp
       61 gvgkttlaqi ianqtkahfv nfsavtssik dirkimeeae anreigekti vfvdeihrfn
      121 kaqqdaflpf vergsiilig attenpsfei nsallsrckv fvlkqlttdd liqliknaik
      181 hpngfpnlei kvdddairli aqfangdarv alntlemavl ngnshdhqvd inrdnlnqlv
      241 ntkslrydkk geehynlisa lhksmrnsdv daaiywlsrm ldggedpiyi arrlvrfase
      301 digladtral sltidvfqac qligmpecdv hlteaviyls lapksnsayr arldaksdvk
      361 ktgnepvple irnaptklmk elnygkgyqy ahstedkvts mktmppeleg heyyhpteqg
      421 nekrfkqrle ylkdwhvqhd ne
//
LOCUS       WP_010621930             138 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621930
VERSION     WP_010621930.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..138
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16076
     Region          4..132
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mdikriahas fkvsdmrksv eyycdglgmk qkfelkdeng dpwinyleik pgqflelfyd
       61 fdnlpyathg ydfrgflhis levedleatk aeleskglai dseikfgpdk syqlwshdpd
      121 gnqiefmqyt kdsfqlrq
//
LOCUS       WP_010621934             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Paucilactobacillus suebicus].
ACCESSION   WP_010621934
VERSION     WP_010621934.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..279
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30262
     Region          1..275
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mrrntkwlig lgviivlfaa ifgiakvnsg sstaklktet igvapgpygd makdvigpll
       61 kekgyqvkik efndyvqpnk alnsgeidan lfqhtaylkt fakqnnmkls aigetptlgm
      121 giyskkiksl kdlksgdtvs landpsnlar slqllaaqhl itlksginva qaslsdiatn
      181 pknltfktld aaqlpqsrdn vtialipgny swnaniksss alalehlkee ykevfvvkts
      241 qknskfakav ksvlkskkfq taiakskfkd fdkpaswsk
//
LOCUS       WP_010621980             402 aa            linear   BCT 01-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Paucilactobacillus
            suebicus].
ACCESSION   WP_010621980
VERSION     WP_010621980.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..402
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42315
     Region          28..399
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mkeknsqtkk rsplnvamga afmmamaavg pgfltqtatf tgqmganfgf ailvcivvdi
       61 vvqlniwrii ivsgkhaqvl anevvpglgy vlsalivigg fffnignigg aglglnvlfg
      121 ispengalia aacaiilflv rnamlvvdrt vqilavikvc iliyilavtt vpyqsaiths
      181 fapttinfys ivtivggtvg gyisfsgghr lleggvsgvn nikyvnegal tgigvasvir
      241 vmlflaglav vmtgakldps npaatifkva agnfgykffg llllaagmts tlgstftsis
      301 fldynksked heswrswviv lfiaastaif yvigspakvl vvvgalngli lpialailli
      361 aatrkkimgt myhhprwllf tgwivvlfma yagiktllsi sl
//
LOCUS       WP_010621750             748 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Paucilactobacillus
            suebicus].
ACCESSION   WP_010621750
VERSION     WP_010621750.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 748)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..748
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81909
     Region          1..>67
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          102..725
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mlcqncqqnp atihlkatvn gqevqvdlcq ncyqmmkdaq nnlmnggngm aqnpfgfgnl
       61 ddllkamqgq ggaqqqsgqq afngqtqaqg gqggnnggns llaqfgvnmt dlakqgkidp
      121 vigrdkeiar vieilnrrtk nnpvligeag vgktavvegl aqaivsgqvp qklnnkeiir
      181 ldvvslvqgt girgqfeqrm qqlmkevskn knvilfidei heimgagnae ggmdagnvlk
      241 palargdfql igattlseyr kiekdsalar rfqqiqvdep svqetiqiln giknryqdyh
      301 nvkytdesid aaaklsaryi qdrflpdkai dlldeagskk nltlktadpa tieneihtae
      361 ahkqqaldne dyekaafyrd qvaklekakk daeenhtdta atvtvedmqk iveektnipv
      421 gdlakqeenq lkdlnknlsa hvigqdeavd kvsrairrnr iglnksgrpi gsflfvgptg
      481 vgktetakql akelfgseds mirfdmseym ekhstsklig sppgyvgyee agqlteqvrr
      541 hpyslillde iekahpdvmh mflqilddgr ltdsqgrtvs fkdtiiimts nagsgdseas
      601 vgfgaeasgs thsildklgn yfkpeflnrf daivefnalt kdnlmkivsl mtddvnkmla
      661 drglfinvtd pvksklvdlg fdptmgarpl rrviqeqied riadfvldnp ktknleavld
      721 ndkivvtgas lpnpgtvttd astsdtdk
//
LOCUS       WP_010621985             273 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Paucilactobacillus suebicus].
ACCESSION   WP_010621985
VERSION     WP_010621985.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..273
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30530
     Region          4..269
                     /region_name="HAD_YbiV-Like"
                     /note="Escherichia coli YbiV sugar
                     phosphatase/phosphotransferase and related proteins;
                     belongs to the haloacid dehalogenase-like superfamily;
                     cd07518"
                     /db_xref="CDD:319820"
     Site            order(9..13,44..46,67,97,99,193,201,223..225,227..228)
                     /site_type="active"
                     /db_xref="CDD:319820"
ORIGIN      
        1 mtiklvavdm dgtflrddnt ydgerfksql skmvergihf vaasgsqlsr lqdqfgemkd
       61 kidfisengs ivysenqfls vkeipndllm qllkiikehf qmpvasttvt gksgaymdes
      121 epqeifelkn ryyaklsrip eilnytegkf kdqivkvgls fassdnfdsq vqllrsllpk
      181 klaslnsgfn teligladvd kstglrnlqn kygvkndeim tfgdnendla mltmtphgyv
      241 mdnakdsikk lvnktapsnn kdgvltvldr lls
//
LOCUS       WP_010621996             248 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621996
VERSION     WP_010621996.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..248
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27537
     Region          3..243
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtleidhlvg gysqipvlkd isfevnngel vgliglngag ksttinhvig lltpfsghit
       61 iddislqens eqykkqiayi setpvlyeel tlkehidlti mayqldhdea wknatrllkv
      121 frldnklnwf pvnfskgmkq kvmiccalmt naklfiidep fygldplavh dllieinrvk
      181 nsgaavlmst hvldtaqkyc dkfvllangq vrakgtldel qelgttpgqs lddiylslak
      241 edrdgksv
//
LOCUS       WP_010622044             137 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Paucilactobacillus
            suebicus].
ACCESSION   WP_010622044
VERSION     WP_010622044.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..137
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15469
     Region          51..129
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mvvgvskali avdvillivi viwigstitq sirrkrfakv leedvfedgm rkaqvidlre
       61 ktdfdkghil garsvpysml kqryveirkd lpvylydqgm tlstraastl gkqgykdisi
      121 lkngyarwsg ktktkky
//
LOCUS       WP_010622121             320 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Paucilactobacillus suebicus].
ACCESSION   WP_010622121
VERSION     WP_010622121.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..320
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34438
     Region          5..320
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtqteiwvyv qtnqtsvept slqlitkake iavnqrvvav mptvvsekli nevqeygpdk
       61 iitleddrfk tatdteiadv lyqvvstrkp nsllipatvi grsvaprlqa mlqtgltadc
      121 ldvyfdgdtl vqvkptygdd imceitcpdh qpqmatvrpn vfkavkqnnd ttiekadfef
      181 hpetqvkast pqsiissaan igdanvvval grgasspaii ekarklaakl ggmvgvsrpl
      241 tdsdefghes qigqsgqsia pdllinfgis gavqylvgie naktivsvnt dpdapilaas
      301 dyafvgdand fmdnlleqvr
//
LOCUS       WP_010622210             237 aa            linear   BCT 01-JAN-2025
DEFINITION  pseudouridine synthase [Paucilactobacillus suebicus].
ACCESSION   WP_010622210
VERSION     WP_010622210.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..237
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26411
     Region          1..227
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 merlqkvmae agvasrrqse klivaghvkv ngnvitelgv kvsnndnvsv ddvplsrqrl
       61 eyyllnkprg vvstahddkg rktvvdilvd dvdtriypvg rldydttgll lltndgdlan
      121 klthpkyevd ktyvakvqgi vtnddlkqlr lgvmvdgrkt kpaktkitnv dqkkkttivq
      181 vtihegrnhq vkkmlkavgh eviklhresy gfltlagvpg gqwrklrtse vmqlkel
//
LOCUS       WP_010622232             147 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Paucilactobacillus suebicus].
ACCESSION   WP_010622232
VERSION     WP_010622232.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..147
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16179
     Region          1..146
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslldnlnqd mktamkakdk ptlsvvrmlk savmneqinl ghdltedeei avlsrelkqr
       61 kdsvaefekg drddlatqtk aeikvvekym paqlsdddvk qivtdtvkdl gaesmadfgk
      121 vmgavmpklk gqadgklvnq tvkdllk
//
LOCUS       WP_010622235             291 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010622235
VERSION     WP_010622235.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..291
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=32286
     Region          6..290
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mediqklier hqyvgragta fiyailvsia vnffwtpghi yssgvtglaq lvntltmrya
       61 pfevttgvml fvlnmplfvl awfkighrft iftfisvtla simmhliqpv tlthdplica
      121 ifggaingfg tglslrygis tggldiigiv lrkktgakmg rinisfnvli ilaagfvfgw
      181 pyalysaigl vvnarvmdmv ytrqqllqvm ivtdrpksvt dsiqnhirrg itivhgaega
      241 yhhdskailf tvisqyemye lraameesdp hafvsitesm qimghfyepk l
//
LOCUS       WP_010622301             171 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Paucilactobacillus suebicus].
ACCESSION   WP_010622301
VERSION     WP_010622301.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..171
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20823
     Region          65..129
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mprvricrka gcyheipydq snpycnqhas lyhgtysrfd khkrrtsyqs ynrykrdkea
       61 ntfyqskqwk klsrwlkeqa yftcaccght ydkpgylvtd hivprrvdrr kqlevnnlwv
      121 ickrchywkg qledelyqsq slienldvsk qwdrdkvtew ivkheqhhnt v
//
LOCUS       WP_010622343             282 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Paucilactobacillus suebicus].
ACCESSION   WP_010622343
VERSION     WP_010622343.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..282
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30767
     Region          12..268
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 msiltetfel pnglqipkvg fgtwqisggk taydavsnai evgyrhidta qaynnessvg
       61 kavrdsginr eeifvtsklp aqiktydgal safdktlnnl gldyldlyli hapwpwsqig
      121 tdhdrdnvet wramekilss graksigvsn fnvhdlknil enstvapmvd qiqyyvgyte
      181 pkitsfseen gilleayspl atgdlvnndq ikamaakygv svpqlalrfc iengvlplpk
      241 atgtahiesn aelnfsissa dmkilndlpd tapmhmhnat qg
//
LOCUS       WP_010622471             197 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paucilactobacillus
            suebicus].
ACCESSION   WP_010622471
VERSION     WP_010622471.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22719
     Region          5..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtekrrhgke lenaifdati dilnddgldg vtfskvaarv ktsrpviyrr wdspfslale
       61 airnkirqdn hghmqditls gqnlsedlsq vlqrymvvmn tfsryyvsll lagtnsddts
      121 vlddvfehgn qeniktmtvi lnraidrdei kedkfsnetk llpfewlryh lfteskvsde
      181 qlktfikcvl vpvytqk
//
LOCUS       WP_010622418             186 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Paucilactobacillus suebicus].
ACCESSION   WP_010622418
VERSION     WP_010622418.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 186)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..186
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20756
     Region          41..176
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 msleekrlss etifhgyvmd lelaqvqlps gqktrreivr hapavallai ndqnemllmr
       61 qwraavnkat leipagkvds rddsalhaai relneetrla adkitevssf ytsvgfcdeh
      121 mtlylatgls pvenelpqde denlqmihvs lnqanqmiat geindaktim aiyywqglkl
      181 rgelng
//
LOCUS       WP_010622482             195 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Lactobacillaceae].
ACCESSION   WP_010622482
VERSION     WP_010622482.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillaceae
  ORGANISM  Lactobacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Lactobacillaceae"
                     /db_xref="taxon:33958"
     Protein         1..195
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22404
     Region          3..132
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,63..64,67)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(62,113..114,116..117,121)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(68,73..74,109,112..113,116..117,120,123)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91..93,109..110,113..114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(122,128..129)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          144..186
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
ORIGIN      
        1 makigyarvs skeqhldrql aalkdvdklf tdklsgantn rpelqkmlay iregdivmvt
       61 eldrlgrnnh dltkimnsiq nkgatldvln lpsmtgiadp nlrqlmtnli ielykyqaes
      121 erkriierqq qgialakqqg kyhgrkpqyt qddprlqhaf klyragmsdi dvsrntgikr
      181 ttfiryrvky gikrk
//
LOCUS       WP_010622511             283 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Paucilactobacillus suebicus].
ACCESSION   WP_010622511
VERSION     WP_010622511.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..283
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31963
     Region          12..279
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mqsltdtytl nngveipvvg fgtwqtpdgd vayqsvksal dagyrhidta aaygneesvg
       61 rgikdssvdr hdiflttklw nddhgyestk qaldvslqkl etdyvdlyli hwpnpikfrd
      121 dwedinaetw rameeayrdg kvraigvsnf rpshlttlmk tatitpavnq nylnpsdmqp
      181 evtrvnaqyn ilneaysplg tgellqvkal qdmatkyqhs vpqvilrwsl qhhflplpks
      241 thadrikdnt nlfdfkisde dmqtidglhg ttrlatdpde tnf
//
LOCUS       WP_010622555             469 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Paucilactobacillus suebicus].
ACCESSION   WP_010622555
VERSION     WP_010622555.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..469
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50907
     Region          18..459
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,138,
                     141..142,145,270,273..274,277..279,282,310,314,366..367,
                     371,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mkqrsqwill latsmvsfms tidagivnia vpqmsrdlnv pmneaewvvs vylvlicvll
       61 iffgklsdqi gripifqigt vifvlgslgc gmstnlpflm garvlqglga smtmatnfgi
      121 itqifpihrh gtalgvnsaf vqlgsiagpg lgglilaaln whyiffinvp igiiafafgh
      181 hifpkeerky hhvsidwtgy ltyalatilf ffaiywgqsi gygkpqiigl lvltvllitl
      241 firiekrape pllnlkifkn agfsigilta mmvfatgyfn nmimpfylqe tlhyssaiag
      301 lilmavpivn ifsapaagvm sdkigaekvs mialvifivp elvfvtveps wsiiwliigl
      361 gmfglangtf qnnpmimgna gqefqgiags iaalarnlgm siglslatsl lyfgiglkag
      421 khitaypsah pawfvsgmhf aygwalgmiv ialvlivwlv rrqtakqhg
//
LOCUS       WP_010622527             295 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Paucilactobacillus suebicus].
ACCESSION   WP_010622527
VERSION     WP_010622527.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..295
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32185
     Region          2..191
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mkltllgslg hinqytipaf vkaghdvtvv tssekrvaai esigahaavg smkdteflts
       61 altgadaayl mlsggfddsa smdetatkqa iifrdavrna gvnrivnlss vgadqgpevg
      121 slhmyhiied tlrelenvni tfvravgfys nwlaniptik sdhaiyrnah aqtvnamtdp
      181 sdiataiiee lpnlksttdv ryvvsdfqtg nqiietlskk lnipdlkwve ltdqqmltqm
      241 ekmgmptpfa qgmttsnrrq dspdfyadlr anlptlgkvk fsdfaerfvs ayqns
//
LOCUS       WP_010622567             255 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010622567
VERSION     WP_010622567.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..255
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27560
     Region          4..251
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgyvialanq kggvgkttts vnlgaclaea gkkvllidid pqgnatsgtg iskasieqdv
       61 ydvlinetpl edvilktvhd gldivpttiq lsgaeielts mmaretrlkd aiesvddnyd
      121 yvlidcppsl glltinafta sdsilipvqs eyyaleglsq llntiklvqk hfnpdlkieg
      181 vlmtmfdart nlgqqvneev kkffgdqvye tiiprnvrla eapshglpii dydpksngae
      241 vyrqlakevl aahgk
//
LOCUS       WP_010622630             370 aa            linear   BCT 01-JAN-2025
DEFINITION  VanZ family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010622630
VERSION     WP_010622630.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..370
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=42880
     Region          78..187
                     /region_name="VanZ"
                     /note="Glycopeptide antibiotics resistance protein
                     [Defense mechanisms]; COG4767"
                     /db_xref="CDD:443799"
ORIGIN      
        1 mwlylydlkl ailmfpfaal iftfpflwwh yyrhgaisrw tilmeysfvl ymmcayflvn
       61 fplppreyva klttatmnli pfhfvsdiik ssplkiteps tylkaltnsa viqpifnifl
      121 tmpfgiymrs yfkkglktti llsfllslff eltqlsglyg lyprpyrlfd vddlmmntlg
      181 gfvgfyvtrf vmrwvpseah lkeslrirak hvslfrhata fgvdwvllll irtaitvllp
      241 qiprllgsls plivfgewlv lmlipellfk rtlgmqtvhl qiesngssgi ilrnilgysm
      301 fvvlvaekil rnllwnnpam nhqvqvlfaf aaviyfgvvi vdllvdifrp shelffekls
      361 rtklistfdq
//
LOCUS       WP_010622666             192 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paucilactobacillus
            suebicus].
ACCESSION   WP_010622666
VERSION     WP_010622666.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22656
     Region          13..134
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mqrdlkinqs snkqrtvrdf ssamfklleh qsfekitvqe icteshyprs tfynyfndkf
       61 dlmnqcwneq ivklnfddgk rvlasqiiel ffsrsyelvq enrddiqlim qhndindqlw
      121 tsfrssinnt lnaiflqceq vtesklpadm lseylsstcl lvlkkcffsk kvvpleeaqr
      181 ylkqiisdsi fd
//
LOCUS       WP_010622657             199 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Paucilactobacillus suebicus].
ACCESSION   WP_010622657
VERSION     WP_010622657.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..199
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21779
     Region          3..167
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 makiavilgs vrqhgvginl fnylknqksd ietslnvelt flnlgqynlp vfdedvppma
       61 nqnrqlpanq qqwlddiqda dgyilmspey nhslpgglkn aldylafqaq gkpvktlgys
      121 dnsrggqfgv aalipvlqrl emivlpkpal ignipailda kgtiiddqas tklhsgvvkm
      181 fkeisfyttl ltanpfprn
//
LOCUS       WP_010622669             264 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase
            [Paucilactobacillus suebicus].
ACCESSION   WP_010622669
VERSION     WP_010622669.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..264
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=29467
     Region          111..213
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mfslvtkgsq rnkiamilig liilfgsdyl lqmmhlghss iqyfglrifi iliaiinlft
       61 lgtnkitsqr igyrrpvrta wiltiiclvi vfmmsgfiin vaqvieqpnh ilqviimals
      121 agmfeetvcr glmfsvfanm akngkhpllw agilnsaifg llhlnnyfsn gqglnitvqq
      181 vfyafaiglt fsvvhiatng lwvgiilhtl fdfqptissa itqannwivl liifvpiiii
      241 aifylvkads lvkpgmdirf niqy
//
LOCUS       WP_010622683             176 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paucilactobacillus
            suebicus].
ACCESSION   WP_010622683
VERSION     WP_010622683.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..176
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20101
     Region          17..>57
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          <136..174
                     /region_name="TetR_C_8"
                     /note="Transcriptional regulator C-terminal region;
                     pfam14278"
                     /db_xref="CDD:464123"
ORIGIN      
        1 mspkelkqkk ledthkalmt lmanekiedi sitelcdlag vsrtyfyhhf tsmddvisef
       61 qvssivaymr alpskqildl stmmqhyfrl nqesyedtli liragkesvl ikafksvyly
      121 lfdknrisks qltnnkywad fiagavvnmm vawlqdgmte satamgenva kflsrn
//
LOCUS       WP_010622139              90 aa            linear   BCT 01-JAN-2025
DEFINITION  KH domain-containing protein [Paucilactobacillus suebicus].
ACCESSION   WP_010622139
VERSION     WP_010622139.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Valverde,R., Edwards,L. and Regan,L.
  TITLE     Structure and function of KH domains
  JOURNAL   FEBS J 275 (11), 2712-2726 (2008)
   PUBMED   18422648
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Grishin,N.V.
  TITLE     KH domain: one motif, two folds
  JOURNAL   Nucleic Acids Res 29 (3), 638-643 (2001)
   PUBMED   11160884
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16911350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..90
                     /product="KH domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10097
     Region          8..79
                     /region_name="KH-II_YlqC-like"
                     /note="type II K-homology (KH) RNA-binding domain found in
                     Bacillus subtilis UPF0109 protein YlqC and similar
                     proteins; cd22533"
                     /db_xref="CDD:411790"
     Site            order(36,42,45,47,50,53..54,57..58,61,76..79)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:411790"
ORIGIN      
        1 mtsteidtli rlivqpivih pesidiqvek tqnfeqytln vhsddvgrvi grnghvaaai
       61 rtivhstind ksrkvrllin dhrnhetpaq
//
LOCUS       WP_010622716             513 aa            linear   BCT 01-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Paucilactobacillus suebicus].
ACCESSION   WP_010622716
VERSION     WP_010622716.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..513
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=56035
     Region          3..455
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 mnyligtdig tsgtksilmd tngkliaqdl eeydvltpkp lwaeqwpevw lkgakesirs
       61 vvqksgvnpd dikgvgisgl yggsgipvdk dmnpvrpdli wmdrraaeet ewvkenvdld
      121 rlseitgndv vdpyygytkv lwvknhepen wkktklflpp nnyviykltg evsidysaag
      181 niggfydint gtwskemmda mgvpvdkmpq kfvdateiag risseaasdl glkegtpvia
      241 ggvdvgaani gmgvlepgry vaaigssmna alvsekpikg kglivwpypy ksrdlvynfs
      301 gsatagaitk wfrdnfgdae vavqnhggkd ayvtlgeesk dvpagsrglv vlpyfmgera
      361 pvwnsdakgm ifglslvhtk adifhafeea vcyalrhsie stgrdlgdyi viaggvthsa
      421 qwvqmfadvt gyavrtpvdd aeanlgdvml aglatdtlsi devqkwqvlg dkvepraeqh
      481 etynkyykly rnlyndlgdd mhnlslisgi ees
//
LOCUS       WP_010622824             127 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paucilactobacillus
            suebicus].
ACCESSION   WP_010622824
VERSION     WP_010622824.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..127
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14403
     Region          1..115
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mhfnfdstep iylqvaeqle eaiftggfae deqvpsttei skqfhinpat vlkgmnllva
       61 kdliekrrgi gmfvkqgatt rimnqrresf yadyvmnlvs eaqklgltqd kleqlisrgy
      121 qdeditr
//
LOCUS       WP_010622731             209 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Paucilactobacillus suebicus].
ACCESSION   WP_010622731
VERSION     WP_010622731.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 209)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..209
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22050
     Region          1..206
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 misflqangv qllvktwqqi yisfislglg iivavplavv ltrlpkvagf viglasvlqt
       61 ipamallamm ipifgignlp aivalfiysl lpilrnsylg iknvdpavld aakgigmnnm
      121 qsifqveirl aapvimsgvr lsatyviawa tlasyigagg lgdfifngln lyrsdlilag
      181 sipvillali tdyllgkvel lvtpktaqa
//
LOCUS       WP_010622828             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Paucilactobacillus suebicus].
ACCESSION   WP_010622828
VERSION     WP_010622828.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..277
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30297
     Region          1..272
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkkwiagla svaavalllv gcgksssske ttltvgasni phaqilkhvq pqlkkeginl
       61 kikvfqdyvl pnkdlangdl danyfqhipf lenwnkenng tlvsagkvhl epigvyskky
      121 kslkdlpqna tvlvsnnvad ygrvltlfkd aglitlkpgt kittatfkdi atnkknitfk
      181 tdlepklmpe fyekgegdav vinanyaeqa kinptkdaia leknsspyan ivavrkgdkn
      241 kpaikklmka lqskstqqwi lkhykgavip vypngkk
//
LOCUS       WP_010622930             612 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Paucilactobacillus suebicus].
ACCESSION   WP_010622930
VERSION     WP_010622930.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..612
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=66870
     Region          28..452
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mwrylkrlli gkplktldeg gqhltkfkal allssdalss vaygteqitt vlvtlsaaal
       61 wyslpiagiv lilllaitls yrqiihaypt gggayvvast nwgrngglva ggsllvdyml
      121 tvavsttsat eaitsaiptl ykysilisvv ivflimamnl rgmsesanll tipvyffvgm
      181 maimivwgfi niltghiayh apagigtavp gmtvvlfira fsagsssltg veaisnsvpn
      241 fnkprsknaa ntlvimclil asffagvtfl sfylgivpng hvtvlsqigs tifgghgvgy
      301 yllqlstami lavaantgfs afpilafnla kdkfmphafm drgdrlgysn givvlalgav
      361 vlicifhgqt tlliplyavg vfvpftlsqs gmiihwfrtr dgvwlgksfi nlvgalisls
      421 lvvflfwqhi dnvwpyliim plllymfhki hehyikvakq lrvagktkvq ikdfegstvi
      481 vlvsnvtrvt sgainyarsi gdyviamhvs fdenpgkehk tanefkaefp dvrfvdihss
      541 yrsiatptlr fvdviakrat arnysttvlv pqfvpkhpwq malhnqtslr lrtllnsren
      601 iivstynyhl ke
//
LOCUS       WP_010622972              96 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Paucilactobacillus suebicus].
ACCESSION   WP_010622972
VERSION     WP_010622972.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 96)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 96)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..96
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11069
     Region          1..90
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mnfkyednri ytvdkdgtll geivfptide dtdtvlvert fvnpiargqg laaklvaefy
       61 eyakqrnlhv qllcpyakka fekhpeyqel ltdren
//
LOCUS       WP_010622979             315 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Paucilactobacillus suebicus].
ACCESSION   WP_010622979
VERSION     WP_010622979.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..315
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34777
     Region          4..314
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mgvflssvsg vfvilvmvai gyilnergwf denstrmisk lvtqvalpay mvttimkdft
       61 aeqlktllpd lrypvismli lfaastvisr avriksshvg lfesmffnsn tvfvglpinl
      121 alfgdrslpy vlvyymantt ffwtlgvwli qrdgmgkaki nllatlkkif spplmgfiig
      181 iilvvlhikl psflqsdlty vggltipmsm lfigiavsna gisrmrfnrd siwiligrfl
      241 capalmallv ipshmeilmk qvfilqaamp vmtnapvvsk lydadadyaa imvtettlms
      301 iivvpilmvv ikslv
//
LOCUS       WP_010623029             302 aa            linear   BCT 01-JAN-2025
DEFINITION  SPFH domain-containing protein [Paucilactobacillus suebicus].
ACCESSION   WP_010623029
VERSION     WP_010623029.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..302
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32517
     Region          21..291
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mlvlgiviiv ivlvllfvsl kivtqpnvgv vvtlgrferv inpglhfikp fisrvvtvnt
       61 aqtpldlnqq vvitkdnaei svkislkfhv tniqdfvfkn edsvrsmvqd traalrgiig
      121 nkelnevlng tqdinaalfk eissvtagyg lnvdrinids vnpskdiqes mnkllqatre
      181 rdatiataqg ksqsitlene annkalletn kaenealvks aqaqadsvki kaqaeafrvd
      241 tingslanad dkyfinlnte afgklansda ntvvipnqtt dslgqlpaig kliagdkkga
      301 ak
//
LOCUS       WP_010623138             148 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Paucilactobacillus
            suebicus].
ACCESSION   WP_010623138
VERSION     WP_010623138.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..148
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17117
     Region          3..115
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(51,54,58..59,68,86,90,96,100,103..104)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mtytikevse kvnlsiytlr fydkqgllpf varnqsgyre ftdgdlnlih ticclkdtgm
       61 klddirqyik yvmggpatie qrkallkkhr hevelqqqki adnlkeidyk ldvyenpqak
      121 eivaqelqfv tnekiannlp npyhvvaq
//
LOCUS       WP_010623143             416 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Paucilactobacillus suebicus].
ACCESSION   WP_010623143
VERSION     WP_010623143.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..416
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44502
     Region          58..413
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mdekqvapea epkgkfpyrl gfgllfgllg wlvpylgvns tllpakiqqi apdqkvqiva
       61 vlatiamvva tvaniiegal sdrtvsrwgk rnpwivlgmf ttlicfyflt kvttitgiiv
      121 nwslfqvaln lmvapivafi adkapkkyrg sisafygvgm nigtpvgtmi asqyitriss
      181 giyvfmvfev iftviglllv gdgsnkgekv kklkgselle afifpihgdv rdfylavfgk
      241 llfvsaqfvi tgyqlyifvd ymklssanat anlsimsmil litgvsfail ggpladkfhs
      301 lkllvavstv amglgvaipa idpapwtmfv yaglsgaamg mynsvdqaln vsvlpnpdna
      361 akdlgivnla nslgqvfgpi casiiigaig yrmmfpaagi mclvgailil mikkvk
//
LOCUS       WP_010623180             139 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin
            [Paucilactobacillus suebicus].
ACCESSION   WP_010623180
VERSION     WP_010623180.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..139
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=15383
     Region          6..116
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 makveikrgd ifyadlspvi gseqggmrpv vivqndignh ysptvivaai tariqkpkmp
       61 thvginseyv giekdsvill eqirtidkqr lrdrvthldd dtmkrvdhal lvsigllnqg
      121 akhkqqrsas stykikktv
//
LOCUS       WP_010623187             458 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Paucilactobacillus suebicus].
ACCESSION   WP_010623187
VERSION     WP_010623187.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..458
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50208
     Region          1..458
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mkmklaeiak aiavkndisk wqdveitsva fdsrnlvgga lfvplqgqtd ghrfassafd
       61 ngasatlwae dhsvttsedq pvlvvdnplk alqelgkyyl hkinpivvav tgsngktttk
      121 dmiasilstq mnvtktyanf nnqigvpmtl lgmepnteav vvemgmdhfg eldflsnmvn
      181 pdiavitmig eahieffgtr dkiadakmei thglkedgtl vyngdeplln erttdlkqvl
      241 rkfgrqlsnd lyatsvnakt heiefhvnvw pedtftipmm geynvnnala amtvgqilhi
      301 stknmknala nveltanrae wingtageqi lsdvynsnpt aakqvlhafa ktptegrrvv
      361 vlgdmlelgd aaphlhasle seispnsisd vyligpqmks lyseltsryg adhlhhydie
      421 qknqltsdll dflsqkdavm lkashglhle tvldsltk
//
LOCUS       WP_010623206             262 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Paucilactobacillus suebicus].
ACCESSION   WP_010623206
VERSION     WP_010623206.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..262
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27858
     Region          4..261
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mfafdfmrha fvastfiavi cgimgvfvia rnmsflthtl aeigfagaaf gvfagwpaln
       61 gmllftivss amvgqmsvks arresvisav salflglgil flsisdqtss satsilfgsv
      121 igisvsevwq ivilsifvli vvllmyrslk fesfdsigar vngvngplis ivflvllals
      181 vsvaaqivgs llifilltlp aasakyfvhg vakmivlatl falvgtwlgl ylgyltnwpv
      241 sffiatievi ifvaalihar ra
//
LOCUS       WP_010623208             319 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Paucilactobacillus suebicus].
ACCESSION   WP_010623208
VERSION     WP_010623208.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..319
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35549
     Region          63..306
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mskkttnfkl aryttgalga glvlgsamvy rfatgfsdkq kvngqtksie qnnpvdndwi
       61 ktlkqedwsi ktedglklsa sfvqnpastg kavilahglh hsrqqvwvya rmfykmgfsl
      121 lmpdarahgk segnviglgw ldrsdylqwi nelikkqged skillfgism gattvlavsg
      181 edlpknvfgi iadsgysnvf segkyrlshk yhfpsvpfva iastiskfhd gyafqegdil
      241 kqvqrnqlpl llihggrdrt vpvknvfely haanqpkkly vepnadhies iyvnpekyqr
      301 vvesflaltd rvqstssdk
//
LOCUS       WP_010623216             269 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Paucilactobacillus suebicus].
ACCESSION   WP_010623216
VERSION     WP_010623216.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..269
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30465
     Region          12..263
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 maiynheqkl niydshthln ddtfydevpa ymarakhfgv nemnivgsna ilneralkla
       61 heydnlhaiv gwhpedskyy nedveeklia qldddevvam gemgldyhwd sspqdvqrkv
      121 farqveiakn lhlpisvhdr dafedtynil kaadvrdigg vmhsfngdpe wlkkfldlgm
      181 hisysgvasf knahevhdsv kqtpidmmlv etdapyltpt pyrgkqnepg ftkfvvdaia
      241 elrevtpkei adatfantvq lfgsqnakn
//
LOCUS       WP_010623287             269 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010623287
VERSION     WP_010623287.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..269
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30317
     Region          2..264
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mtqvitfgnf kggvgktsns tmvalelsnr nfktllvdld pqgnatnlyl ktklnisnev
       61 ghfdktlmss vedsnlsnsv inikdnldll asapdfslyp rymeklhnyd drvkefdrll
      121 kplkekydyv iidipptisl itdsalyasd ycliimqthe hsfegaeafi kyiqeevide
      181 ykaprlelvg ilavllqaga pvdeatvtna isefgeenif knkihsmqrl krygitgitf
      241 kskfdkkvfa vykdvtdell srieviehg
//
LOCUS       WP_010623336              50 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin, partial
            [Paucilactobacillus suebicus].
ACCESSION   WP_010623336
VERSION     WP_010623336.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 50)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 50)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..50
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..>50
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
     Region          1..>50
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mvsqgdifyv nfnpsrgheq mnkrpaials ndlvcqtsnm tivapigstk
//
LOCUS       WP_010623495             237 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010623495
VERSION     WP_010623495.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..237
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26892
     Region          2..>174
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          <148..>204
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
ORIGIN      
        1 midfylleal vkfdeygtla kaaeqlgvtq palthslknl edelgvqlfd rkpnrlyltd
       61 tgkyavqqak rviddnykft dkvklfeqnq ssitiganap gplivihsln ldnlivqnkh
      121 vqkdfekiln eeqvtclltn kslksdkiis vfigsermav nlrqenpltk ieslkfadla
      181 gntflcpqei gfwkdiyesq ipdgkfiyqn esteykells fssmpffttn ltkldpn
//
LOCUS       WP_010623510             439 aa            linear   BCT 01-JAN-2025
DEFINITION  CAP domain-containing protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010623510
VERSION     WP_010623510.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..439
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=47639
     Region          107..250
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
ORIGIN      
        1 mklnkknlav lfstallltt tfgsatnsla dtnntsnntq ttstvtstnq tkntndqnnt
       61 atntnsndni adnntnattn ntnntnsssn ssntdsnnsa tvaktqasts vdvsaiktal
      121 lseinnlrsq ngldpltnve vlnsyaqers dsfasngtgi dnhvgwdssk mapynltaee
      181 nigqlplgtl andptqiakt iteefydenn davpnyghrk nmlnpyvgyi gfgvtvgsng
      241 miyfsqeign datyaakssy tqrnsyyytt mndyanvsqy dsvdaernsg naaqdyvqng
      301 dsytfsdirg gvstrdsyvn mydrdgqlyt nlrlapgtdw asdivsiing tyylhvsnng
      361 fvkaadvlpw asflggpvit akdnapiydd ygkkttryaa ansswvtdrr svdfgnnvky
      421 yrigtnawll esdlsnpin
//
LOCUS       WP_010623528             825 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010623528
VERSION     WP_010623528.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..825
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=89090
     Region          16..655
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mnnqsnnnnh apyspwknif kwlgiligav viafigvfay yamsapaisq etlqsggsst
       61 ivdskgnqig slgsnkrnyv tidkvpqqmq davisiedkn fynetfgidp vrivksafnn
      121 atkgtlqggs tltqqliklt afstdakdqt fkrkmqeawl avkvshdysk qqilefyvnk
      181 vymnngaygi etgaryyygk slkdltlpqm amlaglpnap snydpykhpe qakqrrdlvi
      241 ramldnekit ksqaekaint pidsglqpfk enttgndtdk mvtdpyikea isevkakgfd
      301 pyrdnlkitv nmdydaqkrl ynivnssnyv qfpdskmqvg ativnpnngk vvamiggrkl
      361 sniqfglnra vqtsrsngst mkpildygpa feyldwstyh qlydtkyvyp gtdivlkdwd
      421 qtykgqmslr ealvtsrnvp aiktlstvgf skakkfakkl gitipdnqgt sagigsdvss
      481 lqgaaayatf anggdyykpt yvskietadg ithsyhsepk kamkastaym mtdvlkgvpt
      541 segfaqyaai sglhqagktg ttnysddals snsnlentak dawyngytkn ysmsvwtgyd
      601 sqnshgvsat yqsvagkiyk aemqylakks tnsdwkkpss vvklkiktgg sttpvvaspr
      661 sssssyttel fvrghapnnp yknyssssss ssstgsssee vipnrrqssd ddetndnnnt
      721 neqngdtdtg dgtttngdnd qtvtdgnnnn tnnntggntt ttnppttggg dtntggnttv
      781 gsnnnnntgn tgntgggttd nntgggttqg gntqggntqs gseae
//
LOCUS       WP_010623534            1175 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010623534
VERSION     WP_010623534.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 1175)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1175)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1175)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..1175
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=134111
     Region          5..1149
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mtlnfilgtn qydhhqemik qfqqdletdp kgkfffivpn hikfeseirv lndlgqiqgn
       61 gelvasnsvq cfslsrlawy flrgsdvyni etltdtksam iirrvieqnr sqlkilsgma
      121 dksgfidqlt sqftefengq vtpddvedvm kqnqndiftg kigelnliyr kyteaieqya
      181 tnnfkldala dyldadlhsk hyhfyvegfs sftaselqvi kaillncgdl nislvldtpa
      241 vqpvektsfy arpantfnql ynlakdngvs yhskftktrr vsddigkled ywiqssgvsp
      301 iksshldsin svqiwkstnk qaevsavsty irqlvanqqy rykdflilar dlnqygsfie
      361 pfmaeneipa fvdlqrkmtd hpfkklvdll ftlvdhglqs edalallrte lmipekyqka
      421 diseyrqavd llenyvlang ttrkawlgqd feaqanldse idqniifdyq kineirnfik
      481 eiyqswseff teeqtakdaa tflfnfldkf gvfdrlgvwq qqaadqndlt sagqpeqvvd
      541 kfntildeyv svfgdeqfks defieildaa fesaqysqip stldavnise igmvqpnnrk
      601 itivlgatvn nmpgtsvsng iiadderqli sdnldsdkyl nasdevmnns epflhgltft
      661 tpstrlifty pnytednkqe dissyvtria ehfgitqqdi mlnpdplqte enevlryvgs
      721 aeaslnyvir vsraaldnka klsdqwtyvr nrllqedqtd sefalsslqy qnkpvdlnke
      781 tveklygnni dvsisrletf yqneyeyflk yglrlqprqi fevtsaqtgs lyhavldglv
      841 kllndqqvdi rnlsdqqlta yvadvfknel dkpenkifsa nermgfiskk aqdtllqlvr
      901 aikeqlgrnk fipratevaf grmnnakqdl pglsykipgg hvinvrgkid ridemsldks
      961 dylavidyks sghkfdfdsf ldgitmqmpt ylenlvanke qlssgqdvki agafyshiqn
     1021 pkilvkkgvd vekellkkfk ldglivddde llenldslvs gaslilpisk skakgitink
     1081 knaisnqdly rilnynrhli kqagekiysg klqinpfrds anrtglqfsd yrpilqfdam
     1141 lpeneyheii nhgreakkvv lkrieqilee etnna
//
LOCUS       WP_010623631             240 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010623631
VERSION     WP_010623631.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..240
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26889
     Region          5..240
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mkkitkdiia nsgivinqdk slysfnldtv llydfsipak rgkivdlcsg ngaiglslaa
       61 ktkakiylve lqtqlsklae qsinennlqq qvesinddlk nvqkyiahdt vdtivcnppy
      121 faknettkik dnpvlaiarh elktdlnqil hmsmillken shlflvyrpd rlaellkkmv
      181 enklqpkqir fvrthansea nlllvdaikt nhsaslkilp dlvmydgdsl tgeakeilhe
//
LOCUS       WP_010623739             243 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010623739
VERSION     WP_010623739.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..243
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27231
     Region          3..242
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtleikdltg gygqvavlkk esftvkdgqv vgliglngag ksttikhiig lltprggqil
       61 idgmslkqdv enyrkkiayv pempilypel tlkehidlti maydldhdkt wenanrllkt
      121 frldnklewf pqnfskgmkq kvmivcafmt earlfiidep ftgldplavk dlldiveekk
      181 qagcsvlmst hilatvqdha dkfillnngq vradgtldel kakfnmqdan lddiyikmsn
      241 edn
//
LOCUS       WP_010623767             275 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Companilactobacillus versmoldensis].
ACCESSION   WP_010623767
VERSION     WP_010623767.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..275
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31184
     Region          35..256
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mdfvdrnlsr hfeemiesst kglnlyqhtd ltdfpyaniv ivhglaehsg rydtlanffl
       61 shhmnvfryd qrghgksegk rgdltntdel pddckividi aksqfpnlpt fllghsmggh
      121 tvlkvatkyp givdgiiatd plsisfgpkv dgdpesyikn dlangvntdp rvikkynsdp
      181 mnlkeytvgl mntlrdstse lkqnldkvvd pilllhgadd giipvadsle iyqkfatkdk
      241 eihiyphlmh eilnepsrkw eiyeeilywi kkhsy
//
LOCUS       WP_010623841             329 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010623841
VERSION     WP_010623841.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37718
     Region          16..>238
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msyyleainq eknhrrilkn isleindnsi lailgpsggg kttllnilar idqpsygkfy
       61 ssdnivpkgi mifqdyrlfp nmtvfqniaf glrvkkksrs linircqkim ktmdiadlae
      121 yyphelsggq qqrvslaram ilqpklllmd epfssldenl rlemlnfvkk iqekfkmtiv
      181 fvthfkteay llsnqvaili dgqimqkgtp keiethpesf avakflgqan fipgeldenc
      241 fissiyrgpv eiksdsrqll yipfsnlitv dktdyfafea vvkeinwivn enrlvlnidq
      301 vqiqinsnss qfkigksykf yfkqlpvvf
//
LOCUS       WP_010623970             352 aa            linear   BCT 01-JAN-2025
DEFINITION  permease [Companilactobacillus versmoldensis].
ACCESSION   WP_010623970
VERSION     WP_010623970.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..352
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=37727
     Region          71..347
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mdsqisnnrn kqqivfavlf fvifiagify vkwwpyygka itaasthsig dsiiagvgak
       61 tvgvslqrgy tftiayflsv wkafvvaiii gslvqvlipv rwvrrylggt rlrntvigtl
      121 mgvptmmctc csapvtvgls kskasvnsim afflanplln patlifmglv lgwnftifri
      181 ifgilmviai atlvgklsnn kqvevdkggd fdpveenges llkrwwkafy tlvidsipay
      241 vvivfllgtf egvlfpaiqg glsggwlavi lfalvgtlfv iptageipii qalmalglta
      301 gptaallmtl pavsivslal lkpvlswksl sitfisvfaf glvaglvgaf vl
//
LOCUS       WP_010623991             271 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010623991
VERSION     WP_010623991.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..271
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30359
     Region          5..267
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,198,220..222,224..225)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mgyeliaidl ddtlldkrks itpknksmiq kalkqgvkvv lcsgrthnav idyakeldik
       61 gndqymitng galvetmdqk iltqhtlsne fyrrfvqfvk qnqlhynvvd lqaktytspe
      121 ewfdkytiaq ayenngglyi repdqlpsdf eitkaiingn eaeldavspl vhatfdkdyf
      181 vvrtgegfle vfprdvnkgr alkelaqsln ielsktiaig drdndipmik iaglgiamen
      241 aqpevkqvad tittdnnhdg vgnaiekyli k
//
LOCUS       WP_010623997             227 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010623997
VERSION     WP_010623997.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..227
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25515
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mlrvkkvskv ynrkfkalsd idldvndgef laimgpsgsg kstlinilgl ldndytgdyy
       61 ldnqeykdsd dvsmshirgd kigfvfqnfk llsnytvfen ieipliyskt qtitdrqtvi
      121 nevieqvglq gkennlpsel sggqqqrvai araivnnpqi iiadeptgal dsktgheimd
      181 lfrhlnetfn ttiimvthdk evadfamrtv yirdgklyqd qqsvvdk
//
LOCUS       WP_010624011             467 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar porter family MFS transporter [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624011
VERSION     WP_010624011.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..467
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50745
     Region          11..440
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(23,145,148,152,266..267,271..272,275..276,364,
                     368..369,373,396..397,400)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 mnkvkkipsg fiyffgsfgg ilfgydigvm tgalpfllhd wslqnsagvv gwitsavmfg
       61 aifggalags lsdklgrrkm ilisaiifai gsilsgisph dgqyyliivr iflglavgaa
      121 salvpaymse maparlrgrl sginqtmits gmllsyivdf llkglpeqla wrlmlglaav
      181 paiilfcgvl rlpesprflv knnrldearq vlsfirpsde veteikniqe tatdehvaek
      241 ntslktlfsg kyrylviagv gvaafqqfqg anaifyyipl ivekatgnaa ssalmwpivq
      301 gillvvgsll flliadkfnr rslltlggtv mglsfilpti lnmmipnmsp mmivvflsif
      361 vafysftwap ltwvlvgeif plairgrasg iassfnwigs flvgllfpim tanmsqeavf
      421 aifgiicllg vlfvrtrvpe tkghtleeie eegtrheskk aattqes
//
LOCUS       WP_010624115             718 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010624115
VERSION     WP_010624115.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..718
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=81630
     Region          14..639
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mrkiqnflnk rlgfmtllif flwiktviay yidfslgvad piqhfiliin piatsvlllg
       61 falyinraki syivmgliyf lesallygni lyyreftdfl sfntiagagk vskglgasas
      121 nmasyhdiiy widfiiilil flthfikidk rpfrklnafa itmtglmlfs lnlmlaecnr
      181 pqllgrtfdr ayivkylgfn sylgydsikt aqnsqvrssa vgtdmdnvlq yttdhyaapn
      241 pkyfgkakgk niiiihlesf qqfligqkvn gqevtpflns lyndkntmsf dnffhevgqg
      301 ktsdaetmle sglyglpegs fftslgtsnt fqaapailgq kegytsavfh gnigsfwsrn
      361 dvyknmgydy ffdksyydqd vqnstmeygm kdkiflsesa kyleqlqqpf yakfitvtnh
      421 ypfqlpdeda sndgfvkpdt dndvvngyfe tahyldsslq effqylkdsg iydnsmivly
      481 gdhyglsnsq npalapllgy nadtwnnfnn tqlqrvpfmi hmkglkggvn htyggeidvl
      541 ptilhlagin tkqyiqvgtd llsknhssiv afrnknfvtp hytvlknsnd gynvysnktg
      601 eeidlstnpn lkakvkkwqk avnqklqisd tvnnknllrf ytpngfepid pknynyqnei
      661 nhlldtrsal glkstsiysk nnnqsttsmy htdapelggd rssidnwdyf kknqknqq
//
LOCUS       WP_010624138             353 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein
            [Companilactobacillus versmoldensis].
ACCESSION   WP_010624138
VERSION     WP_010624138.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..353
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38637
     Region          7..345
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 madqneiikl kdidvtfhne gktieavkdi sltvdrgdif giigysgagk stlvrvinll
       61 qrptagevvv ngqnmlalss kelrqarkni gmifqhfnlm nsltvygnid fplrdsklsk
      121 serkekvdhl ldlvgltdra qnypsqlsgg qkqrvgiara landpevlis deatsaldpk
      181 ttkeildllg rlneklgitv viithemdai kqicnrvavm edgrlieegs lltifgkpqq
      241 kltkdfvdts tqvksaleei ktsgivndls grliqlkftg dvtnepivvg lykrfnvsas
      301 ilfsnierls gttigimvla lsgddskvqe avdylngldi svkeielnes eea
//
LOCUS       WP_010624144             270 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Companilactobacillus versmoldensis].
ACCESSION   WP_010624144
VERSION     WP_010624144.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..270
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29873
     Region          1..266
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkklrgfilv avaifsifvl vgcgnnssek tvkigimtsd dpiwkpikqk lkkqginlkl
       61 vefndfnqpn qslaqgeldi nsfqhiyfmn nwnkahntnl vsigttfiap lrvystklks
      121 idelksgdkv tlpndatneg ralellesag lielkktalp tvkditkynk kititpldaa
      181 qtahslddas aavvnntiaa sanlpedevi ykekvtkksk pwinviatdk knkdnptykk
      241 vvkayqsean aknikkqykg ttipawnlkl
//
LOCUS       WP_010624150             385 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Companilactobacillus versmoldensis].
ACCESSION   WP_010624150
VERSION     WP_010624150.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..385
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41577
     Region          180..374
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkkkiitsll isasfiggia fntnqvkads negtvttlrq arlynskgdl vknrslaant
       61 awytdgkssl nnvgtayrvs tdeyvktddv qfsdnnsssd tvvknsgtle isyaptngid
      121 lyqgygpnka atgtkltngt qwkflqkvid sngdawyqig ndqwvsgqyt kvtntsldes
      181 aakvwdpnfa alkitadspv ysdsnyssat skwlytgaia evdstvqagg evwyeisngg
      241 wvpsstvsti sttrptvqln gkskdqvisd vinvakdqlg kpyvwnakgp dsydcsglmq
      301 yifrsatgqn igswtvpqet agtkvaisdl qpgdlvfwgp egasyhvaly lgndqylnal
      361 rpgtnvkidt isssfepsfg vrifk
//
LOCUS       WP_010624198             294 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624198
VERSION     WP_010624198.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..294
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32393
     Region          4..282
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,213,235..237,239..240)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mikiiasdmd gtllndemmi sqrnieainh atengidfli asgrqldeak pflkdqvhpg
       61 fitlngaevy dknetlvssn pittasvqai tnylrqkgly felitdkgvf snslkkrttn
      121 iaellsilnp tttykkaled tkailkhakt iyvddydqil ndndhkimki lvfdsrqkea
      181 fdplkdslkd lddivitsss pnnleinskq aqkgialmey arqknvkpee vmaigdnlnd
      241 lsmikaagig vamenavpti akaadehtas nvndgvaqii dkviennktv gnre
//
LOCUS       WP_010624212             348 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624212
VERSION     WP_010624212.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..348
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37888
     Region          27..343
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mtinsnlell dlvapdfikt vekrfrilqs iklmepvgrr vladdlnvte rslrtetdll
       61 knqgliissk sgmsltktgi qangqlnkll adfqgtalie qqlsqklgia rcivlpgnsd
      121 kqyrvidsfg qrlnqllgti lpngknliav tggstlarva rnlspilskn rdllflparg
      181 gvgesviiqa nsvcaemanr thgqhralyl pedisersfe slqkessiks vldliykcnv
      241 vvhsigtasv maerrnlsdv drlkitnsqa vaeafgdffd qngqlvykvp riglhvrdla
      301 niehvvaiag gaskasaika ymknapahtv litdegaskm ilrdnplk
//
LOCUS       WP_010624219             213 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624219
VERSION     WP_010624219.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24093
     Region          5..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtsqkerqkk teeniihall eagknktlaq isvsditris hinrgtfylh yldkndlvnq
       61 vtknfndkve lilqtemgds mdyryfskde pypvimnlvd lvaenkelvr fmlgtngdpe
      121 fyptiskelk tailndlkrv kgnndfsagi pneyairlit smimtiiktw vdgegdltne
      181 mvakvimkgl ylspyemlgi sgnmgnkkgn eks
//
LOCUS       WP_010624229             299 aa            linear   BCT 01-JAN-2025
DEFINITION  ACP S-malonyltransferase [Companilactobacillus versmoldensis].
ACCESSION   WP_010624229
VERSION     WP_010624229.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Marcella,A.M. and Barb,A.W.
  TITLE     Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as
            templates for engineering
  JOURNAL   Appl Microbiol Biotechnol 102 (15), 6333-6341 (2018)
   PUBMED   29858956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..299
                     /product="ACP S-malonyltransferase"
                     /EC_number="2.3.1.39"
                     /GO_function="GO:0004314 - [acyl-carrier-protein]
                     S-malonyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32861
     Region          2..290
                     /region_name="FabD"
                     /note="Malonyl CoA-acyl carrier protein transacylase
                     [Lipid transport and metabolism]; COG0331"
                     /db_xref="CDD:440100"
ORIGIN      
        1 mwifpgqggq krgmlkdvpt emitrvkelt gieltdssqs yqdsvqiqlg illlqlfnir
       61 qlqqigqkpd avaghslgif aaavtadvis eddaikivyl rstkmkesyp sgygmgaivg
      121 ltrkeveaiv tqvnsktepv ftsnqnaelq tavsgsitgi qkvlelakkq saskalllkv
      181 pvpshsplmh svaddlekgl akvdlkdpkc tylanfngha thkakdieyd minnliypvy
      241 wdtmidvaqe lgvdttlevm pgatftklvk akfpdfrtit mnsmnlddie fllnkwkrg
//
LOCUS       WP_010624239             430 aa            linear   BCT 01-JAN-2025
DEFINITION  alkaline phosphatase family protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624239
VERSION     WP_010624239.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..430
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48316
     Region          1..414
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 msadqnlvvm sldslgfrdi rehqaelptl nklvnvgtwv ksvtgiyptl typshtsiit
       61 gqypkvhgiv nntkiqpqrr spdwywyqkd vqsptvydla nqagmktaaf lwpvtagski
      121 dynlaeifpn riwtnqvlvs lkasspvfll emnhkyghlr ngikqpqldd fitacavdti
      181 knkqprltli hlvdmdsmrh rygvrsdeam qalqrldkhv aqliqatkda gtfeqtnfvv
      241 lgdhyqinvt kmihlntlfa qkgwltanad qtfkkdwqvm aktcdgstyi ytkdfeemds
      301 lktlvknveg vekvysasea aelgadpacs llveaksgyy ftdeserstv vervdpatlg
      361 qpdryhgvhg ydprksdyqt tlvfngpain sghtvekanl vdeaptfakl lglkfenqia
      421 gqciedvfrk
//
LOCUS       WP_010624276             212 aa            linear   BCT 01-JAN-2025
DEFINITION  copper homeostasis protein CutC [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624276
VERSION     WP_010624276.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..212
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23059
     Region          4..204
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mykeiavenf tnipkavlag adrielndnl avggttpslg vlqetskylq eksvplvemi
       61 rprggdfvyn dlelkmmead ifqaqkmgid avtfgaltsd geldedalem migassgmqv
      121 vfnmafdqik eenkadaidw liehevdril thggpletpi setlpdikkt ielaqgkiei
      181 lpgggitsqn cdeiaqqlnl ntlhgtklid ln
//
LOCUS       WP_010624270             806 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK [Companilactobacillus versmoldensis].
ACCESSION   WP_010624270
VERSION     WP_010624270.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..806
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=88552
     Region          <325..799
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 marrkttrta ktksrrtskk tsiddvrlik siiglvlivf silglfqlgi vgkffdnlyr
       61 iivgdsypvl lvisifagaf liatgklpkm npkrnfgfif tyagalvflh klmftkldly
      121 hnynlitwnt itadmgkssv shsvgggmig sylyslfmpl fsnvgtvlia alliiigilm
      181 lfnvsmeqvs qvtkkilaha knslvsvkes fssryenlve nrksrsdekt kpakdiered
      241 skyqdvnsfa kdkksaddap rdedtgfhid lpsgsddyga spkpqaskae imskpygidg
      301 skdkdlptpr saagehnisd ddyqlpssdl lkqvprvdqs aevklidenk dklkrtfksf
      361 gvdvevkkas lgptitkyev qpaigvkvsk ivnladdlal alaakdirie apipgksfvg
      421 ievpnktiss vsfrditenq qdktsplivp lgkdvagnii eaditkmphl liagstgsgk
      481 svaintiitg ilmkakpnev klilidpkmv elnvyngvph llipvvtdar raagalqkav
      541 temerryklf aetnhrnige yndevaefnk taeddqkmek lpyivvivde lsdlmmvagh
      601 eveaaivrla qmaraaglhi iiatqrpsvd vitglikani psriafavss gvdsrtilda
      661 vgaekllgrg dmlfqpigks kpvrlqgayi sedevenvvn fvssqqqaey dqdmipsdvt
      721 edggngekdk pndeywddai dlivhqqsas vsmlqrrfsi gynraarivd qmeekgivgp
      781 segskprkvl ltpeqlenir kkqven
//
LOCUS       WP_010624287             179 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010624287
VERSION     WP_010624287.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..179
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=20199
     Region          4..178
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mvkkitvltg sphkngtssk ladafidgvn dksalyrfda glnaskihfl kidenestih
       61 dddliskevm pkildsdvlv lctslyyygi naelkaiidr fyeynhelkd dkdvyvlisg
      121 fdpgdknsaa yrslieyfdq lckymrwdlk geilgqdswn esaleehvse afqlgktvn
//
LOCUS       WP_010624342             289 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010624342
VERSION     WP_010624342.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..289
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=32718
     Region          1..280
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mptavvtdta ayltpeqikk yhvtvlpitv ilgeqqyket eeldlptfyn ylktekdlpt
       61 tsqvsmgqie qaydrlaseg ydsiisihls sgitsfmdnl rmfcktydka kiypfdslva
      121 sageadlvll aaalvqkgkt peqimpklee lrstrdvyfa vddlkhlmrt grlsnrsafv
      181 gnllnikpll tfdpegkiva idkertmkrc lrmilqkmqn nfekvdypil atvidannee
      241 vaqnwvdqlq etfpdiriar sqlgpaisvh tgektmgilw drdwktmld
//
LOCUS       WP_010624343             502 aa            linear   BCT 01-JAN-2025
DEFINITION  multicopper oxidase family protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624343
VERSION     WP_010624343.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..502
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=56865
     Region          80..502
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mktkrvvlfi flivlvvlgl kqtngvalaa gmmsgdhsmm nddddsdsns hskmmkehnv
       61 dlkdadvpmq elnlpkvlkp dkqtkhdvyy tviaqkgktd fhdggkltkt lgyngsylgp
      121 vlnlkrgqtv hikevnhlde kttfhwhgai isgkadggph epvkpgktkk isfkvrqpaa
      181 tlwfhphpsg ttgkqvykgl agliyihdrk skclslpdny gvddfpvvvq drtfdknnql
      241 nykkdynadr tlgknlmvng tlnpyinvtt ryvrlrllng sntrnynfyl nhhqkmikia
      301 gdgsflakpv kikklqlspg eraevivdth klnvgsnlql ktggmkaltm klnqqrdnlt
      361 slpdklsdrk alkvpkknvn heklvlsgms nmvringkky npdridihak rnqqqiwtie
      421 nkkemmmnmi hpfhlhgvqf riisingkkp sksqrgfldt itlnpgdkyk isfrfeekgl
      481 ymyhchnleh eengmmgqvl ve
//
LOCUS       WP_010624344             157 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside 2-deoxyribosyltransferase [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624344
VERSION     WP_010624344.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..157
                     /product="nucleoside 2-deoxyribosyltransferase"
                     /calculated_mol_wt=17259
     Region          5..157
                     /region_name="RCL"
                     /note="Nucleoside 2-deoxyribosyltransferase [Nucleotide
                     transport and metabolism]; COG3613"
                     /db_xref="CDD:442831"
ORIGIN      
        1 mkiyfanglf sqadrmfnay vvdkirkmsd dievylpqen gdindktkfa dsikiaeedn
       61 kelldsdlvv avldgeiidi gvaseiglaf gkeipvlgly tdlrqhgaen pekleavaqi
      121 genpfqyvnt ytigliklng svvnnvddll agiedyl
//
LOCUS       WP_010623269             630 aa            linear   BCT 01-JAN-2025
DEFINITION  terminase large subunit [Paucilactobacillus suebicus].
ACCESSION   WP_010623269
VERSION     WP_010623269.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..630
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72339
     Region          27..601
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mkidltqthd vigayrsidy dnvrsqytda gtvycfdvld gkvmagydik lacfrhlqdl
       61 srqntsefpy hysstevtki lrfasicpei ktkrpvklmg wqkfvlamlv gwrnenddkr
      121 ftraiisvar hngktylmsi itlysylies lgessqqflv ssinfkqtsq lmsyvkqmli
      181 dlaqkepfkd liddldinqk slasqsdiiv spktfskila vtyesgqyds fhfktaigde
      241 fadpkvadnq ktskitsgqv dvtnkqfiqi ataypdatvp frqdeqriva kmeadykreg
      301 enylvlnwsq dsedeiykpa tweksnpllg maekhdklil diknerdndl lagnvidfqn
      361 ksmnvwtqqs vdsfltlddi eravisdfdr dnrqvyigfd ysmfsdntal afiypyieng
      421 kkkwhveqhs fipwqkagsi dikekqdgin yrelakqgyc titshpqgli nneqvytwml
      481 eyierhhlev iffgydawga tpaikqmein tsypleairq rtselkdptk flqkifvess
      541 vtrlddkima kallnarive dkigiqvdka qatmkidvvd aiidalyqgm yhfedygivn
      601 dksqevsrmt teqieawlts sesgmtdgdv
//
LOCUS       WP_010624358             153 aa            linear   BCT 01-JAN-2025
DEFINITION  GtrA family protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010624358
VERSION     WP_010624358.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..153
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18267
     Region          1..129
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mkmlkqhref lvyclfgfla svlniaifnl ahnnlamqlw lantiawfis nlfsffvtky
       61 yvfqtemtdy kklfheggcf llsrifslvi ddlfmivavl ilpwnnliik aidqiivglf
      121 nyysskwifd ynnrhlmerf knlrtkrqke rqv
//
LOCUS       WP_010624377             408 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Companilactobacillus versmoldensis].
ACCESSION   WP_010624377
VERSION     WP_010624377.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..408
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46162
     Region          2..406
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnkleipklf qdyfkennfe qmtkiqesvy lpfkegkdiv amaptgsgkt lgfvmpmiet
       61 lvpkdglqil ilepsqelai qvrtviqpla kavgcsvqav tgganpqrql kklkekpeil
      121 vatlgrlkel tdsrkvklgn vqtvivdead emlnetklds vrqtldlmpa dvqmtffsat
      181 gneifknmsk wfgkdfllid qrydrsytag ikhyfintgs dgmkntlire mahnkkflgi
      241 vffnnsrslh kiisdlehsk tnfvaldskm ssqqrktalq lfssgkvnlm lttdvaargm
      301 diddvttiin ymiprdnsey lhragrtgrm gksgdvvtfg nshdfrnlqt fndleikkvf
      361 lnhdgtfsdk atyhknkqns askskprnkk rlrdqknkgk rrvkkplq
//
LOCUS       WP_010624431             270 aa            linear   BCT 01-JAN-2025
DEFINITION  SPFH domain-containing protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624431
VERSION     WP_010624431.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..270
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=29853
     Region          3..252
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mfgikivhqn hkglveflgk yhhsvdaglh fyipflqkiy pvslamnplk lpdysiitkd
       61 nadvrasltl nyhvtdavky ryentdsves msqlvrghlr ditgrmdlnq algstskinq
      121 elanaigdlt ntyginvdri nidelkptps iqdsmdkqlk adreriaais kaegesksie
      181 lttkakndal iatanaqaka trtradaesy rieqmnqsld kakegyfknq tinafsqlat
      241 spantvvvsg dnvsdlgkip vikkmldnqk
//
LOCUS       WP_010624433             254 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010624433
VERSION     WP_010624433.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..254
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=29193
     Region          2..>152
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mkilgilash kehglnaeml qnvldnvgeg vetetiylen yhitphkyhe dnpvlnqlad
       61 klmesdvwvf gaptywrecp gllknffdcm rpkfvyfkdn gdtipgpfkd khylsisscy
      121 msttenfltg itdetfktid rvmtaagvik ageivlpntf gmkeipekkk dlcakyghki
      181 skkqekddst vkryiqlffm iavmalitmg iqlplkaimp idnfwvnyis ftiiffvllg
      241 cilhymtfvk hrrr
//
LOCUS       WP_010624438             283 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010624438
VERSION     WP_010624438.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..283
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=31202
     Region          1..280
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 maifkeyskk ifaalfygit saigiqlllq pskiytvgvm gasqlfvnll ikfihvntqv
       61 ylwyfllnvp lvilswiklg kkftilslis iasasifilf iplhpltddp mlasifggvm
      121 vgigsgicfr ygfstggtdi ialiiqkskg gtvgqvafsv naiiiliagv vfgwelalys
      181 ivsifitnmv idrmyiqqqk itvvvyshei dkiskellkt lnrgitmdyn ltgaysgeqi
      241 gsitmvvtkf qlffvkqtvq kidpkafini qptigimgrf ndn
//
LOCUS       WP_010624480             168 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624480
VERSION     WP_010624480.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..168
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19352
     Region          8..>92
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          78..158
                     /region_name="TetR_C_8"
                     /note="Transcriptional regulator C-terminal region;
                     pfam14278"
                     /db_xref="CDD:464123"
ORIGIN      
        1 mvgiknnrra kytqsvikdt vlslledkpv snisvtevck iadinrttfy ryyddiyqci
       61 dsianeflss lkvpetlspi dsmeqlievf yhnrklsnlv fvegktkiln efynkvdssn
      121 dyqkiyislg mqgilkkwvk dgmpetphql aaiiekifya ddlqkfhp
//
LOCUS       WP_010624489             195 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Companilactobacillus versmoldensis].
ACCESSION   WP_010624489
VERSION     WP_010624489.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..195
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=21307
     Region          11..194
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mtypqldldn atgtkvtivt nhgeikiqlf ddlvpkaven flglakkdyy ngvifhrvip
       61 dfmiqggdpt gtgaggesiy ggqfedeftd qlfnfngals managpntng sqffivsnen
      121 mqkrilsqms aagypeevia eyknggtpwl dhrhtvfgqv isgmdvvqni skvkrdaadk
      181 pkedvvieki disen
//
LOCUS       WP_010624491             193 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624491
VERSION     WP_010624491.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..193
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22586
     Region          56..142
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 mitrgneviv iltkkvvtkd lpefqkikel yfqafpaeer vpwswlyhqs kkqfiefiaf
       61 ydqdefvgia ynvtqkdlty ifylavdpqi rgsgyggkil adlakmyqgq rfclsaeapd
      121 seadnnetrl rriafyqrng felshktale kgvkytmmhr ngnfenaeyq kiiayfagff
      181 kfifkvefid enk
//
LOCUS       WP_010624542             180 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624542
VERSION     WP_010624542.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..180
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20128
     Region          3..175
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 marqvilfva qsldgyiakl ngsvdflnqq tahgvdidre ydkltehvdt vvmgrktysq
       61 vvnqlspeiy pyvdfqnyim tskpapsten lhfvsgsvdq lveklkkqtg kdiwiiggss
      121 iitplvnanl idvyqigvvp eilgegiplf phevkthhle lisaekinqv ayltyhrlhe
//
LOCUS       WP_010624559             278 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624559
VERSION     WP_010624559.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..278
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30984
     Region          19..277
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mksfnifkiv qkmfskidwe alaehvttvv lqlifltivl llinwigkkv irhifnnnwr
       61 ptakippkkl ntiytlvlnv fkyvlfffwi yavlsalgip vgtliagagi fslaiglgaq
      121 gfvsdmvngf filieqqisv gdmiktnnie gqvtyvgirt tqvrsidgtl nfipnrnits
      181 vsnksrndmq ammeipiyts gpidkitdiv tdinqgldiq alqitkrpyi vgfsnqndgt
      241 lvlqvaaytk pgaqfqvrnd llkqyltalk aakidlpk
//
LOCUS       WP_010624586             508 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease/substrate-binding protein
            [Companilactobacillus versmoldensis].
ACCESSION   WP_010624586
VERSION     WP_010624586.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 508)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..508
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56422
     Region          2..202
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          237..502
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(243,245,294..295,298,341,343,422,446)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mntlmqtisa qhgeilnsly ehigisfisi iiaiviavpl aillrnhrrw geamlqvtgi
       61 iqtipslall glliplvgig tvpavitltl ygimplyqnt ysgltnidpn leeaaeafgl
      121 srwkqlqrle fplalpmiis girialvmii gtatlaafig agglgnyiml giqqnnnsyl
      181 viggvlsavl aflfsallky iggtskriyv sgiivlliml gfggtkayqa mqpekvslti
      241 agklgsepei lmnmykdliq ednpqtdvtl kpnfggttfl fkalqrnqid iypeftgtil
      301 eslvkykgnt pkdpnkiyqv aseqiqeqhq mkflkpmeye ngydlavtke fskkygvtkl
      361 sdlervndkv haafdpdfsn ladgyvglkk kynldfakvs tmeptlryka iadrrvnlvd
      421 gyttdpqvrq yhlvvlkddk hffppyqgap mmkqsfakkh pqivkslnkl sgkistedmq
      481 kmnyqvtvkh kkasvvahny lkshnlie
//
LOCUS       WP_010624588             512 aa            linear   BCT 01-JAN-2025
DEFINITION  multicopper oxidase family protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624588
VERSION     WP_010624588.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..512
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=57784
     Region          35..463
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mtetvttdyf fdekafdkqd gayiplrvad apekplnvpp llkpdketkd dvyytvtaqa
       61 getqilpgak tktwgynnsi lgktivypag khihvtlqnh lpelttfhwh gllvtgpyvd
      121 ggchapvypg eakqidftln qpaattwlha hpcpstaeqv whglatmvlv tdkhsselni
      181 pnnygvddip vvlqdrifhe nnqldyhady npdgvtgpta mingtvnpyf dvttqklrlr
      241 lldganrrew rlhlsddlqf tqiagdesll phpikmthlm itcaerqeiv idfegyhegd
      301 evtlfsddtp llkfrihkfa kddsvipedl ftvkaptvdp qtpvrkvvms gmdegveidg
      361 kkfqiqrida tqpvgkaqyw divnsndpkq gmvhpfhmhg teflvisrng hepypnehgf
      421 kdtvgvnpge tvrilvrfdl pglymyhchi lehedggmma qiqayepdkp mpkyklmdme
      481 tlmnafaker gikpedlwma gmdsykklgm km
//
LOCUS       WP_010624642             737 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-galactosidase [Companilactobacillus versmoldensis].
ACCESSION   WP_010624642
VERSION     WP_010624642.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 737)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 737)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11245829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..737
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=84212
     Region          29..284
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          290..636
                     /region_name="Melibiase"
                     /note="pfam02065"
                     /db_xref="CDD:307952"
     Site            order(337,368,412,477,481,527,546,549)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          651..733
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mtinvsaepn vfhlqtdhts yifqimengd lgqvyygali hskdsyqnls qreihdatpa
       61 vseelndlqp elvkkeyagf gkgdfrypaf qliqgngsrv sefkyqsyki vdgkerltdl
      121 pasfddqadd vqtlmvtlkd sltgmllvln ytvfphqdvi vrsskfines sqdikincay
      181 saqidlpdad ydliqfsgdw arerhlyrnh lrpgsqgvss lrtasshqqn pfimlarpqa
      241 nedhgdafgf nliysgnfkd sievdqfevs rvliginpde fswkvtagns fqtpeavmsf
      301 tdqgfnrlsq qlgdfydqhl tnqnfvkkdr pilinnweat yfdfnetklm tivdqakklg
      361 iemfvlddgw fgkrnddtts lgdwdvdlnk fpdglghfsq rvhdeglkfg lwfepemisv
      421 ksslyqehpd wllgdknaql tpsrhqfvld msrqdvvdyl fnkisriiqn tkldyikwdm
      481 nrnitesfsd slpadqqlel shryilgvyd lyarltetyp dvlfescasg ggrfdlgmmy
      541 yapqawtsdd tdaverlkiq ygtsygypqs mmgahvsavp ndqngrvtsl qtrgnvafyg
      601 dlgyelditq mtaqeleqvk eqvafykqyr hlfqygkfyr iddpfggdgn itswqvtsdd
      661 qkqaiaaryq llnhpnapyq rqyfkgldpk qlytvnsgse kfygdelmha gyfvatpese
      721 tgyskdfssq lfivsav
//
LOCUS       WP_010624665             434 aa            linear   BCT 01-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010624665
VERSION     WP_010624665.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..434
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=47928
     Region          1..431
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mskqkfdtvr ihggydpkkh nnaaqipiyq stafslgtaa egaevaaglv sdsftysrvg
       61 nptvhtleqr iaeldggids vavgsgmaai tytilnvaeg ggriiapydi ygaaldefqt
      121 lfpkygiifd lvedindier ikslikpdtk aiyaesvsnp iinitdveel akvahesrip
      181 liidntfstp ylfqpikfga dlvvysstkg inghgnvvsg lvvdggkfdw skdkfpqfye
      241 aeyslknsky ptnysfanvy gnqafikrlr mkylrlmgav lgpfdaylem lgletiserl
      301 dkevatgkki aeylnnnphv krvyypglpa snqyelaqky fpkgigsils feldgssedt
      361 dklidsmelf lylpnvgdsr slivnpskit hrevpeerrl kdginnqllr lsigledsdd
      421 likgldnain ktfk
//
LOCUS       WP_010624732             477 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Companilactobacillus versmoldensis].
ACCESSION   WP_010624732
VERSION     WP_010624732.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..477
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51369
     Region          34..469
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(35,67,117..118,120..122,125,145,148..149,152,282,
                     285..286,289..291,294,322,326,378..379,383,387,403,
                     406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mrnkglhlnm tnkvvallsl glfsllssms gsstnlalps isydlhisnl qstwvvqvam
       61 ivasitfvlf gyfgdilskn fvfivggfvf ilgslitgaa lgflmiilgr ifqaigfsmi
      121 manslgivse efddnsrgqa latvsmfttv gqiagpaigg miisvsswrw iylinvplcc
      181 ivmifslksl kfphytlpkl mkslkgfnci geiifaagis ilflsglyfq hgvhgiwkgl
      241 ilvilgsais iaaffqdqha kqalipirlv rnvkylmsif illlvmlvna mtnillpfyl
      301 qsfngmspfy sglimmgqsl amlattpiag yladhkdrmk ltivgllill lsqigyalyp
      361 akvnlvlimv pvllngigia vflspnlait mgsvdkkvlg vagsinsfar tlgatvgism
      421 tsallfsqll hvahitpntg mafmhafsnt lwigvlvnvl avivviarkf itpktak
//
LOCUS       WP_010624733             167 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA thioesterase [Companilactobacillus versmoldensis].
ACCESSION   WP_010624733
VERSION     WP_010624733.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..167
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18673
     Region          5..146
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mksikckdtl sitnhrvfas dlnehdtvfg gqilsaidnn ssiaasraar ietvtasvdq
       61 vnfmhpfvlq dsrcvesyvt gvgstsievf tkiigehlkt gerflgltcf stfvvtdrsi
      121 klpeiipvtd eekyvcsgyk qrkiersekl keqvklnqhm slkfpwd
//
LOCUS       WP_010624747             244 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Companilactobacillus versmoldensis].
ACCESSION   WP_010624747
VERSION     WP_010624747.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..244
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=25193
     Region          32..233
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mntkfrkslv sltaaaslav tgfgisgltn nasshvaqaa tiikdnvpsv vransqvklf
       61 tqpsnssdla grqlavgsdw avvaeakdes gniwyavgnn awvkgvdmta dptstqaatq
      121 apssestvds lintakslvg tpyvwggktp sgfdcsgfts yvyqqatgks iggytvaqes
      181 agthesvqsa sagdllfwgs egstyhvgiy lgnnqyiaap qpgesvkvan issyfmpsfa
      241 vkvl
//
LOCUS       WP_010624748             183 aa            linear   BCT 01-JAN-2025
DEFINITION  guanylate kinase [Companilactobacillus versmoldensis].
ACCESSION   WP_010624748
VERSION     WP_010624748.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..183
                     /product="guanylate kinase"
                     /EC_number="2.7.4.8"
                     /GO_function="GO:0004385 - guanylate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006163 - purine nucleotide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21065
     Region          2..180
                     /region_name="Gmk"
                     /note="Guanylate kinase [Nucleotide transport and
                     metabolism]; COG0194"
                     /db_xref="CDD:439964"
ORIGIN      
        1 mknkvivitg asgtgkttis ryledkyrip hvithttrap rtgekngvdy yfetkesfdk
       61 nhfleqveys gnkygssveg leqawqkspl vsivvdskga iayqkrypeq tiilfmkadl
      121 etvtdrlkkr gdeferlkqr iaseenrrdf eipkelygny yeiinkdikn tkdsvdgivq
      181 kie
//
LOCUS       WP_010624756             346 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Companilactobacillus versmoldensis].
ACCESSION   WP_010624756
VERSION     WP_010624756.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..346
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38911
     Region          108..322
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlkatkitsn kvqrehmknk lkktikpine dtfggeysrd llpnlqkfat akqldddlvq
       61 lrsgnkvvns kdltitdilv aektieywgr tvsleqfipk nadpekvliy fqggsfyggq
      121 iqdvhnmlkl iaeksqvqvv nvdyhlapes pypnaifdgv avslyfqkql glkkiilsgd
      181 saggniglav nkllgklgyk tsianvllyp vvtlsddetk alwdydefpi kkeqilirnn
      241 ygklfhqlna vmrkyylqnd edpshslisp lhddvkndpn tllivgefdf frlqdeqyal
      301 glqahqtqvn fiqyngmaha fapmvgvlpq addaaneiak fvkniy
//
LOCUS       WP_010624770             302 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Companilactobacillus versmoldensis].
ACCESSION   WP_010624770
VERSION     WP_010624770.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..302
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34032
     Region          52..302
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mtitiiilvi vlllivliln alflylqkrn ssalgtdapp vvldpgldea tdqflkmpre
       61 ewtitsnkhk lygwftkake pssttiliih gfavdhasld ihaqmfsnlg ynilqvdnqa
      121 agksegkyqg fgylesidtk kwidellskr pnekivlfga smgaatvmmt agkslpenvk
      181 aviedsgyts mldivnyhfk nrykisgrfl lkmisivaki rsgyfygqad cikalenchl
      241 pilfmhgkld tavpyfmrde llqvgdfpke syaldkgvhi rsyyidskny qhkvtnflnq
      301 yl
//
LOCUS       WP_010624786             924 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624786
VERSION     WP_010624786.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..924
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=101599
     Region          32..735
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mknlwnsivn sikgikswsd fatkanltie virrivlyii aglfvmlslt vglgfgyvsa
       61 ltnqvavpsk hemrtqlqdv nnstslyfad kqkvedlqkt ltgkrvsldn vspylkkavv
      121 atedsdfykh sgvepkslfr ailsditgig tqtggstltq qtvkmqllss ettwkrkave
      181 iflamrvdky ftkdeiledy lnaatlgrnn kgqniqgvqa askglfgkda adlnlaesaf
      241 vaglpqspsi ytpydnkgki kkdislgmkr knivlfrmyr dkkiskaeyn eaknfdlkgd
      301 flkpdkaknk kikygyvynl lteqtrtili krlakndgis ykalkkdksl yqkyytqadt
      361 elhnkhyrvd stinkklynd lneqaqgfqd nlgtthtdna tdpntgksik vkepvqngsv
      421 lldnksgqvl afvggldfkn sqlnhafdtq rspgssikpl itfgpaieng migsqsmlad
      481 fktkykkyap tdygetiqnr fisaretlee synipsvnly nyirqngvss kqymekmgin
      541 lsddeykqlg itlggtatgv tvlqqasafs tfankgthvn pyvvdkitdp tgkviyqhkh
      601 kkkkvfsket syimqnmlhg vvtkgtasal syesnfstkn lfgktgtsnd yrdnwfigst
      661 dgmtlaswig ydnfygnnyn lasnstdinq elwsrmanav ykedpdvmnv hkkfnrpegv
      721 ssykvdketg tntgtieyng itskvnqhtt nslyykgqpk nmsydsfaig akpknyrlfw
      781 nnyfgrnnsy gevkqlgkns ksakeiasen gsgrtsgfsn stnsnqssev ttsgdsstns
      841 nsrgstnstt sngnqetgtg sgngnnrtss snsngttmtd estgnssgnn sesntgssst
      901 ssgsstnsgn gssgvmngli ggte
//
LOCUS       WP_010624815             314 aa            linear   BCT 01-JAN-2025
DEFINITION  ketopantoate reductase family protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624815
VERSION     WP_010624815.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..314
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35742
     Region          1..299
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mglryglllq dagfpvdfve iwdksietik eqggvyqsrd rqnkhlvpvn iyspedyqgd
       61 pdvwivfvkq mqladalkrc qhlfndkqyv vapmngighi eklnqyfdse kvlsgtamia
      121 tvlngpgdvd fmgaagsgsm klvnqnetpd emtykivdef kqanlnpdlt tnfmgtlmsk
      181 vilnsvlntl ctmfeirmge fiqaptaekl gqqlvdeafd vceraniqll ntrqqewqti
      241 ktasetsmpl hypsmyqdmh knrptevdyi ngyiydlgvk hhyeasthdy lrnlvhlaef
      301 aknfdeekfl aske
//
LOCUS       WP_010624820             208 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase
            [Companilactobacillus versmoldensis].
ACCESSION   WP_010624820
VERSION     WP_010624820.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..208
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=23589
     Region          118..205
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mknstnqllt iltylallfi stilsmlrlt ghpffaivtv aaivatfimv ylthtngknd
       61 feqtfdwhrf vtwsligaig avviqfglgl ieqvllhlpt ssqntmsllt svkgypyyli
      121 yilfcapime eivfrrvffa nlikptniyw ailissllfa fmhqdtrfvi ylvmgawfcf
      181 vyyrskniyv satshiimna vvlglsla
//
LOCUS       WP_010624847             158 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Companilactobacillus versmoldensis].
ACCESSION   WP_010624847
VERSION     WP_010624847.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..158
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17563
     Region          11..153
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mkfseeknls fmqmaldqaq laqadgevpi gclivdnqts eiiatgfner eqtqdaikha
       61 eiiaiekacq kvgswrleht slyvtlepcp mcagaiinsr ieevifgayd pkagsvgsin
      121 nlfeekrynh hpdflggmla ddsasllqnf freirrkk
//
LOCUS       WP_010624828             639 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Companilactobacillus versmoldensis].
ACCESSION   WP_010624828
VERSION     WP_010624828.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..639
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73029
     Region          6..532
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          564..629
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 millqaqnit knfgtkklfs nisfevqdns riglvgrngv gkstllkils edesytsgni
       61 alkkdtnigy laqdsglnsd neifkemeav fdylkvqekq mrdleeklad nsvndydqll
      121 kqydqlqttf rqengysyqs eirsvlkgfg fdedvwhekv stlsggersr lamakmlleh
      181 hdillldept nhldietvew lesylknyrg alvivshdqy fldkvateiv einhhsanhy
      241 sgnysfylqe kkrnqevewk hyqeqqaeik kteeyiqkni vrasttkmaq srrkklekmd
      301 vmdkpdsdqg sahfsfeidr esgndvllik daaigyqadq vmsapinldi kkgervgvig
      361 pngigkstll ksvldqipll agsyqfganv qtgyydqnld sldpkkdvlh eiwdrhplld
      421 eqiirnilgs flfsgddvlk pvaglsggek arltltklsm ehdnflvmde ptnhldidsk
      481 evledalkrf agtvlfvshd ryllntladr iveitpsgsk tylgdydyyv ektteaepek
      541 nisdksnnts ekkieyqqsk eqqkaqrklr rqvedlekqi snldeknaai qkemtkpenl
      601 tsytklgdlq keldenkaaq skleddwtek sldlesyed
//
LOCUS       WP_010624970             453 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Companilactobacillus versmoldensis].
ACCESSION   WP_010624970
VERSION     WP_010624970.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..453
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50617
     Region          1..453
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mkmklqevys alkiqadeip nveitgvcfd srkaktgdlf fplkgdrdgh efiesaisng
       61 atatvwqkdh eivdksipyv vvddvmkafe tltkyylakv npkvvavtgs ngktttkdmi
      121 asilavnnnv aktpknfnne igvpftilnm pintevlvve mgmdrpgqid hlsglahpdv
      181 svvtmigeah ieffgtrdki adakmeitrh lqedglfiyd gdeplltera edvqrnkatf
      241 geketntiya ttiesdkqkt sfktnlwpei eftvpimgdy nvnnamaall vgrryhvqve
      301 nmqkalsdly ltenrtewlk arngadilsd vynsnptaaa evlnnlkkls tgrkivvlgd
      361 mlelgsaskq lhesladhid pkdfqkvylv gnemkalydr lvtkydpadl swyskeqldk
      421 ltenlkeetn sndtillkas hgihlenvlk elv
//
LOCUS       WP_010625009             157 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside 2-deoxyribosyltransferase [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010625009
VERSION     WP_010625009.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..157
                     /product="nucleoside 2-deoxyribosyltransferase"
                     /calculated_mol_wt=17748
     Region          9..150
                     /region_name="RCL"
                     /note="Nucleoside 2-deoxyribosyltransferase [Nucleotide
                     transport and metabolism]; COG3613"
                     /db_xref="CDD:442831"
ORIGIN      
        1 msklnrvyla gpffsdqqkk rlddiqalle qndtigdifr pgkdeytaae fgsfewqtav
       61 fkhdvnninn sdivvaeldy qlednlsepd sgtawecgya fannvptfgv rfdeapplnl
      121 mlagsltgff ngpkhieelk dydfnslmtr yenikvf
//
LOCUS       WP_010624980             564 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010624980
VERSION     WP_010624980.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..564
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62885
     Region          37..546
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 mkefsnetra knlqkmqdee ldllvigggi tgsgitldaq srgiqtglve mrdfasgtss
       61 rstklvhggl rylaqfalee vhevgterai vynnapqitt plkmmlpfya ggtygpfmts
      121 vgldvydrla nvkkserktm lepdettqre pyvksegllg sglyveyrtd darltlevak
      181 kaselgalia nytkvtglly danhkvcgvk fvdtqsgetg eihakkvvns cgpwvdeird
      241 mdgsnkgkhl hltkgvhlvi dnakfpisns lffdtpfhdg rmmfaipreg ktyigttdtt
      301 weedpkepni tvadvtyila aanqmfelpq kltpddveag wsgvrpliqe egkspseisr
      361 kdeifqsdsd llsiaggklt gyrkmaekiv nrvaeqlane tdytfegqqt ehlllsggdv
      421 ggdegwstyf dkmvhegivn ynleredaek lvqrygsnvt diyellpdgd kdglprvdwa
      481 mlnyglkaem vehpidyllr rssqmlfnin hmkevkdaii dymadyyswd estkqamtde
      541 vntklaltdl hdikakyadh vaae
//
LOCUS       WP_010625012             235 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010625012
VERSION     WP_010625012.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 235)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..235
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25527
     Region          7..230
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mddqldirsa ikdtlptvfg yigiglafgv vgkasglstf ivvltslity agsaqfvlvg
       61 mlgahspmlt iifsvflvns rmilmsttva ryfkqesllk nilvgslltd etfalsmskv
      121 nktngrlnfe wfntsnliay stwavasfvg allgnmisnp ekfgldfalv amfigllylq
      181 lisdkslnfn lqlimvlitl vlvylglifi psnvtilvvt iiactigvil khvyf
//
LOCUS       WP_010625113             350 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Companilactobacillus versmoldensis].
ACCESSION   WP_010625113
VERSION     WP_010625113.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..350
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40138
     Region          26..329
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mslydkfvan krlrravllv vvivlfylfr smlslflltf iftflsvqlv ravqkhfklk
       61 pmwiiaptyi liiallvfav tnyipqlvhq svkivnsltq fyqskevrdn qylayvydyl
      121 qqinldnqik tfasqlvnyv ssvgatgvni flsfilsffy tsqvdemnqf grqflnsnys
      181 wlfddiryyg qkfintfgvv ieaqlmiavv ntvlttitli vmqmpgvial aamvfflsli
      241 pvagviisli plsfvaysvd glkyvvyiiv mvivihmiet yflnpkfmss mthlpifftf
      301 vilivseell gtwglivgip ifvffldilg vhqiggkkkp kmrpwkfkks
//
LOCUS       WP_010625137             499 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Companilactobacillus versmoldensis].
ACCESSION   WP_010625137
VERSION     WP_010625137.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..499
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53259
     Region          18..476
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msslwsrmtr redpniyqdk dshlsrvltv kdflalgvgt ivstsiftlp gvvaaehaga
       61 avslsflaaa ivagmvsfay aemsstmpfa gsayswinvv fgefwgwisg wallaeyfia
      121 vafvgsglsa nfrgligplg lkfpnslsnt lgsnggildi tavvvialva fllsygvsna
      181 arvenvlvvl kvlavllfiv vgltaihpqn yvpfipeyhv npdgsafggw qgiyagvsei
      241 flayigfdsi aanaaeakdp aktmprgiig slliavalfv avalvlvgmf hysdyannae
      301 pvgwalrnag hgtiativqa vavigmftal igmmmagsrl lysfgrdgml sswlgklskh
      361 nlpnnallil tivgiiigav cpfaflaqli sagtliafmf vslgiyairp regkdlpqpg
      421 fkmplypvlp aiafigaltv fwgldiqakm yagvwfaigl viyfgygirh pylnkkqdkk
      481 ltdleraeaa eesednyqk
//
LOCUS       WP_010625169             148 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010625169
VERSION     WP_010625169.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..148
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17321
     Region          13..123
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(14..16,30,46..48)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(60,63,67..68,77,95,99,105,109,112..113)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mstetmnete rhyrigdfae mtgltsptlr yyekeglvkp hrsenglrfy tdadvkwikf
       61 llhlkstgms ieqlkkyvqw raegdstink rlellknvrs efmkkmedld hsltilddki
      121 dwytgkttgk ikdsegfaty ldnmnhee
//
LOCUS       WP_010625174             154 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010625174
VERSION     WP_010625174.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10084616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..154
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=17282
     Region          16..153
                     /region_name="USP-like"
                     /note="universal stress protein (USP) and similar
                     proteins; cd00293"
                     /db_xref="CDD:467483"
ORIGIN      
        1 mdelkdynvr kieydrilic vdsddfvssk nafnyacsla khynaklgiv svletgdlni
       61 fqsldketlk errnqikell eaygqkakty gvqdlhlmvt egnpghvive qvipkfqpdl
      121 vivgveeknr nrntigsqaa rivndsnvsv svir
//
LOCUS       WP_010625176             284 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010625176
VERSION     WP_010625176.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..284
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=31066
     Region          4..279
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mtekiavfvd sccdipeeyl skegiyelpm qiiykdksyl drvnitagev yehlpeeipk
       61 tslptgdsiq rsldeaydag yrkiiaisis snlsgtynfl rtlldadgrf eyhafdtkqv
      121 aigsgliava akhmiddgks fqevidgvdr acqkaitlfc iptltylrag griglvfsmv
      181 gsvlklapii tcneegiytp iakargmkrg qkimrdkike ftkghhkyll avahgadeee
      241 ggkmlaklee mgihgtheyf eevgpalgvh tgpglvgvac tild
//
LOCUS       WP_010625185             160 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010625185
VERSION     WP_010625185.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..160
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17562
     Region          5..147
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 meqdyekilv pvdgskeaem afrkavkvaq mnnghidvlt vldtkqfigl hggmlngdvi
       61 yqlsedaqky lnelkdeavk ngmsadnvai hvrfgepktv iaqefveeyk ndlimigstg
      121 mnavtrllvg svseyvtgna rtdviivrtd vnnktitskk
//
LOCUS       WP_010625196             161 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010625196
VERSION     WP_010625196.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..161
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18707
     Region          7..154
                     /region_name="YdbS"
                     /note="Uncharacterized membrane protein YdbS, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3402"
                     /db_xref="CDD:442629"
ORIGIN      
        1 mndtkklsvd ikkiwrlkal lefiffmiat agllwwhrla peklqswils valivlflgl
       61 aglifelvlv eyrwnfwtyf nddrqvelhr gfffrkqvvi piarvqnvtl kqgpilrwkn
      121 lqkvvietaa gsseisglkk peadqlkeli melareaknd i
//
LOCUS       WP_010625230             192 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphoribosylanthranilate isomerase [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010625230
VERSION     WP_010625230.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..192
                     /product="phosphoribosylanthranilate isomerase"
                     /EC_number="5.3.1.24"
                     /GO_function="GO:0004640 - phosphoribosylanthranilate
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20874
     Region          1..191
                     /region_name="TrpF"
                     /note="Phosphoribosylanthranilate isomerase [Amino acid
                     transport and metabolism]; COG0135"
                     /db_xref="CDD:439905"
ORIGIN      
        1 mtkikicglm kvedvqavnq aqadyagfif apgrhqlslk qalklrqhld shipsvgvfm
       61 dapleemlqa fdsgaisliq lhgnesegai kalhakhvpv ikvfkpntir ktsadfimid
      121 sgagngklid wqkitvktnk pliiassids rnvqiaikqv kptivdlsrg vetdgkkdpq
      181 kisqivnlvh si
//
LOCUS       WP_010625266             222 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Companilactobacillus versmoldensis].
ACCESSION   WP_010625266
VERSION     WP_010625266.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 222)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..222
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23943
     Region          6..216
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mvdqplwsql vfyfthngmy ileqfgrhfl isfygvliaa vvgiplgiym anhfhlgdfi
       61 isianviqti pslamlsiim lwlglgvntv ivtiflysll pilkntytgm ksvdpntids
      121 argmgmtsfq mlymvklpla msvimsgirt amvvsignta igafvgaggl gdliirgtna
      181 tdgaplilag alptavmail tdliigflqk rfeptgyfke en
//
LOCUS       WP_010625273             168 aa            linear   BCT 01-JAN-2025
DEFINITION  GtrA family protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010625273
VERSION     WP_010625273.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..168
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18593
     Region          44..168
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mnnqaplddk skldtiitdv segindagnt fpapsdpvee snpkqvvryl lwglisvvvn
       61 lgtffilyrl mslnyqlani vawflgvqvg fwvdrvivfr hksntafqem lafygtrilt
      121 ylieaatlwv gisllaangt gskivgqila iignfifsks fifknrak
//
LOCUS       WP_010625271             428 aa            linear   BCT 01-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010625271
VERSION     WP_010625271.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..428
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45584
     Region          9..428
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mdtndkhyrn peavldlyer pplatwplls lqhlfsmfga tvlvpllvgl dpsialfssg
       61 igtilhilit kgripaymss sfsfivpsva lmktagyagv aqgtiavglv ylvvativgi
      121 agsgwidral ppivvgpivi viglsvassa adnammngkh ydltyfgvai ftllvtvlfn
      181 mylkgfwsni aillgivcgy vlsvalgivd fskvistpwl klpafefpyi sytpkkiywd
      241 ailsfapiaf vtmaehlghi mvldelthrn ffknpglhrt lagdgtasif aglvggppit
      301 sygenigvma vnkifsvyvi igaavfaalf gfvgklsali qtipgpvigg isfilfgvia
      361 ssglrilvdn kvdfnrkrnl miasvilvig ignaylqigs fqftgigvat vmgillnlil
      421 prealsee
//
LOCUS       WP_010625275             300 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Companilactobacillus versmoldensis].
ACCESSION   WP_010625275
VERSION     WP_010625275.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..300
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33926
     Region          13..269
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mnyslnstvt lnngvkmpql glgvwkvnna gasqsvqwai khgyraidta kqygneagvg
       61 dgltkalaen slnrediflt tkifngdqgy qstldnfenq lkqlqtnyvd mllihwpvdg
      121 syidtwkale kiyrdgkara igvsnfnvsk ledimsissi kpvvdqmefn pvcqdedike
      181 fcdknnihle awsplgggrv lkderlqkla dkynksvaqi ilrwdlqrgv itipksvhee
      241 rivqnadifd felsdddvae ingydnddrs lwyggffwhg nptgykdgve ewddtkdfvk
//
LOCUS       WP_010625280             476 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Companilactobacillus versmoldensis].
ACCESSION   WP_010625280
VERSION     WP_010625280.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..476
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51028
     Region          15..464
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtqksnkidi dvllanaskd nrkktlglfd lsilgigaii gtgilvltgi vaatdagpgv
       61 vysfliaala sgliglcyse lttsipnsgs ayvyawasig qtvaffagwt llgvyittta
      121 tvangwsgyv hsflaefgwn ipqalltspf nggiinlpav imiflvtlil trgtseskql
      181 nnvlvlvkia iivlfvivgf sdidqsnwkp flpfgmsgvf agastvffaf lgfdplatsa
      241 eevknvqktl praimislvv atlmyvlvsl vmtgfipygr lnvseamsfv llekghniaa
      301 qfvsagailg ivavvlafiy assnvmmsms rggflpkela vlnnktgspn kalwliglit
      361 aicaglldik nlatfanvgs lcvfflislm villrrqrpd lkrpfrvpfg ytipilsmiv
      421 cafllfnlpl saylnyagwl viglliymfy svkhvdleqs iepsepvdnd leadpe
//
LOCUS       WP_010625400             258 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010625400
VERSION     WP_010625400.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..258
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28481
     Region          4..241
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mseiatkkls faydqkkiid nvdlsisdgq ilvilgpngi gkstllscls glhksysgsi
       61 qlgdqelrti pkkvlshhva lvsqgvnvks slkltdylll grsafhsifs qpnqndqlqv
      121 drvltqigle dyrdislqdm sggqkqlaqi gralvqepql limdeptsal dyknqilvlk
      181 likalsdnni siiisthdpn qammvgdlvg llidnqtyiq gsteeiltek ylsdlyktpi
      241 vstynqqlhr nifgtrmd
//
LOCUS       WP_010625423             468 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Companilactobacillus versmoldensis].
ACCESSION   WP_010625423
VERSION     WP_010625423.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..468
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51385
     Region          3..455
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 maketlkrsl ssrqmqmial ggtigvglfm gsastikwtg psvllayala glilymvmra
       61 lgemlyvdps tgsfakfgse yihpvvgylt awsnvfqylv vgiseviavg tylafwwpnm
      121 pqwiagaviv itlcianlts vkaygelefw falikvvtii mmiifgllvi ifgfgnhghp
      181 igisnlwtng gfftgglkgf ifalsivvas yqgievigit ageaenpqen ivkairsivg
      241 rilifyigai fvivsiypwn klgtmgspfv etfakvgita aamiinfvml taamsgcnsg
      301 ifsssrmlyt lglekhlpka ftkvskhkvp yipvitisag iliglmlnya lpaifhtssn
      361 ifvivysssv lpgmvpwfvi liselrfrki nrakmsqhpf kmpwfpisny lsiaalivil
      421 ifmflnpett isllvgvvfl lfmtalyfir erkknnypve ndsskvee
//
LOCUS       WP_010625461             219 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010625461
VERSION     WP_010625461.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..219
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24818
     Region          1..199
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mievknltks fgkqvvfkdi nfkiadgefv sivgrngagk ttlvkilmgl ekktsgeivm
       61 ghknqigyvp qfrnidldyp lnieqfmrln lkftlnpqkr rhdseeveri lqqtnlseir
      121 drplglasgg ekqkaylaqa lvnrpeilil destasldvd vkiqlmdlvs elnkkhgltv
      181 lfithdselt krytkrallf enksvesidv nqiaedmfe
//
LOCUS       WP_010625460             265 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010625460
VERSION     WP_010625460.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 265)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..265
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28256
     Region          4..259
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mfeyefmrea fiastfiait agivgvfvvs rnmsflshtl seigfagaaf gilvgispla
       61 gmilftliss iavgslstes srreasisai sslfiglgil flslssesss yatnilfgsi
      121 vgisakevtq lmflaifviv vfiisykplt fdsfdhigaq asglntrlls vvflitlals
      181 vsigaqivgs llvfvlltlp gatarylvhs vpkllmisvg lslagvwlgl ylafvtnwpv
      241 tffisafevi ayflglsykn wklsh
//
LOCUS       WP_010625495             222 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010625495
VERSION     WP_010625495.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..222
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25109
     Region          2..221
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mlvvkdiyke fkdkkvlkgv sfnvnkkdni allgnngagk stlikiisgq mdsksgqiet
       61 klnfnsevgi mpqddilidd ltvkeiislk lsmcglkned ylfwlkevnl encsnifvgk
      121 lsggqkrrls lvlsmvnepk ivfldepttg mdldavdkfw elmrtkdfal viithdfnqi
      181 dtffnrvlil ndgvivsdtt vdklhsfgqt ieehyrkvme kr
//
LOCUS       WP_010625509             394 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010625509
VERSION     WP_010625509.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..394
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=42185
     Region          1..380
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mahililgag ygglkaardl akttpadtqi dlvdknvlhv ektalhmvaa gtarpesvsf
       61 dirdvipsnv nfiqatvsef dldnkkvsft dhddieydyv iislgfrsed fglegadkna
      121 lilqdldtat eiyetinkni anyknsqdpk dlsiavcgag ftgievlgel vdtikilkak
      181 ygvpeikvtc lemstrilpm fdeglanyav sylekngikl ltgakitkie dggvvykdte
      241 dqehtveast ivwtvgvsgs dvikdsgvda krnrvtttqf lnledhpeay figddsalip
      301 egeerplptt gqlataegga vafniasala gtelkpfvyk sagtvaslgq nhgiaqigdr
      361 kfkgvtasli khlaadrsfl emggvktalk kgsl
//
LOCUS       WP_010625510             399 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Companilactobacillus versmoldensis].
ACCESSION   WP_010625510
VERSION     WP_010625510.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..399
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43089
     Region          1..382
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mdsafmilsv llvwvmtpgi avfyggfipq kdttkmllei flmfgvvgll wfvvgyplsf
       61 egnefgiigd lkhiflsgin ltalypktni sntifilfqm mfailtpglf lgsiatkkst
      121 kyivlfvaiw svlvyyplvh mvwsstgfla klgvldfagg tvihidagvt alilsnfais
      181 khakdakake nahgnaffvl lgtvllwigw ygfnagsala lsaqgleaff tttmapiaam
      241 ityalledyy kksismngvc tgvicglvgi tsatgfvtlp asliigvisa agsyyfinil
      301 kykwhindcm dimgshgisg iigslatglf atkginpnvi nngllqgggf kqfglqlfav
      361 vfaftfvfvm nfiivkvlkr vfkessdsvh rkttaaqhi
//
LOCUS       WP_010625512             185 aa            linear   BCT 01-JAN-2025
DEFINITION  cysteine hydrolase family protein [Companilactobacillus
            versmoldensis].
ACCESSION   WP_010625512
VERSION     WP_010625512.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..185
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20798
     Region          6..184
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mashqallii dytndfvadk galtcgepgq aidknivkia dnmkkdgdwv wlptdvhrpf
       61 dhyhpetklf pahnvrdtwg relygetgkw fqensgkdtv kqfdktrysa fagtdldlrl
      121 rerdvdtihl vgvctdicvl htavdaynlc ynlvihksav asfnqaghdw aldhfenvlg
      181 akvvk
//
LOCUS       WP_010625532             442 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A
            [Companilactobacillus versmoldensis].
ACCESSION   WP_010625532
VERSION     WP_010625532.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..442
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=50026
     Region          1..441
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mkqgslfddq aqqnsplanr vrptdfdeft gqehligkgk ilrdlidqdk lssmifwgpp
       61 gvgkttlaei iahktksqfi tfsavtsgik eirqimqeae enreigqrtv vfideihrfn
      121 kaqqdaflpf vergsiilig attenpsfei nsallsrckv fvlhqltvsd ilellhnalk
      181 npeafpdyqv eisesdlkmi aefangdart alntlemavl ngnrkidkve veegaldqqi
      241 ntkslrydkk geehyniisa lhksmrnsdv daavywldrm leggedpiyi arrlvrfase
      301 dvgladtral slavdvfqac qfigmpecnv hlaecviyls lgpksnavye aiskakvdvk
      361 ktgnepvplq irnaptklmk eldygkdyqy ahntaeklts mktmppdleg heyyfpttqg
      421 neerfkqrle yikewhkrhd qe
//
LOCUS       WP_010625582             513 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Companilactobacillus versmoldensis].
ACCESSION   WP_010625582
VERSION     WP_010625582.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..513
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58052
     Region          6..508
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msvlevqhlt qqfldkklyd daslqvnked hlgitgqngv gkstfikilt gqlepddgki
       61 twqkhltvgy ldqqaklveg mtireylnta fsdlfeandk ltdiymndpd eedlekagkl
      121 qelldandfy eidtkvdqva tglgldaigy dqdvsklsgg qrskiilaki llehpdmill
      181 deptnyldtn hiewlsdyln nfegafivis hdysfldkiv nciadiefgk itkytgslkq
      241 vtkqkaanke tymkaytkqq ekisktkayi rkfkagsrsk saksrekqms hmdvltppgn
      301 ktiasfnfpy keipssrmvl evndlkigyd eplfdqqlnf slisgekmvi kgfngigktt
      361 liktllgmie pkagnfdfsd vvkigyfkqd lawksnmvtp fkvvsedhpe sdnkevrqfl
      421 artgltnqqi msplkslsgg eqtkvkladl mfeptnflfm deptnhldde skaslrkglr
      481 nypgamilvt heedfyssdw vdkvldieqi kkn
//
LOCUS       WP_010625625             684 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010625625
VERSION     WP_010625625.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..684
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=77304
     Region          18..626
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkriiksfsn flntrlgfvi lavvlytikt vyayttkfnl gvkgslqtfl mvinpipvml
       61 llfglalymk grksyiflli idfldsvwlf snilyyrefs dfltmilikg sgsvsnnlgk
      121 simgiveptd flvfldvlvl illlsfrvir mdvkrlkwri pilvsclaal lfganltlae
      181 sdrsglltrt fdnnyivkyl glnafnvydv vkttktsavk skakssdlds iknymkanya
      241 kpnveysgva kgknvfiihl esfqqylidy kwdgqevtpn lnkiyhennt lsfdnffnqv
      301 gqgktadael mlenslfglp qgaamvtdgt tntfqaapai ldqqgyttas fhgdvpsfwn
      361 rdntykswgy dyffsnnyyk qkksynigyg mkdkiflrds aqyiqqlpqp fyaklitvtn
      421 hypytldkkn qsisktdtgd stvdgyvqta kyldqsigef mdwlkatgld ktsmvvfygd
      481 hygisdnhkk amskitgikn fndfdnaqyq rvpfmihmdg lkgginhtyg geidvlptll
      541 nllgvddsnk iqfgsdllsp ehsqlvafrn gnfvspdvtk vgstyyntkt gkvdkkissa
      601 eksklsnkvt telslsdrvi ngdllrfynp tdftkvdkkd ysykkstalk klkkartkng
      661 tsilaqndnk slmdlyqtda pelk
//
LOCUS       WP_010625731             375 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Halomonadaceae].
ACCESSION   WP_010625731
VERSION     WP_010625731.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..375
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40282
     Region          1..375
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 metlniglig tgfmgkahsi alkaapavfd lpaqpfcdll aevddalaer kalelgfara
       61 tgdwrllvkd pevdvvdica pnylhkemal aaiaagkhvy aekplaltaa dagemaeaae
      121 kagvktlvgf nyirnpatql areivasgei gelihfrgrh nedylsdpak pldwhvqrat
      181 agagalgdvg shilnmaeyl tgqrisevfg qlqtliprrp lpdgsggmge venddqaqal
      241 lrfdgglign ietsrvatgr kmglaytltg tkgsiifdqe rlselqlyks eglpgrrgfs
      301 tlligpahpd yaafspapgh glgyndqkii eirdlvvgia gnkplypdfr eawrvnrlie
      361 aiehshvvgs wialh
//
LOCUS       WP_010625754             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: uroporphyrinogen-III synthase [Halomonadaceae].
ACCESSION   WP_010625754
VERSION     WP_010625754.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Schubert,H.L., Raux,E., Matthews,M.A., Phillips,J.D., Wilson,K.S.,
            Hill,C.P. and Warren,M.J.
  TITLE     Structural diversity in metal ion chelation and the structure of
            uroporphyrinogen III synthase
  JOURNAL   Biochem Soc Trans 30 (4), 595-600 (2002)
   PUBMED   12196144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..265
                     /product="uroporphyrinogen-III synthase"
                     /EC_number="4.2.1.75"
                     /GO_function="GO:0004852 - uroporphyrinogen-III synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006780 - uroporphyrinogen III
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0033014 - tetrapyrrole biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28230
     Region          3..232
                     /region_name="HemD"
                     /note="Uroporphyrinogen-III synthase [Coenzyme transport
                     and metabolism]; COG1587"
                     /db_xref="CDD:441195"
ORIGIN      
        1 maagpavlic rpgeraaalt aaieavgypa inleamtlea lpedpalrqa wldfdhfhkv
       61 vvvspfaaec lyhaldrywp qlplgtqwya vgaataealh erlgvrvhlp saaagedtse
      121 allelaslrs lndqrvllva geggrtllad tlaargarvt rvalyrrrlq apppelqqrl
      181 argefralvv ssgellehla rwctrvtlnq plivssrrla tlasnlgfrt pvvaagatpa
      241 alasavaaac nqedadvdqd dlekg
//
LOCUS       WP_010625778             427 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Halomonadaceae].
ACCESSION   WP_010625778
VERSION     WP_010625778.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..427
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45221
     Region          1..427
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtaiilsimi vllllgfpmm iplataafvg fymtfggmgq metliqqmmg girptaliav
       61 pmfilaadim trgqsagrli glvmsfvghi kgglavstaa sctlfgavsg stqatvvavg
      121 splrprmlka gykdpftlal iinssdiafl ippsigmiiy gvisgtsire lfiagigpgl
      181 lilamfsvys ifyaiihkvp tepkatwker alalrdslwp lgfpvlivgg iyggvfspte
      241 aaaacvlyav llefvifrsl kmsdmysiak stglitavvf ilvavgngfs wiisfaqipq
      301 tlleafgine agpvgvliai cvaffiacmf vdpivvilvl tpifapaiaa sgldpvlvgv
      361 litlqvaigs atppfgcdif taiaifkrpy wevirgtppf vfmlilsaal iimfpqialf
      421 lrdmafr
//
LOCUS       WP_010625785             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [unclassified Halomonas].
ACCESSION   WP_010625785
VERSION     WP_010625785.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..305
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31096
     Region          23..305
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mdgvtnalgp lfllillgaa lgrlrqpsdd fwvqlekviy fllfpamlva tlatanvgev
       61 pvvrlaiall ggmlvfagll watqrrlgle paaftsvfqg alrfntyvgv agaaalhgsa
      121 gatvaavava lmvpvvnvlc vasfiaagtl gpsslgkslt alvrnplila clagialnls
      181 giglpgwsgs avellgraal plglvavgva lrpqallrld rgvwtsnlvk lmlmpalvfg
      241 lalllgldav srdvallfaa lptatsayil arqlggdael maalitgqtl lamatlplwl
      301 hlags
//
LOCUS       WP_010625919              92 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HU family DNA-binding protein [Halomonadaceae].
ACCESSION   WP_010625919
VERSION     WP_010625919.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..92
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9443
     Region          1..92
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mrkpelaaai aeraelskdk asqvlnvild eitgsvaqgq dvsligfgtf tvreraartg
       61 knpqtgqpla ipasktvafk pgkglkdavg kg
//
LOCUS       WP_010625932             135 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA thioesterase [Halomonas sp. KM-1].
ACCESSION   WP_010625932
VERSION     WP_010625932.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..135
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14917
     Region          8..133
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mtdlddvpap qgqltlklla drqdtnlygd ipggwlvrhm dqaaelaagr eargrtatva
       61 ietmdflcpv rvgsmvnift avreighssi kidvevwirq pheresselh kvtearfvmv
      121 alddkgrira vrqng
//
LOCUS       WP_010625962             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Halomonadaceae].
ACCESSION   WP_010625962
VERSION     WP_010625962.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..256
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27291
     Region          3..254
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 msqiialtnq kggvgkttta vnlaaslaal drrvllvdld pqghatmgsg idkhslegsv
       61 ldlllgeksa pevmldcpta gysllpgngd ltaaevelld raegrerslt ealasvagey
      121 dvvlidcpps lnmltvnalt aangvliplq cefyalegls alldtveqik dsvnpdlaiy
      181 gilrtmfdgr nsltrdvskq lrdyfgeall kttiprnvrv aeapshglpv tkyarfsrgs
      241 qahrvlakel irrlsl
//
LOCUS       WP_010625943             356 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Halomonas sp. KM-1].
ACCESSION   WP_010625943
VERSION     WP_010625943.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..356
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=38863
     Region          40..333
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mtsvlrpvaa falslmllls gcsendrpld spvrlegaif gsfyqvtiad sltqgqarel
       61 eegllevleq vdasmsiyre daeliafnqs pvgewqplsn elievlaisq svaessngaf
      121 dvtigglvnl wsfgsearpr evpddetlqa rlaevgpdsi evdenamqar rlrdvfvdlg
      181 gvakghgtdr vasyldgegi ehylvnlggd lvargyrdad gepwrigiea plddrqeatq
      241 ivpvqnisia tsgdyrnyfe eegrrfshti dprtghpieh rvasvtvahp snawadawat
      301 amlvlgeees lalareqdlk vlllvregeg wrsvaspafa erfggelsee mdlevr
//
LOCUS       WP_010626066             403 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Halomonas sp. KM-1].
ACCESSION   WP_010626066
VERSION     WP_010626066.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..403
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41511
     Region          7..332
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mtletstteg assrrmivai vafaalapaa lmvapaiagq lvsqlalgps qvgnllaiel
       61 galslatlpa ywwlprvswr raallaglvf vagniasalf gqqdygllmt lrfvtalaag
      121 slmivcisaa altankdrvy glwvmgqlvv gavglallpp mfeifglafl ywllagsmla
      181 clplarflpa kstqrsagqr drplprlkag lgvlaiftfy idisgvwtfi gaiatesris
      241 aehsgtilai atllgivgaa casllgkwaa qgqarramll agyaalvaat lalmghpgma
      301 rfviaalvfk ftwtfilpfa laslaeldps grlmntvnlv iggglatgpl lagqlieaqg
      361 hhtgmllgas aagllslali lsssgasttl rdarttptqg tts
//
LOCUS       WP_010626069             643 aa            linear   BCT 01-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator [Halomonas
            sp. KM-1].
ACCESSION   WP_010626069
VERSION     WP_010626069.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..643
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=69986
     Region          8..642
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mtiraalrtp dvirqvrehl srgqlpvdll dasigrswqr cldhgllpgt rlelsqldsg
       61 elrlqreahr rlieladplv sraaedlrgc qlllatpdat ilksygrgfv igehlrigag
      121 inlderrfgt napalalier apvlvksceh llfpdnpvsc vaaplfdldg sclglidltf
      181 eanhprpeif lrrvqqltga leqrlfirhy qqrwvlqvha slaeldgvsc glvaisdtgf
      241 ilavdsqash wlgqaaaalt gqpvealfgs swpalqrqce rqstllglel tggrlfgrln
      301 ppeqwqpaev vsttlpppta tplgcqlndl vadwpaplar eahraarala aglpvllqge
      361 tgtgkeqlar alhaslgerr pfvalncaal peslieaelf gygegaftga rkgghggrlv
      421 qanggtllld eigdmplalq arllrvlqer vvtplgdhre vpidcqviaa shrdleelva
      481 agdfredlfy rlaavvvelp alsehaglaa rirkrwaalc hdhgrdlald dplverlagy
      541 pwpgnwrele hcleaalmga dpecrkvtle dlsprwqrkl gaggiatcad tpptmpaste
      601 spqqlreler lhmlrtleah ggnmtsaara lgisrstlyr rlg
//
LOCUS       WP_010626110             170 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Halomonadaceae].
ACCESSION   WP_010626110
VERSION     WP_010626110.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..170
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18775
     Region          14..170
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mrqphslgks llillmrgls rlnfllavis avvlvaatga vfaeimsrll fgksllwvve
       61 lsgyallymt flgapyllek nrhvaidivt enlhprwrvp lgcamsllga avcfyatwyg
      121 lavtldqyqf gtrettvlap hsylltwvfp lgmflvaiqf vaqalaclkr
//
LOCUS       WP_010626170             684 aa            linear   BCT 01-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Halomonas sp. KM-1].
ACCESSION   WP_010626170
VERSION     WP_010626170.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..684
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=75378
     Region          1..654
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 madrtglqft ldlagvdsae lavidftlee alsqpfhlev rfasrdagls atelldrpvs
       61 ltiwqdgevl rrvhavvsef grgdrghrrt lyslvarpal wrldlrhnsr ifqevspltv
      121 lntlcnergl tdvafavtrd laereflvqy retdlafver laaeeglfyf hefedtpnga
      181 hrlvfadapq tlahlgerty hgraggspps rhvrklqqla rvapasvtlk dysfknpaya
      241 qlhehaagdl eehaqrddye hydypgryka dasgdaftri rlehlrsgal tcaaesdlpe
      301 lapgvkftlt dhdlselnrd wqvvkvkhtg sqpqaleedg vtqsdaaglg qmtkfdneli
      361 ltpadrawrp tpnakprvdg pqiafvvgpe geeiycdehg rvkvqfpwdr yaepnetasa
      421 wvrvsqgwag ggygsmaipr ighevvvsfl egdpdqplit grtyhavntp pyelpahktr
      481 tvirtqshkg egfnelrfed qageeqiwlh aqkdlelltn ndrteeignd sfltvyhdri
      541 geihaddhlt vhgsrhtqid gddhlivdas rhekygrall veagqeihhk agmkvvieag
      601 aeitlkaggs fvkldpsgvt ivgsqvkins ggspgsgsgq aaqapalpre aeaapeftpi
      661 qapqqaallq qkalcpvcek dgsa
//
LOCUS       WP_010626168             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Halomonadaceae].
ACCESSION   WP_010626168
VERSION     WP_010626168.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..192
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21313
     Region          101..172
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 mlaafkrlfg gerrkeaapa steeavkgle easmedidaf leaarradtk ghspwvlrde
       61 arlatlrral eftvqhgqwl qrdggniarw qgrllklrhg egptlgmlla crpddeaawq
      121 lrfffvepew qgsghgarll raarlslngv plnarlplac qsairsleqa gfarmhvnaf
      181 evasfeapae wd
//
LOCUS       WP_010626199             133 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [unclassified Halomonas].
ACCESSION   WP_010626199
VERSION     WP_010626199.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 133)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 133)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..133
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14042
     Region          26..113
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mvmklasrai amllislsqa vwsgdtsspa lvgdaqrgad maklctschg yqgrsvtsry
       61 psiagmdear fiagmqslra gerghlmasm trglsdqdia dlaayysrla pqaqlephtq
      121 qeprtegada svp
//
LOCUS       WP_010626202             315 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Halomonadaceae].
ACCESSION   WP_010626202
VERSION     WP_010626202.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..315
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34294
     Region          5..223
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnpviechgl tkrhgdltrl ealdltvkeg evlallghng agktttmkli lglispsags
       61 levlggapdg phaetlrrhl gylpenvsfy eqltgrevld yfarlkridr rqvdellekv
      121 glghaakrrv ktyskgmrqr lglaqallge prlllldept tgldpaatrd fyetvrelre
      181 rgctvllssh vlpgvepyid ralilgagrr lalgsleelr reaslpltir akgrwpgvdw
      241 tagwddsria prylngsale lgvhpsakms alrrltgtpg vedidvlppt lehlyahfsa
      301 pvaaasstpd qrgtp
//
LOCUS       WP_010626217             249 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Halomonas sp.
            KM-1].
ACCESSION   WP_010626217
VERSION     WP_010626217.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..249
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26462
     Region          8..234
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mkdrsamrla rlqqalaggg tlplgeaaqm cgvsemtirr dvaasdgami llggrlvman
       61 hyapvydldq qqdshtlakr rlceraagfi edgdtlfidc gttllplagl laerrqltvv
      121 tyalnvanam slvpgvrlvl lgglyhttsh sfgsddmsaa ikrlginraf isaagvhaer
      181 gvscfhfhev apkqaaiaca eqrllvvdes kigqvrpayf aqlddfdvvi tdgdmtlpqa
      241 dggprivaa
//
LOCUS       WP_010626264             273 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Halomonas sp. KM-1].
ACCESSION   WP_010626264
VERSION     WP_010626264.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..273
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=30289
     Region          110..246
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mqmieiaqlp gryapppvkv gdksideesi aremqyhpaa sadeaklaaa ralvvrellr
       61 qravelglls adsrdesehd aaiatlleqe ldvpepeeea crrffdaepe rfsaptriav
      121 rhillaaapd daeardaqyr lgetlleela aiperftefa mrhsacpsks eggelgwlaq
      181 gqtvaeldra lqhlpeglhd rplasrygwh lvsidaregg qrlpfeqvae rvrhtlreqa
      241 trralrhyll aleeeigveg ielddnaags lmq
//
LOCUS       WP_010626267             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Halomonadaceae].
ACCESSION   WP_010626267
VERSION     WP_010626267.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..247
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27625
     Region          32..241
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnipiyppds sstdllfkpk qlrelvngvp wlseldeeev tallqdselq slktrewlfr
       61 qdapahwlyi vingavrlar sagdgrlati rcverggtlg elsmvssagv ylysaealrr
      121 thvlaipaqh creimdrqpa craefmsrla lelterledl alltqadams rlvsyilrql
      181 pagrsksprv vrlsipkrwl aaqlamtpet lsrllaklrd ggvigidrqr ltvldeqklr
      241 damladd
//
LOCUS       WP_010626270             345 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010626270
VERSION     WP_010626270.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..345
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38268
     Region          10..322
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mipvavqepl svgfvllhrf tllpfaafvd clrlaadegd rsrqlrchwt fmtstgeqat
       61 sscgaaispc epfrdpasfd yivviggvqd erdrvdstal aylrrsadvg vplvglctgv
      121 faliqaglmk grrccvswyh hrdmiqrfpa iepvadrlfi ddgdrltcag gaagadlaay
      181 lierhlgkaw amkslhimll deartgvhpq pqpvvfgkie drlvrkaial leqhlgemis
      241 mevlaervgt srrnlerrfk etlgvspqkf srdlrlrygv wllhytgksi teigercgfa
      301 dtahfsrhfr safgmtpsem rksvsepgga rvdpfflhve grpal
//
LOCUS       WP_010626292             221 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Halomonas].
ACCESSION   WP_010626292
VERSION     WP_010626292.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..221
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25130
     Region          15..148
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprgadsdtk wkgsreawld aafellldsg vesvrilpla krlkvsrtsf ywffkdreal
       61 ldalierwre kntqglvrqt eayaesitea ilnvfdcwld pklfdsplef amrswalqse
      121 avareidaad eariealtrm ferfgyepla anvrgrtiyl tqigyismkt qealevrmqr
      181 ipayveiftg qapqprelqr fqarhghame gaqavsgaag h
//
LOCUS       WP_010626331             147 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Halomonas sp. KM-1].
ACCESSION   WP_010626331
VERSION     WP_010626331.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..147
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15184
     Region          28..147
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mqtttiplaa spaqaqaqsq nqahatallr vslgimalah gllkvfvftv pgtvgyfesl
       61 glpafiaylt ilaevgggla lvlgiytrwv slalvpillg aawahigngw vfsnpgggwe
      121 fpvfwaiall vqaglgsgsl vvsrrfa
//
LOCUS       WP_010625406             244 aa            linear   BCT 01-JAN-2025
DEFINITION  HesA/MoeB/ThiF family protein [Companilactobacillus versmoldensis].
ACCESSION   WP_010625406
VERSION     WP_010625406.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus versmoldensis
  ORGANISM  Companilactobacillus versmoldensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Companilactobacillus versmoldensis"
                     /db_xref="taxon:194326"
     Protein         1..244
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26956
     Region          5..242
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mvtsrydrql kieqigekgq kkfgnshvlv igvgglgsfv sselvkagig eitlvdfdkv
       61 eftnlhrqnl ytekdvnndl dklnamnrhl qaansevkin lkdqkysadl itddydlvid
      121 ctdnfpvkyq inqdcyqknv phifatcagn qgqamfmksq ddacleclyp hqniaklgls
      181 anigtnpmiv aitgsleasm alkflvdpda vksgnlivvd nwnfdfrkih vkkqhscpic
      241 gggk
//
LOCUS       WP_010626417             152 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein
            [Halomonadaceae].
ACCESSION   WP_010626417
VERSION     WP_010626417.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..152
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=17134
     Region          44..152
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mfgdlkrfdn gigsgldwfr pwldeifqeg aadirsvprg sfpminvgrt ddavrvyvla
       61 aglaredldi svqdnvltlr grrdalpgek agdrkrpcfr rerfdgefvr sislpdgidv
      121 eraearchdg vfeihlpkre elkprridvq aa
//
LOCUS       WP_010626344             217 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Halomonas sp. KM-1].
ACCESSION   WP_010626344
VERSION     WP_010626344.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..217
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23258
     Region          1..216
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mlefrqvykt yatpqgplav lvgvdlelrg geslalmges gsgkstllhl aagldlpdsg
       61 evlladrsis aldepararl rrdtlglvfq qfhlvpslnv ldnlrlqarl agretpewsa
      121 hlmqrlglag lerrypeqls ggqqqrlaig ralaprpall ladeptgnld ettagevlal
      181 llelvreags allmvthsaq vaapldrclr lthgrlg
//
LOCUS       WP_010626418             129 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein
            [Halomonadaceae].
ACCESSION   WP_010626418
VERSION     WP_010626418.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..129
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=14541
     Region          27..129
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mnevtrheaq asvparerrs ramrppvdiy eendalfvva dmpgvtpegl nvevdgnlls
       61 iegeiridmp eglsatyaea qaqryerrft lsheidtaai earlengvlh lrlprkerhr
      121 srrieiqaa
//
LOCUS       WP_010626443             196 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Halomonas sp. KM-1].
ACCESSION   WP_010626443
VERSION     WP_010626443.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..196
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20643
     Region          1..194
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtetlgfmaa vigllitpgp tntllaasgs qrgmrasvsl ipaelagyll aialwgsvlg
       61 slgerwewlt vtlriasaly iaylalrmwr satdmevaak avvshsglfl atllnpkall
      121 faaaifpqsa frgpvefvlp allfslllip iaafwiafgt avasgrltwl spfviqrgaa
      181 vvlagfslsl gwstlh
//
LOCUS       WP_010626448             251 aa            linear   BCT 01-JAN-2025
DEFINITION  (Fe-S)-binding protein [Halomonas sp. KM-1].
ACCESSION   WP_010626448
VERSION     WP_010626448.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..251
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27507
     Region          <4..249
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mtpvklyppk pekayffgtc lidlfypeag mdgirllere gvevvypqaq tccgqpayts
       61 gyheearava taqldlfpep wpivipsgsc ggmmrthypq lfagtehear anevagriye
      121 ltefllhvcq lrledrgqpe kvamhtscsa rremglgetg pallarmgqv elveqarate
      181 ccgfggtfav rhpevsaamv edktqaieat gakrfitsdc gclmniagrf ehqgkavsge
      241 hiasylwrrt s
//
LOCUS       WP_010626508             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [unclassified
            Halomonas].
ACCESSION   WP_010626508
VERSION     WP_010626508.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..304
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33789
     Region          14..81
                     /region_name="HTH_MlrA-CarA"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators MlrA and CarA; cd01104"
                     /db_xref="CDD:133379"
     Site            order(15..17,31,48..50)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133379"
ORIGIN      
        1 mtakgghpad tplypirevs ritgvnsvtl rawerrygli rpqrtpkghr lyaredierv
       61 erilqwlsrg vpvsqvkeli dqpasapppe pasgdwpsqq rqlvaaveal drsqmetlft
      121 qslalypvnt clselwqpvt releerwrdq lgatlqrrcl esflrtrigi rlyhanqlar
      181 gpllllvplp ddpgtlwlll aalaasdagy riqlldsalp fselplaver lqagavllvs
      241 graeradvir rqlprlaeql daplglcgpv arirdgdlad slvellgddl pqamarlrsl
      301 iqea
//
LOCUS       WP_010626465             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: elongation factor Tu [Halomonadaceae].
ACCESSION   WP_010626465
VERSION     WP_010626465.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     gene            1..397
                     /gene="tuf"
     Protein         1..397
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43370
     Region          1..397
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makekfersk phvnvgtigh vdhgkttlta altrvsaevf ggewrqfdsi dnapeererg
       61 itiatshvey qseqrhyahv dcpghadyvk nmitgaaqmd gailvcsaad gpmpqtrehi
      121 llsrqvgvpy ivvflnkadm vddeellelv emevrellne ydfpgddtpi itgsalmaln
      181 gedengmgtt avanlikald dyipeperai dqpflmpied vfsisgrgtv vtgriergiv
      241 kageeveivg ikdttkttvt gvemfrklld egragenvga llrgtkrdev ergqvlakpg
      301 sinphtvfea evyvlskeeg grhtpffkgy rpqfyfrttd vtgtcelpeg vemvmpgdnv
      361 kmvitliapi amdeglrfai reggrtvgag vvakivq
//
LOCUS       WP_010626565             159 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [Halomonas sp. KM-1].
ACCESSION   WP_010626565
VERSION     WP_010626565.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..159
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17721
     Region          13..151
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mqrrfdqldd vwpaglgrrl gamlydaflv aaiwiaiavl hvafvryvlg lgpedvgage
       61 pqrltlqlll ligafvffaf swtrggmtlg mqawrlrvqt pdgrsitlvq slvryvvawl
      121 slaalglgyl wvlfdhqrrs wpdivsgtqv vvlpkatrr
//
LOCUS       WP_010626568             347 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Halomonas sp. KM-1].
ACCESSION   WP_010626568
VERSION     WP_010626568.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..347
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37296
     Region          24..322
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msrqltagll agalslsllg aavaqadetr irfqldwrfe gpsapflmav ergyfaeegl
       61 nvqidsgsgs againrvasg ayemgfgdln alveflaenp dgpgiqgvyv vydgspasvf
      121 arkdrdiesp adlagksiaa pafdtgyraw gifaaandle agavewqnvd palretllvr
      181 gdvdaitgfy ftsllnlegr gmdeeqltim pfpdygvply gnaiiaseaf seanpeaveg
      241 flrafnrala etladpegai eyvrnrdali dvemetrrlk laiasvidtd earangaggv
      301 deqrlreaiq lvadaydlps vpepervfts sflppqeerm ifperae
//
LOCUS       WP_010626580             205 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Halomonas sp. KM-1].
ACCESSION   WP_010626580
VERSION     WP_010626580.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21705
     Region          1..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mspesallyf laifvfaitp gpgifailar gmssgaracw plalgmtvsd llylmlafhg
       61 lavlaehwge aftmiryvga aylfylawkl wtspvgeadl sagsrrvdlv kgflqgflis
      121 asnpkvilfy iaflptfvdl valasgdmll tvsltfvglm lglmlvavga asarrwlqse
      181 ramkganrsa galmvaagaf lvakg
//
LOCUS       WP_010626612             266 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA-uridine aminocarboxypropyltransferase [Halomonas sp. KM-1].
ACCESSION   WP_010626612
VERSION     WP_010626612.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Funk,H.M., Zhao,R., Thomas,M., Spigelmyer,S.M., Sebree,N.J.,
            Bales,R.O., Burchett,J.B., Mamaril,J.B., Limbach,P.A. and Guy,M.P.
  TITLE     Identification of the enzymes responsible for m2,2G and acp3U
            formation on cytosolic tRNA from insects and plants
  JOURNAL   PLoS One 15 (11), e0242737 (2020)
   PUBMED   33253256
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Meyer,B., Immer,C., Kaiser,S., Sharma,S., Yang,J., Watzinger,P.,
            Weiss,L., Kotter,A., Helm,M., Seitz,H.M., Kotter,P., Kellner,S.,
            Entian,K.D. and Wohnert,J.
  TITLE     Identification of the 3-amino-3-carboxypropyl (acp) transferase
            enzyme responsible for acp3U formation at position 47 in
            Escherichia coli tRNAs
  JOURNAL   Nucleic Acids Res 48 (3), 1435-1450 (2020)
   PUBMED   31863583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..266
                     /product="tRNA-uridine aminocarboxypropyltransferase"
                     /EC_number="2.5.1.25"
                     /GO_function="GO:0016432 - tRNA-uridine
                     aminocarboxypropyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=30063
     Region          45..259
                     /region_name="TapT"
                     /note="tRNA U47 aminocarboxypropyltransferaseTapT/TuaA/
                     YfiP, DTW domain [Translation, ribosomal structure and
                     biogenesis]; COG3148"
                     /db_xref="CDD:442382"
ORIGIN      
        1 mldetgqadl adrapeaghs rapeaghyhd patghsrppr refkargsft ercpgcnlpv
       61 lnclcpyrvn aesearvwli thplehlkpt ntgrlirdvl pdtevftwyr ttpderllal
      121 lddprfapfv ifpddqpdya drvvdmavvg evkasgrtpv filldgtwrq arrifrkspy
      181 ldrlpvlpla ttrltryrlr kpasqahlct aevaaellrq sgdehaaqvl ddyfdafnvs
      241 ydasrryekl eqptaamrrl lacqge
//
LOCUS       WP_010626426             532 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SLC13 family permease [unclassified Halomonas].
ACCESSION   WP_010626426
VERSION     WP_010626426.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..532
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55567
     Region          111..526
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mdkqpheqtq geapggeeag grsarliwgl rafgllvali vwlamgqaeg lspdarwvat
       61 igalmavwwm teaiplsata llpivlipml tertvaqata pyassivflf lggfliaiam
      121 ekwnlhrria lltlarvgvs phrivlgmml atgflsmwvs ntattlmmlp iglsvlalva
      181 ersgestetv saghdhhrag hvdfiadeni krfglcllla iawsasmggl gtllgsppna
      241 ivagyaadel grnigfldwm mlgvplaftf ilvgwvlmtr vlypfkveei pggqemiege
      301 vrklgsltqg ekmvllvfgs aaflwvvpgv lgnipgvgqw lgplgnlddt aiavaagial
      361 fvlpargrne mvlnwkdaed glpwgvlllf ggglslagav agtgldswfg qqitglgvlp
      421 illlvaavat ivlfltevts ntataatfip vlggvavgig tdsmtllipa afaatcafml
      481 pvgtppnaiv fgtgavsigq marggvvlni vgivlitlfc yllggfalgl qf
//
LOCUS       WP_010626690             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: trimeric intracellular cation channel family protein
            [unclassified Halomonas].
ACCESSION   WP_010626690
VERSION     WP_010626690.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..253
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=26722
     Region          4..201
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mtalvywldm agvvvfalsg vilacrsrmd pfgmlvlaav tgigggtlrd lvlgvrpvfw
       61 vadptylwvi latvglsivg fhyihrlsrs flpiadafgl alftvigahk alqleapgvv
      121 avlmglltgv aggmvrdvla rrvpmvlrqe vyatasiagg ityvglgalg vpvgvaigla
      181 lavtlglrla aihwqltlpv fawvvirppq eaqaadpgne qevpqggppa qpksrpkvrv
      241 rmispsqqrr qre
//
LOCUS       WP_010626742             205 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Halomonas sp. KM-1].
ACCESSION   WP_010626742
VERSION     WP_010626742.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22087
     Region          1..204
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdlltlllfv pacfalnmap gpnnllsmsn akrygvrmac lagigrlaaf vvmialaasg
       61 latvlytsek lfllikvlga gylfwlafql wgaessdegm aaapmglwgl srqefllaag
      121 npkailifta flpqfvtpdg dvafqflilg alflvlewva iigyacfgaf lrhwfsrptm
      181 rrlfnracas llasagigll varre
//
LOCUS       WP_010626767             100 aa            linear   BCT 01-JAN-2025
DEFINITION  TM2 domain-containing protein [Halomonas sp. KM-1].
ACCESSION   WP_010626767
VERSION     WP_010626767.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10524121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..100
                     /product="TM2 domain-containing protein"
                     /GO_function="GO:0001540 - amyloid-beta binding [Evidence
                     IEA]"
                     /GO_function="GO:0004930 - G protein-coupled receptor
                     activity [Evidence IEA]"
                     /GO_process="GO:0097190 - apoptotic signaling pathway
                     [Evidence IEA]"
                     /calculated_mol_wt=11448
     Region          5..53
                     /region_name="TM2"
                     /note="TM2 domain; pfam05154"
                     /db_xref="CDD:428337"
ORIGIN      
        1 mietkqknrl ialvlamflg ffgvdrfylg kwktgilkav tlggfllwwf idgalllmda
       61 ffhslgkqkg fvkdgsgnel kyglsmyrlq ngrfeqdwfk
//
LOCUS       WP_010626799             240 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Halomonas sp. KM-1].
ACCESSION   WP_010626799
VERSION     WP_010626799.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..240
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25176
     Region          3..237
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mskvilltga ssgigeatar llakqghhlv igarrterle alaqairseg gnveyraldv
       61 tqredvqafa daalklhgri dviinnagvm plsplsslkv eewdrmidvn irgvlhgiaa
      121 vlptmqtqgs gqvinissig glfvvptgav ycatkfavra isdglrqehd nlrvtcvypg
      181 vveseladti tdagaaeamk sfreialkpe aiaaaiahvi aqpdgvdtsd ivvrptaspa
//
LOCUS       WP_010626830             444 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Halomonas sp. KM-1].
ACCESSION   WP_010626830
VERSION     WP_010626830.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..444
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46827
     Region          5..444
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mdpitmgiiv aialivlmai gtpiafalgg vsllalmydr glpeliyfge tffdriaefg
       61 fvaipmfilm gaavassptg rdlyrsldlw mgrlpgglav snigactifs alsgsspatc
      121 aaigkmgipe mrtrgypdgv aagciaaggt lgilippsvt miiygistet sigrlfmagv
      181 lpglmlaglf miwtmiacrl aggyanpmaq aaaqvkqnik anvdtnlkal vrvvpfllvi
      241 agilfalygg vatpseaagv gaflcvalav liyrmwqvkp vklimrdslr esvmimlvia
      301 taevfayals smfitqtvaa aianmevnrw vlmgiinlfl lvagfflppv avivmtapil
      361 lpiilaadfd pywfavilti nleiglitpp vglnlfiikg iapdislrni llgslpyalc
      421 mvlgivllcf fpgialwlpn limg
//
LOCUS       WP_010626892             233 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Halomonas sp. KM-1].
ACCESSION   WP_010626892
VERSION     WP_010626892.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..233
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25567
     Region          1..230
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 midlhgygpr llegagvtlq lavlslilal ilglltasak msrnwllhkv atlyttvirg
       61 vpdlvlmlll ffggqmalnv atdaiydrfg vdwyinlnaf aagvltigfi fgaymgetfr
      121 gafmavehgq ieagkaygms pwlvfrrirf pqmmrhalpg isnnwmvllk ttalvsvigl
      181 sdmvrvaaea srathepftf lipvaivyll iasvsewmfa rlqkrynvgf ggh
//
LOCUS       WP_010626916             293 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Halomonas sp. KM-1].
ACCESSION   WP_010626916
VERSION     WP_010626916.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..293
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29885
     Region          4..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mkasrrvgli gvglmghgia anilrgghtl cfldhpgnqp vedllgaggv akgsgrevae
       61 aaevvilcvt gspqveavlf epggvlegla pgtlvidcst alpssterva arveaaggrf
      121 mdaamtrtpk eaeegrlnli vgapealfae vrpllecfae niahagpvga ghtlkllhnf
      181 vslgftavla eaaaasrrag iddaalldvl gkgggggvvl erlrpyieag dpsgfrfsva
      241 nalkdigyyr tmtqdlaaeg gvaeavlaly rqasdaghad kpvpelvgll erg
//
LOCUS       WP_010626948             534 aa            linear   BCT 01-JAN-2025
DEFINITION  BCCT family transporter [Halomonas sp. KM-1].
ACCESSION   WP_010626948
VERSION     WP_010626948.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..534
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57801
     Region          20..534
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mhtdytvgqd niegrlgpig fdihnrvfav salasvvfii ltllfperag aifqtivgfa
       61 tgsldwyfml vvdffilfci alvllpygsv rlggpdarpd ygylswfaml fsagigigll
      121 ffgvlepvyh anvslplgia spfgadgeld paaigeatal glagtylhwg ihgwavyvvm
      181 alalaifsyn kglpfsirsa ffpilgervw gwwghvidil avfstlfgla tslglgaqqa
      241 nagmnfvfgl evsataqvii illvtavalv svwrgleggv kklsefnmam avlffffvll
      301 agptlvalsg fwtglatyvt efvplsapfg reddayrqdw tifywawwvs wapfvgmfia
      361 rvsrgrtvre fvicvllips lfifiwmgvf gsvaldqlya apetslvkey vidsyrpels
      421 lfgmlnelpl talmstvgiv laliffvtss dsgslvidti taggkidapr pqrmfwavve
      481 glvaivlllg gglaalqagv tataipfsiv mllmcytiik alngelrhrh pgka
//
LOCUS       WP_010626958             297 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [Halomonadaceae].
ACCESSION   WP_010626958
VERSION     WP_010626958.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..297
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30608
     Region          5..288
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mtistvgfig lgkmgsgfvs rlidegyavv gydieaahce aakargadia dspaavaara
       61 dliqicvtts aaveavvlge ngiaevaqdg gkvvvdhstt elettrrlaa elerrngmaf
      121 vdapvsggpg aaaegrlaim aggtteaiaa vtpvmerlgq fthmgevgag qatklinqal
      181 vlsnycviae acnlgnrfgi dvskipeals sgyagsnlln dllprmvesd feprgyarqi
      241 lkdlhmlqda analnvampm agmanslysm liaqgkgeld gaaivtlled qarqdna
//
LOCUS       WP_010626959             424 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Halomonadaceae].
ACCESSION   WP_010626959
VERSION     WP_010626959.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..424
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45083
     Region          1..424
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mgliilgifl vlfllgfpvv yailipsaiy vlleglplgl mgqrvtyald sfplvavpif
       61 ifvgnlmnqa gitdrifhfa ntlvgrapgg laqvnifssl ifsgmsgasl advgglgkie
      121 ieamkkrgyg apfsaavtas savvgpifpp siplivygsv tsvsivqlll agivpalici
      181 vllmitaall alrhdmprae rwptlmelnr afipalpall apvlmisgml mglftpteaa
      241 avtaayvvfi savlyreltw shlmfsllat lrttsailii vaaaamfgwi lsveqipqrf
      301 aafilqishe plmlllianl ifliagifld sttatllivp ivappmvlag vdpvhlgivc
      361 ifnlmigllt ppmglslflv ssiakvslrq llkalipfyi plvatlaiit faadlvlwlp
      421 sfmr
//
LOCUS       WP_010626978             427 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Halomonadaceae].
ACCESSION   WP_010626978
VERSION     WP_010626978.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..427
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44766
     Region          19..427
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtlpfmiigl lglilmglpi avalaivatv aivvfqglem lpnigltmfe gassfpllai
       61 pmfvlagaim ntggiskrli afasalfgfi rgglaminig vslffaeisg savadvaatg
      121 svlipamkkr gypssfaaav tsssaslaii ippsipmily gvmsgasivq lfvagivpgl
      181 lgaaglmals yyyarkynwp veevfqfkrv rqtareagwa ltlpiiilgs ifggfvtate
      241 gaglavaaai fisaviyrel dlrtlykaiv dggqqtavvm llvaasalig vfltemrmpq
      301 qlaqavlslt dnkyailmml nvfflliglf lhsaaaiilv vpivmplvga agidpvhfgl
      361 vvclnlaigq qtppvasvli tacsiaktdv wsvtrsnlgf isvllfilll vtyipaipma
      421 lveffyr
//
LOCUS       WP_010626994             342 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Halomonas sp. KM-1].
ACCESSION   WP_010626994
VERSION     WP_010626994.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..342
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37193
     Region          22..342
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mksdvmtrta vqvpmaapae llveirdlhv hfgtprrqvq avngvdltla rgevltilge
       61 sgsgksvtlr slmrllperk trltgsvrvd gqdvlamsrr elsrfrgrta amifqepmla
      121 fdpvfsvgdq iaetvcrheg vsrreglara lelfdrvrip sakrrlanyp helsggmsqr
      181 amialalscr pkllladept taldatvqiq illllrelqr elgmsvifvt hdmgvaneis
      241 driavmyagr lvetgavdtv iaqprhpytl glmhsrasge lrgqrlsaip gappdmsapp
      301 pgcafaprcp hadeictqsl pamselgsgh raacwrlekt as
//
LOCUS       WP_010627015             167 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Halomonadaceae].
ACCESSION   WP_010627015
VERSION     WP_010627015.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..167
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18575
     Region          9..164
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mktllrqtnr gidlfnrlvg wglaglllvm tvlifwqvfa rfvvgrplyf sdeiarfami
       61 wltfigagya yrkglmisvd ivlefagprl arvmrvlvvl asalfafilv kygfemvgrv
      121 snqtapstrv smmwpylavp lggivilvns vallidevvg ndkeers
//
LOCUS       WP_010627016             423 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Halomonadaceae].
ACCESSION   WP_010627016
VERSION     WP_010627016.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..423
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44280
     Region          16..422
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 malllfllli vlfvigvpia fslglasait vwqgelmpml ivaqqyitsv nsfplmaipf
       61 filagylmqs ggisrrlvdf sntmvgsmtg glamvaiits lffaaisgsg aattaaigsi
      121 lipamiakgy asgyaaanqa asgalgviip psiplilygi aanvsvgdmf vagvlpglmi
      181 tlslllfayg yaryhghggg ersswremft agrkallail mpviilggiy ggiftpteaa
      241 viavvysflv gfviyreitl kdivgilqea avttavvlsi igaaglygri lqslrvpsml
      301 snfvigaids pllfivlvnv lllmagmfie aaaailifvp illpiavsfg fdpvhfgiim
      361 vvnlamgmft ppvglnlfva sqiskvgvar ltwsilpfva ivlvnlfiis vvpflstwlp
      421 slr
//
LOCUS       WP_010627079             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [unclassified Halomonas].
ACCESSION   WP_010627079
VERSION     WP_010627079.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..158
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17749
     Region          1..140
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkldrydlki leilsrdgri tksklaeain lsvspcwerv rrlekagiie gyaarlnpda
       61 lvkrtpvwvq ielkqhnaes farfealvhe tpevtecvav gggvdylmkv eadsvdayqr
      121 lidawltsdv gieryftyiv tkavkrpapg lergdfls
//
LOCUS       WP_010627062            1035 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Halomonadaceae].
ACCESSION   WP_010627062
VERSION     WP_010627062.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..1035
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112762
     Region          7..1021
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mmrrgpiawm vnhgvapnll mvllivggll aslaikkevf pefeleivhv aigypgatpe
       61 everslllpm eaaladvdgi demtataneg agrvslslid gvdvmrayqd iqqainaitn
      121 lpaaadpprf slagrarsvm nlqvhgwvdd rllhdvaedl raelqaasgi srvelagnre
      181 revqilldee amrrhgldhr glasriadea ldlasgrlat aegewliryq grrdearefa
      241 elpligttdg gqlrlgdiar vvdgfaetdr evlyngapal slevyqignq tpigisdavh
      301 aqlerlragl pegvylsvsq dtseiyrdrl dlllknawlg lalvlvlmal flearlafwv
      361 tlgiptaflg amlflpwlgv sinmmsmfaf iialgivvdd aimvgenihs yreqghslre
      421 aavrgarema vpisfailsn ivafmpllfl pgflgmifav ipvvvvtvfl vswlealfil
      481 pahlahragg rkpapwlrpl drlrrtlqng lthftqqrfe pflqralnqr lltvslaiav
      541 lalaiawsls grmgfslmpr vesdrvqatv tlpvgspiad drrirdqlld aamalserdd
      601 gprfaasraq idgdrlnvrl tierdslnaw ppsrvarewr eeagdimgaq avrfesdfgg
      661 pgagagltlr lshpdsrale aaatrladel tefegltdid sgladgkpql elrlapegra
      721 lgltgadlaa qlrgplqgvt aieqfvgrhe isvavrlpse erdslghlhq lpirtpdgqv
      781 vplariaeih lgraattlqr vdgrrqisvt adtesdaqin qvvatlqadv fpalqaawpg
      841 leltlggrqq etaenvsals hatwltlial yallaipfrs ylqpllvlaa ipfgvigama
      901 ghaimgfgls vislmgmlal sgvvindalv lidyanrrrr egfgareaiv aaatrrlrpi
      961 mmttlttflg lapmifetsr qarfmipmai slgfgmlfat villvlvpcl ylmleglrer
     1021 werltttvtt qettr
//
LOCUS       WP_010627203             348 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Halomonas sp.
            KM-1].
ACCESSION   WP_010627203
VERSION     WP_010627203.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..348
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37287
     Region          51..319
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mnksntstla pqpglptpaa swydrkglvq igllaflllv plalyflghi yyvnlasrit
       61 liamaavgln laigyggmis fghaayfglg gyvagisayh afdftpvigw piaipgsdsm
      121 lviwlaaill cgllalaiga islrttgvyf imitlafaqm myyfanswpt yggedglpif
      181 lrnglpwvdt ndaltfflic fgglvlslal tsrimksrfg aaltmarlnd trlatagvsp
      241 ypirlvafvi samitglaga lyadlngfvs ptmlswhmsg elmvivilgg vgrlygplag
      301 allfvmmetl lggmteywql flglvllfvv lfakhgvmgw lagrerhe
//
LOCUS       WP_010627207             383 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Halomonas sp. KM-1].
ACCESSION   WP_010627207
VERSION     WP_010627207.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..383
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41700
     Region          12..374
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msdtsfldwp ffearhrdla krleawcqre lprdhadvda tciqlvrdlg ragflegtag
       61 daidvrslcl iretlarhdg ladfafamqg lgtgaislfg saeqkqwvdr trrgealsaf
      121 alseprsgsd vaqldttaer dgdgyringe ktwisnggia dvytlfartg egpgakglsc
      181 flvpadtpgl eirerletis phplarlgfa dmrlpasami gqpgqgfria mavldvfrst
      241 vgaaalgfar raldesldra rnrelfgasl adlqmvqghl aemaldvdaa allvyraawt
      301 kdmgaervtr eaamaklyat draqqvidka vqlhggdgvr kghiveslyr eiralriyeg
      361 asdvqkvvia rsclaqqnnt rhe
//
LOCUS       WP_010627216            1027 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Halomonas sp. KM-1].
ACCESSION   WP_010627216
VERSION     WP_010627216.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..1027
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=110876
     Region          34..1019
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mrtlieaald rsrttlllll alllaglaaw qavpkeanpd vpipiiyvsl alegvspedg
       61 erllvrpmeq elrtiegvrk mtsqasegha avtlefdagf dprqaladvr ervdianasl
      121 pdeaeeprvf evnvglfpvl tlglsgpiee trrlaiarql qdafegvpev leveiggere
      181 elmeividpl vldsygvdfd tlfnlitrnn rlvaagsldt gagrspvkvp giieslddvl
      241 nmpvkvdgdr vvtfsdvgwi hptfkdpagf ariddepalv leiskragan liatiegvre
      301 ildqaapllp eelsittimd qsvtvdqmls ellnnvltav vlvlivilaa mgvrsalmvg
      361 ltipgafltg illiwaigyt lnivvlfali lvagmlvdga ivvseladrh lregqpprqa
      421 winaasrmsw pviaatattl avffpllfwp gvvgefmkyl patvilclia slamaliflp
      481 tlggvfsvra sravhgeemi taggrlyrat lakllawpgm tltialllma lifvgygrfn
      541 hgveffpave penaqvvvra rgdfsalekd aivrrvearl tgmsevqaly arsyaipneq
      601 lgsdvigtvq fqlidwqerr paqvimnema ertadlpgvv lefreqdmgp gagkpivlev
      661 saqqeadsaa tvetirreme rlggfrdied nrslpgiewr lnvdraaaar lgadvaavgs
      721 avqlvtnglq vasyrpahap devdisvrfp hdwrsidqld rltlntsrgq vpishfasle
      781 paprvgtlhr idgqraitle advaagyqpd erlrallaal gpppegvrvn vageqedqee
      841 asrflitafl vaiglmllil vtqfnslyqa llvlsaivfs tagvlmglli ngqpfgivmv
      901 gmgiialagi vvnnnivlid tynelrhagl apydaaleag glrlrpvllt aittvlglmp
      961 mvleinvnlf apslgfgaps tqwwtqlssa iagglvfatg ltllltpcml vlwqrrstre
     1021 atepaet
//
LOCUS       WP_010627229             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Halomonadaceae].
ACCESSION   WP_010627229
VERSION     WP_010627229.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..269
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27487
     Region          5..267
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mtleliwlay valgavvgim agllgvgggg imvpiltalf laqgvplehl ahlalgtsma
       61 aiipastasl lshrrhgavr wetvryltpg ilvgtflatf iaallptrgl aiffacfmil
      121 mslqmlanik pkptrnlpga vglggaglgi ggisalvaig ggsltvpflt wcnvklpqai
      181 gtsaavglpi alagalgyvi ngwgtpglpg aalgfvylpa lllmapfsml mapvgarlah
      241 rlpvtilkri favmmmglal qmvytvfta
//
LOCUS       WP_010627243             502 aa            linear   BCT 01-JAN-2025
DEFINITION  amidase [Halomonas sp. KM-1].
ACCESSION   WP_010627243
VERSION     WP_010627243.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..502
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53557
     Region          4..498
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mdieeyrrhd gmglaelirr gevsrgevfd aacaaierdn phlralvrtr ferarseaeg
       61 idlaaplagv ptltkdllma legeplafgs aslaewkapv esalvtrvre aglailgqta
      121 tpelglmgit ephafphpvn pwnprhspgg ssggaavava gglvplamag dgggsiripa
      181 aycglfglkp srgrvpqgpl hgevwrgavv ehavtrsvrd saalleaing mdeggpypvp
      241 rergflaale rppeplriai slgeplskpl gtrldpevrl avegaartle glghhvewad
      301 ppvdgerlan ayltlylghv tadlawisre tgvpvsrldi epstraiarl gnhlpvrdye
      361 lakrdwnaaa ramgafhrrf dvllmpvtaa paprlgelyp ptwqqrlmal laipglpkla
      421 lkagmlgqla rdalsrtpyt qlanltgqpa mslplhvtpe glpvgvqavg pmgderrlla
      481 laaqveaevq wqrhlprvtq dg
//
LOCUS       WP_010627268             167 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010627268
VERSION     WP_010627268.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..167
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18437
     Region          7..145
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mrpaasldqf dmkilvhlqr egrcsnvdls aavglsespc lartkrlqei gvirgygadv
       61 vleklgshvi vfsevtisnh rphdfrkfet gagkydeive cynvsggydy llkivapdia
      121 hfqalmerll eddigiekfs srvvlrrpla qrgdpltvia tgkpswa
//
LOCUS       WP_010627273             262 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Halomonas sp. KM-1].
ACCESSION   WP_010627273
VERSION     WP_010627273.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..262
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28349
     Region          151..259
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mlhsldprql dprqldsrqa sslpahpsii dlrqfarevt adtagqadgq tdaflanryp
       61 laipacpvei gairleagtg svaelpadef iilcdgcltl drqgqtlala dsasavlsag
      121 agfdwhcpep ttllyirylg ksagegnlia ideaatleps gtplvellig ptpscrnhtd
      181 yrsadekfmc gtwdstpyhr ramesrqyel mhllagavtv veqsgatrty tkgdiclvek
      241 gavwswesre dvkkvyaiyr pa
//
LOCUS       WP_010627343              68 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Halomonadaceae].
ACCESSION   WP_010627343
VERSION     WP_010627343.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..68
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7297
     Region          1..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 matgtvkwfn dtkgygfisp ddggddlfah fseiqaegfk tlqdgqkvtf evtqgkkglq
       61 asnirian
//
LOCUS       WP_010627395             159 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Halomonas sp.
            KM-1].
ACCESSION   WP_010627395
VERSION     WP_010627395.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..159
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17341
     Region          5..88
                     /region_name="Putative_PNPOx"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam01243"
                     /db_xref="CDD:426149"
ORIGIN      
        1 mtdlittevr eaversvlcw latsdeagqp nvspkeifav lddttvvvan iasptssrni
       61 rvnekvclsf idifvqkgfk vtgvarevkv qaadfsrcae pllemagerf pihsvlvvsp
      121 tavepilaps yrfypaette esqirsalra ygvsreehg
//
LOCUS       WP_010627406             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SIMPL domain-containing protein [Halomonadaceae].
ACCESSION   WP_010627406
VERSION     WP_010627406.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..253
                     /product="SIMPL domain-containing protein"
                     /note="The SIMPL domain is named for its presence in mouse
                     protein SIMPL (signalling molecule that associates with
                     mouse pelle-like kinase). Bacterial member BP26, from
                     Brucella, was shown to assemble into a channel-like
                     structure, while YggE from E. coli has been associated
                     with resistance to oxidative stress.; The SIMPL domain is
                     named for its presence in mouse protein SIMPL (signalling
                     molecule that associates with mouse pelle-like kinase).
                     Bacterial member BP26, from Brucella, was shown to
                     assemble into a channel-like structure, while YggE from E.
                     coli has been associated with resistance to oxidative
                     stress."
                     /calculated_mol_wt=27757
     Region          24..252
                     /region_name="YggE"
                     /note="Uncharacterized conserved protein YggE, contains
                     kinase-interacting SIMPL domain [Function unknown];
                     COG2968"
                     /db_xref="CDD:442208"
ORIGIN      
        1 mftmrlhcll lgsllmtapl mttaaladep rgrlvaqaea qldvvpdrat lsarlwertp
       61 avaqheeetd shalreardr leeraatlir aleeagverd disagslavq peyvsprrsd
      121 gdqellvrtr lerpfqvrvd dlerlprlld alteagvnam dgitydltdr daatdealvm
      181 alekasrkae lmartmnvtl gsvvnisetr spiyvprmma msadaresag qvdyspgtiv
      241 ieagvsvswe ien
//
LOCUS       WP_010627414             237 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator
            [Halomonadaceae].
ACCESSION   WP_010627414
VERSION     WP_010627414.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..237
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26820
     Region          6..226
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mnsvapeqts pevrtlaerv fhqlqdaivr gelapgskit epglsktygi srgplreamr
       61 rleahrlier vphvgarvvk lsmkellelf dvrealesma arlaaqnmtr eeiaglrevl
      121 alherqadlk sgeayyqreg dldfhyrivq gshnrmlmtm lcddlyylvr lyrtqfsasg
      181 trpqrafveh hrivdaieag daelaellmr rhvsasranv adryaatlkq qqaeetv
//
LOCUS       WP_010627421             298 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Halomonadaceae].
ACCESSION   WP_010627421
VERSION     WP_010627421.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..298
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31878
     Region          4..291
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mtaqiiatll pvfliagcgt lygrfrtpdi rslntlnmei fvpmlvfavl adgqapleey
       61 aglalaaavv vlgsglvlwp lvkllrlepk tflppmmfnn sgnmgvpllv lafgeaalpa
      121 avvvfiveml lhfsvglyml sprtplwrll rmpivlasla glgvnlggvp lpgwllealh
      181 mlggvciplm lfalgvrmld idfrdwktgm lgavlcplsg lilalpmilw leltglqaav
      241 lwvfaalppa vlnylvaeqy rqepqkvasl vlignlgslv vmpivlalvf lhvypgaa
//
LOCUS       WP_010627456             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Dps family protein [Halomonadaceae].
ACCESSION   WP_010627456
VERSION     WP_010627456.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 157)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..157
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=17688
     Region          4..157
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 msdtnaiglh essasqlaek lnallanyqi fymnvrgyhw nvkgpqffel htkfeefytd
       61 lltkvdevae riltlghkpv haysdyvams qiredkdvhd geacvrgvlq gyqtlielqr
      121 ellalasdad degtaaqagd yireqektvw mlnaylg
//
LOCUS       WP_010627493             318 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Halomonas sp. KM-1].
ACCESSION   WP_010627493
VERSION     WP_010627493.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..318
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33112
     Region          1..309
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mleilaittp iflligagyl amgtrlvnre qmqgvatfvl yfalpalvir avtqnpldev
       61 lqphyllayg lgslavfafa llltlglqrk plsegaihal gmsasnsgfi gfpvaamvlg
      121 aspaavflal nmlienllii pmalilaevg rqrgagiatv arktlfrlir npilvglalg
      181 lllavtdtal prplaqavdm lanasgpaal fviggtlfgl qvrgmmndvg qivagklilh
      241 plavlgvfll ipeadpmlla gallfacapm isvfpllgqr yglagvsaat lmvatlaafv
      301 tlsmgiwlmd lasllptr
//
LOCUS       WP_010627535             332 aa            linear   BCT 01-JAN-2025
DEFINITION  porin [Halomonas sp. KM-1].
ACCESSION   WP_010627535
VERSION     WP_010627535.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..332
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36226
     Region          10..332
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mttlqrltlt plafalatav sgqaladtqh sgptfsgnvt ggvldvsdrd ldlwafraea
       61 gvggvytvnp slrirydlva dfanainsvd eqtwtpgayr qddgeiylrt arvllmtdyg
      121 tiglqprvps gswgqiynni dvfeynrfha qtgqnaifgq geqgfnvlsy gsprfggfqv
      181 igavlttnaq ndqdfdvvsg rlvynegpln fgightevrr pgidnlhrta fgigydfgmv
      241 qlggvyernd drensnsasd fdawgvnvsa nlsdawsvsl gyaennrnfd ldndawvgiv
      301 rhhfndkvyg fleaarydrt dnnvaaglsv sf
//
LOCUS       WP_010627614             323 aa            linear   BCT 01-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Halomonas sp. KM-1].
ACCESSION   WP_010627614
VERSION     WP_010627614.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..323
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35500
     Region          14..228
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(57..58,60,74..76,82,84..85,126,227)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(57,59..60)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(82,85,88,95)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(118,122..125,127)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(123..124,147..149,200..201)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          240..323
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mdtanqrltl aidqridepg giarlrlrsl dgtplalfta gahldvhvrd geidlwrqys
       61 lcsdpqvnef yeigvlrdps srggsetlhr iarvgetlei egprnhfplh eeapqsllfg
      121 ggigvtpmma marrlralgk dftlhyctrs rsvtafrgev eaaglsdfvv yhhddefetk
      181 ldldaelaaa regvhvyvcg pqgfmewvis rarefgigde rihreffsad vdvsgdafev
      241 vaersgvtvs vgseetiaka lakagvkvdv kceegvcgtc vadvlegeid hrdhflteee
      301 kqegelmcvc csrakgkriv ldl
//
LOCUS       WP_010627621             465 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Halomonas sp. KM-1].
ACCESSION   WP_010627621
VERSION     WP_010627621.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..465
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49085
     Region          1..413
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mgvgfiiffv vsaaspfsvl aggfpigmml gngagtpvli glvlavllif svgyttlsry
       61 vtnaggfyay sarglggiag gaaaglaifa ynilqiglyg mfggvaagtm savfdlhlpw
      121 wiyslvamas iaflgyrkid lsakvlcviv mveylvilvl nvailssggd sgvnfdslqp
      181 qhvfsgapsi gllfcfaafi gfeattiyge eaknprrdip latyaailli gcfyavstws
      241 miigvgvdki vptlyaledp ttliyglsdh yvgpemtqii rvlflvgiya glvafhnsaa
      301 ryfyaigrdg llpsalgtth pvhqsphvgs llqtliaata vmafaafggd pilqlfawfs
      361 slaalslill maitsvavly yfrrhpelgv gpwrgkilpa fsclalltml viavmhfdvl
      421 tgsskvlsyg lcilialala vggamamrlr qtspeqfqql gshrl
//
LOCUS       WP_010627703             150 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Halomonadaceae].
ACCESSION   WP_010627703
VERSION     WP_010627703.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..150
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16317
     Region          5..140
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msneyrhilv avdltkdshk vleralqiae rnqaklsimh tleplgfayg gdipmdltsi
       61 qdqldehakq rlaeiadphv akenqhvlvg mpdteihrfa eersvdlivv gshgrhgfal
      121 llgststgvl hgaqcdvlav rvgkkgesae
//
LOCUS       WP_010627717             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleoside deaminase [unclassified Halomonas].
ACCESSION   WP_010627717
VERSION     WP_010627717.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..145
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15672
     Region          1..131
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mdhymqaaid earkglaegg ipigsvlvhq geiigrghnr rvqagstvlh gemdalenag
       61 rlsasvyrnc tlyttlspcp mcsgaillyg iphvvigenq tflgeeellr srgvavevlq
      121 leecielmth fvesapelwn edige
//
LOCUS       WP_010627721             155 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010627721
VERSION     WP_010627721.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..155
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17936
     Region          5..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mrnlkldrid rmllealqqd arlttaelae lvnlspspca rrirrleqag litryraeld
       61 ktlldlmvts fvqvrldqhq reqvehfeha vrdmpeviqc hsvsghfdyl lqvittdida
      121 ferwlrhfrq lmavsavdss fsirtikeng alpiq
//
LOCUS       WP_010627776             146 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Halomonas sp. KM-1].
ACCESSION   WP_010627776
VERSION     WP_010627776.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..146
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15265
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mfksilvpvd gsegakkald vacllanqad atlhllhipe elshettlvw gigaiaieas
       61 rteredigrq vvekaaeaar angvaqvetv vgqgdparti vsearrrgve aivmgsrgls
      121 dlrglvvgsv shkvshvaec tvitvr
//
LOCUS       WP_010627779             392 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Halomonas].
ACCESSION   WP_010627779
VERSION     WP_010627779.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..392
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41122
     Region          3..339
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mpfnvmllsl cqallvsgni lliavsplig arlapdpaws tapvatqwlg lmcatipasl
       61 imahlgrkrg fllgnlvgla gvvvaaqalv teaftlfmlg twligigigf gqlyrfaave
      121 aaplalrdra iglvmgggvl aaffgpwlar isreaavtpf lgsfiglgal ylvallvlla
      181 trlppaekth gdgqprplge ilrqpvfvva vlsaligygv mnlamtatpl amagaghhfd
      241 hvattiqwhv vamflpsfft ghltarfgap rmiaagcvll aasglaaqve agvagfhfal
      301 illglgwnft flpatgllte tyrpvekart qaaneflvfs tvavtallag plvnqlgwal
      361 lnallvplsl vpimllgwqr larrrqdphi sg
//
LOCUS       WP_010627810            1000 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Halomonas sp. KM-1].
ACCESSION   WP_010627810
VERSION     WP_010627810.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..1000
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=107874
     Region          46..999
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mswmlaslry krliltvtll lallglaawv amdrqedpff pyrfgqvlvp ypgaepeqve
       61 rlvlnpleee laqveevndi igtarlgvah vtiemhehvy dtdaaweqvr iavnramrqf
      121 pdgvgeaeis drdsdthgiv lavtgsddll elreaakrlr rdlfrlkevs ridlladpgq
      181 qvvvgwddtl aemtgldara lgdqlamrnl tssggtlema grslvldpit efgsleelaa
      241 tpirtrqgdl vplgeltdvs lapqepatar mwhdgrpava lgvvlandrg navrfgkqlr
      301 alvdelrpay aplaieetfy qphwverrla elgfslllgv ailgvllfla mglrlglavm
      361 vivplvtfsa lalyamgggv lhqiavagmv ialgmlvdna ivmveniqyh rdqgrsamqa
      421 vtrsvrelat pllaatgttl aafvplllsg gntadftrai pimvmltlav syvyavfvtp
      481 vfaagilkpr lavgrerlqa igqrvgrvav rwplavlaga gvllvaaiam lplldqdffp
      541 dtdrnqlivd lnfpegthld ytayqaevla aelavrptvq avhrfvgfsg prfyynlveq
      601 prqshlarlv veaesaddls almtwvrava pewlpeaevv arrlgqgppl eapveirvfa
      661 edrtaladaa gailsvvrea egardarhrl geglatlrve tddaraaeyg lsrhdvamal
      721 agasrgievs awragrdpap llvrapeger fslegleglr ltatdgrslp lgeianltpa
      781 wrpaviqhrg lqrmtvvlae vadgwtydgv lgdilprlea lelppgvsys vggaaesagd
      841 antalfqtlp fgglllvvfl laqfnsfrql fivlttlpla iigvvpglwl agqpfgftai
      901 lgvvalvgiv vnnaivlidl mnanrrqges vseavvsava rrtrpvlltt attvaglvpl
      961 tltqstlwpp mawaiisglv astlltllvi palyrllmrd
//
LOCUS       WP_010627820             312 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK 4TM domain-containing protein, partial
            [Halomonas sp. KM-1].
ACCESSION   WP_010627820
VERSION     WP_010627820.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10606305
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..>312
                     /product="DNA translocase FtsK 4TM domain-containing
                     protein"
     Region          25..197
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
ORIGIN      
        1 mprrateesp qqpttrlaih lqgvaregai illlaacvfl llalfsyqgt dpgwsrrgpe
       61 tevgnwmgpf gawladvlys lfgasalwwp gmlgfagwwl irhrrvqiew datavavrlg
      121 glvllllgtt tlgalhfysp nsvlpyasgg ilgeglvgal vplvdsggtg llavaamlcg
      181 fplftglswl avmdelgyrf lrlwrwaasp fglvrerhep hwregddqeq netehdaeaa
      241 aepaprrwrf wqrrrggada evpslrepgl eptfgddgdt dipwevpert psakrpdaay
      301 tarrddvaag ar
//
LOCUS       WP_010627821             694 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK [Halomonas sp. KM-1].
ACCESSION   WP_010627821
VERSION     WP_010627821.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..694
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=74627
     Region          117..691
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mptaamplra tddvqtpaak atspgfqppd petvsstaep aapepaaprg earrepglgd
       61 lqpeestday eprlnwndvg gddfeddgdl deanadeamp pqtasaaqrp taytdqaegl
      121 rawresagrs aatdepsltf iddeeedese sggrvataeq araaaaepdg ptlwtvehlq
      181 sqrptlddmp epdgelpslr lltppephqq nyteqqladm aelletrlre ygvkaevvht
      241 wpgpvitrfe ikpaagvkvs kisnlakdla rslmvksvrv vevipgrptv gieipnphra
      301 mirlrevids dryqqeasal tlalgqdigg gpvvanlgkm phllvagttg sgksvgvnam
      361 lismllkatp delrlimvdp kmlelsvydg iphllapvvt dmkeaanalr wcvaemerry
      421 klmaamgvrn iagfngklde agragaqvad plwepqpwem heappvlekl pyivvvidef
      481 admfmivgkk veeliarlaq karaagihli latqrpsvdv vtglikanip trmafqvssk
      541 vdsrtildqg gaenllghgd mlylpagsgl ptrvhgafvd ddevhrvved wkrrgepeyv
      601 deilsggvsa daltgleadm gegggdaeqd alydeavqfv tesrrasisa vqrrfkigyn
      661 raarlveame aagvvssmgt nggrevlapp pvgn
//
LOCUS       WP_010627937             244 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Halomonadaceae].
ACCESSION   WP_010627937
VERSION     WP_010627937.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..244
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26170
     Region          20..243
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msdsaivnkd eliqrtasgk vmlacrdltr iyhegpqdvt vldslslevr agervavvgs
       61 sgsgkttlln llggldrptr gevaiagesl ldlgeaalgk frnrhigfvy qfhhllaeft
      121 alenaalpli vrgmrkkaae aqarellvkv giehradhkp gelsggerqr vaiaralvtd
      181 pslvlmdept gnldqataas ilalmdelar ttecafvvvt hdtslaahqd rvmkldggrl
      241 teqh
//
LOCUS       WP_010627967             278 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Halomonas sp. KM-1].
ACCESSION   WP_010627967
VERSION     WP_010627967.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..278
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29523
     Region          11..271
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mkqvliaate laqalekdga pqvfdcrarl gdldagrrlc eaghvpgslh ldldrdlaae
       61 pgaggrhplp saddfaatlr rlgvtpqrpv vvlddmggql aaarawwmla iwaghpdvrv
      121 ldgglkawqe aggelvlgqe plpepsqwqp afddsariaa devfsgrelk vdarseerfr
      181 geaepidpva ghipgavcrp satnladtgr fkapealeae lpraeaivay cgsgvtachn
      241 ilayaiagrs lprlyagsws ewvrdpsrpv arsgrgna
//
LOCUS       WP_010628007             275 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Halomonas sp. KM-1].
ACCESSION   WP_010628007
VERSION     WP_010628007.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..275
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30314
     Region          9..258
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mpthrlcsen lsvgyenrlv lesvdfrvae grltvllgpn gsgkstllkt lartltplrg
       61 rvlldghdih hhrtrevaqr lgilpqspsa peglkvrelv gmgrfpyqri wrqwsqeder
      121 avseamslaq vtefaerpvd alsggqrqrc wiamvlaqet dlilldeptt fldlkvqvdl
      181 lellvrlahe rsrtllvvlh dlnlaaayad vlvmmragrv ehrgspddvf taanlkqvfg
      241 ldaavmrapn tgrlvcvpal ggtaargtir eetpa
//
LOCUS       WP_010628013             700 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Halomonas sp. KM-1].
ACCESSION   WP_010628013
VERSION     WP_010628013.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..700
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77395
     Region          4..700
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mptprplals ialvsalvas haqaqrpeea qtetleamti tgqaatktet pfvetpqsts
       61 tiereewesr gaqtvqrald ytpgvftnqi gasnrfdylv lrgfsdgsls ntfldglklm
      121 gdtnshssmt idpwfldsie ivrgpasvly gqaspggvva ltskrpqfeq ggevrlstgn
      181 naqrsvafdl tgplgeqqrv ayrlvglara adtqfgpvee eryaispslt wdlndatslt
      241 lkaylqqdpe ggyhaglpye gtvvdrggrr isnnffeged eydkyqrtqr llgyelehrf
      301 neawtgrqrl nylnadvtln qvyaygwmpg sdseliryys gadesleawt ldnqleasls
      361 tgfidhtvlv gadyqrrdnr vewpsgmfpn vdafdpqyga gpiamyaptr edhelrqtgi
      421 ylqdqmalgn wrltlggryd wvditntnld sndtselddt qfsgraglly lfdngmapyl
      481 systaftpts fvdaegdllp pmegrqvetg lkyqpagtrd rysaalfqin qenvatkeqp
      541 idpyravgei eskgleleay thltdslrlq vaysytdity krsddgnegn raiyaprhqa
      601 slwghyvfqn gtlagldagf gvrhyadiqa drantarvpa ytlvdatlgy dlgglgldgm
      661 sarlnvtnlt neeyvascns lefcyfgaer gvlgtlsyaf
//
LOCUS       WP_010628098             513 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PH domain-containing protein [Halomonadaceae].
ACCESSION   WP_010628098
VERSION     WP_010628098.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..513
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=56792
     Region          16..504
                     /region_name="YdbT"
                     /note="Uncharacterized membrane protein YdbT, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3428"
                     /db_xref="CDD:442654"
ORIGIN      
        1 mseasplger qggelkwqrl spwavlllll sgsasllrqh mplvlgagag lalverlglr
       61 elalggavll ilavlislly yrrfryccdg dvlivqkgll ehrefkvaar hvqsivirqp
      121 vymrpfglvl wevetlagea srialpgirr eraealerel rppeqwpgva sesapaaerq
      181 vvpcfaisgk aivlhglasr siyliaamls plvrplerwl hdrlpqldld twmpgsplla
      241 vlvgllaalt llallailaa wwrfhgfvll dagerqiqrs glfhrqeqtl slarlqvvew
      301 vqtglgrllg rgylvchqyg alggdagesr rflvpglsea qgaaltahfw qtysrqsdsr
      361 qgaagqplrr vdpsyrrvlf lryllllagg avlvlgvlip lelswpawsg laavlpllaa
      421 vlahwrwiat gwaqeqgflr vrrgvvgqrt gifpmqhlis lrlqqswlqr rrgvatlhle
      481 langrqtlpy lkeddarrla dtllftaesa qlv
//
LOCUS       WP_010628105             216 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [unclassified Halomonas].
ACCESSION   WP_010628105
VERSION     WP_010628105.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..216
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23532
     Region          <87..216
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 mkeaketrge gsrhwpfagl llvallvltl gqtvhaqqde aaetdaeeqv eeaadeaiad
       61 eaaddtagqd aaalaeqlea herqlraaqr eiaalrarlp aeeggeidld galrsasvtm
      121 gairstrael mraggrdeal lesidelvee lerdqrlvar aldanlyqvr rgdtlasiag
      181 rfygssqrwq elheanrhvl enpdlvwpgl tlvipr
//
LOCUS       WP_010628111             196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Halomonadaceae].
ACCESSION   WP_010628111
VERSION     WP_010628111.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..196
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21826
     Region          37..182
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtspnplpde asayladprr epleldiegg rgpapfrwlt rlmehliati lvalivsvsa
       61 nvigrsllnr slpwadelar mlfiwlifig aaaafaryeh iavdflvrrl qpraayalyl
      121 lqhliiatlm simvwggylv msrstgrtai lgvpwnlinv slvlcslfiv avalwrawqc
      181 lrlirdpnld qpqagd
//
LOCUS       WP_010628135             157 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [Halomonas sp. KM-1].
ACCESSION   WP_010628135
VERSION     WP_010628135.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..157
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17310
     Region          1..128
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mllegschcg avrfsvesph pypyqrcycs icrktagggg yainlsglae tlqvegaehq
       61 gvyhavidgq kssgerhfck qcasalwvfd pnwpelvhpf asaidtelpv ppervhllld
      121 rkaawvevea kegdqcfagy peesiaewhq rrglemp
//
LOCUS       WP_010628132             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Halomonas].
ACCESSION   WP_010628132
VERSION     WP_010628132.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..197
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21056
     Region          1..182
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslamilpms afalaasisp gpvnlvclss gtryplsqgl vfvtgatlgf ivlfvavglg
       61 lysalalvpg ltqalrwagv afllylswrl frddgrlpen eaqrapgfmt galmqwlnpk
      121 awlasasgig aytsgsdlnq vllfaalylp icwlslgswv yagaflrryv hrptvlvtin
      181 rtlalllaas clyllle
//
LOCUS       WP_010628137             336 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010628137
VERSION     WP_010628137.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..336
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35965
     Region          9..329
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mqtpsptlrt ivilgfdgiq aldlvgpmev fskantycpa gspayrvlla sprggdivsn
       61 aglriagtep lsalpnsvdt livaggdeag lrkvaaegel ldwlqqrads frrlasvctg
      121 afvlaaagll kgrraathws acdtlqamwp dievdrdaiy taeppfytsa gvttgldlcl
      181 alveddcgaq valnvardlv lfmrrpgtqa qfsvalraqg aassrlaplv aqivddprgd
      241 lsvpamsarv gmsertfvrr fraelgetpa qfvkqvrver aktllettrw plariadrsg
      301 fsgldalhrt flkqvgvtpa ayrsyfgvrt nesddk
//
LOCUS       WP_010628147             434 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Halomonas sp. KM-1].
ACCESSION   WP_010628147
VERSION     WP_010628147.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..434
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45662
     Region          5..433
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 msipliasaf fimlslmlls ipvavailfv gviggylmhg fplvdmmggv vwsslnspsm
       61 laiplfmllg elllrggiad rmyaalsvwf nrlpggllht niatctlfsa tsgssvataa
      121 tvgtislpal qkyrypvrps lgslaaggtl gilippsinl lvygqlants vsqlfaagli
      181 pgltlallfs vylfiahgka gstslvevnl plreklalsr hlvppfvifg vvmgsiyggv
      241 atptesaaig vmialafivg ggklsldlli hcslhaaktt gmviivlmca lllnvtlsml
      301 gvtqaltqwv asfgltqvgl llvlllfyvv lgtfmdamsm lvltvpitvp mvmavgvdpi
      361 wfgifivlmc eialitppvg mnlfvvqgvr kdggsfndvi wgslpfvaim alftltimvw
      421 pqivmwlpdl lagr
//
LOCUS       WP_010628206             503 aa            linear   BCT 01-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Halomonas sp.
            KM-1].
ACCESSION   WP_010628206
VERSION     WP_010628206.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..503
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=52706
     Region          1..493
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mfesllnalp valqfeslis lfvgtligil igalpglnpv maialmlplt ygfdpiialg
       61 lvagiyngsm yggsipaill nipgtpaaia ttfdgypmtr kgegglalkt acwssaiggi
      121 vsalalmtla pmlakvtlaf gpaeyfwvav fglvsiallv gkdaskgmlc allgviiglv
      181 gvdtisgaer ftfdtlylvg gfellvvlig lyavppvlem aekrnesyfn aesfrvspgg
      241 galgllrrhw rtwsrsslig vavgilpgag gnlaallsyn eakrkspdpe sfgtgnpvgi
      301 aaaesgnsad naaamipslt lgipgnliaa lvlgalmihg lqpgpqlftr apdvvfgfmw
      361 qmlltamlll llggmvatrl faqvlrmpsa llvpttlvlm avgvytvngn vmdlyvmlgf
      421 gllgyllnrl gfplapvvlg vllgpmaeqn frltmliaqn dwtvlftrpi slgivallva
      481 vllsqlwktl rqrarsaahs qqr
//
LOCUS       WP_010628223             409 aa            linear   BCT 01-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Halomonas sp. KM-1].
ACCESSION   WP_010628223
VERSION     WP_010628223.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..409
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44957
     Region          3..322
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 makeerkhid lalqgggshg altwgvldrl leeerleidg vsgtsagamn avvladglhr
       61 ggregarqal hdfwsgvsda arfspiqptp wdqlmgnssl dnspsylmfe sltqliapsk
      121 lnpmkfnplr dlvcklvdfe rvnacrkakv yvtatnvrtg rakvfsqpei tvdtvmasac
      181 lpfmfpavei dgeaywdggy sgnpalfplv ddmdcqdlvv iqvnplirqt lpdsardiin
      241 rineitfnts likelrsiql lqqlidaegl everyrsmrl hlihaekeve qlsassklna
      301 qwdfvsrlyr qgrgwadlwl kenfdklgqc stfdlnavfs dtfrplarps gtsqdvaaae
      361 qdkpsaeeps arlpadkqpt dkastskast gkapsrndss tktgkgdes
//
LOCUS       WP_010628268             496 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tripartite tricarboxylate transporter permease
            [Halomonadaceae].
ACCESSION   WP_010628268
VERSION     WP_010628268.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..496
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=51611
     Region          1..494
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 meafnnlmyg fsialepini lyvfagvfag tiigmlpglg pisalalmip ltfgmepssg
       61 lilmagvyyg aifggstssi llnapgvagt vatsfdgypm akqgmagkal aiaayasfig
      121 gtvsiiflml vapllgrvav sfgpaeyfsl mvlgltavvs lsdkslikgl iaavvgvmis
      181 imgidlqtgt erftfgtvhl ldgidflvva lgifaltevf fmllrggggk eqprnaigsl
      241 klsksevkei aapigrssil gfftgvlpga gatigsflgy smekrlakdg dtfgkgnikg
      301 vaapesanna actgsfvpll tlgvpgsgst avllgallvm gvspgpamlv drpdvfwgvv
      361 asmylgnifl lvlnlplipl iakildmprp lllslilifc mlgvygmsfs vfdlllllgf
      421 gllglgmrlf gfpaaplila lilgdimees mrralqisgg dwsifidkpi smwlliiaal
      481 sltlplikrm marrsv
//
LOCUS       WP_010628312             433 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [unclassified Halomonas].
ACCESSION   WP_010628312
VERSION     WP_010628312.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..433
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45043
     Region          1..432
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mknilerhfk ltehntsvkt eviagittfl tmayiifvnp silsetgmdy gavfvatcla
       61 aavgclvmgl wanypiaqap gmglnaffty gvvlgmgysw eaalgavfls gfcflllsif
      121 kvrewiihsi plslrlgiaa giglflamia lknagivvsn patyvalgdl sqpaaiyall
      181 gffaitamay lkitgavmig ilgvtvlami lghnqygglm smppsiaptf mamdlmgald
      241 vamlsvifaf lfvdlfdtsg tlvgvahkgg lldkdgklpr lnramisdss asmagavlgt
      301 stttsyiest agiaaggrtg ltavvvaglf lislffapla gsipayatag allyvavlma
      361 gslahanwdd ptdaapvlia alampltfsi aegialgfis yaaiktlsgr frdlnpavvv
      421 lailfvlkfl fld
//
LOCUS       WP_010628317             413 aa            linear   BCT 01-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Halomonas sp. KM-1].
ACCESSION   WP_010628317
VERSION     WP_010628317.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..413
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42287
     Region          14..413
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mnehvaaaqa paeslprvll tgaqmlfvaf galvlvpllt gldpsvalft agvgtlvfhg
       61 vtkvtvpvfl assfafiapi qgsvvnfgvp atmgglmaag lvyvaisqav rlkgtawlhr
      121 llppvvvgpv imviglalap vavsmatget sdnigygpai flsmvsllvt lvlavfgrgl
      181 lrlvpimggi vtgyvlallm gvvdftpvqd aawlampaft apsfhwaail fmipvaiapa
      241 vehigdmiai gsvtrknyle kpglhrtllg dglatttaal fggppnttys evtgavtltr
      301 afnprimvva aciaialafv aklgallqti pgpvmggimt llfgsiavvg mntlvraghs
      361 ltaprnlvvv slilvfgigg mqfgggqftl qgvslaalvg ivlnwvlpta dee
//
LOCUS       WP_010628376             439 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Halomonadaceae].
ACCESSION   WP_010628376
VERSION     WP_010628376.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..439
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47874
     Region          1..420
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtlfselglr aellsaveaq gyttptpiql qaipavlkgg dllasaqtgt gktagftlpm
       61 lqrladgprp gkrqvralvl tptrelaaqv gesvsdygrh ltltshvifg gvgqqpqvda
      121 irpgldvlva tpgrlldlqq qkhvdlsrve ilvldeadrm ldmgfihdik kvlrllpgkr
      181 qnllfsatfs deiqaladkl ldnparieva rrnttaetvd qaiyrvdrek krellahlis
      241 qhgwhqvlvf trtkhganrl aeqlskqdip amaihgnksq sartralssf ksgdlqvlva
      301 tdiaargldi selphvvnfe lpnvaedyvh rigrtgrags egqaislvcv dehgllkgie
      361 rlikrdlekr iepgfepdpn akpepiengr nrrggrsgqp rqgagsgqts qrnsggnsan
      421 gdaqaprrrr srgqrtrra
//
LOCUS       WP_010628391             459 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Halomonas sp. KM-1].
ACCESSION   WP_010628391
VERSION     WP_010628391.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..459
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48481
     Region          24..456
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 meptssladk adgrpsarat gqgsswldsy fgasrrgssv rteilagiat flasmyiivv
       61 npailshagi pfsaalsatv lisfmsslam glyarnpilv apgmgmnalf tytlvqgagl
      121 swevalgcvf wsgvlfatla mfnvreaiin aippslryai tcgiglfitf igfknagfiv
      181 gsdatlvtlg smdaslitff igmmatailv imryngalil gialttllat pmgrlwggdv
      241 vvewsgiaaw pdfsavmqvd iwgalkvayl pfifvmlftn ffdalscfma lsesadlkdk
      301 dgnprnlkrs mtvdafasmi aaplgtsaaq tfiesgagva qggrtglvav tiafmflpfl
      361 flspllslvp giatapalvl vglfmlapvs kidwtqfeqa fpaflaiilm pltysitlgi
      421 afgflsfvli klatgklydi kpamwvsaal svvmlvtth
//
LOCUS       WP_010628438             217 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Halomonas sp. KM-1].
ACCESSION   WP_010628438
VERSION     WP_010628438.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..217
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24358
     Region          2..73
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(13,15..16,18..19,22..23,67,70..71)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(13,52..54,65..66)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(52,64..65,67..68,71)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          87..201
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(90,97,159,162..163,166,170)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(90..91,94..95,98,134)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(97,101..102,105..106,167,170)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mklvignkny sswslrpwll lrmhglpfee iriplaqdit realaahnqa gkvpvlhdge
       61 ltvwdslaic eylsecylsg agwpasrher aearalsaem hagfvelrtc mpmncrangr
      121 rvsisetlea eirrieqiwt qgseryghrg pwlfgefsia dcmfapvafr fasygvklsp
      181 paeayrqtll rsgpmqewve qaraepevie saevgtp
//
LOCUS       WP_010628536             357 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: microcin C ABC transporter permease YejB
            [Halomonadaceae].
ACCESSION   WP_010628536
VERSION     WP_010628536.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..357
                     /product="microcin C ABC transporter permease YejB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042884 - microcin transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40022
     Region          1..356
                     /region_name="YejB"
                     /note="ABC-type microcin C transport system, permease
                     component YejB [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4174"
                     /db_xref="CDD:443333"
ORIGIN      
        1 msryilrrll lmiptligim llnfiivqaa pggpidqmla rfegmdamas trldagggdv
       61 vvqdesrgar gvdprfieql eqqfgfdqpa hirfltmmrd yatfdfgnsf frdrpvvelm
      121 ierlpvsisl glwttllvyl isiplgirka lhhgsrfdvw tsglvivgya ipgflfaill
      181 ivlfaggsyw dlfplrglts pdfeelstwg kikdyfwhit lpvtamtigs fatltmltkn
      241 sfldeihkqy vltarakgas drrtlyghvf rnamliiiag lpgalvtiff tgsllievif
      301 sleglgllgf eavmqrdypv ifgtlflytl iglilklisd ltyvwvdpri dfetres
//
LOCUS       WP_010628560             184 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter small permease [Halomonas sp. KM-1].
ACCESSION   WP_010628560
VERSION     WP_010628560.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..184
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20510
     Region          3..161
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 myrsivifsd wldwltrrla vlcltamlvf vaiqvvarya fsappswtee marymmvwsg
       61 llgatlsfks kddpalfkdp mqdkgspwwq ltalvrgtav liflvpiiyf sifgpgmdtt
      121 rgfiarqarl sadtlgfpms wvamavpica aiilvhllar acelkmaest rmsrisgqep
      181 rgpr
//
LOCUS       WP_010628562             427 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [unclassified
            Halomonas].
ACCESSION   WP_010628562
VERSION     WP_010628562.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..427
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44600
     Region          1..424
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mayviaafmv flttgtafay lmgatailaf iaagypqyla ivpqrifsql dvfafmampl
       61 filtgelmnr tgvtralidl amallgrlkg glghvnimts lffsgisgsa vadaaavsnt
      121 lipamrergy spyyagaita assmigpiip psiimiiygg ltgtsvaalf vagilpglll
      181 acmlfgmngw larrenhpgg dtievpplra sflkaapala ipviilgsiv fglttptega
      241 alavvaailv grllgamtpk lfyeaaeata rltgaifiil caiavlsyla gllgwpqlls
      301 gwvesagltg trylilligv lliagmfmdt pvaltllvpl laptallqgi spvhlgivvc
      361 fnlciglitp plgkclivva aiakldywrl alatlpfiav qivtllmiaf fpeislslpr
      421 ifgfkvd
//
LOCUS       WP_010628638             139 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Halomonadaceae].
ACCESSION   WP_010628638
VERSION     WP_010628638.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..139
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=15774
     Region          15..133
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mketieivse rnrilrqrvr iagfedlyvd vpkafggees apdphdyfdl slgackaita
       61 qmyaqrkqwp legvsvrvnr dvseerkgiy rlevvmtfhg iedeaqrlrl eeishkcpih
      121 rlmtsatvev ttrstvdaa
//
LOCUS       WP_010628641             259 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Halomonas sp. KM-1].
ACCESSION   WP_010628641
VERSION     WP_010628641.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..259
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28435
     Region          2..252
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mlidahchld feafdddrea mferaraagv ghflvpgttr erwpavlalg erddvhvslg
       61 lhpyfmhehg egdvealarl ldehpevral gecgidarfe ealddqwqlf daqlrlakar
      121 rlpvvihcvh andkvskrlr qldlpaggli hafagspdqa wkfldlgfvv glggavtyer
      181 aqrlwravks lpedgfvlet dspdmplcgy qgqrnepari vqvcemvarl rgetpeavaa
      241 qstatagrvf gldlgegaa
//
LOCUS       WP_010628651             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010628651
VERSION     WP_010628651.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32937
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(107..108,110..111,114,118,120..126,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 mtikqlrafl avaqtlsftq acerlhlsqp alslaikgle etlggpllir strsvrltpe
       61 getllplakr lladwdnaee llrqrftlql grvalaamps iacnrlpral rrfrlrfprv
      121 nvtvhdvine qvidmvrqrq velgiafepe tregidflpl fddtfvavlp pdsplaeaes
      181 vdwkallahd fitlqrpsmv rilleqalar qqselpvafe shqlatvgrm vasglgvsav
      241 pslcreqmhe lgarcvplfe pqirrtvgiv lgagqelsta aralhevlqt tlcesppt
//
LOCUS       WP_010628660             199 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar transferase [Halomonadaceae].
ACCESSION   WP_010628660
VERSION     WP_010628660.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..199
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22558
     Region          <1..181
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mkrlfdivvs llalillspv mlvvallvrl klgapvlfrq trpglhgrpf emvkfrtmld
       61 avddsgqplp naqrmtrlgs vlratsldel pelwnvlkgd mslvgprpll meylplytpr
      121 qarrhevrpg vtgwaqingr nalsweqkfe ldvwyvdnrs lwldlrilll tvkkvlvreg
      181 iahdgdvamp rfrggshhe
//
LOCUS       WP_010628668             481 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Halomonas sp. KM-1].
ACCESSION   WP_010628668
VERSION     WP_010628668.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..481
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50863
     Region          18..381
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlnrlvvpar kllpthafar gvsvlvggta gaqlltllaa plltrlyape dfgllavygg
       61 llalftvvas gryqlaiplp etereasavl alsllvvclt tmvslllval ggrglaellg
      121 vpalapwlwl lplgvafagg yqavshwavr trafstiaat rikqslallt iqllaspmgg
      181 aglllghaag qgagtltlar palravrqhg vtprevwava rryckfplfs twsglfntlg
      241 kqlppllfaa lfspvaagly alahrvlamp mtligeaigk vffasaaeah rrgelgalva
      301 rvhgvlaqla mpaaivlvls gpelfalvfg erwreagefa rwmapwlymv fitsplshlf
      361 tvlerqgqgl ifqtvllvvr vaaiatgaaa ndllltvalf slgsalcwig flawiarltg
      421 nrpvslalst ltallmslal laplvvvetl gpvwlpwgaa lllsaalvgi rylllfrkay
      481 q
//
LOCUS       WP_010628749             100 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010628749
VERSION     WP_010628749.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..100
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11337
     Region          30..88
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mkrrqlspde reaklvevvr qllaeeineg dalrilrrdv lglsqdayak lvgisrrtls
       61 dlernranmt letmnrvyrp lglkvgllpr qpgmlerals
//
LOCUS       WP_010628745             419 aa            linear   BCT 01-JAN-2025
DEFINITION  M20 family metallo-hydrolase [Halomonas sp. KM-1].
ACCESSION   WP_010628745
VERSION     WP_010628745.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..419
                     /product="M20 family metallo-hydrolase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45052
     Region          16..414
                     /region_name="M20_bAS"
                     /note="M20 Peptidase beta-alanine synthase, an
                     amidohydrolase; cd03884"
                     /db_xref="CDD:349880"
     Site            order(88,99..100,133..134,141,201,204,224,226,299,
                     365..366,391)
                     /site_type="active"
                     /db_xref="CDD:349880"
     Site            order(204..207,210..211,226,237..241,243,246,250..251,
                     253..255,257..259,261..262,264..265,272..279,283..284,
                     286..289,297,299,364)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349880"
ORIGIN      
        1 msqtpslger ldgerfwadl qaqaeigalh prglrrlald endnrarlwl idqgqalgcd
       61 ayhdamgnvf lrregqepel pallvgshmd sqpsagsydg tlgvvaglav lrtlqeqgie
      121 harpievvaw tneegarfap gasgsswfag qrdaatilea rddqgtrfad alaaclaele
      181 rhgasafrpa pfvphaflel hieqgpvles lgvpvcavsg iqgvnwyeie vhgqanhagt
      241 tpeaarrdal mgahaligal rdavagqdeq vrftigkfsv spgstntipq radftidlrh
      301 psqavlerld tafhrlaqrq wsgcdvslrv tsrvapvsfd palveladsa aksyspnapq
      361 lvsgafhdai hlarvcptvm lftpcragis hhpdehiers daetavrala dtverllnp
//
LOCUS       WP_010628821             716 aa            linear   BCT 01-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Halomonas sp. KM-1].
ACCESSION   WP_010628821
VERSION     WP_010628821.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..716
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=78539
     Region          1..647
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 maatglqftl dlagvdsael avidftleea hsqpfhlevr fasrdgslsa telldrpvsl
       61 tiwqdgevlr rvhavvsefg rgdrghrrtl yslvarpalw rldlrhnsri fqqvspltvl
      121 ntlcderglt dvafavtrdl aereflvqyr etdlafverl aaeeglfyfh efedtpngah
      181 rlvfadapqt lahlgertyh graggtppsr hvrkleqlar vapasvtlkd ysfknpayaq
      241 lhehaagdle ehaqrddyeh ydypgrykad asgdaytrir lehlrsgalt caaesdlpel
      301 apgvkftltd hdlselnrdw qvvkvkhtgs qpqaleedgv tqsdaaglgl rgragsegmt
      361 kfdneliltp adrawrptpn akprvdgpqi afvvgpegee iycdehgrvk vqfpwdryae
      421 pntagaegea agrapsawvr vsqgwagggy gsmaiprigh evvvsflegd pdqplitgrt
      481 yhavntppye lpehktrtvi rtqshkgegf nelrfedqag eeqiwlhaqk dlelltnndr
      541 teeigndsfl tvhhdrigei hadehhtvrg erheqtvanq hltvqgtlhi kagqawlsec
      601 grelhvkagh kvvleagsem tlnaggsflk ldgggvtlvg pkvkinaggs pgsgsgqave
      661 tpllpgravp evheaipptv lpklkdyqls eatllplcgk lsettcsrgd cpclag
//
LOCUS       WP_010628932             218 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010628932
VERSION     WP_010628932.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24881
     Region          8..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtkrqtqeer srqtqsrvkq atiecilekg iratstvdia rkagvsrgal lhqypskell
       61 mqaalediln revesvqdma trikageldf etmlqalheh fkgdmymvtl eflttartdp
      121 aikevlvpla ttfnasleqi weqlvmnaeh sshekrvaln atlcmmrgmg aqsiwredpa
      181 lyrdmllfwk rtllelgfst sentkrvphn dkndrdte
//
LOCUS       WP_010628933             165 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter small permease [Halomonas sp. KM-1].
ACCESSION   WP_010628933
VERSION     WP_010628933.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..165
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18660
     Region          31..164
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtrtieilnd wvaklaltla alflllmalh vtldvalryl fgksfpgtle vvsfyymvav
       61 vflplayvel krehisvdvl vgrlpaslql ilylfacslg llyfgmlcyq syldamratt
      121 rmetamanfr fylwpsrwal pvgfgammla ifanmlkalr lrqal
//
LOCUS       WP_010628947             413 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Halomonas sp. KM-1].
ACCESSION   WP_010628947
VERSION     WP_010628947.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 413)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..413
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43969
     Region          145..412
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mrrtpnrasl anrtrlvlrl alqdlwhdry vslciaaalv aviapllllf glkhgvvsql
       61 qrellddprn levrmltsgs ydeawleeir alpgvgfaig qtrslntqad llrdrqhfle
      121 gielipsaag dpllgesalv pvgsgvvlse paarrleava gerltlaasr rldgqaergr
      181 levsvldvlp aarfprpaaf velplliele rfrdghpspl lgvvsgtqrd dypvrfarar
      241 ifasdgdava gvvqaleaqr idtasrlaei esvrainrvl glifgviaaa aligclasma
      301 gafmanidrk rreyavlrll gfhkhavaaf vtaqvglltl iafaaglalf algsalfnra
      361 latshlaagv vshitvthal ialaltlvva lavaaigvar afgiqpaesl rea
//
LOCUS       WP_010629091             329 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Halomonadaceae].
ACCESSION   WP_010629091
VERSION     WP_010629091.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..329
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=36429
     Region          12..70
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..298
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(115..116,118..119,122,126,128..134,227..232,
                     238..239,241..242)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176111"
ORIGIN      
        1 mttprllnrl tfrqlqvfqa vhrqqsysra aeqlgltqpa vsaqirqleq algqplfkya
       61 gktlhvlpaa dalaastqai fgqvsrlqmt lsdldgtisg elnlaavsta qyvvphliar
      121 frahypnvqv rlrvcnrsqa lerlaarsdd lvimamvpee ddnlvfmpfl enelipivwp
      181 ghplleapsp tledlarhyl lmresgsgvr tafeqlaaeq dvalqhtmel gtneaikqgv
      241 mahlgvtvlp rlavrleiga gllaelplpg fplrrswctv yprdrfptpv telflrfvre
      301 rlgeieahfr apprpipdhg vvclpltsg
//
LOCUS       WP_010629175             270 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Halomonadaceae].
ACCESSION   WP_010629175
VERSION     WP_010629175.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..270
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29274
     Region          5..242
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 miesplvevk glhfsrgekt ifsgvelqip rgritaimgp sgtgkttllk liggqltpdv
       61 grvlidgqdv hglsrkalft lrrrmgmlfq sgalfsdlsv fenvafplrv htelpeamir
      121 dlvlmklqav glrgarelmp selsggmarr valaraiald pdlvlydepf vgqdpiskgv
      181 lvqliktlnd algltsvvvs hdipealsia dyvyviadgq vmaqgtpasl dvdedrrvsq
      241 fvhgepdgpv pfhypapeyf rdildlegrp
//
LOCUS       WP_010629246             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Halomonadaceae].
ACCESSION   WP_010629246
VERSION     WP_010629246.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..264
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28345
     Region          9..258
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msatspetli vdrrgavmei rfnrphrlna vveafysell aalaeaerdp evrcviltge
       61 grafcvgadm kehgsaqrtl fqrrrylqlg ndvceailrh rkpviaavng yalgagaema
      121 vacdfivmae eaqigfpets igtcvgggvs kllpqlvgln marqllytgr ridgreaari
      181 glatschaad ampaeaqkla eslagqapvs iamlkrlvnq gsdtglesql qqeldavftc
      241 stttdwqegv dafaekrapq fkgh
//
LOCUS       WP_010628917             712 aa            linear   BCT 01-JAN-2025
DEFINITION  bi-domain-containing oxidoreductase [Halomonas sp. KM-1].
ACCESSION   WP_010628917
VERSION     WP_010628917.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   5  (residues 1 to 712)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   6  (residues 1 to 712)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   7  (residues 1 to 712)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   8  (residues 1 to 712)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   9  (residues 1 to 712)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11579189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..712
                     /product="bi-domain-containing oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=76095
     Region          73..365
                     /region_name="2-desacetyl-2-
                     hydroxyethyl_bacteriochlorophyllide_"
                     /note="2-desacetyl-2-hydroxyethyl bacteriochlorophyllide
                     and other MDR family members; cd08255"
                     /db_xref="CDD:176217"
     Site            order(81,83..84,87,150,154,174..179,197..198,202,225,
                     241..242,244,266..267,289..291)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
     Region          394..710
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkqvlqdlak gattlteaps prastgslli ststtlvsag termlvdfgr asylqkarqq
       61 pekvkmvlek vqtdglmttm eavrsklaqp lplgycnvgv vsevgqgvlg fkpgdrvasn
      121 gphaeivkvp qnlcaripeg vsdeqaaftv vgaiglqgir laqptlgeaf vvtgvgligl
      181 ltvqllrahg crvlaidfda aklalaekfg aeicnpaqge dpvaaglafs rgngvdgvii
      241 tastksndpv tqaarmsrqr griilvgvtg lelnradfye kelsfqvscs ygpgrydpny
      301 eekgndyplg fvrwteqrnf eavldmlasg qldveplith rfafanvpea yrvlteeraa
      361 lgilleydap leqrtvssvt lnrevqfdat rpvlgmigag nyasrvlipa fkaagaqlht
      421 lvtaggingv ihgekagfae astdlvglla ndtvntvaiv trhdthanfv sqalaagkhv
      481 fvekplaicr eglaeveaay htahasgqqp hlmlgfnrrf apqvqkmkkl lgtvnepksf
      541 imtmnagaip pehwtqdpav gggriigeac hfidlmrfla gspivsvqar rmgdnpgmai
      601 tedkaaitlg fadgsfgtih ylangaasfp kervevftag rvlqldnfrk lkgygwpgfr
      661 kltlwkqdkg qkacaaaflt aveqgratpi paeeifevar vsieaaealr gq
//
LOCUS       WP_010628544             103 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SCP2 sterol-binding domain-containing protein
            [Halomonadaceae].
ACCESSION   WP_010628544
VERSION     WP_010628544.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Burgardt,N.I., Gianotti,A.R., Ferreyra,R.G. and Ermacora,M.R.
  TITLE     A structural appraisal of sterol carrier protein 2
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (5), 565-577 (2017)
   PUBMED   28284963
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Dyer,D.H., Wessely,V., Forest,K.T. and Lan,Q.
  TITLE     Three-dimensional structure/function analysis of SCP-2-like2
            reveals differences among SCP-2 family members
  JOURNAL   J Lipid Res 49 (3), 644-653 (2008)
   PUBMED   18084051
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Bun-ya,M., Muro,Y., Niki,T., Kondo,J. and Kamiryo,T.
  TITLE     New aspects of sterol carrier protein 2 (nonspecific lipid-transfer
            protein) in fusion proteins and in peroxisomes
  JOURNAL   Cell Biochem Biophys 32 Spring, 107-116 (2000)
   PUBMED   11330036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007129
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..103
                     /product="SCP2 sterol-binding domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11073
     Region          6..101
                     /region_name="SCP2"
                     /note="Putative sterol carrier protein, contains SCP2
                     domain [Lipid transport and metabolism]; COG3255"
                     /db_xref="CDD:442486"
ORIGIN      
        1 msistldklq erfdpqaakg mddvfqfhfs dngshylvvk dgtlaieege hddpsvslsm
       61 stdtlkgimt gdvngmtafm tgklkatgnv mlatkltslf pnr
//
LOCUS       WP_010629247             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010629247
VERSION     WP_010629247.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..308
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33100
     Region          23..303
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mlehetqsad ttpeeacppt gldavnqqla aaypelspql klaagyvleh pmeiafqsir
       61 ksaraarvts stlvrlakrl gfdsyeqfre vfqsavqagp velsgrasdl rnlasqtddq
      121 vfldvgdaaf dnigrlftad tqarvrdaam mllaaekiav vgfrdtfaca yhfayvgria
      181 mpnvqlirgq egglltelap fgendvvvaf gfepycaetv raleiaraag vksivitdtl
      241 rsplvpgaai tftvanatph ffpsilsait lievllaecv aygpdslvdn vasfesrmre
      301 mgayvsne
//
LOCUS       WP_010629334             380 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Halomonas sp. KM-1].
ACCESSION   WP_010629334
VERSION     WP_010629334.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..380
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41342
     Region          1..355
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matlqlhdiv krfddtevik gvdlevndre fvvfvgpsgc gkstllrmia glesatsgdi
       61 lidgvrmnev gpaerglamv fqsyalyphm tvednmgfsl klagvskeer rrkvreaasi
      121 lqlepllerk pkalsggqrq rvaigraivr npsiflfdep lsnldaalrv qmrielarlh
      181 eeldatmiyv thdqieamtm adkivvlqsg mveqvgspme lyhhprnrfv agfigspkmn
      241 flevqrvsaa atgvevrlpg gdtctvpvdg sgldddaltl gvrpehlqld pegplsgrie
      301 vierlggvts lyvrmqdtlv tvsadgnvas rvgdtlrfgf erdcahlfdg eglalpslar
      361 hplaglnrqd nrapaaagrl
//
LOCUS       WP_010629404             299 aa            linear   BCT 01-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Halomonas sp. KM-1].
ACCESSION   WP_010629404
VERSION     WP_010629404.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..299
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32175
     Region          8..291
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mqdgvievav kldmslgesp vwsvarqtly wtdinnghvy awrpqeggap traelgekvg
       61 cvaldetglv aaaasgilrl pengeperla nnpewvkerr qagqgnrfnd grcdpagrlw
      121 vgtidadess psaalycldk gelsrrltgl gisnglafsp drrwlyhtds lsrrilrypf
      181 dvesgtlgeg etwvdlerlg lpgvpdgaav dsegcywsal ydggrivrfs pegelvaehp
      241 vpcphptmva fggadlctly ittatqhlda egkarwpqag sllqmrtgva giaepgfkg
//
LOCUS       WP_010629363             211 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Halomonas sp. KM-1].
ACCESSION   WP_010629363
VERSION     WP_010629363.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10606006
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..211
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23962
     Region          61..192
                     /region_name="Methyltransf_23"
                     /note="Methyltransferase domain; pfam13489"
                     /db_xref="CDD:404385"
ORIGIN      
        1 mptcplcasp hsrhfhhdar rdyyrcencw lafvppeqrl speqeravyd qhenrpddpg
       61 yrrflsrlfe plqhrlapga sgldfgagpg ptlslmleea ghpmaiydpf yapdtavlqr
      121 rydfitatev vehlfapgle larlaallpa ggwlglmtkr vtdevafarw hyildpthvc
      181 ffsetsfewl aehldmsvef paadvallqk r
//
LOCUS       WP_010629426             308 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Halomonas sp. KM-1].
ACCESSION   WP_010629426
VERSION     WP_010629426.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..308
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34282
     Region          1..241
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msvttlglvg vgkivrdqhl palaesrdfr llatadpnar lasmpgyagl tamleahpel
       61 eavaictpth lrysqarial ergrnvllek ppgatlseve dlvelagrqg ctlfaawhsr
      121 fapavaeard wlrerriqrv eidwredvrv whpgqawiwe pagmgvfdpg inalsiatei
      181 lprafflrda rlwvpsncqa piaaaltfsd tegtpivadf dfrqpsppiw sihveteagr
      241 lsllrggcrl eldgrcllda eereypnlya rfaelirqrr sdvdlaplrh vadaclaawr
      301 eptepfie
//
LOCUS       WP_010629438             282 aa            linear   BCT 01-JAN-2025
DEFINITION  pirin family protein [Halomonas sp. KM-1].
ACCESSION   WP_010629438
VERSION     WP_010629438.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..282
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30654
     Region          17..275
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 matspsirri erlfhshpsq dgdgvhiqri hcfdgeldpf lmldelgsdr pddyiggfpp
       61 hphrgiqtlt yivhggithe dhlghsstiq agdaqwmhtg rgivhsempl tdsqglhgfq
      121 mwlnlparek msaaryrdvr sdemprlkke kaelialggn wstqqgesvs gpldalagsg
      181 gvaharfead geltltapse tlavyvfegt lqiegenvaa gqlarlspgd svalssqpga
      241 qclllagtph repiahygpf vmnsmheieq alrdyrngtf td
//
LOCUS       WP_010629483             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RDD family protein [Halomonadaceae].
ACCESSION   WP_010629483
VERSION     WP_010629483.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..158
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17174
     Region          6..143
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mkdqgleyag fwvrtgatii daillmmvtf pvlisiygwg yfdpnlygfv agpadflisw
       61 vlpaigivlf wvykqatpgk mavsvkvvda rtgnspsvgq amgrylayil sslplglgfl
      121 wvafdgkkqg whdklagtlv vreaknavpv efvqpkse
//
LOCUS       WP_010629459             354 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [unclassified Halomonas].
ACCESSION   WP_010629459
VERSION     WP_010629459.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..354
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37857
     Region          16..349
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mqeiernesa lsrftrrtli viglaslvav llffasqlid vmllvfasil vavsidgavr
       61 lcqrylplsr pwalllallm iclsmvglga ligprigeql pqlvaelpqa fqqflnnfre
      121 lpgietamae veepaqlige pvidyftnff attfgaiasf flilligfyl vlspakyign
      181 vlllcppakr drlaqvlcmq gralrlwlls rlvsmvfvgv svalglvllg vpmagalglv
      241 aglftfipyl gpiigaipti liaflespql alyalilyfv vetlesnlvm plaakglvrl
      301 ppaytvivql agaavagvag vilstplavv avvtlqalyi ndvlgddiev lggr
//
LOCUS       WP_010629464             436 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Halomonas sp. KM-1].
ACCESSION   WP_010629464
VERSION     WP_010629464.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..436
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47013
     Region          11..404
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mpqrhpetst tdrlvivgng maghrlveal larperpait vigaetapay nrillsplla
       61 gemerdaltl rsaewyaeqg ielvlgerve nidrdartlt tdagrrldyd rlvlatgstp
      121 arppvpglel ggvhvfrdlh dadalaraaa tgrnavvigg gllgleaaeg lrkrgmqvsl
      181 lqredrlmnr qldltaarll eselrgrgld ihtdaqlerl eadaegqvca alladgtrla
      241 adcvvvaigi vpqvelgrva elevnrgivv dewlttsdpt ihalgecceh lgnlyglvep
      301 iwrqvevltd klcrasaesa esaqgyvekp tatklkvsgi slyafgptep epehevlsyr
      361 dpqqgdyrrl llrdgrlega vlygdtasgp wyfeqalagc dlsdcraall lgaadaqarl
      421 ddalnespqr pakeaa
//
LOCUS       WP_010629516             163 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter small permease [Halomonas sp. KM-1].
ACCESSION   WP_010629516
VERSION     WP_010629516.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..163
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=17548
     Region          4..145
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mwywydrfea wlavvllgat sltllassta raigqpfagg aelaqllfiw tavlgaditl
       61 rhggqvrida lsirlplplq rlvtglclvl mlsflallvr ygfplalsnw qrpmgvagls
      121 ygyitlalpv gaslmivsll rrvaakgivm slapdteive khs
//
LOCUS       WP_010629520             295 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Halomonadaceae].
ACCESSION   WP_010629520
VERSION     WP_010629520.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..295
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32826
     Region          1..287
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mfrqlrarfg gplamaivtl lgiwlivmvt lpqlqmieys lrpnllpaqi ggpddrltla
       61 nyatlfnndi hrtiffktiw ssvlvtlltl avsyplawyl akvatprqaa lcillliipf
      121 wineilrtys wfiilafrgp lnevlmmlgl idrpirflsg nggvmvgmvy ayilfmvfpv
      181 ynaieslddn qvraardlga gtvrthrriv iphakpgiat gcimtfmlaa gsyavpallg
      241 spgsrwftqi iynwffeggn wnqgaayafl llvlcigfms limkifkvgl gdigk
//
LOCUS       WP_010629534             248 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Halomonas sp. KM-1].
ACCESSION   WP_010629534
VERSION     WP_010629534.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..248
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26386
     Region          13..231
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mnlqvassps rawltgmsea vpllggyvpv aisfgliatq agfsaweava istliyagas
       61 qflfvgmvaa gaplwlvvam tllinlrhvv yapnlapwlt psrlwpwlmh gltdqifala
      121 harlpqlpaa qrlgwytgaa llawlswigg talgalvgge lvarwalmge ilpfalpalf
      181 lvlvaprfts rrwslalglt ilsallltll gltnmaipla avcgalcfql vkfghtaerk
      241 daqgerhe
//
LOCUS       WP_010629541             490 aa            linear   BCT 01-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Halomonas sp.
            KM-1].
ACCESSION   WP_010629541
VERSION     WP_010629541.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..490
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=51732
     Region          1..489
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mlndlliafq avatfenfli maagiwggvi igaipgmtgt mavtlalpft fymqpipsil
       61 llvalykgst yggsvsaili ktpgtasaac ttldgyplar qgkagkalnm alyssctgdf
      121 isnlslifia aplallalri gppeyfmlmv falttvagvs grslllglvs aclglllatv
      181 gedmygsfrf dltvdmqsgl avapvliglf aipellkivv frnteaqkpm qlgdnkvtra
      241 elrrslksml kgsmigvvmg aipgigpsaa afssygeaqr ssknrenfgk gevegiaase
      301 sanngccgst mipllalgvp gdvitgvmlg afmihgmtpg pmlfennlne vymlfigmlf
      361 ssvllfgagk atmrffshis rippglmapi vlilclfgif sisnsmydvi vllamgvfgf
      421 fmflfaipaa pfliafilgp mleenlrral aisrgdpsil vsspitwlfa slavfvvmit
      481 irqqlkkaka
//
LOCUS       WP_010629549             264 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Halomonas sp. KM-1].
ACCESSION   WP_010629549
VERSION     WP_010629549.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28830
     Region          7..253
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqnngklalc fhtlfviflm aplvvvmlva ftpngyisyp tdgfslrwfr ailenrsfvq
       61 afwnslylgi gaasvsavla vpaalaiary qfrgrealvs lflsplmiph vvlgvaflsf
      121 fsrigvygsf yalvaahvii impytmrlvm asvfgmdrrv eqaalslgas qwtvfrrvtm
      181 piilpgvagg wilafttsfd elsmtifvas pstttlpvqm ynhiahtidp litsvstvli
      241 vltallvlil driygldkvl igkg
//
LOCUS       WP_010629600             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Halomonadaceae].
ACCESSION   WP_010629600
VERSION     WP_010629600.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34162
     Region          7..>134
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,213..218,
                     224..225,227..228)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176159"
ORIGIN      
        1 mahwdgieaf vevvklgtfa aaarqlhvsn shisrqvaql eqelglplly rttrqihltd
       61 ageryyarcr elldgfreae aalqslqekp hgilqlscat afgerfiapl vndflklhpq
      121 lemrlhltnr qvdvidegyd vvirmgtlqd stlvarrlce rreyvvaspd yfqrvsqphs
      181 iaelihhrcl igtrdqwrfd vdglhrevrv sgpwqansgp alldaalkgl glaqlpdyyv
      241 mpylasgelv evlsrfqcrd agvwavmprh rqhaakvrqf idflvehlpq rleqacatea
      301 q
//
LOCUS       WP_010629519             268 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Halomonas sp. KM-1].
ACCESSION   WP_010629519
VERSION     WP_010629519.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..268
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29526
     Region          3..264
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mssqrflafg lrfyvviffi ylflpliima aatfndsrfp tvtpwdgttl rwfgelaadr
       61 gmwqalansl ivaagvlvva vpigiatalf lntvtsrakp flyalilspl ltpgviigis
      121 tlifwrqfgv sggifltvlg qatfiaayvm lmvtarlqrf drtmeraald lgasqwqmfr
      181 rillpylkpa lysaaviafl qsfenynttl fvvgydttlt vyiaskvrtg ltpavnalgl
      241 ililvtvlfa aiyelkrrre aaravqgv
//
LOCUS       WP_010629602             295 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Halomonadaceae].
ACCESSION   WP_010629602
VERSION     WP_010629602.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..295
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31421
     Region          9..295
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mtmifgvpla vfmgqlllgl ingafyalls lglavifgll kivnfahgam ymlgafatll
       61 gmrylginyw aalllaplfv gllgmlierv llrrighldh lygllltfgl alifegtlvn
      121 ffgvsgaryp tpealqggyq tgfmflpkyr awvllaalvv cfatwyiier trlgaylrag
      181 tenpalmqaf gvnvpllvtl tygfgvalaa fagvlaaply pvsptmgsnl livvfavvvi
      241 ggmgsilgai vtglamglie gltkvyypea antviflvmi lvlllrpagl fgkea
//
LOCUS       WP_010629623             814 aa            linear   BCT 01-JAN-2025
DEFINITION  LPS-assembly protein LptD [Halomonas sp. KM-1].
ACCESSION   WP_010629623
VERSION     WP_010629623.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..814
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92857
     Region          63..789
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mgkrhagtal aslitsgltl gapqalalep laawqldwqp wgegrpaeal crgvyimpay
       61 rlpagdepgq vrsesdtayy gddgetilgg evilrradtq lesprvsvpp ererafaegp
      121 lalrdlnllv rgeagevslv tdaasidaah fvvhdqhlrg damqmerled grfrltsasf
      181 ttcdpgdnlw qlvtgdlvld resgfgtarh arlemgnvpv fywpwvrfpi ddrrhtgflw
      241 peiglsggal dyaqpfywni apnhdatltp rwisdrglll ggeyrylfpt dagqiegayl
      301 ssdgggsdep gaasrryege drwyvdyrht grfdtrtsyn lrygaasdgr yfddygsifg
      361 ddpsnmprla qidyrgdvwr ldaraqgyqr lddplrdrdk pfyrlpslta darwmqpggl
      421 yqewrsnvty fwrdvneval srereaavgt rlhlapatgw rfdqswghle prvewlytay
      481 dldygerqte rdttlqravp vtsidgglvf erelelggrp yrqtleprvn yayvpardqr
      541 efpdfdtser alswnqlwsp yrfsgadrvg dlnrlsvgvd srlleddrgr erlaigigqa
      601 fyfddrhidm dgnpdtlpvp peqggdfesw ynatrdrssl vtrldwqind awrsrlqwiy
      661 ddyqqrtert sldlsyrsqa ghvlnlgyrw elqgfdpsve pdddefrdyn reeydlsfaw
      721 klsprvdlig ravydytner lldqlagvqw ndccyglqvv wrewvddqgt asiendtter
      781 glflrfvfkg lggvggdagd yferaipgyr ataf
//
LOCUS       WP_010629697             172 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ferritin-like domain-containing protein
            [Halomonadaceae].
ACCESSION   WP_010629697
VERSION     WP_010629697.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10532247
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..172
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19144
     Region          10..160
                     /region_name="DUF892"
                     /note="Domain of unknown function (DUF892); pfam05974"
                     /db_xref="CDD:428701"
     Site            order(22,53,56,108,141)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mgtepqspkh ledwlrdaha mekqaekmle aqasrlehyp qlksrieqhl tetrgqteki
       61 eqciallgtd lsavkdlggk laafgqgmsg mmagdevvkg amasyafehf eissykvliq
      121 aankvgkpei ariceeilke eeamaewlgn hldeitqqfl ersedsdlra kt
//
LOCUS       WP_010629726             175 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Halomonas sp. KM-1].
ACCESSION   WP_010629726
VERSION     WP_010629726.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..175
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=19097
     Region          8..162
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 myaradqrir viltlngrer sgyaeprtql cdflrhelga tgthvgcehg vcgactvrvd
       61 grasrsclml avqaegrrld tveslageeg lsdlqqafrr hhalqcgfct agilmsceef
      121 ldrvadpsea qvrdmlsghl crctgytgmv qavldvartr reaavpdsqq enndv
//
LOCUS       WP_010629734             369 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Halomonadaceae].
ACCESSION   WP_010629734
VERSION     WP_010629734.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..369
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40820
     Region          36..349
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mtlrevfkgw iehyfsdeea villvllvlg favvilfgrm lapfltalvi afllqggvna
       61 ltrqgvphll avtliflafi gvllalafil mpliwnqlvg lvqetpriva sgqrwlddvq
      121 eryptlvtpd qvqewiavag reltqfgqra ltlslaslgn vlaliiylvl vpilvffllk
      181 dreqlvdftl sllpqqrtlm triwqemdtq ianyvrgkfv eiiivgtvsf ftfaffglpy
      241 sallavlvgi svlvpyigaa vatlpvaava gfhfgmseqf lyvliaygvi qaldgnvlvp
      301 ilfseavnlh pvsiivavlf fggiwgfwgi ffaiplatll kalvyawprg irqyhdsqqs
      361 veleqsaee
//
LOCUS       WP_010629830             139 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [unclassified
            Halomonas].
ACCESSION   WP_010629830
VERSION     WP_010629830.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..139
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=15271
     Region          23..119
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mtkakseaaa grripdysdp sywrgtikms lskffvlsvl hrkpmhgyev vqavekstng
       61 ccspsegtvy pvlnefeagg ylcstnevvq grsrkvyalt ekgrdafqva vdawleatdc
      121 ivesrrmaag avkreereg
//
LOCUS       WP_010629800             200 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010629800
VERSION     WP_010629800.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21800
     Region          6..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpqrgrprgf dreealrram evfwtqgydn asltdltram sinapslyat fgskealfhe
       61 avalyvqteg sgiweqveta ptardaiahv lhataeaftr gdtprgcmiv laapqmqgan
      121 aqvcdalkah rkengcller rlkraveege lpastdcral asyfvtvqhg msiqardgas
      181 retllriadc amaswealts
//
LOCUS       WP_010629834             378 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Halomonas sp. KM-1].
ACCESSION   WP_010629834
VERSION     WP_010629834.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..378
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40094
     Region          31..377
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msdtlglsrr aitatetilq kygvdgekag agfiaevlet laanelltfg fsdplqtgpq
       61 pgdmekactv irllaersgt latiymvagl lgplclsyag tvaqkkallp rvaagelqla
      121 faltepgags daagittqat rwddhyvvrg ektyitgaat adliltvart teggaksygi
      181 llvpggaegl sveplsklsg naypscrvmf eevlvsesgv lggeagvnsa wpqlrktgtl
      241 erlivaamac gfadaatnra lqfvqerhqf gqplrdfqai qhtvvemstl atgmrlfled
      301 airqhaeghd atqaismaky fcsdqlqkvv amaarvmggr ayfdfepvsr lyreapfcly
      361 aggtievqkm liarslgi
//
LOCUS       WP_010629837             170 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010629837
VERSION     WP_010629837.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..170
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18925
     Region          12..146
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkrlryengv pdatdrqlle alvidartsv aelarlvgls ppsvserikr leeagviegy
       61 tarispralg lslaawlrir plpgqlqrvv dllqelpeim ecdritgddc fiarahlesv
      121 ehlerlidei ipyattntai iqsspvprrl pplngaeare afdkrrarcq
//
LOCUS       WP_010629889             400 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Halomonas sp. KM-1].
ACCESSION   WP_010629889
VERSION     WP_010629889.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..400
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41146
     Region          8..390
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mngkrvpllf lnlghayahy fmlihptvav alerrgqgdy aalllpatag fvafaaftlp
       61 agwlgdrwsr rgmialmflg lgaasmltgf asgpyqlaag lflmgsfaai yhpvgiamva
      121 essdgvgqal gvngvwgnmg vaaaplltga itgmlgwqaa ffipgalcla sgiaylalvp
      181 aeskplqplr paddataavq astaipgril aylivtalmg glvfasttva lpkimedafs
      241 gggnallgaa glaslifaca smaqlvtgra vdrvaprqlm lllallqvpl lllmvqggqw
      301 qivalslglm ltvfgvipvq daivarhtas awrarvyavk yvlslgvgal avpivawgye
      361 paagfvrlym llaacavgva maalllparr yaqaalgdsq
//
LOCUS       WP_010629911             207 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Halomonas sp. KM-1].
ACCESSION   WP_010629911
VERSION     WP_010629911.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..207
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22486
     Region          5..194
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 msdslilytn pvsrgriarw mleeigapyr teviefgsam kspaflainp mgkvpairhg
       61 etvvtecaai cayladafpe aglapplter gpyyrwlffa agpleaamtd rdlgmepnvd
      121 qqgrvgygsi eavldtleia vseheyiagp qftaadvylg ahigwglkyg glgpcpafad
      181 ywarvssrpa yrraselddq akdqahr
//
LOCUS       WP_010629947             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator
            [Halomonadaceae].
ACCESSION   WP_010629947
VERSION     WP_010629947.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..282
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31473
     Region          3..269
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mgpgpvissc glevhpqtty rdpnlfthia vcggnnyldp hedkalshyl kdayrqgvkl
       61 vgvctgtfai aragllkgqr vcvhwnvind frqqfphida tpdrlflesv rvitcagssg
      121 atdmalhlir recgpdkaqq airhmmlngm rtsnspqthf feaiqdirde rvrvavltme
      181 qslntrldsq alakrinlsp rqldrlfqqe mgttpmryfk tmrlryaewl lqhtdssiae
      241 iaaecgfsda shlardfqah ytcspkqsrl kglssqasaq as
//
LOCUS       WP_010629958             220 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010629958
VERSION     WP_010629958.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..220
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24704
     Region          1..206
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 meeavqssha glvekvanyl rehivmdhfq pgqrlpertl avelqvsrtp lrealkilat
       61 eglvvisphr gavvaevspa dikekayvls vleqaaaelt cinasdddia elqalhyemk
      121 acflrrdrqs yfrlnqeihn rivalsgnsa lidmhanlsr qlyrvrylsn qknekwatam
      181 aeheaimsal esrdpeqagr elrnhlgktw vkyangepvv
//
LOCUS       WP_010629962             594 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Halomonas sp. KM-1].
ACCESSION   WP_010629962
VERSION     WP_010629962.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..594
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=66727
     Region          271..549
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mkgidawrlp alvalltlaf fvaapsaaql pegvgengne seddeseere wfpldslnag
       61 lgeppdever ltpqgalrsf veltendeya aaahllnlse ldeaeqqqqg pelarqlasv
      121 lrrgewfnvs nlpsrqdaai edpsgqhplv geprrslela tmtvdgedye vrldryrvdd
      181 eqpvwlisae svsviprlye efgpslieay iperfktsfg mlqvwewiai plfllltglv
      241 gwgvyalvgl lahwfphgvp sifagrigvp mallvmafva qmlldyvvsf tavattfirt
      301 lliiliawgv gtialrlvdt vllkvtrrfv geiddtkpkd erqllttlya lrrviilvav
      361 iavsvyvlsq ielfetlgls llasasvlav lvgiagqavl gnilssfqvs lakpirigdl
      421 vmfegqwcyv egifytfirl rvwderrliv pvtyfvsqpf enlsiknakm yrklelilhl
      481 sadvelirhk ffefaeeeen vvehhklccy vtgqteksqt itcylmatdp fagwvaemqi
      541 rerlmnfirt yhpewwprdi vvlsqhdiat eekhekprvr vsaegesgge kaae
//
LOCUS       WP_010629971             299 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Halomonas].
ACCESSION   WP_010629971
VERSION     WP_010629971.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..299
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31647
     Region          3..294
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtfdavivgg syagmaaglq lararrqvlv vdageprnrf ashshgflsq dgtppaeiaa
       61 dargqlmeyl tvewrsgrvt siggeaerft vgladgdtfq arriilaagv sdelpaipgl
      121 aeqwgkrvfh cpychgyelg qtaigvlass elamhhalml pdwgtttlfl naafeptaeq
      181 laqldargtr ierglvthlq agrdervevv lndarripla glfvaprlhl splvedvgce
      241 leetpmgsvi ktdamqatsi pgifacgdia raagsvtfav adgamaglat hrslmfgls
//
LOCUS       WP_010629979             212 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Halomonadaceae].
ACCESSION   WP_010629979
VERSION     WP_010629979.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22209
     Region          1..210
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mewwtwityv gvitaliifp gpvallctth glrfgrhraf atvlgggvas lvlmtlsalg
       61 lgavlatset affvlkllgg ayliylglqa wlsapsspva tasepalasv rstsglfrqg
      121 flvgignpkd llffaalfpn fitvgepqml qfailaltwl vidttlmtly atagaglgrw
      181 fdspgrlraf hrttgglflg aggtliatsa sk
//
LOCUS       WP_010629974              68 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [unclassified Halomonas].
ACCESSION   WP_010629974
VERSION     WP_010629974.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..68
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7242
     Region          1..65
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mttgtvkwfn dskgfgfisp sdggddvfah fseiqaegfk slqegqtvef evtqgkkglq
       61 asnikqla
//
LOCUS       WP_010630008             336 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Halomonas sp. KM-1].
ACCESSION   WP_010630008
VERSION     WP_010630008.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..336
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36031
     Region          56..311
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(71,155,157,159..160,188,244,265,268,280,282,311)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 msgitlnrrk iiltaasaaa glilppggma laqaasaats taqggtasan vgyyhlrvgd
       61 isatvlsdgl iggppriyas dapeaeleev lrqaflptdh mtlnlntlli ethgrrille
      121 agagqtmgpl ggrifdnlaa iglrpddidi vvishthpdh vgnlraadgs kafpratvfa
      181 pradwdffmr nepdlsympv pvdfrrhfaa airqslepvi ndielyeagt eivpglttlp
      241 alghtpgman flvhsgndql lltadlayhp ivnidhswlp gpdrdketal asrrrifdma
      301 aadrlpvlgf hfpfpglgrm lktdtgyawv panwqf
//
LOCUS       WP_010630014             138 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Halomonas sp. KM-1].
ACCESSION   WP_010630014
VERSION     WP_010630014.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..138
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15414
     Region          7..132
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mhfdtlrldh igirvtdlai aeafyaklgf lrdpeefspe akasglvhpt gmrihliyng
       61 epaevgnvll dapikrpgyt haafivesmd elvawlaree ieitegpvtm ghgrrsvcfi
      121 rdpdlnvlef neilpqrh
//
LOCUS       WP_010630021             187 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010630021
VERSION     WP_010630021.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..187
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20239
     Region          3..135
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgtetkilda aaqlleahgp aglttrtvce vagvkaptly hhfgdkdgle ralvrramae
       61 fmqrkrapaa tadlleqlrf gwdvavefal drpalyvvfa qqvrshpela aegyalmrek
      121 vqrlvdtgrf rlpvdaaara vwaasqgals lvgqnmarkd veatsrllfd avvnelsqps
      181 pstqsps
//
LOCUS       WP_010630202             443 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpP1/FadL family transporter [unclassified
            Halomonas].
ACCESSION   WP_010630202
VERSION     WP_010630202.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..443
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48015
     Region          26..443
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mqnkfnritw avaiaaaafa sqanaggyqi neqsvsgqgy ghagrssnvn dativfgnpa
       61 gmsfldraql taggtylnvn srirnarsds sidgaaaglp vapgdvqvpl gpidgtndgd
      121 mvpgtlipfa fyahpvnerl afgfgvyapf gskteyedtf egrnfgnyte vrvisaqptv
      181 syrfndqwsv gvgvtynrvd gelatripgt llgrpggpdg evrvegddea ygynigvmyq
      241 pvpettfglt yrskvsytle gssrasggae alipnqnasl elttpetvnf svtqqmsdrl
      301 klmlgaswar wsrfeeirid gslnpdpitq etqnysnawa fgvggeyqln rqlalragvt
      361 idntptsdef rsvripsddr rifsigagws pteditldfa ysyltergtt idrqrtlgpm
      421 eldyaadykn eahgfgaqlt yrf
//
LOCUS       WP_010630273             245 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Sporolactobacillus vineae].
ACCESSION   WP_010630273
VERSION     WP_010630273.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..245
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27394
     Region          59..236
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mgkqivtqqd dqvkerktnl stdfeklavy aahftqpenq llkgmeekar riyipimhps
       61 smallqqlir wtraakilel gtaigysair mkiaagkdae ifsverdpem ireagenirt
      121 agfsgsihiv tgdatdhlad vrehapfdli lidaakaqye hlfleyaqml rpggiivtdn
      181 vffhglvtni pgvrkkqlrr lvekvddfnh flseqanfqt vfltvgdgla istkkeases
      241 aegwe
//
LOCUS       WP_010630279             353 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Sporolactobacillus vineae].
ACCESSION   WP_010630279
VERSION     WP_010630279.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..353
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39246
     Region          46..353
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mrkwpalqwm killiilllf lngylfyrli pllsvlllfi lrvllpfaaa gvvayllhpl
       61 vnrliragfn rsvailaiyv vffglvgfav vkggpvfihe isglnrefsk yeqiyqtqvd
      121 hvygvtpeav hdqvnkalar irenlghisd rimdwcsgvi qslftliiip flafyflkda
      181 driqrgalhl vpkrwraqta sllaemdhsi geyirgqltv cavlavmasi glwllkvpyp
      241 ivfglfigat dlipyfgpli gaapallmaa tqsayqvvgv iimiliiqfl egnviepliv
      301 gksadihply imlslgigge iagivgmlla ipafivirtc frhlqqkrhl idk
//
LOCUS       WP_010630293             403 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Sporolactobacillus
            vineae].
ACCESSION   WP_010630293
VERSION     WP_010630293.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..403
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=44767
     Region          2..402
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mplfdyigtd tlgkakkgrl taenrqeali qvarkglair svhehtetlw nkplslgssi
       61 kladkvvflr qfatiikagv tvsealdila dqeeknrsfr avieqmaadl kegrtlsqaf
      121 enrgkvfspm iihmirageg sgrleesldh laiyyerlhk srqklttamv ypvfvlclsl
      181 avviflltsi ipmfrsmfts ihaglplitr atlaasdwvr acwpvlilli laavvlvivs
      241 lknkssklri dyaiirlpli gplvyksels rllwmfalli sssvpvidal qsvekitsnl
      301 airraihnva ealdfgtpls eafsrekifp sivyhmtaig ektgmldqml nhvagyfend
      361 vaqanerlka liepatilfl avvvglivls ivipmfqlyq nfn
//
LOCUS       WP_010630496             300 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Sporolactobacillus vineae].
ACCESSION   WP_010630496
VERSION     WP_010630496.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..300
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=32573
     Region          18..299
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mnhtvehaqv pvkerskhkg ltirqlivrl llisigvffe aislesflvp nkiidggvtg
       61 isimmthlsg lpigifliif nfpffivgyk qmgktftvts acavtalall ttfsgipqft
      121 ndlllaavfg giimgigvgl virnggssdg teilavlfne ktpfsvgevv mfinifilgs
      181 agfvfgwnya mysliayfia fkmiditseg lesskavwii sdlhqeigda lndrlgrgvt
      241 ylngegaytg ndknviftvi srleeakvkn ivdsidknaf laisdihdvk ggrfkkrsih
//
LOCUS       WP_010630353             340 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Sporolactobacillus vineae].
ACCESSION   WP_010630353
VERSION     WP_010630353.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11420499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..340
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=38974
     Region          16..>116
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          18..>254
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          24..49
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(25..26,29..30,32,56,59..60,63..64,66..67,91,94..95,
                     98..99,102)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          54..84
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          90..116
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkkrekkpvp gnkiilfpdl earlldkatg lvtekkykea rslfgkmlel drenmkglyg
       61 wavcsvelgd yslaeeavrq llsintpyyn dvfrlyltil iekkdyrqal seirrasgrk
      121 glppesrafl rqmkkfcelr lrepsretgn raepeqtasr adwkrleaad pkqqlllihd
      181 vgdrltkrdl pqveafllde rqnpeiktml lcavrekqla gqidvrkfgk vyhvvfdsef
      241 lhkgftdrve rqirqvlnsq nptladlavd merffmmtvy pkpmvpssvs vwaaafsaqa
      301 ahagqmseqa edmpelfdvr tdafeaacre iaavtddeir
//
LOCUS       WP_010630499             234 aa            linear   BCT 01-JAN-2025
DEFINITION  TerC family protein [Sporolactobacillus vineae].
ACCESSION   WP_010630499
VERSION     WP_010630499.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..234
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24730
     Region          11..184
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 melfsaeflm slllivgidl ilagdnaivi alaaarlqdh qrkrailygt lgavairava
       61 tlavvwllkm pglhlvggll lvwiaygllk nqqkdrkvea ktslsaaigt iitadalmgl
      121 dnvlaiggaa sgnyllvilg llisvpmimg gstlflklvd rfswityags gvlaftagkm
      181 ifaehfitqg vegaswikwa vialiiagvi yfgwrkqqag kltaaapvne trss
//
LOCUS       WP_010630502             250 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sporolactobacillus vineae].
ACCESSION   WP_010630502
VERSION     WP_010630502.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..250
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28051
     Region          5..245
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtailsvahl sggytrrspv lhdlsfaigp gelvglvgln gagksttikh ilglldpyeg
       61 eiriggktir edktgyrrql ayvpelpely eqltleehlq ltamayhldr rtyqerssrl
      121 lalfhmekkl hwfpihfskg mrqkvmimca flvhpdlyiv depfvgldpi giqslldlmv
      181 emkksgssil msthilstae qycdrfiilh egriavqgtl dqirkrfgda gaslqdiyls
      241 vargettwtn
//
LOCUS       WP_010630516             278 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Sporolactobacillus vineae].
ACCESSION   WP_010630516
VERSION     WP_010630516.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..278
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30805
     Region          5..269
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,200,222..224,226..227)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mvyrllaldi dgtlltsnnr ldrrtrdaia yarkkgiivt lvserhfhaa akvaralkld
       61 qplithngaf vsssidhpvy tskidhsvlv qltefletyp cqiqisherl sisnrprqkn
      121 liakmtigmn eplfypvtyv dtlsqyllen yegatdvkvk lndtaalgel ekalnnyfpa
      181 idirrtaptd ltlvrqgtsk fngllffagq lgiplheiva vgdgpedaem iakaglgvam
      241 rtapaevkta adwvtrssdm dgvayavrei frkqlrvh
//
LOCUS       WP_010630522             268 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Sporolactobacillus vineae].
ACCESSION   WP_010630522
VERSION     WP_010630522.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..268
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29682
     Region          5..264
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,195,217..219,221..222)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mtfkmifsdi dgtlltsehr ispktkqail ackerhipfi lvsarmpdgi spiqkqlaih
       61 dpmvcyggal ivnegdighp llnismdpdl vtrfdqlkcn rfpdicfsay sinswlvpep
      121 enkwirqeqe iagtalqvfd fetgnpvppv nkvlcmgnpd qitalenllv erqteatfyk
      181 skptyleitd kkatkafald fltkrlgirr eetmafgdny ndiemlrfag kglamgnape
      241 gvkeaaddvt ssnnqdgiaa alkkfgvi
//
LOCUS       WP_010630546             182 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Sporolactobacillus vineae].
ACCESSION   WP_010630546
VERSION     WP_010630546.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..182
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19547
     Region          10..170
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mkvkeellvs tvsspvgllt lafyrdrlch idfgtaedtt aglihwakrn glpasvsdvs
       61 qageqaaeql hdyfsgrrkt fdldllligt afqkevwkal aaipygetrt ykdvavavgr
      121 pkairavgga nhrnplpivi pchrvigtng alvgygggld rkkrllelek pgkikavsss
      181 ls
//
LOCUS       WP_010630550             240 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Sporolactobacillus
            vineae].
ACCESSION   WP_010630550
VERSION     WP_010630550.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..240
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27042
     Region          18..226
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mvnktdptqi qtnnttmfsd rnleliqsim nkaefkkgan iywegdaadk lyfliegrvk
       61 lfksaydgkd lvlhyfipgd lfgelncfgf edysftahai tdcvvgviae rdleallmpn
      121 sslsfefmkw iglmsrytei klrdllfygk ngalastllr mahgygkrea dgihfsislt
      181 ntdlaqligs tretvnrmlq swksdgaidy ahgtivlrdl gyikaichce dkcpmnicrl
//
LOCUS       WP_010630563             188 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Sporolactobacillus vineae].
ACCESSION   WP_010630563
VERSION     WP_010630563.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..188
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21343
     Region          1..142
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mkivglsgai vgkktriamd rivktlseky peidttlidl adydvrfsdg rnyldyegdt
       61 ryvakkvmea daiiigtpvf qasipaslkn lfdllpvnaf rnkvvgmivt agtpkhylma
      121 eqqlkpilay mkaeivqtyv fieekdfyqn kihnddiidr idrlvedavl ltktyakvhe
      181 ekekeygf
//
LOCUS       WP_010630647             680 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Sporolactobacillus
            vineae].
ACCESSION   WP_010630647
VERSION     WP_010630647.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..680
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=74675
     Region          54..626
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mtrwstwnpi nkkkkkrrlv rlallipavp vlalllvlla akiagpmeip eirpavfhdn
       61 tgkvigkwdt snrqwvpvsq mapslklatl avedrhffqh hgfdlrrvag satvdllsls
      121 kaqgastitm qyaknlflnq dkswlrkate vfytmrlemn lpkekilegy lntiyyghga
      181 ygieaaakty fhkharqltl aessmlagip ngpsryspll hynqakkrqh lvlnmmvagg
      241 yltrsraaaa yrvpldfars dqkarqtapy fqdavrselt grlhfspeql esgglnvytt
      301 ldtevqkeae ywvrktipqk sgiqaallam dpdngavvam iggrnyqqsp ynravaarra
      361 pgsafkpfly yaalrngftp atmlksapsv ftfddghssy apdnfggyya drpitmaqal
      421 avsdnifavk thlaigmdkl vraareagit splapipsla lgskpvsvle ltrgyatlas
      481 ngirnrpelv tkvtdrsghv lyawhpagkq vldpkttfvl sqmmtgifdt rlngyttvtg
      541 apvagqlthr iaaktgttat dswmagftpe lvstvwigyd kgetistype tgyaksiwsh
      601 fvesaltgkp qnsfrppkgv vdvaidpktg liagkgvsgr ptyfvrgtap taysngtgnn
      661 gdssgkpqhh gffyrlfhww
//
LOCUS       WP_010630662             318 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Sporolactobacillus vineae].
ACCESSION   WP_010630662
VERSION     WP_010630662.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..318
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35032
     Region          <106..274
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mteffrliqn enmkiyrrqs akvmlilllg lilaaglivk tsqpapkent hwkqelvqqn
       61 qvlekqqtqv ggnrqainqi kktialnqyr idhnlkpsgg etlwgfvsga agntvllisi
      121 ftiivvagsi asefdtgtik lllirpvyrt eillakylss llfavlclvl lflfswligg
      181 lffgfdgaae ahlsytsgvv hqtswtlavw kdyllngvsl fmmvtvagli aaafrnggla
      241 iglsifmmmg ssiivtllsg yswvkyvlfa nldltqyasg tplrsdmtlg fslvvlavyy
      301 vvialagwlf ytrrdika
//
LOCUS       WP_010630684             158 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Sporolactobacillus vineae].
ACCESSION   WP_010630684
VERSION     WP_010630684.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..158
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=18232
     Region          56..147
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mtepkdsean rpikpirrkp ldeldaffrq dpfrgilksi ddffenhslf sggfpvrlye
       61 trnewvveae lpgatrenih idlyeeriri avendvsvet eqkdkgtysr erqfahaerf
      121 isvpytidra rthasflngv lkihgpkypk tgntlsid
//
LOCUS       WP_010630713             239 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sporolactobacillus vineae].
ACCESSION   WP_010630713
VERSION     WP_010630713.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..239
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26461
     Region          8..232
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mshpikgehl ykkfkkqvvl ddvsltlneg eiygligpsg agkttlvril lglekadsgd
       61 velfeqrptl dafrslgyma qsdalynelt ayqnleffas iqglhgnrkr qrimevaesv
      121 glekemkkgv aqfsggmrrr lslaaalihe prlylldept vgldplirrd iwtlfrflrs
      181 kgatmivtth vmdevakcdr vgllsdghli aegapkelte rygvatvedv flvkegaak
//
LOCUS       WP_010630715             726 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-galactosidase [Sporolactobacillus vineae].
ACCESSION   WP_010630715
VERSION     WP_010630715.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 726)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 726)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 726)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11245829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..726
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=82110
     Region          27..283
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          287..633
                     /region_name="Melibiase"
                     /note="pfam02065"
                     /db_xref="CDD:307952"
     Site            order(334,365,409,474,478,524,543,546)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          647..723
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 miqfdaaslq fhlqtpgssy viqvvngypl hlywgkriri yrgsapvrya yrsfapyadp
       61 kkpgfspgtl pleypasgtg dyrhpafhiq ldngttvsdl rysghriypg kkklpglpat
      121 yvesdqeaes ldlflkdavs glsviltytv frdfdvltrs avlknngagp lrlqralsas
      181 ldfrddqfds ltfygshnne rninrhplhe eiqlvdskrg asspqhdpff allrkntded
      241 hgevygcslv ysgnfaatie vsefhtvras iginpfdfsw llepgesfqt peavlvysgh
      301 glnrlshtyh klyrsrlarg rfrdqlrpil innweatyfk lseerllaia geaakagiel
      361 fvlddgwfgr rdndrsslgd wivdrrklph glgwlagkih dlglqfglwf epemvspdsd
      421 lyrthpdwcl hvpgrtrsls rnqlvldlsr rdvrdylvas vsavldsadi nyvkwdmnrh
      481 msevgsallp agrqretahr yllglyavle tltsaypeil fencssgggr ydpgmlyymp
      541 qtwasdntda isrlkiqygt sllyppvtig ahvsavpnhq vgritslplr ghvamsgnfg
      601 yeldltrlnd aekkqaceqv afykkirpli qfgdfyriln pfdegdaawc fvapdrseai
      661 gfyfrilada syrprffqfk gldpdapyen langetfggd elmhagvnvp nergdfhsyi
      721 wrirrk
//
LOCUS       WP_010630749             465 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Sporolactobacillus vineae].
ACCESSION   WP_010630749
VERSION     WP_010630749.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..465
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51175
     Region          1..397
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 msfsrvkkiy aitvyvslaa fdniviglfp plfqniahdm gvgvsamgvv sainilatsf
       61 ssllwgylsg kfhrkrliiv gtsiwvvgvf ltavssnyli llisqiitgv glgcvasigf
      121 saltdyvpyr srgmilslwg msqgfggivg aliasiistl snwrlpfevl gvvgmilavf
      181 yffveepkfg naepelqkli qrgqsytyri slnqvfamls krsnlllslq gffmniatgs
      241 liwlptlyia kireigygqq tamivaaflf gifqigglft syfgylgdvl qrksykarar
      301 mtaifvfltm plyillfifp ihklslpett nsvmlffalv rqlfvnpwml tlliisllas
      361 aaqsantpnw lalitdvnlp ehrgtvfsia nlanslgktv gnlgigaila ivslnlhspa
      421 dyiltmcllq lplipsalcy hymekfnddd irsvkqtlnr rgris
//
LOCUS       WP_010630755             351 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Sporolactobacillus vineae].
ACCESSION   WP_010630755
VERSION     WP_010630755.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..351
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39909
     Region          10..338
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mdvlinfmkr qttrrvlifa lliisvillr sminlflltf ifsflidrle tflhrhlkip
       61 rrlvvivvyc lialgiylav tiylpivadq tvqlyksiir efkdfhgsyi mtaiidqmkk
      121 nnvgsylgsg vkfvidsfss fgtftidlfl alllslffsl ekarlieftk gfksskigfl
      181 ydevaffgsr fvdtfgkvle aqfmiaivnt vitsvilavl hfpqlfslil mvfvlslipv
      241 agviislipl ciigytiggi qdviymvlti lavhcveayv lnpklmsakt elpvfytfvv
      301 lifsehfwgi wglivgipif vflidvlnvt ykrpnkkkir vygnkdeqsh h
//
LOCUS       WP_010630793             278 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Sporolactobacillus vineae].
ACCESSION   WP_010630793
VERSION     WP_010630793.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..278
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32081
     Region          8..266
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 medfllsngv smpkiglgvy qvkksqedti iwalqhgyrr idtaalyhne alvadaikks
       61 glkredvfit tklwnsdhgr ektlaafqks lerldtdyvd lylihwpsah yaeswqtite
      121 lyhagrirai gvanfekehl eklaqnsdli pmvdqvqtnp nmqqrelhry ltdhhiqhea
      181 wgpfghgnqn lfrqkylvgl aakyskttaq iilrwnlqrn iavipksvhp drlqqnldvf
      241 nfaltdqemd giasldknsr rfvdpnnklf lwlsslih
//
LOCUS       WP_010631079             419 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Sporolactobacillus vineae].
ACCESSION   WP_010631079
VERSION     WP_010631079.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45338
     Region          5..391
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(15..16,19..20,23,54,109..110,112..114,117,137,
                     140..141,144,230,233..234,237..239,242,264,268,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msvnfwklls grilsnigdc fynvsliwli yhltgntfyt gltgflvlap milqflvgpl
       61 iekfnkklll iateagqlvt vlaafvlyet vwhhvgalif ltpvvafltl fsnpaemtli
      121 pqfvdknkla aanslmnvty qtlqivftsl vgvllifisp lflyifsvlf nagsalcfsl
      181 irlrsnktpv teqadsaagl vsgfknyrrs laegfqtvsq tfigrllpat vvanlvlgtl
      241 tavlpayass rggsqwfgff qsaetaglla gaamapimkn iplgrmtifg ftvsglawlv
      301 sffsannals vllyafsfvp igvtnilfvs aiqravpqqk laqiytiivs igagmtpvgs
      361 laggelariw sltpvfisig vtflfvsayw fgdallrkmp paeqlgtgny titldrpek
//
LOCUS       WP_010630906              75 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein
            [Sporolactobacillus vineae].
ACCESSION   WP_010630906
VERSION     WP_010630906.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 75)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..75
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=8094
     Region          1..70
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mkiimqldel tcpscmqkid talkkqkgve dvrvlfnask vkatidpdqv taselsavie
       61 klgfavqsvk mkqgv
//
LOCUS       WP_010631093             380 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-glycerol glycerophosphotransferase family protein
            [Sporolactobacillus vineae].
ACCESSION   WP_010631093
VERSION     WP_010631093.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..380
                     /product="CDP-glycerol glycerophosphotransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=44201
     Region          4..371
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mitlyllafr fafllfryfp qknrvvfvvs fsentrfiad efrsehvave fvflcrgkci
       61 dafkddrsvv lpfetmnpga lfrsayylat akvvfvdnyf gflsvvrfre gvpciqiwha
      121 pgalktfgle dnsiagrser arrrfrkvye kfdkvvagse imadifkrsf gltddrilrt
      181 gfprtdfffq kheagrrpsh hfpadrkkil yaptfrnrqr drfpldldll kkelgheyvl
      241 llrlhpaers gyrfsaedqs fiidcsndss idelmlasdl litdyssipv eysllgkpmi
      301 fypydleayg kergfqsdyl kwvpgpvaft teelikvirq drfnlsqvke faalwnrysh
      361 gdaskklvdy vvgtygltrk
//
LOCUS       WP_010631105            1027 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Sporolactobacillus
            vineae].
ACCESSION   WP_010631105
VERSION     WP_010631105.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1027)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1027)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1027)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1027)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..1027
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=117201
     Region          10..964
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 msnapksaae ktfqenfvke lqkykweapd yldgnkqkvt vadlvthwrk elnrinadql
       61 egvaltdnef sqvmakvsri nnsyeaakil aieeskgkid gvyrddnpki trkqitltif
      121 kkaevrggds syriarevqt pndnrfdivl linglplini eqkrtdktld eafgqfmryy
      181 rdgeysnnfm afsqmmvits eiatryfatp ktigdfnpgf vfhwsdkdnk avndwkdvik
      241 qflmipmahq mvgdylvide ardeenrrhm lmrpyqvhal qavegaafgw dnkgklphgg
      301 fvwhttgsgk titsfktalf lstrvgfdkv vflvdrreld nrtsenfkay aayepvsvdd
      361 tsrtyqlkki lkstkngivv tttfklnalv keleeardns lankkivfii deahrttmgq
      421 mmgtikryfk knglffgftg tplfdenkik gkvneksevi ntteklfgpm lhqytideai
      481 adrnvlgfhv dyintgefks yddlreqlae kmkeehpelt dreierqvqe mseadvekqa
      541 kkrdllvyqd ethiprvvee ilsnwdaqsq grafnailtv aykdrviayy defkkqlkdr
      601 gaklnvamtf sfgnendpas ldpeiikgmf kdyaaftgie fiagdkkhge dayfedlver
      661 atrggsgrnp knidlvivad qlltgydskr lntlyvdrsl elqgliqays rtnrvfgsnk
      721 efgtiinfqy prmteervdq alklygsggk sskaivdtye tavkklaikv temiptlpdp
      781 tewqtiehde kkkeafilaf kdaaeqlnlv eqyykfkwdd aafgidehtw lqyvgayrnl
      841 trkpgtpspp tptnplvgkt klagtqvida nhilrligsk vtstngvqtv dsetlriiye
      901 qiqelsnmge yehaqllkef vdtelvpgkl ssglnfdeaf eawkarklnr avkdfskewg
      961 lnsdllgksv rsysysqpdv vpyideliss vdlnkashqs agnllrhnmm lttklpeeia
     1021 emkqkyd
//
LOCUS       WP_010631116             426 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Sporolactobacillus vineae].
ACCESSION   WP_010631116
VERSION     WP_010631116.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..426
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46706
     Region          12..418
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(23..24,27..28,31,70,128..129,131..133,136,156,
                     159..160,163,246,249..250,253..255,258,286,290,345..346,
                     350,354,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mekktkskll pvvsssiiga tiewydffly gvvagmvlnq lyfpsndpfl stllayvtfa
       61 vgffarpvgg vifghfgdkl grkrmliltv mimggstcli ailptydqig iwapiillll
      121 rvvqgiglgg ewggailmty eyapknkrgy yasfpqigls fglllasgvi glltallsdt
      181 qflawgwrva fglsivllit glwmriavke tpefqkvkdt nketripfkk mwkgntrkii
      241 agmgtryidg vffnvmgvfs inyltnhihi snsmatlgvs vaafvmcffi plfgywsdri
      301 grtkvyfwgs litgisampa fwmmghssgn twliwlaiii pfgilyaivy gpeaalfael
      361 fdaevrytgv sfvyqssgif asgitpiiat sllqagdgsp llltlyvlfs gvvsalsvgw
      421 iaelkk
//
LOCUS       WP_010631118             474 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Sporolactobacillus vineae].
ACCESSION   WP_010631118
VERSION     WP_010631118.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..474
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51930
     Region          51..463
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(61..62,65..66,69,101,151..152,154..156,159,179,
                     182..183,186,298,301..302,305..307,310,337,341,390..391,
                     395,400,416,419..420,423..424,427)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 meaegtisnr riksrgkase raidhyteqe rqqlearinn lpitgtmykv ftlitlgmll
       61 dgfdvylagg vlgslvqtgw stlflnaafi sttfiglfig siatgivgda kgrqfayqin
      121 llifglasla sffapnmitl iilrgisgfg lgaeivtgfa llgefmpaks rgkwvaslsv
      181 iancsaplat ftgfliipsv gwrwmfvivg vaslivwyfr rslpesprwy fsqgrfseae
      241 qvvsiferea ekkygerhpg tdlqdssqfn qideqqgkfs elfgrdeikk tllgcfilaa
      301 lntvaytfvt wvptllvngg itiskslgyt almmvgapvg afigrltvdr fgrkwmivgs
      361 fimtaifgys yafqtnptai miigflmtvc iyilmaigla iyvpelfptr lrmrgngtaq
      421 avgrfftiit pyavagllst qgpvsifiti gifmavvavl tilwgpetkk qilk
//
LOCUS       WP_010631130             252 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sporolactobacillus vineae].
ACCESSION   WP_010631130
VERSION     WP_010631130.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..252
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28028
     Region          2..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mllqvnhlqk ifqtrfskek tialqdvtfs vddgeyiaim gesgsgkttl lntlatlekp
       61 tsgsvilngr dvtkikenkl aefrrthlgf ifqdfnlldt lsvrdniflp lvlgrqkigv
      121 mqqrleelap klniadllnk qpfelsggqk qrvviarali tgpelvlade ptaaldfrns
      181 ehllslleei ngtgqtilmv thsaiaasha krvlfikdgr ifhqlyradr eaaafmqeis
      241 mtmtnllgte vr
//
LOCUS       WP_010631170             394 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Sporolactobacillus
            vineae].
ACCESSION   WP_010631170
VERSION     WP_010631170.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..394
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42518
     Region          1..393
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(98..100,124,174,205,234,236..237,245)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(101,134,198,243..245,274,277)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            237
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mrlaervati tpsstlaita kagelaaqgf dviglgagqp dfntpefiid aatealkagh
       61 tkytptaglp alkqaiidkl krdqgfdytp seiivgngak hvlyllfqal ldpgdeviip
      121 apfwvsypeq vkladgvpvp iqttqeqhfk invadleqaa tpktraliln spsnptgviy
      181 ekedlepiad fclkhdilii sdeiyekliy ngntfysiaq isdavkknti vvngvsksha
      241 mtgwrigyaa gdavlikamt niashstsnp asasqyaaia ayngpqdsve kmrqafekrl
      301 ntvyprlvgl sgvscikpqg afylfpniak tskacgfdtv tdwvaallee ekvavvpgag
      361 fgapehirls yatslekfqt aldriehfik khtn
//
LOCUS       WP_010631284             258 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator
            [Sporolactobacillus vineae].
ACCESSION   WP_010631284
VERSION     WP_010631284.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..258
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28431
     Region          1..249
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlaeerqqfi mrqladsrvv klqdlvcsln asestvrrdl qeleehhllr rihggasllq
       61 rrsdepdmet ktskniqqkk aiaktaagfi rdnecvylda gtttlemipf itasnvtvvt
      121 ngpahaetls trnvlcylig gmmkrttnav vgsmavdnln lfrfdrafig tngidavmgy
      181 ttpdpeeaav kkkalelsgq tyivadsskf sevsfckmfd lekatiitea lpesvreels
      241 srtkvycasp vqdktgve
//
LOCUS       WP_010631214             756 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Sporolactobacillus vineae].
ACCESSION   WP_010631214
VERSION     WP_010631214.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..756
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85068
     Region          5..752
                     /region_name="YprA"
                     /note="ATP-dependent helicase YprA, contains C-terminal
                     metal-binding DUF1998 domain [Replication, recombination
                     and repair]; COG1205"
                     /db_xref="CDD:440818"
ORIGIN      
        1 mkarqsmdel lsdlkrdpnv vhwhtvpgre avsvpfpesl dsricralnh rginalyshq
       61 adafqsvmag kdvvlvtpta sgktlcynlp vlqhllddpt sralyffptk alaqdqknem
      121 eqliqeigvp lksytydgdt sgtirqsirr agqivmtnpd mlhssilphh tkwvsffenl
      181 kfividelhv yrgvfgshva nvirrleric syygshpqfi ctsatirnpr ehaealtgrk
      241 mtlinrngap avrkhflfyn ppvvnkqlnv redemiavkt iaarflknri qtivfarskl
      301 kvellvshlq einsgrdeka kicayrggyl plerrrierg lrngdimgvv stnalelgvd
      361 igqlrvcimt gypgnmasvw qqagragrrq gdaiiimvas snpldqymat hpdyffsrnp
      421 edvrinpdnl miladhikcs ayelpfkkge kfggqpaddl cefladedll hfqagkwywm
      481 ndafpaneis lrsavqdsfa ivdvtdrgha rvigemdrfg amtmlyedai yihqgvqyhv
      541 dqldlderka yirkvnvnyy tdsdlavqmd vletdekkpl qgldadqsfg dvsvralptv
      601 fkkirfetme nigwghihlp ememhtngtw isfseawtnr fgkdvfqgvl aglshllrha
      661 aplfvlcdqs dlsvvprika thnelptlfi ydkypggigl skklyeampd llrkaremaa
      721 acdcesgcps cigfvsegra akqallhllg avapcr
//
LOCUS       WP_010631287             312 aa            linear   BCT 01-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Sporolactobacillus
            vineae].
ACCESSION   WP_010631287
VERSION     WP_010631287.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..312
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=34047
     Region          1..285
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mfktisvigs gvmgsgiaqs favggysviv ndikqefldk akknihenln llvgsgdlte
       61 adrnaalgri rfttdlkeaa geadliieai pevidlkwnl yddlatykkp davvssntst
      121 fpitkltare sfdgkfiith ffnpanlvpl veivkkkdtd lnlvqsvknl llsigktpvv
      181 lkkeingfia nrlqtalmre afslvgqgva daddvdkait agpgfrwafv gptriadfgg
      241 ldtwkrvfdn iapdldkseg apelinklvs thklgtktge glykysgddv raqlkkrdny
      301 flelgrikkv ne
//
LOCUS       WP_010631315             223 aa            linear   BCT 01-JAN-2025
DEFINITION  TerC family protein [Sporolactobacillus vineae].
ACCESSION   WP_010631315
VERSION     WP_010631315.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..223
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24255
     Region          22..183
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mtfdldtvif ilkiifidii lggdnavvia macrklpekq rnkaifigtg lavivriflt
       61 amvvsllnip flmligavfl ifiairlvtn keenyqfhps sslliavrti vvadavmgld
      121 nmlaiagaar ghigyiaagl visvpiiiwg skliliameh ipfliyaggg vllytasemi
      181 hdepvirqli agygfpeylf plilittvli icliyntvss rtq
//
LOCUS       WP_010631318             338 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sporolactobacillus vineae].
ACCESSION   WP_010631318
VERSION     WP_010631318.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..338
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36789
     Region          4..325
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 meklleiqnl nvqfdifgah vqavrgvdle lnigetlaiv gesgsgksvt skaimglnpm
       61 ppgkvtggki lyngqdlaha sdkqmqkirg keismifqdp mtalnptmki gkqimeglik
      121 hqnlnkhdar araiellslv gipnpdkrve eyphqfsggm rqrvviaial acnpkiliad
      181 epttaldvti qaqildlmrd iqkktgtaii lithdlgvva nlanrvavmy ggkivetgtl
      241 deifyhskhp ytwgllssmp rlhaktdkll aipgtppdls dppkgcpfap rcpyamkvcq
      301 dhmpdytkvt dtqktacwll dsrapkvepp ktvvvggn
//
LOCUS       WP_010631357             190 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Sporolactobacillus
            vineae].
ACCESSION   WP_010631357
VERSION     WP_010631357.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21658
     Region          1..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtadrkqsit raaektfaaf gykattmdlv arvagvgkgt iytfyknkee lfyeimnqfi
       61 rkiktvatna ihpddvffnn lhralfqvle frkehqlsik ltqeikeigt aqakralgnv
      121 edaildflvd iikdaekkgd ikpcdptvta fvilklyial vfdweqrhkp ltskeiadlf
      181 elylvrglkk
//
LOCUS       WP_010631366             405 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sporolactobacillus vineae].
ACCESSION   WP_010631366
VERSION     WP_010631366.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..405
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=44754
     Region          3..392
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mgkpqivilg agyggmittv rltkdlsaee aditlvnkhn yhyqttwlhe aaagtihhdr
       61 trmliknvin nkrinfvqds vrsvdrenkk vilkngeldy dylvlalgfe sntfgikgle
      121 eyafairsvn tarrirehie ykfasynndp dakesdltiv vggaglsgie figelvdrvp
      181 elckeydidp akvkiidveg lpivlppfer dlaeyaqkyl edkgvvfrlg tfikeatpdg
      241 vlvqkkdaee meeikagtvv wtggvkanhi vadsgfatnr gkiqvnkdlr apdddhvfav
      301 gdvavffpke gerpypptaq iavqegetaa knlthlikge dtepfvykqr gtvaslgdke
      361 gigvvfdkkl kgkpaatmkk iiddryllel ggvglmlkkg klkll
//
LOCUS       WP_010631377             329 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Sporolactobacillus vineae].
ACCESSION   WP_010631377
VERSION     WP_010631377.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11624702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..329
                     /product="M23 family metallopeptidase"
                     /calculated_mol_wt=36734
     Region          <109..153
                     /region_name="Lyz-like"
                     /note="lysozyme-like domains; cl00222"
                     /db_xref="CDD:469668"
     Region          <194..318
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mnrvskmmfc lmtfffaysg fadaehsdpv tpadqrksly lktaaltgvd wamlaacdqy
       61 arnitasvnr pehrplislt stdrdwaglf nirlhdqdpv sidffggtgk dgngdgkadp
      121 knpedallaf aeqlaafgpg eentriaiwn yfhrgkavel ieenaaifrk fntvnltgya
      181 fplpltanyd yeptwgarrg wgglrihegt dlfadygtpv rataygviem kgwnkyggwr
      241 iglrdlqgny hyfahlngya phlkkgtvts pgqiigyvgs sgygpkgtmg kfpphlhygl
      301 yhdngvseys idpypslrlw enqerlkrr
//
LOCUS       WP_010631408             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Sporolactobacillus
            vineae].
ACCESSION   WP_010631408
VERSION     WP_010631408.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..279
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30912
     Region          1..273
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mterqcmiri esayphlsdk erkiadyiln hpeetihssi nqvsarinva datvfrfcrr
       61 lefkgfqemk ivlaadiakn rqmeqeksky qddetmnlae rvfqdnirtl entfqilsss
      121 afnkavdlls taervaffgs sgsvtiaqea hrkfvragim tyapsdgefq mlsasqlsak
      181 daavfisysa sdkhllqvar aaeaagcpti gltgfmkstl gdmmdvslht vsvptdfrse
      241 syvaraaqmt lidalyanvi srkhaaghea ltqhlmaqn
//
LOCUS       WP_010631419             370 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Sporolactobacillus vineae].
ACCESSION   WP_010631419
VERSION     WP_010631419.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..370
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40952
     Region          35..366
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mfnkhskvif wtvemlaial lifvltkisf ifepvvtlft tlffpvlvag flffllspfv
       61 dflgkfkipk vlgilltyil ltglivllvt svgpplvsqv kalfaqlpdy ignwrrsfdq
      121 laatrgfkwl lhqniysidk iqqsllsmvk yytshagsgl stffgvvvnv altvvtvpfi
      181 lfymlkdgnr lpqavtrffp hqyhhevnti lldlsttlss yihgliivat fvgvnssigf
      241 aliglpysll lglivgvtni ipymgpiigt vpalivalmd spfkallvll vivivqqldg
      301 hlisplvmgk rmnthpltii vlllvsgkwl gpigmilavp syamikaivl hivrlirlrr
      361 kskddtllkp
//
LOCUS       WP_010631448             235 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sporolactobacillus vineae].
ACCESSION   WP_010631448
VERSION     WP_010631448.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..235
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25959
     Region          15..210
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mllsvainea gysaddpvlk dihfsidage lvgligpnga gksttiksil gtvksvkgtc
       61 kvsdyayipe rpllyermtl weyieflftt lntdesaymn lahqllarfq ltrvihqype
      121 nfskgmqqkv mlvlaflrqa klyivdepfm gldpravkrl lqslqqakan gagilmsthv
      181 ldtaekicdr filisdghmi fqgtlgeira hsglingsll dcfdlltede sdvge
//
LOCUS       WP_010631470             445 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Sporolactobacillus
            vineae].
ACCESSION   WP_010631470
VERSION     WP_010631470.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..445
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46345
     Region          14..419
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 metthkpgki fslgiqhmla myggavivpl ivggavglkg aelallisid laacgiatll
       61 qawknrfsgi glpivmgctf tavspmivig ksygmpgicg ailvaglvvl vmstffgkiv
      121 tlfppvvvgs vvmiigitli pvainnlggg vgakgfgsaq nlllgfgvll liilmnrffk
      181 gfmqtisilv siiagtivaw fmglvdfssv gsagwfslis pfsfglptfh ldaiiamsiv
      241 givsmiettg vylalseicd qpindkdmqh gyraeglail vgglfnafpy ttfsqnvglv
      301 qmtrvktrav tivcgisliv lglipkigav tilipnavig gatlamfgmv iasgvqmlgr
      361 vdfkrqenll iiacsvgvgl gvtvqpelfa kfptlvqilt nngivsgslt alilnlvfnv
      421 grhpekesvt klskqmvaet satks
//
LOCUS       WP_010631473             549 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Sporolactobacillus vineae].
ACCESSION   WP_010631473
VERSION     WP_010631473.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..549
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62485
     Region          5..124
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          252..537
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mkvsdlfqip lfhelrlvag gkgtdreicn vnmmdapdii dylkpndwli tsgyhlqdnp
       61 dffyqlvnqm agrgcaalgi ktrrfiggip ervirlanrl sfplidlpns lalvdidnqt
      121 lsmildartk elqfaidthq qftrhimsge gigrllsqls dmigcqvvll dayfkridas
      181 grepkglkta eqipaadqsv frkqraaysa fsvigthrtf slfvlhtykk kryflliegl
      241 vpqtdrlltl tveqalnvla felmkdealr qtdrkvrdaf fsnlvlgsfs tdeeivsrat
      301 efglrdgqtl vcaageldtv repisfihyq metneiyeyi egeirafpfp ahlfvkdhic
      361 vlivemmase ensyrflkpy llnvqkqvtr ffpqtlsfgl sniftdlsgi psayqeavda
      421 lhagmqigrr sfiqayqarg iadllhrvpa edlrklyqdt lqslafpkke enrallhtly
      481 vylesncqis etakklyvhr ntviyridkc eqmlgkdlkd pditfqlrfa lrlkplidet
      541 gtaagkrkk
//
LOCUS       WP_010631552             335 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Sporolactobacillus vineae].
ACCESSION   WP_010631552
VERSION     WP_010631552.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..335
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=37142
     Region          72..334
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mrnysenesr qeikkhqkrh rvfrrlvvll vlilaiaagf tafevhrlnp enrfahlkvi
       61 ggnssapvas gtfnllligs darkgdtash sdsmvlihan lkkhtydlis iprdtrvymn
      121 gygytkltsv qyvsqmkngq qqgildavsa vsgltgvpin fyaetnywgl rdmintlggi
      181 emnlpfkvtl thpwnksftg ktypaglhsf dgttvtelvh eryslpgtdy grqqlqeaal
      241 mgiakkvmqp snvtklpals rslskflvat nlssedllsa glsakgnfnp akqiryrqvk
      301 gtsvrmhddv lnadnaqiil dknqlqtiis kyfks
//
LOCUS       WP_010631500             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Sporolactobacillus vineae].
ACCESSION   WP_010631500
VERSION     WP_010631500.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444071
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34019
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_GltC_like"
                     /note="The substrate binding domain of LysR-type
                     transcriptional regulator GltC, which activates gltA
                     expression of glutamate synthase operon, contains type 2
                     periplasmic binding fold; cd08434"
                     /db_xref="CDD:176125"
     Site            order(107..108,110..111,114,120,122..128,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176125"
ORIGIN      
        1 mnlkqlyyfr dlaetenysl sadrltitqp tlshaisllq selgvllfek qgrnvhlthy
       61 gkcyltyvrk aldelkkgka aldtlidphs gtielafiyt mgaafvpkmv refsdkpvyg
      121 rirfsfhqgt tqdvtnklid escdlavcsy aeghpeisft pvyreelvli tsknhplaky
      181 dridlrqttd ypyilfnrks glypyirdtf rslrlqpkia civeedqama glvsinygia
      241 iipkmkmldt fdvkilkitn kipariiyla ylkhsfmspa adafkdfllk qnhpisld
//
LOCUS       WP_010631567             246 aa            linear   BCT 01-JAN-2025
DEFINITION  YdcF family protein [Sporolactobacillus vineae].
ACCESSION   WP_010631567
VERSION     WP_010631567.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..246
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26702
     Region          12..243
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 meyvikfiyg fmlppglfvt ltaaaavwlw rqkrkaacfc gafsvllyls flpltgallv
       61 hplenryqpp aqvngdvivm lgggategtp dlngtgqlsg daanrllmty rlyqktglpi
      121 iasggkvypd sgreadiarr elialgvpkg kviaenqslt trqnavntek ilkqrrfvrp
      181 vlvtsafhmp ravrnfqkvg aqvipyptdy lvskrialyp aqfvpsdaat aatalkeyag
      241 llatlf
//
LOCUS       WP_010631588             323 aa            linear   BCT 01-JAN-2025
DEFINITION  ketopantoate reductase family protein [Sporolactobacillus vineae].
ACCESSION   WP_010631588
VERSION     WP_010631588.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..323
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35684
     Region          1..309
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkivvigaga mglrygillq eagndvdfve pwepsykair eqggvyvsrd yqnqhlvpvn
       61 vyqpaeyekt pdlvilfvkq mqseeamaac ahfigpdtyv ltnqngigsv diirkyvpdq
      121 hviagialia tvldapgkvd fmgakgaght hlsnvtekpd aftkqvveef qkagmnptlh
      181 tnylgtlwgk llmnsvintl ctlmditmgq yvsypganal tkrlidegya agqadgvrfm
      241 qsreemaevi yhessqvnpl hhpsmyqdmi ngrptevdyi ngyivkvark hglnaeshqm
      301 lvdllhlaet vqqmktekqs svk
//
LOCUS       WP_010631615             387 aa            linear   BCT 01-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein
            [Sporolactobacillus vineae].
ACCESSION   WP_010631615
VERSION     WP_010631615.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..387
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42132
     Region          1..375
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mktffvwlic atllltavlp agtasaettd skssgvksai vieqetgril yqknadkelp
       61 pasmtkvmtl llifkalsqh risltdqvsv sehaasmggs qvflepgerm tvdemlkaia
      121 iasgndasva maefvggsek efvkqmnqea aklglkhthf enttglpvkn hyttahdmav
      181 maqalarykq vfnytskyed ylrqntdqkf wlvntnklir typgadgmkt gftneakycl
      241 tatakrngmr viavvmgaas pkernseiag lmdqafagyt tqklldkgrl vasrpvdkgn
      301 pahlsivtgq qavlllkkgd eagtttkktv inknlqapir agtvvgyyqi skkgrtvskt
      361 plvagenvkr agwwqlftrv tvsiltr
//
LOCUS       WP_010631688             724 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Sporolactobacillus vineae].
ACCESSION   WP_010631688
VERSION     WP_010631688.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..724
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=81478
     Region          <344..723
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mqhvhmmyal nrklkqhheq vfegisngrk kaldnwfrdr wvelenvsri vesysdsset
       61 ekmmhrqlde ssdfiefill detgtvrhst cirhigakms dlpnysrgir nkrlmygpye
      121 dlrtldidcs nlhfhdevtl mfslpgenae grktiflgrv lndtlsnviq dedthvykes
      181 gdnylfmvqs arnilpgtai srsrfedntf tlgdnlkdgv rtgrwgvvrv dkhtefeirf
      241 tdpktgdlhq gvnktitngs nldvwpgypd yrhilvggkg tlihppfsde vwgmmcegdi
      301 aeiynfrsln lriplyysls aaaavavngi cfrfsmfwgl icsaatwlil slyvcltvrk
      361 lvvtplnrtv dilhqvaege gdlttrvnkn sydeigelsr wfnkfinnqm tmvkrvgrsa
      421 kasksaattv ngmtghlses mktvagtvng lvatakqqna ifqdtrsqfn dlseaikemg
      481 llihqvtekt edtsgrtrka nltssetldq igelektmgg tmahidqlhk hseaiteavt
      541 tisgiseqtq mlslnaaiea srageagrgf svvasevsrl adqteeatgs vrhlveniqn
      601 etkrtledir rtdekvriss rnikntidtf hyisenikei tekmerlkei tiqeshdvgd
      661 vvirinraad vikektakna ssseasmdll ndvaeeitrl kqitgnldyv senlqrmvsa
      721 fkvv
//
LOCUS       WP_010631690             329 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease
            [Sporolactobacillus vineae].
ACCESSION   WP_010631690
VERSION     WP_010631690.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..329
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35449
     Region          6..329
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 msqiiqllpq vlvdgltlgf vyavvaigyt mvygilelin fahgdifmtg sfvgagvlft
       61 vmsmgfmssa ptmvlfmimi lvaalitgvm gvgiervayr plrkrnapkl ialitsigis
      121 filedavrfi adwttgnyii ttrplfqhkf tidfhsvfpf fnnatfqgsf lvvsivtiim
      181 lisldlfvsk tkwgiamrav aqdretaslm sinvnrvisv tffigsalgg atgvlfliqy
      241 gtvdpyigfi lgikaftaav lggignirga mfggillgll emfaaanlst ithgamgsey
      301 kdvfafiili lvlifkpegl fgkatiekv
//
LOCUS       WP_010631805             181 aa            linear   BCT 01-JAN-2025
DEFINITION  LemA family protein [Sporolactobacillus vineae].
ACCESSION   WP_010631805
VERSION     WP_010631805.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..181
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20703
     Region          21..181
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mtliiviavi aiiviffivs ynglvkyrnw vqesfsqidv qlkrrhdlip nlvetvkgya
       61 kheketlsqv iearnrlvsg tpqqrieadn qiegalrsif alaesypdlk anqnflslqe
      121 elattenkva ysrqlynktv kdynikresf ptnliaglfg fkreelltip etdrevpkvt
      181 f
//
LOCUS       WP_010631835             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Sporolactobacillus vineae].
ACCESSION   WP_010631835
VERSION     WP_010631835.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 272)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..272
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29631
     Region          18..272
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkrfakalsa llvlslvfal sacgssssge lstkevtvgv tagphqqvme evarlakkdg
       61 ltihlkvfnd ynqpnialnd kdldansyqt mlflkdqikn kgykitdafa tvafpmgiys
      121 ksikklselk ngqkiavpnd panelrglql fekagviklk kgagvtstkr dvisnpkhlq
      181 iveldaaqlp kqldqvaaaa intnfamgag ltvlkdsifh eplvhnpypn yfvvrtankn
      241 dkvikqiqky yhsadvkayi kktfggsvvp aw
//
LOCUS       WP_010631845             210 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Sporolactobacillus vineae].
ACCESSION   WP_010631845
VERSION     WP_010631845.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..210
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23804
     Region          6..198
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mtqfdlpele fspdalepyi dketmvihhd rhhqtyvsnl naalakypel kkasltdlii
       61 hldkvpeeir tavrnngggh ynhsllwkvl ipggaheprg nlkkaidsaf dsfesfrddl
      121 saaaagrfgs gwawltldar kkltigstpn qdsplmdgqt pllgidvweh ayylkyqnkr
      181 peyiknffkm inwdfvsdvy dkvtgrmvae
//
LOCUS       WP_010631856             314 aa            linear   BCT 01-JAN-2025
DEFINITION  ketopantoate reductase family protein [Sporolactobacillus vineae].
ACCESSION   WP_010631856
VERSION     WP_010631856.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..314
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34306
     Region          1..305
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgvga iggffgglla knkldvtfia rgktlerlrs hplevksikg dfslqvevld
       61 agkltgdetf diillavkst alqpsieeik klsgpqteii cllngignee klaetfgpeh
      121 ivggsafisv ireapgvvnh vgegtlvige wkkgknadrl vplikafsas gikatvseni
      181 rqikwekllw niiynpltal tgtrvgeale dpdlndlfnq vkqeflatar avgiqirssy
      241 vdnvllpdpq vqnhktsmlq dfengrkmel eailgfvvqt agnyhvpvtt idtlyhllrf
      301 aersrketeg nnkk
//
LOCUS       WP_010631858             259 aa            linear   BCT 01-JAN-2025
DEFINITION  SH3 domain-containing protein, partial [Sporolactobacillus vineae].
ACCESSION   WP_010631858
VERSION     WP_010631858.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..>259
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
     Region          43..174
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
     Region          126..248
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 miptrsltai gtfaaaaaav aaaaaampgv ahadefktyi gqattllnvr stpstrqpki
       61 grfspgdtfk vtgvagksek gnwlqityqn ktayvdgtyv tqkqqpaank kptqsvqsiq
      121 hyqvfttdnl nvrflpgisg tvlttlkkgs avtvtgktad gwlqisykgg sayvsekyvq
      181 sgstprlsak asvtvqykgt ttdnlnvrtg attsakrltt lkkgstvevv gtnggwlqir
      241 ygggtayvsa dyvkkngsa
//
LOCUS       WP_010631895             354 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Sporolactobacillus vineae].
ACCESSION   WP_010631895
VERSION     WP_010631895.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..354
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41045
     Region          6..216
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mresvkisii ipmhnvtkyi sttiqsiinq sfsdlevlcv ddhstdgsks ivesysrryp
       61 fihliinnkq sgvsesrnlg ldmadgkyim fvdaddklgk dmiklmlsda iqqkadlvig
      121 shkmfndqei lqhnmykifp sltiagekki imnpelfypi yvwgklfkre liqkvrfpkh
      181 iqycedqcft ifaylnaski flspqaiyyy rvreendpsl vkkadqdpsn aindiinvlk
      241 inyhyfeqfi sgvlnrnllf ghylnrvily nvhgivrnmf ifatpndqik iihllndwin
      301 nlddkmvlnv ksiqlilvqq mmnyiqestp evkasyivll rniktkmqra aglq
//
LOCUS       WP_010631934             294 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Sporolactobacillus vineae].
ACCESSION   WP_010631934
VERSION     WP_010631934.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15747380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..294
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34056
     Region          33..>119
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          203..286
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mihysenqfa dsdkfpfrms idefhvgeit glhdhaftem iyvaggagmh qynrrtteir
       61 rgdvliiqpg mmhaysvakg sylklyrimf hqrlldgewa tlnhasayid pffidpsmig
      121 nksfhsslsl sssrqfelvl lldriyseyt rkswgyhcmi rmqlmevfly larwaaaerp
      181 qsvekkdqye eicsyvkqhy mqeislkqmc sfsglsqsaf tmnfkkatgv sfldyrnkvr
      241 idaakdlltt tdltvtmvaq kvgfrdisnf nrtfkrfeac tpnvfrknqs isae
//
LOCUS       WP_010631951             281 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Sporolactobacillus vineae].
ACCESSION   WP_010631951
VERSION     WP_010631951.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..281
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31581
     Region          4..276
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,207,229..231,233..234)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mikliamdld gtllnskrti swdnlkalrf arskgvtlvi atgraffdvr hlmqeidiqt
       61 hvigtngati htiegqliga dvldrtaalq avselaaqhy yigvytdkni yvpregtnwl
      121 yqeldrlhih edrsvgfqga trddfyrffd dpqeiekegr difkiiicsy ddakllkarr
      181 fyeekhryni vssgignfei mgpnvskgna lyhlasfldi pledvmaigd nyndlsmfav
      241 sgisvamgna devikkkctr vtldcsddgv asaiyeelkr k
//
LOCUS       WP_010631989             127 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Sporolactobacillus
            vineae].
ACCESSION   WP_010631989
VERSION     WP_010631989.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..127
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14525
     Region          28..119
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mlswvilivl aaaylgyait srlmlrrylt tlseadfrag erkaqlidvr epnefknghi
       61 lgarnipleq lkmrkqelrh dmkiylydsn gsrsaraaat lkrlgyrnlf dlqggfkkwn
      121 grvkkgi
//
LOCUS       WP_010632039             346 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Sporolactobacillus vineae].
ACCESSION   WP_010632039
VERSION     WP_010632039.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..346
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39208
     Region          113..339
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msgikrqiis gilfslcfli ifstlyflvf ppgnweliwt rqvwhlpfal ivpalaacfg
       61 lasgflsgfy wrstlnridd aladltqgrr qdlslllksd dtkmignklq elerqveeqa
      121 qlsrkmasrk seieekviqn vvseernrla relhdsvsqq lfaasmlmst inesqlpand
      181 aqtrqlhlve etihqsqlem ralflhlrpv qlhgkalkeg medllgelrq kvpmtinwti
      241 epirlekgme dqlfrilqes vsntlrhaka stldvllirr dglaimrisd dgigfrrdqd
      301 kpgsyglmni reraaqiggq lrlvsvpgqg tsleikvpil kgeele
//
LOCUS       WP_010632055             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Sporolactobacillus vineae].
ACCESSION   WP_010632055
VERSION     WP_010632055.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..397
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42844
     Region          13..377
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,138,
                     141..142,145,219,222..223,226..228,231,255,259,309..310,
                     314,318,334,337..338,341..342,345)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mkryndtlrf paligavlic gtaegmllpl iasmleeqgv paivngagtt alyigmlval
       61 pfmerpmqkl gyrtfllvgl llitlalflf plwfnlwfwf vlrlavgigd smlhfaaqtw
      121 itigsphkkr grniaiygla fglgfatgpl lvrllafgia vpfltagflc tlfliplvll
      181 nnafpdqttr qgtrlsdslr ryrkttamvw sgltatfgyg fmeaslnnsf pvfalrnglg
      241 mngvaallpa fvcgglitqi pigmlsdrlg rkkllpiltl lgavtflvsa lipvrfsgff
      301 ftflaagllt gslyslsmgy vsdmlprrli plgniqmsls ysigcmagpv vsnllisvak
      361 kgslffgiag mllivsasvv mqqigrsrks cetvrvs
//
LOCUS       WP_010632056             147 aa            linear   BCT 01-JAN-2025
DEFINITION  VanZ family protein [Sporolactobacillus vineae].
ACCESSION   WP_010632056
VERSION     WP_010632056.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..147
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=16415
     Region          <87..132
                     /region_name="VanZ"
                     /note="Glycopeptide antibiotics resistance protein
                     [Defense mechanisms]; COG4767"
                     /db_xref="CDD:443799"
ORIGIN      
        1 mmklsdpkhr lvlaclliyl aavliltllt hnyytygrsv nltlsksirl mlrsgdslli
       61 lknvagnval flplglllpa llrgrfrflk tvasgflfsl aielvqyfia srifdiddll
      121 lntlgaltga vvfsmtvffr hrifffs
//
LOCUS       WP_010632057             287 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Sporolactobacillus
            vineae].
ACCESSION   WP_010632057
VERSION     WP_010632057.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..287
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32135
     Region          1..287
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mekraekekf getkvlirlf rnrliedhtv dlaatlayyf llslfplvif lfavlpylgl
       61 tkqevipfln qylpgevmsl irenldvvft ksggllsvgv iatlwpassa inalvrtlnr
      121 afhvretrpy iltrflamcf tvamvfaiam tlavnvvsaa wtktlfaqlg lsdnffqlws
      181 vlstlvtfaa iilifaflym lgpnirlklg dvlfgsifag igwqlasyaf smyvryfghy
      241 astygtlggi iilmiwfyit aftvilggqi navyrefaar rqppgkp
//
LOCUS       WP_010632071             172 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma carbonic anhydrase family protein [Sporolactobacillus
            vineae].
ACCESSION   WP_010632071
VERSION     WP_010632071.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..172
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17827
     Region          4..167
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mlhygehfpk vdpsvfiapg aqvigqvvlg arasvwfnav lrgdeagifi gegsniqdgt
       61 vvhvdakdpv rvgknvtvgh nvtlhgctve dgsligmgat ilngavikkg alvaagalvl
      121 enqvveagtl vagvpakerr klsqdnadyl kydaahymaq akkyleagig qs
//
LOCUS       WP_010632110             100 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Sporolactobacillus
            vineae].
ACCESSION   WP_010632110
VERSION     WP_010632110.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..100
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=10828
     Region          1..94
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 myeeitpqav erliegkgev siidvrepwe fakghipgak nisvnellsr ldeidktkdh
       61 iivchsgnrs gvasailsah gytvknmagg mlewngqvvc
//
LOCUS       WP_010632108             190 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [Sporolactobacillus vineae].
ACCESSION   WP_010632108
VERSION     WP_010632108.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..190
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21358
     Region          1..173
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mdetvrcasl krrilaflld yfiiaaygli vigtlsallh sffrplfags aaiaeltgfl
       61 lmtlpvalyf licecapwqg twgkrrlalq vvdrcgrrig pvrsavrtva kfipwetahf
      121 avwqillpgp vpertavtll ilvhimaaiy lfsqltnrer rsvydwiagt rvivrispsr
      181 dtvnflaerr
//
LOCUS       WP_010632098             456 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Sporolactobacillus vineae].
ACCESSION   WP_010632098
VERSION     WP_010632098.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..456
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49479
     Region          11..439
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mwdlttgspi kriimftipl lignlfqqly nisdtiivgr tisvqalaav gatdslfali
       61 igfaqgmtag ltvitaqryg ardhlgvkrs favnilisis vsliltvigv lfarpileim
      121 qtppdiidda qrfivvcfwg isvtvlynlf nntlralgns rpplfflaaa cvlniifdfi
      181 filffhmgva gaglasviaq glaavwclsf ikrhvpelvl frkhfrnvfs qeggqhlrlg
      241 ipmgfqtsii svgavivqim lntlgsdava ayttagridf latqvslsfg itmstyaaqn
      301 lgagkygrir kgvrqatgls cslsivmgtl iiifavplcy lfvgsqkpsv ihmaqiyflc
      361 nstmysvlsi llitrytlqg lghsfvptls givelfmrsf svifliriwg ftgaslanpl
      421 awtgalmiva gayitemrrl eslekgmyap kspgvy
//
LOCUS       WP_010632119             438 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Sporolactobacillus vineae].
ACCESSION   WP_010632119
VERSION     WP_010632119.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..438
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49676
     Region          1..188
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 msglmnllnt ygyptlffal mlelicipip nealmsyvgi lsfhgkmnyl lsvltagggg
       61 iagvsisywi gyklgapffk kygkfihmgp ekmekvsrwy skygkvllif syyvpgirhi
      121 asiisgvirl pfrsfalysy igvflwtstf islgyvlgpq wdkyqgqikk wlvlamvlia
      181 lgvvcylvik anwpfikksa llifqsffkr yrsflrikli lilllvsfva lftlmigmiq
      241 dfvsndagpf nevtrsivyf ffndnwkall qdlyslsswp llgliallti miilvnhtdq
      301 wlellfyglt iaggflfslg vrwlfhflig nrrinmdfpd qhaflitlfc glllmalirh
      361 qhnyllmail fsvfiillla fgasgiylsg lnpndllagy vfgavwgsgm illlelfrfl
      421 sliknndqpv ghgwkgrv
//
LOCUS       WP_010632192             208 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Sporolactobacillus vineae].
ACCESSION   WP_010632192
VERSION     WP_010632192.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..208
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23028
     Region          8..201
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mttlagyklp elpyaydale pfidektmki hhdrhhatyv anlnaalegy aslsdkpiea
       61 llsdlsavpe nrllairnng gghanhsllw tilspngggv pageiaaaid etfgnfsafk
      121 kvftdaamsr fgsgwawlva dkgalevmst anqdsplfvg kqpllgidvw ehayylkyqn
      181 rradyvqaff nlinwdavnr nwekhrnh
//
LOCUS       WP_010632333             341 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Sporolactobacillus vineae].
ACCESSION   WP_010632333
VERSION     WP_010632333.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..341
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38181
     Region          13..339
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mmktgeeenk venrhhalgf sdqdvlnmyr imltarride rlwllnragk ipfvvscqgq
       61 eaaqvgaafa lnrekdyvap yyrdygfvla wgmtvremml nnfakaedpn sagrqmpghf
      121 gdrklrmlth sspvttqnph avgialaaki kgddivsfvt fgegssnqgd fheacnfagv
      181 hklpvifmce nnhyaisvgl khqlacahvs draagygmfg rtfdgndpla ayaavkeaad
      241 rahrgegpsl leancyrlqp htsddndmty rtkeevdahk kydgvltfaq ylrdleiltp
      301 dveqqleeqi rseideatdy aeqapfadpd svlryvyeek d
//
LOCUS       WP_010632365             175 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Sporolactobacillus vineae].
ACCESSION   WP_010632365
VERSION     WP_010632365.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..175
                     /product="YceI family protein"
                     /calculated_mol_wt=19008
     Region          2..146
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 manwtidtah tetsfsvkhm glsnvrgnfd ttsgtvttde qgkitgidat idvasidtrn
       61 edrdnhlksa dffevekyps ihfvatsikg ddedytitgd ltikdvtksi tftaeigepv
      121 ddpyglkrsg aslsfsidrr efnlnwsqsi angslvvgnk vkvnvdaeit qnpna
//
LOCUS       WP_010632400             318 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Sporolactobacillus
            vineae].
ACCESSION   WP_010632400
VERSION     WP_010632400.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..318
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35401
     Region          14..316
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mkmidletkk qyiqiaqmyy eqnmtqseia aavginrtsi srilkklree givkiiinya
       61 vndislaqrl kdrfhlkeai vvpvqqddkq mkltaigqac akyldhitqd ndvigfswgs
      121 tlaevvdald isspkhhvfc ipliggpsgk lasryhvnti cyaaaqkfng hslmidvpai
      181 vetsslkkef letkyfgein hmwdqvniav fgigslqiak ssiwfefygn dsvakfsden
      241 vagdvcshfy dlngdeirth itdrtisipl dklkraeysi gvaesrekvp giigalnghy
      301 vnvlittket aemvldna
//
LOCUS       WP_010632430             527 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Sporolactobacillus vineae].
ACCESSION   WP_010632430
VERSION     WP_010632430.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..527
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57562
     Region          2..449
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mskqgkfkqe islsdltfig lgsmfgsgwl fassqvatia gpagilswvi ggiailllgl
       61 vfaelgaalp ragaivrfpv yshgpiigyl mgfmnlvaft slssieveaa rqylaawipg
      121 ftqknstlpt vsgwlfqlll lviffslnyw svrifaksnt vitlfkwivp tltililfsq
      181 ikpgnftvdg fapfgfsgvq kaistggvmf aylgltpils vasetrnpkr tiplalilsa
      241 vlstiiyill qsafvgsvpt rtltsgwggi sdqfrlpfrd ialmlgfgwf aviivmdaii
      301 spagagnifm sssprvvyaw aksgtlfrlf tridkksgvp rpalwlsfaf cvfwtlpfps
      361 wqvmvnvvsa alilsyaiap isaaalrrna vglerpfylr gmpvigpisf iiaslvaywt
      421 gwttiswllg sqilmylvyl lcrkivpkdq vgfrqqikss lwlifyyigl mvvsffgtfg
      481 gnhlltqpwd vlaivivsli ayywalfscl pkavldkase etekspg
//
LOCUS       WP_010632553             224 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase
            [Sporolactobacillus vineae].
ACCESSION   WP_010632553
VERSION     WP_010632553.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..224
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=25051
     Region          121..211
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mvkrytaivi iyllcllspy ipgfmtlark fptvrqgyga vyttvffvtl aivllllwpd
       61 rqllrdvkra slpvsivwav ggvfalfalq mlatlinfai fgqvsgseht rqvetltrys
      121 pvflltvsiv gpileeivfr kilfgsmrhk igfwfaalis slifavmhqd lhnllvyvli
      181 gvflcftyqm thriavnmfm hatmntvvvl isygvssagf aglf
//
LOCUS       WP_010632556             649 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Sporolactobacillus vineae].
ACCESSION   WP_010632556
VERSION     WP_010632556.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..649
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73267
     Region          6..536
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          571..647
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 millqtndvc ksfaanpilt nisievklge rvalvgrnga gkstllkiia gqmsadsgev
       61 impkdrtmgy lpqnatlnst rgiydelltv fkplteiekk lrkmeeqmad pdhfahrsde
      121 dqllksydtl qaefrsrggy tyqaeirsvl nglnfgsfpe dtpvsnlsgg qktqlalgkl
      181 lltrpdllil deptnhldid tltwlegylq rykgsvlivs hdryfldkva tkiyevaght
      241 vtkydgnytr ymklraaaye namktydkqq kevarltdfv rknivrastt kraqsrrkql
      301 ekmnlmdkpr gdeksadfsf qiekqsgrdv lavtdltvgy aadapmirgl nfhltrgerv
      361 alvgpngigk stvlksiagg stllkgdvrl gsqvtigyyd qeqtsltnek tvlnelwddy
      421 plkpeneirn ilggflfsgd dvakyvsqls ggekarlmla klmmrhdnll ildeptnhld
      481 ldskeilega lidypgtilf vshdryfind iadrilelsr agiteylgdy dyyqekkleq
      541 qqiaeldaqs apqakkeeaa pdgkqqflkd keqkkrkrql ersiddleqq isqmeetike
      601 aedslltpev fndakkagev qeqidrnkak lsklmeqwes dqleleafn
//
LOCUS       WP_010632566             225 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Sporolactobacillus
            vineae].
ACCESSION   WP_010632566
VERSION     WP_010632566.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..225
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25709
     Region          8..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtedqtlrak kkkdqilrsa qklfiskgfe atsmdeirnl agvskqtiys yysgkeqllf
       61 dviekqlfll senafssvle tldfstpqev ehslirftre mldhfmqvdy lqlarvvvse
      121 vvkypelarm freavplrgl knvekmlrka nlsdcvsidh peiaarsfvg tiltyvfidg
      181 vlsdqkssae pseqqirqmv rfylpsilae rqgteknsir qgeak
//
LOCUS       WP_010632600             553 aa            linear   BCT 01-JAN-2025
DEFINITION  multicopper oxidase family protein [Sporolactobacillus vineae].
ACCESSION   WP_010632600
VERSION     WP_010632600.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..553
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=60098
     Region          49..537
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mkkfllivia vfalliinac sastenknaa sqqtagsnsa askspsilrg pnitlvaekg
       61 tqklsngvtv pvwtfngstp gpeirvkkgq kfrvtlknel sapvsihwhg ykvpnqmdgi
      121 pgvtqdavap gksftyefva sqagtywyhs hqdsvnqvdr glygafived pkekfdkdyt
      181 lmldewvtdq nqinsqvkam tpggqnknsd ssgmgsmpgm dmgssdqgss gggnsgmnmd
      241 nmgngssgsg dnnsnnmlpn mmadnmsmyn lytingksgs lvkpltvstg dkvrlrfina
      301 gylphnihih ghsikviatd gqpvnnpqav knqvisiapg erydvsftad npgkwyiedh
      361 gtakgtnrmk alinykgstk stdqpdagtq lpainfadyg tktkpeftln qkydvsytms
      421 lnagmnnngm iytingksfp ntdpikvktd drvkvklvsr dhmnnhpmhl hghefqvlsk
      481 ngkpvtgspi ykdslnvkpg etyevaflad npgiwmfhch dlhhanagmv tevnytdyhs
      541 dyvpkasnnn kpe
//
LOCUS       WP_010632636             184 aa            linear   BCT 01-JAN-2025
DEFINITION  VanZ family protein [Sporolactobacillus vineae].
ACCESSION   WP_010632636
VERSION     WP_010632636.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..184
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21315
     Region          1..161
                     /region_name="VanZ"
                     /note="VanZ-like family protein (function unknown)
                     [Function unknown]; COG5652"
                     /db_xref="CDD:444373"
ORIGIN      
        1 mlknkkafwi wmvlslfiia miyrgsampy sqqdiqpflr ahfqwtsetf phisfnysge
       61 qitsadpyaf fefavrkash vmeymlltfm linmfmttil prffcylfgp gaalcysffd
      121 eyhqtfiagr tghlidsltf dlsgmilami lvflldlyfk llytgsghhh sssrprprha
      181 hseg
//
LOCUS       WP_010632704             288 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sporolactobacillus vineae].
ACCESSION   WP_010632704
VERSION     WP_010632704.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..288
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32281
     Region          5..221
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtsilevnnl tktydqfsld rlsfslqkgc itgfigvnga gktttiksil glinpeagsi
       61 rfdgmemnrq ekqiknrigf vldegyfygm ltvkemknvi apaysswdeq tfsnwigrfg
      121 lnpnqkiasl stgmrmkfav alalshhadl limdeptsgl dpmmrselma illdfmkeeg
      181 ksvffsthit sdldkvadml ilidggkill neekdtlldn harikgdsrw inertrplfl
      241 tlretpygfe glthqkealr qempdavfer ptiedimlay vggaeiah
//
LOCUS       WP_010632721             451 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Sporolactobacillus vineae].
ACCESSION   WP_010632721
VERSION     WP_010632721.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..451
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49372
     Region          4..446
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 magtklerrl knrhiqliai ggaigtglfl gsgksihlag psilfaylii gvalffvmra
       61 lgqlllsnld hlsfidfade yigpwagfit gwtywfcwim tamaditavg kyiqfwfqip
      121 qwipallclv vltilnlltv rmygeiefwf alikvitiva lilvgivmii vgfktdtgrv
      181 siqnlwaygg lfpnglsgff lgfqmavfsf vgielvgvts aetadpektl prainslpvr
      241 vllfyvgalf vilcinpwtq lsadsspfvk vftligipaa agvinfvvlt saasacnsgl
      301 fstsrmlfsl gkkgdapksf silgrssvps lglitstial svgvvlnyfl pdfvftlvts
      361 isaicfiwvw siiliahliy lkkrpdlavs skfkapfapv mnwlillffa fllvligwaq
      421 dtrvalfvtp vwfillaaay ayrknrgvis d
//
LOCUS       WP_010632723             457 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Sporolactobacillus vineae].
ACCESSION   WP_010632723
VERSION     WP_010632723.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..457
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49949
     Region          5..449
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mmgqateekq elrrglqprh imlmamagmi gtgifkgsgd tlniagpsvi iayllcglil
       61 fvvmvalael amaypglniq hlihkafgfr taiivgwlyw inwmivtvve ilaagsfley
      121 wfphtplwil sglcglfiig inlfqvkmyg efefwfagik iaaiicfiml gflillgiip
      181 thvqpiknlf gyggffphgl sgivqaflvv ifsyggseli gltvtetrdv ektlpkviks
      241 vvfrvalfyi lpitiicglm pwnsvsatqs spfvqvfeav glpgvpqlmn fvlltavlsa
      301 ansgiyattr tlysmaerge aprftrklts hgvpigglal tgsflvigvf laflvkdqii
      361 vqlmsipgft isivwiaica aelklrpays ktpffhmigf pyttiigiva lsaifisfvf
      421 npanrvgsit cfviiallvt asmlmknrkt sehaqek
//
LOCUS       WP_010632782             435 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar ABC transporter permease [Sporolactobacillus vineae].
ACCESSION   WP_010632782
VERSION     WP_010632782.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 435)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15767475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..435
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48941
     Region          11..>98
                     /region_name="DUF5683"
                     /note="Family of unknown function (DUF5683); pfam18935"
                     /db_xref="CDD:465918"
     Region          110..368
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mdnkinkkai rkagilsiip glgqfynkqp lkgiifmsin ilfiielltf gissiqnflt
       61 lgtvpirdns mfflvegtlq iiilfiylvv wilniidark tarvylldgs rksssitilk
      121 nvwqkgfpyi ltipayivml fvivfpvlvt lfmaftnydf fhtppahlid wtglsnffsl
      181 iflsayrstf isvlwwtlvw aivastlqii lgiltavivn qdfvkgkrff rtifllpwav
      241 pafitimsfs nifndsmgai niqvisliny llpfihipmi pwktnpfwtk talimiqtwl
      301 gfpfifvivt gvlqsipnel yeaakmdgan fwqrftkitl pmilfattpv mitqytgnfn
      361 nfniiylfna ggpgdvggga gttdiliswi ykltvgdspq fgmasavtii isiivvgvsl
      421 avfkkahtfd seemm
//
LOCUS       WP_010632808             226 aa            linear   BCT 01-JAN-2025
DEFINITION  FHA domain-containing protein [Sporolactobacillus vineae].
ACCESSION   WP_010632808
VERSION     WP_010632808.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..226
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=25199
     Region          150..225
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 msnnltliyl iigvalvanv iliiaimrrk nterpetavs lyqklqdset gqdedrsktt
       61 alsdvqaqqv ekarksmpip enreeektem lhpisnlspk ikgdiknagp edatmllskd
      121 esipplqkqa krtidyqigs ekeqyswtgs epvrigrdpd qcdlviandg yvgrvhaliy
      181 tksgkyylvd ldskngtyie srqvkgqeel aagqyfkigk telvvn
//
LOCUS       WP_010632893             233 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Sporolactobacillus vineae].
ACCESSION   WP_010632893
VERSION     WP_010632893.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Sporolactobacillus vineae"
                     /db_xref="taxon:444463"
     Protein         1..233
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26808
     Region          <32..232
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 msmqksives rtsynvnise eyedihsflq gkryylfmkr lidifgslvg iiflspvell
       61 ialaikienp kgkvifkqrr vgkdgkpfyi ykyrsmvsna eklldnlidq ndttgpmfkm
      121 kndprvtkvg qflrkrslde lpqlfnvlkg dmslvgprpp lprevinysd ydkqrllvip
      181 gctglwqvsg rstvgfdqmv aldlqyikrr sivydlfiil ktitlffgsr naf
//
LOCUS       WP_010632997             393 aa            linear   BCT 01-JAN-2025
DEFINITION  S8 family peptidase [Aeromonas dhakensis].
ACCESSION   WP_010632997
VERSION     WP_010632997.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..393
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40262
     Region          113..346
                     /region_name="Peptidases_S8_Subtilisin_subset"
                     /note="Peptidase S8 family domain in Subtilisin proteins;
                     cd07477"
                     /db_xref="CDD:173803"
     Site            order(119,153,199,224,253,314)
                     /site_type="active"
                     /db_xref="CDD:173803"
     Site            order(119,153,314)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173803"
ORIGIN      
        1 mkriwlgllv agvlgqgama aersrylvql kpgaeaavla qsrgmggela lalkeqnala
       61 lwlpsaaata lahnpnvlwv epdakryvsa etlpygipmv qapqlsdaaa gevlvciids
      121 gysgghpdlp hgpqvqgydd agtgnwdsde nshgthvagt iaavggndlg vlgvlpnqsv
      181 plqivkvfga ngwayssnlv galnackqgm ssrgftrmvi nmslggsvps kteerafnqa
      241 ysqnvlsvaa agnagntsks ypasyssvvs vaaidankql ayfsqrndqv elaapgvsvl
      301 stvptgyayy sgtsmatphv vgvaalvwsq rlecsndqlr qtlrssaqdl galgrdnsfg
      361 yglvqakaaa dklalgcgsg tggggsskpg grk
//
LOCUS       WP_010633179             213 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Aeromonas dhakensis].
ACCESSION   WP_010633179
VERSION     WP_010633179.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22826
     Region          38..178
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mshqtdeetr srgrpvtpea dlrgalaeat ltlllkggyg attvdavakq agvakktlyr
       61 faanrdelva qavrswtdaf qpvfeqdath pgalgemleq glqaiadqvl saqavgmfrl
      121 lqheftgrda llaayqengi trgratlaaw lqrqqqlgwl reldsaqtsd lllamtmaep
      181 lrqmalglla pgsdiharit aavalvlpal vrg
//
LOCUS       WP_010633026             352 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Aeromonas].
ACCESSION   WP_010633026
VERSION     WP_010633026.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..352
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38361
     Region          29..351
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mpntqaphpg ardhgrqlgv ddgqskapil evrdlevefa vddgkikvld gvsfqvapgq
       61 tlgvvgesgc gksvtslaim gllpkphgqv vagsirfqge dllalspdqm ykvrgnrism
      121 ifqepmtaln pvqtvgdqlm evfrlhrpdy nkaqrreaai amlqkvgipe paqrfavyph
      181 nlsggmrqrv miamalacep allicdeptt aldvtiqaqi lelmkelqaq tgmaiifith
      241 dlgvvaelcd evvvmyagra veqadvfelf dhprhpythg lmssiprled epksllktik
      301 gqvpalhemp agcrfsnrcp hateicvsai pateqlaerh gvachhwrel av
//
LOCUS       WP_010633193             829 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [Aeromonas].
ACCESSION   WP_010633193
VERSION     WP_010633193.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..829
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91074
     Region          2..829
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mlkwlvrlfi vmmlgavlgv asligiyfyi kpqlpdvtal rdvklatpmk vysrdgelis
       61 qfgeirripl hldeipqsmi davlatedar fyehpgidpi gilraatvwa vsgqarqgas
      121 titqqvarnf flsnektlvr kikevflawr ieqnlskdei lqlylnkipl gyrafgvgaa
      181 aqvyfgkevk eltldeiaii aglpkapsml npirsperaf arrnvvlgrm letgkitqaq
      241 ydeaskmpik aryhgaettl napylgemvr qkmveqfged aytmglhvyt tvtakrqraa
      301 rqalldgvfd ydtrhgykgv taqlwksgea dwdydkimah lakqptyqpl maavvtklgd
      361 ksativlkng kqaelgwngi kwarsfitdd rqsfapksar dvlkvgaqiw vrekgeelll
      421 sqipevnaal vamnpqdgai ealvggfsfe lskfnrvdqa rrqigsnikp flyataleqg
      481 ytlaslinda pinqwdpskg pmwqpknspa iydgptplrl glaksknvms vrlmraigld
      541 tyidgltrfg fardtispne slalgaaeft plevvrgysv langgfqvtp yfitevtdsf
      601 gaplyqanpa aacrdcgvla aagldsaday antapdwkaq cpidpvvpnn mapqtisaqs
      661 aflvtdtltt aiwggngwrg tgwraardlk rhdisgktgt tnesrdawfs gytpnlvats
      721 wigfdnhqrg lgraefggga aqpiwidfmk talkqiperk mpvpegiitv ridretgllt
      781 nrtdgsstde ffkegteptr fatqssdgnq vyggdgsdtd gpvstddif
//
LOCUS       WP_010633300             412 aa            linear   BCT 01-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Aeromonas dhakensis].
ACCESSION   WP_010633300
VERSION     WP_010633300.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..412
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42582
     Region          3..410
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mfslvkqsva glqilfvafg amvlvplltg lnpsmallga gvgtllfqlc trrqvpiflg
       61 ssfafiapii yatqtwglps tmfglfaagf myfilaalir argmgfvhkl lppvvigpvi
      121 mviglsvaqv acnmamgrag geqvmpasta ltlagislav tliaavfckg wiklipilcg
      181 viagyvsavl mgqvsfdgmv napwlalphf vtpeinwaaa lfmlpvaiap ciehiggvla
      241 iggvtgkdyt knpglhrtla gdgigvcfag figgppvtty aevtgavmit rnfnpvtmtw
      301 aavfaiilaf fgkfnallts ipmpvmggim lllfgsiaai glktlveskv dlglsrniai
      361 vavtltvgvg alemkigdfa lagvglasva aimlnlilpq hseegamesa kd
//
LOCUS       WP_010633309             393 aa            linear   BCT 01-JAN-2025
DEFINITION  M28 family metallopeptidase [Aeromonas dhakensis].
ACCESSION   WP_010633309
VERSION     WP_010633309.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..393
                     /product="M28 family metallopeptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42112
     Region          106..390
                     /region_name="M28_AAP"
                     /note="M28 Zn-peptidase Aeromonas (Vibrio) proteolytica
                     aminopeptidase; cd03879"
                     /db_xref="CDD:349875"
     Site            order(200,220,254..255,282..283,326,328,330,347,351,354,
                     359)
                     /site_type="active"
                     /db_xref="CDD:349875"
ORIGIN      
        1 mkplltalll pllplavqaa epvwitvgad sgvelkqvka klaplfsasg apiqlaqvea
       61 selgtlshlm heghqrcggy vvhstladal qsmaqpisqn lfsapsltqg asvnrllpyl
      121 dqgnivgtis qlaswrnryy ttttgvqsad wvagqwqtls aalpwasvsr vkhsgypqqs
      181 vvltlkgsry pdevvvlggh ldstagsapn srtlapgadd dasgiatlte vlrviaeqgr
      241 qpertlqfig yaaeevglrg skdiatryka antkvlaalq ldmtnyqgsa edivfmtdyt
      301 dqgltgylaq lldaylpqir ygydscgygc sdhaswhnqg ypaampfesr fndynpniht
      361 ardtlqnsdp saahalkfaq latsfaiemg kin
//
LOCUS       WP_010633498             464 aa            linear   BCT 01-JAN-2025
DEFINITION  alkaline phosphatase [Aeromonas dhakensis].
ACCESSION   WP_010633498
VERSION     WP_010633498.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..464
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48240
     Region          5..464
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mksamkqklh ktlistalla alggaaqaqa sdaknvilfi gdgmgptvlt atrlykvgee
       61 gnleimklar sariktfsnd aqttdsapsm aayttgvkmn neviamssdt kavapskdvn
      121 gnkginncts dngkpvptil elakaagksv gavtttelth atpaatyshi chrdaayaia
      181 eqavpggagf ntalgdgvdv lmggganhwt pynstsnkgg radgrdltae ltaqgyhyvt
      241 tkdelsgvns gkvlglfsak shldyeldrv akgaastqps lsemtakaid llsqnsqgyf
      301 lmveggridh alhgtnakrs ltdavaldea vktalgkvdl kdtlivvtad hdhtmtingy
      361 sakgnkvldl vkngdgstqn dvdgkpfttl vfgngpnrad vrptltsdqv maddylqetg
      421 vklgsethgg gdvmlfadga gssrfkgtld ntkvfsklke algl
//
LOCUS       WP_010633534             185 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TMEM165/GDT1 family protein [Aeromonas].
ACCESSION   WP_010633534
VERSION     WP_010633534.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..185
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19781
     Region          1..185
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 mealltstls vaiaeigdkt qllalllicr frkpwpiiag mlaatllnha gaawlgefis
       61 rwldpkvmty lvagafiama awilvpdkmd deespldkyg pfmatfvlff iaeigdktqi
      121 atvllaakyd sltqvitgtt lgmmlanvpv vllgklgadr lplkgiriac ailfvglgvs
      181 tllfa
//
LOCUS       WP_010633563             431 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Aeromonas dhakensis].
ACCESSION   WP_010633563
VERSION     WP_010633563.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..431
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47637
     Region          1..431
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mrfesfdfap eilraisecg yqemtpvqsq aipavrrgrd llasaqtgtg ktaafalpil
       61 qrlvdnpapv qpsnarvlil tptrelaaqv asnindfaky ldittltivg ggkqdvqakr
      121 lkagahiiva tpgrllehlt acnlslsgve tlvldeadri ldmgfsadvq kilqavnktr
      181 qnllfsatfs eavkklanlm ldkpqvvavn kqnstadtvs htvypveqkr krellselig
      241 kqnwqqvlvf astrescdel veelnldgik savvhgdkaq gsrrralref tegklrvlva
      301 tevaargldi pnleyvvnyd lpflaedyvh rigrtgragk sgmaisfvsr eeertlleie
      361 aligqkirri mvpgyevssr delikqlqer rrfgkrpqre dnaaaqamae aklqgqrlkr
      421 laaakkprqp k
//
LOCUS       WP_010633620             373 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Aeromonas dhakensis].
ACCESSION   WP_010633620
VERSION     WP_010633620.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..373
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40001
     Region          5..347
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,234,301,321,323..325)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,182,185,187,234,241,301,321,
                     323..324)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,182,185,187,324)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            187
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mhhdhlfcpl rlgqlhlnnr ivmppmtrsr asqpgdvana mmatyyaqra gagliisegt
       61 qidpmgkgya wtpgihsaeq vagwklvtda vhakggtmfa qlwhvgrvth pdnlggaqpi
      121 sssaiqakgv kvfvdngsda pgfvetvtpr amtqadidav vgqfrqaarn amlagfdgie
      181 lhaangylin qfldsesntr tdgyggslen rlrflkevte avcseigadr vgvrlapltt
      241 lngtvdanpq etylaaarll grldvvylhv aeadwddapl maesfkqglr dafpntliya
      301 gkydgerara aleagwadmi gfgrpfvanp dlperlrhgy plaphdpatl fgggekgltd
      361 yptyqaaaqp hsa
//
LOCUS       WP_010633667             539 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Aeromonas dhakensis].
ACCESSION   WP_010633667
VERSION     WP_010633667.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..539
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58854
     Region          9..538
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mniarrlqli allvmlaltf lswfsinrls aadtdlgyvt dntvpsisli kqvqadfyal
       61 haliqthvln tdnskmnqie tgiadlrtei rsllqkyqae mlsneedrql ttddqriieq
      121 yyqeiekvli lsrdnkntea rdfiasnvmp lfeqfskaid khvkfnidlg aavklqgekn
      181 ydnslqtmlf isggtgiltl vlfiwlfrqv anplrlamat lsdiqhnlnf tlrakvaqqd
      241 eigltlsavn rlldtlqqtf tefsvgslqi kstaeslsqa ahhlassasq andatsliaa
      301 gveemtvsit disqrtqeas ritnesgkla sdggttidrt vkaineiaea irqassevsa
      361 lgdgisrigg vvnvisdvag qtnllalnaa ieaarageqg rgfavvadev rklaertaqs
      421 treisetvea iqqgsqltvt kmvqveekva qgvamatesg eiitqirhas hrvmdqvgei
      481 tiaireqssa aesiahqveq iaqvvqqtss taeetsaaae elnvttenih qqisryriq
//
LOCUS       WP_010633690             935 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein [Aeromonas
            dhakensis].
ACCESSION   WP_010633690
VERSION     WP_010633690.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..935
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..935
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=100386
     Region          1..515
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          459..933
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrwnqfdaav lsripperlv sdpdlrlahg tdasfyrlvp erivrldsld evrfvlavcr
       61 elglpctfra agtslsgqal sdsvlitltd swrghrilde garialqpgv igadanryla
      121 plgrkigpdp asinacklgg iaannasgmc cgtahnsyht lhamtlllad gtvldsgnph
      181 sraafaakrp dllsglaalr aevlanadla anirhkyrlk nttgyainal ldhedpidil
      241 thlmigsegt lgfiaevvld tvpeyphkas allvfrdaeq aclatsrlks apvaavelmd
      301 grslrsvagk pglpdfiktl dltacallie vhgeskeelv drceqvtama aefaqvasvp
      361 fttdsaglwa irkglfpavg avrttgttvi iedvafpier laegvaglqa lfdrfeygea
      421 iifghalegn lhfvftqgfd dpaqvaryga fmdavaelva vrfggslkae hgtgrnmapy
      481 velewgpegm almrrikall dpggllnpgv iinddpkahl tylkpmpasd aivdpciecg
      541 fceavcpsrt lslsprqriv lyrelarrnr adepsnqlar lfdyqgidtc aatglcadrc
      601 pvgintgsli kklradkyrr fvpiarwsad hfagvtrtar salglkgiag kllgekalag
      661 lvngvrhlsg qrtpawlptl pgpsryqwpq gegshggsse diggdravvy lpscasrvfg
      721 qqedapslpd vvlsllrkag crvivparve glccgmpyds kgmsevaeak rtelaealwq
      781 aseqgrwpvl ldtspcvqrl lsgalgkglr vfepsafvle hlrphleltp idetvmlhit
      841 cssrrmglge amlsvaraca revivpehiq ccgfagdkgl mtpelnaaal aslpaqvpsd
      901 crqgfsnsrt cemglsqhag ihyhsilylv dqaar
//
LOCUS       WP_010633769             249 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Aeromonas dhakensis].
ACCESSION   WP_010633769
VERSION     WP_010633769.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26748
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkllvavkrv ldynvkvrvk sdgsdvelan vkmginpfce iaveegvrlr eagvaselvv
       61 vtfgpeaaae qlrhalalga drarhyvtge tltpltvara lqqvceqekp dlvllgkqsi
      121 dsdnnqvgqm laalndwpla tfasaiklve relqvtreid ggletlgmal pavvtvdlrl
      181 neprfaslpn imkakrkple sapfadlgve pagqtrllgv maptarsagi mvssvdelld
      241 klkheakvl
//
LOCUS       WP_010633770             311 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Aeromonas dhakensis].
ACCESSION   WP_010633770
VERSION     WP_010633770.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..311
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32109
     Region          2..311
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 msvliiaehh qgqladnvar lvtaggqlgg evhllllgqg lteageqaaa lqgvdrvlla
       61 ehpmlaegls dgvdpllahi ardyqhclma astqgkdllp rvaarlgvem fsevtgiesg
      121 dtflrpiyag navarvassa pikvltirpt afakaasggq aevaeverlp vsevtcrtrl
      181 ierravrsar pelaaarvvv sggralgska qfaliealad klggavgasr aavdagfvan
      241 dlqvgqtgkv vapelyiavg isgaiqhlag mkeskvivai nkdseapifq vadyglvgdl
      301 ftllpeltak l
//
LOCUS       WP_010633778             264 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Aeromonas dhakensis].
ACCESSION   WP_010633778
VERSION     WP_010633778.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..264
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27885
     Region          184..262
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mdacsprptl pandpdaarl vclaiaialh laafwwlyah qpapitpplp ltlsarwvge
       61 aatndapaka apapappatt aqqiqkvqqk arplpphkkp plkpvkksvk pvvkqlkhrt
      121 ppvqpakvmp vsspqppvsa papattattt qanggstsqs pahnagggag nsasiardar
      181 lnnpepqypy esrrrgeegr vilnvrvtae gtaasvevdk ssgyrrldmt arktvsrwkf
      241 ipakqnnvav easakvtiif klra
//
LOCUS       WP_010633836             211 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar transferase [Aeromonas].
ACCESSION   WP_010633836
VERSION     WP_010633836.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..211
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23604
     Region          <35..210
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mkhpipkatq vlkrimdlag aslgllltlp lwplimlair ldspgpvffr qlrigrshas
       61 htelffmikf rtmradaeag tgpvwcgkad sritrsgnfl rktrldelpq flnvlkgems
      121 ligprperpg ianrledavp ffiertyeia pgitglaqvn qgydeslddv rsklafdlay
      181 svtllhpwrw llqdmqiigk tvaimvgkkg r
//
LOCUS       WP_010633823             306 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Aeromonas dhakensis].
ACCESSION   WP_010633823
VERSION     WP_010633823.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34001
     Region          11..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..298
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(106,110,149,163,166,233,250,277)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(107..108,112..113,115..116,119,123,125..131,193,
                     227..231,238..239,242)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mpiepslvas ltwfahiarh rsftkaatem gvtraalsqh lkgleqqlqv rllnrttrdm
       61 slteegrrll dvlqpsltai ervvselnds hlepsgliri nssriaarll iephmgefla
      121 rhpklrlelv madgfsniia dgmdagirlg esldehvvav pitppltmai vgapgyfrqh
      181 gmpqtpsdli rhnclayrft ssntidrwsf tspdeeqhtq ivdpkgnavf ndddsmlqaa
      241 lqgvglvkhl dlrvrqhlsd gslvrvlapw cppfpgfyly vpsraqmpak iralmdflse
      301 kraqla
//
LOCUS       WP_010633865             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Aeromonas].
ACCESSION   WP_010633865
VERSION     WP_010633865.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 412)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..412
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45550
     Region          128..394
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mqslfssaql lslvlfvsls hvgvaaifay lwhtqrplra llywsasela iaaafgclll
       61 rpltgetsla nilltnllii atpllyergl rhffrreadr fgwlcpllal agfllfalva
      121 sqqpladvhs riitlsgvls lqiglllwql wryqrlapay rvlrfailll alqlalqllr
      181 makhqwwpes aassltdpll gpvillsllf tiarsfills lvhtrqqqam latqrelerr
      241 anqdaltgld srhhfeqqla aracrsarpw qlllidldnf kqindnhghp agdamlravg
      301 rvirkslppa alagrlggde lallvmetpq tlpgychalq qgvteatrpl aggpiglsig
      361 ltslqtgesf eqaylradqa lyaakqsgrm racireahhs eprllqaael hp
//
LOCUS       WP_010633898             294 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Aeromonas].
ACCESSION   WP_010633898
VERSION     WP_010633898.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..294
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31378
     Region          2..292
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mfsallnivi pvfavvglga lygrlrpgga lgyvnranie lftpalvfsa lvkypldlma
       61 hlsliaagal villpgllls llrlrsisrp alilpamfrn tgnlgiplmv lafgeqqlga
      121 iiilfvlsnl lhfsvgmfil santsrwlwl rspvlwaala gllvanlhip lpeylvtsas
      181 llgqisvplm lfalgirlme geldhlglal kcnllyllag gislglavwl lplqpawipl
      241 lmlsvalppa vlnymlceqy qcqpekvasi vlggnalsvl viplavwlal hlgs
//
LOCUS       WP_010633899             122 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Aeromonas dhakensis].
ACCESSION   WP_010633899
VERSION     WP_010633899.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..122
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13418
     Region          5..78
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mgniakqrhq aavrqyfhcf ycglpmweas paalmqqyrl tpaearllqc tgehlqprge
       61 ggsnqpaniv aacqhcnstr hktlkvlspe qyqkkvrarv gkggwfpngi tskvkgnktk
      121 gv
//
LOCUS       WP_010633983             259 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Aeromonas dhakensis].
ACCESSION   WP_010633983
VERSION     WP_010633983.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..259
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28510
     Region          3..256
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mllvdshchl drlsygskqt dmadvlakaa rqdvgyflcv svtqaqfptm leaiapypqv
       61 fascgvhpln qepgvdadll laqaadervv aigetgldyf yspenkevqq asfrehirva
      121 ralnkpliih trdaqqdtlq imreegaeqv ggvlhcftes lemaeaamam gfyisisgia
      181 tfknaaalqs vvkalplerl lvetdspylt pvphrgrene pafvrdvaqf iadlrqmpla
      241 elaqatsdnf felfklakr
//
LOCUS       WP_010634411             122 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Aeromonas].
ACCESSION   WP_010634411
VERSION     WP_010634411.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163535
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..122
                     /product="VOC family protein"
                     /calculated_mol_wt=13339
     Region          2..121
                     /region_name="GLOD5"
                     /note="Human glyoxalase domain-containing protein 5 and
                     similar proteins; cd07253"
                     /db_xref="CDD:319916"
     Site            order(2..9,26..27,42..46,61..72,77..78,81,90,97..100,109,
                     112..113,115,117,121)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319916"
ORIGIN      
        1 mishidhlvl tvsdierava fyssvlnmea itfgagrral rfgnqkinlq llgqeprnra
       61 qvgsgdlcli trwpleqvia qlhchgveiv egpvtksgac gpiesvycld pdqnlieisr
      121 yp
//
LOCUS       WP_010634431             551 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Aeromonas].
ACCESSION   WP_010634431
VERSION     WP_010634431.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..551
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=59411
     Region          12..551
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mntstmtigk kltagfamlg lmmafiggfs llqfgnmnra aigftdsilp avvrtstlge
       61 tintlrryel dvflvaadpq qkahyrdlge qtlqevarqv kahdatiwae dveerrtfdi
      121 vkqdwdkyva lhqrirqmqd ggqlaeaqql fmsegitlyt nlaksvgdli rinhgysvgs
      181 raqvvaafds aklsiivalv lglvlagals tvltrqirdp lvmlarqaqr iasgdlgkse
      241 lqewirgnrf krdelgqlga aidrmqgsla dlvseiagsv sqlssaveev saiseqsatg
      301 marqqsevsq vatamnemqs tvnevarntt damsaakdas rtstqgnqvv rsaissieev
      361 svkieqagav vqqleqdstn ismvldvirg iaeqtnllal naaieaarag eqgrgfavva
      421 devrslaqrt qnstaeiskm ievlqertae agsamqlsrq qmqesvglar eagnsidtin
      481 gavtqitdmn tliatateeq navteelnrs ivnihnaade nalgaqqtaq acvelsklan
      541 tlhhmtqrft l
//
LOCUS       WP_010634468             193 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Aeromonas
            dhakensis].
ACCESSION   WP_010634468
VERSION     WP_010634468.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..193
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21822
     Region          39..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mrvevkpdre yawfirpffw lqqrnygqvl ipgkcwgrsp rlfaavatly gvinrkrspi
       61 dpvlrslvtv rvsqlnwcrf cvdinamtlv kragssekve alanwrespl fderekavld
      121 yteamtgldg vsdeqaarlk pwfdddamve ltgliafqnm sakfnaaldi apqgfcqlpv
      181 qperpaqpns kda
//
LOCUS       WP_010634559             599 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF262 domain-containing protein [Aeromonas dhakensis].
ACCESSION   WP_010634559
VERSION     WP_010634559.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..599
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=67991
     Region          7..>457
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
     Region          432..586
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 miksvfnypv salldieagv vyaipryqre ytwgkwqwda lfedllendl syylgsiici
       61 nqstdtlavq qlelvdgqqr mttlslllaa iyasfqrpgi elameqqiel ynlkhklvlk
      121 knaeqprlvp qvqnanqqdy lavlkeagil keaellanag nrrvfkayrh fmmrieeyva
      181 gtadalqals alldkvnaat lvkievashs daytlfesln nrgvpltaid lmknkllakl
      241 eqvepgsidk sfvswtkvle algddygvqe rffrqyynaf kpelkdiisv pvatksnliq
      301 ifekliahdp qkflqamrsh sawyaqivgh vavagepklt rqlqsldriq gapsyllllm
      361 lfakqealai sssqieqvvr llinffvrrn ttdvpatrdl nrifmelteq llssqgervv
      421 sdiastlsrv sttdehfrqa lsgnlyednt wvcrfilcai eesmmtkenq vdlwavegkq
      481 fvwtiehvfp qganipepwv amiadgdktl aeqyrqshah rlgnltisgy nstlgnksfl
      541 dkrdrmtrdk rpvgynngly lnqelaeaes wsvaqierrt aemvdkaltm fslpemark
//
LOCUS       WP_010634650            1020 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Aeromonas dhakensis].
ACCESSION   WP_010634650
VERSION     WP_010634650.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..1020
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=111530
     Region          1..1010
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnlaktaier piwvavsivl ifllgllsir glpiqlfpdi drphlnisvd wrsaspqeme
       61 seitdpieqe mqgvqglknl tsnsfpgfte idlefalgtd mqraqldvis rlnrvsglpd
      121 kiggpyvnny ssndtltfff iqqlpgakgp iddhqaliea rikpelerip gvstvdiqgi
      181 nerqiqirfd pyraaelgve ipvlasrass gwdvsagtld igrweyklrf agrydvatlg
      241 dkvvdwrdgl piylrdvaei qlareenpvl riqngntaia aqifkesgan alaaleaikl
      301 kvgelnrevl epvglhmeqs fdaslyinra vsmvtanlgl gvllscailw vflrrlkatl
      361 miaiaipisi mltfcllkvl grtlnvisla giafavgmvl daaivvlesi yrrhergdls
      421 kgeaalegts rvwtalvast lttvaiflpv lllndvegql fadlaltiac avtvsmlvav
      481 tvlpavaarw mgrerlidpy eglwqgttrh virwtatprr rwtvitlmms lpalatwall
      541 pkmdylpdvk rdavdvwmnf tpgfnlkaqr eevidtliar ldpymkgeqe palknyyilr
      601 ypggaqigvr pkeenqikvl eqllmkqllv gipdtqvfgg qgslfggfds engislllqg
      661 gdlaelyraa raamaivkqd lpgaqvrpqp dldftapelr lvpqdrrlae vgwdrtpmpa
      721 iiqtfgdglr vgeyfdgeer ldimlmgqts anpdelkavp latpsgrivp lgellrvehd
      781 mgpasifrad grrsislqis ppagmsmeqv ldtlqsksfa airpllpagg elrvsgnads
      841 lqqalgnlga iflfavmill illwgvfasl kdavlvlltl platvggvla lylsgllvpl
      901 pmdlltiigf villglvvnn aillvhqtrt aeregmsrql avadalqsrm rpiamtslts
      961 ifgmlplmls psegseiyrg latvivggms cstlftlvll paflrlgerv dvpqairqra
//
LOCUS       WP_010634689             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: lytic transglycosylase domain-containing protein
            [Aeromonas].
ACCESSION   WP_010634689
VERSION     WP_010634689.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..249
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=26459
     Region          <118..241
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mlmgliplfs apgwsqtpap aevviltaep papppatapv tlhtpgvlpp pepaspplpp
       61 gtrqiqvyks vqkngvvrys dmmpeqghye lllfndcyac dpdskvnwht tglflydyas
      121 tiqaaakayq vepalirali haesafnpla vsrkgamglt qlmpatarel gvgnallaeq
      181 nifggvkyla gllkqyggnv alataaynag agavqkhggi ppyaetrayv ervqllrqry
      241 kdmlsakgl
//
LOCUS       WP_010634752             353 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Aeromonas dhakensis].
ACCESSION   WP_010634752
VERSION     WP_010634752.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..353
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39304
     Region          10..193
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(13,15,99)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(46,98..99)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            97..99
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mshadfrlsl ivpvyneees idafinaidn elaplkdqle ivfvndgsrd rtrevveqai
       61 ardprvtlvn larnfgkeaa mtaglhhakg davvpmdvdl qdppslilef vklwqtgdyd
      121 tvygirvdrs adtpmkrlta ggfyrffnal ststklpena gdfrlidrkv veaikqlper
      181 nrfmkglfaw agfravgvpy erparhaget kfnywklwnf aldglmsfss wplrvwsyvg
      241 vgvsfvafly ilkivtqvvf fgidvpgyas lmsvvlflgg iqllslgiig eyigrmfvev
      301 kqrpvylieg vygqyakqde epkqdaatgs kksagkkaaa akaaddqqeq asq
//
LOCUS       WP_010634720             337 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Aeromonas dhakensis].
ACCESSION   WP_010634720
VERSION     WP_010634720.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..337
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36513
     Region          140..334
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtgslkriga lfyarnlefv rdraaliwnl afplllvlgf tlifsgppkp lvqmgvvgel
       61 pvayaplrav pllkiipyde eekgrlkvrh hqldlllspg tgrywinpda pqgamaeyll
      121 rqavpvqlvr etlsgrairy gdwllpgvig mnlmfsglfg vgfvivryrk ngglkrlgat
      181 plsaaeflca qllsrilitl vvsllvflva yfllgvpllg sgwllllial lggasmaslg
      241 llvaariqne elasgllnvi smpmmflsgv wfslegapaw lqqlaawlpl sqiiaaarav
      301 mlegagwaev aaplgfvllf tlccitlgsa lfkwshr
//
LOCUS       WP_010634766             573 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Aeromonas dhakensis].
ACCESSION   WP_010634766
VERSION     WP_010634766.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..573
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62821
     Region          7..489
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mttlmsthsl qmsaghlplf dhlelgirag drlgligang cgkstllall agertsqagr
       61 vvqaaacrce fvaqqlptrl stlstravll dalgndpsae wqvdkllael qleaqatlpv
      121 salsggqhsr lqigrallrq pnlllldeps nhldlpallw leqfllgwrg afvlvshdar
      181 lldsvtdqtl ilrdgqlhrf alpcsqaraa laaedeqarl rradeqkeid rlsasskrla
      241 iwgrehdnek lvrqaksmek riarlqeeqs qvaalapwrf elrglsmpad tllrlealdv
      301 spapdlppll raeglwlrag drvallgang tgkssllrqc wrelaaqspq agwychpgas
      361 iayydqslqq laddatlsda lyplaplpeg alrqalirag fpyarhgqqv htlsggerar
      421 llflalslgn hhmlwldept nhldlvgked laeaiatfpg gvllvshdre lierscnrfw
      481 likdgriqea hsaerayael lgdaplpaad kapamgqapa gpvddeeall arwyeldall
      541 aadlarkprh qtprlqqqwr delarladll gfa
//
LOCUS       WP_010634851             266 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Aeromonas].
ACCESSION   WP_010634851
VERSION     WP_010634851.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..266
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28576
     Region          1..251
                     /region_name="trans_reg_YgbI"
                     /note="DNA-binding transcriptional repressor YgbI;
                     NF040890"
                     /db_xref="CDD:468826"
ORIGIN      
        1 mipverqqqi lhllaergav sitelterlq vshmtirrdi qkleeqgrvl svsggvslse
       61 riksepshat krslmqeakl aiahsaaaqv aagssvylda gttslelare lapredlmiv
      121 tndfmvcayl iehgrgrlyh tggqvirenq scageatahf lrnlhldvaf lsasswdalg
      181 istpseqkvp vkravveaaa trilicdssk ygkvgtfnvv gweaidqvis dgqlpesare
      241 vlaqhgvrlt lvplggaahd stelag
//
LOCUS       WP_010634868             159 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase [Aeromonas
            dhakensis].
ACCESSION   WP_010634868
VERSION     WP_010634868.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..159
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17352
     Region          1..156
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mirydflpsr cgdllvaide rglvhvdfva glralpdmrd wqqdktalap flaqfeayfa
       61 grlqrftlpl aprgtafqqa vwqalcdipy getrsygdia raigkpnavr avgaangrnp
      121 lsiiipchrv igqngsltgy aggleikkal lqleniser
//
LOCUS       WP_010634963             299 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Aeromonas dhakensis].
ACCESSION   WP_010634963
VERSION     WP_010634963.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32710
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..283
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,222,239,266)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdiahlasfy evvqrgsfsa aadalgvskg mlsrhvsale sslnaqllqr ttrrlsltea
       61 gstlyqqage ifalarqaeq diqalteedg grlrftcpis agdrmvsell arfaelcpgv
      121 avelnftnqm vdmsqgehdi alramsevpd nlvamplgrl rdvvvaspal varegkpatp
      181 yelsgracll mgsnpaweqw hfsregeeah ilvqgkvran hystalqlar agmgyakcpl
      241 vavdallaag elvtvldgwh sglhplhilh aqqrrvprki rlfkqvlaqw fverphyll
//
LOCUS       WP_010634930             191 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Aeromonas dhakensis].
ACCESSION   WP_010634930
VERSION     WP_010634930.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..191
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=21391
     Region          18..188
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtslpsappl aatlaamgla paigeplagr lprltlqpgq pllaqgamqe safyiergia
       61 rachyardgq erckefyfeg elcllydswl tgsparyqle avtalqlvrv plalldeptw
      121 qpvcmallrq qlcykerkea flllhspeer yrelcrtfph wparltqvql anyigispvt
      181 lsrirrrint g
//
LOCUS       WP_010635010             147 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Aeromonas dhakensis].
ACCESSION   WP_010635010
VERSION     WP_010635010.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..147
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16012
     Region          1..147
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslkdqlkdq qklamlakdk qrlgairllm aeikqrevdt rvelddqdil avvtkmvkqr
       61 rdsisqfeaa grqdladkes aeivvlqefl pqqltaaeia alieqaiaes gaavmadmgk
      121 vmavlkpkiq gradvgtvsa qvktrla
//
LOCUS       WP_010635077             415 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Aeromonas dhakensis].
ACCESSION   WP_010635077
VERSION     WP_010635077.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..415
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45013
     Region          5..415
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msiasfadla lsprlqqtlt elgyvaptpv qasaipvila grdlmagaqt gtgktaafvl
       61 plleqllqhp tsdaprpira lvlvptrela vqvhesvtry akgtdltstl vyggvsiaaq
      121 vealkagvdl liatpgrlld hlrqgalsla alrhlvfdea drmldmgfmd eikallkqip
      181 adrqtllfsa tcddnlfals kvllrdpali evaprnttaa eveqrvytvd gdrklalveh
      241 mlkvkgwapa lifsrtrqga dklaqqlgkt ginalafhgd lsqgarekvl lefragtlqa
      301 lvatdvaarg lditdlnyvi nmefpfvaed yvhrigrtgr agnkglaitl fspedaplle
      361 kveavldtrl pqqwfpgfep dltrfdpepr rsskaaqkqr arkqalagnk skarr
//
LOCUS       WP_010635088             188 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Aeromonas].
ACCESSION   WP_010635088
VERSION     WP_010635088.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20191
     Region          1..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrsaefnrdd vlrnameafr akgyakttmq elvaatglhp gslyaafgnk rglllaavdh
       61 yvqeksalrr sffaaaspla gvqayleqvv ndalcgtclv trtlmelaeq deelhlklka
      121 iygeldadla avltlalerg elaagrdipt ltaflliniq glvtfaqcrp dpvllggvvt
      181 qlmtalra
//
LOCUS       WP_010635157             164 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase [Aeromonas
            dhakensis].
ACCESSION   WP_010635157
VERSION     WP_010635157.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..164
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17978
     Region          1..157
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mqysfcdsah gplliaidrd glryvefvrg eqpvtptdqw qrddlalapf veqfaayfag
       61 rlrrfdlpla argtpfqqsv wralgdipyg etvsyleiaq aignpkavra vgaangrnpl
      121 siivpchrvi grsgeltgya gglpikrwll aleqqsadhf vltp
//
LOCUS       WP_010635182             239 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Aeromonas dhakensis].
ACCESSION   WP_010635182
VERSION     WP_010635182.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..239
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25638
     Region          19..239
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mpsatlsssv gaestralww rasidilpls isvipwgilc galalqvgls plqaqlmsll
       61 vyagaaqlsa ttlfgagtpl lpimgstfvi tsqhllygft frrdvlplsl rwraslaffl
      121 tdemfavalk drersgrfdp ayaliagfvf ylfwnvatll giaagqyidg ldqmgldfai
      181 aatfiamtip amknlpmvaa tlvsgamall tkpllaevyi iisalsgmlv gyvlhrmrr
//
LOCUS       WP_010635248             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA-J related domain-containing protein [Aeromonas].
ACCESSION   WP_010635248
VERSION     WP_010635248.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Hahn,Y., Lee,J., Seong,C., Yoon,J. and Chung,J.H.
  TITLE     Structural analysis of phylogenetically conserved J domain protein
            gene
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 325-333 (1999)
   PUBMED   10542335
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Cheetham,M.E. and Caplan,A.J.
  TITLE     Structure, function and evolution of DnaJ: conservation and
            adaptation of chaperone function
  JOURNAL   Cell Stress Chaperones 3 (1), 28-36 (1998)
   PUBMED   9585179
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10574576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..193
                     /product="DNA-J related domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=22142
     Region          20..131
                     /region_name="DNAJ_related"
                     /note="DNA-J related protein; pfam12339"
                     /db_xref="CDD:432489"
     Region          148..190
                     /region_name="DnaJ"
                     /note="DnaJ molecular chaperone homology domain;
                     smart00271"
                     /db_xref="CDD:197617"
     Site            order(169..171,176,179..180,183..184)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mnsaestanp llapllallr qasgsykvhe llaelrrqel ipplpgdeqq qlfrlnflim
       61 nalyqlqael hdegwwllis tldirlepla prntasalaq gealrsyyld wqvfwqtdre
      121 eveallgsfw racerdehra ealtlfalpt gagpdairrr wrelalqhhp drggdadtfi
      181 rlrwawehlk tak
//
LOCUS       WP_010635309             217 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Aeromonas dhakensis].
ACCESSION   WP_010635309
VERSION     WP_010635309.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..217
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23594
     Region          6..216
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 midlhpadar haviwlhglg dsgaglaplv dalalpadlp vrhllpdape rpitinmgyk
       61 mrgwydirsf edpadraves hvresaaria alieqlvaeg faperivlag fsqggviasf
      121 talrlplrla gllcmstyla apdallgems easrslpicy mhgiyddvvs lsmgwdaknr
      181 leaaglspew heypmrheic rpqlgdirsw llarlag
//
LOCUS       WP_010635396             417 aa            linear   BCT 01-JAN-2025
DEFINITION  phospholipase D family protein [Aeromonas dhakensis].
ACCESSION   WP_010635396
VERSION     WP_010635396.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..417
                     /product="phospholipase D family protein"
                     /calculated_mol_wt=47528
     Region          5..411
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
     Region          9..172
                     /region_name="PLDc_ymdC_like_1"
                     /note="Putative catalytic domain, repeat 1, of Escherichia
                     coli uncharacterized protein ymdC and similar proteins;
                     cd09111"
                     /db_xref="CDD:197210"
     Site            order(118,120,133,135,151)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197210"
     Site            118
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:197210"
ORIGIN      
        1 mipaefalid qpelalklrc qlirgarsri qaqyysweed ssgklllael lhaakrgvrv
       61 qlliddlyag dnrflemvah qpgievrlfn pfwlrgwrpl tlllegllsf rrinhrmhnk
      121 lllvdgsqav iggrnigdry fglggapqfv dldlacrgpl cqrveqgfdq fwrsrwshpi
      181 rrllrrplqr aevqvvndfl ltlnepqiaa vydlpaslfd pepiplcwha graevwfdrp
      241 gkglvsrptt arllwrklad nqgtlrlvtp yliltrglrr rlrqqrqagv tidiltnsla
      301 stdvplvyga yrrhrpwlir qgialseleg aslslhakli lvgeeeallg sfnldprsll
      361 lntelvlhla cpalcaelqq wlttwqqrss hsvaappstl rrllarvsdw lplqrwl
//
LOCUS       WP_010635449             362 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Aeromonas
            dhakensis].
ACCESSION   WP_010635449
VERSION     WP_010635449.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..362
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39778
     Region          <1..80
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 mylkqtilac llatlsqgaq adqlklkagy petyvvqkgd tlwdisgqyl aepwlwprlw
       61 ninpqianph wiypgdvlhl swvngeprlg katqggkqvi rlspksryen kanpiptlpl
      121 seigpflqtd hilansqqak qlpyvlgnde ahigmlegdt lyvqgslipg qdygiyhpga
      181 iykdrktgeq lgqeavfvgt araeallpdg rtrvtlshsk revyqgdklm pfppqeslsa
      241 vftpkaapvi spgyivdlps kargggkfdv vlinkgirdq vapgdvlevl rpgtrlvskn
      301 gkvayreyss vydkafysag kpplpseava rvmlfkvydk lsyglilqsq nmvgtgyqvs
      361 nf
//
LOCUS       WP_010635458             498 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase [Aeromonas
            dhakensis].
ACCESSION   WP_010635458
VERSION     WP_010635458.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..498
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53452
     Region          5..482
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(62,64,68,71,75,108,111..112,121..128,133,136,139,
                     232,236,239,242,244,418,420..421,423..424,427,430..431,
                     433,435..438,447,451,453,467,474..479,481..482)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(148..151,159,174,177,207,224..227,230,248..250,282,
                     383,385,411)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(151,248,279,282)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mtyrvsnfid gettesrser fgaifnpatg qqqgqvvlst aaecqdaias aeraladwaq
       61 tpplvrarvl frfkelmeqh rddlarlisr ehgkvfsdaq geltrglevv efacgiphll
      121 kgehslnvgr gvdshsmmqp vgvcagitpf nfpamvplwm fpvaiacgnt filkpsekdp
      181 slslrmaell kqaglpdgvl nvvngdkevv dvlltdprvg avsfvgstpi aqyiyatasa
      241 hgkrvqalgg aknhmvvmpd adldqavsal mgaaygaage rcmaisvavv vgddtadalv
      301 arlsplvaal rvgpglgqsp enemgplisr ehlakvrgyv dqgvaegael vvdgrglshg
      361 egyfigsslf drvspemriy reeifgpvla ivrapdyeta lklineheyg ngtaiftcdg
      421 dtardftarv qvgmvgvnvp ipvpmafhsf ggwkrsifgp lnmhgpdgvr fytrmktvta
      481 rwpqslraga efsmptmk
//
LOCUS       WP_010635468             294 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Aeromonas dhakensis].
ACCESSION   WP_010635468
VERSION     WP_010635468.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32617
     Region          1..>139
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..287
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,216..221,
                     227..228,230..231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdrltaieif vevaragsfa avaerfamtp amigkyikwl earvgsrlln rntrcqslte
       61 agqeylagcq sllqhyrele qntlantgqa agririnapv tfgsyrltpl lcrfmehypq
      121 irieldlsdr lvdvigdgfd lifrigqpkd agyiarplts tgsvfcaspd ylqrhgtplt
      181 ladlashhcl gfspwlgqsr laetfpleql hlwdspfisn hggalkvaal nhagillqpr
      241 allseelacg tlqeiladal paprpvnlly pareplplrl rllidylveq rhql
//
LOCUS       WP_010635479             297 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Aeromonas dhakensis].
ACCESSION   WP_010635479
VERSION     WP_010635479.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32907
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,218,
                     220..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnkitalnvf rrvvemgtfr aaaddlrlsq aavskninel eaylgialin rttrrlsvte
       61 agmtyyrqic avldgleaad qsimatsftp rgrlrigmpm syglirlnpl vcefqrrypa
      121 igievilnda ymdlvdqgld vvirgadtle dstlrakplc qvrrvlcaap dylkeagqpa
      181 hpedlkahnc lryslssspn kwcfsraees vtvdvrpasf canngialkq aavqglgvil
      241 vphefvasel adgtlvkllp dwqpdphalf avypfhkeqs pnvrlfiefl vkafqlr
//
LOCUS       WP_010635681             355 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Aeromonas dhakensis].
ACCESSION   WP_010635681
VERSION     WP_010635681.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..355
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40158
     Region          1..347
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mkylvvqtkq igdvlistal cnnlkqndps gevhylvmdy cagmaqgnpn idrliiieka
       61 rrnewrymkd lllairrery dvvvnsqgqm igllsclfsg arlrigfdsf pwrlghnriv
      121 rfrkdtefqg nstlvddrfs llkplklare drnyylwlse eekqqgrdtl laagvdlnrp
      181 liamgvnslg hykrwpidcf akvaqwlieq hnaqiliycg pgeeeynrgl kpllpatlqa
      241 svfdhiktrs vrelvglfah crlfvgndtg prhmaqaidl plltivapgg dkiianpvnh
      301 pryqaidvfd akgpgfqlpq ntekdfidea llraitpelv iarltalpdw qaatp
//
LOCUS       WP_010635686             312 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Aeromonas dhakensis].
ACCESSION   WP_010635686
VERSION     WP_010635686.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..312
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32884
     Region          16..312
                     /region_name="CeuB"
                     /note="ABC-type enterochelin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4606"
                     /db_xref="CDD:443656"
ORIGIN      
        1 mralllpatl lvlaacslli garplplael lagdglltlt asrlprlaav lltgaglava
       61 gvilqqivqn rfvepatsgg ldaaklgili altqlpaagt tgrmlvalaf cfaasllfiv
      121 ivrrirfknt vlipviglmy gsvlsaiaef yayqhnilqs iqgwmlgdfs kvvegnyeii
      181 ylilpitllt ylyahrftvl gmgeeaaasl glgysatatl glllvavtva atvitvgaip
      241 fvglvipnlv vlrhgqhlrk tlplvalyga llllacdlls rllihpfevp igltagslgg
      301 vlflllilwq rr
//
LOCUS       WP_010635697             806 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Aeromonas dhakensis].
ACCESSION   WP_010635697
VERSION     WP_010635697.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 806)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 806)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 806)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..806
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84464
     Region          11..71
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          75..795
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtthiklpih lqlpltgmsc ancasritta lnklegveat vnfaleqaai dlaspdrlpv
       61 vlesikaqgy dygsetilfq itgmtcagcs arlnkmlaal pgvisadvnf sleqarivlv
      121 pgmqtpaalr eqiealgfga qlaqgsasgr rqqllereaq eaasarqaqt rvivsalltl
      181 pllasmlama gllpwhlpaw lelvlatpvq fwigarfyrg awlaiknrsa nmdvlvatgt
      241 saayfyslyl lltlgmaasg qlyfeasaii itlislgkll eararrstqs airelmalrp
      301 etatvwrges wqsvaidevl rgdrlrvlvg ervpvdgkil sgeseldesi ltgeslpvpr
      361 gegdkvlgga inrsgvleie attvgedssl skiialvesa qmgkaplqql vdkvsavfvp
      421 vvmaialftl lvwytigndf gqallaavav lviacpcalg latpaaivtg tgvaarhgil
      481 ikdvdtlqka haikalifdk tgtltqgrpv laswsgndeq lrlaaalqqa sehplalamr
      541 eaagqdavlp qpeavevrvg agivgqvagh tvaignasll aqlgidvpqq deqaadgatr
      601 vwvaidgvva giaaladtlr pespeaiatl rqrgiaswlv sgdapapvah iaaklgldga
      661 fdsvlpagkv ekvealraqt rglvamvgdg vndapalaaa dvgiamgsgs dvametaait
      721 lmrsdprlva daidisaatw rtiqqnlfwa fvfniigipl aalgylspel agaamalssi
      781 tvlsnslllk rwqpralahv stesnr
//
LOCUS       WP_010635854             452 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Aeromonas].
ACCESSION   WP_010635854
VERSION     WP_010635854.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..452
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46064
     Region          14..447
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 makqdmaaqs gnggfldsyf sisargssvr qelvaglttf lamvysiivv pnmlgaagfe
       61 qgpvfvatcl iaafgsllmg lwaklpmaig caisltafta fslvlgqgls ipvalgaifl
      121 mgvlftlisv tgvrqwildn lpsgiahgtg igiglfllli atngvgmvik negaglpvql
      181 gevtafpvim tvlglaaifg lerrkvpggi lmviiaisil glifdpkvtw qgffampslt
      241 gekgslvgsm dllgalnpvv iptvlalvmt avfdatgtir avagqaglin erghiisggk
      301 altadsvssm vagavggapa avyiesaagt aaggktglta tlvgvlfllm iflsplsylv
      361 payatapalm yvgllmlgnv tkldfndsvd alsgmlcavf ivltcnivtg imlgfvalvi
      421 grlfaaewkk lnigtviiav alvvfyaggw ai
//
LOCUS       WP_010635871             258 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Aeromonas].
ACCESSION   WP_010635871
VERSION     WP_010635871.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..258
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28694
     Region          30..256
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mhdlkpgwpr wvlgalvatl llpllatfly sistrwgatl lpdgftldwy lklwgdprfl
       61 aafgrsllvc fatlllgtlv lvptvlvvay yfpkldpwmn llillpfavp pvvssvgllq
      121 iyadgvlpii gtpwiligtw ftvvlpfmyr alanslqgvp lkdlmdaahl lgassrrafl
      181 lvvipclrkg llaalflsls fllgefvfan mlvgtryetl qvylynmrst sghftsalvm
      241 syflltlllt waanrfhr
//
LOCUS       WP_010635874             348 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Aeromonas dhakensis].
ACCESSION   WP_010635874
VERSION     WP_010635874.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..348
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=37309
     Region          60..343
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 mksviasala lvaisqplfa aeniadleka argegqlssv gmpdswanwk dtwqqlgsiy
       61 gikhqdtdms saqeiakfaa ekgnatadig dvggafgpva vkqgvtqpyk pstwadipnw
      121 akdadghwml aytgtiafli nkdlvkaapt swqsllggdy kvtlgdvgva sqanngvlaa
      181 ayatggsekn lkpalelfgk laqqgrlsln dptianiekg evevgvlwdf nalnyrdqid
      241 pkkfdvvips dgsviagytt iinkwaknpn aaklareyil sdagqinlar gyarpirsnv
      301 tlpddvkakl lpaeqyanak pvedhaaweq sskalprqwq etvminmq
//
LOCUS       WP_010635917             383 aa            linear   BCT 01-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Aeromonas
            dhakensis].
ACCESSION   WP_010635917
VERSION     WP_010635917.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..383
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40281
     Region          3..382
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mpfalphlva gfiavmvgyt ssviliiqaa taagadaaql aswlwtlgig mgisciglsl
       61 yyripvltaw stpgaallit slgnftlaea vgafvissll itlcgisgwf drlmrhipaq
      121 laaamlagvl lkfgldlfkv apadplllgs lllafllgrh lwprytmvlv ltvgilicll
      181 rgelqldaih wqlarpvmvw pafsfdalfg ialplfivtm tsqnmpgiti lrahgyqpat
      241 sslitwtgla glllapfggy afnlaaitaa icmgkevdpd anrrwpaavw aggfylltgc
      301 fgatvaalft afpatlvtcv aglallgtig sslhtalqhd dareaalltf iitassisll
      361 gigaacwgll vgiilhqvnq rrn
//
LOCUS       WP_010635972             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Aeromonas].
ACCESSION   WP_010635972
VERSION     WP_010635972.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21870
     Region          1..202
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtellavvai tffavispgp dfamvsrnsl llsrrsgvlt algigagvcv hvtytllgvg
       61 lliqqslwlf nliklagaay liflgikmlr akpataevla dqpalsslga lrtgfltnvl
      121 npkttifivs lfmqvvqpqt plavqlgyga fivlahavwf savaiffstd svrgrllavr
      181 hwidrvfggl lvgfgmllal tqqtr
//
LOCUS       WP_010635979             447 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: potassium channel family protein [Aeromonas].
ACCESSION   WP_010635979
VERSION     WP_010635979.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..447
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=50715
     Region          367..442
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mnatelwqls peqfnewrra ndypliwdll vaslphfddw mteqkidkqv ifqigiarfi
       61 ssrcvlslcl ymsddkirly etassalesl rksgliraet rfepycmwla gkhgkdevkr
      121 vqsllsvsen nkgeaqvlgr hrllniggve lkspiisgrl ldftcldels ldgavnnskv
      181 ylwhcsakgv rvnggvigld lfdsllwdhr awakkrelal edgvfqdfti eceeirfhss
      241 ravlknfnvr aknfdatmeh tnldkvqvay nengrvdhse asklyrnakr lfssvgdtvd
      301 agecyykekl hemkslaspr elfkecwlrs gwlkkgwltl lcylkcaakf isfitwgfge
      361 rpirslllsm gvillatlty ylapgsvthd hlgrslyfsi vtfvtlgygd isqtssplql
      421 lsaieafcgm fltglflagf asktkqy
//
LOCUS       WP_010635992             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Aeromonas].
ACCESSION   WP_010635992
VERSION     WP_010635992.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..316
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32937
     Region          7..312
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mdllaslhfs lsitgpicvv lllgiwlkql gllpdsfves asrlvfqvtl pallflsmvr
       61 tdfstmpspw livygllgtl tgflvlella arfiperrqr gifvqgsfrg nmgimglayv
      121 qnaygaegig aaallvgsvt vlynvlavit ltrslggskg ikpilrgiak npliiailaa
      181 lpfgllgiel pqlvittgny fanmtlplal lctgaslnlk alrggalltg watanrllci
      241 pvllvmgawa lgfspqalgi lflisstpta aasyvmtram ggdsalaani iatttlgslv
      301 ttslgatlmn ylglmg
//
LOCUS       WP_010636002             271 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Aeromonas].
ACCESSION   WP_010636002
VERSION     WP_010636002.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..271
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29502
     Region          12..263
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mkrdhgsqps gllkyaaigg llflhfpilf iflyaftses ksyqfpppgl tlkwfevtln
       61 rpdvwraiql slevaglatl vamvlgtlaa gaiarsrffg qevvslllvl pialpgivtg
      121 ialrsaygvm eipfsfwtiv ighatfcvvv vynnalarfr rtnqslieas mdlgadgfqt
      181 lryvilpnla tallaggmla falsfdeviv ttftagqqtt lpiwmyqeli rprdrpvtnv
      241 valiivaftt ipillayylt rdgqdvagsg k
//
LOCUS       WP_010636043             669 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Aeromonas dhakensis].
ACCESSION   WP_010636043
VERSION     WP_010636043.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..669
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75302
     Region          19..662
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 maaslwrqtp wgkanggqwr yalrnslamc lslwlafvle ldspywamts aavvsfptvg
       61 gviskslgrv vgsligamaa vvitglgisd pwlfsflial wlalctyisn hhqnnvsyaf
      121 alagytaaii afscvnvtdp qhifdiaqar vsevivgilc ggllmmilps tsdgdtllqs
      181 lqktqarlle haqllwlget spevrtaheg ligqiltmnv lriqavwshh rlrrhnklln
      241 fllhrqlrli slissqrrml hnwptqpeel qallerllae lgqpgcdkyr iarllaplap
      301 tvasdyrlht fwqrlrhfcw sylecqrwld rlaryddqew papprhsslt shtdtleaay
      361 nggrtflcvl lgcafwihsq wdagssaltl lsiccvlysa tpapakgant mlkailllsl
      421 icfvvkfglm irlddfwlfc alllpvlitm qlfkqqqprq avlwgqlivl lgsflaitnp
      481 psydylqyin gslgqalgvm gaglafqllr pssdrrkgrr lirslrrhfm dqlepaprqs
      541 esqfesriyh cisqlsqsqd qtarlwvlrw gvvllncshi vwqlrqwrge dqplylvrdn
      601 circlqgilt eqgvqhasld rtlaelqris aalanhrept arelagmvwr lhsslsqlqq
      661 alpvaaear
//
LOCUS       WP_010636086             221 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Aeromonas dhakensis].
ACCESSION   WP_010636086
VERSION     WP_010636086.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..221
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24912
     Region          24..220
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 meqfyqlaha fmhqdlvtls dpkmafmvcg vlltflvlen gfiptaflpg dslliltgvl
       61 iyqdvlslgv ipllilatfv gtwlgymqgr flghtqlyhr llshveerhq qkvyylldky
      121 givtlitary iafvrtaypy ivgatelpqg rflivnlvss imwicplvgf gyflshtkla
      181 aeyqsqflsi ilclpivllv gglialiwrw lskrkasapr d
//
LOCUS       WP_010636145             792 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Aeromonas].
ACCESSION   WP_010636145
VERSION     WP_010636145.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..792
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=91137
     Region          143..230
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
     Region          474..>551
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 meseqqqhli eqlipllrek dfddifnrlt qdensnsrfl ikmelkrkct pcrrvidmrd
       61 elgdeclvhe fegithfmpa eaiglfqsqc ylykddytlg vyealqywqk yqhgkndgql
      121 qppvspfrqy dvnpisfasy ygrrqermhf sspvvikfad gdklfakssd lslggirvsv
      181 pylpnyqtga qvevfftgle rdhpnpvlhh svsyqilgee skegkywlrl iktgehpafd
      241 qflndfiesn ksryrvsvdy llsaaiikgy eqfylprmtg mplffgsgds psleialrte
      301 nnqhileywr daknrdmlas lfsatrmqal lpakgelket liycfthsvr shlyffsatr
      361 eellqsglms lffqvgarrp swrvykfsle rcdlheadla sqqgkespql qdmllqerlk
      421 qisyvgllqq vgldsqreef qfdassqhna nelqrfghds saapfeietl hyvqlrkear
      481 yihktavaik hngrawlgwt rdisahgmqi eleepfegak ddivtialpr lqelsksmdl
      541 qrlpyrlvsi nltrtvlhlc iegdperhtg rqffkllies nqnklkaaqe qrryrgmara
      601 lrniythhvf ctpvyinklk gapkpasvgh apqprslsrl lkacaeqgdq dnlyplfqge
      661 llkqlimnpl raieredqpq eeevyiaslq tatglpifts rlassfqnva ekrsfieqal
      721 rqgefysvlv gisrtgrpdt nfianeldyi akfaihkakk leeelwsvvg vgeltdtsqa
      781 tlfrlgitap ik
//
LOCUS       WP_010636495             125 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Streptomyces].
ACCESSION   WP_010636495
VERSION     WP_010636495.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..125
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13764
     Region          8..123
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 miaelqcvvl dcseplelar fyrsllggtv nqedrrwavg eewatlhtps glvlafqrvt
       61 pyqpprwpda srpqqfhldf gvpdldqaqe qalasgatll ddgagersws vladpaghpf
      121 clvrh
//
LOCUS       WP_010636500             137 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Streptomyces].
ACCESSION   WP_010636500
VERSION     WP_010636500.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..137
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13977
     Region          <11..>124
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(21..23,25..26,30,33,42,44,46,50..51,54..56,58..59,
                     63,66,75,77,79,83..84,87..89,91..92,96,99)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          44..75
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          77..102
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mseapdpevv elatkifdla rqgqaaqlaa yvdagvpvnl tndqghtlvm laayhghada
       61 vrvllergad pdrandrgqt plagavfkge devvtalldg gadpaagaps aldtarmfgk
      121 dellarftaa qdgpgta
//
LOCUS       WP_010636535             184 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DinB family protein [Streptomyces].
ACCESSION   WP_010636535
VERSION     WP_010636535.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Newton,G.L., Leung,S.S., Wakabayashi,J.I., Rawat,M. and Fahey,R.C.
  TITLE     The DinB superfamily includes novel mycothiol, bacillithiol, and
            glutathione S-transferases
  JOURNAL   Biochemistry 50 (49), 10751-10760 (2011)
   PUBMED   22059487
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Cheo,D.L., Bayles,K.W. and Yasbin,R.E.
  TITLE     Cloning and characterization of DNA damage-inducible promoter
            regions from Bacillus subtilis
  JOURNAL   J Bacteriol 173 (5), 1696-1703 (1991)
   PUBMED   1847907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..184
                     /product="DinB family protein"
                     /calculated_mol_wt=20609
     Region          32..180
                     /region_name="DUF664"
                     /note="Protein of unknown function (DUF664); pfam04978"
                     /db_xref="CDD:428232"
ORIGIN      
        1 mnatprkrad lflpveddpr qngptlgdev ttlmeylrcq rltlevkcag ldaeqlarrs
       61 vepstmsllg lvrhmadver vwfrarmagl dappyfrlpe dpdgdwdgal pdpalveeaw
      121 rllraeqefg dafvarapsl dltgeahgep vslrevlvhl veeyarhngh adflreridg
      181 rvgq
//
LOCUS       WP_010636576             185 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CGNR zinc finger domain-containing protein
            [Streptomyces].
ACCESSION   WP_010636576
VERSION     WP_010636576.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..185
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19495
     Region          10..173
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mlithdtrca ldavvglvnt apgdghsdgl gdvtalrafv dahgvsdvgr lgeadlaavl
       61 rvrerfeavf aagdlgdaar vinelvaaag ttprltdhdg fdwhvhyfap gasvadhlaa
      121 dggmalaifv vagecerlrr ceapdcanaf vdlsrnrsrr ycsgrtcgnr lhvaayrarr
      181 reaag
//
LOCUS       WP_010636615             193 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            albidoflavus].
ACCESSION   WP_010636615
VERSION     WP_010636615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20180
     Region          3..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprwkpdagq rlvmaafelf aeqgydgttv sqiaaraglt rstfhrhfsd krdiltagqa
       61 tlsrlltdgi aaapatatpv eavarglera sagmtafnre lsplmraald adeelrerea
      121 lksvgmaram aealrardvp dpaaqvaael gvlafktgyg rwagaaqdea pgglpaltva
      181 alrelhaaat glt
//
LOCUS       WP_010636695             518 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Streptomyces albidoflavus].
ACCESSION   WP_010636695
VERSION     WP_010636695.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..518
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53495
     Region          32..452
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtaetpsseg irtykgeera lradrlgttg lllsvlaasa plmvvagvmp ttfgvmgitg
       61 qpllfvilgi vlalfslgya emsrhvhnag afyayisrgl ggtagagasl valvaysamq
      121 vgiygifgfe vsvicstylg ldiawwvfal asvaavavla wlkidlnarv lgvllliecv
      181 lvvifdvaai adpgpeglsl hafnpetltg aglgtalcfc iaafvgfeqa pvyaeetrrp
      241 hivvarvmfl aigfvalffm isswaltvas gpsgivgdar eqsagllfhl tesrlgttft
      301 dvlhilfvtg mfaamlsfhn vvaryafamg regllpaafg rtnpgsgapg tgsllqtgis
      361 vvlvaafalt dgnpvgdpta pvlrmftwmg nvgalgiivl maaaslaviv ffarrgaara
      421 qlwrllasgi aglalltiag ytvkdfsvlv gaesgsalsw llpgviglaa vagigyglll
      481 krtrpevhar igqgneafql ekaadaagrp agerattg
//
LOCUS       WP_010636697             175 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Acidithiobacillus].
ACCESSION   WP_010636697
VERSION     WP_010636697.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..175
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18847
     Region          22..>173
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 msvssyflsy lhaavvsasg vvdqyglaiv vaglflesag viflpgetll igagfvasqg
       61 afnplvlfal giigtsagwf tayyigykvg ikwvkkhgrw igitaerlnk thtfmnkygs
      121 ivvlfgrfiv plrqlqgyis gsaettlqdf ylwnilgavi wvafwggagy flgml
//
LOCUS       WP_010636738             225 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            albidoflavus].
ACCESSION   WP_010636738
VERSION     WP_010636738.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..225
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24187
     Region          42..88
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          107..220
                     /region_name="TetR_C_24"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17932"
                     /db_xref="CDD:465574"
ORIGIN      
        1 msaverdpeg sdevvdesag eaagepddaa waevtpdaar rllvaavdaf aergyhattt
       61 rdiagragms paalyihykt keellhrisr ighdralkim rdaadsggta aerldravrs
      121 fvgwhalrht tarvvqyeld algsehraei ielrrgtdaa vremisdgvr dgefevpdip
      181 gttlavislc idvarwfkvg gartpeeiga lyaglvlrmv gagek
//
LOCUS       WP_010636819             149 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010636819
VERSION     WP_010636819.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..149
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16461
     Region          1..147
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslrerlqed mkaamrares drlttirmlq aaikqrevdd rrelddtevl siaeklikqr
       61 kdsasqfrag nrpdladkee aeivilsayl peplsmeaid aliaeavsnt aasgpkdmgk
      121 vlnslkprml gradmalvae kvkarlnng
//
LOCUS       WP_010636907             312 aa            linear   BCT 01-JAN-2025
DEFINITION  MlaD family protein [Acidithiobacillus thiooxidans].
ACCESSION   WP_010636907
VERSION     WP_010636907.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..312
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=33124
     Region          45..243
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mesrahalva vvfllvlgva vaivglwmhh gekpgvnfdv ispysvtgls vqapvrfkgv
       61 rvgevtaigl dptnprmirv kikvdkstpi tratfaelap qgvtglsyls ltdkgtdfap
      121 ithnpgqvae ipmhpsffev lsrngeslvn rsneladrln dllndqnrar fgqtlthldq
      181 atqdlvqmed ammpalkalp amvaatqstm vashqliqhl dtlavqaqap lasatqaaks
      241 lqklgtaseq amntlnyqtl pqvrqltssl lhssealssl sqslkqspqs llygtqgppp
      301 gpgesgfsag gh
//
LOCUS       WP_010636969             374 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            albidoflavus].
ACCESSION   WP_010636969
VERSION     WP_010636969.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..374
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40735
     Region          42..174
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          211..335
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mqesitpgar erqadqpwaa perlwprpaa ppgpadaplp alteldlavv nalqiqprap
       61 wslvgevlgv daatvarrwk rlsdsgtawv dgywppaddg qvraqveivt eadrsweigr
      121 iiahdpetms vkhtsgardl laivwaydmd glvdyiggri aglpgvrltr thvitgapfe
      181 gsrwrlrsls agqrarlapp aaparpepvt avdrriaval gedgrmplae larragtsva
      241 tvgrrvrrlv gsgqfvlrcs larpltgwpv svvyfasvpa ehldaatasl rtlpelrlct
      301 vtagphnlil dvwlrgvpev htleahlvqe lahlrfrvdd rvmvlrtekn vgrvldrrgr
      361 slravpmelp ealt
//
LOCUS       WP_010636958             142 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Acidithiobacillus].
ACCESSION   WP_010636958
VERSION     WP_010636958.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..142
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16193
     Region          34..142
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mdrrllirll akqeltiilp lvqvlnpdvv pdllaqrled mmgqgyqcva afldddcvgv
       61 agiwqgtrfw cgryldvdnv vvdpayrssg igrqlmdwve qyarqqgcei mvldayvtnh
      121 sarrfyermg yqvlghhfvk sl
//
LOCUS       WP_010636978             104 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF485 domain-containing protein [Streptomyces albidoflavus].
ACCESSION   WP_010636978
VERSION     WP_010636978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..104
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=11384
     Region          1..103
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 mpstaafvea qesaefgelr rahrsfafpl tiafvlwyll yvllsnyagg fmgaklfgni
       61 nvalvlglgq fattfliaww ysqhaakkld praeaikarl egda
//
LOCUS       WP_010637231             266 aa            linear   BCT 01-JAN-2025
DEFINITION  YdcF family protein [Acidithiobacillus thiooxidans].
ACCESSION   WP_010637231
VERSION     WP_010637231.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..266
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29436
     Region          27..257
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mllryttvlt lasallqppg vlfllamlgw lgevlgwryw grtliilalg ilyffstaig
       61 arlllmplen rypplnqplt gaehpgaivv lgggevmdsp hsrletanar tlvrlmaaar
      121 larqtqlpvv psggaprfgv aaeattmahi lrqdfhvtsp iwpethsynt aanaadsrtl
      181 laehhiqkiy lvtsalhmpr avawfrlshl evipvptdyr lnqvrelkld swlpraifme
      241 isseacheyl gllwlwlqeq glgngn
//
LOCUS       WP_010637238             388 aa            linear   BCT 01-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein
            [Acidithiobacillus thiooxidans].
ACCESSION   WP_010637238
VERSION     WP_010637238.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..388
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41984
     Region          10..379
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 misrpslisk iflvffgllf astafavvpt prlptppapa lpsvvsyvlm dydtgqiiaa
       61 ksenlrrapa sltklmtayl tyqaihngtl nsneniqisn tawktggssm fiqpglavnv
      121 dqllhgllid sgndaavala etvagsrsgf vtlmnetaaq lglrntnynn vdglpddnly
      181 ttaldvarls rtliqqypqv iqitkqksyt ynkitqrswn pvlfrdpsvd glktgltdas
      241 gycidataqr ngrrliavvm ggpnwagstn avealldygy rffvnhpvyq sgqqvgkitr
      301 ndfspmhvpv gvtqkvtvtv pkghfsdlqr vvelnpnlqa plkkgtvvgt lvfqldgktl
      361 ktvpvvsmvs aekagwlsrm fhkigdal
//
LOCUS       WP_010637312             381 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Acidithiobacillus thiooxidans].
ACCESSION   WP_010637312
VERSION     WP_010637312.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..381
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41087
     Region          43..361
                     /region_name="AKR_unchar"
                     /note="uncharacterized aldo-keto reductase (AKR)
                     superfamily protein; cd19099"
                     /db_xref="CDD:381325"
     Site            order(50..52,80,85,116,183..184,223..224,263,303..309,330,
                     347..351,355,358..359)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381325"
     Site            order(80,85,116,183)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381325"
ORIGIN      
        1 mnaadntlip gaansvgska yvarfaetla eehfsdflnt riklsslgvg tfpgavddvt
       61 dlavaaivaq alqsginvid tganyrfgra gravgagiak amaagilree ffvvgkggfl
      121 tftggrpedp laffreevva kglgkeedla qnvhclspey iawqlddlrg qtgletldvf
      181 lvdqpevhip ligkermyqk llqvftvleq avnenkiryy gistfnacrv etdhtlfqsl
      241 tsliglaeka agegnrhhlr vvelpfnalm peaytrfsqv tgqgnigsti qaafqlkltv
      301 mashtlgkgl lareeipslq egipelanaa qraiqfvrst pgigvtlvgm ssplhladfl
      361 avakqlplpk erylamfeke k
//
LOCUS       WP_010637353             141 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Acidithiobacillus].
ACCESSION   WP_010637353
VERSION     WP_010637353.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..141
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15254
     Region          36..141
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 meakiltfvq aqwplllaav aliimifkgp ltrkaagise vdaktavqli nheeavvidv
       61 reqkewaqgh lpgarhiplg dlpkymkdle khrghhvicq casgmrsara aaslkkagfd
      121 kiyslkggis awrgaglpve k
//
LOCUS       WP_010637377            1065 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Streptomyces].
ACCESSION   WP_010637377
VERSION     WP_010637377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..1065
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=109744
     Region          3..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mswlsrfsla qraliglmsi iallfgaiai pqlkqqllps ielpmvsvla pypgaspdvv
       61 ekqvveplek sidavegitg itatasegna vlmaqfdfgs adtqqlvadi qqavnrsram
      121 lpddvdpqvv agstddiptv vlavtsdkdq qalagqlert vvpslesidg vgqvsvdgvr
      181 elqiavtpdd adlakaglss adlvqalqaa gatvpagsfd ekgenrtvqv gggftsvkqi
      241 edlriapaag gqggqggpga qagpgdagka papvrlgsva eveqqqatat sltrtngeps
      301 lavvvtmdrd gsavaisdav aeklpelrad lgdsseltvv sdqgpavaks ieglttegal
      361 glvfavviil vflasirstl vtavsiplsv vlalivlwtr dlslnmltlg altiaigrvv
      421 ddsivvleni krhlgygeer keailtavke vagavtsatl ttvavflpig lvggmvgelf
      481 gsfsltvtaa llasllvslt vvpvlsfwfl rapkgtpeda eaaraaaeek earsrlqrly
      541 vpilkfatrr rltslaiava vllgtfgmap llktnffdqg eqdvlsvkqe lapgtslaat
      601 dqaaekveal lketegvedy qvtigssgfm aafgggtdtn qasyqvklad sassetvqka
      661 ldkglagldg igdtrvaagd gfasqdlsvv vkaseadvla kaseqvreev aklddvtdvq
      721 sdlsqsvpri svsanekaaa agftdaslgq vvaqsvrgtt agqvvlddae rdivvksakp
      781 aetlaelral plgpvklgqi advelvdgpv smtridgsra atvtarptad ntgavtaelq
      841 tkinalelpe gatatiggvs adqdeafgql glamlaaiai vfmllvatfr slvqplillv
      901 sipfaatgav glliatgtpm gvpamigmlm ligivvtnai vlidlinqyr dkgygiieav
      961 ieggrhrfrp ilmtalatif alipmalgvt geggfiaqpl avvvigglit stvltlvlvp
     1021 tlyamvelrk erraakkaak rdgkadvpgq ggtpaeeqtp epars
//
LOCUS       WP_010637430             102 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010637430
VERSION     WP_010637430.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..102
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11444
     Region          <12..88
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 masyreditt piklkligyi rdmvvqkgwt qteaaknldi srsrfcrimg gqtkdisewr
       61 lmqclamlgs dvkifivptq csqgkieivd isappkqeqn lv
//
LOCUS       WP_010637453             289 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: patatin-like phospholipase family protein
            [Acidithiobacillus].
ACCESSION   WP_010637453
VERSION     WP_010637453.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..289
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31215
     Region          16..286
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 magiakdhgv vnhpvagskk piqvalsgsg fllpvhlgal qaieaagyrv salsgtsgga
       61 ivavlyavhr dipslvnlvl dtdwqpfmnf dswtngwrll trrgicataa ldafltrhtq
      121 gqsfadldle lfvcatdllr gqrtvfcrae tpelpvakaa rassslpfvy ppkrvdgrly
      181 vdggltddip gdvlpkdsev psvgvyltge pprlhgnept lfalaslsvr dllrgqeyld
      241 rhaapwvrfl pvdtgnlnml darmprtdre qlmelgrvgm ekllqnlaa
//
LOCUS       WP_010637498             341 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endonuclease/exonuclease/phosphatase family protein
            [Streptomyces].
ACCESSION   WP_010637498
VERSION     WP_010637498.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..341
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35770
     Region          67..340
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 maqayrtepd sdghehgrpe prlrslarrl rthrgpwrrg lvlaalalll alvmaghari
       61 pnsvgslgsl getflpwlgl alpvllvagl vrrsatalia lllpavvwln lfgglvtdks
      121 atggdltvat hnvnadnpdp aatardlaas gadvvaleel speavpafre alaaayphha
      181 vegtvglwsk yplsatapvd iklgwtralr stvdtpsgpl avyvahlpsv rvkvdagfta
      241 gqrdssaeal glairgeeld rvvllgdlng tmndralspv tsqmrstqga agngfgfswp
      301 asfpmaridq imvqgvepvs swtlprtasd hlpiaarisf g
//
LOCUS       WP_010637526             330 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpP1/FadL family transporter, partial [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010637526
VERSION     WP_010637526.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         <1..330
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <26..330
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 vfwlgvnylq qmpsqlntyp saelngmggp fpnsyaqafs sidfmqmaps iamkvnhhla
       61 vgatlniaae qasfqqtmtg yapaqvmtss gsyatvpggm petggldlss pswaygvgft
      121 vgalykvndm vtlgltyksp iwftpltwqa gaqnlgagat gnpgqysghl nypqqvafgl
      181 aihptkrwlv svegqwinwh stmnnfriyg pwngtnvmsl gmhwknqwva nigtqydvth
      241 wlqvragyth gtnpisdant annlifpaiv anavtfgstq klgmgwklte aymhefsnti
      301 tggqspfggp etpsatmden syglqvgydf
//
LOCUS       WP_010637559             826 aa            linear   BCT 01-JAN-2025
DEFINITION  penicillin-binding protein 1A [Acidithiobacillus thiooxidans].
ACCESSION   WP_010637559
VERSION     WP_010637559.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..826
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91328
     Region          30..805
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 maargissrr rwvfwtlvvl llvalnivvg igvwtwriwq elppvvqlen whpqeplriy
       61 adndhllqvv gpqlryalpl kqipktlqda fisaenskfy shnpiyypvs fpgiiraafv
      121 dlvhmapvqg astiteqvar nfyltpkkti trkvaeilla yklgarlhrp qildlylnki
      181 ylgegaygvq aaaktyygkt vnqltvsema tlaglpaaps dfnpiaspas aktrrdyvlr
      241 hmahygyitk aqeeaalaep ikaryhapas niapyatdwi rnwlekhfga dftyrtglrv
      301 ytsinptdqr aadrdiavgl enygmgldsm dpkawhgpia qlstaameaa lqgqrpsklp
      361 nhnpanlhwg vvvkstpema tvsfegrhlv hlslrdvawa rsapkgnppt avnqvlqpgd
      421 liwlrryvva atsgtgnpvw gtkvwhniph sgwqlaqiph vqgalvslas rsgailalsg
      481 gfsyelshfd ralyafrqpg sgfkpfvyss amdaptylas grkhyltpvs liadtplvih
      541 lgngqvyapt nysrtfsnip fpvwedlads hnvpsvrllm hvgipyakry verfgipakq
      601 ipaspsmvlg sgdftplqia rgyavfssgg flphpylirk ivtahgttvs lmdcplgyrp
      661 ppkqtvippg vaflmtrmme rvirvgtgva aqilhrhdla gktgttnhed nawfngfnpd
      721 ittsvwvgyd nnqsmgtwaa garealpiwi rymhtalaqy pdvgffqppd vvtarynpkt
      781 gdlapqgdpg hqypmgyfls gylppkpkpk isaetqsfih almhif
//
LOCUS       WP_010637560             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: D-alanyl-D-alanine carboxypeptidase family protein
            [Acidithiobacillus].
ACCESSION   WP_010637560
VERSION     WP_010637560.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..389
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40941
     Region          1..380
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mklpivlait avfswgsvac aavpplppmp tlpppppmpa pqltgiqsav lldinsgqil
       61 maendekpvn psglvklmta ylmyqaekqg lvqpgenvhv sndawhaqgs rmfiqpgmpv
      121 tmtqlthgll idggndaaia iaetvagsvg gfvdlmnhda aamglqhthf tnpdglpqpg
      181 qtstaldlar lsarliqsyp qvmqvagkvs ytynhitqyn ynplagqngv nglgvglagk
      241 nswnlavsat rngrtlvavv lgapsrsaag sdasallhyg wngwqnvsly kagatvaqih
      301 ngdwspatvq gvtagpvvvs epkqqktrlq trfvptpnlk tplaagaeig tlqiswhghv
      361 lktvpvqtrs avkpagwftr lihegeswl
//
LOCUS       WP_010637637            1012 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010637637
VERSION     WP_010637637.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1012)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1012)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1012)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1012)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..1012
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=115196
     Region          1..1002
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mkltseaafe taiedvlldd gytrvdaksf nreraifpde alafiratqg kvwekletlh
       61 geqtgtrvle slckwldthg slatlrhgfk cfgrtlriaf frpahglnpe learyqanrl
      121 gltrqlhysp kseksldvvl singipvvtl elknplsgqt aanaihqyrh drdprepifv
      181 fskralvhfa vdteeahmtt rlagsstyfl pfnqgmdgga gnppdragrn yktayvweev
      241 lqrnslldll arflhldvee kttddgkkvr keslifpryh qlqavrrmva aaasegvghn
      301 yliehsagsg ksntiawlah rlsslhnard erlfdsvvvi tdrvvldrql qntiyqfdhr
      361 qgvvqkided srqlaealea gvpiiittlq kfpfvsgqla klneergegg kshlptrkya
      421 viideahssq sgetatelkg vlggaelrkk aqemaeeege ielerlyrsm akrghqpnms
      481 ffaftatpkh ktlaifgrng epfhrynmrq aieegfiedv lknyvtykty yklikkaedd
      541 pnverkkaar alarfmrlhp hnigqktevm vehfqhftrh kigghakamv vtgsrleavr
      601 ykqefdryia ekgypikslv afsgsveddk ipeksyteve mngglkekel pdtfakpefr
      661 vllvaekyqt gfdqpllhtm yvdkrlagiq avqtlsrlnr thplkddtfv ldfvndptei
      721 qeafrqyyeg svmgeqvdpd klyevkagld asgiylqtei adfahvffap krrqspgdhk
      781 amnaildqav arfvqlqnte eeeaelwrgk lqafrnlysf lsqvipyqds dleklftylr
      841 hlalklpkrk sgpgyqfded veldyyrlqk isegsislne gytkpldgpr evgtgmvree
      901 hvslsrlidi inerfggeln eadqlffdqi aeaasqneal qmaaevnsld kfqlvfrqvl
      961 eslfieriel neelftdymg kpdmqelvsk wlgsqvykrl sprgqsspsd ke
//
LOCUS       WP_010637649             314 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ROK family protein [Acidithiobacillus].
ACCESSION   WP_010637649
VERSION     WP_010637649.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..314
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33345
     Region          5..310
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mteqltigvd vggtnlrfgv frgndcldsi rhevdlhakc aaaadsesaa qlftdlleag
       61 iaqlrhqype ivrvgvavpg fvnakgvllq spnipqlihf dlqsavqnac qlpvlienda
      121 naagygefwe ekqenpelrd llyvglgtgv gggwvhndrp wrgehgtame ighiivvpgg
      181 rrcgcgnqgc leqyasargi qssyveltgt apdtaviaqm acdgrpeasq tfqmagdylg
      241 qalasilkva dvrvirvggg vsaawdcfap almqrldadl ipalrgevev krgndddlag
      301 mrgvalladq elsq
//
LOCUS       WP_010637698             793 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Acidithiobacillus thiooxidans].
ACCESSION   WP_010637698
VERSION     WP_010637698.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..793
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85884
     Region          62..767
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mtakntyrvt gslllalcal hsdtsiadai tastrsvgdd ssvnvgevsk adntsiyvap
       61 ksavpsqrqi frsglaekvi gkkqieaagp gasgndmlsm apgvnvisgy tatgggktqi
      121 singvkqgwh ipggaiddgs iattfdgvpm anvatglwas pdvnqsslis girliygpgn
      181 pasrwynsig gtinyiplqp tkkagatigm tygsydfkni hfaintgehd gfaavigggs
      241 ssgnsylssp agsivrpfgs snmssysyaw yfkgiksftn gnvslgayla kgqsykpfmq
      301 llspiegiti ngqdvnkkpi pgplysqqts gfyralpykd dsntvwmlyq ktnvnigagt
      361 elhnmvwfrh gdrlhyqisr ffpedyeyyt phtnvygdkl sfvthlpwne leyggyfine
      421 rytvennnfp ygtydpaaaf kqtylyktfd stalaaylqd rispiesldi tpgvrvvgyq
      481 trytpnmcae spaacvldpk gadsslpass ksyeqvepsl ainwrptrhl alfasyavay
      541 ktpgaaddgg gvfqsiptsa lslekgqeyq agmkfhvkea pylhnflasv nwyflhfsnq
      601 fipitlpdns vinaqgtsdy dgvnisledd pvywlhlftn lsfekaqftn ysiqggksyn
      661 glplpyvpsq tanvgfytqn yvagvdlepr lwmtytgpqa vfnsitnaps pdikmpaftl
      721 vnfslgaklp vhfmglnyls skldimnllg nkynryvqvd sgssgqfgpl gagalvgyag
      781 aprlvyfsvs akf
//
LOCUS       WP_010637795             332 aa            linear   BCT 01-JAN-2025
DEFINITION  NRAMP family divalent metal transporter, partial [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010637795
VERSION     WP_010637795.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..>332
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
     Region          9..>280
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mtannstmpq rhsrwsvfli vlgpglvvml adtdvgsiit aaqsgaqwgf kllllqfilm
       61 pilyivqelt vrlgiftgkg hgeliretfg tgwaylsvag lsiattgall tefsgvagvs
      121 hlyglpravg vilaaatllt ivwtgsyrrv erialimglf elvffgiawv shpdlqdilh
      181 glthapitdk nymmlvaani gavimpwmvf yqqsavadkg lhpenyrhar wdtaigavlt
      241 qaimaavlia taatigrlnp naplntvhhl seaitplpgr hlgtpgvfpv ysggrhgsqp
      301 llppcaetwg lgnnsldssf ssqhnslnsl rv
//
LOCUS       WP_010637807             323 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent alcohol dehydrogenase [Streptomyces albidoflavus].
ACCESSION   WP_010637807
VERSION     WP_010637807.1
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   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..323
                     /product="NAD(P)-dependent alcohol dehydrogenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33726
     Region          9..315
                     /region_name="MDR1"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08267"
                     /db_xref="CDD:176228"
     Site            order(43..45,48,129,133,154..157,159..160,178..179,182,
                     197,214..215,235..236,263..265)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176228"
ORIGIN      
        1 mttmraalfd rygppevlye grlpvpvpkp gevlvkvhat svnggelagr agrvrlvtgr
       61 rfpqrtgidf tgevaevtpg vrgpavgdqv wgvlgrtmgs aaeylairpd riaraprtvs
      121 lteaaslpag gttgltalka haglrpgerl lvrgaaggvg svavqlgkal gahvtavagp
      181 rlldfvkelg adeaysytey gpgdlgpfdv imdtagtdhr lwrrrlapgg rmvaisfdld
      241 hvpsslgyll astvhgkgrv rffsgnprta llreltgyvd sgalrpvvdt vrplaglada
      301 hralesggvr gkhviqvaee taa
//
LOCUS       WP_010637812             196 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            albidoflavus].
ACCESSION   WP_010637812
VERSION     WP_010637812.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20506
     Region          16..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpsaseskga sarstradav rnrqvlldaa aevfvasgvd apireiaara gvgtgtvyrh
       61 fptradlvva vyrhqveaca eagpallads aspfaalraw tglfvdflvt khgladamra
      121 dsggfealha yfldrlvpvc gqlldaaada geigpgtray elmrgignlc agsdddpryd
      181 prrlvglllq glrqae
//
LOCUS       WP_010637832             180 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase, partial [Acidithiobacillus thiooxidans].
ACCESSION   WP_010637832
VERSION     WP_010637832.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..>180
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          6..>133
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mmpsaerpft lvhangerla glihethqdp vgiflpgfas nmngsksrll aeyaqnqgws
       61 wvrfdprgvg rsdglfeqlt lsryledlrl ilqmlekrpv ilvgssmggw latlaatrwp
      121 erlralllia paynfiqtlf qtlspedqhr wqssnlccwq dhyglgelrm rfdlvadswr
//
LOCUS       WP_010637849             191 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Acidithiobacillus thiooxidans].
ACCESSION   WP_010637849
VERSION     WP_010637849.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..191
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20553
     Region          11..181
                     /region_name="PRX_like1"
                     /note="Peroxiredoxin (PRX)-like 1 family; hypothetical
                     proteins that show sequence similarity to PRXs. Members of
                     this group contain a conserved cysteine that aligns to the
                     first cysteine in the CXXC motif of TRX. This does not
                     correspond to the peroxidatic...; cd02969"
                     /db_xref="CDD:239267"
     Site            47
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239267"
ORIGIN      
        1 mamtakdlpv ggampafslp fggksgqwss asargkpllv lficnhcpyv lhisrqlgel
       61 acqwqnqgvq vvainsndpd typedapekm paeaqragya fpylfdadqa vakafnavct
      121 pdiflfdqag klfyhgqfdd srpkntlpvt gkdlseavaa vlekreppak vlpsvgcsik
      181 wragnepegw v
//
LOCUS       WP_010637941             462 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Acidithiobacillus thiooxidans].
ACCESSION   WP_010637941
VERSION     WP_010637941.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..462
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49691
     Region          35..396
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(69,119..120,122..124,127,149,152..153,156,224,
                     227..228,231..233,236,266,270,314..315,319,323,346,
                     349..350,353..354,357)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 mknpeaalnq kerravfsla gifglrllgl flvlpvfsvy ahglrgamdh pvligialga
       61 ygltqaffqi pfgklsdkwg rkpviaigll ifaigsaiaa tatsiewlli grivqgagav
      121 aaaiialtad lvreerwtka maiigitigi sfsislilsa plagwigvsg ifwltavlsl
      181 aaigvlylvi pavptrfhrd aemspamlge vlrdpsllrl dfgifslhtg ltaifvvlpl
      241 vlidprhpll slndqwmlyl pvmllsfvam lpmiivgeak rklkevfiia iaillvsvil
      301 malsahniwl iavalflffm gfnvleaslp slvakfchpg akgtatgvyt tseflgafcg
      361 gllggllyip garnysdifw avaiiyaiwl vvaltmqrpr ylatrvftlt esaerqsnle
      421 trllalpgia evavfkdega vyckvdskvy deqavmgvla gt
//
LOCUS       WP_010637950             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease [Streptomyces].
ACCESSION   WP_010637950
VERSION     WP_010637950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..192
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20811
     Region          61..121
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mphvlvlnas yeplgvvplr ralvlvlesk avcleesgaf lhsesrtvpa psvvrlkrfv
       61 kvpyrgpvpl trralfardg grcvycggva tsvdhviprs rgglhvwdnv vascrrcnhv
      121 kadrhlmelg wrlrnkpapp tglawriigt ghrdprwlpy lqpfggddal arienvgggg
      181 eavavrpara ga
//
LOCUS       WP_010637963             810 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010637963
VERSION     WP_010637963.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..810
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86241
     Region          1..70
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          72..804
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mknleigvsg mtcascssrv ertlnrlpgv qasvnlster atvafdptqt sletlraaiv
       61 digyqpvvaq selevggmtc ascssrvera lgkvsgvlsa svnlateram veyfpdstnq
      121 dqliaavvna gyearavrad argedrkisq lrlmrkdllt avvlavpilc lsmgpllfpa
      181 lgrwlqenal fghfwdwvqa vlatlvlagp grrffrpgli ayrhlspdmn slvatgtgaa
      241 wlfsmivlif pelfsqvggh vyfdsaavvi aaillgkyle elakgrasqa irhlvdlqak
      301 datllkdgqe qrvplnrirt gdhllvrpge rlpvdgivle gesyidaaml tgevlpehkk
      361 agdavvgati ngngrliiea tavgqntvia hiiqmveqaq agklpiqgla drvvrvftpl
      421 vigiallsfm vwlwlgpspa itvallsava vlvvacpcam glatpaavmv gtgraaelgv
      481 ffrkglalet laqvktvcld ktgtltrgtp avceivaddv rqvltlaasl eaasehplar
      541 tivqaarere islspvtdfq avpgrgvegv vagqkilvgt avwlqengva qdakfwtepq
      601 maqnwvyiag nghllgkiai qdnvrpesla vvrqlqsmgm rvamitgdsq saarhlaehl
      661 gieefygevl pqdkanivkq lqsqggkvaf vgdgindapa laqadvglal asgtdiamet
      721 adltlthgdl salvtavqaa rktmatirgn lfwaffynil lipvaagvli pwgfqlnpml
      781 aglamgmssv fvlsnslrlk wlrpwvpdsv
//
LOCUS       WP_010638033             499 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Streptomyces albidoflavus].
ACCESSION   WP_010638033
VERSION     WP_010638033.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..499
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=51985
     Region          4..481
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(61,63,67,70,74,107,110..111,120..127,132,135,138,
                     231,235,238,241,243,417,419..420,422..423,426,429..430,
                     432,434..437,446,450,452,466,473..478,480..481)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(147..150,158,173,176,206,223..226,229,247..249,281,
                     382,384,410)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(150,247,278,281)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mktvhhwigg qavdgasgsf gpvtdpatge vttqvalasa devdaavata kaayaswgts
       61 slaqrttvlf kfralldqhr eeiarlitae hgkvhddalg evargleivd lacgitvqlk
      121 gelstqvasr vdvasirqpl gvvagitpfn fpamvpmwmf plavacgntf vlkpsekdps
      181 aalrlaelfs eaglpdgvln vvngdkvavd rllehpdvaa vsfvgstpia rhihatasah
      241 gkrvqalgga knhmlvlpda dldaaadaav saaygsager cmavsavvav gaigdelvak
      301 ikeraekiti gpghdpasem gplitaahrd kvagyvagaa aqgadvvldg tgftvegyek
      361 ghwiglslld kvstdsdayr deifgpvlcv lraetyeegl alinaspygn gtavftrdgg
      421 aarrfqleve agmvgvnvpi pvpvgyhsfg gwkdslfgdh hiygndgthf ytrgkvvttr
      481 wpdpadaptg vdlgfprnh
//
LOCUS       WP_010638025             219 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Streptomyces sp. N1].
ACCESSION   WP_010638025
VERSION     WP_010638025.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. N1
  ORGANISM  Streptomyces sp. N1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces sp. N1"
                     /db_xref="taxon:576456"
     Protein         1..219
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23264
     Region          1..205
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 maqatptaer ayehvkdlil dgtygsgell segqvaaelg isrtpvreaf lrlrsdgfle
       61 lypkrgalvv pvslgegrdi mqarlllesy aldtlaargp ealrrvgddl aarcglaatp
      121 reardaghay haalvaaagn rtvtglfetl whqhqrftaa aligrqevae dtaehlalar
      181 alqhgdaaga kdllhrhigs ilrragadgd slalpdrva
//
LOCUS       WP_010638049             100 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [Streptomyces].
ACCESSION   WP_010638049
VERSION     WP_010638049.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..100
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9596
     Region          33..98
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mtsdtqaqtq tsgsccsgsa tssggcadtg avttvyavtg mtcghcegav seeisalpgv
       61 ssvkaeaatg kvtvtsatpl deeavraavd eagyeltgra
//
LOCUS       WP_010638072             350 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Streptomyces].
ACCESSION   WP_010638072
VERSION     WP_010638072.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..350
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36307
     Region          35..329
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mgaasaepdd lgdspaaapg tgtpgggpga drgestftvl vaaganlgia vakavagiis
       61 gssamlseaa hsvadtvtel llltalrrsa hppdeahplg yaaaryvwal lasvatfvgg
      121 avfaiydgvh tlavgeelgn ptlsyavlgi afllegfslr tgvrqmrgea rrartplrhy
      181 lrhtpdttvk avvmedsaal vglvlaaggl tgahltgspv fdgvasllig lllvyvawvl
      241 grsnvelllg rplpapvrea ihaellavdq vhsvlelttl mqgpdealaa akvdfrdtat
      301 aaeiewacer aerrlrerfp qikrvyldpt pgagqrrreg ldpwgdegeg
//
LOCUS       WP_010638083             404 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010638083
VERSION     WP_010638083.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..404
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=45163
     Region          9..397
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 msaihhypvl rlrakedrrl raghlwiysn evdvaktplh gmipgsvcri edaqgkaigl
       61 ahinphtllc grllsrdphl lideafyqer lhqalrmrek ffsapfyrlv hgegdglpgl
      121 iidryedtlv iqpgslgmdr dialvanalq allhptgill kaggtarrle gledrvevlf
      181 gqvperlqiw endclfemdp rggqktgwfy dhranrrrll syapgrrvld cfaylgafsi
      241 plakagalev tavdssapal alleenarrn avapirimhd dametlarlr drgeqfdliv
      301 ldppaliksk kdfkegsiay rrfndlamrl lapggilfta scshhlnret llgqiafgaq
      361 rgdyaiigeg tqdmdhpihp avpessylkg fyvhrrelia depe
//
LOCUS       WP_010638155             194 aa            linear   BCT 01-JAN-2025
DEFINITION  Uma2 family endonuclease [Streptomyces albidoflavus].
ACCESSION   WP_010638155
VERSION     WP_010638155.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..194
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21830
     Region          1..187
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mtalpdwmrp praegwfaed ldrlpeaprh telidgalvf mmspqrswrg rivtaltvgl
       61 mnqapegvei eremtirlds rnrpepdllv tslpfdadrt wyaptdvslv vevvspesah
      121 rdrtvklrky aeagiphywr vedekgspvv hvyeldaptg tyapvtiard slerpvpfpv
      181 sldlakltpp ltrp
//
LOCUS       WP_010638180             485 aa            linear   BCT 01-JAN-2025
DEFINITION  TldD/PmbA family protein [Acidithiobacillus thiooxidans].
ACCESSION   WP_010638180
VERSION     WP_010638180.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..485
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53331
     Region          12..483
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mlnsghtive nlrtaayraa dllrgfafws vlieessklt tsvrrgvada pereilkaal
       61 itlgsgnnvs yasttdlses glrraitsak sraealtafr lmemacwpta dqkgqwqspt
      121 gaemslkdrf dymraldaam htdtriknrq vvltsmdrqr ffmhsagaeq iqetqlciph
      181 meatasdghe aqsrsyrpyv qgslnaetlt aldftpvaaq rmaaealell lapecptgtm
      241 divlspaqmt lqihesighp leldrilgde rnyagwsfvk asdfgslryg spllnilfdp
      301 gekgelagya yddegtpalp tyliqngilq rplggarsas ragmeavaca rvcdplrqpi
      361 drmaninlqp gqssfqemia qvekgiwmde nrswsidqrr dkfqfgcewg rriengtlga
      421 wvknpnyrgr tlsfwnslaa vgnrdtyqia gtpycgkgep nqaitvghas pvclfrniet
      481 fggda
//
LOCUS       WP_010638201             187 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Acidithiobacillus thiooxidans].
ACCESSION   WP_010638201
VERSION     WP_010638201.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..187
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=20146
     Region          <36..176
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mfaksplkrg giallfltlt lsgcasmapn spssfslpsq ppvqssdyvq haeattldav
       61 lvhaiseigk nyrwggdtpq tgfdcsgliq yvleqagvdi prtsfaqaaa lpsvplsrir
      121 pgdlvffntm gqpfshvgiy iggqqfvsal nrrqgvavqs lqipywaerl dgvrrpmpre
      181 llamrdn
//
LOCUS       WP_010638244             734 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: transglycosylase domain-containing protein
            [Streptomyces].
ACCESSION   WP_010638244
VERSION     WP_010638244.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..734
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=77857
     Region          17..636
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 msrsdegrag rggigrfftl kkllgafftv cllgmlgfvg lylvvdvpeg nadatrqsnv
       61 ykyadgsqit htgsvnreiv gldripkdvq rtfvaaenkt fytdggidlk gtarglintv
      121 sgkgkqggst itqqyvknyy ltsdqtvsrk vkelvialkv dqrmskddil agyintsyyg
      181 rgahgiqaaa qsyygvdadd ltvsqgayla allqapsqyd wavasdrgkq lvkerwryvl
      241 nnmvdqgwld kataaeqkfp vpdepkpapg lagqkgylvn aannalrkql maegasaeea
      301 qtsveaggwt mtlnidkkkq relersvdss lndkldpkar kvdarvqtga asvdprngkv
      361 lalyggrdyi ehqlsnatrr dyqvastfkp lilasalenk attqdgqpvt agtiydgtse
      421 rplegsptpy appneddvdy gpvtvqkamn ksinsvfaqm gvdvgmdkvm ktagdlgmdv
      481 egleavpaqt lgsmgasple magvyatfah hgklvtpavl ksaenrdrtv dlpkavgeqv
      541 ikrstadsvt svltgvvddg tgaavrnpaq dvagktgtsd dnksawftgf tpklvtsvgl
      601 fgedmekkgq qvslygaagg grvngggfpa qiwadytfdv mgtpasfdld tdmgagvapp
      661 pepdpstppe peestpveps tpaepsdept seeptdpeps deptggpsip eppeesppgp
      721 elptiepgap geee
//
LOCUS       WP_010638276             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010638276
VERSION     WP_010638276.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..224
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23590
     Region          17..>120
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matrerrper rqeplsreri vdaavelldt agergltfra laerlatgpg aiywhvtgka
       61 ellaaatdav iapavapada eatpeqairt lalgifdald thpwvgpqlt lterhspllr
      121 vfegigrqvq algvpesarf taasalmsyi lgvagqnaag srsvppgtdr aahlgavads
      181 waeldpghyp ftrevagqlr vhddeaefla gvdlilggia aglr
//
LOCUS       WP_010638306             520 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [Streptomyces].
ACCESSION   WP_010638306
VERSION     WP_010638306.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 520)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14291541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..520
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57526
     Region          86..457
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
     Region          240..397
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            order(281..283,299,301..302,335..336)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:410865"
ORIGIN      
        1 mpnyreslgh lesfvsarvp lialrtmeqq ralrllreia ssprrsslpf tlytratglr
       61 dlrtnaavle drsltgamdy aasqfagrtn atvvfvepee leddsaytrh faelarlade
      121 nmgsvvlvtd tpvwsglqrl gmtlqldlpd eeerygiisg fltdhrdvip iawteqdarr
      181 aaeflsgtte gecvnlmatv aakgaiepdd vlglarakdr ifsdltglek vplgegeysv
      241 ggltslrkwl rrkeqllhed lrgtglrppr gvmlvgvpgc gkslsakaia sewrlplyrl
      301 dmasiqgkyl gesegrfrea lamadrvapc vlwideiekg lagkddingv qqriigqfly
      361 wlqesssraf vvatandirs lppellrkgr fnelffvdlp daedrreiiq lyhrrylgra
      421 aepheldqla dlsegfagsd ieaalhevge eahlqggldr lppglagdtf antvplsrtn
      481 peqieeiraw greralpagr gggtgegrrp arrrivfadd
//
LOCUS       WP_010638336             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Streptomyces].
ACCESSION   WP_010638336
VERSION     WP_010638336.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..262
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28411
     Region          1..247
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msqtvdrals ilpllaegpa dlgkvadrlg vhkstalrll rtlhehglvh rqadqryrlg
       61 arlfalaqea venldireia hphlvalndc cghtvhlavh eehevlyidk vesrypvrmy
      121 srigkpvait vaavaklila dlpeaerrtl aerldypqyt prstpnaaaf lkelarvreq
      181 gwatdlgghe esincvaapv rgpdgrvvaa msvsapnvvv taeellallp vvrrtadais
      241 reysgsapad qatphqgngk tp
//
LOCUS       WP_010638337             686 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Acidithiobacillus].
ACCESSION   WP_010638337
VERSION     WP_010638337.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..686
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78039
     Region          1..496
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mftlrdyqen gvqhlledae akigsvgifp tgagktvvlr emirrwlrdh peqpvlllah
       61 rtrlltqaqe kfagiptnvi sagmglreep lpgavtvasi qtistlpfaa enypwslvli
      121 deahrvdedn qygqflkrlp ettpisgvta tpwrwekgqh vpiwekgltg ifqrpacwvh
      181 pepliqqgwl lrpemvpiqh tfprigkkle hgefpaakis eylkmdfeqr iqeiqdkthg
      241 cdhvlvfcas iqdaekvsda lrqrgetsmv lhgkhaeter naeivrfqqk ktrylinvdv
      301 ftegldvpei davvmlrmtr svirylqmag rglrpaseeq hhcrildfgh hverlgpiea
      361 ergrngmpvy rsrqriqesa pesgkaspsa mdnmntaprf teseasfcva vqdlqlipas
      421 trngknflvm rfqvdhpean qdrfrtlrve rklfegdpvm ktllyrwqri sgerkyvkge
      481 sqiqrllamf ysgrgflpyv pfavrvrwsg raekwmvdgw qwsgkqkmdi semeekalaq
      541 wiqktqntpd aqdqvlrqvl yrlshegvld lrvetqaalk meqveqvkkv erpeavektl
      601 tadpapeqei ysgfsdssss peslpfydgp pvewvvyske gavldhpvap ahpsapvrps
      661 admsvrempm erpqsaewtg pkgqsa
//
LOCUS       WP_010638377             177 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DinB family protein [Streptomyces].
ACCESSION   WP_010638377
VERSION     WP_010638377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Newton,G.L., Leung,S.S., Wakabayashi,J.I., Rawat,M. and Fahey,R.C.
  TITLE     The DinB superfamily includes novel mycothiol, bacillithiol, and
            glutathione S-transferases
  JOURNAL   Biochemistry 50 (49), 10751-10760 (2011)
   PUBMED   22059487
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Cheo,D.L., Bayles,K.W. and Yasbin,R.E.
  TITLE     Cloning and characterization of DNA damage-inducible promoter
            regions from Bacillus subtilis
  JOURNAL   J Bacteriol 173 (5), 1696-1703 (1991)
   PUBMED   1847907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..177
                     /product="DinB family protein"
                     /calculated_mol_wt=19182
     Region          27..173
                     /region_name="DUF664"
                     /note="Protein of unknown function (DUF664); pfam04978"
                     /db_xref="CDD:428232"
ORIGIN      
        1 msgivvpvdg laervsppvn gsereslrgh ldfhratlla kcagltteql rtkssppsal
       61 sllglvrhma everawfrrt fageeiglvw spegdfqvay daaradagea favwraevah
      121 arrieaaaas ldetawsprw eaevslraim lhlihdyarh nghadllreg vdgavgv
//
LOCUS       WP_010638413             203 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PH domain-containing protein [Streptomyces].
ACCESSION   WP_010638413
VERSION     WP_010638413.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..203
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=21487
     Region          66..133
                     /region_name="bPH_6"
                     /note="Bacterial PH domain; pfam10756"
                     /db_xref="CDD:431475"
ORIGIN      
        1 mstpqssape prtyrstasl vagalllalg awfgvdaiwr gsgrtpwlal aalvllvplv
       61 vaytlrpavv sdedrltvrn pfrtvtlpwa avaelrsgft nevrsdgrty qlwalpvslr
      121 arkkaaraqm rdavadphga tpttvsqptr sdsdqavedl reiaerraaa pgaqgpavvr
      181 wayeiiapaa vgaialvvlv atg
//
LOCUS       WP_010638492             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Acidithiobacillus].
ACCESSION   WP_010638492
VERSION     WP_010638492.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..220
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24093
     Region          4..220
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mnenslilsg isksfpihhg rdmrlilddi sleihpgerw gimgpngagk stliqiisgs
       61 lradagtvhr gmtvswplaf ggafqgsltg rdnarliarv ygadvketva qvedfaelgi
      121 yldepvksys sgmnsrlsfa ismavdfdcy lvdevisvgd arfnrrcede lkrratkamv
      181 lvshhsdlil gncdhaaile ngrlrviedi neavhyytnm
//
LOCUS       WP_010638494             251 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010638494
VERSION     WP_010638494.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..251
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28102
     Region          64..>163
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
ORIGIN      
        1 mlpdsnadwq hiarerpyfg vlseaayaep alsdaqlaqf ldsgqryvnm vldqctrffg
       61 anwqtgsald fgcgvgrlsl plarrfgqvt gldvapamls earrlaqlan lhnvhwllad
      121 dhlsgiagaq fdfmlsfivf qhipeargqr llqqllthla pggmavfhfk yaqvmprhpw
      181 stflshhvpg grwlvnalrg kplkephmqm naynlnrlvq sfqeagiqei htrledhggh
      241 wgvemyvrrg a
//
LOCUS       WP_010638504             339 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Streptomyces].
ACCESSION   WP_010638504
VERSION     WP_010638504.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..339
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37727
     Region          1..217
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mvklsvivpf ynvrqfapdt lrslkanard dvefllvddc ssdgtrdlle raveevpgav
       61 llphevnggl atarntglda argtyltfld gddwyapgyc gqlldaaerl gtdfvrvdhv
      121 qvtgrarqih rmphgrrevp lrpldailpa drstsvdypy awagiyhrrl ldsgvlrfrd
      181 glrtaedrpw iwrlhreaes favtslygvf yrrgvssslt qigdvrqldf lrafdqvvee
      241 taahaqaael lpkairtyca vmahhlesie rfepavartl raesaaalgr lpqdilrstl
      301 salgpdraar lrrvrrhqal rpgapaavpa trvheeaar
//
LOCUS       WP_010638524             217 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YidH family protein [Acidithiobacillus].
ACCESSION   WP_010638524
VERSION     WP_010638524.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..217
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24378
     Region          92..213
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 mmflkrlptv qeprlymale rtylgyfkll fvsigtglvs arlavlflal hyaklghfft
       61 elfnvltwpa ialvfvvgln fmfdlqhiek gppvaakeii dpriymaaer tflawvrtgi
      121 gliafgfvie kfdffleqls imlhtklvmg egfsgmgiif ivlgitnlmi gginfirtvk
      181 kvdegcyhvh kflyglygvi lfgitvalav miirvsl
//
LOCUS       WP_010638553             152 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Streptomyces].
ACCESSION   WP_010638553
VERSION     WP_010638553.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..152
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16105
     Region          12..146
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mtesvvlrrk afrlprhpas vgearhrtgg hlaswghppr saireetvll vselaadtvl
       61 hgprdepdfe vavtvlahgs clvevsdgip deavlptpdp dqtpgaptpt tppdpllpgh
      121 artlvtavse awgvrdrgry gktvwalatv na
//
LOCUS       WP_010638541             367 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Acidithiobacillus].
ACCESSION   WP_010638541
VERSION     WP_010638541.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..367
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39811
     Region          11..364
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mtdrtqsvqr wlpilliava liwilqdfws alawsavlsv vfwpfvarip grwrplgalf
       61 faltaaslil lplafvilev lrglhllgpw isgeelshwa lpawmsqhlp lilldplrhl
      121 wrvatgwlga flpgisaksv llaphftglq vlsgsdalla hgqmvlnvlg gaedtafnas
      181 lallllfffl lhgetlaqgl aervtglaga evwkvvsrgl dilrgtfwsv vitglfeall
      241 fwalyaacgv phaliwgtvs gvfsvipfga savftgvtlw vwlaasepll alvifiagni
      301 ittladnllk plliggrsrm pfmlifmgli gglsvlgilg ifvgpmlmgm lmawwqgwkr
      361 ddaeqss
//
LOCUS       WP_010638561             246 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HAD family hydrolase [Acidithiobacillus].
ACCESSION   WP_010638561
VERSION     WP_010638561.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..246
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28866
     Region          3..234
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 msiravcfdl ygtlinietn edmeeiyrgi shyltyhrvf mnrrevrery favmkerkrq
       61 sterypeidv eaiwhtiliq enskplngre klakelarlh rgisrtrler yegvkrtlks
      121 lqeqyqlali sdaqrcfalp emralnikky fdiriisgdy gyrkpdsrlf qmaaeqleva
      181 phqaiyvgnd mfrdiygaqq agmktifvds nqgaksyndi qpdyfahdfy qvldgvafla
      241 qkhadn
//
LOCUS       WP_010638607             242 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010638607
VERSION     WP_010638607.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..242
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26231
     Region          16..234
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mseihsewlq lengprawya rpggngphpg vvifieafgv nshfqevaer fakagycaiv
       61 pdlyhgkvye yadfenaigh lktlkddlam qeaglaiael qkrpevmkha igavgfcmgg
      121 rfafmanavh adkigasvaf ygggiapdkd pagrqpllhl veqmraplll lygaedqsit
      181 peehgriaaa lstakkrytl tlfpgaphgf fadprdsyrp eaaaegwhlt ldhfsqhlgg
      241 qa
//
LOCUS       WP_010638701             368 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Acidithiobacillus thiooxidans].
ACCESSION   WP_010638701
VERSION     WP_010638701.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20324114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..368
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40278
     Region          10..>66
                     /region_name="MlaB"
                     /note="Binding protein subunit MlaB of the ABC-type
                     intermembrane phospholipid transporter Mla, contains STAS
                     domain [Cell wall/membrane/envelope biogenesis]; COG3113"
                     /db_xref="CDD:442347"
     Region          118..362
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mtdhnpqepr wqlqeqtitl sgrwtlrrlg gsfarqqkml snihadllwd lrnlealdsa
       61 galllwqvwg nrfpekiqln dlhqaiftrl adlqplthpp rrpfqildal gaflvetggd
      121 lwgifllmga lllefgrglr hprsfpwrei sativstgps slpiltligf ligvvisfqs
      181 astlaqygan iyivniagls ilrefgplit aiilsgrsgs aftaqigamr vteeldalrt
      241 fgippirrlv lpkvialalv vpllvlwtdm vgilgamlva kanlgisyhf fiqempvavp
      301 sfnlwlgiik gavfgiliaw iagfhglkvk pnttslsret tnsvvfsitl vilidailal
      361 vfantgis
//
LOCUS       WP_010638724             627 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [Streptomyces].
ACCESSION   WP_010638724
VERSION     WP_010638724.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..627
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=66197
     Region          29..560
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
     Region          <537..624
                     /region_name="PHA02030"
                     /note="hypothetical protein"
                     /db_xref="CDD:222843"
ORIGIN      
        1 msqessaqsr dvtpepaaaa pptdgegydy dvlvvgsgfg gavsalrlte kgyrvgvlea
       61 grrftratlp rnswdlknyl wapalglfgi qrihllgnvm vlagagvggg slnyantlyv
      121 ppkpfftdpq wgaitdwqde lkpyydqaqk mlgvrlnptt tpsdvhlkaa aekmgvgdtf
      181 hmapvgvffg dgkdatgesr akpgeevpdp yfggagpsrr acsecgecmt gcrhgakntl
      241 nenylylaek agatihpmts vvavtedsrg gfavrtlptn akrkgrgrtf tarrvvlaag
      301 tygtqtllhr mkdtgllphl sdklgtltrt nseglvgaqt tdrryrkahg aekadftkgv
      361 aitssvhpnd sthiepvryg kksnamgglt ilqvpyaens srvagflanc akhpllvvrs
      421 lsnrrwsert iiglvmqtld nslttyrkpk gigkglltar qghgapnptq ikeageaata
      481 iaaeingfag snigelmgtp ltahflggcp igatadegvi dpyhrlyghp gitvvdgsav
      541 sanlgvnpsl titaqaeraa slwpnkgead prpaqghpye riapvapvrp avpakafaal
      601 dlpflgmpam pprqrpadap agpgega
//
LOCUS       WP_010638728             560 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: serine/threonine-protein kinase [Streptomyces].
ACCESSION   WP_010638728
VERSION     WP_010638728.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..560
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=60264
     Region          72..322
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(72,96..97,130,135,140..143,155)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(79..80,82..85,87,100,102,138,154..157,161,163,199,
                     201,203..204,206,216..217,220,237..240)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(79..80,82..85,87,100,102,138,154..157,161,201,
                     203..204,206,216..217)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(83,161,163,199,201,203,220,237..240)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(216..224,233..240)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mtnnggqqnd ptsydlrppq qpppprqgep spagqygypp aprppepagp npyatpappa
       61 adpgagrvvg gryrlddrlg hggmgtvwrg fdlvvhrava vkeprlpdql seaerenayq
      121 rmhrearaaa riehpavvtv hdvvveegrp wvvmelvtgq slgdrlqdgt ldareaarig
      181 lavlgaleaa heagvlhrdv kpdnvllgkg drvvltdfgi aqvegeqglt etgafvgspe
      241 fiapervlgq qpgpasdlws lgvvlyaave gvspfrrsht patlqavlsa dpatpsrapg
      301 algqvimqll rkdpafrpgp aevrqaltal aqpaaapatr llgsgpgtsq wlppamqrsp
      361 kakygvlggl vavvlvlvli avnpfggglp edwvsrpeae tvaadigvpk eykrsasdsd
      421 dtsvrfedps gvffvyverv drkektssld ekplapsasa wkryyerggs deseieeakv
      481 tttavehqgr rdsfetvvdh yrygeadded alrrryhelv vpgedqvywr lrvgmpgagk
      541 alddgeelfr titenftvql
//
LOCUS       WP_010638871             482 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010638871
VERSION     WP_010638871.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..482
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54458
     Region          8..448
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 miiedtlpvl lsrldfafit smhilwtpvt igmswllffl evawlktgne hwyrlqrffe
       61 klfivnfggg vatgvtmema fgilygpfsq avgpffgnil gfetitafmy eagfiglmif
      121 gwgkigkgmh afatfnvals sslsamwilv angwmqsptg iqlkdglfqv tnwwqaifnp
      181 nfnigfphmw vatvelalff faavsawfil knrqanlftk llkptllali iitplqifig
      241 delgrevahd qptslaameg hfhtylpdgk pntswnliai pdvsagknlf siqiphvlsl
      301 lethtwdgvv tgmdhfapnd rpnvwvpfya frvmvaigff lffmalwgnw lrlrgkltae
      361 hlrknplflr llvfsgflpy lavwtgwwtr eigrqpwvvy nlmrtwqgvs hmgvtaesfw
      421 ligyiifelm vwggawyfft rviqkgpdmt spvigasdhd ahpsgggiak ptfakptmnk
      481 ln
//
LOCUS       WP_010638927             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Streptomyces].
ACCESSION   WP_010638927
VERSION     WP_010638927.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..157
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17287
     Region          15..156
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mtsatppvpp vhwklvvdaa dphaqalfws aalgytiedn daliarvlsf ggapeeatve
       61 fqgrrawrdl iavrhpddpf dkdtgigegr rilfqrvpep ksaknrlhid lhsgdrpres
      121 evqrltelga tverevaeag gtwvvmrdpe gnefcvn
//
LOCUS       WP_010638965             262 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Streptomyces albidoflavus].
ACCESSION   WP_010638965
VERSION     WP_010638965.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..262
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=26135
     Region          49..261
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 malragvagg vlstiavags anaataaepv tetiemptlt aaltskaals aeatqqaada
       61 yqyraeqqsa aekavkdakk ahkaaekkae aaakkkaeer aaaaeraars aertdlsgvq
      121 taaatssssg ssasapsqdv papasgsvas visflqaqvg dayvmggtgp nswdcsglvq
      181 aafkqvgvdl prtsqeqsta gtqvgtsnlq vgdilywggq gsayhtgvyi gdgkyldaan
      241 pskgvviqdl sgypadgavr vl
//
LOCUS       WP_010638993             335 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [Streptomyces].
ACCESSION   WP_010638993
VERSION     WP_010638993.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..335
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35346
     Region          78..290
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mshplhlaag aldgmgglfs lpvlyalgcg lavgggiall vtairglpak pehekakage
       61 raaellrfag qrgslaagvg lvvllvtrwa vagiaagvlv ffwdklfgga aeeraamrrv
      121 ealaswtesl rdtiagavgl eqaipasara aapvlrphld alvdrlrsrt plpealqhla
      181 deiddasadi ivaalmlnar lrgpglrqvl galaksaree vdmrqrvmaq rsstrrsvqi
      241 vvavsvafvl glavfnrdfv apygtpvgqa vlacvcglfa lgfwwlrkls tietperflv
      301 rdqpavqqfv rprtpdapgq aapygaapeq egtrr
//
LOCUS       WP_010639041             449 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dicarboxylate/amino acid:cation symporter
            [Streptomyces].
ACCESSION   WP_010639041
VERSION     WP_010639041.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..449
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=47045
     Region          58..436
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 msaqnpasep spedaqarga geprtgsrip kipfwaqilg glvlgvllgw larsqqidwl
       61 vttleqvggv figllklava plvffailvs itnlrkvnna arlasrtllw fmitsliava
      121 iglviglvtn pgagtgltpk dgakpentgs widfltgiip tdvitpftel nvlqivfmaa
      181 vagiaalqlg ekaqpilals esvlsllqka lwwvirlapi gtvgligsai atygwdligk
      241 yatftadiyi gcaivlfgvy plllstvakl npvqffkgaw paiqlafvsr ssvgtmpvtq
      301 kvterlgvpk eytsfavpfg attkmdgcaa iypaiaaifv aqifdiqlgl tdylliafvs
      361 vvgsaatagl tgatvmltlt lstlglpmeg vglllaidpi ldmirtatnv agqalvpvlv
      421 sarenildrt aydnatsfel dakeapaaa
//
LOCUS       WP_010639104             159 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peroxiredoxin [Acidithiobacillus].
ACCESSION   WP_010639104
VERSION     WP_010639104.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..159
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17294
     Region          12..153
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(46,49,124)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mssekiavgq dapqfhaaay gkdseirlrd lngkivvlyf ypkddtpgct tegqeftaly
       61 pdfqaagaev lgvsrdslas hekfackfnf pfplladtde alctafdvlk eknmygkvsi
      121 gverstfvid rqgkiayver kvkaaghaaa ildivkklp
//
LOCUS       WP_010639125             741 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010639125
VERSION     WP_010639125.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..741
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=84304
     Region          640..738
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mgiwrclhpr llfqenltli lgsllflmgm gitigfslst qakpqasqav ftmillpaff
       61 ivagflihyw riisedllri lpgfrrqaig ifvfililll viiagemrfs niplagafil
      121 tvyvafwaaf yaillntggs rrkdrkywqg fpllpvypli ffppardvfl aipapvdsvl
      181 gilllllivl lmrktprewq eflsaylhrp qdiriqnisw sapwrwmpgn whnpildtar
      241 rpqgilavlf iqplfpaali alqflrvgts hwpqvlpflp vifllpvlsw gnwsarafdw
      301 qyltltgyfg gnhqqasthi vksyaahtsl lalvllfwpa lilillgypi lqismillil
      361 ymgilvlawa pmgiiglgft gilqqiilll sfgldavlvl rsahywfyrh lihvpfhlrg
      421 tlvlmfmalv svgfaaylar qrlsrsdwnl sqfsaqkirq tgqkytlsae nnkqrttrks
      481 lsthwgpwaa iilflsfffg qaiiviimvm lrdfvvgaql gmhyallhek mpplvleksl
      541 hqisttfriw lgilsytlca lailifllmk fprevwrkae gfawrkpsrp yayllalila
      601 ilielfahgl fqifplpshl npralglfeg lkgsglthyv vlllliviap faeeiifrga
      661 iyaglrrrfs agwsalfvsl lfvlahipsk ieqfhyppal iiiallaaal iflriryrsl
      721 wpgillhmvw ngsgfllllw h
//
LOCUS       WP_010639129             468 aa            linear   BCT 01-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Acidithiobacillus thiooxidans].
ACCESSION   WP_010639129
VERSION     WP_010639129.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..468
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=50306
     Region          4..423
                     /region_name="ASKHA_NBD_FGGY_SePSK_AtXK1-like"
                     /note="nucleotide-binding domain (NBD) of Synechococcus
                     elongatus putative sugar kinase (SePSK), Arabidopsis
                     thaliana xylulose kinase-1 (AtXK-1) and similar proteins;
                     cd07783"
                     /db_xref="CDD:466801"
ORIGIN      
        1 mptylgidfg tsglrgivid enlntiasaa lpypgcpses ltdsqgwlqg lemlaqqlrs
       61 ihtrawsaik amsldgtsgt lllsdrrdnv lgpvlaysdq raaaqaqqlk qqwpeggicl
      121 spasslskll wlrchlhnfs eahyvhhqad wvaahltnhw gisdrgnvlk mgldaqhmky
      181 pekmlnilkt adidpailpk vvhegisigt ldkswaqrlg lstavqirag ctdsvaaata
      241 aglympgtal sslgsslafk vvhgkpintm glyshylgdf clvgaasnag asillqhfqr
      301 eqmralessl hpaypsaall yplassgerf piqaptwpgs tipsgqnaet fqmlleglsy
      361 ieawgydvme kaevsiqgpi ktvgggsmna awmqmrahil nrpveitvdt eaakgsalia
      421 aaadlgglki lgqtpvqpgr ifypaadave ryapyvqkfq ekfsrfsd
//
LOCUS       WP_010639153             310 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010639153
VERSION     WP_010639153.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..310
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34622
     Region          26..285
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mstdqkegqq cfgkkedgpr plpharrgfv lrfgfrwyra whgfwkddci dragllsytt
       61 lfgliplavl vfsmwnlvgf svmhrtqvdr lilrsfvpqt gytilhevnl laakgaqlgl
      121 lgviglslta vfllhaverh lnaiwgvaph cwwcrvlryl amlvvaplsv alllpllgpl
      181 qpllkylghi pvlppffshi ltflvvtvmm lllykilpaa aprwrdallg gmtvaflfel
      241 dkfglsaylr fstfetvyga lgafpvfllw lymawasilf gaemaeagvy sdqnalnpah
      301 kpaapvktdk
//
LOCUS       WP_010639173             227 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Acidithiobacillus].
ACCESSION   WP_010639173
VERSION     WP_010639173.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..227
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24872
     Region          18..215
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mvlneniwpe glwiraaaqq eapcimlmhg lgaskedlap ladfvdpekq frwvlpdapv
       61 rpvtlnggrp mrawydiygl grdsgedaag mehmatrlaa lmeheqqqag tqplilggfs
      121 qggamalyla fhhacpaaav lafsaylplr qtlpqsaqvt pifwghgrsd tvlpleymei
      181 ardimeslgy alsthiypmd hsicavelvd arkfldsivm qgnlkks
//
LOCUS       WP_010639352             333 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010639352
VERSION     WP_010639352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..333
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34230
     Region          3..315
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtvlsvrglt vrfrmresap vravtdvsfd laageclalv gesgcgksvl asallgllpg
       61 naetagsall agagddpatd liaadeatla rtvrgrrvgl vpqspaahlt pvrtvrahlt
      121 etvrrltgtr grdalrtate aaaarvsfpa ghldrhphel sgglaqraat alalvgdapl
      181 lladepttgl drdlvdrtvd elrrhtgatr allmithdla aaariadrva vmyagrlvei
      241 adadaffgap gprhpyargl ldalperafr pvpgrppela alpagcafaa rcahadtaca
      301 tqppltggla chhphtapad lvhppqaaea pga
//
LOCUS       WP_010639358             373 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces albidoflavus].
ACCESSION   WP_010639358
VERSION     WP_010639358.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..373
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37572
     Region          10..366
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msatpsllat eteddlraav rslltthsaa drvlaraesg apydrelwkt ltgsmglagl
       61 lvpeadggqg aghreaavvv eelgravapv pyltgavvtp atllalpert aevsallaev
      121 aagsavavla vplttapgdp lpevttdggg lhgtvrsvad aagadvllva tdsglyavpa
      181 gapgvtvtpl taldltrpla avqldgaqgt llapaadaap avragllsga gllaseqlgl
      241 aewcltetvr hlkdrhqfnr plgsfqalkh rlaqlwldva girpaataaa dllatgeggp
      301 aeaqlavava qvyaspvavr aaeealqlhg gigmtwehpv hlylkrakgd svafggagrh
      361 gqevarlael pap
//
LOCUS       WP_010639385             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Streptomyces].
ACCESSION   WP_010639385
VERSION     WP_010639385.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31974
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mftlsqlesf vavaetlhyg raaerlsmtq pplsrriqll erelgvelfd ragrsvrlta
       61 agqaflgdar rilglseqaa lsvrrtlege vgtvalgfta saahsvldgi vgavhaelpg
      121 vglvlrervs gaqleelrsg eldlglvrpp vpgtgiahhp lhreallvav paghplaapd
      181 raphisdldg epfvmyspae aryfyevlvg vfrraevvpr yvhylsqvht ilalvraelg
      241 lalvpraaea lkldgvvlrp vvgvegepve lvaawragdd npalhavrdv vtgladrgaf
//
LOCUS       WP_010639467             433 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Streptomyces].
ACCESSION   WP_010639467
VERSION     WP_010639467.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44934
     Region          21..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(31..32,35..36,39,71,126..127,129..131,134,154,
                     157..158,161,234,237..238,241..243,246,268,272,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mkstfaavlp dlspwrssrd frllwgqgli tffgstmalv alplqikelt gsplavgamg
       61 avelvplvvf glyggalada vdrarvivst eaglgllali llvnsmlpep mlwplyvvaa
      121 gvaalaglqr paldsllari vpheqlaaaa alnalrwqag aiagpaaagl vvayagnvpa
      181 yattvtcfav svlmclrlsp appsenaakp slrgiaegar yawsrpvllg tyaidlaamf
      241 fafpntifpf ladeldadws lglmyaagsv gsllvsltsg wasrmrrhgl lvvfgatgwg
      301 laiaaagwms nvwlvlvcla lagagdmlsg lgrstiwnqt ipdglrgrla gievlsysig
      361 pqlgqvraga magwtgarpa iwtgglacvv svglltaalp klvtydahtd edarrrreah
      421 tpksageevp dat
//
LOCUS       WP_010639515              66 aa            linear   BCT 01-JAN-2025
DEFINITION  ferredoxin [Streptomyces albidoflavus].
ACCESSION   WP_010639515
VERSION     WP_010639515.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..66
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=6821
     Region          1..62
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mkvtvdqekc cgagqcvlia pevfdqrded givvlldaap paalhgdvre saevcptaai
       61 evaqee
//
LOCUS       WP_010639639             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Streptomyces].
ACCESSION   WP_010639639
VERSION     WP_010639639.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..161
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17199
     Region          17..147
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mnarfplfen alstrfakrf fgaaqvilqs plphstqelv slrasqingc ghcvdmhtke
       61 ataagesatr lhlvatwres tvfteaeraa lalaeegtrl adahqgvsda tweqvrahyd
      121 ddqiaalvcq vavinaanrl avivrqpggs yqagmlaaad l
//
LOCUS       WP_010639704             224 aa            linear   BCT 01-JAN-2025
DEFINITION  urease accessory protein UreF [Streptomyces albidoflavus].
ACCESSION   WP_010639704
VERSION     WP_010639704.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..224
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22348
     Region          2..224
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 msraallvla dgrfpaggha hsggaeeavg agrirdaadl gafcrgrlht aglvaaalaa
       61 aaadgtdpla ldeaadartp spalrtaarr lgrqlmraar aawpdpalda lavarprgah
      121 qpvvlglaar aagltpldaa haaayesvsg patatvrlls ldpfdatavl arlareldqv
      181 aaraaeaarr categpdalp aasaplletg aeahaarpvr lfas
//
LOCUS       WP_010639745             164 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010639745
VERSION     WP_010639745.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..164
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=17971
     Region          1..138
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mivkvqkedf elsaacaema tvngagalvt fvgtvrdysd asdilsleie hypgmtekel
       61 ervsmqaana ydildsliih rygllqpqdn ivlvavwsrh raaafdacrf lidvlktsap
      121 fwkkeitpqg srwvtdcpgc ragsreghsh svpsahpdrq llss
//
LOCUS       WP_010639803             492 aa            linear   BCT 01-JAN-2025
DEFINITION  amidase [Streptomyces albidoflavus].
ACCESSION   WP_010639803
VERSION     WP_010639803.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..492
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51514
     Region          4..492
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 meyaeyrahd avglaalvag gevsaaelle vavaraeavd gklnavvrpm hdlarerart
       61 pltgpfagvp flikdlsqdy aglptgsgsr slahlpaerh savverwlea glvifgktnt
      121 pefgakgite pevngptrnp wdltrtpggs sggsaaavaa gvvpmagand gggsiripaa
      181 ccglfglkpg rglvpagpat aedlhgaatn gavsrtvrds aalldvltar pdpggpylaa
      241 rpelpyaela rrprplrigf ttrspigtev dphavaavde takllarlgh evepaepeid
      301 hrqlaldfla mwttqlaqtv deirratgag pgdfeldthl laaagrslpa pryfaahqrw
      361 ntysrqlaaf herydllltp tlarppvrig eldtpapvra laralmkagl lgtlagtkaw
      421 eravianlaa tpytqlanit grpamsvpty rtpeglplgt qfvgplggeg tllalaaqie
      481 aeqpwaqlep el
//
LOCUS       WP_010639859             441 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010639859
VERSION     WP_010639859.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..441
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48094
     Region          1..416
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mahvvilgag tggmpaayem rdllgpkhev tlisenpyfq fvpsnpwvgv gwrqreqivf
       61 diephtsrkr infiaqradr idperntidl angssvhydy liittgpala fdavpgsgph
      121 aghkkathsi ctvdhaekay aaymnlldsn npdpiiigam pgascfgpay eyamivlsdl
      181 ekrgarskik efhfitsepy vghlglggvg dsqeiltrgl gemgvqvhtn mnttkvddgk
      241 mfcehlnakg ekigvgthdf gfsmmlpafk gvdavakvpe lcnpkgfviv dehqrspkyp
      301 niysagvcia ippveqtpvp tgapktgymi esmvtalvhn iqaeiqgkap taemgtwnai
      361 cladmgtsga afvalpqfkp rrvdwfgegp wvhwskiafe kyflakmkag vsepfyeklv
      421 fqmlgisrlk sdepthlrkv g
//
LOCUS       WP_010639816             314 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tyrosine recombinase XerC [Acidithiobacillus].
ACCESSION   WP_010639816
VERSION     WP_010639816.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..314
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=35337
     Region          1..302
                     /region_name="xerC"
                     /note="site-specific tyrosine recombinase XerC; Reviewed;
                     PRK00236"
                     /db_xref="CDD:234698"
     Site            order(138,152..153,228,230,248,283)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271175"
     Site            order(152,248,251,274,283)
                     /site_type="active"
                     /db_xref="CDD:271175"
ORIGIN      
        1 mlmqeavtdf tetlarsgrs spatvaayhr dlqgwlhfmq srghqdiahi qpgdlraylm
       61 aersrgvavr slrrrfaalr alyrhlqqas pdlsnpvqgi mmpkseqrlp dwltvdqakq
      121 lmdpvekpst apnfaqsrdq lilellyssa lrvselagln lqdldrhggt vrvmgkgske
      181 rivpagksvw rmldlylplr hallvdkhll eenalllnaa ghrlsvrsiq irvkemgekr
      241 lgqhihphtl rhsaashflq sagdlravqe ylghagiatt aiythmdyqq lahvydaahp
      301 rarhtkrpet edkl
//
LOCUS       WP_010639872             304 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010639872
VERSION     WP_010639872.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..304
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=31787
     Region          12..291
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 melflpiahm dvniwlivsf glavgflsgl tgvgggilit pllifigvpp lvavgtgaaq
       61 ivggsaigsy ahwrmgnvdm rmafvllags wtggligvhi arileagghf glvvtflyvi
      121 llgvigtsml iesllalrgw hghasqknrt knqsilqrlp gqmdfpvsgl rlsfltpvll
      181 gfgvglltal mgvgggfvmv pimlyvlkmp tkvvvgtslf qllfttaevg ilqagmnhav
      241 dpylalalvl gsifgtqfga ragahmkgeq lrlvlalvvv gvaikmglgl fiapehifsm
      301 arvv
//
LOCUS       WP_010639880             281 aa            linear   BCT 01-JAN-2025
DEFINITION  CinA family protein [Acidithiobacillus thiooxidans].
ACCESSION   WP_010639880
VERSION     WP_010639880.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..281
                     /product="CinA family protein"
                     /calculated_mol_wt=29751
     Region          138..267
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mnsgellhif lpmrpavlpd aqrleawalr sgvrarielt avlpdiegaa lgigafanaa
       61 awkvipqral vpagdwqglr dwaehylppy pqsfshfsdq sqgteilpge fwlqekisda
      121 fdlsmappew allqhcpkag gprlalaesc tggglaarit alsgssallq hgivtysnta
      181 krhflgvqak tlmrygavse etalemlngl lreadlgvai tgiagpggav pgkpvgtvci
      241 awgqrngqqq vrtchfrgdr wnvqyasgsv alggllgllc g
//
LOCUS       WP_010639925             431 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Acidithiobacillus thiooxidans].
ACCESSION   WP_010639925
VERSION     WP_010639925.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 431)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..431
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48864
     Region          <236..424
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 meqllqkwek lptrqvktsl eetnhgasee vncegwqklf ktvirhsird qdppgallle
       61 qldgllneke iqadalfpla rdilqhqqel dekeikirkg lqellqlllr nvadlldnda
      121 flsgqmdvvr qavqladnhe eldlaihrvk evifqqgklk sevreareai rdlvnlvlms
      181 vesmagengr nhqqleslvn eldsttdwqq irkivskvln tsknitkqsi earntliqak
      241 nrlsaaqeki rkleeemesi sqlvhvdplt gtlnrrglna aflresaraq rlnqpltvai
      301 vdidhfkkvn dqyghdlgdq vlrgmakvlq dtlrandvit ryggeefvil mpdttpenal
      361 dilervqlql grqlfqaqdr plkisfsggi svwqnscsqe qsiaaadkam yrakkdgrkr
      421 iyladqanss t
//
LOCUS       WP_010639996             187 aa            linear   BCT 01-JAN-2025
DEFINITION  Uma2 family endonuclease [Acidithiobacillus thiooxidans].
ACCESSION   WP_010639996
VERSION     WP_010639996.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..187
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20894
     Region          1..184
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 msactehrsl seteyldaea ladvkseyla gevfamagas erhnriagni ffhlravsrg
       61 hpcrafmadl klristhqay yypdamlvcd pednyplyks apcflaevls paaaaidqre
      121 kwlayrdiha lryyllvdse rvyarlfsre gstwgeqild pgdilqldcg glsislsldd
      181 lyedsgl
//
LOCUS       WP_010640066             213 aa            linear   BCT 01-JAN-2025
DEFINITION  class II aldolase/adducin family protein [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010640066
VERSION     WP_010640066.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..213
                     /product="class II aldolase/adducin family protein"
                     /calculated_mol_wt=22755
     Region          57..207
                     /region_name="AraD"
                     /note="5-methylthioribulose/5-deoxyribulose/Fuculose
                     1-phosphate aldolase (methionine salvage, sugar
                     degradation) [Amino acid transport and metabolism,
                     Carbohydrate transport and metabolism]; COG0235"
                     /db_xref="CDD:440005"
ORIGIN      
        1 mntantseeg vtkfllhwtp aaapdqreit tlqdwrdvff arqligadpq ryggigfgnv
       61 scrspqgflv satqtgglpt lsahnfctvt gwdiqrneir argpqppsse alshaacyda
      121 csdihwvfhv hspvlweaaa rldmpatpld aeygtpamae aissiirnah lpvllqmagh
      181 edgiiaagns aaqcgallle avlraqlssa lrk
//
LOCUS       WP_010640112             277 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Streptomyces albidoflavus].
ACCESSION   WP_010640112
VERSION     WP_010640112.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..277
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29041
     Region          19..262
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mvkavntrsv dqelvkgpvd kamevlealv lpggphrlgd iarrtgltkp tvhrhlrtmt
       61 eygfaepaeg gsyragprll glaaaalnds raielirpvl adlrartghv afyavrhagd
      121 avyleqsepa reyrvstrpg hstplhacgv glamlsalpa eeaeavlgvp eleartpqap
      181 tdpaalravl araalcgyav ddeydepdvr svaapvvdar gevvgaigis gltftldpes
      241 tqvygpmvra aartvstqlg artpvlgavp aegrgkr
//
LOCUS       WP_010640142             405 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ammonium transporter [Acidithiobacillus].
ACCESSION   WP_010640142
VERSION     WP_010640142.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..405
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42838
     Region          10..400
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mlatgvtppg gnvffllmga ilvfamhagf aflelgtvrr rsqvnalvki lsdfgistiv
       61 yffigyhiay gisffgnvqt ltagdhgfem vrffflltfa aavpaiisgg iaerarfypq
      121 llataflvgl vypfyegivw dnnygiqawf tqtfgapfhd fagsvvvham ggwmalmavw
      181 llgprrgryg kdgtvhampp snipflalgs wiliigwfgf nvmsaqqlaq vqglvalnsl
      241 malvggmlaa lavgkgdpgf vhngalaglv aicagsdvvq pigalaigai agiifvylft
      301 fvqhrlrldd vlgvwplhgv cgvwgglavg ifglkmlgga ggvsfwsqll gtslgvlial
      361 lgsgvvygti kafigirlda eaeyagpdls ihhvsaypee diera
//
LOCUS       WP_010640149             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Streptomyces].
ACCESSION   WP_010640149
VERSION     WP_010640149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11100057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..316
                     /product="universal stress protein"
                     /calculated_mol_wt=32351
     Region          6..135
                     /region_name="Usp"
                     /note="Universal stress protein family; pfam00582"
                     /db_xref="CDD:425765"
     Region          176..298
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mstlpviaav dgsddstral ewaleearlr eaplrivhav rtatprgaep pagaaapdss
       61 vivetrqalt grpglpelsf ttldstaasi lpelgaeaql lvlgsrgrgg faslllgsng
      121 macardadsp vvvvprpgrd vhtdapepap gprvvlgmsa efpltadaap dpalafayre
      181 aairsarlhv vcaypwpvva waaageylps aadqeaaeae crqlvaerva tlkdtypqvt
      241 veaevspgda aghlvaaarg adlvvvgrhr prafspvrml gsvthavllh apapvavvpt
      301 aqelaeaaaa tgedaa
//
LOCUS       WP_010640297             401 aa            linear   BCT 01-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010640297
VERSION     WP_010640297.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..401
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44111
     Region          11..>240
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mnevrigaae tiglvlsggg vraaafhagv lrylaeqrll ekvqhissvs ggslfigmvf
       61 rhanyhwpss eaylnevfpr fqqtlttqsl qfsafsmlil nplnwrfils ranilaqair
      121 glwgveasls sldtvpvwsi nctsgetgrr frfkngtmgd yelgyaavdd fdlakamais
      181 aalpggigpl tiktkkflwk krkqwgeges epfqptfnsl hlydgglydn lgiepmfdvg
      241 sqslkvdetl rsditylvvs dggaplarkg iphplnpfrl kriadialdq cralrvrafv
      301 nflqknpkag vyvgigtaae ssikrfangr gavaagflnq awltadearr aatysttlrq
      361 lseyafdlle rhgyetakwn lemmsqvpst hatipqgdqq l
//
LOCUS       WP_010640278             293 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: 3-hydroxyacyl-CoA dehydrogenase family protein
            [Streptomyces].
ACCESSION   WP_010640278
VERSION     WP_010640278.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..293
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=30932
     Region          13..290
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mrsgsrppat tpigvvgagt mgvgvaqcfa eagypvtlhd pdpaaraage rrlrtglraa
       61 rllrrpapgd ppaevaarvr wasapdalad aalvvecgpe rmdvkerilg tldaacgpdt
      121 vlasctsaip vdilaghtgr pdrvlathfm npahlkdave vvrgprtsee slatvlalld
      181 aigkrahlvr dspgfvsnrv lmpmindaaa rveegtadae tvdlvftdcf ghamgplrta
      241 dligldtvld slvvlrettg dprfeptall rdlverghrg rksgrgfhny eir
//
LOCUS       WP_010640310             478 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Streptomyces].
ACCESSION   WP_010640310
VERSION     WP_010640310.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..478
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50291
     Region          35..460
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnssagpdrt prpaapegdf arpagdtpgl paaasfdelg lpagirellt argvetpfpi
       61 qaatlpdala grdvlgrart gsgktlafgl pllvrtagrr aearkplalv lvptrelaqq
      121 vtdalapyar elglrtatvv ggmsigrqat alregaevvv atpgrlldlv erkdvrldrv
      181 eitaldeadq madlgftdqv talldlvreg gqrmlfsatl drnvdllvrt ylhdpvahaa
      241 dpagaavstm dhqvlqvhga dkfatateia ardgrtimfl atkaavdrft ahlrgsgvra
      301 aalhgdksqp lrtrtlqrfa ggevsvlvat nvaargihvd eidlvvnvdp padhkdylhr
      361 ggrtaraggs gtvvtlvtpe qrkdvlrlma daglrprvtq vrsgeaelsr ltgaqapsgv
      421 pvdgsapsae rpkrggaqfr gigtvpgkpg raknasrrsa edrklaeark aarirrgh
//
LOCUS       WP_010640115             795 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Streptomyces sp. N1].
ACCESSION   WP_010640115
VERSION     WP_010640115.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. N1
  ORGANISM  Streptomyces sp. N1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 795)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 795)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 795)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Streptomyces sp. N1"
                     /db_xref="taxon:576456"
     Protein         1..795
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89179
     Region          1..791
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mtswtweyde wvpadeqlre slctlgngyf atrgafpecd addihypgty aagvfnrlts
       61 hvsgrdvene dmvnlpnwlp lrvrrvdgen stwftpgtar vvehsqtlrl dagvlerrtr
      121 yedpdgrlll vrqtrlvsme nphlaalrte ltaenwegev eveaaldgtv tnsgvaryrd
      181 ldgrhltalr tgagnsgdva wltcsttnsd ieialaarya lppgtqveha dtegrsvrrf
      241 rldlrsghsq vvdkivalyt ghdraiadpr daaveharta pafdqlvadq raawrdlwrr
      301 aeldvpnkag lilrlhlfqv lqtlsphtae ldagvpargl hgeayrghif wdelfvlryl
      361 nlhfpevsra lltyrhrrle havaaaeaig lagamypwqs gsdgreetqq lhlnprsgrw
      421 ledhshlqrh vgsaiaynvi kyyeasgdah fhhtkgaeml lqiarfwvrs atwepelsry
      481 rilgvmgpde yheaypgaer pglddnaytn itatwvitra ldllrnlpap rraelalhtg
      541 fdaeeeehwe evsrnlhipf hsgvisqfdg ygelqeldwd gyrakygdir rldrileaeg
      601 dtvdryqask qadvlmlgyl fspselaelf arlgytfdda lwgrtveyyl rrtshgstls
      661 glvhgwvlar vrrtdawtfv lealrgdiad lqggttgegi hlgamagtld lvqsgltgle
      721 trpgglaldp vplpelshyr fslryqghwg vhiqaspgtl diavpasdrf pititlpqds
      781 felapgesrr vlldd
//
LOCUS       WP_010640418             733 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Acidithiobacillus thiooxidans].
ACCESSION   WP_010640418
VERSION     WP_010640418.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 733)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..733
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80598
     Region          62..714
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 minrrkkvly laiisatvsl yginaeades lgtvtgtata sndffgsspn vntgetpksd
       61 iqriqkfnkk atnqetlitr gqfemlaptd sytqvlnnmp namvvssgds mdgddvying
      121 fgkslinftl dgiplndnds ytyytnefip svlvagtkyy pgaesaaipg lsafggsvet
      181 yslkpspspf vrpivgagsf gkynvgglin tglfaksfap tsawiyvnki qrdgyfqnna
      241 alqnqflfks vtqigpgalt lffsqnnqrf nyyngataaq iaqygqdyns ytsnpllpdg
      301 kanynytgyn ynqylnwlgy akyegeigkv kfsdqlyyyy gngfsasatt ytqtlltpag
      361 tigrfsparn gvllgnsvnn thrwgnlari iyplgpvste lgfwfnhnnt lhdsryfsas
      421 ntylgssyse pvvtntyqpy inltykpvda ltlaagfkyl yvtrdfkntv alaqnkpgqf
      481 nvnfgsvlps vganlritdn whafanftqn tnppgynqfy tgtynaelkp qkantyslgt
      541 hwdigpwsss lqafrvdfqn yilsttilvg slnqtvlana gtainqglsw qnnvvlndif
      601 sayanfgvld arltsshqpf pyaphhteal gliaryhglr atvslhemgq syynlggkfl
      661 plgsrffada slrytfrnap lgqslgfknv taslnlnnlf drrfvqsytg sssnpnlkln
      721 lptnvyasid atf
//
LOCUS       WP_010640437             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: arsenate reductase ArsC [Acidithiobacillus].
ACCESSION   WP_010640437
VERSION     WP_010640437.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..163
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=17521
     Region          6..137
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(10,12..17,106,108)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mktpeilflc tgnscrsila evtmnglads rlhatsagsh pagyvhprsi qllqqegfat
       61 eglsskswde lkttpdivit vcasaageac paylgpaira hwgvedpaka tgseaeidaa
      121 fqtayrilrh rieallklpv aewlekdpaq lrqelnrigs mep
//
LOCUS       WP_010640505             958 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Streptomyces sp. N1].
ACCESSION   WP_010640505
VERSION     WP_010640505.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. N1
  ORGANISM  Streptomyces sp. N1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 958)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Streptomyces sp. N1"
                     /db_xref="taxon:576456"
     Protein         1..958
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=101110
     Region          254..932
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mqmcpafspa dvralsacat vfvpgdpara gslaffpaeg sgppevpgaa pgelslvlpd
       61 edgslrvrpv ratllpvawa lpvltrarvr ddahpsaafw gaaallaldl larglllpgl
      121 spadhdawrc gplgpdelrr vrelaasmpp vahcgpvaap pgsdaaelal aeperllrhf
      181 ldavadtlpr taaapalags daytagppqh lpgqrgwaad vaaghdagvr lslrvetpag
      241 aggeesgpev vgafravlql hslsdpgrva daaevwagag addgafgpra rvdallalrr
      301 aagvwaplsp llaagvpdtv eladeeiael lgegqkalag agvevhwpre lareltargv
      361 vgrdgeaggd dtgagflsad slltfswrfs lggrgltree ldvlaeakrp lvrlrdqwvl
      421 idpaqagrar drrdhtlapm eavgaaltgs advggervev rasgaleelr ariadphrae
      481 pvpvpeglaa tlrdyqqrgl swlagmtslg lgacladdmg lgktvtlial hlhrqahpat
      541 agptlvvcpa slmgnwqrei erfapgtpvr ryhgasrasa glpaegfvlt tygtmrldaa
      601 alagagwgmv vadeaqhvkn pysstarqlr aipakarval tgtpvennls elwavldwtt
      661 pgllgrlgtf rrvyaraves gddpaaarrl arlvgpfllr rrksdpgiap elppktetdh
      721 avgltaeqtg lyeavvretl aavaaadgme rrglivqllt slkqicnhpa qylkedrprv
      781 ggrsgkvell delldtilae gagvllftqy vrmgrllerh laargvatqf lhgqtpipar
      841 eemvrrfqdg evpvfllslk aagtglnltr aehvvhvdrw wnpaveaqat drayrigqtr
      901 pvqvhrivte gtiedriael lvrkqalada vltggeaalt elsdaelael vtlrtatr
//
LOCUS       WP_010640583             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein [Streptomyces].
ACCESSION   WP_010640583
VERSION     WP_010640583.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..143
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=16060
     Region          32..135
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mlmrtdpfre fdriareltv pgtwsrptam pmdacregdt yvvsfdlpgv dpeaieidie
       61 rnmltvkaer rpagnaenvr mevaerplgv fsrqlvladt ldteqvrady dagvltlrip
      121 iaerakrrrv kvgqgephrq itg
//
LOCUS       WP_010640586             306 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Acidithiobacillus].
ACCESSION   WP_010640586
VERSION     WP_010640586.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..306
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34112
     Region          7..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtdcpaihiq glrkayqsgh laltgvdldi hageffgllg pngagkssli nilagvvrrs
       61 sgvaeifgfd verdfrrtrq llgvvpqela ydpfftvref lhmqsgyfgl rhnddwidel
      121 maeldladka nanlrnlsgg mkrrvliaqa lvhrppvvvl deptagvdve lrqglwqfir
      181 rynaegrtvi ltthyleeae elceriailq qgkivaldrk enllsaaswr ilkvtfdhdp
      241 gelgpaledl ltgasenirv fridaqrnpl gavlaqlqql paqildlhlq eprledaftd
      301 ilgrmr
//
LOCUS       WP_010640601             303 aa            linear   BCT 01-JAN-2025
DEFINITION  transketolase family protein [Streptomyces albidoflavus].
ACCESSION   WP_010640601
VERSION     WP_010640601.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..303
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32017
     Region          1..301
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mdsmrdrfad tvhqlmdadp rvalviaeis rdrlqgaita hpdrvvnvgi reqllvsaga
       61 glalsglrpv lhtfasflve rpfeqvkldf ghqgvggvlv ssgasydmps ggythmspgd
      121 valldtlpgw tvhvpghpde aealvraava agddkvyvrl sertnaegra ldgtrfrqvr
      181 egrsgaalva vgpvldtvla ategldltvl yattvrpfdg aglrraaidp drgtaqvvlv
      241 epylagtsvr aadealsvvp hrllglgvgk eelrrygrae ehdaahglda aslrrdisaf
      301 las
//
LOCUS       WP_010640596             274 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Acidithiobacillus].
ACCESSION   WP_010640596
VERSION     WP_010640596.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 274)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..274
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29179
     Region          2..242
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 maaealveld nvrfargshp vlagvdmhip rgaivalmga sgggkttmln lmagtlrpqs
       61 gqiriagqdl qklsedamya lrrqmgmlfq hsalftdlta fenvafplrr hfrlpenllr
      121 klvmmkleav glrgaaglfp aelsggmgrr ialaravvmd pmlifydepf tgldpisvgi
      181 iaslikrlnt algatsvlvs hdveetfsia dygfilaggk iiaegspadl rasdsalarq
      241 flggqpdgpv pfhyparqdy aaalrdshaa gevl
//
LOCUS       WP_010640384             483 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LVIVD repeat-containing protein [Streptomyces].
ACCESSION   WP_010640384
VERSION     WP_010640384.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Adindla,S., Inampudi,K.K. and Guruprasad,L.
  TITLE     Cell surface proteins in archaeal and bacterial genomes comprising
            'LVIVD', 'RIVW' and 'LGxL' tandem sequence repeats are predicted to
            fold as beta-propeller
  JOURNAL   Int J Biol Macromol 41 (4), 454-468 (2007)
   PUBMED   17681373
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..483
                     /product="LVIVD repeat-containing protein"
                     /calculated_mol_wt=52069
     Region          55..456
                     /region_name="COG5276"
                     /note="Uncharacterized secreted protein, contains LVIVD
                     repeats, choice-of-anchor domain [Function unknown]"
                     /db_xref="CDD:444087"
     Region          73..107
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          114..169
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
ORIGIN      
        1 mlaslltvgp amavpgpgdt pevaervsks eaadtkeais agdipgvdei vhtenikhla
       61 nipkdalsgt nsdlafqgky afagnydgfr vfdisnpkkp ktvsqvlcpg sqndisvsgd
      121 llflstdssr sddscastsq patekssweg mkvfdisdkr kpryvaavet acgshthtlv
      181 perknvyvyv ssyspsaafp dcqpphdgis vikvprkaph qaavidfpvl fpgdgpdggg
      241 npgaptnpgv skttgchdit alphkdlaag acmgdgilld iknpekpkvi drvqdnenfa
      301 fwhsatfnqk adkvvfadel ggggaatcne eigpkrgadg iydlvrkgkd ktpklvfrsy
      361 fkidrhqadt encvahngsi ipvkgrdimv qawyqggvsv wdftestkpr eiayfergpl
      421 sedtlvgggs wsayyyngfi ysndmakgfd vlklddrrtd pakkvkldel nvqtqpdyfd
      481 rsr
//
LOCUS       WP_010640239             175 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SigE family RNA polymerase sigma factor
            [Streptomyces].
ACCESSION   WP_010640239
VERSION     WP_010640239.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..175
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19742
     Region          5..158
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mappdfetfa aarwprllrt aylltgdhhe aedlvqvtla klfpawprvr gldepdayvr
       61 ralvnnnlsr frkrrvvqll tprlperaqe ggaarteers lllealgtlp prqravvvlr
      121 ywedlseqqa aevlgcspgn vksqasrglr klrdhpalae fqprpgreep aderp
//
LOCUS       WP_010640702             241 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endonuclease V [Streptomyces].
ACCESSION   WP_010640702
VERSION     WP_010640702.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..241
                     /product="endonuclease V"
                     /EC_number="3.1.21.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003727 - single-stranded RNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=24700
     Region          11..233
                     /region_name="Nfi"
                     /note="Deoxyinosine 3'-endonuclease (endonuclease V)
                     [Replication, recombination and repair]; COG1515"
                     /db_xref="CDD:441124"
ORIGIN      
        1 mrarpapaav tvpadwpate aearsvqdtl rarvdltgpg pevgtgtatg vdvayddvrg
       61 lvaaaavvld aatlevveea tavgpvsfpy vpgllafrel pavlaalaal tappglvvcd
      121 gygvahprrf glashlgvlt glpavgvakn pftftyeppg errgdqtplt dgseevgral
      181 rtrtavkpvy vsaghgvpld ravahtlhla payrlpettr hadalcraal kaavtgeadq
      241 d
//
LOCUS       WP_010640719             442 aa            linear   BCT 01-JAN-2025
DEFINITION  NADH-quinone oxidoreductase subunit N [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010640719
VERSION     WP_010640719.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..442
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=46027
     Region          6..439
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mdysptllpl livgaaalia fladalrlgr lmpwlggiss iaaaasifve hmalgadlyw
       61 dlsatllgvy lglamaaglf fitfhplsrk mtgslvglll tmlagslilv saqnlllmfv
      121 glelqvlpff allawpgsgr aavesafkya vlaglasaqf aigialiylg dgslavippm
      181 gdmtsnvfgl mgvlallaal sfeiaaapfh awvadiyqga papfliflgg vakvaimgal
      241 itlaaatpkl eipiaviaat sivvgnvlay raghlrrmlg ysaiahagyf laalavgplg
      301 iiagaiyalv yglmnmgtfm glsalpensi aipwaalrer qpvlagllgl tllslagmpp
      361 sigffakllv iiadvhdqay wlailialgs afsfayylst lwkpsvlsnp drllqrgswe
      421 tfaalgilil lfgwllaplg mg
//
LOCUS       WP_010640793             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [Streptomyces].
ACCESSION   WP_010640793
VERSION     WP_010640793.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..161
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17057
     Region          6..158
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mseqltigle idgrphteei eprtvlldll rerhgltgvk ascergvcga cttlvdgvpt
       61 ascsmfafsa dgssvetvag qspdgvpgpv qrafaecggf qcgyctpgmi mlttallreh
      121 pepddaqvre wissnicrct gyqmiidsvh raaallkees a
//
LOCUS       WP_010640863             181 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Acidithiobacillus thiooxidans].
ACCESSION   WP_010640863
VERSION     WP_010640863.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..181
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20218
     Region          <35..177
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mpykppftit seilnlvaei sqqvkrldas alnangrmgr lwqtlilsrw hplflslple
       61 svikdhqqty yraleqgdeq adstpfirfm lsiiartltq nasvsapana pvnperdvrg
      121 lkipeailvl laynpqrtrq qlaelmgkdl rtigralakl qqagkinrvg sdktghwevq
      181 p
//
LOCUS       WP_010641115             275 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            albidoflavus].
ACCESSION   WP_010641115
VERSION     WP_010641115.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..275
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28589
     Region          87..274
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <213..275
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mrealarlrr atglpiafgg liegrhqvri aelsgtgtta lrglnvssgn glggkavalt
       61 rpcavtdyra srrisheyda avaaeglrsv lavpvvvhrh vrgvlygalr aptpvgdrtl
      121 saavaaardi eqalvareea ahllsragep prtsspaawe evreihselr tlagrlpdpa
      181 lraellaact rlaragqpga vappgapklp ptvltprevd vlvcvaggat naavagrlgv
      241 rpetvkgylr samrklgaht rleavvaarr qgllp
//
LOCUS       WP_010641149             165 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Streptomyces albidoflavus].
ACCESSION   WP_010641149
VERSION     WP_010641149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..165
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17749
     Region          38..149
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mgrstrhgph agsppgrser pgpdrkaggr lhrtlhhadl rsvpevrral rallrpclae
       61 dqaataella sevltnalih sdhdalftat vhdgslrvev rdftgrpprp rtprpheats
      121 grglllveal addwgvrrhg vgkavwfelg pvqngaehgg rkdaa
//
LOCUS       WP_010641220             284 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cell division protein FtsQ/DivIB [Acidithiobacillus].
ACCESSION   WP_010641220
VERSION     WP_010641220.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..284
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30691
     Region          51..280
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mvsvmrdyrh gqqpqrpaat lkekpkaapr tapvkaaaka hkplpwklyg kvlagglsis
       61 ilawggwsgw qwlqqpslmp intltitgss pkiplaeint vlkpyaargf lwanpeqirh
      121 sldalpwvad aevrrvwpdr ltvnikpytp varwlggagq mvdaqgkvfs vppaqvpngl
      181 pnlagpadsg sqllaqlakf nsivaplglk vvslqedqrg gwrcilnnqv rlllgsedvi
      241 palkrwvaia pqvkeylvag atmdlrytng favampsatt vnsq
//
LOCUS       WP_010641260             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein
            [Acidithiobacillus].
ACCESSION   WP_010641260
VERSION     WP_010641260.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..322
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35727
     Region          6..187
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(9,11,94)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(40,93..94)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            92..94
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mprisvvipl yneidnvtpl cdalsaalag adaeiiivdd gsrdgsaaal dreaatrgnh
       61 fkmihlqrnf gqtaamqagi daaqgevivt ldadlqndpq dilplaerll aenldvvagw
      121 rknrqdglfl rkipsrianr lirrftgvrl hdygctlkay rasvikgvrl ygemhrfipa
      181 wlstltytdr ivevpvrhha rvagkskygi srtfrvlvdl lfvkfflgys qrpmhffgtv
      241 glfslfigsg mliylfidkf aegaeisgrp mliagvlffl gglqflntgi vgemlsriyh
      301 esqdkktyvi rhtvhldpga ep
//
LOCUS       WP_010641419             208 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010641419
VERSION     WP_010641419.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..208
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22495
     Region          17..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mastagrpgr vaklppreri ldaaeelfqs egirrvsvqa iaekaattkm aiyrhfetkd
       61 alvaewmriv aadyqaafdr veaehpgrpr eqivglarfi aeglpalshr gcpfinslae
      121 lpdrshparq vieehkahqt rrlvgmcaea glpdpgqaaa eitfvlegaq vstqngsidr
      181 agerlmsive givdrhgspl dtprpavg
//
LOCUS       WP_010641402             295 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010641402
VERSION     WP_010641402.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..295
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31535
     Region          27..278
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mktaaknsaa ptpaspggvg appekglgar gvtlsyggep vvrdvtldlp hggltviigp
       61 ngcgkstllk gygrilkpeq gtfhlhgtdl hayrgkeaar hvallpqspv apegitvrdl
      121 vrrgryphht llrqwspddd raiafaldrt gltelaeeqa gqlsggqrqr awiamvlaqe
      181 tdlllldept tfldiahqyd llelcaelnr egrtivavlh dlnqaarfas hlvvmdrgev
      241 yaqgapeevm taelvqkvfg lacdiapdpr tgtpmvvphe ryqapasaep epaea
//
LOCUS       WP_010641477             339 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Streptomyces].
ACCESSION   WP_010641477
VERSION     WP_010641477.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..339
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34555
     Region          34..329
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtgdlltapg eksaapaprp grrlrltdpv tgvwlaalav tllgwavvaa qggqfltttn
       61 vvavlqnsva lglvavgqsm viltgsldls vaylislgtl vaaqtmqsgg vllavlatla
      121 lsvavglang livaglkvna fiatlgtafi lrgwiedqyt gpagqvtagf qrlgydrigp
      181 vpvsvfllla vagaawfltr rtrlghhlya tggdehaarl sgvrtrrtvv vahvlcslcv
      241 gaaalflaar lgagapwagt earydlesia avvlggtala ggrggvagtl ggvlvlavld
      301 svfnqlavdp ffknvvrgvv iiaavalyar rrtprrrta
//
LOCUS       WP_010641647             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: inositol monophosphatase family protein
            [Streptomyces].
ACCESSION   WP_010641647
VERSION     WP_010641647.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..269
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28092
     Region          20..245
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(37,42,48,71..72,87..92,213..214)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(41,43,93..94,96..101,153..155,157,159..160,168..169,
                     173..174,177,182..188,196,200..203)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 mtdpntglla laleaarrag dflrdgrpad lavaatktsa idvvtemdia sekmitgfla
       61 drrpedgflg eegastegts gvrwiidpld gtvnylygrp awavsiaaer dgvtvvgvvh
      121 apmrgetcra vlgggahldd tpiqvntapt ldralvgtgf gylagrkahq aavaariipe
      181 vrdirrggsa aidlcdvatg rldayyergl npwdyaagel iareagaltg grpgalaste
      241 ltvaappglf eplqerleey gawhdgtla
//
LOCUS       WP_010641655             275 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Streptomyces albidoflavus].
ACCESSION   WP_010641655
VERSION     WP_010641655.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..275
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27767
     Region          10..269
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mnaiisatal agelqgprpp vlldvrwqlg gpgqrpayla ghlpgavhvd ldgelaggpg
       61 kggrhplpdv eafgaamraa gvdagrpvvt ydggqgwaaa rawwllrwag hpevrvldgg
      121 laawdgplee gevtpepgdf tpepgrlell dadgaaalaa sgvlldaraa eryrgdvepi
      181 drvgghipga vsapttentg edgrllpaae lagrfaalga kpgrkvgvyc gsgvsgahev
      241 lalavagvda alyvgswsdw sadparpvat gpqpg
//
LOCUS       WP_010641632             142 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Acidithiobacillus thiooxidans].
ACCESSION   WP_010641632
VERSION     WP_010641632.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..142
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16101
     Region          34..142
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mdrrllirll aeqelaiilp lvqvlnpdvv pdllaqrlqd mvgqgyqcva afldddcvgv
       61 agiwqgtrfw cgryldvdnv vvdpayrgsg igrqlmdwve qyarqqgcei mvldayvtnh
      121 sarrfyermg yqvlghhfvk sl
//
LOCUS       WP_010641659             393 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkaline phosphatase family protein [Streptomyces].
ACCESSION   WP_010641659
VERSION     WP_010641659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..393
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41956
     Region          28..389
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mppsawpepl plasapvpay gsgsladllp tlaagsgvpg mtatltelpp adrncvflid
       61 glgwhqllah paeapflssl iptsrggtgq pltagfpatt atslasvgtg rtpgehglpg
      121 ytalnpdsge lmnqlrwkpw tdphawqphp tvfsladaag vhtaqvsapg fhhtpltqva
      181 lsggtfhgrl sgeermdlaa aqlaagdral vytyysevdg kghrfgvdsd awrgqlmyvd
      241 glarrlaeql pprsalyita dhgmvdipfd drhrfdvded welnagirll ggegrarhly
      301 avpgaardvr tvwrevlgeq cwvagrdeai eagwfgphve krvrdrlgdv ivaarddvai
      361 tatrrepnes altgmhgsmt paeqlvplle vrt
//
LOCUS       WP_010641881             251 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerophosphodiester phosphodiesterase [Streptomyces
            albidoflavus].
ACCESSION   WP_010641881
VERSION     WP_010641881.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..251
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27366
     Region          18..242
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mstahrtnsp rgtaptpprt vavahrgdpy qiqentlpsl rsaldrgada vevdvrvtrd
       61 gvpmllhdat lerlwgherr laslsadavt dltvgrlprl dealrvtlds rlmidlpgtp
      121 srrdvaamig tvresgaadr vywsgdaaam lqvreldgea eialtwttla pprpallsav
      181 rprwlnyrfg lvgrdlvdrv hrdgllmsvw tpdtkrtmrr llalgvnsvt tnridvlrgl
      241 lspaarpgaa t
//
LOCUS       WP_010641906             775 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Acidithiobacillus thiooxidans].
ACCESSION   WP_010641906
VERSION     WP_010641906.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 775)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 775)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..775
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..775
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84519
     Region          80..738
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mskakkqllr qsilvavgll gssllpahaa tsatptkkvy kikqvskdll rmvdkaaltk
       61 vkpvygaeta lipkkflhgq estqnastil sfvpginats tnpigvkthi svrgfsqtqv
      121 gytfdnlpia dlfngglsgg nnnyadltnl ipvtlgetsg iqvtygtppp dvnavgaigg
      181 ninylpkvps skqyesvfag ygsfntrsyg aeintgaaag ygnlllrfss rqtagylehs
      241 pdreysyyaa ydlpqispts kwslvfllnk nqgataarmp kalldqygpy yqwptsftya
      301 nskaehmmai lqnktlissh avfgfkgfya ytnshrleyv npeadyqyns fvtfylnpaq
      361 tvcqysgndf mgndsaacqa qtingdnyhs ytyttntfgl npsiewlnhy vnlkagglav
      421 istydsrdyv ygtpnvpevp gynnlwdehg wrvygkvyaq akikptsnla itpgikyeti
      481 strindvpgy yysvgatsgk tysevspyvg iqykptkavt lyanyakgfk ypnitafyaa
      541 dsnatttspa tpvtikpesv ntyqfgaayn kgpvdasisf yrsdfnntfs syydttnglt
      601 yeynigssqy qginiataya ldanlslygn ysiqeaeyts nsssaygvst sigesrpntp
      661 tylaglgvlg hymgtrarly gnlvgpqyie astgapthls mpayatmnfn lahtfmihqy
      721 giknvtlsls gvnllnseas vlekqfpytn gvsgnyleae pmmprsffgt vkmvf
//
LOCUS       WP_010641981             244 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HAD family hydrolase [Streptomyces].
ACCESSION   WP_010641981
VERSION     WP_010641981.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..244
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26409
     Region          6..231
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mgtnrikavv wdvddtifdy gradldgira hlavegllee hggeeaalar wktvsgthwr
       61 rfvagetdfe ghrrdrvref lgtplteaqa aawwdryvth yesawslfpd aaetlaavag
      121 lcrqavlsna sllvqerklt tlgvrdhfen vvcavelgia kpeagaflhv cealglapae
      181 vayvgddrev dgvgardagl rsvwvdrdgt rgpapegver itglaelpal ltgqtrfgar
      241 stfg
//
LOCUS       WP_010642003             194 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010642003
VERSION     WP_010642003.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..194
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21364
     Region          3..183
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 msrssgpvsq awhftreflr dpqaigavlp sspflarrma amvpdgpglv ielgpgmgpv
       61 tkallargid asdlvlveqa ptmvrhlrhq fpqleviegd aarlqemiah rgkvraivss
      121 lplrtiprev vtrifqqlpa vsqqgtvfiq ftyhfrsscq gmptefrrgr pamvlrnlpp
      181 aridqfifhg nglv
//
LOCUS       WP_010642156             192 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            albidoflavus].
ACCESSION   WP_010642156
VERSION     WP_010642156.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19985
     Region          5..>107
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtgrrsdaer nyrriltvae aeiaelgaaa siervartag lgsatvrrhf ptrqalleav
       61 faeraqalqa raaeltgesd sraalvawlr dftdyavsar gfadvlayep paeaggeage
      121 aapsscgttl eaalapllar aqregaarpe aschdlvtav agialatehh rdpaaqaarl
      181 lelfvtglsp rg
//
LOCUS       WP_010642128             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Acidithiobacillus].
ACCESSION   WP_010642128
VERSION     WP_010642128.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..231
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25173
     Region          18..226
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 meaitdnvps llretslfsa wpealldsll khsktvhlgs gdilfvekat anafylvlsg
       61 rihliaaaat gqekiveiir endlfaeava flggcypvta aaegsttvle iplalfleil
      121 eqrpqlmrqm larlsmrlhf lvkelrqlsv esaeqrlvsy lldlcpvlda aavvelpakk
      181 savaarlglt petlsrlllr mrkaglitvn rrvldipdpr alqcwaaghs s
//
LOCUS       WP_010642317             459 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Acidithiobacillus thiooxidans].
ACCESSION   WP_010642317
VERSION     WP_010642317.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..459
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50136
     Region          22..411
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,266,269..270,273..275,278,306,310,365..366,
                     370,374,390,393..394,397..398,401)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 msnllsaidd eqkvtrrhrr ilwasglgif ldgydlsima ivlillkpqw hlgptvlgll
       61 gtaalvgali gglfggiiad rygrktvyli diaafffaal lsgfawdits lvilrfilgl
      121 gvgadyplss tyiaefmpkn krgsamtwif glwmggalvs slvglallht gpdawrwmla
      181 sgalpavlvl wlrrslpesp rwyiyrgrlq eaaqvlrwlv pdvdaherer lvqetassmq
      241 asrnvswtml fskpylrrtv yacvpwfmmd vmgyalgifl pfmlmhmglk tpeqaiigns
      301 fftasfvlgw iplalmidri grrraqiwgf lgdaislglv glfalsgepp fiivaaglii
      361 wqiansfgpg nttwiiptel yptelratgh gfatafsrfg gvvsvfflpt lqaelgnggl
      421 llvlagagli gvlttwwlgs emagqalpem lepgsqraa
//
LOCUS       WP_010642327            1039 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010642327
VERSION     WP_010642327.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..1039
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=111270
     Region          1..1022
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnlsepfirr pvattvlava vallglfayl qlptallpnv sfpmvmvtae lpgaspktms
       61 savatplerq fasipglnsm savsqngvtq itlqfdlsks algatqqvsn avsqaqhflp
      121 pgmpeppsvr qmnpsaqpvf yigmsapnmp lyeldkyaqt kvstalsgis gvsdvqiyga
      181 qtyavriyvn pfalsarels lqavqsalgn anvnlpggtl dggdqafatq vhgqlhtaka
      241 ynhlvlayeg gqavplsavg kavnstednq qetwinktpg ivlavtrqpg sntveisnki
      301 rallpqlqaa mpggvhltnv fdladyiraa vhevlmtlil asilvagvmw lflrrpsatl
      361 igavaiplsl lgtflvmmll gfsintltll altlsvgfvv ddavvmleni nrhidrgetg
      421 mtaalngsre isftvlsmtl slsiiflpli flggfvghlf sdfgvsiavv ilisgmvals
      481 vtpmlcsryl kpnhahartd lhdtghlped gifqrffkds rdfyirtlkv alnhkywmla
      541 laglalagsv wlvmivpkaf lpsqnsgmin anieyptgmt faevrheqse iarivksnar
      601 iqsvvssagq gaggfgsrns ghmfihirsg yapqteniiv dlqratrrfh naqivfqgpq
      661 sahsgtasgn gsyiyelmgs nwtdlnaatl kmtealqklp qlnsvsnsle nnnpqvtihi
      721 nraratalgv tpaaientlg lafgghevgt iygasnqyev imelepryqk ninalstlsv
      781 pgagstlvpl savasfhyda aplnlmqhng qpsttisfnl apgvqlgsai salqhtahqv
      841 lpagivghlg gnaaqfqsaf kslpflllat vlliyvvlai lyehflhplt iltalplaaf
      901 gallslvifh epldlysfig iimllglvkk ngiilvdfav srrregeday naiidactir
      961 yrpimmttfa ailgvlpiai gfgagagsrv plgiavvggl ifsqfltlyi tpafylwfdw
     1021 lswprrkrtq avvlnpdls
//
LOCUS       WP_010642334             761 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Acidithiobacillus thiooxidans].
ACCESSION   WP_010642334
VERSION     WP_010642334.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..761
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82957
     Region          23..730
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mlallgmssm aladvtastv ssvnaatatt grgnapvtig evekeapper gtgslskelv
       61 khaspnenfq svlrnvpgft vtssgpgnlt tndstftyqg fnsdqigvnl dgvplintfr
      121 ggtngqgddh altplgmgqf sgvsvysgan tpsetginal gatldykprm ptskfyaevs
      181 gsgglysggn gnsaaggfsi nsgvlpytgt klyanyyysp fhsfldhvys innnyyfaav
      241 qpynhgmsql slitiynhei aqqpetvpla llqkygrnfq wardiannht ttssyttivg
      301 wksilnqyml akakffitqn tndrtayana aykdgyegyp lptalkgyan pvssghpsnt
      361 ynptalfgns yngtqyqryi dnfgnagfmp sltfllphnt vtlgglymfs kdnsaeywyg
      421 apdvpmidgy ndawdehdtr nyadvyvqdr islfnhrlii tpgakyymvg ttcndiegyy
      481 ynyggtvsnt fnywepsfgv sflatkdadl yfhygrvykv pnisayyavi gdtptpgpml
      541 vkpeyvdsid agirynfgai ktslayfrrm fsnkfgyfyn dqtgqtfqyn vgsalyqglt
      601 asvdgklpyn mnafinyslt dakytsnfda adgaavssge yvgdvpmynl nfglgyhyag
      661 fsaritdhvi gsqyintnkg apagialhpy nitnlnlgyv wrpaemgvkk ltfdvyvdnl
      721 fnanyipyey lqlqsakdgg nfiaaqasap afvgaslaak f
//
LOCUS       WP_010642447             237 aa            linear   BCT 01-JAN-2025
DEFINITION  PilZ domain-containing protein [Acidithiobacillus thiooxidans].
ACCESSION   WP_010642447
VERSION     WP_010642447.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..237
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26934
     Region          112..210
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 meylplvfls gaedlllpep edlgiavgqs aivydeeedd sgtlchtqgw dlgdlvlkps
       61 lstldnmpsy rkslifilak pyllgffadw kyfqkeahhf rrpqrvlrrr trktqrirle
      121 gkitirrrdg tslfahlydf tptgagfyts atgfrvgeml lvefdiadcg tcettvtiar
      181 ienllhssha yligvhfklt eaqhrkaeql ylckkaemiq qlasperhrw tppsssg
//
LOCUS       WP_010642478             499 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA recombination protein RmuC [Acidithiobacillus thiooxidans].
ACCESSION   WP_010642478
VERSION     WP_010642478.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..499
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=56638
     Region          <26..>212
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          176..464
                     /region_name="RmuC"
                     /note="RmuC family; pfam02646"
                     /db_xref="CDD:460637"
ORIGIN      
        1 miwelflvfl vglllglgil fflsrqnlgr qrdeaaavqa rqeqviselr ahiqaqqsel
       61 lkqnesrvra etenqqipll ndalknshne iiklqndlnq irgqqaelqe rleqerlrsn
      121 ekltlleear qrltetfqsl sadalrrnnq sfldlarenl erfqenaktd wdgrqkavgq
      181 liepiresme kvgqrmdame ktridaygal neqlrglvqd hlprlhqeta alvkalrqpa
      241 argrwgemql krvvemagml aycdfaeqes vqtetgqqrp dlvvrlpggk rlivdakapl
      301 nayleamese deqkrqqfll khaqelrthm tqlgkksywe qfqptpefvv lfvpgevffs
      361 aalqadpali efgveqkviv aspttliall ravsygwrqe slaenarais elgkelydrl
      421 htlaghwsrv gknlgqavda ynkatgsleg rvlssarkfr dlkaiadnke lsvsepveln
      481 prqlqadeli geklpdssd
//
LOCUS       WP_010642492             272 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces
            albidoflavus].
ACCESSION   WP_010642492
VERSION     WP_010642492.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..272
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29506
     Region          72..159
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 mphsssdtpa prspgsapea gfdalvaeae aapvdgwdfs wfegrateer pswgyqrlla
       61 grladpavra aldlqtggge vlagagpypp amaateswpp nlaratrllq prgvvvvagp
      121 eepplpfadg afdlvtsrhp atvwwpeiar vlapggtyfa qhvgpetvfe lsefflgplg
      181 gevrrlrhpe aeraqaeqag lemtdqrter lrmefhdiga vvhflrkvvw tvpgftveay
      241 rdklrelhar itaegpfvah strtlvearr pa
//
LOCUS       WP_010642535             401 aa            linear   BCT 01-JAN-2025
DEFINITION  GspE/PulE family protein [Acidithiobacillus thiooxidans].
ACCESSION   WP_010642535
VERSION     WP_010642535.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..401
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=44099
     Region          <23..390
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mssvvttsfi stndrdrrit grlneifama agkrwsdihf esledgsaev rvrirgklkq
       61 leivhpddak llinklryra nldvsdtrhe qdgrfvqefe grridvrlni vptnfgysav
      121 vrlldsanag vpieklqmpe gveaafrwal sqreglvlna gptgsgkttt lyaglnsknt
      181 edvkiitaed pveyilkriq qiqvgsgtgr tfasalrafm rqdpdiilvg eirdtetgsi
      241 amragmtghl vmasihanss letyfrlhdl eipphiigas vrlfiaqriv qtvcqscrek
      301 apvalpevfa gsgveapdwe wvgkgcedcd gtgydnrmai feaikmtraf raalgdekam
      361 eaaaklqpqy qslrtagcnl ivsgetnsle idralsegma e
//
LOCUS       WP_010642591             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Streptomyces].
ACCESSION   WP_010642591
VERSION     WP_010642591.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..135
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14509
     Region          14..109
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 migvidtrgd caawtfpadp gvvrtartvv rrqlaawgld aledvtallv selvtnslry
       61 ahgpigvrlt hpeeagspll vevsdpvpda prerragpde etgrglqlva ctscrwgtrr
      121 grrgktvwfe lalpg
//
LOCUS       WP_010642632             302 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010642632
VERSION     WP_010642632.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..302
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=34438
     Region          2..302
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mididdwiqq fekwlsgpnf tnpysqvsir gycaharrfl daldydgved lsevsiamvr
       61 kyirigqhge kskrssqyvk matlmlfyef icakddslpn lalsyqeens aqrerrsggr
      121 ggfkekrlvp vlswqemerl lthidrgtsy aamrdkalir fildtglras evvamtikda
      181 geyfegrirl vgkgnkerlv rfqpegveam rnwlqirhrs hpetdalfvt dqgkaipaka
      241 lhtmvsrlli rsgiekpqcg phllrhtaas awlakgmdlr qvqenmghan iatssrylhl
      301 le
//
LOCUS       WP_010642755             561 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Streptomyces].
ACCESSION   WP_010642755
VERSION     WP_010642755.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..561
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62216
     Region          3..498
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mdkyvqeqpr dflavatpga gkttfaltla swmlhhhvvq qvtvvapteh lkkqwaeaaa
       61 rigikldpey sagplskeyq gvavtyagvg vrpmlhrnrv eqrktlvild eihhagdsks
      121 wgeacleafe patrrlaltg tpfrsdtnpi pfvtyeegnd girrsaadyt ygygsalgdg
      181 vvrpviflsy sgqmrwrtka gdeiaarlge pmtkdavsqa wrtaldprgd wmpnvlraad
      241 qrltevrkai pdagalviat dqdqarayak lireitgnka tlvlsddsga sqriddfsks
      301 ddrwmvavrm vsegvdvprl avgvyattis tplffaqavg rfvrsrrrge tasvflptvp
      361 mllgfaneme verdhvldkp kkdgeedpya esekemdean keqdedtgeq eqfsfeales
      421 eavfdrvlfd gaefgmqahp gseeeqdylg ipgllepdqv qlllqkrqar qiahsrkkpd
      481 seadllelpa errpvvshke llelrkqlnt lvgayvhqtg kphgvihnel rracggppsa
      541 eatagqirqr idkvrewatr g
//
LOCUS       WP_010642763             545 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: beta-N-acetylhexosaminidase [Streptomyces].
ACCESSION   WP_010642763
VERSION     WP_010642763.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..545
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60100
     Region          3..524
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mhhlipaprh hrpesgpetr ltlgpdtalr tgagtgtaar wlrttvgaat glalpeaaae
       61 npgpvvdlri tgeagglgae ayrltvsadg vlieggdaag vfwgaqtlrq llgpdafrra
      121 plnpgrawql ghvriedapr fawrgmmldv arhfmpkdgv lrhldllaah klnvfhfhlt
      181 ddqgwrvdir rhpelvrtgs wrprskwghr aselwndtph ggyythddir eivayaaerh
      241 itvvpeieip ghsqaaiaay pelgntdvtd taslgvwdtw ginphalapt edtlrfyegv
      301 feevlelfps rfihvggdec ekdewrrspa aqariaelgv gdedglqswf irhfdrwlga
      361 rgrrlvgwde ilegglaega tvsswrgyag giaaaraghd vimcpeqqvy lnyredggpd
      421 epvpigyvrt ledvyrfepv ppeltgaeaa hvigvqanvw tevlenqdrv dyqlyprlaa
      481 laevawsplp aseerdfagf darmethlrr ldalgvayrp psgphpwqrr pgvlgrpfeg
      541 apqpg
//
LOCUS       WP_010642776             135 aa            linear   BCT 01-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010642776
VERSION     WP_010642776.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..135
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=14861
     Region          4..119
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 mysmnkvqfv ghlgkdvdlr yspagnafgs tsiatsrrvk qsdgsyedat dwhnlvlmgk
       61 taenahhhls kgsyvfvegr lqtrkwtdke gndkyttevi vntigyletk dgaasgsqdq
      121 qaqptdfped sdipf
//
LOCUS       WP_010642862             323 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Streptomyces].
ACCESSION   WP_010642862
VERSION     WP_010642862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..323
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34042
     Region          6..302
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 msasggtkai vaalsanlai avakfvaflf sgsssmlaes vhsladsgnq gllllggkra
       61 krqatpehpf gygreryiya flvsivlfsv ggmfaiyegy ekikhphele hwywpvgvlv
      121 faiiaeafsf rtaikesnpl rgkqswsqfi rrakapelpv vlledlgalv glilalggvg
      181 lalatgdgvw dgigtlcigv lliviaivla aetkslllge sagldevrki eaalvdgdtv
      241 trvihmrtlh lgpeellvaa klavqhddta aevaaainaa earireavpi araiylepdi
      301 ydeaaaakgt npamtpspda spr
//
LOCUS       WP_010642902             169 aa            linear   BCT 01-JAN-2025
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            albidoflavus].
ACCESSION   WP_010642902
VERSION     WP_010642902.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..169
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17552
     Region          3..169
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 marpsapgpl vlvqdlvntl dletgadtla teegraafgl readvaaara lrealraacl
       61 ahaghgapae vaaldtllaq aplvttvdpa dgsarlapad pasltarvaa avargsldgs
      121 wqrlkacede tcrwayydrs pagrgrwcsm evcgarakmr ayrarrage
//
LOCUS       WP_010642904             340 aa            linear   BCT 01-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Streptomyces
            albidoflavus].
ACCESSION   WP_010642904
VERSION     WP_010642904.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..340
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35768
     Region          1..>44
                     /region_name="MalE"
                     /note="Maltose-binding periplasmic protein MalE
                     [Carbohydrate transport and metabolism]; COG2182"
                     /db_xref="CDD:441785"
     Region          58..333
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mrrttlrsla giaalttlal tgcgtqqgla ddspaaagpa ertitakrla rltqpheqtg
       61 mtllegplld akgrllvvdv tapagepkmi rvdvrtgkgt pfhtdergay tsaqysphdg
      121 riyltdyahg eivslapggg drqvfftgkv dgaamhpddl afdrsgnlyv sdsrglsegt
      181 aegrvvrisr dgkkatvlad klaatngisf daeyrglwfs eltenrisyl rlddqgevts
      241 rhtairvdgg laqtdsiavd adgnlyqglh graamavydr hgarlatvev paghrglesa
      301 tnvaitpggt rayltvsgpa ggyvytfdal aegirqsngg
//
LOCUS       WP_010642906             118 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Streptomyces].
ACCESSION   WP_010642906
VERSION     WP_010642906.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..118
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12763
     Region          9..116
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mpiatldvvv ldtpaplala tfyqailggt veqpadywve lhgpgvklaf qeapdmvppt
       61 wpspdnsqqf hldlnvpdle aaesqvlalg arpldtrpdr sfrvyadpsg hpfclcre
//
LOCUS       WP_010642907             405 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dipeptidase [Streptomyces].
ACCESSION   WP_010642907
VERSION     WP_010642907.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..405
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43350
     Region          22..385
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mtstptgpvp naellptale flaehpvvdg hndlpwalre qvrydldrrd iaedqsahlh
       61 tdiarlragg vgaqfwsvyv rsdlggdeav satleqidcv dqllarypad lapaetadam
      121 ekartegria slkgaegghs innslatlra lhalgvrymt lthndniawa dsatdterlg
      181 glsafgrevv remnrtgmlv dlshvsagtm rdalatseap vifshsssra vcdhprnipd
      241 dvlgrlpang gvamatfvpk filpaavewt lradenlrah ghhhldtgee amalhrafea
      301 ahprpvataa tvadhldhmr evagvdhigi ggdydgtaft pagledvagy pnlvaellsr
      361 nwstadlakl twgnavrvlr daeavsrdla arrgpsnatl eqldg
//
LOCUS       WP_010642926             387 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010642926
VERSION     WP_010642926.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..387
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41831
     Region          15..297
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mtetisrsdr gkknmrvtlm gagtnlvlff tklaggifgh sdalvadavh slsdllsdlg
       61 lilamhfssq ppdqehpygh erfetlaalg tgtllalngt gigyeavqrl vighygmpav
      121 wtlyiaafai faketlyqit irvarktrsa alranawdhr tdaissvivl igiggsllga
      181 pyldsvvali valmvlrigl vtawealqel adrglddavl aqirevilgc egvrdlhllk
      241 trkvghqala evhlqvtnpl lsvseghqia ervrmsllqa vddlvdatih idsendeegg
      301 avlpprsvid ekvesgllar nlplpqqmtl hylkdgvvic lrypfppaas leslqaqekq
      361 iqealqgkvs glqrvdvawq tsateke
//
LOCUS       WP_010642946             266 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Streptomyces].
ACCESSION   WP_010642946
VERSION     WP_010642946.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..266
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26670
     Region          69..263
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtssphadad arpaaalaal taralgtcar tpsllltplf tsafflviye aqlsavagta
       61 tpggryvdlv lplcllttaf tggatagqll vrditsgyha rlwltpvprw allaapvlag
      121 iavltaqaaa ltglgvllga tpaagpgala alvgatvllg tgflllaaav glhtgntaav
      181 gsvtlvffpl sfftatfvpr dllggwmgta adlnpltppl ealrgllald wpdqtpwpga
      241 avtavilvlg avaarlalvr rtrtgv
//
LOCUS       WP_010643072             603 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Streptomyces].
ACCESSION   WP_010643072
VERSION     WP_010643072.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..603
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66699
     Region          8..507
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          540..600
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mavnlvnvea vskvygtral ldgvslgvse gdrigvvgrn gdgkttlirm lakleeadtg
       61 rvthsgglrl gvltqhdsld paatvrqeii gdladhewag nakirdvltg lfggldlpgf
      121 pqgletvigp lsggerrria laklligepd liildeptnh ldvegiswla ghlrarrsal
      181 vcvthdrwfl dqvctrmwdv qrgdvheyeg gysdyvfara ererraatee tkrqnlmrke
      241 lawlrrgapa rtskpryrie aaneliadvp pprdtselmk fasarlgktv fdledvtvqa
      301 gpkvllqhlt wqlgpgdrig lvgvngagkt sllrtlteaa rtggeaqpva gkvvvgktvk
      361 lahlsqevae ldpatrvlea vqqvrdrvdl gkgremtagq lcekfgftke kqwtpvgdls
      421 ggerrrlqil rllmdepnvl fldeptndld ietltqledl ldgwpgsmiv ishdrffver
      481 ttdrvfallg dgalrmlprg vdeylerrrr maetegpsap vpaqqaerke kpaadqraak
      541 kelqrlerql dkistreqkl htqiaenatd fakvaeldae lrqlsgerde lemrwlelae
      601 dag
//
LOCUS       WP_010643104             229 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor
            [Streptomyces].
ACCESSION   WP_010643104
VERSION     WP_010643104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..229
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24184
     Region          14..130
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
     Region          169..224
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 magheeqttp pirvlvvddd qlvrlalrlv idgepdltvv aeatdgdtal teaelhrpdv
       61 vlmdvrmpgr dgldatrell trpsppavlm lttfdaddlv lgalragalg fvlkdtppar
      121 iaeavrtvaa gepvlspsvt arviaaatgp hssdartaar eaarrrlatl tdrerdtaha
      181 iaeglsnpei atrlhisvat vkahttalft klsaanrvql allvrdaed
//
LOCUS       WP_010643167             151 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Vibrio campbellii].
ACCESSION   WP_010643167
VERSION     WP_010643167.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..151
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16996
     Region          18..148
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtdtaknlvn ryddlistlq agfvplillf crlwvawvff nsgliklssw gstlylfele
       61 yqvpilpwel aaylgtaael vlpvflalgl itrpmaailf vfniiavvsy pllwekgfyd
      121 hqlwglmilv vivwgpgpls ldhilkkkit n
//
LOCUS       WP_010643215             212 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Streptomyces sp. N1].
ACCESSION   WP_010643215
VERSION     WP_010643215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. N1
  ORGANISM  Streptomyces sp. N1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Streptomyces sp. N1"
                     /db_xref="taxon:576456"
     Protein         1..212
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=22583
     Region          26..199
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mpapdpaslh sedpapvtge tlrgddwygr dltgltytac dfydtdwtet tgsgarfdrc
       61 tfsgvrfnvs hltatafthc efrrcsffda rldqckavgs tfdacsfrll kvtggdwsft
      121 sfpradlrka vldgvrirea dlrgarldea evtgtdlsga llagvsltga dlrgsdlsal
      181 dahtldrtal agaridpaqa vgiavamgfe va
//
LOCUS       WP_010643257             407 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Vibrio campbellii].
ACCESSION   WP_010643257
VERSION     WP_010643257.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..407
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=44872
     Region          9..407
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mktiapqlkn yrwkginssg kktsgnvlam teievrerld aqhikikklk kgsisfitki
       61 shrvkgkdit iftrqiatml mtgvpivqal klvsenhkka emksilmsvt raveagtpms
      121 kamrtasthf dplytdliat geqsgnlsqv ferlatyrek seqlrakvik aliypamvvl
      181 valgvsylml trvipefekm ftgfgadlpa ftqmvlnlsa wtqnwgpfig lsfvsllisg
      241 kimsqrsdsf rllaarsslr vpilgpvlsk aaiakfsrtl atsfsagipi ltalkttskt
      301 sgnmhyqlai eevyrdtaag mpmyiamrhc hvfpelvlqm vmigeesgrl ddmlnkiaai
      361 yefevdntvd nlskilepli ivflgvvvgg lvtamylpif nlmsvlg
//
LOCUS       WP_010643258             192 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            albidoflavus].
ACCESSION   WP_010643258
VERSION     WP_010643258.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20792
     Region          8..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msvqerkere radrerliva tarelaeqqg wdavttrrla erieysqpvl yshfrgkrei
       61 igavalegaa elaaslraat gaerdprgrv salaraylaf aarnpavyda ifqldgglaf
      121 aredtpeplq dafaallesl gevsgdgvhp alftevfwas lhglatlars grlppgdaea
      181 rtellvdrla vl
//
LOCUS       WP_010643273             532 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA carboxylase subunit beta [Streptomyces].
ACCESSION   WP_010643273
VERSION     WP_010643273.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..532
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56668
     Region          21..530
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtvlataldt asaeyaahre allgkidald aehakalagg gekyverhrg rgkllarerv
       61 ellldedtpf lelsplaawg seyavgasli tgigtvsgve clitandptv rggasnpwtl
      121 kkarraneia fanrlpcisl vesggadlps qkeifipgga lfrdltrlsa agiptvavvf
      181 gnstaggayi pgmsdhvimv kerskvflgg pplvkmatge esddeslgga emharvsgla
      241 dhlaedepea llrarrvvar lnwrkahadp apaeepkydp dellgivped lktpfdphev
      301 iarlvdgsdf dafkplygps lvtgwarlhg ypvgilanaq gvlfseesqk aaqfiqlanq
      361 rdipllflhn ttgymvgkey eqggiikhga mminavsnsr vphlsvlmga sygaghygmc
      421 grayeprflf awpsaksavm gpqqlagvls ivarqsaaak grpyddeada glramveqqi
      481 eaeslpmfls grlyddgvid prdtrtvlgl clsavhtapv egarggfgvf rm
//
LOCUS       WP_010643298              85 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Vibrio campbellii].
ACCESSION   WP_010643298
VERSION     WP_010643298.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..85
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=9160
     Region          1..81
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkkrnscgft lleliiaivi lgilavvaap rflniqdday eakmeaiadq fetavrftqs
       61 qwlvnggtpe aqqdlegygg gelck
//
LOCUS       WP_010643336             153 aa            linear   BCT 01-JAN-2025
DEFINITION  NfeD family protein [Vibrio campbellii].
ACCESSION   WP_010643336
VERSION     WP_010643336.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..153
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=17315
     Region          7..152
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mdlfsllegv tfwhwiafgl allavellgt agyflwlgls alivgailsf lpiswqmqws
       61 tfaafslvtt wlwwrkqwsk drksdkardl nqkhkqlign ivtleedfti gmnrlrvadt
      121 twsaesehdl pagtrveiva vegiilkikp vsr
//
LOCUS       WP_010643375             145 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Streptomyces albidoflavus].
ACCESSION   WP_010643375
VERSION     WP_010643375.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..145
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15402
     Region          2..125
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 meprislitl gvtdlararr fyealgwrgq eveetvffqa gglglvlwgr eklardsgya
       61 eagpatgfgg ivlahnvrsr eevdallaqa eraggrvtkp aaasphgfys gafadpdghp
      121 wevahnpgfp laedgtltlp dfdtl
//
LOCUS       WP_010643359             174 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Vibrio campbellii].
ACCESSION   WP_010643359
VERSION     WP_010643359.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..174
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18437
     Region          1..164
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mkiiafgast sstsinktla tyaanlvega evqvldlnsy dvplfsedke keigqaedak
       61 afladiatad alvisfaehn gsypaayknl fdwatridrn vfqnkpavyl atspgpgwaq
      121 tvlaaatgsa pyfgaevkas qsipsfydnf dletgqfrna evaeqvkaav aaln
//
LOCUS       WP_010643405             355 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Vibrio campbellii].
ACCESSION   WP_010643405
VERSION     WP_010643405.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..355
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40323
     Region          <63..>176
                     /region_name="PTZ00341"
                     /note="Ring-infected erythrocyte surface antigen;
                     Provisional"
                     /db_xref="CDD:173534"
     Region          205..344
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 msnndilsse qalddyfsal lgeevevieq eeeldllaqe lssaepepep epepepepkl
       61 qlqyaepesy qysdsyspel eapnledvqr llsqlestnv vaeldideil eqntidiate
      121 akamepeiev etavetveei qewvideepi ptveveqpep vwerleiemv eptvdvevei
      181 eqhtetetel eteagaklpn twestqrsad fqvlyfdvng vtfavpldel ggihriteln
      241 hligrpawyl glqtsreqqf dvvdtakwvm adklrddnyk dnyqyvvmlg esmwglasnq
      301 lmgtetlnid kvrwreqagk rpwlagmvke kmcalihvqa lidmlnagld vksln
//
LOCUS       WP_010643406             259 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Vibrio campbellii].
ACCESSION   WP_010643406
VERSION     WP_010643406.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..259
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28623
     Region          1..248
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mivwsvanqk ggvgkttstv tlagllsqkg hrvlmvdtdp haslttylgy dpdavtsslf
       61 dlfqlktfsr etvkplilet elegmdiipa hmslatldrv mgnrsgmgli lkralqavaq
      121 dydyvlidcp pilgvmmvna laasdrilip vqteflamkg lermirtlti mqksrpggfk
      181 ltivptmydk rtkaslqtlt qlkkdypnqv wtsavpidtk frdaslkhlp ashfasgsrg
      241 vfaykqlliy lerlafdeq
//
LOCUS       WP_010643496             191 aa            linear   BCT 01-JAN-2025
DEFINITION  PilN domain-containing protein [Vibrio campbellii].
ACCESSION   WP_010643496
VERSION     WP_010643496.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..191
                     /product="PilN domain-containing protein"
                     /GO_process="GO:0043107 - type IV pilus-dependent motility
                     [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=22036
     Region          3..183
                     /region_name="PilN"
                     /note="Type IV pilus assembly protein PilN [Cell motility,
                     Extracellular structures]; COG3166"
                     /db_xref="CDD:442399"
ORIGIN      
        1 mlyhinllaw renqreehrr rfiglillga iaalgvqwgi gkyyqyqqdq qqqrldylah
       61 yisqldtrie amkiaeqehs kilerlktve glqngrnktt efmnlmpsvi pegvyvdkik
      121 mndyeieisg isdstsrlat mldnmersak lldvdmhsiv hgkarfgkef qtfkvsfmfk
      181 dasikggkqh g
//
LOCUS       WP_010643530             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010643530
VERSION     WP_010643530.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..228
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23893
     Region          3..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msleltdvtl typdgdsrlt aldrvslyvp egsltavvgp sgsgksslla vaatlitpds
       61 gtvrvagret aglgrgelsa lrrsrigivf qqpnllpslt aaeqlqvmar idgrpkaaar
      121 erarelldav glagqadrrp hqlsggqrqr vniaralmnd arvllvdept saldrergaa
      181 vldlitelth rtatatvlvt hdphhlagad qvvrvadgrl taqgtpvg
//
LOCUS       WP_010643578             418 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Streptomyces].
ACCESSION   WP_010643578
VERSION     WP_010643578.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..418
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=45622
     Region          18..348
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 msteipddpt wdvavvggsl agcataihfa dkgyrvtvld kkpltdqhyk qlcthfvqph
       61 tvpllarlgl ghlsepahsv ttkavfvtpg gvvdtpgpgy dpeqpdsyal nlerrvldpa
      121 ireaarqrgv hflddtaveg vteddsgwtl dtrdargthr lrarlvvaad grrsrlagll
      181 gneaevrpne rvalfgyftg idtradnrsv fimnewdlac typlvggrte lvlfadkarv
      241 aewrgadsrm eeflkyfdgl aeapsvadav pespllgysd ypsqlrapva gsvpfvgdaa
      301 lsldamagvg cgfalltael ladsldgrsl agddlregld qyrrrfeenl lphaegicgd
      361 slvgkneatr lrmfetices qelsqkylal tgrmvrpaef qrefmrglma rskraart
//
LOCUS       WP_010643592             377 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010643592
VERSION     WP_010643592.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..377
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40187
     Region          1..376
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matvtfdkat riypgsekpa vdqleieiad geflvlvgps gcgkstslrm lagledvngg
       61 airigdrdvt hlppkdrdia mvfqnyalyp hmtvadnmgf alkiagvnks eirakveeaa
      121 kildltpyld rkpkalsggq rqrvamgrai vrepqvflmd eplsnldakl rvstrtqias
      181 lqrrlgittv yvthdqieam tmgdrvavlk dgllqqvdsp rnmydkpanl fvagfigspa
      241 mnlievpitd ggvkfgnsvv pvdrdalkaa adrgdttvtv gvrpehfdva eqngaaaeal
      301 tkqssdapag lavtvnvvee tgadayvfgs vdldggskdl virvssravp ekgatvhvvp
      361 rpgelhvfat stgerls
//
LOCUS       WP_010643600              69 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Vibrio campbellii].
ACCESSION   WP_010643600
VERSION     WP_010643600.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..69
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7504
     Region          6..69
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 msnkstgtvk wfnetkgfgf iqqengpdvf ahfsaiqgdg frtlvegqkv efeitqgqkg
       61 pqaekitlv
//
LOCUS       WP_010643680             430 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Vibrio campbellii].
ACCESSION   WP_010643680
VERSION     WP_010643680.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..430
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47956
     Region          1..416
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfssqgfap evvkalaecg yekltpiqqk aipmarkghd ifataqtgtg ktaafslpii
       61 qqllesgrsa srktaralim aptrelaeqi adnikaytky telsvaaifg grkmssqvta
      121 leggvdilva tpgrleehie qgnvsvanie flvfdeadri ldmgfihavr kimmdvdtdp
      181 qimmfsatts sqlnllakdi lrkpkrieie ranttaqtia hvlypvdqer ktellselig
      241 rknwkqvlvf vnyketandv vkelkldgik avvchgdraq sarrraleef ktgkarvmva
      301 tdvaargldi edlphvvnyd mpflaedyvh rigrtgragk qghavsfvnr eeeltvvqve
      361 nliqqrirri elagyepkqr esyieklnsk pafknrqgrr nnpnqsatdq gsaerrlamv
      421 krlkarrssk
//
LOCUS       WP_010643729             497 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [Vibrio harveyi group].
ACCESSION   WP_010643729
VERSION     WP_010643729.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi group
  ORGANISM  Vibrio harveyi group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Vibrio harveyi group"
                     /db_xref="taxon:717610"
     Protein         1..497
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54250
     Region          5..481
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(62,64,68,71,75,108,111..112,121..128,133,136,139,
                     232,236,239,242,244,417,419..420,422..423,426,429..430,
                     432,434..437,446,450,452,466,473..478,480..481)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(148..151,159,174,177,207,224..227,230,248..250,282,
                     382,384,410)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(151,248,279,282)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mtrtvplfid gefresqatd wvevtnpatn eviarlpcat deemhaaies akatftcwkd
       61 vavserarlm lryqhllkeh hdelatllsh etgkifadak gdvwrgievv eqaaniasnm
      121 mgetvenvat didsysliqp lgvccgitpf nfpamiplwm fpiaiasgnt fvlkpseqvp
      181 ltsirlaelf eeagapkgvl qivhgrkeqv dlllkhpdiq avsfvgsvpv aqyiyttgtq
      241 nfkrvqafag aknhmvvmpd anknqvvnnl vgssvgaagq rcmaisvavf vgsskewiad
      301 lkqemakvhp gawddenaay gplisaqakq rvlglieegk qqgavceldg sqcevegfpe
      361 gnwvgptlfs gvttemsiyt qeifgpvlvc ievdtlqeai elvnrnpygn gtsiftanga
      421 aarkyqheiq vgqvgvnvpi pvplpffsft gwrgsfygdl haygkqavrf ytetktvtar
      481 wfdddiptgp nltinlr
//
LOCUS       WP_010643746             125 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nuclear transport factor 2 family protein
            [Streptomyces].
ACCESSION   WP_010643746
VERSION     WP_010643746.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..125
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13555
     Region          13..106
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mqeetarsai dtfisafnas ddsyvtalls qaltsdvvfw gplgrsegia averfvldir
       61 rhpagigtmv rcsavdmpde waryqwvftt pdggprlagt dvvhlrrsli dqvivfagei
      121 epsvs
//
LOCUS       WP_010643761             158 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Streptomyces albidoflavus].
ACCESSION   WP_010643761
VERSION     WP_010643761.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..158
                     /product="VOC family protein"
                     /calculated_mol_wt=16605
     Region          13..134
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(13..18,20,35,49..50,57..58,60..62,79..81,83..88,94,
                     115,120,128..131)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 mpatetvpaa yrhavvphll vddadaalaf yqrafgaepr frldgdqgev vhaeltvaga
       61 vmmlgdarda lrspaalggt pvilhvyvpd vdtltarata agaellegpa dqfhgdrtam
      121 lrdpfghlwi flthledltp eqiaerlaea dgtagatg
//
LOCUS       WP_010643831             191 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Vibrio campbellii].
ACCESSION   WP_010643831
VERSION     WP_010643831.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21767
     Region          2..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 markanfdrd ekllvamdvf wrkgfantsi sdltdelsin rfslyntygd kqqlyyeald
       61 aylkkvslps lndlekddas lpelesflks ftelqrkrnc gcfiqnalie hagedddvlr
      121 kghflfdhli diiadaltna qketlvpktl kpeelarfvl nnmqgmrvlg kakryadldt
      181 alscllvlir k
//
LOCUS       WP_010643905             208 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Vibrio].
ACCESSION   WP_010643905
VERSION     WP_010643905.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21918
     Region          1..206
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdlssillfa vaclginmip gpdviyivsn tmkgkmasgm kaalglgvgy fahtlaaclg
       61 lsaivlssal afsivkwmga aylmylgiqs lfsmwrgdsn lkfdesvean knvfvqgviv
      121 svlnpkvalf flsflpqfie pslgsvstql fvlglvfsal atacnvlyas vgcwvfnrpn
      181 sriytraleg vsgalligla gkvaiseq
//
LOCUS       WP_010644029             229 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Vibrio campbellii].
ACCESSION   WP_010644029
VERSION     WP_010644029.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..229
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24500
     Region          5..229
                     /region_name="carb_red_sniffer_like_SDR_c"
                     /note="carbonyl reductase sniffer-like, classical (c)
                     SDRs; cd05325"
                     /db_xref="CDD:187586"
     Site            order(9,11..14,34,58..59,81..84,106,133..135,151,155,
                     180..184,186,188..189)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187586"
     Site            order(59,65,100,105,108..110,113,116..117,137..143,149,
                     152..153,156..157,160..161,163..164,167..168,228..229)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187586"
     Site            order(107,135,151,155)
                     /site_type="active"
                     /db_xref="CDD:187586"
ORIGIN      
        1 msqtvfitga nrgiglslte lylqqgdqvh atsrnlaesk elqalastyt tltlheldvt
       61 nyphvaqlak elpaidllin nagyygpkgy gfgntdveew rkvfeintia plklveafyp
      121 llqagstkki acisskvgsm kentsgggyi yrsskaalns vvkslsndlt segfsvlalh
      181 pgwvrtamgg pnaliepqts aaglakviaq stqknsgqfi nydgtqlpw
//
LOCUS       WP_010644057             628 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Vibrio campbellii].
ACCESSION   WP_010644057
VERSION     WP_010644057.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12036995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..628
                     /product="methyl-accepting chemotaxis protein"
                     /calculated_mol_wt=68375
     Region          39..256
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          <265..627
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 msaklkills mialstitil stsllnwsdf qtsstlnskq qlqyksqlis dalsqkisry
       61 fdillltseq idieakskin iastvdlitk amrtagvvnv yvsledgtsy saktnglipg
      121 fnarskqrew ylramngeek iitrpfssst gdtvmalaqp iyrdnqvvgv ialnllvndi
      181 sayttqltse nqvfvsrndg filsakdrsl igknifteip qlklqdpeke esfeyqhknt
      241 eyvgsaseip slgwsvwtwm tegsinqdsn dnlvetlits tiflvlstvc iyfvveklvy
      301 kpiggepkei ehlvtqvakg dlcmkhepsn sygvngavfn mvgdlketis tirvssdell
      361 nfasgiskaa knvnlgssaq meqleqtsta msemsvavne vaqnaqrasd saiqasaaav
      421 hgnelfvevn dsiislsnai advstvinsl gektvnigav levirdiadq tnllalnaai
      481 eaarageqgr gfavvadevr nlanrtqest neiqqviaal qqeannsiem mntnklaaen
      541 tlnkssqaqe slskildsit iiedmntqia tateeqtlva geinqsivci ndqardtyel
      601 sisnqeksne ligisehlks tvsvfkln
//
LOCUS       WP_010644164             327 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_010644164
VERSION     WP_010644164.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34932
     Region          8..224
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mntedhvidv tdlrrvyggg feavrgvsft vgrgelfall gtngagktst levleglarp
       61 asgrvrvlgh dpfserdavr prigvmlqdg gfpseltvre tlrmwagcts garpigeale
      121 mvglgkradv rvkvlsggek rrldlalall grpevlflde pttgldaegr qdtwslvrel
      181 raegttvllt thyleeaeal adrlailheg riasegtved vvsaqpsrit fdlpdgwfpg
      241 dlppldqlgv tghshdgrtv rlmtqnlqqa atslllward agvslgsldv raasleeafl
      301 hiareadgrg dsataaasld prketaa
//
LOCUS       WP_010644272             615 aa            linear   BCT 01-JAN-2025
DEFINITION  acyltransferase family protein [Vibrio campbellii].
ACCESSION   WP_010644272
VERSION     WP_010644272.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..615
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=68220
     Region          1..335
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          390..597
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 mtyraeidgl raiavllvif fhadiqafag gfigvdvffv isgylittiv indldknqfs
       61 lfdfyerrir rilpllllvi avcyllswwl flphahkevg efsvssilsa snvllylkgh
      121 nyfgleeqan plfhtwslgv eeqyyvvipl llmllargkl msyltffivv falslmtvwy
      181 asgdpdfafy mifsrawela agslialamr ktvikpnntl amigltlvla ssllfdkskd
      241 gtgimllipv igttliilfs skdntlgkal slksvvfvgl isyslylwhi pllvfyryvl
      301 tagqdfslaf ylvalfafsc ltwrfvekpf rsrkkigmst ltaslvlvtl pllafgfvgh
      361 knggfpgrsa ffeamrvnng ygiacngntg indtcssssq psvavlgnsh smvfvqqlan
      421 dtptgvvqlt qdscavgyvd kvsgtnhlsc snfftdaiet ilntpsirrv vissnfnkel
      481 skqdyqaslt rllneledre vlvfgptpsa phaigeclwk arlfgdntgn ecdftprqsh
      541 phhvatlaay fdqfehvefv dltnyicqeg kcamkvgsnn amytdashls ykgaeivlgs
      601 yqkevmsnqq vtaqy
//
LOCUS       WP_010643806             309 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Vibrio campbellii].
ACCESSION   WP_010643806
VERSION     WP_010643806.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The SHS2 module is a common structural theme in functionally
            diverse protein groups, like Rpb7p, FtsA, GyrI, and MTH1598/TM1083
            superfamilies
  JOURNAL   Proteins 56 (4), 795-807 (2004)
   PUBMED   15281131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12255408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..309
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=35240
     Region          3..148
                     /region_name="SRPBCC_1"
                     /note="Ligand-binding SRPBCC domain of an uncharacterized
                     subfamily of proteins; cd07818"
                     /db_xref="CDD:176860"
     Site            order(6,8,10,19..21,23..24,35,49,51,53,55,57,69,70,79,81,
                     95..96,98,100,108,110,112,114,127..131,133..135,137..139,
                     142)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176860"
     Region          165..304
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mlsyqvnrsi eiektqseti nylkdftrwp ewspwiilep dceltysdeq gvvgagyqwn
       61 gkrigtgamv lestqehrld melhffrplk thakvtlivt psqagctvew lmqsrvpwfl
      121 fflknvfksm iemdydrglr mlksqletgq vlslltdlgs rkqnevsyig lsgagtisdl
      181 gpmmqshvar lyemaeqenl svtgelfcyy lsmdmkqgyf efitclpvkt gvvatgefva
      241 gtipesetyv iehkgeyqfl gnawsyamnl tryngikvkt qplgieryld npsdtdkadl
      301 ltevilfkk
//
LOCUS       WP_010644314             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Streptomyces].
ACCESSION   WP_010644314
VERSION     WP_010644314.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..239
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24571
     Region          5..178
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mydptvarlt yrallgrrra lilfvlpall lviaaavrll tgaddstaea vlggfslavm
       61 vpiigvvagt gaiapeiddg svvyllakpi krptiiltkl fvaigvtmaf saiptliagf
      121 ilngnggqla vaytvaalva siayaalfll lgtvtrhavv fglvyaliwe glfaslisga
      181 rtlsvqqwal avaekvtgge avtsdvalpt avillvaatv latwyagqkl rsltvagee
//
LOCUS       WP_010644319             133 aa            linear   BCT 01-JAN-2025
DEFINITION  HIT family protein [Vibrio campbellii].
ACCESSION   WP_010644319
VERSION     WP_010644319.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..133
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15331
     Region          1..128
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mativeqivn reidsvivye sdkviafadh dpinfghili cpktqyrtfi dlpesvflei
       61 idvardlykr ieakfnpdgi gfmqnngeap hfneldhyhl hifprfhgdq ygwvsselgi
      121 qtmdklresl kdl
//
LOCUS       WP_010644327             502 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Streptomyces albidoflavus].
ACCESSION   WP_010644327
VERSION     WP_010644327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..502
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55838
     Region          7..480
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdlalapetl srwqfgittv yhflfvplti slagltaglq tawvrtgkek ylkatkfwgk
       61 lflinialgv vtgivqefqf gmnwsdysrf vgdvfgapla fealiafffe stfiglwifg
      121 wdklppkihl aciwmvsigt ilsayfilaa nswmqhpvgy ridevtgrae ltdfwlvltq
      181 ntalaqffht maaavltgga fmagiaayhl mrkkhidsmr lslrlglvtl avgglltavs
      241 gdtlgkimyq qqpmkmsaae alwegeepap fslfavgdvd kghnvvtvev pgllsflahn
      301 nftdrvpgin elnaqyqeky gpgdyrpnip vaywgfrwmi gfgmtsfgig llglwltrrk
      361 fllphrlrtg edevpnlvlt rtrllsprls rlywrltlwt lafpliassw gwiftetgrq
      421 pwavygvlrt adsvspgvsq gevltsmivf tllyavlavi evrllvkyvk agppeltead
      481 lnppkkiggd psdadrpmaf sy
//
LOCUS       WP_010644402             277 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Vibrio campbellii].
ACCESSION   WP_010644402
VERSION     WP_010644402.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..277
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30879
     Region          20..269
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mftvmmpnnq splisaeeaa kklndqstkf fdvrgrwged iqcsrqafls ehitgarfld
       61 wtktfvntdl pialapvaei eqaqadfaal ginqddlvil yddyfhmfag riwwamrywg
      121 fhnvrvldgg lkrwkflalp tsnnlnsarv gnyvvkkeqs wialsddvln rsdntvllda
      181 rrsenffasd vshipgainv pfatlldsdt gmfkapeeik qvievaisgq didhvisscg
      241 sgyagtilli alqligidst lydgsyaewk alqypsn
//
LOCUS       WP_010644339             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Vibrio].
ACCESSION   WP_010644339
VERSION     WP_010644339.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..135
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15103
     Region          1..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mykgsclcgs iqfeldgivt diihchcslc rkasgsayat ngfinaqelk ltdqdktltf
       61 yessegkrky fckscgspiy ssnvqspery rlrlgaldsd iserpishnf vtskanwedl
      121 naelphyekh epgrk
//
LOCUS       WP_010644443             422 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Vibrio campbellii].
ACCESSION   WP_010644443
VERSION     WP_010644443.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 422)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..422
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46117
     Region          23..251
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          156..419
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mgklipvsvr lawlnlqrnr rrsllsmlii aiavfaltsa ggfglytyds lkestardtg
       61 hltlttpgyf akeeemplsn glthadditk qliglnevrg vqprvefsgl isngnkssif
      121 igigvneref dmkgpfldvr egqtlsniha lrydpaepev mlgvdlannl svhvgdwitl
      181 latttdgaln aydfkvrgiy stgvpeldkr qlyvhinsaq sllgsdkvsa lsvflfdtsl
      241 tnqveqqvas vlsknkqnfg dqdieitpwq eraffylkvk glydrifgim gavmalvvfv
      301 alfntmtmsv tertreigtl salgsyprei iagflreagl lavigsliga lftglvtvll
      361 mvvdvqmppp pgrtegyplt iyfswelvav agfavlmicl vaaffsarkg vnkpiteali
      421 yv
//
LOCUS       WP_010644471             480 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type IV secretory system conjugative DNA transfer
            family protein [unclassified Streptomyces].
ACCESSION   WP_010644471
VERSION     WP_010644471.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..480
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51162
     Region          34..426
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mhhpqphefg yalgfsqrpk glelwsradr acrvigpmgs gktlrffapt irhwagpvla
       61 tstkpdlvel tldarrrdga pvlafdpqni apslprvrws pitgaeetet ammrakalva
      121 gsrtpgkaaq ssegsnfyrg qaakvlaafl haaaldgagl dwvlrwarsl tdpaplgils
      181 ahpgagpgwa hmlrtsttgd srtvgntatt ldaalepfmh etvvralqgn gtaaptdfre
      241 vldaggtvyl lgkdsevnsv aplttavaed lldiaeahal sapagrldpp llaaldeapn
      301 iapipslrqr vadgrgrgit viyglqgwas ararfgedta nelasftnnl ivfggakdpa
      361 flrdmsdlcg qverarttkt rsggdrghst athmalesvl rgdeikglpd ghalvladnl
      421 ppvvtqldgm wtwdsweeie ghvralraen esarirqdae rtaqaaehaa awtrqrevaa
//
LOCUS       WP_010644525             177 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Vibrio campbellii].
ACCESSION   WP_010644525
VERSION     WP_010644525.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12134272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..177
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19959
     Region          11..147
                     /region_name="Acetyltransf_3"
                     /note="Acetyltransferase (GNAT) domain; pfam13302"
                     /db_xref="CDD:379112"
ORIGIN      
        1 mpaqptlfte rlilrpfhhn dcervallag ekiiadmtan vphpyetsma ktwidchgpm
       61 fyerrgvvya itlrntgell gavslpried gygilgywig vpywgkgyaf easktlvefa
      121 qsyfelvgir vihlaenqrs ksvikklnvp yignttlsmq gverevcvyq crfeann
//
LOCUS       WP_010644538             412 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Vibrio campbellii].
ACCESSION   WP_010644538
VERSION     WP_010644538.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..412
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44660
     Region          1..412
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mlfstlslss elihalpkdf kkptdiqala ipellsgkdv lalantgsgk tlayglplle
       61 klsvnpeqka lilvptrela tqvseainqv gqaiglnaec lcggvnkelq lqalaadpki
      121 lvattgrlvd lannglelsn ihylvldead rlldmgfwpd vqniaeqvsn qrqtamfsat
      181 fsdelkgkak qlmhapkqva ahqenstnqd iaemlylvnk gsktkaliel ikqnawaqvl
      241 vfigakenad glakklnkag ittnalhgnk sqaereeala qfksgqtqvl iatdllargi
      301 hieqlpvvin felpmhaety vhrvgrtara geqgvamslv chgetdalta irnltqrelp
      361 tqdlegfpvt dkpstgeskr aprdkkanrr tnakksikqf qgkpkrqask ak
//
LOCUS       WP_010644574             154 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010644574
VERSION     WP_010644574.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..154
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17044
     Region          8..145
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 maeqpeprpl davdrdilrl lqadgrasir svadtvhvsr anayarinrl medgvirgfg
       61 arvdheragq gacayitlki vqnswrtire elrrlpgaah ialvsgdfdv llmihaadnr
      121 alrelvltrl qsipdvlstr tllvfeeeel speg
//
LOCUS       WP_010644582             327 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-quinone oxidoreductase [Streptomyces].
ACCESSION   WP_010644582
VERSION     WP_010644582.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..327
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33741
     Region          1..323
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,122,126,129,147,150..152,171..172,176,191,
                     215..216,237..238,240,262..264,312,317)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mhaitipepg gpealvwapv pdpvpgegev lvevvagavn radllqrqgf ydpppgaspy
       61 pglecsgria aigpgvsgwa vgdevcalls gggyaekvav pagqllpvpa gvglktaaal
      121 pevvctvwsn vfmvsqlrpg etllvhggas gigtmaiqla kavgarvavt agspeklryc
      181 gelgadflin yreqdfveei revtagagad vildimgaky ldrnvkalat ngrlaiigmq
      241 ggtkaeldia tllrkrgavt atslrgrpas ekaaivaavr ehvwplidtg rvrpivdrev
      301 pmrdaaaghr vleesshigk vllvtge
//
LOCUS       WP_010644646             532 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA carboxylase subunit beta [Streptomyces].
ACCESSION   WP_010644646
VERSION     WP_010644646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..532
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56537
     Region          18..529
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 msvveespln saapadghlr draaelaalh ervrrgpger ateaqhakgk ltvrerlall
       61 fdegtfteie elrrhratgf gleqrrphtd gvvtgwgevd grtvfayahd frifggalge
      121 ahaekihkll dlaesagrpv vglcdgagar iqegvtalag yggifarnvr nsgvipqisv
      181 ilgpcaggaa yspaltdfvf mvrgtsqmfi tgpdvvqavt gevithdalg gadahasvsg
      241 vahaayddee scladvrhll sllpsnnrel ppaapgadpa srrtealldl vpadpgrayd
      301 mraviteivd dgevfeiqes watnivcvia rldgqavgiv anqpaafagv ldihasekaa
      361 rfvqtcdafn lplvtlvdvp gflpgvdqeh ggiirhgakl lyaycnatvp rvqlilrkay
      421 ggayivmdsr sigadvslaw pgneiavmga egaagvvfrr eiaaaddpea trarlvkeyr
      481 aelmhpyyaa erglvdsvid paetrsrlig altmlrakha plptrkhgnq pq
//
LOCUS       WP_010644662             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SCP2 sterol-binding domain-containing protein
            [Streptomyces].
ACCESSION   WP_010644662
VERSION     WP_010644662.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Burgardt,N.I., Gianotti,A.R., Ferreyra,R.G. and Ermacora,M.R.
  TITLE     A structural appraisal of sterol carrier protein 2
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (5), 565-577 (2017)
   PUBMED   28284963
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Dyer,D.H., Wessely,V., Forest,K.T. and Lan,Q.
  TITLE     Three-dimensional structure/function analysis of SCP-2-like2
            reveals differences among SCP-2 family members
  JOURNAL   J Lipid Res 49 (3), 644-653 (2008)
   PUBMED   18084051
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Bun-ya,M., Muro,Y., Niki,T., Kondo,J. and Kamiryo,T.
  TITLE     New aspects of sterol carrier protein 2 (nonspecific lipid-transfer
            protein) in fusion proteins and in peroxisomes
  JOURNAL   Cell Biochem Biophys 32 Spring, 107-116 (2000)
   PUBMED   11330036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007129
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..144
                     /product="SCP2 sterol-binding domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=15299
     Region          41..142
                     /region_name="SCP2"
                     /note="Putative sterol carrier protein, contains SCP2
                     domain [Lipid transport and metabolism]; COG3255"
                     /db_xref="CDD:442486"
ORIGIN      
        1 msvqqeqvte lidlvqsvpa kevegvvatr pggvdgaltl ifdllvsefn pakaegekgv
       61 fqfdiacadg rkhhhvevvd gtcrtgqgvh dhpditigik fpdmlamgvg klpgakaflt
      121 gklklrgspl mgtklgewfd hpet
//
LOCUS       WP_010644675             128 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Vibrio campbellii].
ACCESSION   WP_010644675
VERSION     WP_010644675.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 128)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..128
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14354
     Region          5..108
                     /region_name="MutT"
                     /note="8-oxo-dGTP pyrophosphatase MutT and related
                     house-cleaning NTP pyrophosphohydrolases, NUDIX family
                     [Defense mechanisms]; COG0494"
                     /db_xref="CDD:440260"
ORIGIN      
        1 mkniamgvvv rdgkvliqkr frrgqgmvfe fpggsidpge sgneaavrel weetglqglk
       61 rlgshqaknd fggeihyvvl ragndtepqm idevrqqtff wlepsaiplg dfyradiefi
      121 enhlsqyt
//
LOCUS       WP_010644796             284 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LLM class flavin-dependent oxidoreductase
            [Streptomyces].
ACCESSION   WP_010644796
VERSION     WP_010644796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..284
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29391
     Region          57..284
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mkigigipnq irdvkadvip ewarraeeag fstlgsvgri aypgvmdtva laaaagatsr
       61 iglisnvllg pvwpahllak eaqsidgvsg grltlgiglg grpddfvveg lgprgtgkrl
      121 drdietyksv wrgetpagcd nplvpqgsre vpllfggmvq asfnrvarsg rgyigasvpa
      181 nmiagafdgv raawkeagre gspylvaiay yavadaeggr anvydyysta gaetagfias
      241 avsggtdaik ktvgefeaig adelilnpts ddvdelrrva dvvl
//
LOCUS       WP_010644805             147 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: arsenate reductase ArsC [Streptomyces].
ACCESSION   WP_010644805
VERSION     WP_010644805.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..147
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=15081
     Region          16..139
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(21,23..28,114,116)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mpapeptpar lparprvlfl cvhnagrsqm aaaflrhlag eavevgsags apaetvnpva
       61 vaamaeagid lsgarpralt pedvraadlv vtmgcgdtcp vlpgtayrdw alddpagqal
      121 pavrrvrdei grrvrelaee lgvaasa
//
LOCUS       WP_010644860             206 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Vibrio campbellii].
ACCESSION   WP_010644860
VERSION     WP_010644860.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..206
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22326
     Region          1..206
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mntalltmfi ptfffvsitp gmcmtlaltl gmsigyhrtl wmmagelvgv alvsvsavlg
       61 iaaimlnypw lftalkligg gyllylgiem wrsrgklain venvdvptsg nwdlvlqgfv
      121 taianpkgwa fmisllppfi nqnaalapql ivlvsiilmf eficmslyat ggkglkrllg
      181 qsknvrlmnr iagtlmmgvg vwllms
//
LOCUS       WP_010644867             222 aa            linear   BCT 01-JAN-2025
DEFINITION  SH3 domain-containing protein [Vibrio campbellii].
ACCESSION   WP_010644867
VERSION     WP_010644867.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..222
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25544
     Region          59..>133
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 mkkalialai llllggagag yyfffmqkde pvveqkpepe qpsepeekpk pimdleapap
       61 eiteyyvter rinvynkper qalivdslyk gekvsvleka dgwfrlsdyi vyeeggeeta
      121 ewvdskglsd aepvikeqer leildgylqk sddlkthldm frsktqqlld detcdpsdfe
      181 elggwvrsvt ykkrnvyfiy cggleqenki yldvdkgeif yr
//
LOCUS       WP_010644963             404 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Vibrio campbellii].
ACCESSION   WP_010644963
VERSION     WP_010644963.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..404
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43980
     Region          6..391
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(17..18,21..22,25,60,107..108,110..112,115,140,
                     143..144,147,221,224..225,228..230,233,263,267,317..318,
                     322,326,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 msifrfpilv wlgigiliic lgirqsfgif mmpisdhfqt greffsfaia lqnllfgvfq
       61 pfvgmasdrw gakriiilga isyafglylt staveltmmy lslgvlvgfg lsatsyvivl
      121 gavakvvpaq haakafgltt aagsfgmfam ipgaqallsd fgwqgalqvf avlcsfmvmf
      181 alfmrsakpq tnnaasaqed kqtlkealte afahkgywli hagffvcgfh vmfiathlps
      241 yladkdlpas taamalayvg ifnifgsyfw gvmadrfnkr hvmsalylmr tvvigafvtl
      301 pvtehtaaif ggaigfcwlg tvpltsglvr qifgarylst lyglvffthq vgsflgawvg
      361 griydyygsy dpiwwstvvl afiaalihlp indkpvprlt mata
//
LOCUS       WP_010644910             218 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Vibrio
            campbellii].
ACCESSION   WP_010644910
VERSION     WP_010644910.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..218
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24582
     Region          20..163
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 mlsntnrtei kkgahkaisd vdklhaiide sliahiaitn esgpvvtpml awrvddyvyi
       61 hgannsrllr slkqgvqtcl tftlfdgwvl arsafhhsah yrsavvfgqf emvadnqekd
      121 rllnhfieqi apgrtkdirl snekelkatm llriplteas vkisnfgvnd daqdmdipvw
      181 agvlpyrtvv gplqacedly egikepdyrh aypnrwqe
//
LOCUS       WP_010644983             280 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Streptomyces].
ACCESSION   WP_010644983
VERSION     WP_010644983.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..280
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29420
     Region          26..272
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mvllaadgva ieavhepadf dadvthdaag rvpvtvvahg ftgsagrphv rraaavfrry
       61 gavitfsfrg hgasggrstv gdrevldlaa avawarrlgh rtvwtvgfsm ggsvvlrhaa
      121 lyravgpnah gpghgdvrgs asadphgpah tdavvavsap arwyyrgtaa mrrlhwvvtr
      181 plgravgryg lrtrihtsdw dpvpldpaea aariaptpll lvhgdrdpyf pldhpralat
      241 aagpqadlwl epgmghaena adeallaria dwaarrapgg
//
LOCUS       WP_010644991             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfurtransferase [Streptomyces].
ACCESSION   WP_010644991
VERSION     WP_010644991.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..279
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31383
     Region          13..274
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 msrsdvlvda dwvqenlddp nvavvevded tsaydknhir nairidwtkd lqdpvrrdfi
       61 dqegfeklls akgiandtlv vlyggnnnwf asyaywyfkl yghenvklld ggrkkwelds
      121 rdlvaevpqr pataykakpq ntairafred vvdaignqnl vdvrspdefs gkllapahlp
      181 qeqsqrpghv psarnipwsk nanddgtfks deelkalyad eqvdlakdti aycrigersa
      241 ltwfvlhell gvenvknydg swteygslvg vpielgank
//
LOCUS       WP_010645041             177 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide biosynthesis/export family protein [Vibrio
            campbellii].
ACCESSION   WP_010645041
VERSION     WP_010645041.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..177
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19414
     Region          21..177
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mnslatlfsl vlvllstpsf asaneqdyll dtgdtisvqv ygeedlsinn ilitsdgyfd
       61 ypylgrikai nktpkqlkye ietglkgdyl inpkvmvain sfrlfyvnge vrkpggfeyq
      121 pgltiekaia laggltdras rksinltqha tgntvesvsm qrsvepgdiv fidqsff
//
LOCUS       WP_010645042             284 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Streptomyces albidoflavus].
ACCESSION   WP_010645042
VERSION     WP_010645042.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..284
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29880
     Region          5..265
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
     Region          5..>125
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mplsptfvlv hgafansfsf aplqaelgll gqrsvavdlp ghgfeatfpa syqapqdfaa
       61 laaepgsikg vtladnaarv iealerarrn gptvlvghsr ggatitavan arpdlvdrlv
      121 yvsawcpvdl pvgdyyaepe masvdpmafa psllgnpael gllrtnfrts dpaalatfke
      181 afgadltdde frtflntfqp desldagtea draqaatwgt vprtyvrlad dtsltpaaqd
      241 rmireadalt pdnpfdvhtl dgshlrwlvh pgpaaavlag laag
//
LOCUS       WP_010645066             292 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Vibrio campbellii].
ACCESSION   WP_010645066
VERSION     WP_010645066.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..292
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31339
     Region          5..288
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 meklrvafig lgvmgypmag ylskagyetk vynrtkakad kwaeeyqgva setpreaaeg
       61 cdivftcvgn dddvrsvvyg eegilvglka davlvdhttt ssdlavelae acvkhgnhfi
      121 dapvsggqag aengvltimc ggeqsifgrv spamdvyakq mtllgengqg qrckmvnqic
      181 iggvlqglse alllaqksgl diaqvvetlk hgaagswqme nrantmaedk fdfgfaidwm
      241 rkdlgfclqe aervglelpl tkkvdeqyad lqrdglgrmd tsvlikavak nq
//
LOCUS       WP_010645070             311 aa            linear   BCT 01-JAN-2025
DEFINITION  ADP-ribosylglycohydrolase family protein [Vibrio campbellii].
ACCESSION   WP_010645070
VERSION     WP_010645070.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..311
                     /product="ADP-ribosylglycohydrolase family protein"
                     /calculated_mol_wt=34136
     Region          4..309
                     /region_name="DraG"
                     /note="ADP-ribosylglycohydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG1397"
                     /db_xref="CDD:441007"
ORIGIN      
        1 mtlrnarslh aiigalvgda aslglhwlyd qelirqfgsp hpefhqpnrt eyhdkgyfah
       61 gskqvgdlth ygaqlvamld alvqtghyde aryirsfrew fdfggkwqgy tdkptkqtml
      121 niheleakel rvtlcgaddt qnpalskipp lvafhsdddk laklvdsavr vtnnndtavm
      181 yaqaiavmiq lalqgvapka cviaaqtiss tiandikrae amsersatsv aesvgmhcgl
      241 dasfvvichl lmnsesyett mreniycggd ssgraiplga ilgasyydtp msipnhwmdk
      301 talphrllqc l
//
LOCUS       WP_010645096             464 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Vibrio campbellii].
ACCESSION   WP_010645096
VERSION     WP_010645096.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 464)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..464
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51447
     Region          106..461
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mdmllifkiy lfyglalfai ffailfrdlr ksriaiasal pilalfgfih gfhewselyl
       61 vmyeheftlt kgvetfkvfk llfsfialga fawkmlgltd wknikaieyg avavialfaa
      121 slvirfgnke yaiyihdtan qvrwifglgs glisglamms yanileqegh gaslpfkltg
      181 lsliaygisa glltvdlglw vlivrmvcal silctlwial rvfddekskq lesniqisqq
      241 daklkelgel tsavaheikt plssatmscd llekqlpdne asqrhlarir qgleraaeis
      301 hevlnyahhk piqreivslq qvveqalsln qyrlegfavs tsldntlsvl gdagqleevv
      361 tniignaida sqehkqldie tyqdklmail sisdwgtgmp ldkiakaktp fyttkprgeg
      421 tgmglaisnq iilqhggeld lrdskksghi tgltveirlp rnie
//
LOCUS       WP_010645154             527 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Vibrio campbellii].
ACCESSION   WP_010645154
VERSION     WP_010645154.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..527
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59961
     Region          370..524
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(403,447)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(408,411..412,416,420,443,445..448)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(439,467)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 meqllskvtd agmdpssvag eealilwehi rlhiastnqe kahcyiisae yrskikqlqe
       61 sieelrhald llklpedved ilsvksslsd rlvekgdyns alteyiastn iaveygyide
      121 yvlaiigmgn lcdaygdhnr alryyqkida idhavgsrsl rlryklymla cyislqriga
      181 atdllsecee lsilvsdknl tgqihlyrak llrlqkeynk allaisqiqy atgkqhtvwl
      241 stmvkietay clnevghqsl snlllastgk rineqaspli anrfynamsq vcasqglfke
      301 alnyekkafr vesdlvkhip iselgpaqlr rlsrfelqlk lilseienke lkettkqhkn
      361 tvaqlqqdvf tdpltslhnr rwlevklkdl llhdtpfalm vididhfksi ndelshlvgd
      421 kaivnvskel sgyfkfrgss cvrfggeefl vilentevak aemhaenyre riyqfgwhei
      481 lgergltvsi gitlhregen tqrtfyradk alyrakangr nqvcteq
//
LOCUS       WP_010645180             542 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Vibrio campbellii].
ACCESSION   WP_010645180
VERSION     WP_010645180.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..542
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58881
     Region          22..542
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mqlslknlsv rtqvlvpvlf taitlfitlw itqnnleaeq elvasnsdsl vfykdtlaqi
       61 ddqvyplris avyaiydaar rdafltelka gakaidtdld lidargtfsk eaekvrqsid
      121 ayidystrav effnrhdrgl vsdneytnfi sgyrrvgnem vaiinalsqr vneiateata
      181 esarqhtrvq nnammsviav fafsllgawf lsgmivtpiq klqevmrkla ggdlsvradi
      241 dgdneisqls kdvnqtakql hdtvdqlmri seevassste laavmtqaea naqqelaeie
      301 qvasavnela stannvsdna tsadatarea dglaqsglai fresaqaseq msqalndaaq
      361 vvlrlkeqsv qindvievir gvseqtnlla lnaaieaara gesgrgfavv adevrmlaar
      421 tqdstqeiss iieelqaqsg landsmqvsl emlnrnnelt qqandaligi tesvaninds
      481 ntqvataaee qsqvtqdinr nvvnmselvn qnvagisqsa sastelshla ekqkeqlsff
      541 kl
//
LOCUS       WP_010645266             257 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Streptomyces].
ACCESSION   WP_010645266
VERSION     WP_010645266.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..257
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26924
     Region          61..257
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtatatparp tafsaartla taarvlrqlr hdprtialll lvpcvmitll ryvfdgspgt
       61 fdaigasllg ifplitmflv tsiatlrert sgtlerllal plgkadliag yalafgalav
      121 vqsalatals vwllgldvtg spwllllvav ldallgtalg lfvsafaase fqavqfmpav
      181 ifpqlllcgl ftprpdmhpv leavsnvlpm syavdamnev ltrpgvtgtf vrdlaivags
      241 avlvlvlgaa tlrrrtt
//
LOCUS       WP_010645318             126 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Vibrio campbellii].
ACCESSION   WP_010645318
VERSION     WP_010645318.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10547098
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..126
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=14145
     Region          6..124
                     /region_name="bPH_1"
                     /note="Bacterial PH domain; pfam08000"
                     /db_xref="CDD:462337"
ORIGIN      
        1 midfenssif klkpietskv redfhkflid gesifagfkt vrdqvvftnk rviaanvqgi
       61 tgskvdytsl lpyskinvfs ietsgtldld ceielflsev grvrfeirgs fdlvsfnkmi
      121 sehvla
//
LOCUS       WP_010645400             362 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Vibrio campbellii].
ACCESSION   WP_010645400
VERSION     WP_010645400.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..362
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41357
     Region          216..362
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(247,290)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(252,255..256,260,264,286,288..291)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(282,310)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mkvqpnvpkq gpssrsktll lifastllva nivllqetra ltktysdqqn qatwflfhls
       61 kelselvgea rrlnesinnf dsaelqyela wsrfdllihn kevdsflsre evrvyfislf
      121 drfkqlepil veaktgnsva asqfyratqn lymemidyvt qhfrvasply kqqqkqaydl
      181 lqaqyvllgi fvitvallty fykqeskfhk elalsdsltg lanrsalfid lqnnqesgtt
      241 fslllldlng fknindtqgh qagdialtev aerlkhmald nfkvyrmggd efavvinstv
      301 kqdieeakrh ihvvfekpif vsdqasslst slgaacypqd tdnidflinl adkrmykmkf
      361 qr
//
LOCUS       WP_010645502             134 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Vibrio campbellii].
ACCESSION   WP_010645502
VERSION     WP_010645502.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..134
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15746
     Region          5..131
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mtiqlhhvsi tcrnleqccr fyekigfdky rsyqdddvti llmrgnhtyi elfnfpkedq
       61 kditindsqt lpelkktgit hfalqvsdlk ktreklspny qcseiqkarl glfsyffald
      121 pecnqvefiq rnni
//
LOCUS       WP_010645629             301 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Vibrio campbellii].
ACCESSION   WP_010645629
VERSION     WP_010645629.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33821
     Region          7..>49
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,110,149,163,165,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,192,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mlnkvnladi rsfvliaqlg nftkaaeals vsrshvsrqi sgleaqmgvt lltrttrtlr
       61 lthagerfyq ecekalrdid qaliaavddt qevrglirvn cvggyigedi iakyvnefml
      121 eypnitvdld fsspridlie dqfdvairmg eledagfvar klmmidmvtl aspnylkthg
      181 epitpkelak hrtltgsvtr wsyrnvanpk ehsdvivkgn lrckngralv mgalhgngii
      241 rvplsycdee vkqgqlvkvm peweipsvpl saifhrdryq pkrlrtfidf vkakfgqefa
      301 e
//
LOCUS       WP_010645750             183 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma carbonic anhydrase family protein [Vibrio campbellii].
ACCESSION   WP_010645750
VERSION     WP_010645750.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..183
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19883
     Region          4..177
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mssirsykgi rpqlgkrvyv dstsvlvgdi rigddssiwp lvaargdvnh ihigdrtnvq
       61 dgsvlhvthk nadnpfgypl iigndvtigh kvmlhgceih drvlvgmgai vldnvvvesd
      121 vmigagslvp pgkrlesgyl yvgspvkqar plseqeqafl qksannyvqn kndyineved
      181 ink
//
LOCUS       WP_010645765             268 aa            linear   BCT 01-JAN-2025
DEFINITION  sporulation protein [Vibrio campbellii].
ACCESSION   WP_010645765
VERSION     WP_010645765.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..268
                     /product="sporulation protein"
                     /calculated_mol_wt=29897
     Region          11..218
                     /region_name="Spo0M"
                     /note="SpoOM protein; pfam07070"
                     /db_xref="CDD:429274"
ORIGIN      
        1 msflkktlas fgigsskvds ilnqdvlypg qsvdvsihvy ggateqaidn idlklccryi
       61 aeapddrgar eghimrrvpq thvlakwnlp yaftihpged rtfevkldvp wntpvtigda
      121 kvwletgldv amaldptdkd iltvrpdplm davlsafesq glrirqvece evkgfdlpfv
      181 qefemvptdg pyhgvwrele fvahrdeqnl klwfevdrtr tgasgmlasl lgsgklkrel
      241 sipvntklde vgslilnyle rttaahef
//
LOCUS       WP_010645827             296 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Vibrio campbellii].
ACCESSION   WP_010645827
VERSION     WP_010645827.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..296
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33969
     Region          1..202
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkvsvviptf nssstlgral qsiveqdysp levilvddcs sddeinrmke iirsfqprly
       61 vqfvlntkks nasatrnqga rlatgewvaf ldsddlmlpn kiseqvqfme vnnadvsfhq
      121 iyrselgsey vednvfpkld fdaetrvsdy lladggviqt ssimlkrcvl ekvqfneslr
      181 rhqdfsfvld lehagiplfy lkrplshwvl eqesnclrkk gqnldfslfw lelyknkltp
      241 karfaylsgt clsfakqerr lgfylqyllk hfglisplqv vqcalknkln rdsnll
//
LOCUS       WP_010645915             363 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Vibrio campbellii].
ACCESSION   WP_010645915
VERSION     WP_010645915.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..363
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40111
     Region          3..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,232,299,319,321..323)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,101,108,180,183,185,232,239,299,319,
                     321..322)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,101,180,183,185,322)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            185
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msklfepaql kqltlqnrvv mapmtrarts qpgnipnqmm atyykqrata gliiseatqi
       61 sedsqgysft pgvytdeqva gwktvtqaak eqgaaifcql whvgrvshpr fqkgeqpiap
      121 salkpvetqv wiadeqgngn mvdcvepram tqadidrvvr dfahaakram eagfdgveih
      181 ggngylidqf lrtnsnhrtd syggtrenrl rfllevveav seatgankvg vrlapfitfk
      241 dmncpdivpt ildaskqlqa rdiaylhlse adwddapvip esfrielrey ftntiivags
      301 ytqeradevl ekgyadlvaf grpfvsnpdl varlqhqqpl aeldgstlfg gnehgytdyp
      361 alg
//
LOCUS       WP_010646083             177 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Vibrio campbellii].
ACCESSION   WP_010646083
VERSION     WP_010646083.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..177
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=20341
     Region          2..175
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mnhplereyh daewgvpvyd dnvlfefitl egaqaglswi tilkkregyr eafehydldk
       61 liqrdeerte fivenydvvk hrgkinsvfs nakaamqlie eygslsnalw qfvdgkpivn
      121 hwtdmsqvpv steqskamsk flkkkgfkfv geticyvlmq avgmvddhmv scpkksn
//
LOCUS       WP_010646102             580 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 36 protein [Vibrio campbellii].
ACCESSION   WP_010646102
VERSION     WP_010646102.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 580)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..580
                     /product="glycoside hydrolase family 36 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65757
     Region          196..476
                     /region_name="GH36"
                     /note="glycosyl hydrolase family 36 (GH36); cd14791"
                     /db_xref="CDD:269892"
     Site            order(202,235,272,347,351,390,405,408)
                     /site_type="active"
                     /db_xref="CDD:269892"
ORIGIN      
        1 maqsiqlanh teisvsdndl qfevvgnqih fsfagihnkt ftdrevlfqm pflyeqgatv
       61 lgdgfqmlaq tsgtisqpid igrcpdnnns yriypesapk ryynylaved aagytlfgft
      121 schrfagyfe vqthgehwvl sasidgehtq vadwehntle svailrgqsl selyqqysem
      181 laehhpvrng vtqdapigwc swyayyadvt egnvlenvec mqdnlaelew vllddgyqaf
      241 mgdwltpsdk fsggvkelih nirakgkrpa iwmapfiaqp eseifkkhpd wfvrhedgdl
      301 lkaedvtygg wrctpwyild tsnpevqdhl thvvsvmree wgvelfklda nywgtlkgkr
      361 sqsgvtgvea yrmgmeaiak gaedawllgc napmwpslgl vdamrvsddv erhshrfeqi
      421 aketffrswq hrklwqidpd catftslpnq aasredyqfh rnvllacggl llsgdplpei
      481 tpfasktlak lmlrqrrnqe sakftalgln haflpltskn dlhclfnytn deateftlta
      541 dqptdwydyw tgeklnqepc qlllvsldkg lkakavvtai
//
LOCUS       WP_010646181             318 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Vibrio campbellii].
ACCESSION   WP_010646181
VERSION     WP_010646181.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..318
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33507
     Region          8..315
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mdavlhqlqf slsitgpicl mlvlgvlfkr iglindnfie vgsklvfqvt lpamlflsiv
       61 vsehdfsaas gfvnygivas isffiftyis vklffksspd qgvliqggfr antgiigiay
      121 vanaygsqgv alaalyvavt tfiynvqavi clspkgatsg sqaaklmmrt ltrnpliisi
      181 vsgmvfylls ipvpdvaida gnylskmtlp lallctggsl dlslmkkekg pswfassykl
      241 ivapiaittg ayfvgfrgie lgilffmnas pvaaasyvma rsmggnsvla aniialttvl
      301 stvtctvgiv ilkaygli
//
LOCUS       WP_010646234             308 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Vibrio campbellii].
ACCESSION   WP_010646234
VERSION     WP_010646234.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..308
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35395
     Region          74..304
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mnktrissia qyfsreiade qynptlwtnr lptddllpkh ieftsqqser yrtnletglt
       61 emaygegefs gkidiykpkg iakdapiviy ihggwwqwfs keqfgfiakp fnqngftvym
      121 psyrmaqdwt ngapmesilk qmqlavkeil slavennspa vylvghsagg qlvsmlhktd
      181 weqfgveaeg keklkdvfsi aglfdirplv nsfvndnirm tnesserisp llndfpseee
      241 laplhlivpe ldtpeffrqt keyhakvlda kqecriylar krdhldvien lindnddvln
      301 ymlenmkn
//
LOCUS       WP_010646272             690 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Vibrio campbellii].
ACCESSION   WP_010646272
VERSION     WP_010646272.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..690
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76897
     Region          5..690
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mftksqlalv igavlaapav aevqttdehl vvegrefgyk adtnstamrm emtqletpgq
       61 vavideavid eqrastlgev lqndasvsag gtsrnrerfs lrgfelsssd gflrdgrqhw
      121 shyrqpiell ervevlkgps gllygksepg glvnmvskkp ttetqaslsq digsndhsrt
      181 vldvsgalne eetlrarail akesygswre ygdgtepqtd rvvgglvvey ditedimvsa
      241 hydrtkddgs vdsgayivdg kpvrgdkyiw daqwsnidnd venygidina qvtdrvnvka
      301 gynrqdfkrf dvesypsfsk yaqenkiihs gnertdnwvf dtayldvttd fsllgsentf
      361 liganyldyk ydrfqkyyst veiepgqtvp rpdysgkvke stseydtwgi yaqnmmtind
      421 hwqvlagvry dekrsdtlte sqvspklgvi fhpasngsvy vqysesfmpq gevssgrkly
      481 sndgeeldae rgisyevgtk welfdkrllv sgavfditle nlaldvkdgv naggdvmykk
      541 tqdgeqvhrg aeilaqgfvt eelsltasam yldaeitesa dykgnrpadv pefsasvwss
      601 ykvqnntnvn lgliyegery gdagntfkkd gyaridmgvs ythkydenld ivtrfnvenl
      661 fdtdylagge rdgvvigegr nymatiqfky
//
LOCUS       WP_010646279             206 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Vibrio campbellii].
ACCESSION   WP_010646279
VERSION     WP_010646279.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..206
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22898
     Region          127..204
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mgrlllalpa siliavslfs fmawmvdkgn qrapkpseav rfdmvmvend advqrrqrsv
       61 peqpeppkap epmdlsqaet qvepmsqvtp tsalglntal dgiaisapnl kgtmgnqqal
      121 plyrvdpryp skalkrkmeg yvvmrftida tgrpkdievi dakpkrmfek eairalkkwk
      181 yqpkvedgvs ieqfgqtakv efklak
//
LOCUS       WP_010646505             245 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome c1 [Vibrio campbellii].
ACCESSION   WP_010646505
VERSION     WP_010646505.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..245
                     /product="cytochrome c1"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27029
     Region          11..245
                     /region_name="CYT1"
                     /note="Cytochrome c1 [Energy production and conversion];
                     COG2857"
                     /db_xref="CDD:442105"
ORIGIN      
        1 mkkwivilfa mlpslamaag anvpldkanv nlsdkaslqn gaklfmnycf gchstqyqry
       61 ervatdldip adlmkanlif dpeakigdlm vnampakqag dwfgapppdl tlvarvrgad
      121 wlytylrsfy vdpsrpfgvn nivfpsvgmp hvleelqgip tpvygmkvvd geevqvvvgt
      181 etngtgelss geydkavgdl vnflvysgdp vqlerhalgw wvmgflvllt ivvvmlkkey
      241 wrdvh
//
LOCUS       WP_010646565             130 aa            linear   BCT 01-JAN-2025
DEFINITION  GFA family protein [bacterium endosymbiont of Bathymodiolus sp. 5
            South].
ACCESSION   WP_010646565
VERSION     WP_010646565.1
KEYWORDS    RefSeq.
SOURCE      bacterium endosymbiont of Bathymodiolus sp. 5 South
  ORGANISM  bacterium endosymbiont of Bathymodiolus sp. 5 South
            Bacteria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="bacterium endosymbiont of Bathymodiolus sp. 5
                     South"
                     /db_xref="taxon:1181670"
     Protein         1..130
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14813
     Region          1..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mhqgeclcgk vkfqitqkit divmchcsec rrvqgtafat ngnvesknfk flrgennlte
       61 fkendnksrf fcqscgapim aklknnpdyt rvrlgtmttd vneaiekhif tqskacwdti
      121 cddipqhkew
//
LOCUS       WP_010646574             239 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Vibrio campbellii].
ACCESSION   WP_010646574
VERSION     WP_010646574.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..239
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26925
     Region          4..235
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mkseriqtkg fkfkqfsihg gesgmpvstd gvmlgawanc tqqnkildig tgtgllalmc
       61 aqrfpsaqit aldieitaie aakqnfaqsp wsdrlslhhs dvlqfepehr feriicnppy
      121 fnsgeqskqs qratarhtdt lqhsallnrc hellteegta nfvlpitege qfitialqqg
      181 whlsrlcrvq psqkkpvhrl lfelakqacd tqethliihs segysddfiq ltrefylkm
//
LOCUS       WP_010646662             253 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Vibrio
            campbellii].
ACCESSION   WP_010646662
VERSION     WP_010646662.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27319
     Region          1..250
                     /region_name="trans_reg_YgbI"
                     /note="DNA-binding transcriptional repressor YgbI;
                     NF040890"
                     /db_xref="CDD:468826"
ORIGIN      
        1 mipaerqrti lsllshqevl sisdltdhlg vshmtirrdi vklessgkvv svsggvqlaq
       61 alhselshda kveqqadekv qigklaatli gkdatiylda gttsleiahq iadrddllvi
      121 tndfsiagfl mthsqcelyh tggkidrenq stvggkvaef lnelnidiaf istsswslkg
      181 lstpnenkvl vkkaiikaaq tnylvsdstk ygqiasfhal nieqlngiit dsnlsdvvtq
      241 elmdkglsvi rgn
//
LOCUS       WP_010646819             229 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Vibrio campbellii].
ACCESSION   WP_010646819
VERSION     WP_010646819.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..229
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25887
     Region          33..168
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 meniklskhd iqtmeqrqrt rlvnslagyk sanligtrdr qgqenlaivs svihlgshpp
       61 lfgfivrprk srrhtlenif dtkhftinai gvdfvqkahq tsarypkqis efeavgltpy
      121 yddafpapfv lesnlkmglv lrerikiesn htemligevl avhaperaim pdgyldlell
      181 dlvtisglds yhvtqrlhrl syakpdsrlf pltregepss wgalevdmd
//
LOCUS       WP_010646862             316 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Vibrio campbellii].
ACCESSION   WP_010646862
VERSION     WP_010646862.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35384
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkiraltvf rrvvelgsfv aaaedlnlsk aaiskninel esylksplin rttrnlhitd
       61 ngqlyyqqvc qvldalnnad rsviesshtl kgtlkismpm slglielnpi icefmklhpe
      121 lsievvmsde hidlieqgvd iairgggelg nsslrsrkll dirrvlcasp qylkesqpfq
      181 sprdvikhrl lsyslsstsr rwtfqngsev levdlpasvy tvnsglaltq aacaghgval
      241 lpdffvepql asgelveitp ewqmekhaly ivypyhkeqs qklrafidyv vesfqarfsr
      301 qsdpqqmyss iiklgs
//
LOCUS       WP_010646875             203 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Vibrio campbellii].
ACCESSION   WP_010646875
VERSION     WP_010646875.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..203
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22375
     Region          3..203
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 melfsfallg ilivispgad fvlvlrnsln ngrragiwsa vgislaismh itysllgisy
       61 lisqnewlfs lirylgaayl iylglkgvfg adsqqkiege tqesisiwqf ffqgflcnvl
      121 npktmlffls ifsqvidpnt esqhlalgyg vymialhgiw fsmvailfts prlqslllrv
      181 khrlnqacga gllvfgamlg lks
//
LOCUS       WP_010646948             134 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [bacterium endosymbiont of Bathymodiolus sp. 5
            South].
ACCESSION   WP_010646948
VERSION     WP_010646948.1
KEYWORDS    RefSeq.
SOURCE      bacterium endosymbiont of Bathymodiolus sp. 5 South
  ORGANISM  bacterium endosymbiont of Bathymodiolus sp. 5 South
            Bacteria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="bacterium endosymbiont of Bathymodiolus sp. 5
                     South"
                     /db_xref="taxon:1181670"
     Protein         1..134
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15444
     Region          6..133
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mksnvsllrr lgaiaydgfl afslaffiig vilivffdkq aqtnififfv vlltyyfyft
       61 wswvkggqtl gmkawkfhiq qnngkrithq qafirfilsi vsfttlglgf vyqlfnsdnl
      121 alndrfsntr ltkn
//
LOCUS       WP_010646964             165 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Vibrio campbellii].
ACCESSION   WP_010646964
VERSION     WP_010646964.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..165
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19224
     Region          1..165
                     /region_name="COG5628"
                     /note="Predicted acetyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:444356"
ORIGIN      
        1 mevqlvkier eerhilenlf cyyvydmsey mkwnpakdgt fggydvskfd pywnrddhtp
       61 yfikvnnela gfvlirryps dltfydvaqf fvlrkfkgqg vgklvleqvv kafpgkwqir
      121 illensgals fwksavsniv gedytlskan dvdlimffih fesas
//
LOCUS       WP_010647090             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Vibrio].
ACCESSION   WP_010647090
VERSION     WP_010647090.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..155
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17219
     Region          32..153
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 msqhtavikw qrqtdeifsd nqysrahvwq fdgglcvpas psphvvplpl svaenvdpee
       61 afiaalssch mlvflsiaak rryvidsyvd eavgeltage ngkewvskvt lrpnivfsgd
      121 kqptreqlek mhhmahencf iansvktdvv telld
//
LOCUS       WP_010647162             275 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio campbellii].
ACCESSION   WP_010647162
VERSION     WP_010647162.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13673967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..275
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31222
     Region          17..149
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          <176..271
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mkeknkevat fkiaqelggl elleakyekq nfsrhshegy tigviekgaq qffrtggnhi
       61 apqdsiilvn adevhnghsa seggweykam ypvpeqfqtl geelgasnva lpyfpqpvvy
      121 dpelanqlrl vfdtleksdn rllretlvyg tliklaskhs thraplqdvt kaqrqvhlvr
      181 efledfpqtd vsleelakla glspfhllre fqkqfgfpph afqiqqrlrm akkllklgqk
      241 isdvaqecgf hdqshlhrhf kkamgvtpgq yikhf
//
LOCUS       WP_010647178             715 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Vibrio campbellii].
ACCESSION   WP_010647178
VERSION     WP_010647178.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..715
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79504
     Region          12..715
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtthvrfkys slavalltaf stqvlaeeav tatdsnieti tvlgkayrnt atksalepee
       61 tpqgitvide eqleqrgvks lnqalryapg vvteqkgasv tmydtfsirg fsnnqsyydg
      121 lvlpfltgwn lqpqidpiai qqvevfkgpt svlygamppg gmvnmiaktp qedgstkvgv
      181 stgsrnlmea sidttgqlgd snfsyrllal arkqdsqvdh aeeeryviap sldwqlsdrt
      241 linfnlyyqn dpsmgtnsam plevlkasdp svsmgdknws tferevlmlg ykinhqindd
      301 wtflqnaryt daslyqenty htatnfnpvt gslirnvyst dedsqsfvid nqvsgrveig
      361 glehnllfgv dylkltgdsl ykeftanasf ygfdaynpnn dlldrsqlqe nyreshditt
      421 eqlglyfqdq vrydalvlla ggrydvfkas ddknssypty dgkdeadhnq fsyrvgalye
      481 ldngispfvs yatsfepaag tdingnslkp qlgeqielgi kylspdmsqq vtasyfhitk
      541 kdsiaadpsd ptyrskiqlg evrsqgmele grwfvtedwd vnasytyidm evtedanpdl
      601 egttpiyvpt haanlwsnyy vyggalsgtr fsvgarymge memdatntqg kvpsytvvdl
      661 svgydlgeas dtlsgatanl lvnnlfneey ytcydqsncw fgaeqsvels vnyef
//
LOCUS       WP_010647181             261 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Vibrio campbellii].
ACCESSION   WP_010647181
VERSION     WP_010647181.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..261
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28435
     Region          1..246
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mfqlsniriv rdertilsid elsiptnelt vilghngsgk stlvnllsgq mapdhgmval
       61 ngaslssfks rklakkiayl pqklptsagl tveelvhlgr fpwrgtfglw nsedrsiiqq
      121 amertgvaef sqaladdlsg gerqrawvsm llaqqspvli ldeptsaldv hhqfqlmgll
      181 sdlnkkedvg vivilhdlnl alryathiva lkkghiafeg nadklldeqa lcalyessir
      241 lidhpvpadt aasekvavvc e
//
LOCUS       WP_010647212             308 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Vibrio campbellii].
ACCESSION   WP_010647212
VERSION     WP_010647212.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..308
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34519
     Region          6..226
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mteysiqaen vvkkfgdfta innitlnvpk gsiygflgpn gcgksttirv ltgllspseg
       61 nvdvlgleip kqsellrlki gymtqkfsly ddltvqenle figqifgmet kalkvrieeq
      121 latygldqlr kqrvggmsgg qkqrlslaaa tihkpellfl deptsavdpe nrrdfweqlf
      181 dlsdqgttil vtthymdeae rchrlaimea geiradgepe elmaqmgvni veikadnlre
      241 lkekviqrke vrsaaqlgir lrilihqhie qpiewltqtf pelegcemni arpsledvfv
      301 svtgegrq
//
LOCUS       WP_010647196             255 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Vibrio campbellii].
ACCESSION   WP_010647196
VERSION     WP_010647196.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28150
     Region          1..251
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 myqltnasfe idgktilspi nlsfepkkvt tllghngcgk stlikllsrq ntpskghiff
       61 dekpissysh lefahqvayl pqhppitdgv tvrelvcfgr ypwkgafgry skqdyaivde
      121 aiekvglskf aqrfvatlsg gerqrtwvam llaqqsqcil ldeptsaldv ahqhellali
      181 relnhslglt vimvlhdvnm aakfsdhlia lhsgeviasg ppqeimtpdt lskiygmela
      241 lfnhpttgqp isyip
//
LOCUS       WP_010647247             535 aa            linear   BCT 01-JAN-2025
DEFINITION  BCCT family transporter [Vibrio campbellii].
ACCESSION   WP_010647247
VERSION     WP_010647247.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..535
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57635
     Region          19..533
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mdnalkkysi dttdyqvgqd nvqkwgfdih npvfgisagl vllclaslli vdpttardal
       61 nglknsiisd fdsffmwsan ffilfaiail lsplgkirig gkdavaehst vswlsmlfaa
      121 gmgigllfws vseptayftn wfgtplnvep yteeakslam aatmfhwgih gwaiyaival
      181 slaffafnkg lplslrsafy pifgdrawgw lghvidilav latlfglats lglgaqqats
      241 ginhvfgleg gigtqmivia fvtfiavlsv irgidggvkl lsninmavaf allafvmfis
      301 fdiattsiwd tavayaqnil plsnpagred tewmhgwtvf ywawwvswsp fvgmfiarvs
      361 kgrtvrefif avivipttvt lvwmavfggi aldqvvnkvg elgangltdi sltlfhvyda
      421 mpfssiisvl sivlilvffi tssdsgslvi dsitaggkid apvpqrifwa ciegsiaavm
      481 lwiggkealq alqsgvvatg lpftlvllvm cvslikglrs elpayqnaaq nasva
//
LOCUS       WP_010647328             328 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Oceanobacillus massiliensis].
ACCESSION   WP_010647328
VERSION     WP_010647328.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..328
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36344
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msekiyditi igagptglft afyggmrqas vkiieslpht ggqltalype kyiydvagfp
       61 kvraqelvdr leeqasmfdp eivlgqavdk lerlednsfk mtsstgevhy tktiiitagn
      121 gafqprrlnl gesesfegkn lhyyvkdmdq ykdknvvllg ggdsavdwal mlekvaksvk
      181 lvhrrdqfra hehsveqlma ssvevltpft psdiiisdki dkiildevkg erklelevdd
      241 iicnygfiss lgpikewgid ieknsilvnt kmetnipgiy aagdictyeg kvklivtgfg
      301 egptainnak nyidpkariq pkhstamf
//
LOCUS       WP_010647379             343 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010647379
VERSION     WP_010647379.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..343
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37900
     Region          1..339
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 misieglski falnkkkita vddltlhiee geiygvigys gagkstfvrl lnrleepsfg
       61 kvtidnqeit glstkqlrla rqdigmifqh fnllwsrtva dniafpleia gipkaeraer
      121 vqqlidlvgl sgrekaypsq lsggqkqrvg iaralannpk vllcdeatsa ldpettnsil
      181 nllmdinqkf gltiilithe mhvirkicnk vavmeqgkiv eqgqvldvft hpkqqvtkkf
      241 veqimgaseq dddiselist ysdgkllrlh figettnqal isqvakkfnv einilqgkit
      301 qtkaggygtl fiqvkgedee ietavrfvqe etsvevevip nvd
//
LOCUS       WP_010647458             399 aa            linear   BCT 01-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010647458
VERSION     WP_010647458.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..399
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44605
     Region          1..337
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrkiilfitt ivavnslfgs kafgephpsp psleseaail lernsgqvlf dknansqmyp
       61 asvtkiatai yaietgnldd ivtissnara knvegttvyl eegekvtlke liqgllinsg
      121 ndagvaiaeh lngseeqfsk dintylknvi gvqdtnfenp hglfnsehrt taedlaritr
      181 yamknetfre ifgtkelewn gqtwdttils hhklvkeeip ykgvtggkng yvnqsgytla
      241 ttaerdglsl ivitlkgsmk nvpyddtikl ldygfenyrt siiskgtkfk vedqeytase
      301 tiaythpkne qlskdikedg tmeiiaqdge vaasyqleev snktinvktk lentttnkvr
      361 ydtifdeldp ylayfsiafl lsmigifyrq niyylrkik
//
LOCUS       WP_010647488             523 aa            linear   BCT 01-JAN-2025
DEFINITION  arylsulfatase [Vibrio campbellii].
ACCESSION   WP_010647488
VERSION     WP_010647488.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..523
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58404
     Region          24..466
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16142"
                     /db_xref="CDD:293761"
     Site            order(32..33,73,126,128,258,315..316)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293761"
     Site            order(32..33,73,126,128,258,316)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293761"
ORIGIN      
        1 mrlkplvasl gtvlpnlvsa adkpnivvif gddigwqnvs aygmgtmgyk tpnidriane
       61 gikftdhyaq psstagraaf itgqypirsg mttvampggs lgmkagspsl aevlkrvgya
      121 tgqfgknhlg dhnfalptvh gfdeffgnly hlntqeeheq rdyqnfakay sgsvenyakk
      181 fgtrgvlhcf adekddktvd prfgvvgkqk ctdtgplgqe rmkdfdkaem ipaalkfidk
      241 siedgkpfft wintsrmhly trlndkwrya aeqytsefdy hgsgmlqhdh digylldeld
      301 krgitentiv lyttdngpeh sswpyggttp frgekmttye ggvrvplmvr wpstipsgqv
      361 lngiqghqdl fttlasaagv kgvkeqmike kkqyidgidn lpywtgkses sarqsifyyf
      421 edqlsairig pwkfhfaiae nyydnllpls kpkiynlrad pfesfdsida nghliqkmsw
      481 llapasemvs ehvkslveyp ptqggttfdm tkiiedamkk tqq
//
LOCUS       WP_010647485             304 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Oceanobacillus massiliensis].
ACCESSION   WP_010647485
VERSION     WP_010647485.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..304
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34520
     Region          26..287
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mdntfwltts ddveifvkkw ysitkkpkai iqlahgmaeh igrydtfany lteqgflvfg
       61 ndhrghgrtg erqgiqgyfa dengfhktae dlyevtkhir qddsetpiyi ighsmgsflv
      121 rnyiqahsdi isgavlsgtg fypkavslag kgiasmlppk qasklmnhla fssnnhkike
      181 rkngfewltr desiletymn dpftgfiptg rffydlltgi ltmqskkqnk yirkdlplll
      241 isgdadpign yakgvwktan lykksglqnv svmlytdgrh ellneinree vfesiikwin
      301 hqll
//
LOCUS       WP_010647497             262 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Vibrio campbellii].
ACCESSION   WP_010647497
VERSION     WP_010647497.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..262
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29200
     Region          25..>124
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mfnfgckknd kqegcrvasg ltkkqqaiad revelvqlak slvreqgfan ltmdkltaas
       61 syskgtiynh fcskedvila lcihslksea mffertanfd gntrekiiam hvgyriyarm
      121 epvlstcaiv aktpwvieka sparlnelnk leeevisgad alvnhaveig dlkfspavgs
      181 daivfanwsi afgsnalaqn asnsrciqrl qdpfsvlhna nmlldglgwl plstewdyrk
      241 twrrveqelf seelayldsv nr
//
LOCUS       WP_010647541             554 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Oceanobacillus
            massiliensis].
ACCESSION   WP_010647541
VERSION     WP_010647541.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..554
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61575
     Region          37..549
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 mtefssykra difnqlenns ldvlvigggi tgagisldav rrgmktglie mqdfaagtss
       61 rstklvhggl rylqqfevkm vaevgkerai vyengphvtt pewmllpfhk gstlgpltsn
      121 iglrvydfla gvkkserrim fkpeevlkre plikskdlrg ggyyveyktd darltievmk
      181 kaveqgvhav nyakavefiy dntnkaigvv vedqisgesh kiyadkiina ggpwvdevre
      241 ldgskngksl hltkgvhlvf sndafplqqa iyfdtpdgrm ifaiprdgkt yvgttdttye
      301 gdiahpvmke adrdyllkai dymfpslnis addiesswag lrpliaeena sspseisrkd
      361 eifisdsgli smaggkltgy rkmaeqavdt ivkqlkeekg ilytksntkh lpisggdvgg
      421 segfekfkkq kiekgiglgl ketdaaqlvs kygsnvddly eifqnkkeea ntenidpvvf
      481 aqlnyaieye laykpvdffv rrtgalffni hwvekhqenv inylaktfgw kaaqkesyaa
      541 elkqllheav tpgk
//
LOCUS       WP_010647656             187 aa            linear   BCT 01-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Vibrio campbellii].
ACCESSION   WP_010647656
VERSION     WP_010647656.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..187
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=20184
     Region          12..187
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mensnqsqqp tflskgwkyf vivgviialm gigamslpvl agvtistivg avllfsglvq
       61 ayhtfsinvw kdklwyvlsa vlyivgglfi lfkplaglvt itmlmvivmi lngltriffg
      121 lsnrslpssn vivfsgvisv liggyffmll ddpafsttll gtfvgislli egisfifmgl
      181 qmkklsq
//
LOCUS       WP_010647736             344 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010647736
VERSION     WP_010647736.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..344
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37829
     Region          1..343
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msklrmgfig vggiaqsrhi paylsmpekv eivavqdlnq araeeaaakf nipqvygdyh
       61 dlfkvvdavt ictpnkfhae isiaaleagv hvfcekpmai tvaecermle asdkagklls
      121 iayhyrfmea srvaklamed igdplvtrvq alrrrkvpgw gvftnkdlqg ggslidwgch
      181 fldlslwlld gpkpvevmgs tynrlsktpd qlndwgafnh etfdvddhvs ayirfedgss
      241 mifecswaan ikedtthvsi sgvdggvnvf pleihqpkyg tfmtnavtie edsaqvgllq
      301 aqnfvesclg eaelickpqe tlkvtqiiea iysssetass ikfs
//
LOCUS       WP_010647738             343 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010647738
VERSION     WP_010647738.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..343
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37537
     Region          1..342
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msklkvavig cgsiarhrhl veyannpeve iaavcdives raqeaaeiyd akaytsfeal
       61 ldsenidavs vclpnylhap vsiaalnagc hvlcekpmat skeeaedmir aakannkklm
      121 ighnqrfvss hqrarklieq geagriysfr ttfghggpeg wsadgedswf fkkdqafiga
      181 mgdlgvhkad llryildeef vevgafvets akentdvddn atlilktekg vigtlaaswa
      241 ytaeednsti iygekailrl eddpryslvv qykngevvny elggiqsnde ggqttthvid
      301 hfveailqda eplingeegk kslevilgal esvktnricr lek
//
LOCUS       WP_010647759             472 aa            linear   BCT 01-JAN-2025
DEFINITION  CpaF family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010647759
VERSION     WP_010647759.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..472
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52130
     Region          60..458
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 msllariqsk slenvqeqta dkstnvqpll peeeitvsve atsaenesay tpelsdddve
       61 lknlifryil kerndeevee ivadldsiit eilneneaik disdwknlke eikndltgyg
      121 pinplllden vtevmvngpk qvyaerngkl gltkiqfrdd ehvmavleki vaplgrride
      181 sspmvdarlm dgsrvnaiip plalngptit irkfskdpft ihdlirfgtl teemadfika
      241 sveaklnifv sggtgsgktt tlnvlssfis nqdrivtied aaelqlgqdh vvsletrppn
      301 iegkgaisir dlvrnslrmr pdrivigevr ggealdmlqa mntghdgsla tghsnsprdm
      361 varletmvlm agmelpvkai reqiagaldl iiqqsrlkdg trritnitev qglegdiivl
      421 qdiftfkqsg vdqngkivgr lvptgirpkf yermenegih lpaaiftekv es
//
LOCUS       WP_010647893             265 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Oceanobacillus massiliensis].
ACCESSION   WP_010647893
VERSION     WP_010647893.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..265
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30080
     Region          1..251
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mflkmdnvgk yfhneekqst fevfsgidis veenqfvsil gpsgcgkstl lsmvaglepa
       61 segemilegk eikqpgpdrg mvfqqpalfp wlnvrdnvtf plkgkmsrte ankqadhylk
      121 mvqlsrfken yiyelsggmq qrvaiarala mdpkillmde pfgaldeqtr yimhdelmki
      181 wqetkktilf vthsiqeaik lsdriivmgt rpgriiadit vdiarprkrg ileaieleer
      241 imgllegein kvlkeeltne veftr
//
LOCUS       WP_010647890            1613 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Vibrio campbellii].
ACCESSION   WP_010647890
VERSION     WP_010647890.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 1613)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1613
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..1613
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=183290
     Region          1..1605
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mtarenvvpv llekvyqliq dklelshqpl vtklaqhlfs niadddliqr nesdlygavv
       61 slwhrvnekk pedisvrvfn ptvsrqgwqs thtiveivvp dspflvdsik maltrldlvs
      121 hlmlnnptql erdkkgqvtd vngeggvlqs lfhievdrlt skdemqalkn elltilsdtr
      181 lvvddwkqmv eklkivtndl eknkdrvsmk tdrldetiey lrwlgdhnft fmgykeydlv
      241 nvngdtelqp vkekglgmfa ddsrvrsikl selsdsarle akkpyaliit kgnqasrihr
      301 paytdyigvk kfdkngkvig ehrftglyts avynqavqsi plirekvdri leasgyrngs
      361 ysykalhnil enyprdellq areeellevg mgvvqmqdrd llrlfvrkdp fgrffscmvy
      421 vtkdryntel rrqtqrilkq yfgceqevef ttffsespla rthyivrvdn nnidvdvkki
      481 eqnlmevsts wddrlkesii anfgeskglp lskeymsafp rsykedmmpg savadierle
      541 alsddnklgm lfyrpqeeaa eskavrlkly hrdepihlsd vmpmlenlgl rvigespyei
      601 etnngqtfwi ldfsmlhksd ktvdlreard rfqqafaaiw agnlesdgfn rlllgaslsg
      661 reisilraya rymrqvgfpf sqqyiedtls hypdlatglv nlfakrfdpk hkgsekgqnd
      721 likkiteeld rvesldddri irrymemita tlrtnyyqld edkqpkpwls lkmkpseipd
      781 ipqpvpafei fvyapdiegv hlrggkvarg glrwsdrqed frteilglvk aqqvkntviv
      841 pvgakggfvc krqhtltnrd difaegqrcy krfiralldv sdniiegevi ppksvvrhde
      901 ddpylvvaad kgtatfsdla nsvsdeynfw lgdafasggs ngydhkamgi takggwesvk
      961 rhfremdinc qttdftaigv gdmagdvfgn gmllskhirl qaafnhmhif idpnpdsats
     1021 weernrlfnl prsswedyna elisqgggif srrsksiqlt peiqkmlgtk kaslapndli
     1081 kmilqmevdl lwnggigtyv kassethtdv gdrandvlri dgrdlkakvv geggnlgmtq
     1141 lgrieyattg grvntdfvdn vggvdcsdne vnikiflngl vsngdltvkq rnqilesmed
     1201 evgeivldda yrqsesisvt eqqgvgivke qirfihtmek agyldraley ipddetlier
     1261 ekqglgltrp elsvlvaygk mvlkeqlvad eiandefhgk qlvayfpsel rcnykdqmvn
     1321 hplraeiiat alanqmvnem gcnfvtrlqe etgasvvdia naysatreif elegilkqtr
     1381 aldnvataea qyeimfyvrr alrrisrwll rnrsgkstva elvavykddv htitetldtm
     1441 lvaseveehn elaqkwierg veeklahhva rlsslqsald isavasetgk tveqasklyf
     1501 nlgdrlslhw flkqingqav dnnwqalara afredldwqq rqltaqvltc gcstedldvm
     1561 qaledwmttn elslhrwesi lnefkvgsvh efakfsvalr elvllnlncs sne
//
LOCUS       WP_010647920             467 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Vibrio campbellii].
ACCESSION   WP_010647920
VERSION     WP_010647920.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..467
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=50467
     Region          9..462
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkeipfrwid kylihlkiqe kfyllfflpl lalviltlvl nsaanslisd lyqeelmlmk
       61 glieagnlsq sqvaslitss dtitlgtgpd svsvmngafs lvasheqslw talsttqvsi
      121 ilvtlfiial gvyyimtfig gamftmnkal ntladgdlta rmnffrvrde fseiaitidk
      181 vadreqkmvq siqesvalmq qissdlnlsi qnsseisntq qehlnslasa teqmastire
      241 vatlahdsst qtddarsvaq sgqvkventl hsisnlstei qsasqaveel danaaqidev
      301 vttingiseq tnllalnaai eaarageqgr gfavvadevr alagrtqqat veiqamieal
      361 qrnsqsltkl mevtvhnane gqtlmaevnh eigsladknq tisdssiqia taaeeqgvva
      421 dniassveev riqannvcmm isttsqnveq lraqsdtmes lltglka
//
LOCUS       WP_010647927             376 aa            linear   BCT 01-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Oceanobacillus massiliensis].
ACCESSION   WP_010647927
VERSION     WP_010647927.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..376
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41135
     Region          1..376
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,85,161,165,184..185,187..189,208..210,214,
                     229,253..255,278,295..297,320..322,362)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,59,161)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(89..90,92,95,103)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mlavtnqgkn kvevkdveap kiqkdtdmiv kitttaicgs dlhlyrntip lskdyvighe
       61 pmgiveevgp gvkkvkkgdr vvipfnvscg echfcqnqme sqcdnsnphq dtgayfgyse
      121 mfgdypggqa eylrvpyadf ssfvvpesse lddenllfls dvvptaywsi ensgvkegdt
      181 vivlgsgpig lmtqkfawlk gakrviavdh nefrlahaak tnkvetynfk efddigkhlh
      241 eitkggaeav idcvgmdgdv tvkehlktlt gqigsidpii taahsvkkfg tiqltgvygs
      301 patayplqsi fsrnvtvktg qapvihympe lynmveegvf nptdiithre sltnaahaye
      361 vfnaqadnci kvilkp
//
LOCUS       WP_010647933             421 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Oceanobacillus massiliensis].
ACCESSION   WP_010647933
VERSION     WP_010647933.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..421
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44467
     Region          1..421
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtillfsimi llffinvpia ialamaasii fliqgdvslv vimqrmfnsv dsfpllaipf
       61 filagklmes ggisrrlihf anvifgrvng glaivsiaac affaaisgsa aattaavgsi
      121 lipamvkkgy dksfstavqa aggtigvmip psvplvlygv tagvsisdlf iagiipglmv
      181 tislmilvyi islkqgyggg eifsfkdllk afadailail mpviilggiy ggvftpteaa
      241 vvavvygliv gifiyreisi kdfpdifsss vvtsavimfi iagasvfgyy ltrervprel
      301 aefmlgitdn wiialliinl llliigtfie tsaaiiimtp ilapiaaalg idlihfgiim
      361 ivnlaigfit ppvgvnlfva snisntkieh viraiipfvl vmvislliis fmpvfslllv
      421 d
//
LOCUS       WP_010647962             155 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Oceanobacillus massiliensis].
ACCESSION   WP_010647962
VERSION     WP_010647962.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..155
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17184
     Region          1..140
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mheyflskti dlavesleng ggpfaaivvd kdsniigtgt ngvtknndpt ahaevlaird
       61 acskledfql kdcilytsce pcpmclgaiy warvkkvyya adqqiaamgg fddafiydei
      121 akehvnrkip fqsislenrs lpfekwlehe akisy
//
LOCUS       WP_010647970             169 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Vibrio campbellii].
ACCESSION   WP_010647970
VERSION     WP_010647970.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..169
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=18853
     Region          1..>67
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mtlafkrsss gftlielliv mtivglsvsm vgpslykqye karanqqiqk veltfkylae
       61 lafynyrpie vetngreika yfvgeltkgk aqedgeleea snkdeedvnv qsnllfsqef
      121 kevfiapqtl iisgngipsi paitvtqnet kheirlhhvv kktngndan
//
LOCUS       WP_010648011             481 aa            linear   BCT 01-JAN-2025
DEFINITION  dipeptidase [Oceanobacillus massiliensis].
ACCESSION   WP_010648011
VERSION     WP_010648011.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..481
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52893
     Region          44..374
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mpitifwfii slllntsnpv peieklvdtf kpaeqqeqnq dnihfastvv dghidtmmnv
       61 inqetwlpev nigedtslhi dieklqkggl dagffaaytt dyygntprni srtlallhal
      121 ywteennten fkiastsldv lntvregkta aipsieggys fdetnaigll hqyydlgvka
      181 vgfnwnysna lseganevyn dpaktpshgg ltelgeqvaa emnklgmiid vshmaesafw
      241 dvietteapi mathsgvksl hdhqrnlsde qlkalaengg vvgivfypef ltgtgqanvk
      301 dvvdhidyav nligvdhval gsdfdgsgmp adikdvtdlp kitnelidrg ysnediekil
      361 gkntlrllmd veqaaevnpy sgtgnelviq pdlemgekvd sktpslsaai naesgskidp
      421 dslriivdgi synaqydsek sissiqlkep lqekfhvvtf eaatekgein retrifyiet
      481 r
//
LOCUS       WP_010648039             259 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010648039
VERSION     WP_010648039.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..259
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27998
     Region          1..>195
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 miialyflig flasllgsma glgggiiikp lldffghydl ptigllsast vlamstmsli
       61 evkrmnhnfd rsiglliacg silggfigkg lfnhlvsdqs ltyfisifqs allaliliii
      121 flymryknal rayrltnkwi ilavgialgm lssflgiggg plnvavlyll fsmnaknavi
      181 sstfiiffsq lsalaliavt tgfsgydlsm igymigggil ggwigsrmvs klsnkrietv
      241 fnltilliii iniynlffy
//
LOCUS       WP_010648044             325 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010648044
VERSION     WP_010648044.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..325
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36299
     Region          1..246
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mniatigtgs ivelflsave evdgaqclav ysrkeetaer ladqfdisai ytdlaemlqn
       61 eaidciyias pnslhfeqay lalqhgkhvi vekpftstsr eaeqlielak ekqlmlfeai
      121 stihmpnykl irnhldslgp ikfiqcnysq fssryeklmn getpnvfnpk fsggaladin
      181 iynmhfvmnl fgvpervsym ankhangidt sgvavmkypn yiaecvgakd tqsmnfamiq
      241 gekgylkvvg gangcqevvi tngdreitmn aqlksnrlyy evaefqkifq mrdfqrcydl
      301 ldytksvvgv lesarkdggi sfdad
//
LOCUS       WP_010648060             287 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Oceanobacillus massiliensis].
ACCESSION   WP_010648060
VERSION     WP_010648060.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..287
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31753
     Region          13..286
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mntiplvvtt ewleerldds klrlidatty mqtengevkl wpgretflkg hipgavfadl
       61 mndfsdpead fgftapsreq fiekieqlgv gdedtftvvy dqtyanvgsd aiasdwasrl
      121 awqlryegld nvavldggfa kwseenrpvs tevtaypkav ftgkrrpelf vnkedvkaal
      181 dndnvillns lgeadfnsgr ipgscnvpfi shsnpetkgl ydeeklkeaf ekvgaldpnk
      241 kvitycgggi aatwnallln klgqknvavy dgsmvewtad kelplek
//
LOCUS       WP_010648098             327 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Oceanobacillus massiliensis].
ACCESSION   WP_010648098
VERSION     WP_010648098.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..327
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36901
     Region          11..297
                     /region_name="AKR_AKR11C1"
                     /note="AKR11C family of aldo-keto reductase (AKR);
                     cd19086"
                     /db_xref="CDD:381312"
     Site            order(19..21,51,56,81,121..122,152..153,172,200..206,265,
                     282..287,290,293..294)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381312"
     Site            order(51,56,81,121)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381312"
ORIGIN      
        1 mnynqlgktd lkiselsfgt waiggawgkt ndsealkgle ramdlgvnff dtadvygdgh
       61 aeellakatk gkeseihias kfcragdiyd pqnysmdkvr eycentlkrl greqldlyqi
      121 hcppleilqd gqvfdvleal kkegkiryyg vsvetveegm fclehskass lqvifnlfrq
      181 kplealfpaa mekgvgilar vplasglltg kfnkdttfde edhrhfnrdg qafnvgetfa
      241 glefekgvel srqlewiaeg renmtkaalk wiveqkavts vipgfrnvkq vednlgalhv
      301 rdfstdekkr lerfyednvk ehirgay
//
LOCUS       WP_010648141             407 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Vibrio campbellii].
ACCESSION   WP_010648141
VERSION     WP_010648141.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..407
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=45050
     Region          2..405
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mptfryqgrt ldgsstsgkv davnseaaae almnkgiipl nlrlekeavk skvslskllv
       61 paipleviil fsrqlfsltk agvpllrsmr gllqncenkq lkealedvvs elsngrglsy
      121 amqphtkvfs plfvsminvg entgrldqal lqlanyyeqe letrkrikaa mryptfvivf
      181 itiamfilnt lvipefasmf trfgvdlplp triliatsnf fvnfwgllia aivgafllfr
      241 awvatadgre kfdkfrlrlp ivgdivnraq lsrfartfsl mlksgvplnq slalagealg
      301 nkflenrife mksaieagst isvtainski ftplviqmia vgeetgride lllevsdfyd
      361 revdydlktl tarieplllv ivagmvmvla lgiflpmwgm mdiikgg
//
LOCUS       WP_010648143             574 aa            linear   BCT 01-JAN-2025
DEFINITION  GspE/PulE family protein [Vibrio campbellii].
ACCESSION   WP_010648143
VERSION     WP_010648143.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..574
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=63736
     Region          1..558
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mkiqlrkrlg dllveegivs edqvqqalsa qhstgqklgd alidlgfise kqmleflsqq
       61 lglplidlsr apvdadavqi lpevharrlr amvvarngdt lrvamsdpad lftqeslmnl
      121 lgeydlefii aperqlvesf dryyrrtkei asfaeqlqae hqdvegfdyg idegdseevt
      181 vvklvnsmfe davqvgasdi hiepddkvlr lrqrvdgvlh etllnevnia salvlrlklm
      241 ahldisekrl pqdgrfnikv rgqsidirms tlptqygesv vmrllnqssg lrkledsglp
      301 pellarlrrq lsrphgmilv tgptgsgktt tlygalseln epgkkiitae dpveyrlpri
      361 tqvqinskid ltfsrvlrtf lrqdpdiili gemrdqetve iglraaltgh lvlstlhtnd
      421 avdsalrmid mgapgylvas avravvaqrl vrrvcpdckt tdvldesrqq wlagrfpnqv
      481 gqtfhkgtgc qncnltgyrg rvgvfemlel enemmdklra ndavgfaqva rrsenykpll
      541 asamelalqg tvsldevmal gegdasgktd pifm
//
LOCUS       WP_010648226             132 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF423 domain-containing protein [Vibrio].
ACCESSION   WP_010648226
VERSION     WP_010648226.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..132
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=14273
     Region          1..128
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mkskwllsft glsglisval gafaahglka klspyllgvf etgvlyqfih tlaiafcail
       61 lllnlgqkaq kyffiaaicf iigifcfsgs lyalaltgik wfgpitpmgg llfmigwclf
      121 ffaafnikev sk
//
LOCUS       WP_010648333             191 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Vibrio campbellii].
ACCESSION   WP_010648333
VERSION     WP_010648333.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..191
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21309
     Region          6..191
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mamkplleqy gylalivsif legigipmpg qslmiaasii ssehvmnlsl vmivswlscf
       61 fgntcgylig yyfegwldkk gyisgpkmqk lqstiqkygp aclvvsrfve gmkqfmplac
      121 giakmprkef llgnalatti wvavfslltn ftfehlsvls qfytdhryvv wssaallfsl
      181 mifallkrkk a
//
LOCUS       WP_010648324             160 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Vibrio campbellii].
ACCESSION   WP_010648324
VERSION     WP_010648324.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..160
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18048
     Region          30..150
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mdirainktn cldlvpiffe leqyyfneqa asekelthyl kykvfseysg vkviaayngd
       61 tiigfatytv mfpapklsgq mylkdlfvss sargkgvglk lmkyltslav nhgchrldwt
      121 aestnpiagr fyqsigaerv tekeyyrfsg dtllefsqak
//
LOCUS       WP_010648336             331 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Oceanobacillus massiliensis].
ACCESSION   WP_010648336
VERSION     WP_010648336.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..331
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36334
     Region          4..325
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mekilevenl hvtfttyggt vkavrgvdfh lnegetlaiv gesgcgksvt snaimrlipd
       61 ppgkitngti lfkgenlaaf sekkmrsirg vdismifqdp mtalnptlti gtqlmeglqe
      121 hrnvsgkear kkaiemmdlv gipnpeerlk qyphqfsggm rqriviaial icepdlliad
      181 epttaldvti qaqilelfek iqgttgvsii lithdlgvva kiadriavmy agkiietgtk
      241 reifynpqhp ytqgllnsvp rldlaeerlt pidgtppdlf sppdacpfaa rcpyvmevcd
      301 kvypaktelt gshrvncwlq ddrakqliav k
//
LOCUS       WP_010648409             247 aa            linear   BCT 01-JAN-2025
DEFINITION  copper homeostasis protein CutC [Vibrio campbellii].
ACCESSION   WP_010648409
VERSION     WP_010648409.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..247
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26207
     Region          2..247
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mntqlevcid nieslhnaia ggatrielcs slalggltps ygfmqqaakh stiavyamir
       61 prqgdffyse eeiemmrwdi eaakqaglng vvlgvltpdg nihmpyatal cefaqalglg
      121 vtfhrafdqc rdaekaleev islgcerilt sglapsapqg idvlkalveq aqgriaimag
      181 agvnadnvgq likqakvtev hlsgkttrps hmtfiaeqsk mgaadvddfs ipvtntdaia
      241 nmvtaln
//
LOCUS       WP_010648428             679 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010648428
VERSION     WP_010648428.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..679
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=75868
     Region          4..626
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mqfwprrmip kliialiava llsaaliyll aflmgppnlp gdqatliydq ageiigeerg
       61 iqtnqwlsld eisddvidst liiedrhffd hngfdykrig svilknissg slqqgastlt
      121 qqyarnlfls pektwsrkik eafytvrlem fyskekileg ylntiyyghg aygieaasny
      181 ffnksaaelt laeaamlagv pkgptyyspl ndeenanqrq kvilrsllhe rrisetdyrk
      241 aveeklvyat mpeepriaay fqdqvlless ellglepssi rsggyrihtt lnrdfqgqle
      301 etiqetiqds seieaaaism dsesgailam vggrdyrksa fnravdarrm pgstfkpfly
      361 yaalnygyta stqlmskptt fqldngnvyq psnfngyyan qpitlaqala lsdnvyavkt
      421 nlylgpekli asakqfgiss dlpkvpslal gtasvsvtem tsaygllann gkemtsytve
      481 kivdqdgktv yerksdkaeq vldekktfil thlmtgmfde emngytsvtg sgitdqltri
      541 yagksgttds dswmigysps ivtgiwtgyd dnrrmevvse sayakeiwaa ymeavhqgqp
      601 edtfdlpsgv igipidplsg kratpdcehs rimyfekgte preyctehdd eneleadtet
      661 dshpaeergi ferlfdlff
//
LOCUS       WP_010648441             123 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF423 domain-containing protein [Oceanobacillus massiliensis].
ACCESSION   WP_010648441
VERSION     WP_010648441.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..123
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13050
     Region          1..121
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mklllilaai ngflavalga fgahglegri sekaiatwek avtyqmfhtm alvavgllla
       61 kyqngslfat sgwmffagii lfsgslyvys ltsiktfami tpiggvafli gwvllgiali
      121 kyl
//
LOCUS       WP_010648478             538 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Oceanobacillus massiliensis].
ACCESSION   WP_010648478
VERSION     WP_010648478.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..538
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60568
     Region          4..527
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mitvtnvslr ygdkklfedv nlkftsgncy gvigangagk stflkvlsge iepqsgnvsm
       61 spgerltvlk qdhyayeeyd vletvlmghe klykvkqekd aiymkadfse edgmraaele
      121 gefaemngwe aesdaavllk glgieeslhd mkmseipgdq kvkillaqal fgspdillld
      181 eptngldiqa iqwleeflin fentvivvsh drhflnkvct hiadvdfgki qvyignydfw
      241 yessqlatqm aqdankkkee kikelqafia rfsanasksk qatsrkkmld nislddikps
      301 srkypyiaft pereigndll rvegltkiig dvkvldnvsf imnkddklal vgkddiaktt
      361 llkilageme pdegtykwgv ttsqsyfpkd nakyfengdl tlvdwlrqys pedetetflr
      421 gflgrmlfsg eealkkadvl sggekvrcml skmmlshanv lmldeptnhl dlesiqslnn
      481 glikfkgail ftshdhqfin sianrlieit psgiidkems ydeyvqdrkl qkqisgmy
//
LOCUS       WP_010648486             184 aa            linear   BCT 01-JAN-2025
DEFINITION  TMEM165/GDT1 family protein [Vibrio campbellii].
ACCESSION   WP_010648486
VERSION     WP_010648486.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..184
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19539
     Region          1..183
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 msvlaisitt valaeigdkt qllsllltsr yrkpipiiaa iflatianha laawlgvvva
       61 dyfspevlkw vlvvsfvama awvlipdkld ddeqisnrgp fiasfivffv aeigdktqia
      121 tsilgaqyad alswvilgtt igmllanvpv vligklsadk mplglirkvt aflfvalaig
      181 aalf
//
LOCUS       WP_010648488             347 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Oceanobacillus massiliensis].
ACCESSION   WP_010648488
VERSION     WP_010648488.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..347
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38043
     Region          4..325
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mskllevkdl rvsfntynge vqavrgvnfd lnkgetlaiv gesgsgksvt smslmqllpk
       61 phgviksgqi lfegedlvnk ssqamqkirg kdismvfqdp msalnptmkv gnqiieglik
      121 hqnmnrtdak kkaielldlv gipqpevrmt qfphqfsggm rqrvvvaial acnpkiliad
      181 epttaldvti qaqilelmkd iqketdsaii fithdlgvva nvadrvavmy agkiveigtt
      241 edifynpkhp ytwgllgsmp tldseeeelf aipgtppdml npptgdafaa rnqfaleidk
      301 vmeppmfkvs dthyaatwll hedapkvepp esvkrrmqgf sntggdk
//
LOCUS       WP_010648505             445 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Oceanobacillus massiliensis].
ACCESSION   WP_010648505
VERSION     WP_010648505.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..445
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48808
     Region          12..438
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mekqhdfteg nivkqlfvfs gpiiltnllq tsyqfidslw vgnllganal gaigvastii
       61 fiilsfiigl nnaaltilsq qkgkdnhsgl ksylnafvvi ltviavvlgv vgyqfseqfl
      121 kllgtpdvml eeanvylqin flgilflfgy nfistvmrsl gdsktplrfv tiavilniil
      181 dpllirtfnw gvegaayatv lsqgiafiyg lfhvlhkkla pfsipslpsr eeiklilnlg
      241 ipsglqmsvi sggsaaimsv vtvfgsgvva gfssaqrlds llmlpahals tavssmagqn
      301 igvknwkrvs diskygilyn fsvmlligii vaffaeygve lfireeeave fgtkylqiia
      361 lcypflginf ilngivraag amyqvlvlni isfwvlrypf talfamkfge igiaigmgls
      421 fmisslfail yyrfgkwrek elfrr
//
LOCUS       WP_010648517             178 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010648517
VERSION     WP_010648517.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..178
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=20448
     Region          2..176
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mkiivfhgst rangnteclt yhavpkdkgt hiylrdynik pimdqrhdes gfdaveddhk
       61 glidlmlshd vivfstpiyw ysmsgpmkif idrwsqilrd pgythfrdel akkkvyliav
      121 ggdtpkvkgl plvqqfnyic qfykmsfegy vigrasrpne ilenktalkd asmlikwl
//
LOCUS       WP_010648525             512 aa            linear   BCT 01-JAN-2025
DEFINITION  amidase [Vibrio campbellii].
ACCESSION   WP_010648525
VERSION     WP_010648525.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..512
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55516
     Region          26..509
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mlnnsikkyi ifiisfvfsy svaaidldna tlneihialk nkkitseqlv esyleriekn
       61 kalnavvsid dnalknakkw dksgdknsil ggipflvkdn ynvvnqpnta gsialqdnia
      121 kydakvvell kqqgaivlgr tnmselaasy grfgysslag qtlnplnlqr dpsgsssgsa
      181 savaahlapf algtdttgsi rgpasvtgli gyrpsmglts rtgvvplslt fdtigplvss
      241 vedlviimdi iavedtkdqa svfyystqsa pnftrslnea tlenkrlgyi nnysgandev
      301 dviieqslik mkgqgaevie lslpeemasi gatvssfiia aefkpqleth lrtnnttlnl
      361 seiikklkad kenphpinpk rlaaleqnml nhdtnssryi sllnqhlplm rakldsikkq
      421 yqldgfvfat rpcpaaplps iiddsyqcrs qdlleagyia sllgypeisi pagvtqsnip
      481 islsflggfa qdvemiqlgh afeklahfsv en
//
LOCUS       WP_010648535             278 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Oceanobacillus massiliensis].
ACCESSION   WP_010648535
VERSION     WP_010648535.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..278
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30764
     Region          23..239
                     /region_name="yflN-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Bacillus
                     subtilis yflN; MBL-fold metallo hydrolase domain; cd07721"
                     /db_xref="CDD:293807"
     Site            order(78,80,82..83,166..167,185,238)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293807"
ORIGIN      
        1 mehdsympmt svgsgdliqv addvycftnq ivnlcfvgns dnwvlvdagm pksfdkiieq
       61 aeeiygenak pkalilthgh fdhvgaaael vekwdipvfa htlelpfltg kesypepdwt
      121 vegglvakls mffpdepinl rgisqlpddg tvpgmpgwkw ihtpghsrgq vslfreadrt
      181 liagdafitv kqdellkvtl qtkevngppr yftpdwraae esvqqlaaln pqkaitghgv
      241 pisgeelqeg lkrladnfke lavpdhgryv teqkndrd
//
LOCUS       WP_010648550             209 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Vibrio campbellii].
ACCESSION   WP_010648550
VERSION     WP_010648550.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23062
     Region          1..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnfdtllafg givfflaiip gpnallilft altqsrrfai anifgvalgf lihafvsakg
       61 lslllsqsal afnilkwigv ayliwlginn lrsglkladq klkldrkiek qtlkqafvkg
      121 lltnllnpki vlfylsifpq fvqpehileq simlgalqas ivaswflfvi ffatkvkaml
      181 tssktskwln yvsgglfiff giglantrf
//
LOCUS       WP_010648562             212 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010648562
VERSION     WP_010648562.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..212
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=24031
     Region          25..211
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 maekfkierp kipaelsaes fhyredayys riiiegetir aeevhrikfd evifknvvfe
       61 qvsfqnielt dcvfdhcdls nsdfsegsih rvefreskml ginfsdatia nvlftgcqgn
      121 lssfgfaklk hvmfeaclln ngdffeckfq kvgfrdceld evnfsntsln gvdlssctfh
      181 nlqasleslr gcivnteqai gfaqflglri ke
//
LOCUS       WP_010648564             262 aa            linear   BCT 01-JAN-2025
DEFINITION  ion transporter [Oceanobacillus massiliensis].
ACCESSION   WP_010648564
VERSION     WP_010648564.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..262
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=29804
     Region          14..219
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mnhfrkksae iaahpifina ilvlivinai lvgletypyf agtyfkwini adqiilwift
       61 veiiirligs ksissffrnp wnvfdfviva sgylfigahy vtvirilrvl rvlrvvsvip
      121 slrrmvrall ltipsmgtil llmgiffyif avigtmmfqs iapeyfgtlh dsllslfqvi
      181 tleswasgvm rpiladdpas wwffvtfiii gsfviinlfv gvvvnnveea sreekptptd
      241 ikleevqnel kdikrllekk te
//
LOCUS       WP_010648584             379 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Oceanobacillus massiliensis].
ACCESSION   WP_010648584
VERSION     WP_010648584.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..379
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42937
     Region          129..367
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mqhwyhifpk ntglslfawi afcllpfyfi frstapaefi agifmiflff vayrlafikk
       61 gwtvyvsvgi eiainigmtl yigyvyfslf laffigsiqn kagfitlyiv hlvttiaaim
      121 vgfytqsqvl mpqlpfviic vigvillpin mfnrnkrekl edqledanek iaqllileer
      181 eriardlhdt lgqklsligl ksdlagklve akpeaaksei kdinhtarma lkevrelvad
      241 mkgtklkdem irvrqllsaa qiefrlegkp eledtpllve nvlsmcmkea vtnivkhsga
      301 tvcwisidqs sdkwlmkikd ngtglkdkak ykegngilgm kerlefvngn lkmstlngti
      361 lilqiprviq qkeqeestk
//
LOCUS       WP_010648585             645 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Vibrio campbellii].
ACCESSION   WP_010648585
VERSION     WP_010648585.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..645
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=72514
     Region          15..639
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkkpafgplq piavfalfsl aflsvsrill aiwladries fndliyilgq glrvdfatic
       61 wlfilpglls allpvqgkig acwklvlrcw mvaglwilvy melatapfiq eydlrpnrlf
      121 veyliypkev fsmlwtgykl elfigtvgta itlflgwkws kkltdnaqqv nwkwrpliai
      181 lvvligvgga rsslghrpln pamvafcndp llndlalnss ysllfavnnm kseksaeqfy
      241 gkmdnqkmle lvrssstksd fnpsllptmn tnkatyqgkp knlvillqes lgaqfvgslg
      301 glpltpnfdk lmaegwqftq myatgtrsvr gieavttgfp pspsravvkl sksqtnffti
      361 adllkangyh tefiyggean fdnmksfffg ngfdqiieek dyenpefvgs wgvsdedlyt
      421 kadqeferls ktdkpffslv fsssnhspye ypegkiepyd sefmtrnnav kysdyaigtf
      481 fdkakkssyw ddtifiviad hdarvsganl vpvkhfhipa liigkgvepr kddriannld
      541 mpptllslig vdatspmigr dltkplared erammqydkn fgyltrdnlv vfspgekvst
      601 mqynfdnqtm epievepaii erakanalfa skayqnnwys skatk
//
LOCUS       WP_010648603             353 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Oceanobacillus massiliensis].
ACCESSION   WP_010648603
VERSION     WP_010648603.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..353
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=38735
     Region          18..346
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mkriviiggg yggikilagl ldqplpediq itvvdrnpfr slktefytia agtaadqdvr
       61 vdfpkdprvn yvfdeismid tsknqllfkd sersipydyl aiavgcedny hgvpgaeeft
      121 esvqtfakar htgvaignlk aygkvsivga glsgievase iresrpdlni rlldrgstvl
      181 kafdskiqny veewfvkndv dvlhhsniey vekdgvcnng vcfindvtiw tagvqpnrlv
      241 relpftkdiq dkivvnefyq vpesqniyvv gdcasseysp saqlaglqge qvaevllavl
      301 kdkepkkpka lklkgtlgsl gksdgfgnmv ktpmtgllpr laksgvlwls krh
//
LOCUS       WP_010648654             463 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Vibrio campbellii].
ACCESSION   WP_010648654
VERSION     WP_010648654.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..463
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50754
     Region          27..438
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkntgklwil gllsssisla chsapitfdd awnlllenny slkaqranve syeyqqsatd
       61 nlnlpqvsig anytrldtdv tvsgqqllds tgahitlppl fnvtstiter difsssirai
      121 wpiftggrin aaqaaaegkt deaksqlame qqarfedlsk yyfsvvlake vlatrqavek
      181 gltkhrdfai kmeeqgqiar verlqaeasl dkakvetrka asdlsiaqaa lgkilaqnda
      241 vepsetlfin nnlpplsafv dqtlltypgl dlldakhkqa sslikaekgk yypevylygd
      301 yslyeddsla sqmkpdwlvg vgvniplies tgrsekvkaa qsmvtqvdal ksqakqdlsl
      361 lvqktyleaq qaidevqgld ssialadenl rlrekaftqg lsssldvvda qlyvasvqtq
      421 qsaarfryli sltkllalss emnsfaqyqh tayvpastsk eak
//
LOCUS       WP_010648675             508 aa            linear   BCT 01-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Vibrio campbellii].
ACCESSION   WP_010648675
VERSION     WP_010648675.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..508
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=53509
     Region          1..498
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mldgilqgls tavmpmnimm vivgcfvgtf igmlpglgpi saialmipit ygldpssgli
       61 lmagvyygav fggstssili napgcsstvv tafdgypmaq kgqsgkalal aayssftggt
      121 lsaimllvaa palanvslsf qssdyfalml lglsavaafa gkgqvikawm mtilglmlst
      181 vgidkgvgve rftfgltdlm dgfsflllam atfalgetlm gilkpsedtr deeqdklsni
      241 gsmkvtkeei kevapvsirs silgfftgvl pgagatiaaf lsygmernla pkdkkeqfgk
      301 gsirglvape sannaassgs fvplltlgip gsgttaimlg aliaygiqpg prlfvehpdv
      361 fwsviismyf gnivlvilnl plipyiskll avprtvllpm ilffsitgvy lvsfntmdvf
      421 vmllvamaai alrlanfpla plllgfilgg lmeenlrral misdgelsfl werpitltft
      481 vlavlvlgsp lfvklfqklk aqpvkveq
//
LOCUS       WP_010648668             587 aa            linear   BCT 01-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator [Vibrio
            campbellii].
ACCESSION   WP_010648668
VERSION     WP_010648668.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..587
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=65421
     Region          11..584
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 melqhitnsn wlstswdrse qaglkqrrrp ddirvtsafl edrrhqlnfl idavkqfalp
       61 lfnqlfthcd srliltdadg viigswgqpk freklteial ssgacwqekl kgtnaigtal
      121 veakpvsvig dqhfiqhhrf iscsaspifd hlgnligvld itseqkkhdf stqvlvqnmv
      181 qqvenqllnq ipqghirvdl aceqgllnsg wqgiiianee gqilahnqva sqlldqinvv
      241 gqqlasilds ssnnqslvfk tqplserkas sraisasndl hygdstvehc wqqanrvidk
      301 disllilget gvgknefvka lhknsqrkng plvsvncgal pkdlveself gyvagaftga
      361 snkgyqgkir qahkgilfld eiadlpleaq srllhvlqdk tvlpvgsnqt iqvdtqiiaa
      421 thkdlerlve qgefrqdlyy rlnglivelp rfqersdkqa lienihhrha eseqsicphl
      481 lslmlgygwp gnlreldsli kvsalmaqge aqlelshvpn hlakklsqas vieqvdtskt
      541 rdmrttvedk lvktyqanqg nisktsrmlg lsrntiyrkl kslgmlk
//
LOCUS       WP_010648684             162 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Vibrio campbellii].
ACCESSION   WP_010648684
VERSION     WP_010648684.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..162
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17727
     Region          1..>49
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkqkgfslte lvvaivvlai iglfaapkim hmqrearint leafvgafha tnevvmtkak
       61 iqgvanapla klsdhdiyvr mgslalddfn vanameidgf nlvntgssqt pslivylgke
      121 ksllkirdse cfisisrpft aydkqgtvsm yelkvnkfhd nc
//
LOCUS       WP_010648704             349 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Oceanobacillus massiliensis].
ACCESSION   WP_010648704
VERSION     WP_010648704.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..349
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38344
     Region          7..321
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkqdelfdvt vigggpagly safysglrem ktkiiefqpv lggkvhvype kmiwdigglt
       61 ptpaaklidq iteqgltfnp tvvlnekivs iqkneedifi lqaesgdvhf sktvimavgg
      121 gilnpqrlsi egaerfevsn lnytvkslqr fkdktviisg ggnsaidwan elvdiaknvy
      181 ltyrkdvlpg heapasrlmd snavcyfncs itklishsnk dmiehveltn hhtnevlsip
      241 ideviinhgy erdaslmens pldiemvdgy fiagnpkges sipglyaagd ilhhegklhl
      301 iagafqdaan avnrakqfie pnaeksamvs shnelfkern kaivrqlvn
//
LOCUS       WP_010648705             261 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Oceanobacillus massiliensis].
ACCESSION   WP_010648705
VERSION     WP_010648705.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..261
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28950
     Region          3..255
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mfrlqtenis isygeslivk dlsieipdkk ittiigangc gkstllkait riishqagsv
       61 vldgediskq ntkllaqkma ilpqsqegsn gltvgelvsy grfpyqsgfg rlnkkdydii
      121 nwalevtgta afkyrpvesl sggqrqrawi amalaqetei ifldepttyl dmahqlevle
      181 llqklneeqg rtivmvlhdl nqaarfadfi iamkdgeiiq sgdsesvltr dvlkqvfqid
      241 aeigrdprtn kpmcitynli k
//
LOCUS       WP_010648781              78 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutaredoxin family protein [Bacillaceae].
ACCESSION   WP_010648781
VERSION     WP_010648781.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Shelton,M.D., Chock,P.B. and Mieyal,J.J.
  TITLE     Glutaredoxin: role in reversible protein s-glutathionylation and
            regulation of redox signal transduction and protein translocation
  JOURNAL   Antioxid Redox Signal 7 (3-4), 348-366 (2005)
   PUBMED   15706083
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   4  (residues 1 to 78)
  AUTHORS   Fernandes,A.P. and Holmgren,A.
  TITLE     Glutaredoxins: glutathione-dependent redox enzymes with functions
            far beyond a simple thioredoxin backup system
  JOURNAL   Antioxid Redox Signal 6 (1), 63-74 (2004)
   PUBMED   14713336
REFERENCE   5  (residues 1 to 78)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..78
                     /product="glutaredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=8740
     Region          4..76
                     /region_name="GrxC"
                     /note="Glutaredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG0695"
                     /db_xref="CDD:440459"
ORIGIN      
        1 mnqtvtvyts sfcpvcgmvk sfldsfdity kevivdlnpi armkvigktk rltvpqtnin
       61 gewisgfdpe rmlkilik
//
LOCUS       WP_010648709             124 aa            linear   BCT 01-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Vibrio campbellii].
ACCESSION   WP_010648709
VERSION     WP_010648709.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..124
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13560
     Region          9..115
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 mefkliqevi naehrlkasm vssdlavlde lladnlvfin hfghrvskqe dialhqsgll
       61 siasielsdl qvephgncvl vyanaeiigt ydgaesngrf afsrvwlkkd gklqvvsghs
      121 tvfv
//
LOCUS       WP_010648788             177 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Vibrio campbellii].
ACCESSION   WP_010648788
VERSION     WP_010648788.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10644999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..177
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=20249
     Region          127..175
                     /region_name="DnaJ"
                     /note="DnaJ molecular chaperone homology domain;
                     smart00271"
                     /db_xref="CDD:197617"
     Site            order(152..154,162..163,166..167)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mfdiftsaha eqravlfegs eelsvktakl mlsrlhtdyy ndtereraty vlaklgyles
       61 gskreskese nslldkanet irkanhrine lksllskaer didflthena nlrsqllesn
      121 ctlterdilg yeslpssqel rkrykslasi yhpdkggskp mmqrindsye klkneva
//
LOCUS       WP_010648795             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Bacillaceae].
ACCESSION   WP_010648795
VERSION     WP_010648795.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..259
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26941
     Region          3..258
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mdltfiivvf aigfigsfls gmlgvggsii kypmllyipp lfglvaftah evsgisavqv
       61 lfasiagvwa yrkggylnkq liiymggail igsligsygs sflseqavnv vygilaviaa
      121 vmmfvpkkkm ddvplnevtf nkplaailal ivgiasgivg aaggfllvpi mltvlhiptr
      181 mtiatslavt fissiggsvg kiatgqvdyw paaimivasl laaplgakvg krmntrilqv
      241 ilalliagta ikiwidilt
//
LOCUS       WP_010648860             399 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Oceanobacillus massiliensis].
ACCESSION   WP_010648860
VERSION     WP_010648860.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..399
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43201
     Region          110..399
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mgyydqnyrt psrrrgrwll plimgviigg livvivvpef mndnhstgdr dvteetdlag
       61 sdpgmnrslq vdvstqltei veevtpavvg isniqqskdy wqqqegveag tgsgviykqd
      121 ndtayvvtnh hviegadtve vvladdthle akiigsdlfs dlavlkmdss nvkkvidigs
      181 sanikvgepa iaignplgly lsstvtqgvi sgtertipqd fnqdgradwq aeviqtdaai
      241 npgnsggali ningqligin smkinqeave gigfaipids ampiieelea ngevvrpylg
      301 veiysldevp qtewkntlnl ppeveggvyv wstealspad kagierldvi teldgepimn
      361 midlrkilyq ekeigddvav tyyrngekaq ttitlgtqq
//
LOCUS       WP_010648933             407 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Oceanobacillus
            massiliensis].
ACCESSION   WP_010648933
VERSION     WP_010648933.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..407
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42583
     Region          28..406
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 msltkkiiia lilgiiagia ltfasdkvft gldtyllgpv geifinlimm lvvplvfvsi
       61 tlgtagvgdp aklgkigvsa vtfflistai aiaiglsigy ilepgkegvf dvenaefeae
      121 evppvmetlv niipdnpias masgemlqii afaifigval aflgektagi rslfeqanei
      181 lnwlvntvmk aapygafali assigdagld algsmamylv avilglfihg aftyslaiwg
      241 lgkanplhfy kaffpamsvg fstsssnasl piamktlqek lgvkkeistf vqplgatinm
      301 dgtaimqava tvfisqvyai pldftdllmv vltatlasvg tagvpgvgml mlamvlsqvg
      361 lpvegialvi gvdrlldmlr tslnitgdat cayiisekek rkemkas
//
LOCUS       WP_010648894             257 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010648894
VERSION     WP_010648894.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..257
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27877
     Region          3..254
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgkimsianq kggvgkttss vnlsaclasl gnrvllvdtd pqgnatsgvg inkadvsnci
       61 ynvlvedlpa eevvvptkvn nldiipatiq lagaeielvp iisreirlkk aldslkekyd
      121 yiiidcppsl glltinalta sdtvmipvqc eyyaleglsq llntirlvqk hlnkqlmieg
      181 vlltmldart nlgiqvieev kkyfqdkvys tiiprnvrlg eapshglpii iydpksrgae
      241 vylelakevi angervr
//
LOCUS       WP_010648969             247 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Oceanobacillus
            massiliensis].
ACCESSION   WP_010648969
VERSION     WP_010648969.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..247
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27859
     Region          8..246
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mvqlfdderl dyllndehmq iiqsptafaf sldavllanf ayvpakrgsi ldlctgngvi
       61 plllskrtra nitgveiqer iyqmaarnie lnglnaqldi vhgdlkemqp vlgqscfdvv
      121 tcnppyfktp svtehnhnef ltiarhevyc tledvvkack lhvrpggkva mvhrpgrlvd
      181 imelfrkynv epkrmrlvyp krgkeanmll iegvrdgkad lkilpplyiy endgsytkea
      241 egiiygk
//
LOCUS       WP_010649028             134 aa            linear   BCT 01-JAN-2025
DEFINITION  GtrA family protein [Vibrio campbellii].
ACCESSION   WP_010649028
VERSION     WP_010649028.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..134
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14871
     Region          12..131
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mgkltkfapl erfalvggig fvvdtlifsl lfhvaglelm varsiaflfa atttwlgnrw
       61 ltfsqadkhn plyqwlkfma sacisavpnf aafkgwtlmf gkqdymvfla lalgilvgmm
      121 snyllsskwv fsqq
//
LOCUS       WP_010649036             412 aa            linear   BCT 01-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Vibrio campbellii].
ACCESSION   WP_010649036
VERSION     WP_010649036.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..412
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=45385
     Region          <10..>193
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          38..60
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          61..83
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          84..105
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          106..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          129..151
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          152..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          209..400
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(209..212,215,217,234,236,265,281..284,339,343..344,
                     346,356..357)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
ORIGIN      
        1 mqtleqlktg qlvgikqlkl aqgltefpme ilelaetlev ldlsgnalsd lppeleqltk
       61 lkiifasnnq fthlpevlgk lpnlemvgfk tnkikevsea slpsqlrwli ltdneievlp
      121 nslgerprlr klalagnrik qlpnsmenlv nlelirlsan qlehfpdvlm klpklawfaf
      181 agnafckhps sldsvpkvtt gsyslnhvlg qgasgvisha nwtdaqyefp sevavkvfkg
      241 evtsdgfphd eleaclqagh hnnlvksiaq vddgnelalv melipdshyn lglpptletc
      301 trdtfpqgft ltveqvnaiv eqmvdvfnhl hnnkvchgdl yahntlvneq gemifgdfga
      361 asiygylseq qqaaiktiea raltyfiedv csvcedskaa levmnrfasi aa
//
LOCUS       WP_010649162             589 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Oceanobacillus massiliensis].
ACCESSION   WP_010649162
VERSION     WP_010649162.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..589
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=68487
     Region          28..>575
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mtktiatyqr teyprpqfqr tswknlngtw kfafddenig ekeqwtnkpg fttdiqvpft
       61 yettasgige eafhpyvwyq rtfeipeaei gkrtilrfqa sdystkvwvn gkyignhigg
      121 nasfsfditd aidykkknel vvkaedsmsc yqprgkqrwr denfgcwyvq ttgiwqtvwl
      181 eflneasidn vkitpdfdah svqfdyalsg sfskdltlet tisfsgetvk qfsitpdrss
      241 vsfgvdihsd lhewkvmhwt pqhpnlydvt fklyengrll devdsyfgmr kisikdgqvl
      301 lnnepfyqkl lldqgywset mltppsddai lediektiem gfngvrkhqk lederflywc
      361 drkgllvwse maatyefsde aienftkewl nivqqhynhp siitwvpfne swgvpnissn
      421 kkqqaftesi yyltksidsq rpvivndgwe htvsdiialh dyeelgelfl erykdkdsii
      481 nnelphnnkr yafangyeyk gqpimiteyg giafndesgw gygnqvntea eflsryrsit
      541 daiksipyit gycytqitdv qqevngllke drtpkielgk ikeindstk
//
LOCUS       WP_010649255             276 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Oceanobacillus massiliensis].
ACCESSION   WP_010649255
VERSION     WP_010649255.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..276
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31417
     Region          160..269
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 melhydgdqg mkdfirdnrk eferklldea vqvrdkvdqi niigninlld naynlalsvv
       61 qnkrdevtal gtkegvawag hsltlafkle wiqairktlw eflyeydkeg dklsqkdeyy
      121 nlqikinglv deffrsffls yssykdklle sknklvesls apiipiseki svlpligmld
      181 efrgniieek vlndigkkgv qvlvldfsgl aqmegnaihf fmklldgitm mgckaiitgv
      241 rpevvplfie qdlsfgknie tkatlqqalk dflepk
//
LOCUS       WP_010649184             453 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Vibrio campbellii].
ACCESSION   WP_010649184
VERSION     WP_010649184.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..453
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48154
     Region          1..447
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mdilflflmv igfmligvpi avslglssil fllmhsdasl asvaqtlfna faghytllai
       61 pffilassfm stggvakrii rfaiaivgwf rgglamasvv acmmfaalsg sspatvvaig
      121 siviagmikn gyskefaagv icnagtlgil ippsivmvvy aaatdvsvgr mflggvipgl
      181 lagvmlmiai yiaariknlp kqpfvgwket fdaakdaswg lllvviilgg iyggiftpte
      241 aaavaavysf fianfvykdm gpfadkqntk pvlvkifqtf vhkdtkhtly eagkltimll
      301 fiianalilk hvlteeripq mitesmlsag lgpitflivv nvllliggqf mepsglliiv
      361 aplvfpiaia lgidpihlgi mmvvnmeigm itppvglnlf vtagvakmsm mnvvkaalpw
      421 vavmflflii vtyvpwvstw lpttlmgpei itk
//
LOCUS       WP_010649336             244 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Vibrio campbellii].
ACCESSION   WP_010649336
VERSION     WP_010649336.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..244
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27360
     Region          7..241
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mkeknivvef sgvnkwygey halkdinfsv htgeivvvcg psgsgkstli rcinhlesiq
       61 egelsvfehp anskaqkpgk vgmvfqhfhl fphltvlenl tlapirtlkl skqeaeeram
      121 hylkrvniee qankypiqls ggqqqrvaia rslcmepdll lfdeptsald peminevldv
      181 mvelaqsgmt micvthemgf akkvanrvvf mdegeiiemn spvalfekpq hprtqaflnq
      241 ilsy
//
LOCUS       WP_010649357            1019 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Vibrio campbellii].
ACCESSION   WP_010649357
VERSION     WP_010649357.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..1019
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112784
     Region          1..1015
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msiaeysikn kviswlfivi laiggvtsfl elgrledpaf tikdamviat ypgatskeve
       61 eeltypleke irklpyidki tstsssgmsq imvsmkmdyg pdelpqiwde mrrkindlqp
      121 tlpqgvqslq iiddfgdvyg vmlmltgddy dyvelkryad qltrelelid gvgkvdiage
      181 qqemlfveis ldrlaalnld mnvisgllnq qnnvvsagev mvngesliir psgtlntvea
      241 lesliihgrd tgnlirlkdv atisrgiqek pgnvllyngk kainigisfa sgvnvvevgq
      301 rieaellsle tikptgidmn yfynqsqevd dsvkafvisl aeavaiviiv llftmglrsg
      361 viiglvlllt vfgtfilmny nnielhrisl galiialgml vdnaivvveg ilvglkkgrt
      421 kvqaatdivk qtqwpllgat viaitafapi glsqdatgef mgslfwvlcf slflswitai
      481 tltpfladll lkeedknada ededpykgwl fvafgaslkf alrfrwltva gmvallvgav
      541 vafgsvkqqf fppsntpmfy vdmwmpegtd iretikkaee vesyirtqdd vdfvsasigq
      601 glqrfaltyq peksyeayaq fqvrttdren mfkllhkldd slaktfdkpt fqfklmefgp
      661 spaskieari tgpdpqvlrd lavqvedilh tdpgarnirh dwrertkelv pvfneskarr
      721 lgiskedlss tlqmafggst lgflrdgthi lpimtrlpea ervdfeslqn vniwspslqs
      781 yipvdqvidg vkldweepli qrrdrkrtlt vladhdvlsd dtaaslfarv qpkvmalhip
      841 egyeitwgge yesskdaqeg lfgslpmgyl lmfiitmllf nslkkplviw ftvplsiigv
      901 sfgllttnmp fsftaflgll slsgmilkng ivlldqinle lesgkdpyla ivdsaisrvr
      961 pvsmaaltti lgmiplvfda ffgsmaitim aglgfatvlt livvpvmfai lfkikptta
//
LOCUS       WP_010649345             317 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Vibrio
            campbellii].
ACCESSION   WP_010649345
VERSION     WP_010649345.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..317
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35750
     Region          3..316
                     /region_name="COG2374"
                     /note="Predicted extracellular nuclease [General function
                     prediction only]"
                     /db_xref="CDD:441941"
ORIGIN      
        1 msnknhitfa tanllnfvap pgayydfeni yslddwqdkl twtksqfdql npdiiglqev
       61 fsieetqtff aeigyqyfac vdtphiegdy iysrpvvava srfpiesfea vtfdrdtlna
      121 fgdidappfs rkpvratiih piighicvyv thlksqrpad setpeqasrp iarwlstqqr
      181 gweaailrda mqkhyannpm ptllmgdmnq aitktsvnnv lveqygdsvt glqlcdgwel
      241 qvvpslesrp athyhftkgn vldyillsqe fdahadvsia evtnyqvldt hlinpsferd
      301 knasdhafva ltveikl
//
LOCUS       WP_010649463             274 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Oceanobacillus massiliensis].
ACCESSION   WP_010649463
VERSION     WP_010649463.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..274
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=31483
     Region          14..237
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mskknivsie dripklkqar kkkanrrlif ylsiffflia iivylqspls hiktinvegn
       61 gfianekiie ysnlttntni wtidqheiek airkdpives vsverslpwt vnidvkeqrv
      121 igyiskdmmy ypilgngeil keagesfrgd aplffdfeee eylqrmaael ealpqdildv
      181 isevhwdpae dnknnillym ndgytvkgti rnfadrmevy psivsqldpe drgiihigvg
      241 vyfesfnend endenendes esnpetdghp vted
//
LOCUS       WP_010649371             151 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Vibrio campbellii].
ACCESSION   WP_010649371
VERSION     WP_010649371.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..151
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16843
     Region          29..145
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 melkyrsadf edleslvall sndplgskre dasvplnsay ieafeaikrd pnnellvvel
       61 enslvgvlqi tfipylthig gwrcliegvr ihsdyrgqgf geqmfahaie lakskgctiv
      121 qltsdkqrpd airfyeklgf kathegfkla l
//
LOCUS       WP_010649471             454 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Oceanobacillus massiliensis].
ACCESSION   WP_010649471
VERSION     WP_010649471.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..454
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=49969
     Region          1..454
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mlfttnwlsk vfpdfkgkla peaeidevtt dsrnvggnsl fipivgdnfd ghdfanqaie
       61 agagamlwdk nkeipnevpe dyplflvedt lkalqrlaah yrndinpivi gitgsngktt
      121 tkdltaavtq tsyrthytng nfnnhiglpl tilsmkrdte vlilemgmsn fgeielltkl
      181 arpdyaiitn igeshieflg sregiakakl eivkglkeng vlivdgdepl lqnlqlsqrv
      241 isngftaend nvltnisiva getafqlsdg frykipllgk hhaknasfai tigkllnida
      301 ekcsqafdtl srtamrfeli kgkngvtiin daynasptsm kaaievvkqm dgfeqkvlil
      361 gdilelgshs eelhrsiaya iespitavyt ygedaklise evkdnqincq hylskeelan
      421 alepylskda lllfkasrgl kfetmiaqil eetk
//
LOCUS       WP_010649559             541 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Vibrio campbellii].
ACCESSION   WP_010649559
VERSION     WP_010649559.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..541
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=59467
     Region          4..533
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mrsiitfkll laliavftcv lavstgyqyy qqktlinnvl seqlhdkasn yfdslnmmml
       61 tgtmaqketl rkkalaqegi eqvrvlrada vskfygpgda nqkpmddidq ralngelvie
      121 pisadwgkgl vvalpmksse nyrgtncvac hiapegevlg airleynmnh vnslinrqam
      181 famgimsvia fvgflitmgl irkiivcpiq ntsrfmsnvs askdlskrle ckqrdevgql
      241 sdsinsfmdt vseslervrn tshsladsag rltdvaqstd eaadnqqvet nevqtnisgm
      301 leqqdiveqa tidatilvnh tvdvattsas qahhvsgdik slvtdidkvr ekiatlnqqt
      361 eevssilgvi kgiaeqtnll alnaaieaar agdqgrgfav vadevrnlas rtaeatsnie
      421 niisqfqqgs eesltsvdnv cqfahqrsvd venlsetirn vvdemhqvlk haeniqqqtq
      481 ttsnvskhiq skvdtitlha ddtsqsasht reisvdlehl serlesllnq ftlseeqrtr
      541 k
//
LOCUS       WP_010649618             452 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Oceanobacillus massiliensis].
ACCESSION   WP_010649618
VERSION     WP_010649618.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..452
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50082
     Region          14..447
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mydsryqwin kltpvqmllf fyliavilst iilalpvahq dgveiafidv lftavsaisv
       61 tglstisiad slsttgiill glimqlgavg imaigtliwl llgkriglke rslimtdqnq
      121 tsfqgmvrli keivyvllvi eligflilgt yflqyfptag eaylhgffgt isaisnggfd
      181 itgqslipfk ddyfvqfini lliifgaigf pvlievkeyl fqktdarhpf rfslftkvtt
      241 ttffilvvvg siviylldmn yffadktwhe slfyslfqsv ttrsgglatm dvskltesne
      301 lfmsllmfig aspssagggi rtttfalali yvftyirggs tirifnreih eedlakavav
      361 tlvafiivfl sllvmtiiep fslgqllfev asafgtvgls lgitgdlttf skillmllmf
      421 lgrvgimtfl lifkrkkskv nyhypkekii ig
//
LOCUS       WP_010649663             200 aa            linear   BCT 01-JAN-2025
DEFINITION  2OG-Fe(II) oxygenase [Vibrio campbellii].
ACCESSION   WP_010649663
VERSION     WP_010649663.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Chowdhury,R., Leung,I.K., Tian,Y.M., Abboud,M.I., Ge,W., Domene,C.,
            Cantrelle,F.X., Landrieu,I., Hardy,A.P., Pugh,C.W., Ratcliffe,P.J.,
            Claridge,T.D. and Schofield,C.J.
  TITLE     Structural basis for oxygen degradation domain selectivity of the
            HIF prolyl hydroxylases
  JOURNAL   Nat Commun 7, 12673 (2016)
   PUBMED   27561929
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..200
                     /product="2OG-Fe(II) oxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=23466
     Region          4..189
                     /region_name="EGL9"
                     /note="Proline 4-hydroxylase (includes Rps23 Pro-64
                     3,4-dihydroxylase Tpa1), contains SM-20 domain
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG3751"
                     /db_xref="CDD:442965"
ORIGIN      
        1 mnklidalst hgyyiwddfi sqeevaelrd cipddwkkar igrnddvtri etirsdkiqw
       61 lkrdmgapva sfldkmeeir leanryfflg lfeyeahfak yekgdfyqkh ldcfkgnenr
      121 rlttvfymne swseedagel vvydlndnei akipprsgrl lvflseqfph evlptnaerf
      181 siagwfring vkdnqldiah
//
LOCUS       WP_010649666             120 aa            linear   BCT 01-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010649666
VERSION     WP_010649666.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..120
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14005
     Region          1..115
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mivyydsyck ictnsstvwk kldwrkkltf dsfrtmqnyp pamekslhvq hngkwfngys
       61 aiieiakmlp llwifvpfmy lfkfiglgdv iyklvaknrk lvpvnqckdg escqinpdsh
//
LOCUS       WP_010649652             403 aa            linear   BCT 01-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Vibrio campbellii].
ACCESSION   WP_010649652
VERSION     WP_010649652.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..403
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44723
     Region          68..332
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mqykpedsik iaiadvgigm fvtaieqnkr vnlanagrvs seqgikklha sgvkyvwvdq
       61 klsaqqcvfk pveeehdvtl saseitispk vqrafrsrea qhkrakklia eakglaqkll
      121 nqtfegklie vneieswadd miesvfidsd alqcvsalrq kdsyllehsv nvacllvsfg
      181 khlgldkdkl kqlaiggiih dvgkikvddg ilhkparltp eefehmklhq vfageiilgv
      241 kglsdvsrdv clmhhekldg tgyphglsge qipmhgrmsc ivdiydalta drvykkgmss
      301 aeafkillsl tpfhldpdlv ykfincigvy pvgsivqlsd grigivwtsn dsqplkpivk
      361 cfysrkykry idvamvdlks ssysvekaia psslevdpkp fyd
//
LOCUS       WP_010649688             740 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Vibrio campbellii].
ACCESSION   WP_010649688
VERSION     WP_010649688.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..740
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82177
     Region          25..740
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mnrqfmltpa tvaiamvlvt pqvlaqeden ivviglqdds avgpdfsylg aksrtatkmd
       61 lainetprav svvtreqmdd rasisvsdal qytpsiqtny fgednkqdwf iirgfkqans
      121 glyqdgtrly ssgfyswqid pfalervevl rgaatvlygq nppggvinlv skrpqfdggs
      181 gqvsvgygse drkqisldmn sevneklavr vqglarkngt rvdgveaerf liapsltykf
      241 tdmseitllt syqkddsdpy lqflpvegtl kpnkngkisd slalgntdwe tfereqlslg
      301 yelshvfnds tsfvqstrys qmdvnlrqmy syvyaadvpg lgplldplne rksilraast
      361 eegssdafni dnrlmhnmqw gsvehnlmvg idyqmvsidg kdfasdplva dgnsilntpi
      421 gmlpdprfdv fnpnysnnvw lldpttlqpl tdadkqrtkv dneqlgiylq dhilvndkwa
      481 vllgaryddt snevhnvttg srikvdneew tfsvgtayis eagftpyfsy sqyfdpiiqq
      541 dsagkpakpe sgdqfeigvk yqprtfdgyf niaayqatke nlarihlnql tqigevenkg
      601 iefeavanvt psltllgnia yvdseikedv naswvgnsps qvantvssaw ahyrflegtl
      661 dglavglgar ytgesygdnt etlkvpgyfl mdatvsyrig dyklqvaakn ladkeyvatc
      721 dgfcwygdrr nviasltydw
//
LOCUS       WP_010649708             408 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Oceanobacillus massiliensis].
ACCESSION   WP_010649708
VERSION     WP_010649708.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..408
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44603
     Region          2..395
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(8..9,12..13,16,51,98..99,101..103,106,129,132..133,
                     136,228,231..232,235..237,240,270,274,323..324,328,332,
                     348,351..352,355..356,359)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 miaglgvffs gpgqtysnsa fidayitdfg wsrsqvsgiy saatlvagli mlfvgrfidr
       61 fgprimmvsi gtifaiacfw nsivssiwml algfffirll gqgsmslipn tlvaqwfikk
      121 rglafsimtl gsflsamlfp ivntwlintw dwrfawqfwg illlvifvpi alfgvrnrpe
      181 dmglepdgfq skqatsvkpl igspfikeaa edwtlseark tkafwailvc vgipamvntg
      241 itfhiisifg snelspavaa tvlslmavvg ipmsfvsgfi tdriptnyll taifiieiil
      301 llmllvtsnf iiailfgtvw giangleria lnviwpnyfg rryigsingv gvtigvigss
      361 lgplpfgigy dlfhnytlvl litlvfpvig vissliakkp dksqlisn
//
LOCUS       WP_010649732             100 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Oceanobacillus massiliensis].
ACCESSION   WP_010649732
VERSION     WP_010649732.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..100
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11617
     Region          5..65
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mpkirppret wfksirpivw krdggicckc gieislyecn idhiisgvrg snkllnlrtl
       61 ckkchvlrld hnhrgmiqaa iknelippnw rnmvwdedke
//
LOCUS       WP_010649754             247 aa            linear   BCT 01-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Oceanobacillus massiliensis].
ACCESSION   WP_010649754
VERSION     WP_010649754.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..247
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27466
     Region          1..237
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mqgilyvshg srvmeataea safiqsvknq vnvahqeicf lelseptvaq gidllieqga
       61 srisivpvll lgaghyfkdi paevnkirrk yprvqftyge plgiqeritd vlaarinetd
      121 vpiepdakvl lvgrgsrnpq tkrdieqvta dlqqkmnipv dacylaacep sfetefqtsl
      181 reshaqlfiv pylwftgvlm qfletrvaes qgenksiilc rqlgnhssmk kalqervhea
      241 cssvkti
//
LOCUS       WP_010649741             457 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Oceanobacillus massiliensis].
ACCESSION   WP_010649741
VERSION     WP_010649741.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..457
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49994
     Region          1..457
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mdtalnnvvs elhnfleesq issndsilel hsrdesyhlp srpdvvvypk taeqvvaivk
       61 lasensvsiy pfgmgssleg hvipyehgit idfslmnkii dikekdflvt lqpgvtrtql
      121 nkelkkyglf fpvdpgadat lggmaatnas gtlsvkygtm rdnvrdmevi ladgmkihtg
      181 tlaaksssgy hlnglfigse gtlgcitelt lkvcgipefm taaratfqtv edaiegvvai
      241 lqagipmgri eivdeesirq vnrfsesnyt elptlflefh gneaglqqdi aftqeivadf
      301 nclniqfetd taarnllwda rhnlayayih sypgrkmmvt dvclpisela gaigharqvl
      361 dklglpggit ghvgdgnyhi ilmidmndle evqkakdlne qiveyslarg gtctgehgvg
      421 igkrkyqeke hgdalkimqk ikqvldpnsi lnpnkli
//
LOCUS       WP_010649833             146 aa            linear   BCT 01-JAN-2025
DEFINITION  HIT family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010649833
VERSION     WP_010649833.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..146
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16554
     Region          6..146
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mehkkecvgc alanrlepvy vvyeddyvsc fldhepfneg halilpkrhv veadeldidt
       61 asaimnasil lskalkliyk pdgitiiqng gifnelthyh mhvvpryenq qfgnfysdep
      121 qdfsmgegnl letknmlkea iqklkk
//
LOCUS       WP_010649878             238 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Oceanobacillus massiliensis].
ACCESSION   WP_010649878
VERSION     WP_010649878.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..238
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27633
     Region          1..230
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mdtiifdvdd tlydqalsfk rtchkmfqns ftdeeldkly itsrkysdal fdrnvageit
       61 tkdmhiirik aaceefglti sdeeamefqe syveeqqkit lfdeveemle llyqnnvqla
      121 iltngaeghq smkikqlkle rwvpknnlfi sgaighakpt revfqfienk lkldksktiy
      181 vgdsfdndiv gakqagwqav wmnhrkrelp mnsyipdnvv ysarelmelf ckdylpvk
//
LOCUS       WP_010649926             484 aa            linear   BCT 01-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010649926
VERSION     WP_010649926.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..484
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54479
     Region          50..479
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mkaimdglfn segekvilst fssdytvndi knkvdyyink lqekdlrnkk valivpeiss
       61 ftalvlaank lgaivipisw qyrkedltdi ldyldphvff tidqfngfaf geeilswarn
      121 retetiiyes dsdgewkdys ieglpkplet keigliccss gstgvpkgmv yrpdileaay
      181 ktlpeymglk ptdnviltap ptafygital fygiysgstv iypdtfdllk mvqlmerrnc
      241 nkvvstpsif kaiyqvakel spsvavnlel vhlsgemite eymnqfelme kcsfvgmygs
      301 seggamgycd lrekvvftip kensykimdg elliktptsf vayynnpeln ktysdadgli
      361 ymgdmvtele kgkieivgrk kdmikkggqq iipgeieill tshdkvkqtv vigvahpvyg
      421 eqviafiipn eevdvkdlty yctqhiagyk vpdkiikvee fpvtngkvdk itlrkihres
      481 fqrv
//
LOCUS       WP_010650041             280 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010650041
VERSION     WP_010650041.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..280
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30449
     Region          5..280
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mfmveakrii ivifgallna lslnlfliga nvyasgftga aqilssvfkd figinistgi
       61 lllllnipvl lvgwfkvgkg ftlysivsvf fsslflqfip vvalsndiil navfggvigg
      121 lgvgltlkig astggmdiva milsrlkdkp igiyflvmns viialagily lpenalytll
      181 tlyvstrvid aihtrhekvt amivtlktde lqqaihrkmv rgitilpakg aytkadkslm
      241 ylvitryely dlekiisevd pdaftnivet agvygffrrd
//
LOCUS       WP_010649928             304 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Oceanobacillus massiliensis].
ACCESSION   WP_010649928
VERSION     WP_010649928.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..304
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34057
     Region          181..299
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mkgifhkirq ahatpveett esyepelthl dsyelvkkra lvgwivsrca aalqiverer
       61 ealfylafsn esfeqledgv rkellmlads aadwiaanav ieeemksvnp ghssktvler
      121 vlneiqsdvk fseqlrdesq ktwqvyrdvi yaatqgrfll igkqdvakyk sngllcemdi
      181 rerqdvpkar nvakeafakt gmksskvlsy nliiseavtn ilkhaeygkm liyqnedvfn
      241 iviedkgpgf plailpkatl magfstkesl gqgftlmmkm anqvlletsd kgstlilvle
      301 agke
//
LOCUS       WP_010649949             243 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Oceanobacillus massiliensis].
ACCESSION   WP_010649949
VERSION     WP_010649949.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..243
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25595
     Region          5..241
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msvlngkvvv itgassgige taarmlasmg ahvvigarrv erleslasdi qgaggsvviq
       61 qldvteleqm qaiigaaksr fgkvdaiinn agvmplssle alkidewnrm idvnirgvlh
      121 giasglpvmk kqgfghfini asigayevtp saavycatky avraitdglq qetvglgirv
      181 tlvspgvtes elaesitdnq arefmneyrr nalpataiar aivyaleqpv hvdvselvik
      241 pam
//
LOCUS       WP_010650044             288 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010650044
VERSION     WP_010650044.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..288
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=31580
     Region          1..282
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 msikiladsa sdlskhyynq yniemvpltv hldgkeyedg qtiepktvyd smragkspkt
       61 sqvspqlfka vftkyaeane pllyiafsse lsgtyqtakm melevkesyp dapihiidtk
      121 casigcglva ihaaklahng atleeiiesa eyqaehmehi ftvddleyly rggrvsktaa
      181 fvgtllkikp llhvedgkli plekirgakk vlsrmveime ergtdfqnqt igishgddle
      241 kaellasmis eklgvnkddi vidmvgasvg shagpgtial ffsnkpik
//
LOCUS       WP_010650083             726 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010650083
VERSION     WP_010650083.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..726
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=81133
     Region          1..629
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mrkkenkgrk rttvsrklkl flwmagflii igllgygavl yggnlvvdde dlildaatti
       61 etregeiigk lynenrelvs ieqipdhleq afvaiedrrf ynhegvdlks itravyrdii
      121 amskvegast itqqlsknlf lyndktwtrk ikeamaaiyl ernyskaeil elylneiyfg
      181 eglygvetas nyffskpvee lsisesamla glakapngys aidhpekale rrnivlqame
      241 dagyisaetr kseqektlgl vlqekeptpw tdsyidlvmk eaadkhqlsv dalkkggyri
      301 vvnmdpaiqq iayeqfqndg ffpgstegve gafvmmeegt gnivsaiggr nyqlgdlnrv
      361 tvqrqpgstf kpvavygpam mqeekfnpft llpdqqigey svsnadgeya ntvtiyealm
      421 tskntsavwl leqigidysk eylkrlgmpi edegpaialg glthgvtplq maqsyqsfas
      481 egnvmdssti nqifdrdnqm dyeaeispkq vfnpqvawnm temlaetvts gtatsgeysk
      541 alagktgstq hprvegqtkd awfvgytpey vsalwmgydk sdedhyltgg sayptsltks
      601 ilneidkqtg gslaaefvkp envdalpepi rleqitnlta eyefggfslv kgkltwdgsd
      661 ddrivyriyq dnegidkrig evtgkkeysi snalfrnnry yvvaydpltk meggrsetve
      721 ldwqnr
//
LOCUS       WP_010650087             159 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010650087
VERSION     WP_010650087.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..159
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17976
     Region          63..154
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(84,87)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mgkkmliiig aivvlfialy fvvdyknnqa ldnsenpygs keldqatidq lddplyqnqi
       61 lpeqlsetln ngeeatvyfy spvcvycqnt tpylaplaed mdvdmkkfnl lefgqegtay
      121 niestptlvh yedgeevarl vgqqaeedye affneyvle
//
LOCUS       WP_010650159             292 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Oceanobacillus
            massiliensis].
ACCESSION   WP_010650159
VERSION     WP_010650159.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..292
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32342
     Region          10..290
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mdhsenlkkg ekgawisiia yiflsfikly iaaigssdal radglnnttd viasiavlig
       61 lkisrkppde vhryghyrae tiaslfaafi mmfigvqviy dtfkkvfnqe viqpdmltaw
      121 talgaaciml fvyrynsnla kkvessslna aakdnlsdal vsigvfigii gaqsgiswld
      181 plagmlvgli icktawdifk dstitltdgf deeqlqriqr siskdaevke vldvkgrvhg
      241 nqalieitil vdptlnvees hkiterieyy ldkkhditha hihiepytek qg
//
LOCUS       WP_010650183             274 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Oceanobacillus massiliensis].
ACCESSION   WP_010650183
VERSION     WP_010650183.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..274
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=30823
     Region          113..>267
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mdnnhdnnkd ndiidedlye efedeelyel vqeerrkale raknedefvp krpfhkwafw
       61 lisialafnm fallpqtfsi paidflmtsa klstntdven ykkavvvvet enskgtgfsi
      121 aadgtiltnn hvvegeqyvt vafpedglft aevtktfpei dlavlqvegr elpyltlaeq
      181 aeytkaepir fignplrfng ianegkiigg tklsdwdeev imieapvyrg nsgspiinqe
      241 gkvlgvifat addeeygkvg lfipidlyyk yatk
//
LOCUS       WP_010650245             432 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010650245
VERSION     WP_010650245.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..432
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45144
     Region          7..412
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mktaalgfqh vlamyagail vplivgeslg ltaeqltylv aidilmcgva tilqvvsnry
       61 fgiglpvvlg ctftavgpmi aigvqygisa iygaiivsgv fvvlisgffg klvrffppvv
      121 tgtvvtiigi tlipvainnl gggegapdfg sltnislgfg tllfiilmyr faegfvksis
      181 iliglivgti vaacmgkvdf tavaeasyfh mvqpfyfgsp tfewsaiitm vlvamvslve
      241 stgvyfalsd itekkldekd lskgyraegl aiflggifna fqytafsqnv gllqmtgvks
      301 rkvilvtgam litlgfipki aalttiipta vlggamiamf gmviaqgikm lgkvitnspe
      361 nsmiiacsvg mglgvtvvpe ifaqlpsgiq iltsngivag svtaitlniv fnmtpsrrka
      421 aaelsalrkq ea
//
LOCUS       WP_010650257             249 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010650257
VERSION     WP_010650257.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..249
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27944
     Region          3..245
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mylsvkglak sfgeqkvlkn idvgiekgkv lsiigpsgsg kttllrclna leqpnsgiys
       61 fedgfkldfe qkitkqdilr lrrksgmvfq synlfphkta ienvtegpyi vqkrnkaevk
      121 ehaegllekv glkdklnlyp hqlsggqqqr vgiaralame pelmlfdept saldpelige
      181 vlkvikdlak enwtmvivth elqfaeevsd evlfmdggyi veqghpkevl rapkeertkq
      241 flqrilnpl
//
LOCUS       WP_010650372             223 aa            linear   BCT 01-JAN-2025
DEFINITION  SIMPL domain-containing protein [Oceanobacillus massiliensis].
ACCESSION   WP_010650372
VERSION     WP_010650372.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..223
                     /product="SIMPL domain-containing protein"
                     /note="The SIMPL domain is named for its presence in mouse
                     protein SIMPL (signalling molecule that associates with
                     mouse pelle-like kinase). Bacterial member BP26, from
                     Brucella, was shown to assemble into a channel-like
                     structure, while YggE from E. coli has been associated
                     with resistance to oxidative stress.; The SIMPL domain is
                     named for its presence in mouse protein SIMPL (signalling
                     molecule that associates with mouse pelle-like kinase).
                     Bacterial member BP26, from Brucella, was shown to
                     assemble into a channel-like structure, while YggE from E.
                     coli has been associated with resistance to oxidative
                     stress."
                     /calculated_mol_wt=24609
     Region          15..223
                     /region_name="YggE"
                     /note="Uncharacterized conserved protein YggE, contains
                     kinase-interacting SIMPL domain [Function unknown];
                     COG2968"
                     /db_xref="CDD:442208"
ORIGIN      
        1 myygyyppyw qsrhqalvps pparmltvkg ngrvpvqpdi aiiqlevlte gesvtvaqge
       61 narimdqviq alinlevprd diqttnfain prydfvdgvq vfrgyevrne itvkispiaq
      121 agriidtavq ngvnrvsnir fsvedgkvhy qealslalsn aigkaeaian amqldldrip
      181 vsiiekeqpq pirtfsvaae glstpiepge mivsaevmvk fqy
//
LOCUS       WP_010650377             327 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Oceanobacillus massiliensis].
ACCESSION   WP_010650377
VERSION     WP_010650377.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37397
     Region          5..234
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 meyiidvqnl kksyrkrrsk eyvhavsevs fkvnrgeilg llgpngagkt ttikmicgll
       61 rpdsgsimin ginnkekrlk alrhisavle gnrnlywrlt vkenleyfag nrgisrkdis
      121 ekveefltmf klkdkenelv nrlsrgmqqk laiavamlad sevilldept lgldvetgye
      181 vreilkalvr dynrtiiiss hdmdviqdic ertviinqgr ivtddkvenl iklfdvrays
      241 vtlgeslsrq qeklllqkfp dyefkqdghq ctldidlaks eeiydlfdil kmentpveai
      301 drktinfeqi fmkivkgedq damakss
//
LOCUS       WP_010650404              91 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF485 domain-containing protein [Oceanobacillus massiliensis].
ACCESSION   WP_010650404
VERSION     WP_010650404.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..91
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=11025
     Region          12..87
                     /region_name="DUF485"
                     /note="Protein of unknown function, DUF485; pfam04341"
                     /db_xref="CDD:461268"
ORIGIN      
        1 meehiwrliy ekkrmmtlsl glvflfyfll plsliffpdv mnrisfiqgm swawlygflq
       61 ipmtwmmgwi yhvkaknfdr kveeikqgel l
//
LOCUS       WP_010650425             291 aa            linear   BCT 01-JAN-2025
DEFINITION  glycine betaine ABC transporter substrate-binding protein
            [Oceanobacillus massiliensis].
ACCESSION   WP_010650425
VERSION     WP_010650425.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..291
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32377
     Region          1..290
                     /region_name="ProX"
                     /note="ABC-type proline/glycine betaine transport system,
                     periplasmic component [Amino acid transport and
                     metabolism]; COG2113"
                     /db_xref="CDD:441716"
ORIGIN      
        1 mkkvllgmis alfvmfivgc sqqnvdsksq tgdeeqqtit lgvtpwtstv ppteiaqill
       61 edmgynveqt qadagstyig lsrgdidvfm dgwfpvhdvy iekygdsiee tavsysdada
      121 glvvpsymed vntvediagm edqfnnelyg ieegasvtgi iddliegygl dmeqvnsseg
      181 gmlaqamrkl eneepvvfyg wrphtmfnkl dikviedtkg ffetatvkvi tnkelqetap
      241 dayeflsnws iplddveemi vkieeedvpa revaqewidn nqdkvnemlg k
//
LOCUS       WP_010650461             535 aa            linear   BCT 01-JAN-2025
DEFINITION  multicopper oxidase family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010650461
VERSION     WP_010650461.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..535
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=59750
     Region          61..517
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mkkitiltvi igiiflaacs qqstdsqald nsvegdntsi eesssqevvh vktedtegkk
       61 vnefnliaqv sewnlspenk itawtyngtv pgdeirvkeg evvkvnltne leepvsihwh
      121 gisvpnkqdg ipgvtqdavv pgetytyefv andpgtywyh shqngveqld kglygtiive
      181 saedenydrd ytlmldewes gnhseadase medmegmdmd emdhdsmdme gmdmngtgqd
      241 pmmghdmssy diytingkty eeneplsvke getvklrfvn agymahqiqi pvdykvthld
      301 gqkvnnpqiv ngslfevapg ervdvefiad gsgdftidch gemeasqdmq ldvvyedgng
      361 kktehnsspd liditklgek tesqfsldde ydvsyemdla temnadaemg mvwsingetf
      421 pnvpplevnk gdkvkvtltn nsmdqayhpm hlhghffqvl skngeklegs piikdtlnvk
      481 ygetyevafv adnpgnwlfh chdlhhasng mvttvnynnf eefyndtgev dnqpe
//
LOCUS       WP_010650475             212 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Vibrio campbellii].
ACCESSION   WP_010650475
VERSION     WP_010650475.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10606006
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..212
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24855
     Region          62..193
                     /region_name="Methyltransf_23"
                     /note="Methyltransferase domain; pfam13489"
                     /db_xref="CDD:404385"
ORIGIN      
        1 mhtcplcknq rthhffedkq rdylqceqcs lvfvnpdqrl daetekahyd lhennpedmg
       61 yrrflariad piserispqs ngidfgcgpg ptlslmleea ghnmalydly yhpdtcvlek
      121 qydfmtatev iehlyhpdlv wkqwlnlvkp ggwiglmtkm vidveafrtw hykndpthvv
      181 ffsrdtfqfl aerdklelef igndvillrk tq
//
LOCUS       WP_010650604             362 aa            linear   BCT 01-JAN-2025
DEFINITION  type III polyketide synthase [Oceanobacillus massiliensis].
ACCESSION   WP_010650604
VERSION     WP_010650604.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..362
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40253
     Region          1..360
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 mtnicsigrg ipeytieqae ikeivqdifs ysdkqikrll pvfdnaaver rqfvvdkswf
       61 veehsfkern diyqkaaeky alaaiddclq npdflnsapp yeaidmiifv sstgistpsm
      121 dvhlmnarpf rqdvnrmplw glgcaggaig larahdwita hptktaliic celcsltfqk
      181 gdskksnmvg talfgdgvsa alavgddspy lsyrkksvps itsassylkr dsvdvmgwdi
      241 nnsgfevvfk ksipalvdsf wrkhvdtffh dsglsvdqih sfishpggrk vmeameevvh
      301 cpkdklkysy nvladhgnms satvlyvmre wmlqnikage ksilsalgpg fssellllew
      361 ne
//
LOCUS       WP_010650633             204 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Vibrio campbellii].
ACCESSION   WP_010650633
VERSION     WP_010650633.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..204
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22445
     Region          79..184
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(86..87,120..121,124,128..129,132,174,178)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mkatkillal gvmlathhvt aedkyeytet pkaeqiadlq dddndgvina rdlcpgtpat
       61 seidndgcge yikssekmev rvlfandsde iapvfrrqir elseflkeyp stsielqgya
      121 skvggsehnl dlskrrannv raallgygie sdrvrivgfg dthlaeqgtd evshalnrrv
      181 tasvigykge ikkewtifta lpks
//
LOCUS       WP_010650644             268 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Vibrio campbellii].
ACCESSION   WP_010650644
VERSION     WP_010650644.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..268
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29264
     Region          4..264
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,195,217..219,221..222)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 myklialdmd gtllnsekvi seenkqaiak areagvtvvl asgrplegmq dkldelnids
       61 dkdfvlyyng smvknigtne iihqqiidgk aakkiarkar elgayvhafs qehglitedn
      121 npytdieaki ngleitemnf daleddhgii kammvaepsk lteviaalpa elkeeftvvq
      181 sapfflefln pssnkgigvs aiaeylgiea eevicmgdae ndhhmleyag lgiamaname
      241 etkrianyia esnddhgvak siekfvls
//
LOCUS       WP_010650649             480 aa            linear   BCT 01-JAN-2025
DEFINITION  bifunctional NUDIX hydrolase/phosphatase PAP2 family protein
            [Vibrio campbellii].
ACCESSION   WP_010650649
VERSION     WP_010650649.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Stukey,J. and Carman,G.M.
  TITLE     Identification of a novel phosphatase sequence motif
  JOURNAL   Protein Sci 6 (2), 469-472 (1997)
   PUBMED   9041652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120911
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..480
                     /product="bifunctional NUDIX hydrolase/phosphatase PAP2
                     family protein"
                     /EC_number="3.1.3.-"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=53486
     Region          33..108
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cd02883"
                     /db_xref="CDD:467528"
     Region          243..351
                     /region_name="PAP2_like"
                     /note="PAP2_like proteins, a super-family of histidine
                     phosphatases and vanadium haloperoxidases, includes type 2
                     phosphatidic acid phosphatase or lipid phosphate
                     phosphatase (LPP), Glucose-6-phosphatase,
                     Phosphatidylglycerophosphatase B and bacterial acid...;
                     cd01610"
                     /db_xref="CDD:238813"
     Site            order(258,265,285..287,325,331,335)
                     /site_type="active"
                     /db_xref="CDD:238813"
ORIGIN      
        1 mlrqlfflil ysislfispt saanplpedi kgalcvvrad dklvliheil tnkislpggt
       61 iiegespklg aqretweetg lvvtvgdelg rtdtavffdc vsdseviafs rtnsldgnel
      121 piwfaphygv evasamlvep snmaaslyry ptqwadvagf yshatdqpvv yvdqliesap
      181 sfrqaelswm vdlqsrvgsf sessremaca vadmitglss ptfllflfpf vmmkfdshfv
      241 yrlffavtat slmalvaqqg fslprphvym pmaeltqsfg fsfpslpiav wfcvmtflfq
      301 rtnsfglnri tlsgalvtlt vmackfflgt afildmfiga vlgvlvawhv lrlesnpnvd
      361 vdkllssksv wftmtaitav isviwplpvf tnwlailita salvmtfkes eirferqqml
      421 fvilalllve qlylylgttv sfsgfwslvf ntfhypllmi ifvilsrkli teseidvakq
//
LOCUS       WP_010650742             310 aa            linear   BCT 01-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010650742
VERSION     WP_010650742.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..310
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34585
     Region          18..259
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrlfllliil llfnlgfpti gqaapsvsan nailieqstg rvlfeknand qasiasitki
       61 mtaiiaiesg kmeemaeasr eaiytegssi yleqgermkl edlvyglmlr sgndaavaia
      121 ehvggsedgf iflmnekakw lgmtnshfdn phgldsdthy ssaydmgllm ryamendlfk
      181 kitasetyks enrsyswqnk nklltqfyey ctggktgytk ktgrtlvsta ekdgveliav
      241 tldapddwqd hmsmfewgfd nyqmeslsne gpsdyivnnn qtipgyigeq isyplteeeq
      301 lslnkkiill
//
LOCUS       WP_010650872             191 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Vibrio campbellii].
ACCESSION   WP_010650872
VERSION     WP_010650872.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..191
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21469
     Region          1..163
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 myilvvsssl dpnsrsrqia klcidelqsl drqvkfvdla eldvpnfdnd kiyhteqyka
       61 lhkltseasg ivlcspiynw gccselkkyi eyvgstppdg sltgalfdkv vtfvtsaglp
      121 hsymadsals tslsidfkcv inpynlyvhn rhwdndtlsd erlprleksm kvmdelcsll
      181 sartyksgwe l
//
LOCUS       WP_010650891             423 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Oceanobacillus massiliensis].
ACCESSION   WP_010650891
VERSION     WP_010650891.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12081071
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..423
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48155
     Region          61..341
                     /region_name="MFS_1"
                     /note="Major Facilitator Superfamily; pfam07690"
                     /db_xref="CDD:429598"
ORIGIN      
        1 mqklldfyrs kmesnrdllv llligglysg giflsntfvn iylwkqssdf vtiaiynfsi
       61 sifqtvafvf agrltkkidr ivvlrlgvff lslfflsvli igehaaefnf mlgsmlgigy
      121 afywlafnvl tfevtepdtr dffngflgil qslggmtgpl fagfiiakmt dnigytvifa
      181 isfflfacav gasfllkrrg aegvfhfrri leernhnrnw krilhahffq glregifafv
      241 isiwvflvte selalgtfnm flsglsvify miatkfikpa mrkkailfgg lllyfsifii
      301 lfeinyfllm vyavvigiay plitvpyvsl tfdvigkawk agemrveyiv vrelflnigr
      361 vlsiliflag vkffvaedvi plvltvlggg himiyffvrn iylgsskrke ilmkdqitde
      421 knr
//
LOCUS       WP_010650936             148 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Oceanobacillus massiliensis].
ACCESSION   WP_010650936
VERSION     WP_010650936.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..148
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16648
     Region          1..148
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mtlldrlnqd mkqamknkdk etlsvirmvk asiqnesikl gkdelseded ltilsrevkq
       61 rkdslqefks agredlaekl enelvileky lpeqlsdeel mliiqstiqe vnaasmkdmg
      121 kvmgavmpkv kgkadgsqik kavqqqlq
//
LOCUS       WP_010651063             240 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010651063
VERSION     WP_010651063.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..240
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26515
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mirveklnks fgklhvlkdi dltvnesdvv vligasgsgk stllrclnfl eiknsgkimi
       61 egnqvepkth dlnkvrqkvg mvfqhfnlfp hktvmgnvie apiqvkgikk sqaikeakvl
      121 ldkvglgdkh dvypsklsgg qkqrvaiara lamkpevmlf deptsaldpe lvnevlftmk
      181 glaeegmtmv ivthemgfar evgdkvvymn dgkiveagep eaifnhpkeq rtqdflrsil
//
LOCUS       WP_010651209             217 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Oceanobacillus massiliensis].
ACCESSION   WP_010651209
VERSION     WP_010651209.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10136841
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..217
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24995
     Region          41..>118
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mehvktyhsl tyktelgpiv iegplhsnel kqyhfheklt afrpaekqfe allsiadfpe
       61 grilvartas tivgyvtylh pdplerwsef nmddllelga ieiipdfrga gvasnllkvs
      121 mldrymenyi visteyywhw dldgtklsiw nyrkvmekmm atggllpapt ddpeiishpa
      181 nclmvrigkn vseesiekfd klrflarnky rnmregl
//
LOCUS       WP_010651224             105 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010651224
VERSION     WP_010651224.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..105
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12104
     Region          8..101
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(28,31)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkhlesveqf nelkdneqvi fifsagwcpd crviepvlpe iedaypqyqf vevnrdefie
       61 vcqehdifgi psflaftdgk eagrfvskdr ktkeeieqfi dglta
//
LOCUS       WP_010651272             304 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Oceanobacillus massiliensis].
ACCESSION   WP_010651272
VERSION     WP_010651272.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..304
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34248
     Region          1..303
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mssfndqfiy siviiaagyi lkkmhvikee dgeglariif nitlpalilv tfndfvmeys
       61 lfllviisfa ygllaamlgv llfkgnpsrh akgmlsmmvp gfniglfafp lvegiwgreg
      121 iqhfvmfdvg nsfivfgicy figshyagee trldiktmll kmtrsiplmt yivvlmlnls
      181 glklpsfive tadiisyanm plsllllgiy lnftiekkyl rllfhymamk yglgifagfa
      241 lffllpfddm fnytvligli lpaamsvlpy avefnydkrf igtvsnltii tsfmliwiia
      301 nfmi
//
LOCUS       WP_010651237             377 aa            linear   BCT 01-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Oceanobacillus massiliensis].
ACCESSION   WP_010651237
VERSION     WP_010651237.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..377
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41420
     Region          1..377
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,85,161,165,184..185,187..189,208..210,214,
                     229,253..255,279,296..298,321..323,363)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,59,161)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(89..90,92,95,103)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mkavtyqgky kvevksvkap siqdpqdvii kitstaicgs dlhlyqgnfp lpinyvighe
       61 pmgiveeigp evtkvkkgdr vvipftvacg tckyckghld sqcdnsnphy dsggylgyse
      121 kfgdypggqa eylrvpfgny tpflipedce ledekllfls dvlptaywsv enagvkqgdt
      181 vivlgcgpig lmaqkfawqk gaerviavdy fgyrlnhaks vnrtevydft qyddmgetlk
      241 eitkggadvv idcvgmdgkk splefveqkl klqggtlgpi qistkavkkg givqitgvyg
      301 gnynlfplga ffsrnitlkt gqaparsymk elyeqivagk idptdiithr lpldkaehay
      361 difngrkddc vkvilkp
//
LOCUS       WP_010651357             199 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Oceanobacillus massiliensis].
ACCESSION   WP_010651357
VERSION     WP_010651357.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..199
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22036
     Region          10..188
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mdvdirelet keayklmtgs viprpiawvs tananggfnl apfsfftvas rkppmlcisi
       61 gpgvgeregt vkdtlvnire kqefcinivs selgnpmqks senvgsdvde fqlaglktap
      121 skkidtprik eapiafelkl hqilelgtdh liigeiihyh ikedyylgny kvdieklkpl
      181 grfaggryse ltelftlpk
//
LOCUS       WP_010651303             254 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Oceanobacillus massiliensis].
ACCESSION   WP_010651303
VERSION     WP_010651303.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..254
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28076
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mlqvkqvski yegkiayral tdidltiedg efvgimgpsg sgkttllnmi atidepttgq
       61 ilidgsnphq lrkddlakfr rrelgfvfqd fnllhtltve enivlpltld gkkvkvmkqk
      121 vqeiaaklgi adilkkrtye isggqaqrva varamihspk lvladeptgn ldsksskdvm
      181 gmlesinkke datmmlvthd pqaasycnrv vfirdgkfys eihrgdnrqa ffqkiidtls
      241 llggdgndls qvrv
//
LOCUS       WP_010651361             219 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Oceanobacillus
            massiliensis].
ACCESSION   WP_010651361
VERSION     WP_010651361.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..219
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25401
     Region          3..212
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtayqiikda iitgkyqqgk rlteeelaeq lhvsrtpire aikqlesegl iipfrkrgvi
       61 vreftetdir qiynlralle syatgeaaiq rneeeifqme qgnhdyeqai rllnnptlgd
      121 iesiqqknqs fhskvfaaah nehvmnhier vvvvplifra fywysekqli qsieahktil
      181 qaikdresdr akaamhehiy lgrdhvlkhi gekkltaef
//
LOCUS       WP_010651368             395 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Oceanobacillus
            massiliensis].
ACCESSION   WP_010651368
VERSION     WP_010651368.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..395
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43863
     Region          1..389
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(100..102,126,176,207,235,237..238,246)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(103,136,200,244..246,275,278)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            238
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mtnisnrisq ipfssireif eeatamemng daithmeigr pdfdtpdhik eaaikalkdg
       61 hvhytpnrgi qelteaiadk lkkenhvtin pedgvvvsvg ckeaitntif afinpgdevl
      121 vpdpswleyq yivrlaggip ipmtlkeeeg fllniddirn klspktkmmi insphnptgs
      181 vlpeenlrei aqvamdhdll vlsdeiyekl iyddarhvsi aslpgmfert iiingfskay
      241 amdgwrlgya agprsliqsi lkmhqyntss atsfaqygav eayngtqepv gemvrafdlr
      301 rkllidrlsa mpnvscvvpk gafyvfpsfr ginmtskdla kkilreahia cvpgsafgna
      361 gegyirmays sgyeqieqam drlekvmkdi fskav
//
LOCUS       WP_010651369             271 aa            linear   BCT 01-JAN-2025
DEFINITION  ZIP family metal transporter [Oceanobacillus massiliensis].
ACCESSION   WP_010651369
VERSION     WP_010651369.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..271
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28369
     Region          8..269
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 midfflsldp viqagiatmf twgmtalgaa vvfatkefnq klmdsmlgfa ggvmiaasfw
       61 sllspalema eagptpawvp aavgfalggi flwgidkvip hlhptspved aegirhdkkk
      121 rstllvfait lhnipeglav gvafgalaad sttasitgav ilaigmgiqn vpeglavamp
      181 lrrdgmtrrr sfmygqfsgm ielfagviga lavayidpil pyalsfaaga mifvvteevi
      241 pgsqeegnkd lasmslmigf tvmmildval g
//
LOCUS       WP_010651372             137 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Oceanobacillus massiliensis].
ACCESSION   WP_010651372
VERSION     WP_010651372.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 137)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..137
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15273
     Region          8..121
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mtvpkhivsa aaivindene illikgprrg wempvgqvee geslteaair etkeesgidi
       61 eiirfcgvfq nvtssicntl flgkpvggee rtspeslevg yfpieealem vtlknfrqri
      121 eyclnresqp flvefka
//
LOCUS       WP_010651489             303 aa            linear   BCT 01-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Oceanobacillus massiliensis].
ACCESSION   WP_010651489
VERSION     WP_010651489.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..303
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=34777
     Region          26..101
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(37..38,40..41,43..44,47..48,50,57..64,66)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          90..298
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mankkysnyr keakslkyev kepeelltfl lkvmsnrsrn svksilargq vtiddhietk
       61 ynynlrpgqt vtilknkaai kenvligmsi lyededvivi nkeagllsia tekekkqtal
      121 hqlmeyvrre dpenrvfvvh rldkdtsgvm mfakseqvkr kmqdnwkdiv kertyvalve
      181 gkvvkekgyi sswlkeskth lmyssptknd gmhaithyqv iqaneefsll evqletgrkn
      241 qirvhmqdlg hpvvgdkkyg skqrnaigrl glhakvlsfn hpttdqlllf kadvpqsfls
      301 ksk
//
LOCUS       WP_010651492             561 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Oceanobacillus massiliensis].
ACCESSION   WP_010651492
VERSION     WP_010651492.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..561
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=62169
     Region          1..560
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 myrlfnrfls katlrsrlli lfitlivisi vsvgtasyiq aknitmntie drlaretqlm
       61 gyiaenlhfl yvsdphyfmq qlnasirtqq eeletdgiks qffyisdnva npftvsadtl
      121 ppisdslita iteegngqik reiegeryti sfqqmeeigg iytllvpdss fmepviemgy
      181 silsiiaasv listilltlf vqtltkpltf lrntmrgvre gnlqqtpapn ttlpefvslh
      241 ksydamigqm rtmldelkrt tselhhtged lqhssnsalq sshdliesin vvkagaeqta
      301 sssedsvsss iamknkteim agnmdhvfan aermqlsaln geknikklit sfqsfetdfy
      361 qldkivqkvn ddaisisklv gliqgiakqt kllslnasie aaragasgkg fsvvanevgk
      421 laeqssaaad qitssisnme eitdhattef rqmllktssn leianeskas fdhlmkeiae
      481 ttnnlkgtek elrelkkelp klelsaedfa sisqetlast eemltssehq yqqtedthdi
      541 glklmtlsns lstitkqfki k
//
LOCUS       WP_010651494             391 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter permease [Oceanobacillus massiliensis].
ACCESSION   WP_010651494
VERSION     WP_010651494.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..391
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=42700
     Region          5..391
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mkkenssvat pfwrdkrivp illqllfvia lifsiyflls ntlsglnqlg mqigfdflsn
       61 tsgftisesi lnfqstdtyg kailvgilnt lkvaffgiil atiigiiigi arlsknwlvs
      121 klafgyveif rntpllvqmf iwyfavflpm pqiedalkvg pfyltnrgta ipwfeansns
      181 llwgiiaaag iilaiisykl lmkkevesgk rrypiisafg iliialgaaf ittqsgpfqv
      241 iapsiegksf iggntlspgf savllglviy tstfiaeiir agimgvsngq keatkalglk
      301 sstslrlvvf pqairiiipp ltsqylnltk nsslavaigy qdivsvgnti mnqtgraiea
      361 iiimiavylt islltslfmn ifnkrmqlve r
//
LOCUS       WP_010651604             119 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Oceanobacillus massiliensis].
ACCESSION   WP_010651604
VERSION     WP_010651604.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..119
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14118
     Region          42..107
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mpkrpdtpck hprcaklvpy gasyceehap lhihdvkstk ekgydsrwrk arkrflkshp
       61 lcekcfdkgk lekakvvdhi iphrgdqelf wnetnwqplc kpchdrktmt vdryqefky
//
LOCUS       WP_010651662             236 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Oceanobacillus massiliensis].
ACCESSION   WP_010651662
VERSION     WP_010651662.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..236
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=26170
     Region          7..236
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mkpligitas metdksnylv anrnvkaiqa aggipiilpy flrteeikei tnridglyat
       61 ggydidpilf geephpglgn iiperdqsel avikemleke kpilgvcrgs qilnvaaggd
      121 myqdintqin tellqhsqka pfdyrshfvd vaegsllhrl tgkhklrvns fhhqanrsvh
      181 egfrisgtas dgiieaiese ihpfvlglqw hpealiheed dpslqiyqgf ikacqq
//
LOCUS       WP_010651747             120 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin
            [Oceanobacillus massiliensis].
ACCESSION   WP_010651747
VERSION     WP_010651747.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..120
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=13279
     Region          2..113
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mivqrgevyf adlspvvgse qggvrpvlil qndignrfsp tvivaaitaq iqkaklpthv
       61 eidakrygfd rnsvilleqi rtldkqrltd kitkldkemm dkinqaleis lglkdvysgn
//
LOCUS       WP_010651808             388 aa            linear   BCT 01-JAN-2025
DEFINITION  M20 family metallopeptidase [Oceanobacillus massiliensis].
ACCESSION   WP_010651808
VERSION     WP_010651808.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10145376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..388
                     /product="M20 family metallopeptidase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41770
     Region          9..366
                     /region_name="M20_ACY1L2-like"
                     /note="M20 Peptidase aminoacylase 1-like protein 2-like,
                     amidohydrolase subfamily; cd05672"
                     /db_xref="CDD:349921"
ORIGIN      
        1 mknlldkeie kiiqslwdms dhlyenpelg nqeyqsmqll adflkehdfv vetgtvdlpt
       61 afkaeynsgk pgpriaylae ydalpgvghg cghnligtms tgagvalskl vnetggsivv
      121 lgtpaeetng akvamseqgt fsdidaamiv hpgdvsyesg eslamdaiqf sysgksahaa
      181 aspekginal dsviqlfngi nalrqhvtsd vrihgvipeg gqaanvvpdk aiaqfyvrak
      241 nrsyldevvr kvkqiaegaa lmtgasleis nyelsydnmi tnealskkft enlkktssyp
      301 vlpakdsygs idmgnvsqvv paihpyigmn kpgliphtke fadqtitgdg hqalrdgals
      361 lamtgydilt dadllrtiqe efeinrmk
//
LOCUS       WP_010651814             325 aa            linear   BCT 01-JAN-2025
DEFINITION  ring-cleaving dioxygenase [Oceanobacillus massiliensis].
ACCESSION   WP_010651814
VERSION     WP_010651814.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10327061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..325
                     /product="ring-cleaving dioxygenase"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36189
     Region          5..129
                     /region_name="VOC"
                     /note="vicinal oxygen chelate (VOC) family; cl14632"
                     /db_xref="CDD:472697"
     Region          156..319
                     /region_name="PcpA_C_like"
                     /note="C-terminal domain of Sphingobium chlorophenolicum
                     2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and
                     similar proteins; cd08347"
                     /db_xref="CDD:319935"
ORIGIN      
        1 meikgihhvs aitadakkny qfytevlgmr lvkktvnqdd tsvyhlfyad ekgnpgtdlt
       61 ffeipnagnt ypgtgsisat slrvpndaal eywnsrltey evdhdgisiq gerkvihfrd
      121 hekqrlllis denntgvpgg kvwdqspvpa dkgiiglgps rltvrnpdpt veiltklltl
      181 kqvgsypsni dgqpdiivfs tgaggtgaei hlearkdlpq erpgrgsvhh vafrvedkee
      241 ltkwknrled iqlpnsgmve ryyfkslyfr dpngilfela tdgpgfatde dfdhlgesla
      301 lppyiesqrt kiesklrpld tkssh
//
LOCUS       WP_010651837             238 aa            linear   BCT 01-JAN-2025
DEFINITION  DsbA family oxidoreductase [Oceanobacillus massiliensis].
ACCESSION   WP_010651837
VERSION     WP_010651837.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..238
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27145
     Region          3..204
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(11,14)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mkievwsdfv cpfcyigkrr lekameqfsh rdqvtvqfks yqldptakhi pgkdfyetfs
       61 elkgmpldqv kamnrqvaqq aagvglkynf ddmkyantfd ahrvakyade qgkgkevter
      121 flhahftesq llsdretlvk laeevglnpa evdnvvnsdk yrnrvnedid vahqigvqgv
      181 pffvfnekya vsgaqpvevf sevlekvwee ekekpvlksl npkksetsyc tdegcdvn
//
LOCUS       WP_010651872             315 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Oceanobacillus massiliensis].
ACCESSION   WP_010651872
VERSION     WP_010651872.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870074
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..315
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35487
     Region          12..230
                     /region_name="ST1585-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Sulfolobus
                     tokodaii ST1585 protein; MBL-fold metallo hydrolase
                     domain; cd07726"
                     /db_xref="CDD:293812"
     Site            order(72,74,76..77,161..162,180,230)
                     /site_type="active"
                     /db_xref="CDD:293812"
ORIGIN      
        1 mrekdpirld nrihlidgfd ldvshrtgty vineeqltlv etgpspsvky iksglaalgh
       61 sldevryiiv thihldhsgg aglllkdcpn ativvhsrgk rhladpkkla sgaraiyges
      121 fselfdpiip vpedrivvkg egdtlqigpe ctlefwdtpg hakhhlsifd pisnglftgd
      181 tvgvryqqlq qngidfflps tspnhfnpne measikrire kdldriyygh fgmtenteea
      241 lnqvskwldv ymdvgeqavl egrgydtisq rllerirqhl rekgiedehe vyilinldlq
      301 vgslgiidyf kklkq
//
LOCUS       WP_010651896             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Oceanobacillus
            massiliensis].
ACCESSION   WP_010651896
VERSION     WP_010651896.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..245
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28621
     Region          1..103
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(49,52,56..57,66,78,82,88,92,95..96)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          128..240
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mkvkevadla gvsvrtlhhy deigllspke reesgyrvyt htdleklqqi lffkelgfpl
       61 kkikeiinds sfnqkealen hykllldkrr ridsligtve ktiqykkgei vmtdeerfag
      121 fdfsenpyeq eardlwgekt vndsnakigg mskqqqqelg eefneiyrkl aeirheapds
      181 edaqkrieew ydylnkigdy sldafkglgq myvdderftk nidkfgegla vfmrdamayy
      241 sdmhq
//
LOCUS       WP_010651899             516 aa            linear   BCT 01-JAN-2025
DEFINITION  BCCT family transporter [Oceanobacillus massiliensis].
ACCESSION   WP_010651899
VERSION     WP_010651899.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..516
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56714
     Region          3..480
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mdskkkkeid wpvfiisggf llafiflsli nnekvgevvn tlfayssdlf gaywqlllla
       61 nffiglglai skygkvrlgk qdkpkysyfg wvsmilvtll asggvfwaaa epmyhymdtp
      121 plfgggqfnn msaafaqafm hwgftawail gtlsvivmmy vhynrglplk prgllypmfg
      181 ekiyhksvig stadifsiia tvagtlgplg flglqisygl nhlfdvpntl avsiivvmvl
      241 vliaaisaat gvdrgiyhls nwnvkftill aaivlvigpt tfiidafvgg tgahlqnfft
      301 msmfrgdegw lslwtiffwg wfigyapmli vfisrisrgr tireliiavs iiapivnnfw
      361 fsivggtgvf fennnpgsis nalneggmpa avmaitdqlp mgtlmgmgfl lvsiifvatt
      421 tdtmaytvaa tlsgndhpkr wlrvfwalif gattmvilti gedsitsiqn sivitavpvs
      481 llllpplwha priakkmale qgliwqremm kkqdrk
//
LOCUS       WP_010651905             398 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Oceanobacillus
            massiliensis].
ACCESSION   WP_010651905
VERSION     WP_010651905.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..398
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=45351
     Region          7..395
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mtqiielivk hdfvrqyknk yplinkesiv npdalsrega ivhlhddhht flakgyygeq
       61 nkglgwvlsf degekidgvf fknkiltain krqsfykdes ttafrifnge gdgiggltid
      121 yfdgyylinw ysegiysfke kvitvldelg dykaiyekkr fdskgqyidd ddfvkgvrge
      181 fpiiikengm nyavylndga mvgifldqrd vrqairdqya kgkhvlntfs ytgafsiaas
      241 lggaskttsv dlakrskskt ieqfsingid feqqdiivmd vfdyfkyakr kdlkfdliil
      301 dppsfarskk htfstaknyp dlikdslail ekngvivast nnasfgmkkf kgfiekgfrt
      361 mnmkfnilde falpadfqad rnfkqgnylk vvivqkvn
//
LOCUS       WP_010651910             120 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Oceanobacillus
            massiliensis].
ACCESSION   WP_010651910
VERSION     WP_010651910.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..120
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13452
     Region          12..107
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 msnaqehmdk lmqelrrgti tigvlsqlse pqygyslvtt lsekgiqvep gtlypllrrl
       61 ekqglleskw dtnesrprky yllsktghdv fglliaewks maqsldqlig eegsdhsgnd
//
LOCUS       WP_010651917             253 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Oceanobacillus massiliensis].
ACCESSION   WP_010651917
VERSION     WP_010651917.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..253
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27421
     Region          1..246
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 msfltlslsl ifvlipials kalnlglekd tiiatvrsii qllavgyvlt fvftadhymy
       61 iilmimlmig aatqnarkkg asikgitwkl vgtfffveil tqaillgfqi tppiaqyiip
      121 isgmvvgnsm vlsilflnrf taeiasrqde telilslggt pkqaihtsli tsikasmipt
      181 iesqktiglv qlpgmmsgqi iagadpvqav qfqllilfll lttaavtsvl lgflsyptlf
      241 nkqmqllkls ekn
//
LOCUS       WP_010651920             198 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Oceanobacillus massiliensis].
ACCESSION   WP_010651920
VERSION     WP_010651920.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..198
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21991
     Region          10..198
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mkhifkkgkd qsrptllllh gtggteqdll qlaeiidkea nilsvrgnvl engmprffkr
       61 laegvfdedd lifrtkelne fldeaamkye fdrsnitavg ysnganiaas llfhykdaln
      121 kailhhpmvp rrgiemtdlt gkavfiaagt ndpicpaqes eeltsllkna gadvelhwen
      181 rghqltidev qaaaawyk
//
LOCUS       WP_010651934             265 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF4097 family beta strand repeat-containing protein
            [Oceanobacillus massiliensis].
ACCESSION   WP_010651934
VERSION     WP_010651934.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..265
                     /product="DUF4097 family beta strand repeat-containing
                     protein"
                     /calculated_mol_wt=29049
     Region          <125..263
                     /region_name="YvlB"
                     /note="Uncharacterized conserved protein YvlB, contains
                     DUF4097 and DUF4098 domains [Function unknown]; COG3595"
                     /db_xref="CDD:442814"
ORIGIN      
        1 mfnlkkvslv alillvvglv gslltfhsvs stqveteeti kdqfqqidis tdnarveilp
       61 adsnvatvkf sgndednrky dfntnvegdt lrinvkergf rffsfdfsfs tpslkvyipe
      121 kmyqtvnves nngritaigl qsddisaktn ngkiefnnvv ssamraetdn geirlenieg
      181 evsgrtnngg islitdridr pinfetdngr iaihtekepv nttldiktdn gkvtvfgdsn
      241 wdavagngen kvklttnngs itign
//
LOCUS       WP_010651941             251 aa            linear   BCT 01-JAN-2025
DEFINITION  GTP cyclohydrolase II [Oceanobacillus massiliensis].
ACCESSION   WP_010651941
VERSION     WP_010651941.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Ren,J., Kotaka,M., Lockyer,M., Lamb,H.K., Hawkins,A.R. and
            Stammers,D.K.
  TITLE     GTP cyclohydrolase II structure and mechanism
  JOURNAL   J Biol Chem 280 (44), 36912-36919 (2005)
   PUBMED   16115872
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Ritz,H., Schramek,N., Bracher,A., Herz,S., Eisenreich,W.,
            Richter,G. and Bacher,A.
  TITLE     Biosynthesis of riboflavin: studies on the mechanism of GTP
            cyclohydrolase II
  JOURNAL   J Biol Chem 276 (25), 22273-22277 (2001)
   PUBMED   11301327
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10089835
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..251
                     /product="GTP cyclohydrolase II"
                     /EC_number="3.5.4.25"
                     /GO_function="GO:0003935 - GTP cyclohydrolase II activity
                     [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009231 - riboflavin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28453
     Region          82..242
                     /region_name="GTP_cyclohydro2"
                     /note="GTP cyclohydrolase II (RibA). GTP cyclohydrolase II
                     catalyzes the conversion of GTP to
                     2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'
                     phosphate, formate, pyrophosphate (APy), and GMP in the
                     biosynthetic pathway of riboflavin. Riboflavin is the...;
                     cd00641"
                     /db_xref="CDD:238348"
     Site            order(97..102,104,113,115,118,140..143,150,154,157,163,
                     175,177,198..200,203)
                     /site_type="active"
                     /db_xref="CDD:238348"
ORIGIN      
        1 meqmkleskv fsilkdkiql irsddraiyl vgpiqlpvnl ygetvifqwy cwlnydevte
       61 dyekiiekls ssnlaeyqqs svlvygdfke addalirmhs ichtgdifgs krcdcgfqlk
      121 esmkkikehg tgalfylanh egrgiglfsk amayvlqeng ydtveanesl gfvndsrdys
      181 daievlktlr tkpvtlitnn pkklealdns gtlvsgrtpl wgdvseynqk ylqtkvvksg
      241 hmqeertcdn d
//
LOCUS       WP_010651999             352 aa            linear   BCT 01-JAN-2025
DEFINITION  Mrp/NBP35 family ATP-binding protein [Oceanobacillus massiliensis].
ACCESSION   WP_010651999
VERSION     WP_010651999.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Vitale,G., Fabre,E. and Hurt,E.C.
  TITLE     NBP35 encodes an essential and evolutionary conserved protein in
            Saccharomyces cerevisiae with homology to a superfamily of
            bacterial ATPases
  JOURNAL   Gene 178 (1-2), 97-106 (1996)
   PUBMED   8921898
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..352
                     /product="Mrp/NBP35 family ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0140663 - ATP-dependent FeS chaperone
                     activity [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=38458
     Region          108..347
                     /region_name="ParA"
                     /note="NUBPL iron-transfer P-loop NTPase; pfam10609"
                     /db_xref="CDD:431392"
     Site            order(117..124,249,251,276..277,313..314)
                     /site_type="active"
                     /db_xref="CDD:349757"
     Site            order(117..119,148..149,151,154..155,195..196,226,228,231,
                     255,258,314)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349757"
ORIGIN      
        1 mltkeevvql lnpvkdpflh itlketggit nvsikedkkh vsvkigiskt ntaeqmqlqq
       61 eivgilkrng antvglrfeq lpeeviqkyq paaeeaqvss lmggnsntkf iavasgkggv
      121 gkstvtvnla vslmrlgkkv giidadiygf svpdmmgveq rpavrgqkii pverfgvkvi
      181 smgffvedns piiwrgpmlg kminsffsev ewgdldylll dlppgtgdia mdihellptc
      241 keiivttphp taafvaarag qmalktehei lgvvenmayf eskktgekef vfgegggtkl
      301 aevlqtkvlg qlpiqqpyee edvfapsvyq edhpngkefh riaakiiakl ee
//
LOCUS       WP_010652052             119 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Bacillaceae].
ACCESSION   WP_010652052
VERSION     WP_010652052.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..119
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=13300
     Region          26..118
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 meilqwiffi iiiafvvnff lptkgvsnit akeakdkfae kdvqfvdvrt pgeykanhqk
       61 kfanvplahl skrtgeldkn kevvvicqsg mrsakaakml kkqgfekisn vkggmnawv
//
LOCUS       WP_010652017              75 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Oceanobacillus
            massiliensis].
ACCESSION   WP_010652017
VERSION     WP_010652017.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..75
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8619
     Region          5..70
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 msnvkvlsnr irvfraerkm tqkelaekvg vsrqtiiste kgnytpslil afdianifnv
       61 rvdevfqyek treel
//
LOCUS       WP_010652053             260 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Bacillaceae].
ACCESSION   WP_010652053
VERSION     WP_010652053.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..260
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27131
     Region          5..260
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 meyslmfilv lfligfggsf lsgmvgiggs ivkypmllyi ppllglsaft ahevsgisav
       61 qvlfatiggv wayrkggyln ktliiymgis illgsfiggy gsqfmtdggi nfvygvmati
      121 aavmmfvpkk giddtpldqv tfnkwlaaff afvtgigagi vgaagafllv pimllvlkip
      181 trvtiassla itflsavgst agkimtgqvl lipavimiia sliasplgan agkrvntrvl
      241 qgilavlila tavkiwsdff
//
LOCUS       WP_010652058              99 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Bacillaceae].
ACCESSION   WP_010652058
VERSION     WP_010652058.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..99
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11024
     Region          1..95
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mksvktnkle eriknksdvn vidvreddev aqgkitgakh iplgeisdri neidknkhyy
       61 mvcrsggrss kaceilmnqg fdvtnvdggm lawtekvek
//
LOCUS       WP_010652228             542 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Fluoribacter dumoffii].
ACCESSION   WP_010652228
VERSION     WP_010652228.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..542
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60762
     Region          193..532
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mmlinkmqat fsscmpgyff rpklvrttlf fliflfgikg wslpnpdeaq vkqaeerlqk
       61 aienpefmlh nwielptspa artkavhhlg lrdaillalr ynpniqnael drivqryqlr
      121 lahnqfelqy algasgviqk stfngvgsdt thtllaspef nlktklgtea nlsinnnvne
      181 nnnynpvlnf sltqpllrgf gkavneaall dakdnewlnk lnlqqsvadq itqvivayrm
      241 lilsgnnlqn qrlqlkeakk syeinekkik agqleptgni qqsyqiesls lmveqaendf
      301 qtasqdllqt igldpemhis vpsdvvldkl tvpnlqqaia lalqhntvyl aqkmtlrvde
      361 raykvaknqq lwqldvsgnv qsgvvndvsg inggfkgiyn gnnvteaarl tltvpfhdis
      421 rrsqlinakv rlekdrlnll atkralitni tntinniksl akryqlalkq vklaeqsyal
      481 ekkkqqagis saldvnntqn qliqaqsgli nakiaylnqi snlqrilgtt lehwqiklry
      541 gg
//
LOCUS       WP_010652238             393 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Fluoribacter dumoffii].
ACCESSION   WP_010652238
VERSION     WP_010652238.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..393
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42848
     Region          16..384
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(26..27,30..31,34,66,117..118,120..122,125,145,
                     148..149,152,224,227..228,231..233,236,264,268,315..316,
                     320,324,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 mshqknptqd aalkfiiltg fvslfadmty egsrsitgpy lallganaaa vgfvsgfgel
       61 lgyvlrmvsg yltdrtrkyw titilgytcn llavpllaia dywwiaaali iterigkgir
      121 tpardamlah aghrqgmgwa fglhqaldqt gamlgplila lalyfkmgyq scfalllipa
      181 lcalstllla rwlyprpqdl evhhdtlevt amsmntafwl ylsgaaliaa gyvdfpliay
      241 hfqktgllsp lwipisyala kgfnigsapl lgylydrygf iilviislis cffaplvffg
      301 nstfaltgvi lwsigvcahe slmraivagm ipkekrgsay gvfntgfgif wflgsvvmgv
      361 lydisisalv ifsiaiqlla fpflglvmqk lkk
//
LOCUS       WP_010652425             310 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Fluoribacter
            dumoffii].
ACCESSION   WP_010652425
VERSION     WP_010652425.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..310
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34137
     Region          4..294
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 msmhshgdsp hhhghhhaap vtydkafiis iianglfvil qivfsylsns tslladafhn
       61 lgdvlglila wiaavlmkra ptrkstyglk kisilsalan gillvftcgi iatdavyklf
      121 spspvqatsv miiagigivi nfataflfsr nsedlnirga ylhlfydalv svgvvlsaal
      181 lywtgwlwid pvvgllisli ilkgtwslfa gsfrliidgv peniswtavs efllnkpgvk
      241 gfhdlhiwal stqenamsvh lympdgelsd eiraewveql rhefniqhvt iqiektqtnc
      301 ndachhpkyl
//
LOCUS       WP_010652372             370 aa            linear   BCT 01-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Fluoribacter dumoffii].
ACCESSION   WP_010652372
VERSION     WP_010652372.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..370
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41616
     Region          3..270
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mskkalylag ggargayqag vlkaighilq vktlpfemvs gvsvgsmnaa vlaenaddfp
       61 taldkletiw seihcqqvyr asnlalsksv vrnmstmmik qrqaahlldt tplkqmiadg
      121 ldftkiaqni nngfletlei isncyetrqt isfyehnnpe ftdwnyprhg skrvsfqaeh
      181 ilassalplf fptvlldgfh ygdgsvglaa plrgsirfev dkililgtra lptfveqenl
      241 rnhedipfsh ifgnmlnalf ldnldrdiem vnrmneiaml lsmwkkrrsp wrpittlhlr
      301 pskdlaplaq thfkalptll ryllnflgek khsgdllsfv lfesdftrel lelgfqdtin
      361 nakevlaffe
//
LOCUS       WP_010652428             252 aa            linear   BCT 01-JAN-2025
DEFINITION  uroporphyrinogen-III synthase [Fluoribacter dumoffii].
ACCESSION   WP_010652428
VERSION     WP_010652428.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Schubert,H.L., Raux,E., Matthews,M.A., Phillips,J.D., Wilson,K.S.,
            Hill,C.P. and Warren,M.J.
  TITLE     Structural diversity in metal ion chelation and the structure of
            uroporphyrinogen III synthase
  JOURNAL   Biochem Soc Trans 30 (4), 595-600 (2002)
   PUBMED   12196144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..252
                     /product="uroporphyrinogen-III synthase"
                     /EC_number="4.2.1.75"
                     /GO_function="GO:0004852 - uroporphyrinogen-III synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006780 - uroporphyrinogen III
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0033014 - tetrapyrrole biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28484
     Region          5..234
                     /region_name="HemD"
                     /note="Uroporphyrinogen-III synthase [Coenzyme transport
                     and metabolism]; COG1587"
                     /db_xref="CDD:441195"
ORIGIN      
        1 mkdslnglci lntrpqsqah elsqsiraag gnvielptie ieampndwih llpnlktvdk
       61 aifisanavh fcftqllqkh ldwpssiqvi aigqgtaaai ekfgiqvsei peipdsehll
      121 alktfqqpek qnvllfkgeg grelieeqlt qkganlvvlk vykrvipqin pqwveslwrd
      181 dlvdiillts elslhnifkl fdkeahnwlr nkkwlmiser laqvafslgi knirvchpgr
      241 vmntlfdyvd kd
//
LOCUS       WP_010652430             184 aa            linear   BCT 01-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Fluoribacter dumoffii].
ACCESSION   WP_010652430
VERSION     WP_010652430.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..184
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=20316
     Region          11..184
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 maktteiytp nllrknwgwl lglgillvfl gciglsmvig ltlvsmyffa alliisaish
       61 fidifkhrdw kgifwqtiia ilyligagvv lydpflasti itallawvli iigitriila
      121 fslknakgwg wllfagitai ilgvlilmqw pisglwvigm fiaidmivng wtyifialsv
      181 rasa
//
LOCUS       WP_010652437             211 aa            linear   BCT 01-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Fluoribacter
            dumoffii].
ACCESSION   WP_010652437
VERSION     WP_010652437.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..211
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23286
     Region          1..198
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mllhylfiig icveavtgal aagrkkmdff gvmliasiaa lgggtvrdtl fntypltwvt
       61 hpeyllytsf cafltiffah slirilklfl ildalglstf viigtqkaln hglspsiaii
      121 sgmitgicgg mlrdilcndi plvlrkelya vialagallf ialdyfhtpe ninviatfvs
      181 ifvvrliaif fhieipvfdy seslrkrrrk l
//
LOCUS       WP_010652503             431 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Fluoribacter dumoffii].
ACCESSION   WP_010652503
VERSION     WP_010652503.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..431
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46813
     Region          15..421
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mnkihesrve iynrksylgf awlvwglaaa fyfsdymarv apgvmhrylq idfgineagf
       61 giltasfyip yifmqipvgl tvdrlsirwl ltvmslvtaf gccvfgladg llmgsigrml
      121 igfsaafafv cslrlatswf pptmlgllag ltqalgmlga aageapvsfl vtnvgwrhsm
      181 liiaflfial aallyqfvqd kpgehrsevr svnqlsilqs lkvilscrqt wlnalyagfl
      241 fgptavigea igpaylqfgr glgahaaafa tglifigwgi sgplsgwlsd kmgrrkplmi
      301 lsamfgiift slyvfsptls qnyayllffl fgltntgvai ayavsteihd rnvigtsiaf
      361 tnmisifvga llqplvgrlv dmvsgarayn vetlllsdfq aglkllplcs vvalilaftv
      421 ketyckpinh a
//
LOCUS       WP_010652593             391 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Fluoribacter
            dumoffii].
ACCESSION   WP_010652593
VERSION     WP_010652593.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..391
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42778
     Region          11..386
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mkhlknktlp gdsatvains lvqqkmnegv kiynlsagep klpphpsiva aatraleqgq
       61 tlyppvagis elrhrastwm nttygcslak enclvvnggk fgiyllmqll iqphdeviip
      121 apywvsypal tqlfgglpvi vetekaqgwk ltpqslkkac tpqskvliln nasnptgaly
      181 tqeellallh vaheqdllvi adevysalty dgqpfiscgs flqfrdrvii iqscsknfsm
      241 tgwrigfvfa ppsmissltv lmsqstsgvn tisqwaalaa ldeknhvssw vqqcmqkrrd
      301 tvieaigtsf gitvqpplss lyvflslhnl gfeqnnseef ckqaleeahv alvpgvafgq
      361 egyvrlsfgg needlragik alahwvhtrk k
//
LOCUS       WP_010652624             133 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF423 domain-containing protein [Fluoribacter dumoffii].
ACCESSION   WP_010652624
VERSION     WP_010652624.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..133
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=14912
     Region          12..130
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mlrstsqsrr fkwfmligif yamtatilga faahalrtqf sdyqmhifqt gifyqfihsl
       61 allfvglilw qsntrilqvs gwlfiagill fsgslyllsl mqikaigvvt pfggvcfifg
      121 wlllavgiyk nvs
//
LOCUS       WP_010652649             149 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Fluoribacter dumoffii].
ACCESSION   WP_010652649
VERSION     WP_010652649.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..149
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16623
     Region          18..148
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mestnnklle ttvqeskkgk ftqeiiigeh hliadeptsf ggndlgpspy dfllaalgsc
       61 tsmtirmyae nkkfpleqvi vklthekthv edcvgcekas akidritrri elrgklteeq
      121 rsrlleianm cpvhrtltsk ilintelig
//
LOCUS       WP_010652698             270 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Fluoribacter dumoffii].
ACCESSION   WP_010652698
VERSION     WP_010652698.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..270
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31563
     Region          <203..260
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 myelndspyf iysnlikeyc lplfnltpvk gftfcrtyed ktafllttey qfnleciqhe
       61 krisklemlr tpmhtlegyf lnspaldgks safyettaqk fgygysftiv rkhenysdyf
      121 hfigdkyqid mnnyyvhnka slnkfcdyfi eraakiltys ekqnkfilpn taiepfpiks
      181 yagtldeffk dyslersgik sislsqrqie carlliigkt aeeiaiilgl skrtiehyin
      241 ilkrklnahn kgflitkllq ffpdeftsis
//
LOCUS       WP_010652770             144 aa            linear   BCT 01-JAN-2025
DEFINITION  Dps family protein [Fluoribacter dumoffii].
ACCESSION   WP_010652770
VERSION     WP_010652770.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..144
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=15876
     Region          3..141
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mgaiikklev iladtyalyl ktqnyhwhvk gvqfkslhel femqyralae aidqiaeril
       61 imghkapatf talnqlktik dgdssidank mvselaqdng vlvkdlnaai klaqedgdeg
      121 tvallseria ahekarwmln astv
//
LOCUS       WP_010652810              69 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Legionellaceae].
ACCESSION   WP_010652810
VERSION     WP_010652810.1
KEYWORDS    RefSeq.
SOURCE      Legionellaceae
  ORGANISM  Legionellaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Legionellaceae"
                     /db_xref="taxon:444"
     Protein         1..69
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7452
     Region          6..68
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mtnkirgkvk wfnegkgfgf iessgkdyfv hfsaiqssgf ktlpegatvl fkvgkgqkgp
       61 qaedvelvk
//
LOCUS       WP_010652930             432 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Fluoribacter dumoffii].
ACCESSION   WP_010652930
VERSION     WP_010652930.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..432
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47418
     Region          14..417
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtqipffrfk thympfvvwf fplsffafqf ilrlwpglmm qeimvhfsid assfgllaaf
       61 yyygyagmqi pvallldrfg arlvifvfal lcglgallft stnnfylalf srfligacsa
      121 vgflgvskvv sewfhteqys hmiglsfsvg llgavyggkp ltqllstygg qrlglvlaig
      181 aiaigvlacm vvrtpkkskt iptnnislsq lsvlftfkkl wvlalanllm vgalegfadv
      241 wgvpyltaay gfaksdaall vsfifmgmlf ggpmlallak klgnymilga cgvglslafl
      301 vllsenvsnw wllsalffsv glmccyqvlv fatgsafvss qylgitiafl ncinmlggsf
      361 fhtligkimd yywegnlsqa glkqyslqay hhallaipvc allgtvliyl lhkrtrknse
      421 ketvkqttmv ea
//
LOCUS       WP_010652855             898 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation-translocating P-type ATPase [Legionellaceae].
ACCESSION   WP_010652855
VERSION     WP_010652855.1
KEYWORDS    RefSeq.
SOURCE      Legionellaceae
  ORGANISM  Legionellaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Legionellaceae"
                     /db_xref="taxon:444"
     Protein         1..898
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=98578
     Region          5..893
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mtqiwhdkkp qevakvlktd lsvglteeea qrrleesgan vlvkqkktsf lkilfqqvns
       61 lvtwvllgav visfllgetv daiaifaivv lnaiigfiie fradrailal qklaspkarv
      121 irdghakmit tsdivpgdtl lfeggdlvaa darlfelssl kteeapltge slpieknlnf
      181 csvetplaer knmvfmgtsv angtgraivv atgmstemgr iatmlneasr desplqkrln
      241 qvgsrllwlc fsivllifil gwlrripffe lfmssvslav aaipeglpav vtvalalgvq
      301 rmvrravlvr rmsavetlgc lqvictdktg tltvgemtar klitaeevys iigegyhldg
      361 hfisqgqeid vakdnllqtv lnaasacnna eirlqqgqls tvgdpteial lvaaakgdiw
      421 rdnlestfpr irelpfdser krmtiirrqa eqltafvkga pevifercth iltregikkl
      481 tpkerarmqq scqlmaseal rilafaqrqc dsslleaade diennlvllg liglqdppha
      541 dakasvkrck magikpvmit gdhpdtakai areleilnpg drlmtgneld kmsdddfmac
      601 vkqiavyarv taehklkivr awkkhhmvva mtgdgvndap alkeasvgia mgitgtevtk
      661 esadiilmdn nftsivdgie egrtiydnia ktlayllagn mgellvvfsv lligwplpll
      721 piqllwinlv tdglpalala tdpaepgilk rpprssqqsl mnfsffkqvs figcltalvt
      781 fgvfayeylv nadliqaqda afsvlvtael lrafgarsqt ktiwqvglfs nmrlffivsi
      841 sfalqifihh vpflqrlfgi spvtlsecll wivlgtipll ilelkkmitl rnspheaf
//
LOCUS       WP_010652939              69 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Fluoribacter dumoffii].
ACCESSION   WP_010652939
VERSION     WP_010652939.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..69
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7748
     Region          6..68
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 msekirgtvk wfnerkgfgf iqcdgqdyfv hfssiqgngf kklcegdhve fkqgkgqkgl
       61 laedvqlvh
//
LOCUS       WP_010652947             212 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Fluoribacter dumoffii].
ACCESSION   WP_010652947
VERSION     WP_010652947.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..212
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24050
     Region          7..194
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mphknttifi vdddpeicks frwlfesinl qvqtyenakd fldnynnqsg cliidvrmpv
       61 msglellehl hstknqlsvi iitgygdiam airamkagae dfilkpvnhq nlleitqrcl
      121 kkiknnttqs qgdfqermns ltkrekqvmd lvvegklnkq iayelnisis tvevhranvm
      181 rkmgvkslae likinliydk vinspavlne st
//
LOCUS       WP_010652987             362 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Fluoribacter dumoffii].
ACCESSION   WP_010652987
VERSION     WP_010652987.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..362
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39281
     Region          6..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,231,298,318,320..322)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,179,182,184,231,238,298,318,
                     320..321)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,179,182,184,321)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            184
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mnhdilftpf nlsgltlknr ivmapltrnr slhgmdtpse lnaeyyaqra dagliiaeat
       61 qisptgkgya wtpgiysaeq iagwklvtda vhakggaiyl qlwhvgrish sslqpggtap
      121 vapsaiaatg qrtfiengtf vevgtpralk igeipgiied yrvaarnail agfdgveiha
      181 angylihqfl cdgtnhrsdq yggpvanrlr falevaeaiv seigahrtgi riapvshang
      241 itetspsavf fplvqelnrf nlayihvieg etqgprefyg fdfhalrkef agpwmvnngy
      301 tlemaaeavs sgyadliafg ryfisnpdlv trfeknapln eldratlygg gekgytdypf
      361 lp
//
LOCUS       WP_010653039             197 aa            linear   BCT 01-JAN-2025
DEFINITION  YdcF family protein [Fluoribacter dumoffii].
ACCESSION   WP_010653039
VERSION     WP_010653039.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..197
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=22116
     Region          7..197
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mklflqlgvf ffvisllvys slaiyvikna etdekkqadv ilvlgakayr ensynpclva
       61 rvkhavnlyk ahyapnllfs ggtdiedgan ealtmkkial slgvpakdil lesastttye
      121 nllfsekifq akkykriiiv tepfhapral lvakkfglea vsspatksic wtkhkylsry
      181 flkeplaimy ykvrnql
//
LOCUS       WP_010653023             287 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Fluoribacter dumoffii].
ACCESSION   WP_010653023
VERSION     WP_010653023.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181037
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..287
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33190
     Region          21..251
                     /region_name="CE4_NodB_like_1"
                     /note="Catalytic NodB homology domain of uncharacterized
                     bacterial polysaccharide deacetylases; cd10960"
                     /db_xref="CDD:200583"
     Site            order(26..29,94..99,131,133..134,160,166..167,215,217)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:200583"
     Site            order(28..29,94,98,133..135,160,215,217)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:200583"
ORIGIN      
        1 mlkllflfia lfssvcfade keiaitmddl plvasrmntp gnrqrsterf tqivqtfqky
       61 kvpvigfvia gaiekgqwdf leqfrqagfm lgnhtyshyd lnhtsakkyi adveradkil
      121 tpimtnpkyf rypylaegnk ekkqevydyl kehnytiapv tidskdfdfn emlykvpyrs
      181 ranyvqkikp rylayiwkqt lkaeksgkgk kqillihanl lnsyvlgdil emyqkngykf
      241 isltealnnp aptinfspsp tkdssnndle eellnlpktk qnyvtpe
//
LOCUS       WP_010653048             136 aa            linear   BCT 01-JAN-2025
DEFINITION  GtrA family protein [Fluoribacter dumoffii].
ACCESSION   WP_010653048
VERSION     WP_010653048.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..136
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15561
     Region          8..136
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 miqhfkskqf iafliagfis ftvnfcsril ynesfsfsts iflayitgmi tafilgklfv
       61 fkqsgqtlvq sliffilvnc igmlqtwlvs lllvfyvlpa ldihqfsrei ghvmglifpv
      121 ftsylghkfw tfrens
//
LOCUS       WP_010653088             145 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2147 domain-containing protein [Fluoribacter dumoffii].
ACCESSION   WP_010653088
VERSION     WP_010653088.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Barison,N., Cendron,L., Loconte,V., Proctor,E.A., Dokholyan,N.V.
            and Zanotti,G.
  TITLE     Protein HP1028 from the human pathogen Helicobacter pylori belongs
            to the lipocalin family
  JOURNAL   Acta Crystallogr D Biol Crystallogr 69 (Pt 8), 1387-1394 (2013)
   PUBMED   23897462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..145
                     /product="DUF2147 domain-containing protein"
                     /calculated_mol_wt=15557
     Region          10..144
                     /region_name="COG4731"
                     /note="Uncharacterized conserved protein, DUF2147 family
                     [Function unknown]"
                     /db_xref="CDD:443765"
ORIGIN      
        1 mnlwklacgf fvavfylpaa laasqapvgk wvtiddktgk kravvtises ggqlsavink
       61 ifpqpgdtgi cqkcpgsfkg kkiqglqfmw glknegdnew gggsildpks gkvyrakltv
      121 egnkllvrgy vgisllgrtq vwqkq
//
LOCUS       WP_010653129             249 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Fluoribacter dumoffii].
ACCESSION   WP_010653129
VERSION     WP_010653129.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27420
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkvlvavkrv idpyvkirvk sdhsgvetqn ikmamnpfde iaveealrlr eknwatevia
       61 vciggdssqe tlrhalalgv drailvqtqd sleslniaki lkkivedekp nlvlmgkqai
      121 dgdnnqtpqm laallnwpqa tyaskiepqg eqlmvtreid ggletisvrl pavvssdlrl
      181 nepryaslpn imkakkkpld vlrlenmgls lkkhveilkv tapavrsagv kvesvtelld
      241 klqheakvl
//
LOCUS       WP_010653148             881 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Fluoribacter dumoffii].
ACCESSION   WP_010653148
VERSION     WP_010653148.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 881)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 881)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 881)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12356329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..881
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=99134
     Region          5..34
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          6..94
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Site            order(7..8,11..13,15..16,20,23,34,36,38,42..43,46..48,
                     50..51,55,58,72,74,76,80..81,84..86,88..89,93)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          36..72
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          132..161
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          143..423
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          163..193
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          196..226
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(197,201..202,205..207,209..210,214,217,226,228,230,
                     234..235,238..240,242..243,247,250,259,261,263,267..268,
                     271..273,275..276,280,283,292)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          228..259
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          261..292
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          294..325
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          304..566
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          326..353
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          355..421
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          423..454
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(471..472,476,479,489,491,493,497..498,501..503,
                     505..506,514,517,530,532,534,538..539,542..544,546..547,
                     551,554,563)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          491..530
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          532..563
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mitqaliaai kqgnlgqfkk lmssvneenf lmsdengntl vhlaaihnqa eilslllesa
       61 eeyaspvlgv snsngftple cchiyssska lsllesapkl sdssrfviar eyekikklpa
      121 ggfrregfgk iimvasalgd vsaleilfsi rsredlllyr tkdgwstahf aayndrldai
      181 klfpekfaae itdnqgntpf miaagrgslk vieyllekga dlhkknkdge nasffaveng
      241 qletlqflnk agidlflsna kgettlmraa qhghldmvry lleqgipvnq knkqgktafq
      301 lvleaknlei adflftkisq kekedalfda ikkgdfeavq wlvrqgvsls aqneskmtpf
      361 llaaslgniq lmdyflsqqp ssihdgddeg dkflfvaikn hqvhlvkilv erglvshedk
      421 nskgqtplla aakqnaeglv dlfrqkgfsl edrdaegnna fhlllakgyw gktmeylfnh
      481 cphllleknn nnetplhtai llqrtdeike mlrlttshpq iktkmmedrd aegntpllla
      541 lqcknwdavp vlcnagadil aknnkhqsvi tinylnmvpq eilksffeay qldyreyynr
      601 rrlyfifgge klnevlkfpn aevklglglf ddgvcvlkty lkafiqekhp ecssqfnpll
      661 saldklqlds tvidiinrld segmafqatg ftghsvlatl knmqdgsmkl slaerggrlg
      721 gapflndenr kfaasrsiiv paekrqevie llfkakyepq tqgidmlfnq ipvlvgkpyq
      781 fstvyqkkff dicfysnpkt glyeeirqil geekgktfyk efelymreqe lkqykefcel
      841 nhpgenvqen piivaaqeli ekrqealyas qespkargep f
//
LOCUS       WP_010653238              65 aa            linear   BCT 01-JAN-2025
DEFINITION  CsbD family protein [Fluoribacter dumoffii].
ACCESSION   WP_010653238
VERSION     WP_010653238.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..65
                     /product="CsbD family protein"
                     /calculated_mol_wt=7631
     Region          1..65
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mnkdifegkw eeikgkmkqt wgkltdddfk viegnhqeif gklqkhygys kdeaervvkd
       61 fttkh
//
LOCUS       WP_010653282             379 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 3 protein [Fluoribacter dumoffii].
ACCESSION   WP_010653282
VERSION     WP_010653282.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..379
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42376
     Region          26..>374
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mnyffsllls flfsanclag ttsevslrdk igqmlligfn gktinskssi vqmidkdnig
       61 gvilfdynyh tntfdknies peqvrklnhd lhsfakqsnl qhhrmqlpll isvdyeggqv
      121 nrlgkqygfp stlsaaeigk rgfkkaessa esmaqtlkka efnldfapel dvnvnpdnpv
      181 igkkdrsfss dpqkvthyaa iythhflnkk iqcaykhfpg hgsstkdshq gfvdvtdtwh
      241 ayelepferl fqsqevcgvv mtahivnrql dpsglpatls hkiltgllrn qlhfkgviit
      301 ddmqmkaisd nyelgqalal ainagadmlm fgnnlsvpqq nptqvidiie akvksgeitq
      361 erineayqhi melkkslrd
//
LOCUS       WP_010653346             485 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpP1/FadL family transporter [Fluoribacter dumoffii].
ACCESSION   WP_010653346
VERSION     WP_010653346.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..485
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52260
     Region          56..474
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mkkmhkpirt lvnaavisil aaggahaagf slygegagyv vgnyaagsaa eaadastgwy
       61 npaglallre qqivlggigi fptlkvdgts tfttatglpp pfppvvqyvq nfdgldgsyn
      121 afvpsfhyal plgerttfgl svtapfglst dwapdspvry satyteiltt dispelgtrl
      181 tenfalgagl dlqwarakfn qmigaptlfq ilqedpatvd slsynkaksw gvgfhvgvmg
      241 ifndnhtrig lnyqskirhv fyghsrlsgi lanndfelvf pvlpasasrt nndlfsdpqe
      301 fpdvvtlsay qdineklall gsvvytgwhv vknitlnnva vpnigtpplf tvtqanitsn
      361 vpqnyhdawr valganyhvn qklmlrvggg ydqtptndtd rnmrlpdvdr waiavgahyq
      421 wrpnvgvdvg ythlfagakp nvdsfqplsq tsiynvdvnd ghfaadlvga qltwvidkvp
      481 aaptk
//
LOCUS       WP_010653386             316 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Fluoribacter dumoffii].
ACCESSION   WP_010653386
VERSION     WP_010653386.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..316
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37196
     Region          29..261
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mvwadtlkki sdetafqaal qwvenpkhlh linnqincvy rfesegkgfy lrmthekirk
       61 pqellaaidf qqhlhlndap vcqvlsskng syietvrqdn fdfltqvcae vpgtimhfsy
      121 qdkntyflwg qalarlhraa gtyqanrhhf rswsdlwhet asylddeeqe irdlfhtldq
      181 rfkcltvnes nfglthgdhr pgnvlfdgrq ihfidfdepv yhwfiadiak pyldlcsipf
      241 nawsekftwm iegyrsvlpi dnclvqsind fsqmksldiy lwcknnwfes tapggtpreq
      301 wlnelrymal kplfrf
//
LOCUS       WP_010653417             272 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Fluoribacter dumoffii].
ACCESSION   WP_010653417
VERSION     WP_010653417.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..272
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30268
     Region          <132..264
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mkwnlfypgi talllvchgq sfsrdnemtr npvphsvspt qnnwfvslgg gaqfpdlnsh
       61 mkvnngsgfp hpfdydryai tsdnggviaa sagrrwqnes fwfpsyslsv fwqyffkthl
      121 rgeitqyslp eftnynynld ftsnlllasg kinlfrygif spyvnggigs sfndvsnyre
      181 halagitprv spgfrgsnts efaynigagi evqflpqlif slgyiyqdlg pvsggkgvdt
      241 wteqslnpgs yrsnevlvta tylfgaeknd ik
//
LOCUS       WP_010653440             431 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Fluoribacter dumoffii].
ACCESSION   WP_010653440
VERSION     WP_010653440.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..431
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47394
     Region          20..419
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mahyntrsds vvtygiqsim pwmvwglgcl fyfyecllqv spsvmsnelm rdfsvtsqtl
       61 gilsgvyfys yaamqlpggv lmdyfgphrl ltlatvvcav stiafgmtdn ffmacvarlm
      121 igfgsafaav gtmklaanwf paqrfalltg lmvtlgmlga iggeaplall idsfgwrhsm
      181 limgfiglil svlliviakd tpqnhekthp qvleeerlip sflalvknkq lwlvacyggl
      241 mymatpvfcg lwgvpflmnk mmitkttaan yislvfigwa iasplwgifs nriglrkppm
      301 yigcigallc sllfifapit taiymeillf afgifsagfl paftvakelc nrkyvatgls
      361 fmnmmnmigi alaqpligyi ldimwkgeln gnvrvyplea yhtglailpl gmlialiilp
      421 kiketycqsv h
//
LOCUS       WP_010653457             362 aa            linear   BCT 01-JAN-2025
DEFINITION  saccharopine dehydrogenase family protein [Fluoribacter dumoffii].
ACCESSION   WP_010653457
VERSION     WP_010653457.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..362
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39828
     Region          26..362
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mynvmitgag kigsliacll sdsgsyqvhl vdidfngsdv krlleavpki ktvaldvrdq
       61 qstqaymekh divavisslp yflntyvaea akaakahyfd ltedtavtea ikaialdaet
      121 afvpqcglap gfisiaansl mqefeeshhv klrvgalpqn annalqyslt wstdgviney
      181 gnpcyaikyg ravtlapleg letiqidgce yeafntsggl gslaeihagk vqtmnyktmr
      241 ypghcskmrl lmndlrlnqd rptlkrilen sipktyqdlv ivyvsvegik rgelteknyv
      301 kkiypeeicg lewsaiqist asgvcavvdl vmgqsneykg lilqekfhla ailenrfgry
      361 ya
//
LOCUS       WP_010653537             431 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Fluoribacter dumoffii].
ACCESSION   WP_010653537
VERSION     WP_010653537.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..431
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47749
     Region          14..408
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(27..28,31..32,35,74,132..133,135..137,140,160,
                     163..164,167,249,252..253,256..258,261,289,293,346..347,
                     351,355,371,374..375,378..379,382)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 maiirrdpks kasrrvslas figttiewyd fylfgtasal ffntlffpki spvagimaay
       61 atyavgffar plggvifghf gdkisrksml vitlclmgls tfligllpty dtigifapil
      121 lvilrciqgi avggewagav vlsaeisrek ergfysswpn sgapfglvls igiflffsnm
      181 pneqfltwgw rvpfllsffv vlvglymrlh imeskaflna tknkrppkip alemlqshlk
      241 nfllavgarl iesssfyilt vfvlsygtfn lhlsktllly avmsgaifev llipyfgmls
      301 dligrrpvyi agsllmgifa fpffwllqtk npqliffavm fgmcvphamm hgaqaafyse
      361 lfktrirysg taiayhlsaa lsggltplia tglvewahdk twpvsvylii maiitiicly
      421 matekaqksi s
//
LOCUS       WP_010653550            1093 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Fluoribacter dumoffii].
ACCESSION   WP_010653550
VERSION     WP_010653550.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..1093
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=121069
     Region          16..1085
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnknipqrpl lnsagrlsra finskltlli iigsllfgil aleftprtyn peivvpvvai
       61 svsrpgsdaq emlhqivrpl eglmasipgv dhtygmaind savvtvrfkv neneenslvk
      121 vynqinsnmd kmpagtlmpf vqsislydvp lltinlsssh fstthlqtla trvledlrnv
      181 pqvgkswvmg aspsalrvwl npdkmasyfi plqkikqale vsnvsfnagk lepnlhespl
      241 riegnlitpd dlgqiiigvn egkpvllkdi ahielapqdd airsyfafgr asadqqpgel
      301 kpsvtiafar qkgsngveva navlqrlkli eqskiipegv tatvtrnygd eandavntlv
      361 ehlgiaiasv villmlflgw reasivifsi plilcivlgv gwiagqtinr itlfalilsl
      421 gllvddsivv ienihrhire htqhnfarli ifaaneigkp tiiatftvil alipmafvsg
      481 mmgpfmgpip fnaplamlvs liiaytavpy layrwlraka hqlpkvedns rmehqlslsh
      541 kvylylfssl lksrwkrylf yffvlfllil viiqplwqfi rpsgtngpls pmgvelkmlp
      601 ddnvntflle inagagaslq qtsnivkeis kvlahnnfvt nyqvflgqaa pedfaamvrg
      661 damqhgtnya qirvnlinkh drrigshkia qqfydslwni rhsypqahik lfesppgppv
      721 rsqmeaglyg pdyehlrdlg qfisnrvypk vygminidns vtdnleeyni vinrnatlla
      781 glvpsmlahd lqgyfkgvqv gnghrpglle peniilrlpk psrenssvlk klflinqqnq
      841 lvplakvvdl kkgiqkkpvf trdqhqvvyv tgemlhsspa ygvttvtqml khldlpnnsh
      901 lsvgnlgfke eqpqdvaknq lfwlgemrlt ldvfrdlgsa fivaivliyi lltgfyrsff
      961 ipliimgaip ltiigvfpgh wimqqpftat smigvialag ivvrnsllli dfiienlrsg
     1021 asidtavtqs gvvrltpill talaiilgss vmlsdpvfgg laislifgaf astlltlfli
     1081 pliylgwwkw rhs
//
LOCUS       WP_010653563             424 aa            linear   BCT 01-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Fluoribacter dumoffii].
ACCESSION   WP_010653563
VERSION     WP_010653563.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..424
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47025
     Region          2..424
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mkrnkffrhl gpglitgisd ndpsgiatca qsgakfgfgq lwsvllmlpl miaiqemcar
       61 igavknrgis siikkhygnk iliplafllf tantinlgad lgamsaalsl lipvnqligl
      121 ifftgiilfc iiyfpykryv qilkwlclfi lvypislfiv rtpwlevlkn tfvpnitfss
      181 eyffmltalf gtsispymfi weasqeaeen rkmkissshg faqisnirln slkkdnfigm
      241 ffsqictwsi ialigitlht hgisnintaa daakalepiv dgfpyagyva klifslgiig
      301 lgllsipila vssayalavl lnrrsglfhk cknaryfyli tivstliglf mnllqinlik
      361 gliiaavinc ivalplifii llitnnkqim geyknkllsn vlgwitfllm aissllmfys
      421 fffs
//
LOCUS       WP_010653695             404 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Fluoribacter dumoffii].
ACCESSION   WP_010653695
VERSION     WP_010653695.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..404
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47122
     Region          81..235
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 meinltvfaa pvflvligle ffltyhkksg iyqlndsinn fsagifeeia alpvrglvif
       61 syyylyehfa ffhikpnlvs swillwlsvd fcyywyhrts hrcvffwigh svhhqsehyn
      121 lsvalrqgyw qtltswvfyl plaligfptw mfvivsscnt iyqfwihtqs inkmgwfeii
      181 fntpshhrvh hgknpqyidk nyagsliiwd klfgtfepee tpaeygvtep ldswnpfyan
      241 ikvikdvmyy gknlknkvdv vraffmppew imnrlqqegq tvskqavpqk nfnspklyll
      301 fntalaialy aylsfifkln slnswligaf ilftlyilga vangkqkilf ielsrsilvl
      361 ftlvafkinl flsllisllf llinlrlfss hftqnhsytp sisv
//
LOCUS       WP_010653720             367 aa            linear   BCT 01-JAN-2025
DEFINITION  type III polyketide synthase [Fluoribacter dumoffii].
ACCESSION   WP_010653720
VERSION     WP_010653720.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..367
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40912
     Region          3..363
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 mqskitaigi atppfmrtqd eiaelistgf hldeaqkkil kkiykssgie trhsvltdyc
       61 kkpgqfeffp ntahgsfpst fqrmqlykdn alnlavesie nclnsinfdr skithlitvs
      121 ctgmyapgid ieivqklnla ssvkrtainf mgcygafngl kvanafcqte phsnvllvcv
      181 elctihfqna fnienivsna ifadgaatal iqaktdteky fniesfycdl vpqtsrdmaw
      241 ticdygfdiv lgsyvpeaik sgilmftekl leqasysfnd idfyaihpgg tkilqaceha
      301 lnispddlqy syevlkrygn mssatvlfvl kkiwdklniq dkaknvfsca fgpgltlesm
      361 ilkiqhh
//
LOCUS       WP_010653598              66 aa            linear   BCT 01-JAN-2025
DEFINITION  carbon storage regulator [Fluoribacter dumoffii].
ACCESSION   WP_010653598
VERSION     WP_010653598.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..66
                     /product="carbon storage regulator"
                     /calculated_mol_wt=7443
     Region          3..60
                     /region_name="CsrA"
                     /note="sRNA-binding carbon storage regulator CsrA [Signal
                     transduction mechanisms]; COG1551"
                     /db_xref="CDD:441160"
ORIGIN      
        1 mdiislhfee pliihigdat vkilafktqe hgnikfgvda prsvnvhree ifhaikqkqq
       61 lletve
//
LOCUS       WP_010653733             375 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Fluoribacter dumoffii].
ACCESSION   WP_010653733
VERSION     WP_010653733.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 375)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..375
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42738
     Region          92..371
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mlfnlgkeat lmllegtkna ipfnivfasl ivliflynrv pisltigwyl gillismvrw
       61 ffcrqninnh lfkvnkknll ikfllltlsm gvawgicyli sltyvsvlye fiiilvfggl
      121 sagsiaflsv ylpayyayvf pmfipviiyn ylvfnmgrti fatmfilfil mlllsaimnk
      181 klldktfqls qdketliyel qitsitdplt glynrrhfev llpqelrrak rnqyplnlis
      241 ididnfklin dnfghpsgdk vlvslgsllt hickrandti frlggdefaa ilvnqpvgea
      301 vhichkinnl fkrnllndfn skelailnqv tlsmgivnih fnssynmetv invadkalyq
      361 akkngknqiv ieqih
//
LOCUS       WP_010653737             332 aa            linear   BCT 01-JAN-2025
DEFINITION  sodium:calcium antiporter [Fluoribacter dumoffii].
ACCESSION   WP_010653737
VERSION     WP_010653737.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..332
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=36110
     Region          16..330
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mwlevlfmli lilisaqlfs naleyfgeri distgvtgsi faaistalpe ttvpilaiia
       61 gtsdrqinee isvgailgap lmlstlstfi massiikkrg ingyikpest gfqrdmnffl
      121 vaftlgalam flpiepnymr ilfsiilisl ylvyllltfs askdlvktgh avitseplfi
      181 tklgvktnlk tiliqlfigl illvagakgf ihgihavads igvpvlllsl liipiatelp
      241 ekvnsviwvr knqdtlgfgn itgamvfqgt llpalgillt pwqpsrivlt gilityigta
      301 wlrftmtsrg ikikflflng llyvtylgiv lf
//
LOCUS       WP_010653791             377 aa            linear   BCT 01-JAN-2025
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Fluoribacter dumoffii].
ACCESSION   WP_010653791
VERSION     WP_010653791.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..377
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41629
     Region          3..373
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mpisqkikny tnqlahegll rnrrvhadds slihfdsndy lsltrdkria evyqrgyaly
       61 ptgsgasmll sgyhsnhrav eeafanllav ddcilfssgy aanlavtall gklkvhcfid
      121 keihasiydg lalshvnytr ylhnnldvle gklitgsali tegifsmsgq laplmqlsml
      181 cnrnqgallv deahsfgilg sqgkgavahy gltqnevplr iiplgksfaa qgalvagkad
      241 wiyallqagr sviystaisp alsygllhtl efvvnaedrr lkleqlialf ktyrtqspfn
      301 wadssspiqq lrlgcpylal yferelkkqg isccairkpt vsakasglrv ilnynhtpeq
      361 irelfdklin iyeckhp
//
LOCUS       WP_010653886             482 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Fluoribacter dumoffii].
ACCESSION   WP_010653886
VERSION     WP_010653886.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..482
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52951
     Region          3..479
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mhtnsekhpk slriffatem werygfyvvq sllalylalh fkwpdkqvya lvgsftalty
       61 lspvvggwia dkligqkrav llgavvlfls yctlslvdnt naltaslaai avgtgllkpn
      121 issllgneyl mssarresgf tifymgittg iilgttlpsi lndyfgwaas fisaamgmvv
      181 afvvffygir kynirdynpf vfqykkiita avlmlflwsl sfyilnspql anivfglvvv
      241 fsagyilysv sgenanqsrq tlvigllcii svvfwsfyfq mfmsltlfis rvveptfcgi
      301 qfpppyyvti qsigmliigy flakknpqln lverglsigk kflfaifitt vayavialvs
      361 nftdknalls pllivpaylm fslaelllsp vglsaitlla dknkvstlmg iffvslgigg
      421 flsgklaslt aipsgetnta vlktlyaaaf tqqlgilfia tlcclvlyav ikfllthvhl
      481 te
//
LOCUS       WP_010653815             390 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Fluoribacter dumoffii].
ACCESSION   WP_010653815
VERSION     WP_010653815.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008671
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..390
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42374
     Region          1..>388
                     /region_name="RosB"
                     /note="Predicted Kef-type K+ transport protein, K+/H+
                     antiporter domain [Inorganic ion transport and
                     metabolism]; COG4651"
                     /db_xref="CDD:443689"
ORIGIN      
        1 mhdgsvfyti flifagaafl stlvlytkqs llvayillga mfgpwglglv sdvtivkqig
       61 dvgivfllfl lglhlqpqnl vhmlkkvtwi alissalfav taywigrafg ltvteswilg
      121 gsmmfsstii glkllpttil hhqhtgevmi svllmqdvia iivlilinga qqtggfsidd
      181 lilvgidlpa lclfafaiek hvlirllarf drtqeyvfll sigwclglsv laqkiglsed
      241 igafiagval aaspislfia eslkplrdff lvmfffsiga tfnfglsyqv ivpalilsal
      301 vlvfkpvlfy illgksgekk qvakevgirl gqasefsllv asialttnli sdkasnliqa
      361 ttiltfivss yfvvlkyptp iafsdkmrkd
//
LOCUS       WP_010653969             390 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Fluoribacter
            dumoffii].
ACCESSION   WP_010653969
VERSION     WP_010653969.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..390
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=43003
     Region          4..389
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mkakvillka kqntvlrghp wifpkaiakt hgklitghli diysaeeeli gvgiynehsl
       61 yrvrvlalsn esldtsnlht lithrlnqak qvrdclslpn eettayrlfn seadglsglt
      121 idrfnqncvv assaywveln reviinalkn lfpadqiiwm pqskplsqdg wkqisvqeqh
      181 yntkvleagv iyevefaqaq ktglfldqre nhqriaqlsk gkkildlycy sggfalhaar
      241 agatkitavd ssaqaiaqak nnaalngvtq iefieadard yltkagdydl vvldppklvp
      301 skqhverakn yyrflhrevf knmkagsllm tcncssalss sefcslvsaq agavgkqari
      361 lgvygpasch ptltsfpegn yltaillavv
//
LOCUS       WP_010654003             475 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Fluoribacter dumoffii].
ACCESSION   WP_010654003
VERSION     WP_010654003.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 475)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..475
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54170
     Region          67..463
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 meihkllkrq lqhtslapdk kpetdeqwqt fiqrinntyi dadqerylhe rsikissrem
       61 mslneklaya qhiaglgyws ydgiidraiw snelfslfhl npqnkapsld efmklvheqd
      121 qfelrqkvqr sleekidyec eiriknsdgn yrwyriisqc qqgekqlagi iidihkskaa
      181 eekikelnqq isstarragm aevattilhn ignilnssnv sitilknsfk ldyhkkllki
      241 memmenhqtd lvhflthdpk gkiipqylla igkiimeene knnlevenlq edlrhitqiv
      301 dtqksisgls slnekvylpe lidtamsiim nsskkkdiqi tknfnptpmi nvdkskllqi
      361 linliqnakd svlentsslf keiklkvqkk gkkwveiive dngvginadn lqrifafgft
      421 tkknghgigl hssaisarem ggsliaaskg egygaqfllt lpindssykq ggpde
//
LOCUS       WP_010654076             406 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA recombination protein RmuC [Fluoribacter dumoffii].
ACCESSION   WP_010654076
VERSION     WP_010654076.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..406
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46240
     Region          87..392
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mqflsstisl egvicvlalq flfliwlvik qnqqkkqsmq lhektletft sqlhqmhlnv
       61 sekmaqgqlm tqqlihdtvq kqmtdvreqi nhsfkqhasa ltshlqllte eirnhlhvlt
      121 qqvnsklteg fektsstfid vvkrltiide aqkkitelsn hvvslqdvlv dkkargafge
      181 vqlatlisnm ippnhfemqy tlsnqkradc ilflpeptgn vvidakfple tyqrllcada
      241 gsvekkslqq qfrqdiqkhi kdiaekyiip nettdgammf ipaesifaei hanypdlial
      301 sqrlkvwlvs pstlmavltt akavlkddat rkqvhiiqkh lqaladdfqr fekrmdklsk
      361 hinlahqdvs dvntsakkit srfqkiesvd ieldelelie tdasie
//
LOCUS       WP_010654031              59 aa            linear   BCT 01-JAN-2025
DEFINITION  Trm112 family protein [Fluoribacter dumoffii].
ACCESSION   WP_010654031
VERSION     WP_010654031.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 59)
  AUTHORS   van Tran,N., Muller,L., Ross,R.L., Lestini,R., Letoquart,J.,
            Ulryck,N., Limbach,P.A., de Crecy-Lagard,V., Cianferani,S. and
            Graille,M.
  TITLE     Evolutionary insights into Trm112-methyltransferase holoenzymes
            involved in translation between archaea and eukaryotes
  JOURNAL   Nucleic Acids Res 46 (16), 8483-8499 (2018)
   PUBMED   30010922
REFERENCE   2  (residues 1 to 59)
  AUTHORS   Bourgeois,G., Letoquart,J., van Tran,N. and Graille,M.
  TITLE     Trm112, a Protein Activator of Methyltransferases Modifying Actors
            of the Eukaryotic Translational Apparatus
  JOURNAL   Biomolecules 7 (1), 7 (2017)
   PUBMED   28134793
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006712
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..59
                     /product="Trm112 family protein"
                     /calculated_mol_wt=6743
     Region          1..58
                     /region_name="Trm112"
                     /note="RNA methyltransferase activator Trm112/YbaR
                     [Translation, ribosomal structure and biogenesis];
                     COG2835"
                     /db_xref="CDD:442083"
ORIGIN      
        1 mdrklleilv cplckgklll kkqelickfd rlafpvhddi pvmlehearv lsleekdsl
//
LOCUS       WP_010654174             500 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Fluoribacter dumoffii].
ACCESSION   WP_010654174
VERSION     WP_010654174.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..500
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54806
     Region          18..493
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 misqevknyl pelalrqkqa sniiyitfws qfsvyalnti mvlfltrpvw sqglgysqak
       61 ayafigvaha tgylmpmlgg fmadtvvgir raillgsvml amayllimis gytvntlgdt
      121 ffiaayalip atnsllmgts ssmvshiysd davkaksamt yyyiainvga llatliapll
      181 lesrygplsi ltlafvgksi aalnfarrys iyenviwgkd lssfskpgif rligyiiliy
      241 tltlfayshv yiastiiasg cgigiawflk ktlalkgitr ekqmiallli ieavvffviy
      301 nqmnstlilf aennsdhnlf gltvspahyq ilnpllilai gsqlprfykf fphftipyqf
      361 aagtalagva llvmafaast tdtgiingny ialtyilisi aelwvsaigl smvglycdkn
      421 siafamgvwy lasslahais griagwvaip ntihsaidsl pyyedyylvl gitamilgii
      481 myffayilqk tmrkrgvilg
//
LOCUS       WP_010654225              64 aa            linear   BCT 01-JAN-2025
DEFINITION  carbon storage regulator [Fluoribacter dumoffii].
ACCESSION   WP_010654225
VERSION     WP_010654225.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..64
                     /product="carbon storage regulator"
                     /calculated_mol_wt=7232
     Region          3..>51
                     /region_name="CsrA"
                     /note="sRNA-binding carbon storage regulator CsrA [Signal
                     transduction mechanisms]; COG1551"
                     /db_xref="CDD:441160"
ORIGIN      
        1 mvvlsrkige kvfvddgeie vkvlcskgnk illgfkvpan mevereedyl rkilqvpefl
       61 kvnq
//
LOCUS       WP_010654263             464 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Fluoribacter dumoffii].
ACCESSION   WP_010654263
VERSION     WP_010654263.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..464
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53071
     Region          160..447
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrfknqfilg lcylllssvc sasetdkltl hkvlhrvnly ypkikiarle itkaqgthls
       61 algkfdpsld astrsqpagg yinnygdtql tvptlyngvk lfagyrngng nwpiyyqnyl
      121 tnsggeyrag lslpllrdrl idkertnllt taesiemkih daeavkikiy qetikaywqw
      181 veagwqlktf rhllelakkr qhaieqqanq gdlpklaite nlqqivqreq llnqgrmife
      241 qaginlslyy rdaqgnplip tesnlpsqvl nnprqlspgl sqltqhpslk rlqnysriir
      301 lkrdlaqnel lpnldatayt fkqngtggyp llipeaafvg vsfkfpvlrr eakgnlirtq
      361 selyqiraek kllydqlkne ltnlyigirr iqqqvaflkk eyhlalkvqh getqkfhagd
      421 stlflvnqre qvttqvqlnw inaqvqqeel kdlvrffsst elgk
//
LOCUS       WP_010654307             409 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Fluoribacter dumoffii].
ACCESSION   WP_010654307
VERSION     WP_010654307.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..409
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44327
     Region          1..396
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mstsrviawf vwiiasifya yqyilrvmps immnditaqf hidatvfgqf sgvyylgysl
       61 mhlpigilld rfgprkimtl cillpvvgll pllfsehwvy plmgraligi gssaailgtf
      121 kiirmtfkeq hfsrmlsfsv migligavyg ggpvsymcqa mgykmvielf iviglvlacv
      181 tylivpdekp tyhtsviani ktvfgnkkvi llccfaglml gplegfsdvw gagflkqvyg
      241 lnsatanylp smiflgmcfg spilsliaek tgyylgtiia agitmclvft alvagiltvs
      301 sitvsfiivg mccayqilai yivstyvpen laglttaian miimifgygf htvigyline
      361 hggireagaf vygigvipat lamgvigfsi iayrekyals kylpagspg
//
LOCUS       WP_010654316             213 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Fluoribacter dumoffii].
ACCESSION   WP_010654316
VERSION     WP_010654316.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..213
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24050
     Region          8..195
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mdftdaavfi vdddpeicqa lrwlfesvdi pvstyenakd flvnydprqq gcliidvrmp
       61 lmsglelleh lnasktqlsv imitgygdip mavramkaga tdfilkpvnh qylleitqkc
      121 lqkssdypvq pqtdfferie rltkrerqvm dlviegklnk qiaheldisi stvevhranv
      181 mrkmeaktla elikinliqt lggdnpnslg emp
//
LOCUS       WP_010654336             143 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Fluoribacter dumoffii].
ACCESSION   WP_010654336
VERSION     WP_010654336.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15924
     Region          1..141
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykqimvavd dtkastlalk eaikvaktqn sklyvihiid tlyegdvdre sfveltrkqg
       61 qdvlnsmkkl lsrsklefel klgelipskp qiaeklidea knlnadlivi gthgrrgfhh
      121 mltgsvaeev irisktpill vrg
//
LOCUS       WP_010654421             146 aa            linear   BCT 01-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Fluoribacter
            dumoffii].
ACCESSION   WP_010654421
VERSION     WP_010654421.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..146
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=16272
     Region          1..144
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 milqspafah nafippeytc nginhspple wkdvpentqs fvlimddpda pmglwvhwil
       61 fnlpsnchel kigkgipsst isalnswgks gyggpcppng thryffklya ldtmlnlgeh
      121 atkkeietam qnhiieqtel igkyhq
//
LOCUS       WP_010654438             378 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Fluoribacter
            dumoffii].
ACCESSION   WP_010654438
VERSION     WP_010654438.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..378
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42100
     Region          10..292
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mmqqdrywqa kkvtilgavs nallgiikll ggyffhshal vadgvhslsd litdamvlfa
       61 skygsldada shpyghqrie taatlllsll livaglgiaw dslydmihss yhmpnwltlp
      121 iicisimsne tlfhytlhig krinsklita nawhhrsdaa sslvvligli gsiagysyld
      181 aaaaiivglm ivkmgwdyaw nsvkelvdta vspellarie eviqnvdgve kihqlrsrsm
      241 gedvlidvhi lvsprisvse ghyiaqhvhh aliaqiesvn dvivhvdped detscpslhl
      301 psrkvlqell anevridfpq ilfwnlhyld gtigidivcd egftqwqelr ervilalklq
      361 sdivevrlfs lhesmyhn
//
LOCUS       WP_010654460             591 aa            linear   BCT 01-JAN-2025
DEFINITION  CocE/NonD family hydrolase [Fluoribacter dumoffii].
ACCESSION   WP_010654460
VERSION     WP_010654460.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 591)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..591
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=67148
     Region          40..583
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mkkwlnsnfi prarlnhyql agwkparvae sglgcklqad vmipmpdgvh lsadvytpak
       61 agkypvilqf saynrdlhtt glpsgnneig sppvitdrgy vqvvvtarsi grsegdfqpw
      121 qneqetqdhy hciewaaqqp wsngdvclfg tsyygmnqas vaslnppslr affaneictd
      181 fyrhvfhygg vfnagfmnlw vganfnsptv hryvapwkra lisyfisypw fwkrfikpnl
      241 tkivqefkkn hpipevlqwy ihlmidsnsr eetkitqgpf krlnkidipf vvaqnlgnie
      301 lhqfgcydlf ehsstpankk wmilgpaeye lpvyswqlea laffdhilkg vdngyanlpp
      361 vrywvegknq yesatsfpsp etqvrkfyle ksqeaevrgl qqqipaeaed cwisippgse
      421 vlpgieqfek qklayellfe qettiagpit vqlkfscnei dsyviarlgk mdhdgkyhpl
      481 smghlrpatr tvdedsgsrc evaintsivt plqrnipvll rfsmtpvatl lkkgerllle
      541 fasrsdqlfv smkegflvpd tvvppyfcrn kihcgadsfi elpceqkaql s
//
LOCUS       WP_010654500             425 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Fluoribacter dumoffii].
ACCESSION   WP_010654500
VERSION     WP_010654500.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..425
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46963
     Region          14..416
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mqvvdefqey ndlkssllpw mvcfaatlff fyefiqgnmf asiaadimqa yqiqadkmaw
       61 lssiyylsnv lflfvagmvl drfsikntll iamflcvast fllahsdsfy malfcrfitg
      121 igsafcflgp vrlashwfpp rrmalvtgai vtmamaggml aqypltklvl mvgwrqavqd
      181 vgilgfvmll vmffwikekp knplkvvppi nvisaakkay fnaqyiraaf yaslmnmaia
      241 vfgammgtly lvqrldinsa qasmvngmlf lgaiigsplv gwisdkmglr ivpmkigvia
      301 slltllsvly lpvsysqmaf lffllgffts aqvisyalva essppamtat avsvisiltq
      361 ggyivyqnlf sylltnhggm hmvngtpvyl lsayqyaaii lpiglliafl mlfglkethc
      421 qhted
//
LOCUS       WP_010654504             326 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Fluoribacter dumoffii].
ACCESSION   WP_010654504
VERSION     WP_010654504.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181037
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..326
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37829
     Region          66..293
                     /region_name="CE4_NodB_like_1"
                     /note="Catalytic NodB homology domain of uncharacterized
                     bacterial polysaccharide deacetylases; cd10960"
                     /db_xref="CDD:200583"
     Site            order(71..74,130..135,167,169..170,196,202..203,256,258)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:200583"
     Site            order(73..74,130,134,169..171,196,256,258)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:200583"
ORIGIN      
        1 mkikniikki psmlmllmac snlsfslnpn eiainannst ldsenklqap eppelppkqt
       61 pvalkktvsi tiddlpfvge yrnfhlnmmi ntmtkeqvpa tgfiiarevr kdnweilrkf
      121 rdagfglgnh tlshanlnkm nteeyiqeik gadrilhpvl tepkyfrypy lamssgqkke
      181 dilcylakkn yhvapitvds kdfvfnqrll svpelnrray leelkpfyld fiwqqtlrae
      241 ehnqfhrnpq qaqillihan llnayvlpdi inlykekgye finleealkt fkypiqcsrh
      301 ailahnkkmp lqqktkndve tfvewd
//
LOCUS       WP_010654534             450 aa            linear   BCT 01-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Fluoribacter
            dumoffii].
ACCESSION   WP_010654534
VERSION     WP_010654534.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..450
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=49661
     Region          9..439
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mhflnsdspn kialdftgqp lsfaeletai hkmslqfkkl psgilllqaa pkplfviqll
       61 aalntgkpia lygeeltgdk rtllgtsitv nelgelsdiq enalitphpe lalvlftsgs
      121 tgqmkavqls lkniiancra vidslkfrev edqllflpls ysfgllgqll pglitgiktq
      181 lisqftdlka llesgevpqm wsgvpshwva vtkmaalfpe sagkikavvs agaplsislr
      241 nhlmhtfpra tvynnyglte asprvltyss kdplfledya gypvgdwqir lsdaqelliq
      301 gsqlmlgylg eekptriqdg wfftgdlaee lpsgliaikg rldeivnigg ekvnlieieh
      361 kicqikgire vivlpladel ygfrllacle rsnfsanite hmlseqlknh flpkklpisv
      421 rfleklprnp hgkldrkkll lshkdklhah
//
LOCUS       WP_010654540              75 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl carrier protein [Fluoribacter dumoffii].
ACCESSION   WP_010654540
VERSION     WP_010654540.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..75
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=8424
     Region          4..72
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mkitdselkk iisklsganp edihedtali edlhldslki vellailsee ysltvteeda
       61 mnfhtyknlf eftqa
//
LOCUS       WP_010654602             149 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Fluoribacter dumoffii].
ACCESSION   WP_010654602
VERSION     WP_010654602.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..149
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16448
     Region          5..138
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 msvpheryld eaikearqsl aeggipigav lvyqgriigr ghnqrvqkgs tilhgemdal
       61 enagrqkakv yeqsilyttl spcamcsgai llykipyvvi genqtfmgee allkargvtl
      121 evvqneecis mmrhfinkng rlwsedige
//
LOCUS       WP_010654621             264 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Fluoribacter dumoffii].
ACCESSION   WP_010654621
VERSION     WP_010654621.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..264
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29266
     Region          2..261
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mflqrlittl ilvplvlali fygnkwllgg ivllvflaac keclqliplr nlglqigffv
       61 lmllglwacg ylfsywmvig lilwglnila ilsfpgsqky wgypvvvaav cffllplfiq
      121 slihlytlpn gkallvyllf liwvsdtgay lsgkllgkhk lipqvspgks wegvlggvil
      181 smliawigft yfnpaatvyw fvlalctiii aifgdlfisi lkrrchlkdt gavipghggi
      241 ldrldsliaa lpifyfgitw vilq
//
LOCUS       WP_010654030             466 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Fluoribacter dumoffii].
ACCESSION   WP_010654030
VERSION     WP_010654030.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Gournas,C., Athanasopoulos,A. and Sophianopoulou,V.
  TITLE     On the Evolution of Specificity in Members of the Yeast Amino Acid
            Transporter Family as Parts of Specific Metabolic Pathways
  JOURNAL   Int J Mol Sci 19 (5), 1398 (2018)
   PUBMED   29738448
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Vangelatos,I., Vlachakis,D., Sophianopoulou,V. and Diallinas,G.
  TITLE     Modelling and mutational evidence identify the substrate binding
            site and functional elements in APC amino acid transporters
  JOURNAL   Mol Membr Biol 26 (5), 356-370 (2009)
   PUBMED   19670073
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..466
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51880
     Region          9..427
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; pfam13520"
                     /db_xref="CDD:404414"
ORIGIN      
        1 mnhwssekis vlalvllitg aidsirnlpg talfgsslif ffifsaivfl ipvalvsael
       61 sstwsdeegg iyswvkhayg enlafftiwl qwintlvwyp tilsfiagvl aylinpelaq
      121 nkyylisvil vifwsltlia lsglrasahf aglcaiigmi lpmgfiifla liwvikgnpi
      181 aidlspsnll phwkdtqswv sltaimtsfl gmelaavhvr nvknpqvnfp kamffsvlli
      241 lstmifgsla iafvlpkeki slidgvlqaf nnffqaynle wllpiligll llgslgsmin
      301 wiispakgll maanhsflpk fmcqlnkrgi ssrilitqav lvtllcsgfl lfpsvnaiyw
      361 lftalstely immyvlmfia awklkskfah lerpfaipgk kagyyltcil glcgctmtli
      421 vgfippvefm nfgsaghfrl vfsmgivimm vpafllywrk kyitrs
//
LOCUS       WP_010654625             450 aa            linear   BCT 01-JAN-2025
DEFINITION  S41 family peptidase [Fluoribacter dumoffii].
ACCESSION   WP_010654625
VERSION     WP_010654625.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..450
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48065
     Region          52..380
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mlirkiypct laivyaftlm lpltgfaddq antdtstnss ttskavpled vqrfsnaige
       61 ikkyyvkpvd dkelfdnair gmlngldphs syldeeefkd lqtstsgefg glglevtmed
      121 gvvkvvtplv dtpafkagik sgdyiiklgk esvqglslkd avnlmrgkag stiqltvlrk
      181 gvnkaltfdl ireviqiksv qskmlapgyg yirltqfqal tgkdmlqaid rlkqqsggnl
      241 kglvldlrnn pgglldsaiq vsdaflgkdk sgkpetivst kgrlpgsdft alskgvdvlh
      301 napmvvlinn gsasaaeiva galkdnkrav ilgttsfgkg svqtvlplde ktgiklttal
      361 yytpsgtsiq atgivpdivv neleipktas kpsdltgfse anlsghllnq tngensktks
      421 tkaqidelmh ndyqlyaalt vlegmalanr
//
LOCUS       WP_010654697             182 aa            linear   BCT 01-JAN-2025
DEFINITION  peroxiredoxin [Fluoribacter dumoffii].
ACCESSION   WP_010654697
VERSION     WP_010654697.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..182
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20270
     Region          4..178
                     /region_name="PRX_Typ2cys"
                     /note="Peroxiredoxin (PRX) family, Typical 2-Cys PRX
                     subfamily; PRXs are thiol-specific antioxidant (TSA)
                     proteins, which confer a protective role in cells through
                     its peroxidase activity by reducing hydrogen peroxide,
                     peroxynitrite, and organic hydroperoxides; cd03015"
                     /db_xref="CDD:239313"
     Site            order(4,55..56,59,119,129,142..144,146..148,152..153,160,
                     171..174)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239313"
     Site            order(53,87..88,110,112,124)
                     /site_type="other"
                     /note="decamer (pentamer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:239313"
     Site            order(54,57,130)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239313"
     Site            order(57,171)
                     /site_type="active"
                     /note="peroxidatic and resolving cysteines [active]"
                     /db_xref="CDD:239313"
ORIGIN      
        1 mltvgqkipe fsvvaakpgf nnheeqgesa fevvteksfp gkwkviffyp kdftfvcpte
       61 ivefaklnge fsdrdavvlg gstdnefvkl awrrehkdlh klnqysfadv hgkltdgfgi
      121 reeesgcalr atfivdpnnv iqhvsvnsln vgrnpqeilr ildalqtdel cpcnrpigge
      181 tl
//
LOCUS       WP_010654763             304 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Fluoribacter dumoffii].
ACCESSION   WP_010654763
VERSION     WP_010654763.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34028
     Region          4..226
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mhaldikqly ktyangvqal kgidltidtg dffallgang agksttigli ttllnktsgs
       61 isihgydldk epekaksclg lvpqeinlni fetseqilln qagyygisrk qaqprvesll
      121 qqlglwekrd siarhlsggm krrlmiaral ihqpkvlild eptagvdiei rhsmwefltr
      181 tnaegttiil tthyleeaeq lckniaiidk geiiknssmk allqtlrhqt fifntenrie
      241 slpdlhpfkp tlidsttiel rvdnnlnlnd afalltqhgi kihsmrnktn rleelfldli
      301 kngh
//
LOCUS       WP_010654678             678 aa            linear   BCT 01-JAN-2025
DEFINITION  M13 family metallopeptidase [Fluoribacter dumoffii].
ACCESSION   WP_010654678
VERSION     WP_010654678.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..678
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77192
     Region          1..678
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mklnislftf aflcsssiys vstelpkspa eqalhlnwld tkvapsenfy ayadgnwqkn
       61 npippdyssw gsfniindkv qdiihqmlid asqnthakpg sieqkvgdfy ysgmdeksin
      121 qlgikplqae fdrierlknm kdlqreiahl hqigvdvffs fgsmqdfkns eemigaamqg
      181 glglpdrdyy lkedrkfkqi rdayvnhvak mfellgdspd kaaaeantvm kletqmakvs
      241 msqidqrdph aiyhimnqak lmtvtpdfsw pdyfsaigqa qiksinlamp dffkdmdkql
      301 ksvslqdwkt ymrwhlidaf asflsqpfvd qnfkmaavlt gtekilprwk rvvrtensal
      361 gfaigkmyve ryfssedkkq aleilknira vlrediqtls wmtpatrkaa lkkldmmedr
      421 vgypskwwdy sklkidrgpy vlnviranef linrdlnkig kpidrsewvm tpqtinayyd
      481 psmnnlnipa gilqspffds napaavnyga igfvmghemt hgfddqgaqf dghgnlknww
      541 tpsdlekfkk atqcivnqys qyvvdgdlhv qgklvvgeat adlggitlay rafkrskeyk
      601 naptiagltp eqqfflstah vwalnirpqq lrnqvttdph ppaeyrvngs lanipqfqea
      661 fnisndspmv nknrcviw
//
LOCUS       WP_010654703             369 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Fluoribacter dumoffii].
ACCESSION   WP_010654703
VERSION     WP_010654703.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..369
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42701
     Region          7..>365
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mrslknllnr igyadpmdry arqyrliwyi sleliaicli liflyslmql whmvvlfssg
       61 icialinlwv lsrtantffc ghlitliafi iiclvnymiw gigtlhnqwf yiipllaaal
      121 vgrsgliiys ilsffmilgf stfslppfyn lpyhkleiie wgnhllayli vvttlvnlly
      181 ehdkyerklt dlnyllqsek dkyhylarvd qltnlpnrry fnqylqevis slssnycatl
      241 ffidldnfky vndcyghnig dhllleasrr lkisfregdf iarvggdeft aivlhtiddq
      301 ipqliaqrii qefdreikfg eielncpvsi gfatypidvh gvtdlmikad ramyaakkik
      361 gssyckaea
//
LOCUS       WP_010654773             157 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Fluoribacter dumoffii].
ACCESSION   WP_010654773
VERSION     WP_010654773.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..157
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=18097
     Region          18..>113
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mnmltrfkff lwkfshfkvp mlgylkpkli kltdteivvk lpltrrsrnh lnsmyfgalc
       61 vgadlagglh gfyhaaqkql kfslvfksfq aqflrrpead vyficqegtk vkamleesqk
      121 trervtqpiq iraytdypgl telvaefvld lsvkirs
//
LOCUS       WP_010654848             363 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu, partial [Fluoribacter dumoffii].
ACCESSION   WP_010654848
VERSION     WP_010654848.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     gene            1..>363
                     /gene="tuf"
     Protein         1..>363
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
     Region          1..363
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makekferkk phvnvgtigh vdhgkttlta aittimakkf ggtakaydqi daapeererg
       61 itistahvey esanrhyahv dcpghadyvk nmitgaaqmd gailvvsaad gpmpqtrehi
      121 llsrqvgvpy ivvfmnkadm vddpellelv emevrdllss ydfpgddipi vvgsalkale
      181 gdesdigvka ieklvetmds yipepvrnid kpfllpiedv fsisgrgtvv tgrvesgivk
      241 vgeeieivgi rdtqkttctg vemfrkllde gragdnvgil lrgtkrdeve rgqvlakpgt
      301 ikphtkfeae vyvlskeegg rhtpffngyr pqfyfrttdv tgtcdlpsgv emvmpgdnvq
      361 lti
//
LOCUS       WP_010654902             150 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Fluoribacter dumoffii].
ACCESSION   WP_010654902
VERSION     WP_010654902.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..150
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17046
     Region          4..>146
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mnktiyivdd ddnvlsalkw lfesmsfdvk tflnaksfle qynpqhvgcl itdvrmpdmd
       61 glelfdllkk qncllkviii taygdipmav raikggaidf itkpinesdl lklikkcleh
      121 ypnlttnamn tyellserel qaleliwtns
//
LOCUS       WP_010654889             140 aa            linear   BCT 01-JAN-2025
DEFINITION  HIT family protein [Fluoribacter dumoffii].
ACCESSION   WP_010654889
VERSION     WP_010654889.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..140
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15706
     Region          3..134
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 masecvidli vakkesafiv fededfiafl dsrplfpght llapkqhikt lydvpdslvs
       61 plftltqkig kaiekamgaa gsfiamnntv sqsiphlhih ivprnrhdgl kgffwprthy
      121 kdeqhmhevq eqikhqlalg
//
LOCUS       WP_010654905             305 aa            linear   BCT 01-JAN-2025
DEFINITION  pirin family protein [Fluoribacter dumoffii].
ACCESSION   WP_010654905
VERSION     WP_010654905.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..305
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34377
     Region          27..285
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msyfkakdpi catqncpqqi rmeliprsvd lggfqveril pskekrtvgp fvfwdqagpg
       61 elltskgidi rphphiglst mtylfsgrle hrdtlgshqi itpgevnlmt agrgiahser
      121 tplpdrlypq pffgiqcwla lplnkeetdp sfthydksai paldeekmsi rviagewmgh
      181 kssvntqida ffiecklkth aelvipstle eraihllcgk iiidnifykd prmlilkpga
      241 klkviaasdv hmiilggppl eerrylwwnf vasskekieq akldwkegkf gkipgddkef
      301 iplpn
//
LOCUS       WP_010655006             147 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Fluoribacter dumoffii].
ACCESSION   WP_010655006
VERSION     WP_010655006.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..147
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16444
     Region          8..111
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mekaklvgin hvalevgdve qalefyskif nftlrsktqn hafidlgdqf ialmkssssh
       61 edkirhfglv vddasqvkel akkagaelig grfldfrdpw gnyiqiieya diqftktaev
      121 lagmnlhlqk nqtvlkelae kgmaprh
//
LOCUS       WP_010655109             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease [Legionellaceae].
ACCESSION   WP_010655109
VERSION     WP_010655109.1
KEYWORDS    RefSeq.
SOURCE      Legionellaceae
  ORGANISM  Legionellaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Legionellaceae"
                     /db_xref="taxon:444"
     Protein         1..190
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22636
     Region          <16..68
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 matyrtykpr lridfnyscg yckanepeig gaknsfqidh yqpkkefpel innyenliya
       61 cracnqykgd ywptpfesll qkiilnprvd nlekhidlrn fewmaktlrg kwnilklrla
      121 sephitrrkd rakiqqmikk lldkiptfqk eildletkgd ilncqklrqe yeehledint
      181 lkrkiegpme
//
LOCUS       WP_010655294             146 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Fluoribacter dumoffii].
ACCESSION   WP_010655294
VERSION     WP_010655294.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..146
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16887
     Region          1..130
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mnylhtmirv tdlkasldff ckklgliein rienekgrft lvflaapndl drakqlktpm
       61 leltynwdlq eykegrnfgh layrvdniye lcqrlqdagv vinrpprdgy mafirspdni
      121 siellqkgep lplqepwasa pnvgyw
//
LOCUS       WP_010655359             161 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Fluoribacter dumoffii].
ACCESSION   WP_010655359
VERSION     WP_010655359.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..161
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=17830
     Region          5..>56
                     /region_name="DnaJ"
                     /note="DnaJ-class molecular chaperone with C-terminal Zn
                     finger domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0484"
                     /db_xref="CDD:440252"
ORIGIN      
        1 mnqydalkvl glsgqvsqdd ikkaykkacs kfhpdrnpag leimkminva yealknfdgi
       61 ahvtsdaaly gdevanalnq ictlglilei cgawvwvsgn tkphkdtlka agfkwapkke
      121 cwyfrpadam rsrsfgkysm nairekygsv hvsqkeqarl a
//
LOCUS       WP_010655313             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Legionellaceae].
ACCESSION   WP_010655313
VERSION     WP_010655313.1
KEYWORDS    RefSeq.
SOURCE      Legionellaceae
  ORGANISM  Legionellaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Legionellaceae"
                     /db_xref="taxon:444"
     Protein         1..304
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34056
     Region          1..>232
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkvittagnk ggigkstial tlaqylakck nmkgafidld pqgnssssli pttrdpahpt
       61 gympkahpew dpnnlpeddp hwdgvssiad ifigksiypy ptwvdnlhcf psfaslleda
      121 qrvlkvdvke kvinrlkeft emlsthsdyq fviidtnpqf gpltmaglra athgllptel
      181 eqygingtig miqaisqeql rrvkddtiki agilpnqvrk tavhtkflnd lrsiekseew
      241 llppiaqrti yselvvedak pncvfnlpqt hlariesekw csyvydrvfh nvynkieeke
      301 asyg
//
LOCUS       WP_010655441             152 aa            linear   BCT 01-JAN-2025
DEFINITION  regulatory protein RecX [Fluoribacter dumoffii].
ACCESSION   WP_010655441
VERSION     WP_010655441.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Ragone,S., Maman,J.D., Furnham,N. and Pellegrini,L.
  TITLE     Structural basis for inhibition of homologous recombination by the
            RecX protein
  JOURNAL   EMBO J 27 (16), 2259-2269 (2008)
   PUBMED   18650935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..152
                     /product="regulatory protein RecX"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /calculated_mol_wt=17574
     Region          6..149
                     /region_name="RecX"
                     /note="SOS response regulatory protein OraA/RecX,
                     interacts with RecA [Posttranslational modification,
                     protein turnover, chaperones]; COG2137"
                     /db_xref="CDD:441740"
ORIGIN      
        1 mntlidaaik ylsnhycsek elirqlerdf shvpeleaqi hativrlrel hlindnrlae
       61 slsaryihkg nrfiqqilkq kgvkeevieq ilehieleev raldearkkm rgfkndtdea
      121 intklarfls grgfshatik tvlkqlseeq tt
//
LOCUS       WP_010655489             464 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Pseudomonas].
ACCESSION   WP_010655489
VERSION     WP_010655489.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..464
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52469
     Region          1..>393
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 msmglrtwqd qckntalaqy letphffcqa tpgagktrma aelakalldq gridlvlcfa
       61 psrqvvegfr rtfsdvlsrr ldgligavga vctyqgmeyr detfwklfdd yrvfavfdei
      121 hhcaghdall snawgqriiq rvqdraaytl alsgtpwrsd qkaivlarys tpegnlicdy
      181 rygleeaisd evcrsprivi ldntmvrlte aiesdntvtv fpniaslltd spvtyesllf
      241 hedvlrqlll lgcrklkeir nvkpdagglv vatniehahq vaamlrlege scdvvtnktp
      301 naqrvindfr hsnrpwivav gmisegtdip rlqvcchlsr irtelyyrqv lgrilrrsas
      361 ndteawlyvl aepslqqfse rvaddlprdv avlnylqgvs eevaaspven sadqynchpv
      421 tpfqgecfer esqqlpdeiy sydvgrtyel nfsqhyrtql lrvc
//
LOCUS       WP_010655404             100 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Legionellaceae].
ACCESSION   WP_010655404
VERSION     WP_010655404.1
KEYWORDS    RefSeq.
SOURCE      Legionellaceae
  ORGANISM  Legionellaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Legionellaceae"
                     /db_xref="taxon:444"
     Protein         1..100
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11497
     Region          <24..94
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
ORIGIN      
        1 milnnkpkml dttiiennwr srgfsfelwe dppgqiwkdf rhetdelfml legeviltvg
       61 nktlkpaige evlipagvdh tvqtssttgs rwyygykirr
//
LOCUS       WP_010655518              66 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010655518
VERSION     WP_010655518.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 66)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 66)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..66
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6702
     Region          1..61
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mfildvsgig cggcvskitk aiqsldnkat isvdrsagkv svessesseq irkavealgf
       61 psqist
//
LOCUS       WP_010655648              94 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [Pseudomonas].
ACCESSION   WP_010655648
VERSION     WP_010655648.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..94
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11107
     Region          2..91
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mlkviaedfi khehletvrp wyaelvektr lepdciaydl yvdhqdpghf ifveqwpdqa
       61 aldahcqseh frrlvpqina cqsqecrfmf mnaf
//
LOCUS       WP_010655754             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Pseudomonas].
ACCESSION   WP_010655754
VERSION     WP_010655754.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..207
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22519
     Region          <21..194
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlkrfaplvp lalvtllfgc aahtpvsqqv vqqqvqkpsa sqasavyqee latekelaqf
       61 sanskpyelp aladsilerg msligtryrf ggtseagfdc sgfigylfke eagmqlprst
      121 reminvkapl varnnlkpgd llffstngrg rvshagiylg ddqfihsssr rsggvridsl
      181 gdtywnktfm eakralamap tnvvark
//
LOCUS       WP_010655855             633 aa            linear   BCT 01-JAN-2025
DEFINITION  acyltransferase family protein [Pseudomonas paraversuta].
ACCESSION   WP_010655855
VERSION     WP_010655855.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas paraversuta
  ORGANISM  Pseudomonas paraversuta
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Pseudomonas paraversuta"
                     /db_xref="taxon:2750624"
     Protein         1..633
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=70213
     Region          1..327
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          384..628
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 mefrnninal ralavisvvl fhfkvqgfgg gfagvdvffv isgflmtgii ftglqtqrfs
       61 llgfyasrar riipalltlc iallifgfvf lplddyrdai rtlkssllfs snftfakggs
      121 yfdaplhenw llhtwslsve wqfymlypll lmalykfvga kntrstlvll alisfaasvv
      181 ltrtspvfaf ymlptrawem iagglvflyp lqlgkrsssi ceglglvail asvmcfseqd
      241 qwpgylallp vlgtalviyg ntqsafstnr alqytgkisy svylwhwplv vllytcgllt
      301 swpyvtgaii lsfvlgalsf ylvesransa tsatktiiky asyalgaval savtssvvkd
      361 ypgvrfafvd lgqpaysgtl ysqecfpndy aaadcklgtg evsvilfgds haqstaaavq
      421 lenkqaalsw arggcptlqn femrdkelqr qcqafnqekl evlknsykgi pvvlfsraal
      481 ywdqsrnnkh riffpeakdp dgssfvetyt akyidvvcsi aqnhpvyivk pipempfsvy
      541 kglnlhrrif qhttdisipl heyekrnria itaietaakr cnatvvdptp ylcpdgkcmg
      601 srdgvplyyd dnhlvdagne qlkglfkdvf kgi
//
LOCUS       WP_010655866             295 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Pseudomonas].
ACCESSION   WP_010655866
VERSION     WP_010655866.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..295
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31695
     Region          5..294
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mstsnihgii gytitpftad geqidlsalg rsidqlidsg vhaiaplgst gegaylsdae
       61 wdqvsqftla hvakrvptiv svsdlttaka vrrarlaeqy gadvvmvlpa aywklseaei
      121 lahyraighs istpimlynn patsgtdmsv elilrifnav envtmvkest gdiqrmhrlq
      181 qlgegqipfy ngcnplalea faagakgwct aapnlipaln lglyeavlan dlktarelfy
      241 rqlpllqfil kgglpatika glrltgieag dprlpvfpls esavsqlqqi lktlr
//
LOCUS       WP_010655995             311 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Pseudomonas].
ACCESSION   WP_010655995
VERSION     WP_010655995.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..311
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33610
     Region          4..218
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 msdlilhhya aspfaqkarl llgfkglswh svhvppmmpk pdltalsggy rktpvlqvga
       61 dvycdtalia rrleqeksip alfplgqemv vsafaawads vvfqhavslv fqpesaavrf
      121 akmppdmlka fvadraalfs ggsatripae qavlqwpvim grleqqlqhe qgdylfgeps
      181 iadfalahsl wflkatpvta plvdaypava awlqrvldfg qgtpieitae qalaiakgve
      241 pvalpefdsa fgfskgqrvt vaatdygvdp vagelvhiga eelvvrredp rtgvvhvhfp
      301 rigfrieavg q
//
LOCUS       WP_010656022             136 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010656022
VERSION     WP_010656022.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..136
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15255
     Region          1..109
                     /region_name="HTH_MerR2"
                     /note="Helix-Turn-Helix DNA binding domain of MerR2-like
                     transcription regulators; cd04769"
                     /db_xref="CDD:133397"
     Site            order(2..4,18,34..36)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133397"
     Site            order(48,51,55..56,65,83,87,93,97,100..101)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133397"
ORIGIN      
        1 myigkaaqrs gttiksirhy edigllpppq rrgnyrvyse qsverlmfik caqqlgfklk
       61 emlaildehh gqalpwdvvr naitdkkqsv leqiqalhnq haglvafetr flaadqscqa
      121 snlleqpvda rllama
//
LOCUS       WP_010656116             439 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010656116
VERSION     WP_010656116.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47145
     Region          26..421
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,158,
                     161..162,165,256,259..260,263..265,268,296,300,358..359,
                     362,366,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnlktsapas stladhadas rpttvrwrif lillllsain yidraslsva mplisaefem
       61 tpaleglmls affwsyalmq ipggmlldrf qvrnivgvat vgwgffqaia ggahswitll
      121 atriglgvae spimpagakl ngawltpner grgatlvdgg aplgtafgai iiaglitwfd
      181 swriafviag vgtmivgvwa wwyirnspae hpkvnaaela yitdanaeaa rthgerkail
      241 kdllksrsvl amfagyacyn svfyglltwm psylhkahnl dikamggatf lifmcgfige
      301 ifggwladkw kdaggapnkv mrcmfggsaa iaalcillva ytpdavtvis llcvalffir
      361 wcgmywclpa ilggkskagv lggsmnfcgn mvgvivpili glivqftgsy flaliffvvm
      421 afglmlfssl idyrergla
//
LOCUS       WP_010656140             398 aa            linear   BCT 01-JAN-2025
DEFINITION  XdhC family protein [Pseudomonas sp. TMW22089].
ACCESSION   WP_010656140
VERSION     WP_010656140.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. TMW22089
  ORGANISM  Pseudomonas sp. TMW22089
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Pseudomonas sp. TMW22089"
                     /db_xref="taxon:2506433"
     Protein         1..398
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=42344
     Region          7..368
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 msdlygllda ldqadsnnva vvlatvvkve gsayrrpgar mliprdgqav gtvsggcleq
       61 elvrkawwlt esglpvirry staahdedds deegaaltfg lgcngtvhvl lerleagaps
      121 lltdvlqgvr atgqpaalat vlaagagsga rmgarlglta lsrssqgfcc dvlesrvqad
      181 llatlerkks srmiyasgaq avevlleyip aqrrlvvfga gndaqplvrf avqlnwqvhv
      241 vdgranfara erfagarevl vasidqpfal rtlvdgaavv imthsyrqdr fwlqsvlaca
      301 payigqlgpk erterlldem gggaaaarae lhypmgldlg gdtpqsvala ivseitacln
      361 qreggmlrlr karihdpada qhaalsarsp eardarrq
//
LOCUS       WP_010656461             422 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [Pseudomonas].
ACCESSION   WP_010656461
VERSION     WP_010656461.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..422
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47612
     Region          84..401
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 metqtlwtqi qdlyanldqh pwvstilgli vlvsiallag hvariiilri tkilgrqpal
       61 hwisdlrqhk vfhrvaqltp slmvqfgrnl ipemsetgrh flgnlalait ifvltrvisa
      121 lldalldiys rtnyaktrpi kgyiqltkml lyvfsaiiiv atlidrspml llsglgamsa
      181 villvykdtl lsfvasvqlt sndllrvgdw iempqvgadg dviditlhtv kvqnfdktiv
      241 siptwrlmse sfknwrgmqq sggrrikrsl fidagnigfl tdeqeqrleq vrllsdylhr
      301 kqaelkswne aqgnvaalsa nrrrmtnigt frayalaylk shpeiqpnmt cmvrqlqpta
      361 qgvplevycf trttvwsdye qiqgdifdyl lsvmpefgls iyqqpsgndl rnglmpaltk
      421 da
//
LOCUS       WP_010656517             166 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Pseudomonas].
ACCESSION   WP_010656517
VERSION     WP_010656517.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..166
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17876
     Region          29..154
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mttqlgcslq dsaapegvcf gcgtsnvhgl hvksfwhedg vhviaehlpd akycgwpdlv
       61 yggliamlvd chsnwtamaf hyraqqrevd slprincvtg nlgikfikpt pmgvpltlra
      121 rvegevgrks rvicevyagd vltavgdsif vrvdtaelas qahgrv
//
LOCUS       WP_010656560             367 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkene reductase [Pseudomonas].
ACCESSION   WP_010656560
VERSION     WP_010656560.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..367
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39790
     Region          10..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(29,31,62,104,232,302,322,324..326)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(29,31,62,104,106,113,180,183,185,232,239,302,322,
                     324..325)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(31,106,180,183,185,325)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            185
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtdnatrtdl ftpinlgamk lanrilmapv trsryaedgi pnelhaeyya qratagliva
       61 eatnisaqgr gyaatpgiws eeqvagwkkv tdavhaaggk ivsqlwhvgr fssvelqpdg
      121 aapvapsaik aegdtyttng fvpvsmpral etdeipgiie qykraaenak ragfdgvevh
      181 sansylldqf lrdstnhrtd qyggsienra rltlevteai vkiwgndrvg irlspvtpda
      241 gntppdsnvm amygyliqql nafdlaylhf vegatatsrd vpegvdmdal saqfngpfig
      301 nnnydldmai erraqgkida vafgrlfisn pdlverlrrg aeltiapres yygggakgyt
      361 dwpvgny
//
LOCUS       WP_010656734             388 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [Pseudomonas].
ACCESSION   WP_010656734
VERSION     WP_010656734.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 388)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 388)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..388
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42889
     Region          1..383
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mlttlavany rsinqlvvpl arlnlitgpn gsgksnlyra lrllaetaqg gvinavareg
       61 glestfwagp evisrrmklg evdisrtvls gvkrlrlgfa addfsyaial glppndetss
      121 fnldpqikhe siwsgpiyrk aselverkgp vvrsrdgraw kvlaqhtpvf dslfdqvgsm
      181 daspevlqlr esirgwrfyd hfrtdpdapv rqpqlgtrtp vlhhdgrdla aalqtiieig
      241 dpqalhtais dafpgarlei qfvsggrfal efyqegllrp lsvaelsdgt lryllliaal
      301 ltprpptmmv lnepetslhp dllpalarli irasqqsqvw vvsharrlia alqqdlecnc
      361 ivleknfgqt eivgqrlldq pawywadk
//
LOCUS       WP_010656754             381 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010656754
VERSION     WP_010656754.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..381
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40055
     Region          9..368
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(16..17,20..21,24,56,106..107,109..111,114,134,
                     137..138,141,209,212..213,216..218,221,245,249,298..299,
                     303,307,323,326..327,330..331,334)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mrwatyfavl asvlsvglal gvsmplvsfr leswgyggfa igvmaampai gvlvgaslas
       61 klasrfgtpa lmrlclwcga lsigllallp sypvwlvlrl ligvvltiif ilgeswinql
      121 vveqwrgrlv alygsayals qlsgplllgl vgsegdygfw igvalltlap lllmgrdgap
      181 vteaysvtfk dllefcrglp aiawavglfa afeamiltll pvyclrqgft adialamvst
      241 vvvgdallql pigaladrls rrslftgcav llmlsslavp lllntlliwp lwvifgasag
      301 glftlslili geryrddalv ranahiaqlw gigcligpla agagsqwisg halplfmaag
      361 alvlvilvlr qgafgaeqta a
//
LOCUS       WP_010656765             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Pseudomonas].
ACCESSION   WP_010656765
VERSION     WP_010656765.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..256
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27580
     Region          21..256
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkklfaavaa vaafsahagd lsvaatpvph aeilefvkpa lakegvnlkv kvftdyiqpn
       61 vqvaekrlda nffqhqpyld efnkakgtnl vsvaavhlep lgaysskykk lddlpngatv
      121 vipndatngg ralllldkag liklkdssni lstpkdieqn aknlkfrele aatiprvltq
      181 vdlalintny aleaklnpek dalviegsds pyvnilvarp ddkdsadmqk lvaalhspev
      241 kafinekykg aiipaf
//
LOCUS       WP_010656785             529 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Pseudomonas paraversuta].
ACCESSION   WP_010656785
VERSION     WP_010656785.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas paraversuta
  ORGANISM  Pseudomonas paraversuta
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Pseudomonas paraversuta"
                     /db_xref="taxon:2750624"
     Protein         1..529
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57937
     Region          6..528
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msqvfdadvi vvgsgalgsn aafelakqgk sviileages iprwkivenf rnssnksnyn
       61 spypnepwar hsydeqyien igsfefrpgm lklvggttwh waaacwrylp ndmklntlyg
      121 vgrdwpmeys elepyyarae valgvcgsdt qdqsghdgea fpprstpypm ppegdtylfq
      181 rlrarlapag yvflhepngr atmpyddrpa csgnnncmpv cpigamysgd vharhaqqag
      241 arlltdatay klekgeggki vavhyrsskg dnvrltakyf vvaangletp klllisevan
      301 ssdqvgrnlm dhtgqglqfl adepvwpgrg avqqggifnr rdgafrkera svkhafannv
      361 pnmavanrli eqgifgkeld erirhdsarw vdvstvyetl plasntirps ttrtdalgip
      421 mmvinyevgd yvkaakpgvd adyadfvkvm ggtvvedntg wqnrdhlmgt vimgtdakds
      481 vvnhecrtfd hpnlflattg vipasgtinp tltgvalsir vadiiarev
//
LOCUS       WP_010656794             694 aa            linear   BCT 01-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Pseudomonas sp.
            9.1(2019)].
ACCESSION   WP_010656794
VERSION     WP_010656794.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. 9.1(2019)
  ORGANISM  Pseudomonas sp. 9.1(2019)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Pseudomonas sp. 9.1(2019)"
                     /db_xref="taxon:2580568"
     Protein         1..694
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=74851
     Region          11..662
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msdsllprcg ftgppgssal lfaglhgheg lselfeyrvk vlspegelna ddwlgkalgl
       61 elhhsaqnsp ssrkvhghvc gfrrlgdegr fpcyefllrp wlwfascasn crifqnqsvl
      121 evlkavlapy pgevewaate syaaleycvq faetdaafvs rlmeeaglyy ffrhsgeghs
      181 lvvtdsmseh rsleagdtly wrmgsddnfh slwdwvpqqa lcsgrvsaad fdfskantre
      241 asvlaaaasi aaghdqagfe hyrypghfnn sasgeaatkv rvqalhalrq rvgatgcapy
      301 llpgctfkls ghadpgqnae ylitratlta tcrvsstgvs apsfscdiea igsnaryrap
      361 vqtprprmpg pqtafvvgka geqlwvdefg rvkvqfhwdr geqtdencsc wvrvaqplag
      421 qrwgaiflpr igqevivefl dgnpdrplit gslynggmrp phelpaqvar sgiksqslga
      481 rdvynelrfe drdgaeqllf hagrnqdvtv rndalehvgn drhvkvggns fqqvlkdahq
      541 hlggefnvyv agghslevvg drsikvgagy smetgadhrf kvagghslev agdsdtkvgg
      601 kfrlgaasvd lkgsqtltle agqtltlkag sstlvlgpkg vaingalvti dakgkvding
      661 ggdssadpae apqpiptqkp qmpkqpeead hgrd
//
LOCUS       WP_010656950             545 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Pseudomonas paraversuta].
ACCESSION   WP_010656950
VERSION     WP_010656950.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas paraversuta
  ORGANISM  Pseudomonas paraversuta
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Pseudomonas paraversuta"
                     /db_xref="taxon:2750624"
     Protein         1..545
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58576
     Region          2..444
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msgkgkfkkq lslidltfig lgaifgsgwl faashvsaia gpagifswll ggfavlllgi
       61 vycelgaalp raggvvrypv yshgpllgyl mgfitliafs slvaievvas rqyaaawfpg
      121 ltqagsnspt vigwlmqfgl lclffmlnyr svktfakfnn lvsvfkfivp llvigvlftf
      181 fkpanfevhg fapfgmagie mavsaggvif aflgltpiis vasevqnpqr tipialilsv
      241 llstaiyvll qtaflggvpt emlvngwtsv skelalpyrd ialalgvgwl aylvvadavi
      301 spsgcgniym natprvvygw aktgtffkif trideksgip rpalwltfal svfwtmpfps
      361 wealinvvsa alvlsyavap vsvaalrrna pdmprpfrvk wmavlgplsf viaalivyws
      421 gwntvswllg lqiamfvvyl mcgrfvptwh lnlaqqvrss mwligfyavt ivlsklgsfg
      481 gmgvlthpfd nlvvatcalg iyywgaatgv pahlvrlede deddeqvvhq aaahsahpag
      541 ayaga
//
LOCUS       WP_010656983             284 aa            linear   BCT 01-JAN-2025
DEFINITION  glycine betaine ABC transporter substrate-binding protein
            [Pseudomonas sp. TMW22089].
ACCESSION   WP_010656983
VERSION     WP_010656983.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. TMW22089
  ORGANISM  Pseudomonas sp. TMW22089
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pseudomonas sp. TMW22089"
                     /db_xref="taxon:2506433"
     Protein         1..284
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30659
     Region          29..283
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(38,40,86,114,143,147..148,193)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mkmrrilsag aalvlamsag lanaqskptl nigyvdgwsd svatthvaae vikqklgydv
       61 klmpvatgim wqgvatgkld amlsawlpvt hgeywaknkd kvvdygpnfk dakiglivpe
      121 yvaaksiadl kddagykkki vgidagsgvm lktdeaikdy gldyklqass gaamtselgr
      181 ayaknepivv tgwvphwmfa kwklrflddp kgvygaaetv nsigskeldk kapevaaflk
      241 kfawnskdei gevmlaiqeg akpeaaakew vakhpervae wtak
//
LOCUS       WP_010656997             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Pseudomonas].
ACCESSION   WP_010656997
VERSION     WP_010656997.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..144
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14549
     Region          7..144
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mskliqtvlg tragygltvl rvfvgiifaa hgsqklfgwf gggglagtaq wmesigltpg
       61 tlmallsggt effgglaliv gllarpaalg lsftllvaif svhihnglfm anngyefala
      121 llggtvavll egagklsidg aiak
//
LOCUS       WP_010657175             156 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: arsenate reductase ArsC [Pseudomonas].
ACCESSION   WP_010657175
VERSION     WP_010657175.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..156
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=16802
     Region          2..135
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(7,9..14,104,106)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mrilfmctan scrsilseal fnhlapqgfe avssgslpkg qvlprslstl qqagisidgl
       61 yskgndafeg hppdivisvc dkaagescpv yfgpalkshw gledpsevtg defaidaafr
      121 atlahierrc kaflelplnr lsrdelktel drigvl
//
LOCUS       WP_010657398             323 aa            linear   BCT 01-JAN-2025
DEFINITION  FecR family protein [Pseudomonas paraversuta].
ACCESSION   WP_010657398
VERSION     WP_010657398.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas paraversuta
  ORGANISM  Pseudomonas paraversuta
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Pseudomonas paraversuta"
                     /db_xref="taxon:2750624"
     Protein         1..323
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34861
     Region          15..52
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          77..316
                     /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"
ORIGIN      
        1 mdsrdctgds asvrdaaatw farvqaqsls paeqaefeaw rardasheae yqwlaslwsa
       61 tdllpkarlq alcelpdrap krrsvmawgl aaslllalga glslqwqepg ayhgefstla
      121 geyrevqlpd gssielnsrs rvkvsfegqq rrveleqgev mfsvahdtsr pfvvragagq
      181 vtvtgtrfdv rrdgdqarva vesghvrvqg sdasgavslt aglgtrvdaq gqvdaplavd
      241 traltawrtg qlqfndasla qvaaevsryr qqplhvtdpa varlrltsvf ktadtdallk
      301 alprilpvai ntradgsqei var
//
LOCUS       WP_010657423             380 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010657423
VERSION     WP_010657423.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..380
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42423
     Region          19..380
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mavasgaykk alegdhtpkq vlvkidrvtk kfdetiavdd vsleinkgei famlggsgsg
       61 kstllrmlag ferptegrif ldgvditdmp pyerpinmmf qsyalfphmt vaqniafglk
      121 qdkmssseid arvgemlklv hmtqyakrkp hqlsggqrqr valarslakr pklllldepm
      181 galdkklrsq mqlelveiie rvgvtcvmvt hdqeeamtma qriaimhqgw iaqigspidi
      241 yetpvsrlvc efignvnlfd gevvddaegy arincpelen diyvghgvst svedkhttya
      301 irpekmlvtt ekptceynws rgkvhdiayl gghsvfyvel pggkivqsfv anaerrgarp
      361 twddevyvww eddsgvvlrs
//
LOCUS       WP_010657504             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010657504
VERSION     WP_010657504.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..256
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28494
     Region          185..250
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mekpstpsla ivrqleavgf rawpatsvhy dgtwairmta ahpsrrlnsi npldpgdtrd
       61 iptrvelaaq rfraygrvpc frlsplapre ledyleglgw krrdetivmt anleeldlsd
      121 aidqiplkdi grfvdaslsi herpedmrpg fsellnsvrp nkgmfvleeg gravsnllcv
      181 qdgvmaglfd vgtlrdarrk ghghaivgsa lkwavklgak tawlqieadn vaglalyesf
      241 gfreayryay resnek
//
LOCUS       WP_010657527             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Brucella].
ACCESSION   WP_010657527
VERSION     WP_010657527.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..206
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22004
     Region          1..204
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslevwlafs aasivllvip gptvllvvsy algqgwkaaf pmavgvalgd ftamtlsmlg
       61 vgallaasat vfttvkwaga ayliwlgikl fraggtlhas arhdkvhpar mlvhawlvta
      121 lnpksitffv aflpqflsph rdfltqmlvf estflvlafl nafayallat rarrffsser
      181 alrifnragg tlligagvat asmrst
//
LOCUS       WP_010657556             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: EVE domain-containing protein [Brucella/Ochrobactrum
            group].
ACCESSION   WP_010657556
VERSION     WP_010657556.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Bertonati,C., Punta,M., Fischer,M., Yachdav,G., Forouhar,F.,
            Zhou,W., Kuzin,A.P., Seetharaman,J., Abashidze,M., Ramelot,T.A.,
            Kennedy,M.A., Cort,J.R., Belachew,A., Hunt,J.F., Tong,L.,
            Montelione,G.T. and Rost,B.
  TITLE     Structural genomics reveals EVE as a new ASCH/PUA-related domain
  JOURNAL   Proteins 75 (3), 760-773 (2009)
   PUBMED   19191354
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..144
                     /product="EVE domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=16389
     Region          2..137
                     /region_name="EVE"
                     /note="Predicted RNA-binding protein, contains EVE domain
                     [General function prediction only]; COG2947"
                     /db_xref="CDD:442190"
ORIGIN      
        1 maywlfksep fkwswemqka rgekgeqwdg vrnylarnnm ramklgdkgf fyhsneglev
       61 vgivevcala hhdsttddpr wecvdiravr dmpkpvtlkd vkanpklekm alvtsmrlsv
      121 qpvtedewie vcrmggldak sala
//
LOCUS       WP_010657541             302 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YdcF family protein [Brucella].
ACCESSION   WP_010657541
VERSION     WP_010657541.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..302
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33517
     Region          103..283
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mktfsdtdaf ktrfssaspt srrnagydgr rdgtripqal sgghrssdda vaqrqtangf
       61 ssgdvvwrrs rngahlqsla lasgnflwsv mmrmfrrlqp vsivlfvill aflvgfvafg
      121 ekvtsmqppa idepadaiiv ltggqsriqa avdllkdkrg krllisgvhp atnekalqra
      181 thadqslfdc cvdldrsaln tignateser wirtnnyrrv ilvtnnyhip rstlemsyrm
      241 kdvefipypv vngdrrehsw vsegdtlrvl fieyvkylga avrvgttelf gtqtnqgvtt
      301 en
//
LOCUS       WP_010657633             333 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Brucella].
ACCESSION   WP_010657633
VERSION     WP_010657633.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..333
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34962
     Region          3..331
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 makwgligas tiakewviga iratggevvs vystnaarge tyarengiac svtsldalls
       61 dpeidavyis ttnelhrdqa iaaakagkhi lcekplaltl sdahqmlkav reagvvagtn
      121 hhlrnaashg amrdaiasgr igkvlgarvf havylpphlq gwrierpdag ggvilditvh
      181 dadtlrfvlg enpvealafs qqgglsgegl edgvmgvlrf ssgviaqfhd afttkyaetg
      241 feihgsegsl iarnvmtqkp vgtvilrdkd geyelpldqk nlyetalqaf hnaiagkgqp
      301 satledgiws latglavlea aktgkatavh sgl
//
LOCUS       WP_010657705             203 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Brucella].
ACCESSION   WP_010657705
VERSION     WP_010657705.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22385
     Region          6..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvprgrprsf drdaaldkvm kvfwakgyec aqindfttai gitppsfyaa fgnkeqafre
       61 avdyyrrtig tapfdalena ttiqdglrqw leqsadsafa cpaggcmisv ssiqckpenv
      121 pvkeflqair hanherlskr lqqavgagdl psnadtaqmt efyhmiqqsi sfeardgnsr
      181 aavqkiidma mmalpartrq aae
//
LOCUS       WP_010657645             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Brucella/Ochrobactrum group].
ACCESSION   WP_010657645
VERSION     WP_010657645.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..265
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28594
     Region          6..260
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mnkmsriiti anqkggvgkt ttainlatal aaigetvliv dldpqgnast glgidrrnrp
       61 lssydvltqe ssvpdaampt dvpnlhivps tldllgieme iaqsadrtrr lrdalrfdss
      121 vserfsyvlv dcppslnllt lnamaaadsv lvplqceffa leglsqllqt vdqvrssina
      181 elsiqgivlt mfdsrnnlaa qvvddvrafm gekvyrtvip rnvrvseaps hgkpailydl
      241 kcagsqaylq laseviqrer qlqaa
//
LOCUS       WP_010657799             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CpaD family pilus assembly protein [Brucella].
ACCESSION   WP_010657799
VERSION     WP_010657799.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..239
                     /product="CpaD family pilus assembly protein"
                     /calculated_mol_wt=25752
     Region          30..230
                     /region_name="CpaD"
                     /note="Type IV pilus biogenesis protein CpaD/CtpE
                     [Extracellular structures]; COG5461"
                     /db_xref="CDD:444212"
ORIGIN      
        1 mtysvrgfcr isarpalval slallagcan rqhvtvgalp ddyrtnhpit iaereqvtdi
       61 pvaqadqkls pmqrgivqga ianyrrggsg mlyvlvpsgt snqaaayrls tevsamlrrg
      121 gikanniaie nypvenpeaa apirisyyam tagttpcgrw pddlastpen khyanfgcas
      181 qnnlaaqian padllgprvm spidsdrtte rlngdqgyvk mspaqtdnwq eprskqaey
//
LOCUS       WP_010657806             202 aa            linear   BCT 01-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Brucella
            anthropi].
ACCESSION   WP_010657806
VERSION     WP_010657806.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..202
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=22101
     Region          17..>99
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mcvpkiashf secilersia mrnclrkfln dkrglgavef aliapallli ylgsvdladg
       61 vdtnkkvsrs assladlvar qlsvtkndln dmfnisrasl lpygrstpki ritairidgt
      121 arasnltpev dwsyaniadf aakkgdvgdi psslldegsy fikvdveldy rplnawists
      181 ipmsetyyla prytntlpct nc
//
LOCUS       WP_010657845             659 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acetyl/propionyl/methylcrotonyl-CoA carboxylase
            subunit alpha [Brucella].
ACCESSION   WP_010657845
VERSION     WP_010657845.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..659
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70522
     Region          1..461
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          589..654
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(611,620..622,629)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            621
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfkkilianr geiacrvirt arelgiatva iysdadaqal hvemadeavr vgpaisaqsy
       61 lnveaiikaa ketgaeaihp gygflsenag fvdaveaagl vfigpsakai ramglkdaak
      121 almekagvpv vpgyhgdnqd gsflkseadr igypvlikar aggggkgmrr vdqaadfaaa
      181 ldsarreaea sfgdsavlie kymtkprhie vqvfgdshgn avhlferdcs lqrrhqkvie
      241 eapapgmtpe mraamgeaav kaalaigycg agtvefiadv seglrpdrff fmemntrlqv
      301 ehpvteaitg ldlvewqlrv asgealpkrq delsingwaf earlyaedpa rdflpatgkl
      361 alfappenar vdsgvrtgdt itpfydpmia kiiahgatrd ealnrldasl nktriaglvt
      421 nrqflsalcn leafragdvd tgliaretaa lfadkqpsdi afalaalgal dlldapvigd
      481 pqgdpwsslr gfrlwgeasr svlidhhger htvsfttmgd rhfgfafgti eirfhenglv
      541 rfavdgrvse asvvrighdv avqlegrdti fhhvqsvgae edassesril spmpglvrlv
      601 svvegasvak gdplvtmeam kmelsltapr dgkvssvtva agdqvnegil lveleeehg
//
LOCUS       WP_010657881             298 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: lytic transglycosylase domain-containing protein
            [Brucella].
ACCESSION   WP_010657881
VERSION     WP_010657881.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..298
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30383
     Region          <139..234
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mryalsssss aglvrkglml lgcavalsac nttndgkpvk talitqtdts sqtasaagsa
       61 asatantagt atadagaaag tqtvaavsdp sdpvlpavvp ipgirgqsep mmayagaqaa
      121 aspasvaanm afetpdhape eldalitkys vaydvperlv rrvvhresrf npgarngpyw
      181 glmqishpta rgmgytgaak glldaetnlk yavrylsgay kvaggdesqa vryyargyyy
      241 dakrkgllqe tgldgswkrs gptrdaaasi qpvslpegga aplpgvapiq asyapagq
//
LOCUS       WP_010657969             229 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: outer membrane protein [Brucella/Ochrobactrum group].
ACCESSION   WP_010657969
VERSION     WP_010657969.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..229
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24191
     Region          74..229
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mklkalllas tvalvaatga kaadavieqe pvpvvvaptf twsgayiggq igygwgksdf
       61 sgdvysfgnv kpdgflggiy agynfdlgns ivlgidgdvt yndvskdidv ysgdlavgdf
      121 etklrwsgav rarvgyavdr fmpylaggva fgniknsgsi dgigsfsesk tltgwtagag
      181 vdyaatdnli vrleyrytdy gdkdiefggl nvnqdfktne vrlgvaykf
//
LOCUS       WP_010657987             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Brucella].
ACCESSION   WP_010657987
VERSION     WP_010657987.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..206
                     /product="L,D-transpeptidase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=22769
     Region          71..204
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnsrvlkltt alflagalag cstvggtfyt asyssvtdag yvvpaipsek iqaqyrrqiv
       61 kyptdeapgt iivdtrekfl ylimpegkam rygigvgreg fewsgtarva mkrewptwtp
      121 psamikrqpe lakyrngmdp glrnplgara lylynkggdt gyrlhgtpew wsigkamssg
      181 cirlmnqdim dlydrteqga kvivkq
//
LOCUS       WP_010658037             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator [Brucella].
ACCESSION   WP_010658037
VERSION     WP_010658037.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..253
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28127
     Region          25..237
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhsgkqitdp siealiglle appilaklea retdalsslt viendyaada tlieqgarvr
       61 sihlvrsgwg cvyrdlssge rqiidfpmrs dflglrtadg ysyntiaait pmsafeipla
      121 sleasierap rlsliliell arqrsmlieh ltnigcraaf vrtahlflel sdrvkscgmg
      181 dpnsfycplt qyqladalgl tpihlnrmlr dlreeglilf rsnrveildr krvvalaqyd
      241 gefmrmsvfg ktd
//
LOCUS       WP_010658166             332 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010658166
VERSION     WP_010658166.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..332
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35704
     Region          9..318
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mkkaislclg taglalalms ssamaadklt lqlkwvtqgq fagyyvakdk gfyeeenldv
       61 dikpggpdva ppqviaggga dvvvdwmpsa latrekgvpl vniaqpfkks gmmltcrkdt
      121 nitkpedfkg rtlgvwfggn eypflswmsh lkipteggkd gvtvlkqgfn vdpliqkqad
      181 cistmtyney wqvidagipa dqlvvfpyee qgvatledgl yvlekslddp amvdklarfv
      241 rasmkgwkya senpgeaadi ildndasgaq tkevqermvk eigklvdgsd gtldvaaadr
      301 tvetllgggs dpvitkkpeg awtakitdam kk
//
LOCUS       WP_010658182             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Brucella].
ACCESSION   WP_010658182
VERSION     WP_010658182.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Grant Pearce,F., Hudson,A.O., Loomes,K. and Dobson,R.C.J.
  TITLE     Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and
            Evolution
  JOURNAL   Subcell Biochem 83, 271-289 (2017)
   PUBMED   28271480
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Laber,B., Gomis-Ruth,F.X., Romao,M.J. and Huber,R.
  TITLE     Escherichia coli dihydrodipicolinate synthase. Identification of
            the active site and crystallization
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 691-695 (1992)
   PUBMED   1463470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..300
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0009436 - glyoxylate catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31695
     Region          13..287
                     /region_name="DHDPS-like"
                     /note="Dihydrodipicolinate synthase family; cd00408"
                     /db_xref="CDD:188630"
     Site            order(16,48,51..53,145,175)
                     /site_type="inhibition"
                     /note="inhibitor site"
                     /db_xref="CDD:188630"
     Site            order(48,51..53,145,175,216)
                     /site_type="active"
                     /db_xref="CDD:188630"
     Site            order(52,57..58,89..90,114..115,123,127,274..275)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188630"
     Site            175
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188630"
ORIGIN      
        1 mahnnsgqer fglsaalttp fdvdgkidvs ralkhararl dsgcssvtlf gttgegssia
       61 daervallda fiaqgfpaan ivvgvmensi adavlqsada lrrgckaill appsyfknls
      121 deglfnwfsa vfkglgsnar siilynipsv tavelsvdli grlratfgdi iigvkdssgn
      181 waytekllaa hkdiailigd erdlaagvrl ggqgaisgma nlfpdrllgm indgqddael
      241 vgavqqllny pvtpavkamv arhtgdkewr rvraplisln dadfdaigsv fdrlhmakaa
//
LOCUS       WP_010658183             220 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Brucella anthropi].
ACCESSION   WP_010658183
VERSION     WP_010658183.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..220
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25073
     Region          7..220
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 maddhnepvk lrdkayqsft qhllardfhp gqfvsqrqlv tmtglplgai reliprleae
       61 gliktvpqrg lqiahidlnl ireafqfrlf iekesiaifc qsasdellrs lraehedtln
      121 raisegetpe leeraqnidw slhdtivgsl dneiiwrayq tntikmrlin qerfritgrv
      181 ipvmqehlav laaietrdpq tamdaiavhi nnarklalqi
//
LOCUS       WP_010658235             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide deacetylase family protein
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010658235
VERSION     WP_010658235.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..233
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26587
     Region          65..220
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(69..70,135,139,175..177)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mpvpiflyhq idvppqhrtp yrsmivhpdr frqqmawlkr lgyrglsvrd aipyiyggkq
       61 gkvavitfdd gfenvfrnal pvlqefgfta tnyfvanqig gfnlwdqkig varancmsvs
      121 elrewadlgh evgshtldhv llpeiseqea itqiqqsrmk iedllgrevt sfaypyggen
      181 avtrkiveaa gytnatttek rrarsnddpf giprltirrn dillqflrkt ftr
//
LOCUS       WP_010658257             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: superoxide dismutase [Brucella/Ochrobactrum group].
ACCESSION   WP_010658257
VERSION     WP_010658257.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..202
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22033
     Region          4..197
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 msftlpplpf atnalegagm gtetlelhhg khhqayvtal ngfvekndal kgksleeiil
       61 fakdkadlap vfnnagqhwn hdlfwqnlsa tggrlpgale kkivedfgsv dqfkeafkaa
      121 avgqfgsgwa wlvlandgkl kvtktpngsn platgegkal lgldvwehsy yldfrnrrpd
      181 yvtnfldkla nyefaeatlk aa
//
LOCUS       WP_010658277             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010658277
VERSION     WP_010658277.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34051
     Region          3..>174
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 msyldnlrvf vrvvelgnls aagrdqrasp avasnrikel ekhlgvrlfn rttrkltpte
       61 hgrvfydgal kileavdeae aavaelaknp kgsiritapl gfgrrliasg ipefhdkypd
      121 ievrlrlsdh evdimsegvd vafklgvlen snlrmrgimn cervicaapa ylekhgvpqs
      181 pdellgdkhd clllrfpgsk eyfwslqtae glrkfevtgp fdsddgdvlt qwalggrgii
      241 nkplfevkey irdgrlvpil estppapiql aaiyphkrfq dpkvrliidf mtercqrlir
      301 ealv
//
LOCUS       WP_010658318             130 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Brucella].
ACCESSION   WP_010658318
VERSION     WP_010658318.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..130
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14469
     Region          1..121
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mdkvtggclc gnvrfeasgq pyrvgichcl dcrkhhgalf hasaifpeaa vtvegetrdy
       61 agrffcprcg spvfgrsade veinlgslda pdqfkptyel wtirreswlp sfpdmkgyer
      121 drdgssrfed
//
LOCUS       WP_010658325             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator [Brucella].
ACCESSION   WP_010658325
VERSION     WP_010658325.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17779
     Region          5..144
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mptlkldaid rkiltalqdd arlsnvqlae kiglspspcl rrvkmlekag viqgyhaald
       61 rnavglgltv fvgirverhh eetatafrts vqnlpevfsc hlvsgesdfl lqvvvpdlaa
      121 yerfltgtll rlpgvidirs nfaiqtvksq gelplahltg rkd
//
LOCUS       WP_010658460             283 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Brucella anthropi].
ACCESSION   WP_010658460
VERSION     WP_010658460.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..283
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32236
     Region          28..283
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 msievsriam shnvvaaept kgakvaiadi sealskyrla lifgwqdvaq ryrrsrvgaf
       61 wltlnmavfi galglifgtl fqsemreflp ylcagvitwg fittclsegc vtftssdgii
      121 lqvrmplfth imravwrnvi ifahnivifp illlilgrmi spnvlwaipg fvilclnlsw
      181 mmlilaivca rfrdmtqvvm nilqvlfyat pimwmvkilp dhvsrlfiel npfyhfielv
      241 raplfgspps sldwifgfac aiigwiitil ffgryrwrva ywl
//
LOCUS       WP_010658468             357 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Brucella].
ACCESSION   WP_010658468
VERSION     WP_010658468.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..357
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40813
     Region          191..336
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mnvqtkssdy qrlsphaeig gelswhycat nserlaarld ksgriflfge agafraeasl
       61 tfdrqtialq dvrldplhsd atmllaalld avflrfpdia altlppasel apvsalalre
      121 veglavvdrc vlhqlpllwr kqaahmpyps irsalgpadr lpllrpprps gifyerwipd
      181 lnktvsfrpi drrtdldlfy gwmnqgrvsf fwelaqspea letyladqer dphifgvian
      241 fdneptgyfe fywaredrlg phyesedfdr gwhglignpr hlgrpktlal frsvthylfl
      301 deprtqrivg eprashqkml sycadvaydk vkefdfphkr aalvccerdr ffkevpl
//
LOCUS       WP_010658472             739 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Brucella].
ACCESSION   WP_010658472
VERSION     WP_010658472.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..739
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80940
     Region          34..723
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mnrqfivlll sgcgfttaaf aqetagndag vtrldqiiit agrnessiaa vaqsvqvidr
       61 eqveeamris pnasdlisrl vpgfapsnqt isgasetfrg rsvlimvdgv prntplrdls
      121 rilsmidlns verievvnga sslygaggtg gtinfitkrg tsdkptvtvr tglsgytenl
      181 gkstapetsi siegrkdkld yyfsgtgdwt rrtydghgne mpsdamlgqg ggdrtvngnf
      241 fgvvgyesgp rrfevsfdwt yakqkpewft nyttnpvspr fgsaytgepl redskyltak
      301 ytdqdfalgn levkafynki fkqspftels avntqvyysg nprqptawfn qskydfdrtg
      361 vnmtittpmd fitngskltw gvdyaydkva qtllndedai apmtqnsiaa faqaevpvte
      421 rfrlqggarf dqfyldvndf trptavawpa rslaniypai svlggsfdyn awtfnagavy
      481 dvteevqafg nfsqgysltd igaftrragv nslaeicday gsiaaiygcr gtpdytisya
      541 diapkpqlvn tyevglrgdw gdlrstvssy istskdgvny diaanrvsqq keriwgvear
      601 adydinsmft igglvayqeg kydanrdgsi gsdeylpnnr ipttwkglay ttvsfeggyk
      661 vrgeveyfsg rdrikgqqid datlvnmafs ktfengseas lavrnvfdty yinptatatr
      721 napvaglgrs vflsykvtf
//
LOCUS       WP_010658528             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Brucella].
ACCESSION   WP_010658528
VERSION     WP_010658528.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..201
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21868
     Region          13..201
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mttqtyehrl kagangaplf ivfhgtggde nqffglaeql lpeativspr gdvseygaar
       61 ffrrtgegvy dmedlaratd kmadfiaglv aqhkpsevig lgysnganim anlliekgrv
      121 fdkaallhpl vpfrpkdnpa legakilmta grmdpicppd ltealahyfe rqkadvelvw
      181 hpgghelrqt elaavqsllq n
//
LOCUS       WP_010658533             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010658533
VERSION     WP_010658533.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..202
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=22586
     Region          2..201
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mhdnlreaii sgriksgekl nerqlasdlg istsplkeal rqlegeglvr tearrgtfvs
       61 fnarqaeemt laraalesii arqaakhgge eafgflravi eemraaveag nvdqlielne
      121 kfhdgiheas gceylrrlqn aqrmydhaar vtvlsredvr rqsfneheai mkaitarngd
      181 laerlmrehi vkagdthiel vf
//
LOCUS       WP_010658558             196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Brucella].
ACCESSION   WP_010658558
VERSION     WP_010658558.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21088
     Region          13..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msdpatpssk parerllqaa aelfydagis atgidaiiqr agvakqslyn nfaskaelva
       61 tylehrhaew lglydkrlek aaspmdgila ifdayrdhae fayehgfrgc gllnaaaelp
      121 agdpgrkavr khkeevegll vthltglipd dpprvrqlav qlsfilegai mraglegnsa
      181 rlgeakamvt tilkpv
//
LOCUS       WP_010658566             223 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor [Brucella].
ACCESSION   WP_010658566
VERSION     WP_010658566.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19827043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..223
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24338
     Region          1..>124
                     /region_name="AmiR"
                     /note="Two-component response regulator, AmiR/NasT family,
                     consists of REC and RNA-binding antiterminator (ANTAR)
                     domains [Signal transduction mechanisms, Transcription];
                     COG3707"
                     /db_xref="CDD:442921"
     Region          <72..206
                     /region_name="PRK10651"
                     /note="transcriptional regulator NarL; Provisional"
                     /db_xref="CDD:182619"
     Region          155..208
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlpllviidn raldreclah gltnhsiems iatfssfeqw qhqrkgrtag avlfniggqk
       61 vsdpavgnyl nrivtdcapa pvilladkee isqvlkaldh gvkgyiptsv nvnvcvealr
      121 lamaggtfvp assvlalrha tdpnsqrlqp lggmftqrqa evvnalrrgk ankiiayelk
      181 lrestvkvhi rnimkklkas nrtevaciin elfpsetsfs dlq
//
LOCUS       WP_010658590             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PIG-L deacetylase family protein [Brucella].
ACCESSION   WP_010658590
VERSION     WP_010658590.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..218
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24963
     Region          16..210
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 midlrslanq srplqllclg ahsddieigc ggtllslies gtplhvewcv lsgneerrae
       61 aeasardflr gidrfnihla sfedsyfpaq sreikqwlie qrgrgqpdmv fthrhgdahq
      121 dhrtvneltw nlfrdqvile yeipkwdgdl gqpnaysalp aaimdrkidl lmkhfgtqrs
      181 kdwfdaetfr glarlrgmec rapetyaeaf harklrlf
//
LOCUS       WP_010658598             489 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Brucella].
ACCESSION   WP_010658598
VERSION     WP_010658598.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..489
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52722
     Region          18..474
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mpietmkatp aerevfieed rgyhkalkpr qiqmiaigga igtglflgag grlamagpal
       61 vfvyalcgff aflvlralge limhrpssgs fvsyarefyg eklafvagwm ywlnwamtsv
      121 advtavalym nffkhyvpwl qgidqwvfal talvivlsmn llsvkvfgel efwfslvkvi
      181 alvtflvvgi yfvvsgtpid ghsagfsiit dsgglfpngi lpafiiiqgv vfayasiell
      241 gttagetedp rkvmprairt vvfrllvfyv gsvlllslll pytaysages pfvtffgkig
      301 vegadiimnl vvltavlssl naglystgri lhsmaisgsa paslakmnkn gvpymgiavt
      361 avvtvigvvl navvpaaafe ialnlsalgi itawgvivlc qlklwhlarr geivrpdfrm
      421 fgapytgilt lafllgvlvl maldypvgtw tiaslaiigp alilgwymmr erihrlater
      481 avdasipgk
//
LOCUS       WP_010658658             388 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Brucella].
ACCESSION   WP_010658658
VERSION     WP_010658658.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..388
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41844
     Region          2..359
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtktlgvgii gcgnisaayl rlspmfrgie imacadinpa aakaradefg vkaqtidell
       61 qndgidivvn ltvpdahyav tkqilaagkh aysekplvls meqglelkal adgrnlkvgc
      121 apdtflggah qlarreidng nvgritsgtc hvmshgmehw hpnpdfffrk gggpildlgp
      181 yyianlvnli gpvkrvaalt saatptrtis seprkgeaip vetpttihal lefeqgatvt
      241 lsaswdvwah rhanmelygt egslylpdpn ffggevqmak pgepvepvkn wehpfgvane
      301 qhsqgmmany rtagladmaa ailngrdirc sleralhgvd vmlailrsge ekrfidietr
      361 ctrpealdia aaeallrpae nrekraan
//
LOCUS       WP_010658680             422 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010658680
VERSION     WP_010658680.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..422
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=46329
     Region          7..398
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 msekraphlv vvgagfgglq lihdlrnvdv ritlidqrnh hlfqpllyqv attilatsei
       61 awpirhlfkd rkevttllgt vtdvdtehrq vllengteis ydmlvlatga rhayfgndqw
      121 ealapglkal edattirrrl llaferaere sdeakrqall tfaivgggpt gvelagiiae
      181 lakqtiwpef rnidtrqtrv mlleagpril aafpedlssy alkaleklgv evrlgipvkd
      241 itaegvtvge efipcrtaiw aagvaaspaa twlnaesdra grvkvlsnln vpghedifvi
      301 gdtawvegpd gkpvpgiapa akqqgayvak viksriegkt ppmpfrykhq gnlatigrga
      361 avvdmgrfkl kgliawwfwg iahiffligt rsraavawsw lwtyisgqhs arlitqgkpv
      421 er
//
LOCUS       WP_010658692             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pyridoxamine 5'-phosphate oxidase family protein
            [Brucella].
ACCESSION   WP_010658692
VERSION     WP_010658692.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..220
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24034
     Region          21..163
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 mttapsersr vkrlhergay daatvhaiid aqplahvayv fngtpyvtpt lvwregdfiy
       61 whgssasrml escdeaevcv sftlldglvl arsafhhscn yrsvmafgta rkvsdiavke
      121 hhlrsfvngl fpgrweslrp mmakelkatm llelelneas akvrsgppkd ddadyalpiw
      181 agvipmttqm gapvndgril pgvaapdaim qfgyvaeaae
//
LOCUS       WP_010658717             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Brucella/Ochrobactrum
            group].
ACCESSION   WP_010658717
VERSION     WP_010658717.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..240
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25030
     Region          4..239
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mkqmgfldil sfgpdgwgyv lmmgalvsva lavlgfllga aigvfaawak isggrtlrav
       61 adgyttiirg ipdllviylf yfggsaavta lgkyfgaegf igfpgflagv laiaiscgah
      121 htevfrgafr avskgeleaa tacgmgqmlk frriiaplal rhalpglgnv wqvslkesal
      181 vsvagvvell rqaqigagst glpfnfflia galyllissv sggllqfaer hfsrgvrrak
//
LOCUS       WP_010658693             138 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010658693
VERSION     WP_010658693.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..138
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14924
     Region          1..133
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mddldqrlis elrinarasi ptlasilgva rgtiqsrmer liasgviagf tvrlkdhgat
       61 dmirgimmie ltgrniksvi atlrknpgfs avnttngtwd liaeievpnm nefhrlvtgi
      121 ramdgiakse thiflgpa
//
LOCUS       WP_010658751             437 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrolipoamide acetyltransferase family protein
            [Brucella].
ACCESSION   WP_010658751
VERSION     WP_010658751.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..437
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46910
     Region          4..436
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mahftiklpd vgegvaeael vewhvkvgdv vreddllaav mtdkatveip ssrggkviav
       61 ngevgekiav gselvrleie ggateekseg naeepaptav etakpqpapt petpvllqtp
      121 vppkaaapkr eatsrafsga gpirsegerp latpsvrlra rdagvdlrrv rgtgpagrit
      181 hedldlffqq etgaspalsg yatdtsvnei kviglrrkia ermaeakrhi phitiveevd
      241 vtqleelrsg lnnekkedrp rltllpfiir tivkavkeqp glnahfddea diirqfggvh
      301 igiatqtpng livpvvrhae smsvfaaase lsrvtdaarn gtakreeltg stititslgp
      361 lgaiattpii nrpevaivgi nkmavrpmwd gvqfvprkmm nlscsfdhrv idgwdaavfv
      421 qklkslletp amifveg
//
LOCUS       WP_010658777             314 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Brucella].
ACCESSION   WP_010658777
VERSION     WP_010658777.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 314)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..314
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33907
     Region          32..276
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mraartaypm twrimdalea iaaflwparf nravpylmll paialvgllv lgliqiadts
       61 lrtldtstfl msdyytlany kralteslfa tvawrslfgs lvvtaftlll afpyaylmvr
      121 tpsaalrkfl lialflpffi gqvvraygwl iilgnqgmvn ealgfvgiap mrllynypav
      181 lfgliqymlp favlmlapal taipeemeaa asslganwlr tfahvvlpma rpgligaglv
      241 vmtlsltdfa vpailgggsq dfianaiydq ffrtsdqglg atlalllvgv gsilvgivft
      301 lfgagtlamg rark
//
LOCUS       WP_010658806             589 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [Brucella].
ACCESSION   WP_010658806
VERSION     WP_010658806.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..589
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=65794
     Region          5..584
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 marqekkkdv vvvglgwtga ilamelaqeg leivalergh dqntvpdfky pnmidelkyg
       61 vrlklmqras qqtvtirrne nevalpyrsf gsflpgngvg gagthwngln wrpqpeelrl
      121 rsyvqerwge qiipedmllg dypihydele pffdrferia gisgkagnlk gktveggnpf
      181 egwrsndypm ppmhttwdgr kfadaaqgmg yhpfpspggi astayvneyg mqmgpcnhcg
      241 fcerfgcyqy sksspqtail dalkrmpnfs yrtesevlrv emapdgktat gvtyfdeatq
      301 eevfqpadiv ilasfslnnv hlallsgigq pydpatgegv tgrnyayqmn ggvtlffkde
      361 efnpfigtga ngmciddfgv nqidfgregf iggsywragq tngqpirsmp lpsgtpgwgg
      421 awkkaiaewy ghamsigshg shmayrtnhl dldptykdrh grplmrmtfn wnpndirmtq
      481 ymktkmeela ktmnpdlmqs sfkkegaqyd vrpyqtthnt gghsmsenpr egvvnrysqa
      541 wdkhnvfmtg agnfvqntqy nptgllggla ystahairtq ylsnprpli
//
LOCUS       WP_010658889             357 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Brucella].
ACCESSION   WP_010658889
VERSION     WP_010658889.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..357
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38587
     Region          3..357
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mpaflevada rvrygnnevl kgvnlsvkkg efvallgssg cgkttllrai agfnmpsnga
       61 irvdgrdvtk sppdkrgmal vfqsyalwph mtvaqnmgyg lrirgttket ikqkvdevac
      121 llgldaller kpaalsggqr qrvalgrala iqpdilllde plsnldarir lsvrheisal
      181 qrrlgitavh vthdreeamv madrivilnn geiaqagape evynhpasdf vaafmgaenl
      241 ievpiqikad rieiaagann kastisagrr nlsdgmasar frseaacltk pgvdrnspts
      301 elalngtveq tsypgglwrh mirvgdrhim vdaqeshqpg anveihipeh alflfdk
//
LOCUS       WP_010658892             270 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Brucella].
ACCESSION   WP_010658892
VERSION     WP_010658892.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..270
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29113
     Region          7..261
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 msniidwrwi prgillglla faifgplanl llwavaerwy fphtlplqyg fsfwtnvfsp
       61 rgnalsslgt svliagltvi vslglaipag yalarlklpf rglilltlli pqafpnlpvy
      121 vniaqmfysf glngtitgvv lvhvthglvy avwiataafs aidreleeaa rsmgasalkt
      181 ffditlpiaa pgllasaifv flesldeftg tyfvgapdis tlplllytas sggnyqiasi
      241 salillvpsi afmfvverfl radvlskvgr
//
LOCUS       WP_010658895             345 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aldo/keto reductase [Brucella].
ACCESSION   WP_010658895
VERSION     WP_010658895.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..345
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=38297
     Region          11..337
                     /region_name="AKR_Tas-like"
                     /note="Escherichia coli Tas protein and similar proteins;
                     cd19094"
                     /db_xref="CDD:381320"
     Site            order(17..19,24,46,51,85,128,179..180,205,233..239,242,
                     244,253..255,289,306..310,314,318)
                     /site_type="active"
                     /db_xref="CDD:381320"
     Site            order(46,51,85,128)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381320"
ORIGIN      
        1 mkplgrtglt vteiclgtmt wgvqntesda heqldialda ginfidtaeg yaipmssesy
       61 gktetyigsw lkksrkrdki vlaskiaggg rqkwirdgar psrtsvreav enslkrlqtd
      121 yidlyqvhwp mrahyhfgqs wsfdpsntdc aaetqqmhdv llglgdmvrd gkirhiglsn
      181 etawgtmqwl rlaeqhslpr iasiqneysl lqrqfdfdma elalcedvgl laystlaagv
      241 ltgkylggrl pagsravise ggiwrnnvhs epairayidv akkhgldiaq maiaftltrp
      301 fmtsaiigat tvdqlktdia ahqvklsedv ltdiekvyrq yprpl
//
LOCUS       WP_010658899             367 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: saccharopine dehydrogenase family protein
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010658899
VERSION     WP_010658899.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..367
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39645
     Region          1..>49
                     /region_name="trkA"
                     /note="Trk system potassium transporter TrkA; PRK09496"
                     /db_xref="CDD:236541"
     Region          26..360
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mkeivvvgag kigatiadll astgeyavtv vdrsqaqlda lesgaevktq aldiedakal
       61 etaltgkfav lsaapfhltt riaeaaakag vhyldltedv astrrvkela keaktafipq
      121 cglapgfisi vaydlakrfd kldsvrmrvg alpqypsnal nynltwstdg vineyiepce
      181 aivngelsev paleereefs ldgvtyeafn tsgglgtlce tlegkvrtln yrtirypghv
      241 almkallndl glrhrrevlk difenalptt lqdvvvifvt vsgtkngrlv qetyankvya
      301 apvgkiirsg iqittasaic avldmlakgd lpqqgfirqe ditleaflsn rfgkayaqed
      361 hcarmva
//
LOCUS       WP_010658901             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Brucella].
ACCESSION   WP_010658901
VERSION     WP_010658901.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..262
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27568
     Region          1..258
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mgrfakilfg vaavvfliap lfailplaft ssvfltypvp gwsvrwfeel atadvwrrai
       61 vnsliigsgt tilatvlgtm aalglrsril flsgpiktlf llpmvvpavv mgvgmqllfv
      121 rlgiansylg viiahtvisi pfvlvsvtga lagidrrvel aaeslgaspl tvfrkvtlpl
      181 ampgiasgav lafatsldev vltlfvagpn qrtlarqmfs tirenispai aaaaflfiag
      241 tvllglaaml frrkrtsgtv si
//
LOCUS       WP_010658945             480 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [Brucella].
ACCESSION   WP_010658945
VERSION     WP_010658945.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..480
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=51244
     Region          13..470
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mygsgdmtgn kqadlvallg vdlvmtgknd mlgycrdwpg dventavavi rprstadvsa
       61 avktcyslgl siipqggntg lvqggvpdgr dnlvilsler mnhirkidpd dfsavvdagc
      121 ilselkdkla aegmffplal gaqgscrigg nvstnaggin vlrygmtrel vlglevvlpd
      181 gtifnglstl rkdnrgidlk qlfigaegil gvvtgvaikl mplpdkveta llglnslddv
      241 ialyrrarvq ccdlmsafef mppvaftlaq eampelampl gqypayvlme vsgsglvdil
      301 slmeqflaga medglvldgt iassraqgqn lwtfreamne gqalrgkhlr tdisvplskl
      361 asfvgeaere lakvlpdcla vsyghvgdgn vhlnvipesn ldvatkdmki tlaketinav
      421 ldryagsisa ehgigrlkre dfekridpar rkllegikqv idpdnimnpg cqlsldsskg
//
LOCUS       WP_010658947             293 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [Brucella].
ACCESSION   WP_010658947
VERSION     WP_010658947.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..293
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30304
     Region          2..284
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mtrkiaflgt glmgapmasr lldagfdvtv wnrnsakaap laekgaklaq saaeaaetae
       61 lvitmltdgp avrdvlfdqg aaaalkkgsa vidmssispg farehtkhlk aidinhidap
      121 vsggvvgaqe gtlaimaggd eaiiagladv fkpmgrltrv gpsgagqlak lanqqivavt
      181 igaiaeamvl vekgggsraa frdairggfc esrilelhgk rmidrsfepg gtsriqlkdl
      241 nsilktasdl slslpltetv reafaafvde gggekdhsal llhleklneg qks
//
LOCUS       WP_010658925             276 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Brucella].
ACCESSION   WP_010658925
VERSION     WP_010658925.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..276
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30529
     Region          2..267
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mlvdiknlqi sfetrtsrfd avrgislqlg reklgivges gsgksltara lmkllppiae
       61 vkadrlsfdg idilsaterg mrqirgkrag filqdpkysl npvktigvqv aeawrthkgg
      121 skrqamdaav dlldqvmirn prdvaklyph evsggmgqrv miammlapdp elliadepts
      181 aldatvqaei lrliddlvsk rgmglllish dlplvshfcd rvmvmymgrv meelkaaelv
      241 raehpytkgl lncipslmhp rdrlpvlnre eswlns
//
LOCUS       WP_010658950             174 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010658950
VERSION     WP_010658950.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..174
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19204
     Region          1..159
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtkaidffyk mlgailvfll agmaimvfvn vilryaansg ltvseelary ffvwvsflga
       61 vltfrenshl gietlvarfg rqgritcmai sylivalcsg iffwgtwkqf dinasmvapv
      121 tglsmiwvyg vglftggamf iiaaerflra vtgrltdeei atfagehsld hlme
//
LOCUS       WP_010659022             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010659022
VERSION     WP_010659022.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..277
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29503
     Region          13..277
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdspapssin vptnikefea kllevsdrlp krlkqcadfv aanqdriavs tvaemaegag
       61 vqssafmrfc qimgfsgfse mqklfrdsya ggwpdystrl qhlretatgs apallaefae
      121 agrtslegll ktidpdalek avqllasaqt ihivgirraf pvasylayal ekmqvpamlh
      181 savgklenlh airegdvlla itfspyspet vamaetvaar gidvvgitdt fvspmsksak
      241 qtllvsevdf gafrslsatl claialavav gtarqsd
//
LOCUS       WP_010659027             136 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Brucella].
ACCESSION   WP_010659027
VERSION     WP_010659027.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..136
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14307
     Region          6..131
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 msangwtaay qpimlsilri vaalvlfsyg tekilgfpsg rspamfslsw tagvlelvlg
       61 ftlliglfsr fsafilsglm acayfiahas qsffpgqngg vaailfcfif lylfiagpgp
      121 lsidasrann alpagr
//
LOCUS       WP_010659054             266 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: creatininase family protein [Brucella].
ACCESSION   WP_010659054
VERSION     WP_010659054.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..266
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=29103
     Region          4..256
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mkrywsdyts eafsrldrek lvavlpvgai eqhgphlpla vdaaivdgmv ketiarlpet
       61 shalflptqa igksnehsly pgtltfsaet iirmwceigg cvaasgvrkm allnshggqi
      121 svmdivarel rirhnmmvvs inwfglgmpe gvysdhdakh gihagdmets vmlemhpdlv
      181 dmskaqdfrt ltetfardfk hlalsggakp awqiqdinpy gaagdatlat aekgratidf
      241 aaerlvevla eieraplswl dnqpaw
//
LOCUS       WP_010659055             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Brucella].
ACCESSION   WP_010659055
VERSION     WP_010659055.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..269
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29117
     Region          9..258
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msvapnsqas sslieidgvy kqygtgvmav sdmsltieqg qfvsflgpsg cgkstalrmi
       61 aglesisagd irvnghapgk gpigaqdigf vfqeptlmpw asvfdnvylp lrlagisrke
      121 atprveeala qvglsrfaka fprelsggmk mrvsiaralv trprlllmde pfaaldemtr
      181 fklnndvlrl wqehgltvif vthsvyesvy lsnrvivmaa rpgrvvadip iigsypraen
      241 yrttdayaky cakvsdalta tlssqdidh
//
LOCUS       WP_010659072             288 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycine betaine ABC transporter substrate-binding
            protein [Brucella/Ochrobactrum group].
ACCESSION   WP_010659072
VERSION     WP_010659072.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..288
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31716
     Region          30..287
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(38,40,86,114,149,153..154,199)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mlgkltkfgl aavvagtmtm gaafaqdgkp vkigwapwsd aefvtklakk liednlgqkv
       61 elvqtdvapl yqgvsrgdid ammmawlpet hadyyarvkd kvedlgplye gaklgwivpa
      121 yipeseissi edlkkpevre klkgeiqgid pgagltrlsq eaikkygldy klnisseaam
      181 lttvdratrs dgwfvatsws phwmfgkykl ryiadpegal ggaehidaia rkgfkednpk
      241 vaslltkmsi piseleaamf daqetsyeka vdkyiadhpd rikewlae
//
LOCUS       WP_010659097             315 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Brucella].
ACCESSION   WP_010659097
VERSION     WP_010659097.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..315
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32701
     Region          11..315
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msgltiltnr pwiwsfiata vvwiitilft ggagahglsh aaftfasfsv ivglgqmfvi
       61 tlgpgnidls vpanmtlaat lalklmdtqd gmvlaglgva ilvgvaigic nytlikllri
      121 ppiiatlsms fliqstaiws nrglrvkppe slaqfttsst lgvpnvalva lilsvigwvl
      181 lkksiygrwi saigqnpfaa rmagvpvdgt rfityllcav laslcgflla cfsggaalnm
      241 gaeyllmsia vviiggtava ggdsnipgiw gaalfmfliv smlntygfga gvrlvltglt
      301 iiaviilasg rraer
//
LOCUS       WP_010659130             401 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Brucella].
ACCESSION   WP_010659130
VERSION     WP_010659130.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..401
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41389
     Region          14..380
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(24..25,28..29,32,65,116..117,119..121,124,144,
                     147..148,151,227,230..231,234..236,239,266,270,319..320,
                     324,328,344,347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 mastqktasi pstvwilgfv sllmdissem vqtllplylv aglgasammv gfieglsvai
       61 atvtklfsgv isdwtgrrkp lavagyglaa isklifplat taggivmaka idrvgkgirg
      121 tprdaliadv tppeirgaaf glrksldtvg gfvgpliaig lmlatggnii tifwiaaipa
      181 fiavallivg irepetpskr plarskgfpr fadagklnat vwivitvasi ltvarfseaf
      241 lllkaqeagf aaawvpitmv vmhavyglta ypvgalsdrl grkgllaasl gflivadlvi
      301 aqsttiypfl agivlwglhm gfsqgilatl iadtapghlk gtafgmfnvi tglvmlvgni
      361 gagwlwesyg ssstflagai lsavallsla llpgiaarkt g
//
LOCUS       WP_010659151             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Brucella].
ACCESSION   WP_010659151
VERSION     WP_010659151.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..247
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26514
     Region          <1..245
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 madpllnadq lvvrygdala ldgvsltiqp getlalvgps gsgkstlara llrlhplasg
       61 tirfegedwl alkgaslrkq rarmqmvfqd plsafnpras vydllreplr ihglkrdias
      121 llqavgldpa larrgvqeis ggqrqrvaia ralattpsli vldeavsald vtvrgailnl
      181 lrdiqkaeqt aylfithdla vaaqmadria vmergqivec rptrelitap qapvtkalie
      241 avprlsv
//
LOCUS       WP_010659163             360 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010659163
VERSION     WP_010659163.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39350
     Region          1..352
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mlelrniskt vggathihpt slvlprgsln vllgptlsgk tslmrlmagl dkpsegsilf
       61 dgqdvtgmpv qkrnvamvyq qfinypaltv yeniaspmri agkaqseids evrkaadllk
      121 ltpyldrtpl nlsggqqqrt aiaraivkka nlvlldepla nldyklreel reelprifae
      181 sgaifvyatt epsealllgg ntaalsegri tqfgrtidvy rrpldlvtar tfadpplnta
      241 rmvksgdrfl radrpaiavp sqladisdgp ltiafqphhl lvrpaenatv pirartlvse
      301 iagsesfihl dyegdrwvml ahgiqivepd reievyldtr hlmafdetgr avgrtvglaa
//
LOCUS       WP_010659180             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010659180
VERSION     WP_010659180.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..308
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=32532
     Region          2..308
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mlnlfllqsl ngiqfgillf lvaagltlif gvmdlinlah gvlymvgayl tatftamtgs
       61 ffygilialp vtlvigivle vlvfrrlyer shldqvlatf glilivnelv kiiwgaapls
      121 vpmpdslsgs iqlfgnlryp vyrlliiaag lataaglyvl vnhtrigmll ragatngdmv
      181 salginirrl fmvvfglgam lagfaggmis pilsvdpgmg dsililtfvv iviggvgsvr
      241 gafvaaitvg lvdtlgrtfg pmllrnlldp aaasqmgrtl vpmltyilma avlyfrptgl
      301 fpaqggtr
//
LOCUS       WP_010659181             337 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Brucella].
ACCESSION   WP_010659181
VERSION     WP_010659181.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..337
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35958
     Region          49..332
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mseithnstr dtampetaks rtsplldagp wlvfaafaiv pllasvlnds fllvivtrim
       61 ifalaalsln fimgygalvs fghaayigig ayavgilssy giddlilqlv aaivvaaffa
      121 lvtgyislrt sgvyfimitl afgqmafffm vslsafggdd gmtlstrstl fgntllssnl
      181 vlfyfvlavl mgaffifrml vhsrfgrvlr gtrdnpvrmr aigfspfsfq ltayviagva
      241 aaiagvllan qiqfvspafm swqrsgeliv mvvlggmgtl igpvlgataf ivleevlahf
      301 sehwklglgl flvlvvlfsr dgiggllrkl rggsdvg
//
LOCUS       WP_010659198             391 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Brucella].
ACCESSION   WP_010659198
VERSION     WP_010659198.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..391
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41577
     Region          19..390
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdssaakplt reyldwpffd kahtdwaakl dafakspala gvdhsdtdna cralvkalgq
       61 aglleaavsl tggegidsrk lciaretlay hdgladfafa mqglgtgais ltasdelkqt
      121 vlpkvasgew isafalsekl agsdvaamnc aaradgddyv ldgektwisn ggiadvytvf
      181 artgeapgtr gisafvvfat dpgfsiaeri dviaphplat irfdncripa srrlgtpgeg
      241 fkiamrtldi frasvaaaal gfarraasea lsharsrpmf ggaladlqlt qatlgdmatd
      301 idaaalltyr aawrrdiqkl nttkeaamak mvatenaqqt idkavqmfgg rgvksgeive
      361 rlyreiralr iyegatevqk liiarellka n
//
LOCUS       WP_010659232              88 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutaredoxin family protein [Brucella/Ochrobactrum
            group].
ACCESSION   WP_010659232
VERSION     WP_010659232.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Shelton,M.D., Chock,P.B. and Mieyal,J.J.
  TITLE     Glutaredoxin: role in reversible protein s-glutathionylation and
            regulation of redox signal transduction and protein translocation
  JOURNAL   Antioxid Redox Signal 7 (3-4), 348-366 (2005)
   PUBMED   15706083
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Fernandes,A.P. and Holmgren,A.
  TITLE     Glutaredoxins: glutathione-dependent redox enzymes with functions
            far beyond a simple thioredoxin backup system
  JOURNAL   Antioxid Redox Signal 6 (1), 63-74 (2004)
   PUBMED   14713336
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..88
                     /product="glutaredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=9609
     Region          8..69
                     /region_name="GrxC"
                     /note="Glutaredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG0695"
                     /db_xref="CDD:440459"
ORIGIN      
        1 mthtstphil iyttptcpdc halkrwlseq glsyeerdls epeiaeeaka rtgvrvapit
       61 ivgseifygt fvrqkpgllk alglndgl
//
LOCUS       WP_010659336             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carbon-nitrogen hydrolase family protein [Brucella].
ACCESSION   WP_010659336
VERSION     WP_010659336.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..279
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30898
     Region          2..270
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(41,97,114,118,130,155..156,158..159,180)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(41,114,155)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(115..116,136..138,156,159..163,165..166,188..189,
                     192..193,195..197,199..200,233,263..264,267..268,270)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mkisliqtsp qtdkadnlri trglmedavr tdspdlivlp eyfeyyggtp eeklaaaesv
       61 pggpaykmaq dfarehkvfv hagtlmekvp nekriynstf vfnregkeia hyrkihmfdi
      121 vgpdgtayke satvkpgenv vvydldgfkv gcaicydirf aelyleleka gadvivlpaa
      181 ftlqtgkdhw evlararaie tqtyfaacgq tgstvsnger rhtyghslvc dpwghvvara
      241 sdgvgfvtar ieraqiervr slipmvshrr igkqlqaca
//
LOCUS       WP_010659355             276 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator, partial [Brucella anthropi].
ACCESSION   WP_010659355
VERSION     WP_010659355.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         <1..276
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <1..30
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          58..258
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(76..77,79..80,83,87,89..95,187..192,198..199,
                     201..202)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 vshrmkklea dlgvrllnrt srsltpteag aalatqleng lrtigealea ltsqrdfpsg
       61 rirlnalrda arliiapilp rytqtypdmh lditiddqmv divaegfdag irygdrvpqd
      121 migvaltgpl qwivvgspvl isragcpetp ddllrlpcie trlgdnsrya welgngaslr
      181 rvdvkgpica neteqaveaa lggigfaycl eplvknylda gtleavlpdw asegppltmy
      241 ypsrrqvpsg lrrlidlire dqglaklvva eevgsr
//
LOCUS       WP_010659358             459 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Brucella].
ACCESSION   WP_010659358
VERSION     WP_010659358.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..459
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48337
     Region          30..458
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(37..38,41..42,45,77,127..128,130..132,135,155,
                     158..159,162,284,287..288,291..293,296,324,328,380..381,
                     385,389,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mkhetaihqg tsvapdglpk priywawatl mvgltlavid gtianvalpt iaadfsagpa
       61 asiwivngyq laivvtllpl aalgeiygyr rvylggvalf tvasvacvfs rslealtfar
      121 iiqglgaagl msvntallry tvpqakfgta iglnalfvav sstigptlag vmlsslswpw
      181 lfviniplgi aavvmglksl penehsarkf dvvsailsal tfgllvttid sagneigsfv
      241 vllqavgcvt aavlltrrsl rmadpllpld llripvftls ictsimsfla qmmafislpf
      301 lfqvvfgfrp ievgflmmpw pialaivapl sgklsdkhsp ailgllglii faiglalvgm
      361 lpehpsipdi cwrmaicgig fglfqapnnr mmitstprsr sgaasgmlgt arllgqslga
      421 afvafllsqw gvegtpyilf fasgfalfas lisvtrlgr
//
LOCUS       WP_010659393             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase family protein [Brucella].
ACCESSION   WP_010659393
VERSION     WP_010659393.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..228
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24929
     Region          2..200
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrriivgtfl sldgvmqapg gpeedrtgqf eyggwtvpyw ddvvagamge sfskpfdlll
       61 grrtydifaa hwphqvtdpn dpgfvsgege iarmfndvtk yvathrpesl nwqnsellgd
      121 diiaslraik ategpdlsvs gsselvhqll asdlvdelrl liypvvlgkg krlfdgqsvp
      181 safklvsstt spsgviiany qrsgelktgs famdhpseee ierrknls
//
LOCUS       WP_010659445             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: gamma-glutamyl-gamma-aminobutyrate hydrolase family
            protein [Brucella].
ACCESSION   WP_010659445
VERSION     WP_010659445.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..253
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27273
     Region          11..248
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mpktsrplva vptdvkpfen ytwhaapqqy laaaidvagv tpllvpsfgd kmdldailda
       61 vdgvlvtgsk snvnpalygv epsaafepyd nardatslpl iraaiekgvp vlaicrgiqe
      121 lnvalggtla teiqemegrm dhrapesesq aerfaiqhpi klnpnsclae ilkeesvrvn
      181 svhrqaidkl apqleveava edgtveavsv rnakgfvvgv qwhpeywahs dapsrkifea
      241 fgeavrqhra vgq
//
LOCUS       WP_010659462             352 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methionine ABC transporter ATP-binding protein
            [Brucella].
ACCESSION   WP_010659462
VERSION     WP_010659462.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..352
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37138
     Region          13..346
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtiekppats apivemkdvr rmfgdtaain gvslsvarge ilgiigrsga gkstlircvn
       61 glekpdagsi liegreitgl gedalrplrr rigmvfqhfn llsaktvaen ialplkiagk
      121 pkaerarrva ellelvglsd kakhypaqls ggqkqrvgia ralaaepavl lsdeatsald
      181 pettqsilal lkdintklgl tillitheme virriadrvi vldhgaiaee gpvwkvfanp
      241 qspvtqsmlq vltpelpavw rdqleksgal avlkvklsga aakgaffndv saatgvapql
      301 ihgsmdtiqg epvgtlfigl paedkaklda aitylnthad atevlgyvsg da
//
LOCUS       WP_010659463             278 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Brucella/Ochrobactrum group].
ACCESSION   WP_010659463
VERSION     WP_010659463.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 278)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..278
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30520
     Region          13..277
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mssvlsrytl trraglkall ftaaaltvgf asapshaedk tikvgimgge dedvwkvvae
       61 egkkhglnie rvtfndynqp nealerkeid anafqhkpyl deqvkqhgyk isvagytavw
      121 pigiysrkhk sldelkegav vgvpndpsne gralrvleek gliklkpdag ilatpidive
      181 npkkleikel dagvvgrsid dldaaivnnd waakaglkke eaigwesken npynnfiavr
      241 tedenaewvk nlvasfqnda vkaeidrayk gtgipawk
//
LOCUS       WP_010659489             311 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Brucella anthropi].
ACCESSION   WP_010659489
VERSION     WP_010659489.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..311
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34152
     Region          9..248
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 maaepniala ivglgkiard qhlpsieavd gielkaiasr nagldglpsf hdidellgsd
       61 vaidavslct ppqgrfsqay aalkarkhvm lekppgatis evqalerlaq aedvtlyatw
      121 hsreaaavep areflkdaei rsvsvtwked vrhwhpgqqw iwepgglgvf dpginalsiv
      181 thilperffl tqsdlyfpen raapiaanlk fqtesgipvs feldwrqtgp qtwdirvetd
      241 kgtvllshgg srltiagtek maepnreyqr lykrfvqlig agrsdvdlap lthvadafll
      301 gkrhvveafe d
//
LOCUS       WP_010658998             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RlmE family RNA methyltransferase [Brucella].
ACCESSION   WP_010658998
VERSION     WP_010658998.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Hirata,A., Okada,K., Yoshii,K., Shiraishi,H., Saijo,S.,
            Yonezawa,K., Shimizu,N. and Hori,H.
  TITLE     Structure of tRNA methyltransferase complex of Trm7 and Trm734
            reveals a novel binding interface for tRNA recognition
  JOURNAL   Nucleic Acids Res 47 (20), 10942-10955 (2019)
   PUBMED   31586407
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Caldas,T., Binet,E., Bouloc,P., Costa,A., Desgres,J. and
            Richarme,G.
  TITLE     The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S
            ribosomal RNA methyltransferase
  JOURNAL   J Biol Chem 275 (22), 16414-16419 (2000)
   PUBMED   10748051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..240
                     /product="RlmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=26110
     Region          36..240
                     /region_name="RlmE"
                     /note="23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ
                     [Translation, ribosomal structure and biogenesis];
                     COG0293"
                     /db_xref="CDD:440062"
ORIGIN      
        1 mskaggnkgg vktggrggag ssnlqvrvkk kagtikessr rwlqrhlndp yvhksrqdgy
       61 rsraayklie indrydllkk gqkiidlgaa pggwsqiaak ivgstdenpn vvgidylhvd
      121 plpgvvllem dflddeapqk lmdalgdkpd lvisdmaapt tghrrtdhlr tvhlcevaad
      181 faisvlkpgg hfltktfqgg tenellallk qkfrsvhhvk ppasraesve lyllardfkg
//
LOCUS       WP_010659516             285 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: outer membrane protein [Brucella/Ochrobactrum group].
ACCESSION   WP_010659516
VERSION     WP_010659516.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..285
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=31002
     Region          86..284
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mkctsaiaiv aislmagsga afaadiiadp viepmpepvn ssgwyirgdl gynfksstdg
       61 dwsfwnqfdp pyrgiddtlr yddfdlkaga tygvgvgyrf tdmfradatl dffragingr
      121 tacpsyvksa kgfnpvednc nyedsstani wtamanayvd lprvgpvtpy lgaglgaayv
      181 qyddwkthev cagctyssek dgldswrfam almagvsydl teqlkldvgy rymringgka
      241 ygfdaadrst npygnaegpg atgtqakdng fnmhtiragl ryefr
//
LOCUS       WP_010659538             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010659538
VERSION     WP_010659538.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..145
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15735
     Region          1..135
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mddldeklit llrhngrrsi sdvaidlgvs ratvrarmer leqsgdiigy tvilrsdavd
       61 lpvrgimmie iegnvadrvv kalggfsevs avhttngrfd lvvelgaatl tdfdavlrri
      121 rlvpgikase tnlllatprs trarl
//
LOCUS       WP_010659549             318 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Brucella].
ACCESSION   WP_010659549
VERSION     WP_010659549.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..318
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35520
     Region          4..237
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mapriavlgc gywggnhirt lkslgalqav sdsraeqaer fatefnvpsi pvdelfthpd
       61 idgivlalpa qfhsqyaiqa vkngkdvlve kpialdipaa eaeveaaren grvfmvghvl
      121 rfhpafekll dmvksgelgd iryvhshrvg fgkfhnefda lwdlaphdls milaitgeep
      181 gavrgegvat ldhltdiahl hldfpngirg hlfasrlnay rerrltvtgt kgmavfddge
      241 pwdrklalys hevwrendqw sfksvepvyi pveegmpltr elqhflhcie trekprtdgk
      301 eaisvlrilt egtvrhph
//
LOCUS       WP_010659569             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Brucella].
ACCESSION   WP_010659569
VERSION     WP_010659569.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..283
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30553
     Region          3..268
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 malleiknlt vsfdtstgpf ravdgidirv dkgevlaivg esgsgksvgm lavmgllpkt
       61 atvtadtmtf dgkdlqamsd kerrkiigrd ismifqepva slnpcftvgy qleevlkqhm
      121 gmngsasrar aiellelvgi rdaaerlksf phqmsggqcq rvmiaiaiac npklliadep
      181 ttaldvtiqk qildllmrlq vehgmglimi thdmgvvaet adrvivqykg hkmedadvls
      241 lfsapkhpyt rallsalpen atgdrlptvs dfvfenngag ear
//
LOCUS       WP_010659578             430 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Brucella].
ACCESSION   WP_010659578
VERSION     WP_010659578.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46029
     Region          18..418
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(29..30,33..34,37,72,119..120,122..124,127,151,
                     154..155,158,247,250..251,254..256,259,290,294,344..345,
                     349,353,369,372..373,376..377,380)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 misarlasfl aqrnihygwv vaaitfltml ataaamgsag ilieplqref gwtnanisfa
       61 malrlvlfgl mgpfaaafmn qfglrrvvaa alimislglv gsifmteewq mvalwgvvig
      121 lgtgmtalvl gatvaarwfe krrglvvglm tasnatgqlv fmpilasvsq tigwrtslti
      181 vvcflvaalv lvlalmrdhp adiglkpygr taplpapgpr msfgtmlasp lvtlreasst
      241 atfwvlfltf fvcgfstngl iqthwitlcg dfgiapvgaa gilavigafd ligtimsgwl
      301 sdrfdnrwll fwfyalrgls liyltftdft vyelalfavf ygldwvatvp ptvklaaerf
      361 gpekaglvfg wvftghqiga aaaaafaglv rtdydsytpa lilagamcfa aaamvfiinr
      421 paarpvlqas
//
LOCUS       WP_010659637              71 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Brucella/Ochrobactrum group].
ACCESSION   WP_010659637
VERSION     WP_010659637.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..71
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7368
     Region          3..69
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 maqtglvkff ntekgfgfik pddggadifv hisavqasgl tgladnqkvs yetepdrrgk
       61 gpkavnitvt g
//
LOCUS       WP_010659659             400 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent aminotransferase
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010659659
VERSION     WP_010659659.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..400
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43377
     Region          1..400
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,207,236,238..239,247)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,200,245..247,276,279)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            239
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mafladalsr vkpsatiavs qkarelkakg kdviglgage pdfdtptnik qaaidainrg
       61 etkytpvagi pelrqaivak fkrengldyk peqvivgtgg kqilfnafma tlnpgdeviv
      121 papywvsype mvainggnpv fintkiednf kltaadleka itpktkwlif nspsnptgaa
      181 yteaelkalt dvlvrhphvw iltddmyehl vygdfvfttp aqvepslydr tltmngvska
      241 yamtgwrigy aagplqlika mdmvqgqqts gacsiaqwaa vealngtqdf ipenkkifqa
      301 rrdlvvsmln qakgikcptp egafyvypsc adligkktea gkviesdedf vtelleaegv
      361 avvhgsafgl gpnfrisyat sdalleeact riqrfcaslr
//
LOCUS       WP_010659682             185 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fasciclin domain-containing protein [Brucella].
ACCESSION   WP_010659682
VERSION     WP_010659682.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Clout,N.J., Tisi,D. and Hohenester,E.
  TITLE     Novel fold revealed by the structure of a FAS1 domain pair from the
            insect cell adhesion molecule fasciclin I
  JOURNAL   Structure 11 (2), 197-203 (2003)
   PUBMED   12575939
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..185
                     /product="fasciclin domain-containing protein"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=19362
     Region          12..183
                     /region_name="FAS1"
                     /note="Uncaracterized surface protein containing fasciclin
                     (FAS1) repeats [General function prediction only];
                     COG2335"
                     /db_xref="CDD:441906"
ORIGIN      
        1 mnpftfrals aatvmlvaat sayaenpnvg gspmyankni venamnskdh ttlvaavkaa
       61 dlvetlkgkg pftvfaptne afaalpkgtv dellkpenka kltkvltchv vaadamskni
      121 kkmiaddkgs hdvktvggci lkakesgdki tltdengnva nvtiadvkqs ngvihvidkv
      181 llpkm
//
LOCUS       WP_010659733             311 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cell division protein FtsQ/DivIB [Brucella].
ACCESSION   WP_010659733
VERSION     WP_010659733.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..311
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=33700
     Region          90..286
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mfalngksdg ygrsgsmrda sgatgaafvl prflrkpfrf aarlfqgnvn iprhagtvgm
       61 lgflgatgly gmavgghtpe vvkatastlg faiedikvvg nnetsdidil gqldldgets
      121 lvglsaeear qsidklpwve saevrkvypg tvlvslherk afaiwqndkd lalidaagdt
      181 ivpfrpgryn slplvvgdga ekkvkgfvde iaaypglagk vrayirvgdr rwdllldngv
      241 rimlpetdpl kalaqvekld qdqhllsrdi aavdlrlddr vtvqltasgm eqrqkflaer
      301 kkelsrtgkr v
//
LOCUS       WP_010659770             263 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Brucella].
ACCESSION   WP_010659770
VERSION     WP_010659770.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 263)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..263
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29897
     Region          8..262
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mrfhkseraf filivlmfgi glllyqarvd igqlqtlpld anayelvsrl dqlnhvtiwv
       61 liatiacglf liypqirtda ldhgklqvit qdlsersqtl ehaaltdslt gmqnrryfde
      121 alkeylvqfd riqrpvglmi idldhfkavn dtyghdigdv vlqevarclk dytryhdvva
      181 rlggeefavl apnmdaelmi klanrirkai stleidlgde klgvtvsigl aiwdrretsk
      241 dlyrradkml yaaknmgrnr vca
//
LOCUS       WP_010659788             147 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Brucella/Ochrobactrum
            group].
ACCESSION   WP_010659788
VERSION     WP_010659788.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..147
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15990
     Region          1..146
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myknilvttd gsefaerglv hafklartvg akatvltvta pysvsglpgg wtdspafier
       61 feqewneyad kslararela aetevevhtl hvvaphpats iietskelrn dlivmashgr
      121 rglkgmllgs qtyevltrsn tpvlvvk
//
LOCUS       WP_010659797             376 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Brucella].
ACCESSION   WP_010659797
VERSION     WP_010659797.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..376
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41158
     Region          11..373
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 madraevvva gligsgfmgk thalalanvn rvfdlpidvq lhtladvnse taskaakqlg
       61 fanatgdwre litnpdinli dittpnrfhk emalaaieag khvycekpla ptaaeclemt
      121 laaerrgvqt avgfnylknp miklakeiid sgelgeirsf rgihaedfma daripwtwrl
      181 ypaggggala digshiiaaa rylvgpittv mgdavtiine rpdslnlsqm kpvetddvcr
      241 afvrfengat gtieaswias grkmqhdfei sgskgslffs qerfneldlf lfsdkkgqqg
      301 frkifagpeh epygafcvag ghqigfndlk tievrdflla iagqktnhad fregyevqka
      361 vetiyassre hrwknv
//
LOCUS       WP_010659799             376 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Brucella].
ACCESSION   WP_010659799
VERSION     WP_010659799.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..376
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39553
     Region          34..373
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mseplpheka ntaalskder lqsaspmqrl lsrpelgavs glilitvffv svanpamfta
       61 agimnfmapa sqlgilavaa allmiggefd lsigsmvafa glifaaalvv wqvplgvaii
      121 vtllfaafvg mvnaqivirt glpsfivtla flfilrglsl vglkwatgga tqlrgvkeav
      181 agsylaglfs gdafqglfaw maendlidkf pngepsvkgv pvevlwfiai aliatyvlvr
      241 trfgnwifaa ggdalaarns gvpvrrvktt lfmctamaaa lvailtvlda gstdarrgfq
      301 kefeaiiaav iggclltggy gsaigaffga iifgmvligl tytqidqdwy lvflggmlli
      361 avlfnnfirk ratger
//
LOCUS       WP_010659806             344 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Brucella].
ACCESSION   WP_010659806
VERSION     WP_010659806.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..344
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36514
     Region          4..323
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mmplveisnl kvafdgvpvl hgidlsierg eavglvgesg cgksvtwlaa lgllpkkasi
       61 sgsvllegte lltasrstle gvrggriami fqdpssslnp virvgrqiee avrlhrnlrg
      121 paarsevlrl melvgipdar rridnyphef sggqnqrlmi amalagnpdi liadepttal
      181 datiqaqild llaalraetg mavvfishdl gavsqicerv svmyagrive qartealfaa
      241 prhpythglf dsipnldsgr nrlipiegtv pepgklpqgc afsprclsan dlcarslprl
      301 gvpqddageg rmvacfhpys aasyllpsig ghistpastr aiaq
//
LOCUS       WP_010659885             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Pseudomonadota].
ACCESSION   WP_010659885
VERSION     WP_010659885.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadota (proteobacteria)
  ORGANISM  Pseudomonadota
            Bacteria; Pseudomonadati.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     Protein         1..146
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16603
     Region          1..129
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mrylhtmvri rdidesldfy vnklgleeir rtendkgrft liflaapsdt drakaerape
       61 leltfnwdpe tytggrnfgh laymvddiyt tcqklqdagv tinrpprdgh mafikspdgi
      121 sieliqkgdr lapqepwasa enigsw
//
LOCUS       WP_010659869             212 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: outer membrane protein [Brucella/Ochrobactrum group].
ACCESSION   WP_010659869
VERSION     WP_010659869.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..212
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21917
     Region          71..212
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mlkrsitava lgaaivafag safaadmmga tdysyndpva agphdwsgny igaqvgasss
       61 rvpgpftnrt galggvvvgk nmqsgnvvfg gelegnfaea ehrignggsl qqswngnakg
      121 kvgyafdktl vygtagygvt rfkakdntts apgweggalv gagveqalsg plsvkaeydf
      181 qrfndvksrv ngveqrnnlk nhsikaglny kf
//
LOCUS       WP_010659962             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YdcF family protein [Brucella].
ACCESSION   WP_010659962
VERSION     WP_010659962.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..264
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29487
     Region          22..257
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mffslskifw lffqpvtiil vlvliaflai wrgsrrlsms vlglsiailf faafttlgsv
       61 llapledrfa kpdamprhvd givvlggymn gdvnagrkgf elnsaadrif eamrlarlyp
      121 darvivsggd gaffeesvke adstrqmlvd lgfsgeryiy enksrntven aifskelaqp
      181 kpgetwllvt sayhmprsvg cfrkadfdiv awpvdyktra serfalyles pnealsrfsv
      241 amrewvglaa ywlagktdml lpqp
//
LOCUS       WP_010660000             230 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Brucella/Ochrobactrum group].
ACCESSION   WP_010660000
VERSION     WP_010660000.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..230
                     /product="L,D-transpeptidase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24974
     Region          95..229
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mfsrrilmag iatlcigata pafatspvsa eaqlneaaas vqqvalssda kanpekpkkk
       61 kasksgnavk ankynidpkf raqevaftgy kpgtividpk qrflylvets ttarrygiav
      121 gkqglefkgt gtinakrewp rwiptkemie rdpahygrfk ngmdggpgnp lgsralylfq
      181 gnkdtyirih gtvqpwtigs sasngcfrmi nedvmdlyer vglgtevvvl
//
LOCUS       WP_010660015             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CinA family protein [Brucella].
ACCESSION   WP_010660015
VERSION     WP_010660015.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..163
                     /product="CinA family protein"
                     /calculated_mol_wt=16689
     Region          7..160
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 msaliaedka iavleacrka gvmiamaesc tggliagslt diagssdvvd rgfvtysnea
       61 kaemigvpme linrvgavsk evalsmaega lsrsragvtv avtgvagpgg gsdekpvglv
      121 hiasarkghp plhreyhfgp ktraeirhat vfaaldlvle nlr
//
LOCUS       WP_010660033             260 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP12 family chaperone protein [Brucella].
ACCESSION   WP_010660033
VERSION     WP_010660033.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009246
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..260
                     /product="ATP12 family chaperone protein"
                     /GO_process="GO:0043461 - proton-transporting ATP synthase
                     complex assembly [Evidence IEA]"
                     /calculated_mol_wt=28577
     Region          29..260
                     /region_name="Atp12"
                     /note="Mitochondrial FoF1-type ATP synthase assembly
                     chaperone ATP12 [Posttranslational modification, protein
                     turnover, chaperones]; COG5387"
                     /db_xref="CDD:444150"
ORIGIN      
        1 mrdilsdlea gkqlsdenpi vraqkqmlaq lpkrfyekae vaeveggfav hldgrpvktp
       61 arnllllptk aaaqivadef taqekvidpg kmpatrlvnt aidgiaqdpq avfedilrfa
      121 gtdmlcyrad spqelvsrqt eqwdplidwm eglgarfsla egvmhveqpr eaiaafgvhl
      181 agfkdpiala slhtmttltg saiialaiak geitaeqgwn lahidedwti ehwgsdaeai
      241 errenreiem mmaarvlkal
//
LOCUS       WP_010660055             331 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MlaD family protein [Brucella].
ACCESSION   WP_010660055
VERSION     WP_010660055.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..331
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35614
     Region          1..319
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 metkanyvlv gvftlivsll afafvfwiar fgeardslel dvripgsvtg lsigsqvlfn
       61 gikvgdvral rldpsnpemv ivktrvnatt pitrstaatl gfqgltgqay ielkggrlde
      121 pnllteaanv dsvaridadp ssinnllata qdiaaranav lgqlegfvkd argpltdtin
      181 ntktftdala qnaniiqelg entgninqiv tdakdmmarl naasvrvdai laktdkllss
      241 ddkdgvvaqa katlesirqt sdnldkrmgp iadnlqrfsg qglrdvqsvv vdsrrsiqri
      301 eqaitdlern pqrlifggkg nvpqydgrtr h
//
LOCUS       WP_010660116             196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptidylprolyl isomerase [Brucella].
ACCESSION   WP_010660116
VERSION     WP_010660116.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..196
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=20584
     Region          27..194
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 msfirsalaa vaffalsqga vqmasaanae ntvvlklkdg dvaiqlrpdl apkhvaqiek
       61 lvgegayngv afhrvipgfm aqtgdvkfgn vdkgfdasrv gtggsdypdi paefskepfv
      121 rgtvgmarsq npnsansqff imfadgafln gqytvvgkvv sgmeivdkik kgseadngav
      181 enpdkiikat lqadkk
//
LOCUS       WP_010660156             294 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Brucella anthropi].
ACCESSION   WP_010660156
VERSION     WP_010660156.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..294
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=31695
     Region          64..167
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mskifslkla rqtaeaflke egllslpvdp faiaasrdiv vegkpenteg vsgmllrhgn
       61 nfgivyathi qspgfqrfsi shelghyflp ghvdqvikng vhvsragfat ndpyeleadh
      121 faagllmpek pfrnalegfg hgleaidqma dlcitsrtat airyaelsds avavivstrg
      181 vidycfmsda mkslpkldwi rkgtplpsgt ataalaadpd rvvggdravd evdvrdwlgg
      241 ttratvseea lglgsygrvl tvltsgtigq edesdedadd eealveswtp rfrr
//
LOCUS       WP_010660252             141 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein [Brucella
            anthropi].
ACCESSION   WP_010660252
VERSION     WP_010660252.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..141
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15373
     Region          31..76
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(46,48..50,52,63..64,68..69,72,76)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 marlefskkt krdalersqm rceasgplyg leegqrcsip lsngvefdhe laasnggdns
       61 ienckavclr chrwktanld tpraaktkrq sdktkgivrp kgaiksagfi kavkpskals
      121 kplpprkrdi fgrpvsegar p
//
LOCUS       WP_010660290             265 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Brucella anthropi].
ACCESSION   WP_010660290
VERSION     WP_010660290.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..265
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28306
     Region          6..251
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mssnlslekg llilnllkea realgvreig rrldltpsva qrllnslasq gyveqesnrr
       61 yqigyavlgl aqhvfqrgrl lalaeeelkk laaggcfngf lgirrgsvgv yvlavqsdsp
      121 vviraqpget malhstalgk allldmgdtg vrtllgdkpl lrltertvie ldrladqlhl
      181 grslgyttai senlegvisv gapiydasgs itaaisvafp ravypkvkig dvaqgilaaa
      241 crisrglgfe rqriseedet vdvat
//
LOCUS       WP_010660334             122 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2147 domain-containing protein [Brucella anthropi].
ACCESSION   WP_010660334
VERSION     WP_010660334.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Barison,N., Cendron,L., Loconte,V., Proctor,E.A., Dokholyan,N.V.
            and Zanotti,G.
  TITLE     Protein HP1028 from the human pathogen Helicobacter pylori belongs
            to the lipocalin family
  JOURNAL   Acta Crystallogr D Biol Crystallogr 69 (Pt 8), 1387-1394 (2013)
   PUBMED   23897462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..122
                     /product="DUF2147 domain-containing protein"
                     /calculated_mol_wt=13169
     Region          1..122
                     /region_name="COG4731"
                     /note="Uncharacterized conserved protein, DUF2147 family
                     [Function unknown]"
                     /db_xref="CDD:443765"
ORIGIN      
        1 mkwiltigim tvsfpftaqa aeingnwvrg dgnarvkiae cgkdicatnt wikpgtpkek
       61 tgdrlvmsin etangqysgt afdpqrnlty kisvkvdgdt mtsngcvlag llcrnvgwtr
      121 ik
//
LOCUS       WP_010660356             125 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system VapC family toxin
            [Brucella].
ACCESSION   WP_010660356
VERSION     WP_010660356.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..125
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /calculated_mol_wt=13862
     Region          2..107
                     /region_name="VapC"
                     /note="Ribonuclease/mRNA interferase VapC, contains PIN
                     domain [Defense mechanisms]; COG1487"
                     /db_xref="CDD:441096"
ORIGIN      
        1 miladtsiwi dhfrrgdndl vkiigndlll chpavigela lgslrdrtav ltflraqret
       61 ivathdevmt lierhsvfsm gigytdahll asvlldqrts lwtrdkrlkl aalkagaaly
      121 epfhs
//
LOCUS       WP_010660368             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor [Brucella].
ACCESSION   WP_010660368
VERSION     WP_010660368.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..214
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23798
     Region          6..200
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 msisqlvfiv ddderireal eellasygmr tlsfgsardy vnahkpdvps clvldvelpd
       61 inglelqkqi svqehppivf itghgdipss vramkrgavd fltkpfsdak llaainaaie
      121 qdqqlrnsra eiellrqryg eltsrerevm plvvsgllnk qaaaelgise vtlqlhrrnv
      181 mqkmaaaslp dlvriaerlr ipithsrrsk geel
//
LOCUS       WP_010660361             403 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Brucella anthropi].
ACCESSION   WP_010660361
VERSION     WP_010660361.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..403
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=43442
     Region          3..382
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mskhilivga gfagvmaala asrlrheknv saedleitvv spepelvirp rlyepepekm
       61 taplgdlfst teinfiagtv ekidvagsqv aiidgngrsf lqsydrlvla agsrgfqppi
      121 pgleeygfas nhldeavild qhlhrlvdrp aspardtivv ggagftglev ateletrlrg
      181 ilgsrahpri iivdrnphva pamgenprpy ieqrlkelgi etrlntgiak ldensvtldn
      241 gerietatvi wsggmraspl tsqleaerdq lgriivepdl rvpghsqifa tgdtakaatd
      301 negnfslmsc qharrlgafa ghnaaaellg eptlaysqpa yvvcldlgad aaiftrgwsg
      361 kveitgtdak kvkqeintvw iyppapdrat ayenvhiart vdf
//
LOCUS       WP_010660377             303 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Brucella].
ACCESSION   WP_010660377
VERSION     WP_010660377.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..303
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33451
     Region          22..278
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(37,124,126,128..129,158,212,233,236,247,249,278)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mkhetnlsks gpdelvpsry alrigeidvl visdgvlplp temlghnidp dvraewfddm
       61 ylppdsfdws lnvvvvrsgn qtilvdaglg ldpdlnlpra gqlvkrlaga gidlasvtdv
      121 vlthmhmdhi ggllvegvke rlrpdlrihv aaaevefwes pdfthahmpd gfpdalrata
      181 krfveqyrdq lclfdeqcev aagvvayrtg ghtpghcvvr lasgedrltf agdaifavgf
      241 dhpdwyngfe hdpeeaarvr vrlltelaet geqlvathlp fpsvgrvavd gdayrwvpvf
      301 wdy
//
LOCUS       WP_010660399             299 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Brucella anthropi].
ACCESSION   WP_010660399
VERSION     WP_010660399.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33313
     Region          1..60
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..283
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(105..106,108..109,112,116,118..124,217..222,
                     228..229,231..232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrqlqcfvvl aeelsftraa qrlnmsqppl stqiqtlere lgvdlinrts rkvaltragk
       61 lfrqyatnml vqyerslqem reiqhgqegl ieigttgsil rgglsellsn faqahpqitl
      121 riheqsptaq idevrrrrtd vsfnrsiphg nelayehawq eelvalvrsd hklagrtsit
      181 mtdlrddpfv ilqpessdfa ayvmsyvvas gyrprisqqv idaqsipsli aagfgvsivp
      241 agiahltsgp lvflpirpdp pvsdiymiyh addpapalql fltrisqevn strsgqkar
//
LOCUS       WP_010660447             549 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [Brucella].
ACCESSION   WP_010660447
VERSION     WP_010660447.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..549
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60719
     Region          1..534
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mnevadyiiv gagsagciaa nrisadpsvt vhlleagrkd rnpwihipvg yfrtmhdpny
       61 dwcyqtepds glngrslswp rgkvlggsss lngllyvrgq kedydrwaqf gnsgwswqdv
      121 gpifesfetf hrpaaadrgt mgelqvsapr lkraicekwi esarangydy npdyngatqe
      181 gvghfqltmh kgrrcssaaa flrpirhrqn ltiqtdahim rvvvqngrat gveyqrpdgt
      241 rhtiharnei ilcagaigsp qilmlsgigp aeqlaahgis vqydapevgq nlqdhlqarl
      301 vfkcneptln devrslikka aigleyalfr tgpmtmaasl vfgfvktrpe latpdiqfhi
      361 qpwsadspge gvhpfsaftq svcqlrpesr gtitlrsrnp fdhpviqpny latrndqqtl
      421 vegiriarri arteplksai aqefrptadl ngddelldwa rrnsttiyhp tgtcrmgvde
      481 rnvvddrlrv rgieglrvad csimpeivsg ntnapammig aklaqmvled rkraltaqna
      541 atptyekva
//
LOCUS       WP_010660461             326 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Brucella anthropi].
ACCESSION   WP_010660461
VERSION     WP_010660461.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..326
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35593
     Region          12..311
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mlvrpidqii hkaawlyyth glrqdevaqr leisrasiam ylrkaremgi vtistsself
       61 sddvlarele datglntvwl vpedrqamdp aaempvvaas vflellnkgd rvgvawgrtv
      121 yhiadvmpfa dlssvtvvql cgnlgapysy rpdqctteia rrlnaeginf yaplvlsser
      181 ladelrgepv ikeqlatipd cnlalysvgg ieddshlvkc galsaadmha mgekgaagvi
      241 agqlidrdgq wldcnhnrrc isadlasira ikkrmlvvqe dnkfeplvaa lkgdfashlv
      301 ittsmarril drwsedglgk ggsska
//
LOCUS       WP_010660492             284 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Brucella].
ACCESSION   WP_010660492
VERSION     WP_010660492.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..284
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31691
     Region          1..281
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mskeilirlq saelrkskad kliasyiern laelpfetak siaerlgisq mtvgrylrrl
       61 gfdgleelkt alrrgrsnpa wqvkgpvarl qqdfregkll aglvqqqien lgtvyelttr
      121 pewqetidal igasevyvaa yqnvrgiaqy fasqlsysrp gvsfmdglng tyaevldgsr
      181 enrvlflhdv rrfaskarpl aiearrmgvk vilftdefcp wasevadial ivpgshgplw
      241 dgaatmtaim dlmlshiiiq lgsqvdervq sltrlqdifg dfes
//
LOCUS       WP_010660612             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010660612
VERSION     WP_010660612.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..231
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25781
     Region          15..227
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mslidrglvr klslfakmsd geldklvsya ttkrvppgea ifeqgddavl fylllhgrlk
       61 vnqitpdgqq iivrmvhpgd lfgfaralqr sdypgtaiav aesivlawpt elwdyfveqn
      121 pglamnaiqt igkrleeaht riremsteev errvahtvlr larqagrked dgiridfpit
      181 kqdiaemtgt tlhtvsrilt gweaqgfvrg grqkltvlnm sgvrrladge r
//
LOCUS       WP_010660556             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Brucella/Ochrobactrum
            group].
ACCESSION   WP_010660556
VERSION     WP_010660556.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28774
     Region          3..255
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mtkngpfalf fhtlivifml apmvvvclva ftpentltmp wnglslrwfa avfahndfmt
       61 sfynsvqlaf fsasistlla vpsglaiaqy nfrgrdalna lflspliiph lvlgvaflrl
      121 fslmgftgsf vwlvaahsiv vtpyalrlil aslgsmdrna enaartlgag ewtvfrrvtl
      181 pllvpglsgg wllafinsfd eltmsifvts pstvtlpvrm ymyasesidp mmaavsalmi
      241 lvatvtmiii drmfgldrll vgkg
//
LOCUS       WP_010660569             288 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010660569
VERSION     WP_010660569.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..288
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30362
     Region          3..285
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 meqviangly lgaqyalial gltlifalmn vlnfahgqmy vlggfvtytv ygqlglpfvv
       61 allasavtlm ivgaliekfl frpvikrslr destmllaaa vaffldavil llfgekqrgv
      121 pkivngvfvs dslimpydri ligvlavvfi aafvlfmqyt kpgramrala qdrvaaqlmg
      181 vnvdrysmig falgamlagl vggllvaitg vnsgiggais ikafmmvmig gagvvsgaia
      241 ggfilgmmes vgltvlrsyg ditylvifaa lmvflsirpn glmgkpwg
//
LOCUS       WP_010660621             341 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Brucella].
ACCESSION   WP_010660621
VERSION     WP_010660621.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..341
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35056
     Region          7..313
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mqktsnqlam lvvinlglla lgayisggsf lslfnlqsma gqvpeiglla igvmlamcag
       61 nggidlsgia lanlsgvlsa vivsmfissa enqlgfslaf iglalvigla ggivngilia
      121 rfnitpilct lgtqmaftgl avvvsggrav mvgspdllsr igndmflavp isflifiava
      181 lliaavvrft pygywlmlmg tnpkaavfag fprngvliat yatsgflaai agiiiaarnv
      241 nvkfdygssy llvailiavm agvkpeggyg rvicvvlsai alqlmsslln fgglsnfvrd
      301 fawgllllaf lavgkydiag fftlgnrqkg nigaqpsgtr t
//
LOCUS       WP_010660627             304 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Brucella anthropi].
ACCESSION   WP_010660627
VERSION     WP_010660627.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33419
     Region          8..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..295
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     224..228,235..236,239)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mdrnllpala afaevaregs ytraagrigi spsglsqair tleqqlgvrl lnrstrsvsl
       61 tddgrkllsq vepglamish avvavgeard kpsgeirlna prvvahhfie phlgefarry
      121 pevrvelfvd dglgdivreg cdagirlres vtdtmvavpi tlpvslaivg spayfaanpp
      181 pkrfedladh ncrgfrqtss gtvfrweltd prsgeerlfq pfgtfatnsd dvmlsaalqg
      241 vglvmhldfa vrqhlasgal vrvmeewclp fegfnlyvss reqmpaklra fvdflvekrr
      301 qlep
//
LOCUS       WP_010660672             329 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SPFH domain-containing protein [Brucella/Ochrobactrum
            group].
ACCESSION   WP_010660672
VERSION     WP_010660672.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..329
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35687
     Region          22..292
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mtgfditlli laalvlatlf agiktvpqgf nytverfgry trtlnpglnl ivpffdriga
       61 rlnmmeqvld vptqevitrd naivgvdgva fyqvlnaaqa ayqvanlqya ilnltmtnir
      121 tvmgsmdlde llsnrdaind rllrvvdeaa hpwglkmtrv eikdinpped ivtsmarqmk
      181 aerdkraqvl eaegdrnaqi lraegqkqsq ileaegklea akreaearer laeaeakatt
      241 mvsdavangn vqalnyfvaq kytealsnia saknqkvvlm pleasaligs lggigaiake
      301 vfgdgsrpvd papqpptpsr prsvpsagr
//
LOCUS       WP_010660707             353 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010660707
VERSION     WP_010660707.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38595
     Region          1..353
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 maflniknlk ksfgantvvh dfnlavkkge fvsflgpsgc gkttvlrmia gfeapdngai
       61 eidgkdvvdl kpnqrnigmv fqayalfpnm tvaqnvsfgl rvagkpkaei datvqemlgl
      121 irldhladry pyqmsggqqq rvalaralat kpqvllldep lsaldakiri slreeiraiq
      181 qklgittvfv thdqeealsi sdrivvmheg radqigspfd iynrpasrfv asfvgtlnml
      241 easvsepgkn sieldgrtit vqekldhhpk gkpvtlalrp eavslearks hdtsldatie
      301 dvhflgsvir trvalgknrl sfdtfndptq pppqrgdkvt vhfashdllv lad
//
LOCUS       WP_010660758             138 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Fur family transcriptional regulator
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010660758
VERSION     WP_010660758.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..138
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15300
     Region          13..135
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 msthhhhhap qdltrnqtlv fdvlskaegp lsaytildql rddgfraplq vyraleklld
       61 ygmihrlesl nafvacahpq chqqglvafa icekcgqvte fsdaaienlv sawslqngfk
      121 srkttlelrg lceacgeh
//
LOCUS       WP_010660788             117 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Brucella].
ACCESSION   WP_010660788
VERSION     WP_010660788.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..117
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13293
     Region          <44..115
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 mtkqavvlkr eewarrddaw sgrvegkrfd tdasiiffst divghgpklh rhpydeifiv
       61 rqgnalfivg deqievtegq vvfgpaniph kfinlgpgrl ettdihvtrh feqedle
//
LOCUS       WP_010660812             546 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: N,N-dimethylformamidase beta subunit family
            domain-containing protein [Brucella].
ACCESSION   WP_010660812
VERSION     WP_010660812.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20801894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..546
                     /product="N,N-dimethylformamidase beta subunit family
                     domain-containing protein"
                     /calculated_mol_wt=60469
     Region          98..525
                     /region_name="DUF6605"
                     /note="Domain of unknown function (DUF6605); pfam20254"
                     /db_xref="CDD:466405"
ORIGIN      
        1 mserhlnefp dfgltpaqrr eavlghyyey pgmdgprgei wcytdaysyl pgatvhlqvs
       61 atasrfdiei vrdgavetpv fskrgidckw qetpaqcsvv gcgwettfaf ktdenwpsga
      121 yritlkahgn dgqpihchhl filrpaagrk pgrilqvaat gtwtayntwg gsnhyqgitg
      181 pngdqyattv sierpfcrgf vvlpsdaprv pleivtppaa ppryphmewa yangyskkyt
      241 ssgwasydsl ffrwaeregy avdlasqhel hfspeilegy dcvafvghde ywtwemrdav
      301 dnyvdgggra arfagnfmwq trledngkrq tcykyrarae dpvyrsadpr rtsgcweate
      361 tgrpaaetfg lnalrglyvg wggcaprgvr gfpvyrpehw afagtgiyyg dllgseghaf
      421 gyevdgldyv irgglpepee gsgapdglqi lalgmsslke esadipaddq flsdadakfv
      481 adtligdngd aaverikrgc gmivnfprgk gevfhagsce wvaalkrgdr mvervtanvl
      541 nqylkr
//
LOCUS       WP_010660843             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CDP-alcohol phosphatidyltransferase family protein
            [Brucella].
ACCESSION   WP_010660843
VERSION     WP_010660843.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..201
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21241
     Region          28..174
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 msvyqlkshf qnllrplvvr laaggvtanq vtvaaalvsi ilgaflalsg naawfalvpi
       61 wlflrmalna vdgmlarehg qkstlgayln eigdvvsdaa lyapfaiiap ftgpwlfaii
      121 flatltefag vagasvgasr rydgpmgksd ravvfgvlga wisidgilpq wifwlqpllc
      181 lllvattvkr itngineaks g
//
LOCUS       WP_010660881             317 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Brucella anthropi].
ACCESSION   WP_010660881
VERSION     WP_010660881.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..317
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34638
     Region          10..317
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mifepsdeel svtllvlpdc slmslaatld pmrganrvtg rslyrwrvvs pdgsdpvtss
       61 glkvaangrf evgaqdilii vsafhaleha tprllamlrq aakqsklvvg veagswvlak
      121 agllngrkat thwedmeafs qrfpevemqs drwvrdgafl ttggaapald mmlalirarh
      181 gysialdvas lyiydevkqa sdaqplvslg rllnreprla daikimethi drpipvssia
      241 rrlglstrsl ellfanvigq spgnyylslr lkaarrlild thlsmadtae qtgfssissl
      301 srafkrhfgq spsklrq
//
LOCUS       WP_010660911             178 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Brucella anthropi].
ACCESSION   WP_010660911
VERSION     WP_010660911.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483007
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..178
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18794
     Region          26..173
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; pfam01613"
                     /db_xref="CDD:460266"
ORIGIN      
        1 mmnrnvlhid rdaigavskr efadamsrma atvsvltacd ageahgrtvt avlslsaepp
       61 mvlvsvksds alatailsdg gfslamlakg qemigdafag nvppaqrfli gvwgewpsgr
      121 prlfgasaai dcelagnipm adhtlfaglv tntdlplhsr pllwarrnyr alrhdadl
//
LOCUS       WP_010660905             348 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Brucella].
ACCESSION   WP_010660905
VERSION     WP_010660905.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..348
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38190
     Region          1..333
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrllilgtgg maknhaeafk aiegvevvaa cdvsaervdg fsenhdihnr ftrledalew
       61 grfdavanvt pdaihhpttl alvgagkhvf cekplaesye kaaemadaae qanvinmvnl
      121 tyrnvaplqk aremvmagei gqvrhfeasy lqswlvsktw gdwkteskwl wrlstrhgsn
      181 gvlgdvgihi ldfasyaigs dverasarlk tfekadnnhi geyvldands fvmmaeytng
      241 algvihasrw atghlnelrl rihgdkgale ilhtptgssl rgsigediet pvwrdidagt
      301 vetnyqrfar avadgaelep sfrhaanlqr vldhamtvdr plpevvsg
//
LOCUS       WP_010660896             435 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Brucella/Ochrobactrum group].
ACCESSION   WP_010660896
VERSION     WP_010660896.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47311
     Region          25..407
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,262,265..266,269..271,274,302,306,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mvnstlsavg atpdlrdsti rklnlrivlf cficfivnyl drvnigyaal hmnndigltp
       61 ymfgigagif figymlfevp snmmlhklgs rvwiarimvt wgivscamaf vqgpvsfyvl
      121 rfllgvaeag fapgvllylt ywfpakergr atalfmtatv lsivvgapfs gwlmdagegl
      181 fglhgwqamf ileglpavil gvvtffylvd spekdkrwlt aderawlmae lakenagkqa
      241 dtrhslkevf sdyrvwlltl vymfngiavy gvimwlpqiv kslgdytaaq tglisaipfv
      301 faaiglvvis rssdrtgerk ihtaiaglfg gvflaasala pspilslvll svcafflwsy
      361 lgvfwtlptq flsgaaaagg laaingfaql ggftgpylvg wvksttdsfs lsllalsifp
      421 ilgfflcmsl kakrd
//
LOCUS       WP_010660914             132 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Brucella].
ACCESSION   WP_010660914
VERSION     WP_010660914.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..132
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14252
     Region          15..128
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mprfianild shaslllarv vltfifwssg laklfnfgan aaemesfglh pgwlfnsatl
       61 llqivgslmi ifnrgiwlac galavftilt ipvahpfwak egeeafrdmt valehislig
      121 glalaailsr kv
//
LOCUS       WP_010660932             471 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aspartate aminotransferase family protein [Brucella].
ACCESSION   WP_010660932
VERSION     WP_010660932.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..471
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=51830
     Region          40..456
                     /region_name="ArgD"
                     /note="Acetylornithine/succinyldiaminopimelate/putrescine
                     aminotransferase [Amino acid transport and metabolism];
                     COG4992"
                     /db_xref="CDD:444016"
ORIGIN      
        1 mnktnttlkp klltvaeaka ldlprmtelf tthlnpgqlh fmkllgfhkv kieraegmyy
       61 ydqngraild ffggfgslaf ghnhprilea rrqfqeemrh eiaiafmsqy aaalaydiaa
      121 cspgdldmvf lgssgseame aaikvaeraa gpkkpkivya ensfhgktkg vlsitdggly
      181 rgefklvdnt vrvpfgdiaa ienvfrsdpe igvivletvq ggggiiqada efwqklrslc
      241 dqygviwvad evqcglgrtg kfyafehygv ipdvtalaks lgggktamaa miarrdvymk
      301 aygtpktami hamatfggig eacvtsieal nvlydehlid naadvgeyll drlhelqsry
      361 pallkdvrgk gmmvglefhd fsqtmpvvlr pvlamldekl kgslpgfigs hllrdhgvlv
      421 afteynrnvi rlepplicgr ehvdafikal devlsrgivr ivrdfvkaqi k
//
LOCUS       WP_010660945             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Brucella].
ACCESSION   WP_010660945
VERSION     WP_010660945.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..282
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31308
     Region          1..280
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 masrlvlriq eryakltage qkiaqlvler eddilihsat eiaemagvsk attarffqhl
       61 gyadfnevkl qareernrte pfeysstvde evplvrtisa hldleianit rtfealrsdk
      121 mreaaeliae aprvwviglg deegfaryar llfsrlrhsv mllginqgsw aedlamtgpk
      181 dvlllitlpp hrallkqilg yavtsrlniv titdrgsvfe aqryarvvlp chvdsiglga
      241 sytavssair llaltyasya gksaqqrlei vagihdeldd td
//
LOCUS       WP_010660953             275 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Brucella].
ACCESSION   WP_010660953
VERSION     WP_010660953.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..275
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29614
     Region          24..274
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msassstvpa etapaddtea kstrrsrvsg idralqvidy lyetgapagp yaiakaikap
       61 lstvyvtidd lveknmlarn adgviwlgar lyhyglayar sldfmsvath emhdlcrean
      121 eavqlcgrdg dhmlvlamad gpspfqvasr vgtrvplnwt asgrllvghl aanerielfk
      181 rcartsptgr aeidaaslse aaakafderl siqiaesdya vaciaspicd rdgqcvatis
      241 ivlpeqkvls desrytsqvr asaakieklm gwrnh
//
LOCUS       WP_010660980             215 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA-3-methyladenine glycosylase I [Brucella].
ACCESSION   WP_010660980
VERSION     WP_010660980.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..215
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=24331
     Region          15..206
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 msdvaeaktg livgadgmtr cfwpgelpdy layhdkewgv pvsddfrlfe kiclegfqsg
       61 lswltilrkr enfraafdgf dfhrvaqynq edvarlladk givrhrgkie stinnakrai
      121 elvaekgsla ayfwsfepgv kdrptvvdyp tlvanpktet siriskdlkk rgwsfvgptt
      181 vyafmqamgl vndhiegchc rthieklrqs fkrps
//
LOCUS       WP_010660986             133 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Brucella].
ACCESSION   WP_010660986
VERSION     WP_010660986.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..133
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13291
     Region          9..133
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mssitpqsng avtliarifl silfilagyg kltaisgtag yfaglglpvp tvtavivglv
       61 efvgglailv gfqtriaaai vglftigatl vahmdfsqgm nammaqknla iagglfilal
      121 hgagslsida krg
//
LOCUS       WP_010661019             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RsmB/NOP family class I SAM-dependent RNA
            methyltransferase [Brucella].
ACCESSION   WP_010661019
VERSION     WP_010661019.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..429
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=46287
     Region          6..427
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mrlggrlqaa ievldqieag trpasdvlkd wgashrfaga gdravigniv ydalrrklsi
       61 awrmdaddar alafgallad ggmdiatida aldgdkfapk vleqprriaw esrdvteapa
      121 hvqadvpqwc assleelfga rwvdegrala trppvdlrvn slkatpektl talekagaap
      181 apflaqalri ppiealgrhp nvqgeqafld gwfevqdlgs qlaalfagak pgqqvldyca
      241 gaggktlala aamqnsgqih aydaerarls pmherlqrag vrntqvhgnl daldpltgqm
      301 dlvltdapct gsgtwrrrpd akwrlndqql errvqdqkev lesakhyvkp ggrlayitcs
      361 lfaeentrqi aqfltgnadf tevapealwd tivadagdvk pvfsshgavf splstgtdgf
      421 yvsllqrsn
//
LOCUS       WP_010661041             582 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycerol-3-phosphate dehydrogenase/oxidase
            [Brucella].
ACCESSION   WP_010661041
VERSION     WP_010661041.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..582
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=64207
     Region          15..>46
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Region          32..556
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 mnrkeildgl rqspkvdvcv vggginglsv frelalqgvn vllveqsdyc sgasaalsrm
       61 vhgglrylen gefslvkesl verdrllrna phyvaplptt vpifdifsgl gngivrflgl
      121 trrpsrrgai aikaglgiyd fltrkralmp khrfrsrktt lakwpslnpa irssatyfda
      181 wvshperigv ellrdglsag pnakalnyaa icesgggdfq lfdgissetl siqprlvina
      241 tggwidiang tlfpkeaqpa plmgvtkgsh livdnpalsd sldghmiyye nedgricilf
      301 pylgkvlvgs tdirvddpgt vrceaderdy ilqslafvlp eikirpeeiv fqfagvrplp
      361 asndsftgri prdhfctvle gqdnrppvlc miggkwttfr sfgemaadma lkrlglsrri
      421 dtteraiggg rafpkdraiw ieklttatrl padrveilfk rygtgateia hfiaegsdya
      481 lpnaaysrre lsylirteai ehlddlllrr ttlaisgels lamteavldl lateknwspk
      541 yrdaelmrfl tlmrerhgva aetlsarneq rselcektak sg
//
LOCUS       WP_010661033             504 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Brucella].
ACCESSION   WP_010661033
VERSION     WP_010661033.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..504
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52851
     Region          22..496
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,147,
                     150..151,154,278,281..282,285..287,290,318,322,374..375,
                     379,383,399,402..403,406..407,410)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mttvlasapr vtnstfillt astgcamtvl dtnvvamvlp tiarefsasf advewvisty
       61 vlcfaslllp agaladrfgr rtvfligiga fafsswlcgv adsatslyla ralqgasaaf
      121 qlapalaiig htfhrdeern rawsiwggim gltmvlspii ggliahslgw rwafyinipi
      181 givlalatlr sitdskdena rrvdpigiva fastmfgltw glingqahgw tsstaiagfv
      241 gglaglaifl vaetvqqrpm ldlslfrnpr figgvwamfa yaacaqvmas mlplflqngf
      301 gqpplqagfa mlpfasamli fpnvgrflgk rmssreilsf glmivgigsl vtsfgahsga
      361 wsivmsgmfl igsgggllng etqkaimstv ardragmasg isttarftgi llgfavlsgv
      421 lasavrthlm qagcndptcr enfadaivag dlpnalgmva psariaatel amrgysagfs
      481 vailvsaiva iassllvycl mkrq
//
LOCUS       WP_010661063             397 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter permease [Brucella anthropi].
ACCESSION   WP_010661063
VERSION     WP_010661063.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..397
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43007
     Region          1..397
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 masysaterr qdsggtslly dprirgifyq vivfgaviga iywivgntit nlqraniasg
       61 faflngragf disqtliqyn sdsnygrafl vglvntlyva algvitasii gflvgigrls
      121 rnwlirkict vyveifrnip pllviffwyf gvlsvlpqar dsfalplgty lnnrgffmps
      181 piwgegawll pvalligiva svivarwakr rqmatgqsfh tirvsaalii glpilaliat
      241 gfpvsfdspk lgtfnltgga qikpeflalf lalsfytasf iaetvragvl gvnkgqteaa
      301 yavglrpgqt mrliivpqal riiipplssq ylnliknssl aiaigypdlv avggtilnqt
      361 gqsvevvaiw mviylgisli vsglmnwfna kmalver
//
LOCUS       WP_010660923             599 aa            linear   BCT 01-JAN-2025
DEFINITION  dipeptide/oligopeptide/nickel ABC transporter permease/ATP-binding
            protein [Brucella anthropi].
ACCESSION   WP_010660923
VERSION     WP_010660923.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 599)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 599)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Monnet,V.
  TITLE     Bacterial oligopeptide-binding proteins
  JOURNAL   Cell Mol Life Sci 60 (10), 2100-2114 (2003)
   PUBMED   14618258
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..599
                     /product="dipeptide/oligopeptide/nickel ABC transporter
                     permease/ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63492
     Region          11..286
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
     Region          319..588
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msalpeisaa ptavrmsswr llmsnrlaaf gffmlvlicl villapvlpl pnpdatspam
       61 rlkpvfsegh llgtdqlgrd ilsrviwgtr vsvavgfaat liaaivgsai glvagyaggr
      121 tdnlmtrgid mlmafpyill alaivavlgp glmnalyaia vvnipffarn vrgvtlglah
      181 refidaarls gkspvsills evlpnvlpvi vitmsttagw miletaglsf lglgaqppqa
      241 dlgsmlgegr aqlfnaphvs ivpglmifll vislnvlgdg vrdvldprlr sgalgrpgav
      301 tdiakdrssp mikdsqkals iagletgfvn gghftaavrs vslelergec lgligesgsg
      361 ksvtalsvmg lvasppglir ngaiylgdrd vlsmsetelt aargarvayv fqdplttlhp
      421 mypvgrqvee aiaahrriga serreqaivl ldkvgipdaa eranhyphql sggqrqrvgi
      481 amalandpdi iiadepttal dvtvqarile llrdlqrerg mallfithdf gvvseicdrv
      541 avmkdgeive tgttsevlsn pqhsytkrli acvpelgqga dflervaglf krenrrvag
//
LOCUS       WP_010661071             138 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Brucella/Ochrobactrum group].
ACCESSION   WP_010661071
VERSION     WP_010661071.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..138
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15176
     Region          1..127
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 mpkmifvnlp vknvaqstsf yeaigatknp mfsdetasgm vfsdtihvmi ldhekfsqft
       61 pkkiadantv sevlvclsae nkaevdttve kavnaggkad pgpkqdygfm ygrsfedldg
      121 hiweimwmdm eeakkvmg
//
LOCUS       WP_010661112             196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide biosynthesis/export family protein
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010661112
VERSION     WP_010661112.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..196
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21083
     Region          42..194
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mtaktihnkr kghallvalg laamtlsacs syrpappafh ealnqpymld agdriritvf
       61 eqpsltntys vdqagyiafp lvgsipargk tskqlegiia sklrggylrd pdvsaeidry
      121 rpifvmgevg aagqysyvpg mtaqkaiaaa ggfspranqe nvditrqfng kvltgrvlis
      181 dpilpgdtiy vrerlf
//
LOCUS       WP_010661126             115 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Brucella].
ACCESSION   WP_010661126
VERSION     WP_010661126.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..115
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13011
     Region          7..113
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 msrfldfdlt giepeegapl periisgapk frtwnleent egtlfagiwe stpgkwriey
       61 dewefchils grsviseegg esrevvagds fvirpgfkgs weviettrke yvikl
//
LOCUS       WP_010661130             797 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L family deacetylase [Brucella anthropi].
ACCESSION   WP_010661130
VERSION     WP_010661130.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..797
                     /product="PIG-L family deacetylase"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0000225 -
                     N-acetylglucosaminylphosphatidylinositol deacetylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006506 - GPI anchor biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=86870
     Region          37..173
                     /region_name="PIG-L"
                     /note="GlcNAc-PI de-N-acetylase; pfam02585"
                     /db_xref="CDD:426852"
ORIGIN      
        1 mltalqrier qksspalvrl hralsrlrst vtlmhtgahp ddeqsglmay lrfglgirvv
       61 iacstrgegg qnalgpergg algvirsrem eeaarildcd vhwlghgpdd svhdfgfskd
      121 gdgtfahwge kktverlvra yrterpdivl ptfldvpgqh ghhramtraa etairlaadp
      181 dafpehfaeg lmpwqvakfy lpawsgggdt yddelpppdt tltvhaagrd aatgadydri
      241 gewsrachat qgmgrwpetp ksewplhlkl pescaettil egipeslatl aevdgltlet
      301 rkqlldahls vertiaafpe retivnnllg aakslktvlt gapqgflvqh ghrlerkqwe
      361 idaalieaas lferayleea ilptggetrl vveygpgama vaitadpilp escstaceyv
      421 tpereilavs lakeaalspl fepawrslgg ngqayirlka qfddhlaacs fdleeplaiv
      481 psaslridpp aviisgkqyp spirlvvdge tgqvtftaqn gwsvgvigqd avlhgpfdpe
      541 pgltalqati ngrlawqtqv asyphigktv wrepavlpvl aldvklpdar igyigagadn
      601 vglwlkrmgf dvtdvearhl sgdlsqftti vvgifafglh adlaaatdnl hrfvengghl
      661 vtlyhrpsdg whpdrtpprk laigspslrw rvtnphaavt vldpehpllv gpniiserdw
      721 ngwhkergly fasawdddyq pllsmhdege qplfgalvsa sigkgrhtht slvlhhqldk
      781 lvpgafrlia nlvqpvr
//
LOCUS       WP_010661162            1051 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Brucella anthropi].
ACCESSION   WP_010661162
VERSION     WP_010661162.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..1051
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=111793
     Region          1..1034
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 misevfirrt rlaivisiii siagaiaifs lpiqqypqit pptvnvsavy pgasaeviad
       61 vvggpletai ngvdgmmyms stssnagqys lsvtfevgtd pelaqinvqn raqlaisrlp
      121 aavaqqgvsv rsrspdfvlg iafyspddsl naleitnftt ttivdaisrv pgvgeasvvg
      181 aseysmrvwl npqrmdalgi tvdevsaaiq rqniqatlgq agappmrvgt elqytlvaqg
      241 rlrdtdefgg ivirtgadga kvflrdiarl elgarnyasr asfaghesam lqinqspdan
      301 aiqtatavqa elerlssrfp sglqyhvvyd atrfveaslq ltartlfeaf vivlvvtfif
      361 lqdwratlis alaipasmlg avavllavgy slnmisllal vlaiglvvdd ailvvenvkh
      421 vlddtpdisv ieatrkamhq itgpiisttl vllavvtpta flegiggqly rqfavtissa
      481 lilssfvalt lspalaalll krgqggykrg plawfssfme ktregygkiv gflvkywivp
      541 vagivacfal ayfvfvnlpa tflpdedqga lfvdiqlpsa asldrtnliv envrkvlset
      601 egvqdvitva gfsilqstst pngamavaal tpwedretea lqlnniintl raqfsqvpga
      661 nisvfappai agigavggld frlqalqdqp pqeiaqvtsa llgyfnrrpe iggaattfna
      721 nvpqiyvdvd raraealgls vsdiyasiga nfgsryvndf tlngrvfqvn lqadsdfrah
      781 sedilklhvr srngtmvplr svvslttvla pfvitrynls vsaqvnavpa pgsssgqama
      841 ameqvaseal pdgygyewsg lsfqesrssg qevivfalaf lfaylflvaq yeswalpavv
      901 ilslgaallg avaaltffgl qnslyvqiam vlliglaakn ailivefake kreagltaae
      961 aartgaeqrf ravmmtavsf ilgilplils sgagagarqa vgvtifggml aattiglilt
     1021 pglyfvvqrl serlgrqtde kkdtasetvh e
//
LOCUS       WP_010661174             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Brucella].
ACCESSION   WP_010661174
VERSION     WP_010661174.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..146
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16022
     Region          5..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mgagerlngq clcgevkfta spvkmemdvc hcsmcrrwsg gafmavncgt sveieneaal
       61 atysssewge rrfcskcgss lfwrgvhdgm tvvsmqafae perfhfaeei fidnkpanyd
      121 fandthrmtg eeflaalaak qeaehg
//
LOCUS       WP_010661185             558 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease J [Brucella].
ACCESSION   WP_010661185
VERSION     WP_010661185.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..558
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=60937
     Region          5..557
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 marsnttelv flplggvgei gmnlamygfg padnrewlvv dmgvsfagpe qpgadlilpd
       61 iryleaekhn lrgivithah edhfgalldl wprlkvpvya tpftagllea krqsehgape
      121 ipitiykage kfevgpfkle avavthsipe pvslaittpl gtvvhtgdwk mdpepslgpv
      181 idearfraig dagvlalicd stnalreges pserqvgesl relienargr vaittfssnv
      241 grirsiteaa rdagrqvlvv grsmkraisv atelgymegl peylseedyg yiprenvvmi
      301 ltgsqgepra alaklardem rslaltagdt viyssraipg neksildikn rlidrgikii
      361 gdedalvhvs ghprrselrr myswvrpqil vpvhgeaahl vaqgslgame gieqvaqvrd
      421 gdmlrlapgk aeiideapvg riykdgklig deeeigmver rklayvghva vsvlldrehk
      481 iidepdlvtf gvpeenaqgd lledilldaa ieaidsiprv rrkdielvre svrravraaa
      541 neawgkkpvv tvfvnrir
//
LOCUS       WP_010661272             819 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [Brucella/Ochrobactrum
            group].
ACCESSION   WP_010661272
VERSION     WP_010661272.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..819
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=89539
     Region          2..788
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mvrligyffg igtvlmllva ggvalyvgsl tkdlpdyevl akyeppvmtr vhasdgslms
       61 efarerrlyi piqavpnrvk aafvsaedkt fyehhgldfa glaramitnv knmgsgrrpv
      121 gastitqqva knflltskqt ydrkikeail amrieqaysk drilelylne iffglgsygi
      181 asaaltyfdk svgelsiaes aylaalpkgp nnyhpfrqpe raierrnwvi drmsengyit
      241 aeeateakkq plgvkersda hyvfaseyft eevrrqiiqk ygvdalyegg lsvrttlnpt
      301 lqvearkslq aallrydear gwrgpmknve lgndwgtafg dmqsyadvpe wqlaivlnvs
      361 aagadiglqp pleasgsrsk erkrafiaad dmkwamrvvn iggkrtsaks pegvlkagdi
      421 vyvskegdsr frlqqppkle galvamdpht grvlamvggf syaesefnra tqayrqpgss
      481 fkpfvyaaal dngytpasvv ldgplevnqg gtlgvwapkn ysgkfsgpst lrygieqsrn
      541 vmtvrlaqdm gmklvaeyae rfgiydkmlp vlsmalgage ttvlrmvtay siianggqsi
      601 tpsmidriqd rygktvfkhd arqcegcnaq dwanqdeptl idnrdqvldp mtayqitsmm
      661 egvvqrgtaq ilksldrpma gktgttndek dawfvgftpd lvvgvfmgyd tptplgrgnt
      721 ggglaapvfk sfmeqalvgt pkvdfrvpeg mtviainrkt gmranqgdpn vimeafkpgt
      781 gpsdsysvig mdsfregspv apqspqatra insgsggly
//
LOCUS       WP_010661301             206 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Brucella anthropi].
ACCESSION   WP_010661301
VERSION     WP_010661301.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..206
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23196
     Region          1..202
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mlkiwgrins tnvkkalwta relnldyeqi nvggqfgglk dpaylarnpn gliplledgd
       61 tvlwesntit rylaaaygkg tlwiedpakr aqaekwmdwa sasfytnfsn vmkhlirlpe
      121 aerdpaileq slqglaqsmq ianeglkeap wfsgenfgig diptgcyaya wfefpierps
      181 lphledwygr lkqrpayqaa vmtplt
//
LOCUS       WP_010661320             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease [Brucella/Ochrobactrum group].
ACCESSION   WP_010661320
VERSION     WP_010661320.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..190
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21635
     Region          79..138
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mtvavsprtv stsglpalvl nadyrplsyy plslwswqda ikavflervn ivaeydhivs
       61 spsfsmrvps viclkdyvkp prypaftrfn vflrdrfecq ycgsphdltf dhvtprchgg
      121 ettwenvvaa cspcnlrkgg mmpavahmwp rqkpamptvq dlhnngrlfp pnhlhdswld
      181 flywdvelep
//
LOCUS       WP_010661418             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Brucella].
ACCESSION   WP_010661418
VERSION     WP_010661418.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43063
     Region          10..370
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(17..18,21..22,25,57,107..108,110..112,115,135,
                     138..139,142,209,212..213,216..218,221,245,249,300..301,
                     305,309,325,328..329,332..333,336)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mriyiqvlal lcgtafllia sglhglllpl rggvegfsva slgmlgttwa ggfvagclfa
       61 prlvrrvghv rafgcfaasa aviallsgif vdatiwvilr aftgfsmaga fmvieswlne
      121 ratnesrgki fgmymmvnyg atmsgqmlva agdvrsdhlf misgiffcla liptaistav
      181 spkpltevql dlkalynnsp aafvgcilig iangawgtlg avfgaksgis tteialmvsv
      241 tiaagalmqi pigrisdlvd rrfvlasvaa laalvgliaf lvspssgpvi itmtgcygal
      301 ayalypvava handhatses fvkvssglll lygfgtmlgp llaaaamdif wpsglfaitm
      361 lahisitgya lfrsrkrasv pkeekdqfks mpsergatpe alnldpraet eg
//
LOCUS       WP_010661458             302 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010661458
VERSION     WP_010661458.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..302
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=32408
     Region          1..302
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 meyffqqvin glalgsiygl iaigytmvyg iigminfahg dvfmlgafma livflmittf
       61 igalpialml llmmivamll tglwswtier vayrplrgsf rlaplitaig msialsnfvq
      121 vtqgprnkpv pqllngsyni mgtnvtislk qivvivvtav lltifwyivn rtslgraqra
      181 ceqdrkmaal lginvdrvis ltfvmgamla avagtlylsf ygvisfadgf ipgvkaftaa
      241 vlggigslpg avvgglligl iealwsayfs idykdvaafs ilaivlifmp sgilgrpeve
      301 kv
//
LOCUS       WP_010661473             364 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [Brucella].
ACCESSION   WP_010661473
VERSION     WP_010661473.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 364)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..364
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39700
     Region          2..364
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mrlvsfsakg yrslrsvrfd lgqvtvfvge ngagksnlyr alqlvkaaae gnlstevvre
       61 ggmqsamwsg nrrkhesari ileadfeder lasrlsyrve aglpppvsga fpfepqikee
      121 qlnldtgrrp vdlmdrrgpa vfardgegrr mehparllts esglavlgqs ghypeigdls
      181 aqirgwrfyh gfrsdrdapv rqpsiaataa mldedggnla svfatlahir qdtvdldrlv
      241 adaledaklv ipypeetatf glnfpafppr tfrpgelsdg qirllalaga llsyrlppli
      301 alnepeaslh pdmipslarm iaqasersqi wvvthsaala saiaehcgar pirvskqdge
      361 tvle
//
LOCUS       WP_010661482             469 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RsmB/NOP family class I SAM-dependent RNA
            methyltransferase [Brucella].
ACCESSION   WP_010661482
VERSION     WP_010661482.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..469
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=50671
     Region          21..469
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mndkkpapkr gnkkpqtnns aadlrpglaa rlcaarllga viekntsldg ltdnthghpq
       61 ylaleprdra lvrailgsal rnrgsierai nkrldrplpe navalkhllh vaiaqifyln
      121 lpdhsavdla veaanndprn rkyaglvnal lrrlsrnker alahtlqpet nvpewfaksi
      181 tdaygaekaa ailamhayep pidftvkgda kawaeklggv alpngsvrlq tvegnltdlp
      241 gfaegdwwvq dvaaslparl mgdikgkrva dlcaapggkt aqlvlqgadv taldlsenrl
      301 krlrgnlerl gfeaktvatn lmdfqpdelf davlldapcs stgtvrrhpd vpwtktpqdi
      361 aklaelqgkl lahaatlvkp ggvivfsncs lhplegeema rkaaenplle pfpiteqdcp
      421 slnglldglv taegflrstp adlppdrfeg nphmagmdgf faarfkrra
//
LOCUS       WP_010661527             494 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MATE family efflux transporter [Brucella].
ACCESSION   WP_010661527
VERSION     WP_010661527.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..494
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52305
     Region          12..448
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mkqsidltta pinqalllfa lptlgssilq sangsidtiw igqllgenal aattngnlvm
       61 flltafvfgf gmastiligq afgrrdveta raiagttvgt fvplsivvai igwllapkvl
      121 dllgtpeaie plaraflqvt flampailmq ttlmmalrgs gdamtplifm gmavlldial
      181 nplfilgwgp lpalgiagsa lataaanyis laamlyyiyy rdlplrlrge elwllvpdre
      241 llrliftkgl pmgvqmivvs ssmltmmrlv nqegvdttaa fgatqqlwty vqmpamalga
      301 avsamaaqni gagkwdrvss itrigaiyav lmtgalvvll lladrqamqi flgadspait
      361 igqhigqiat wgfiafgvsm vlfgtvrang qviwpliilf vsmypvrlgv aiglreqfgs
      421 dalwlsfpaa mvstllmatv lyfhggwkkn ssmhidahel qgeaacvsqs teaapssnal
      481 apnaplvaev kagt
//
LOCUS       WP_010661650             333 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Brucella anthropi].
ACCESSION   WP_010661650
VERSION     WP_010661650.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..333
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36165
     Region          23..330
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msdqadivrv vpvyvvippr vllldvagpl evlrkanleq hklrfdvcyi gpastvlssi
       61 glpvaggepl pealpddalv ivsgaadipl gnaeihrsad aaleneivlw lrravrpgvr
      121 lvticsgall aaraglldgy sctthhltlg elerlapaar vhenrlfved gerltsagit
      181 agidlmlhiv agltdhatal avarylvvyl rrsgndpqls pwldgrnhmn pvvhraqdai
      241 ahdpaaewsv erladiggas prnfsrlfne yagmtvtdyv nrlkislare mllnseldie
      301 nvaaqagfas arqfrrvwqr iyneppsrvr fgv
//
LOCUS       WP_010661655             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SOS response-associated peptidase [Brucella].
ACCESSION   WP_010661655
VERSION     WP_010661655.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..259
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=28852
     Region          1..229
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgrfsltas reeleafaaa liaedfppry niaptqpilt ilggetpppg snrpdrvgll
       61 vrwgfvpswv kdpndwplmf nirsetaaek nsfraalnhr ralipasgfy ewrregknka
      121 qaywvrprkg givafgglie twssadgsqi dtggilttsa ngllrpiher mpvvvqpedf
      181 arwldckrfl prevadimrp aqddffeaip vsdkvnkvan ttpdlqerve eqvpsehakp
      241 krknkpesdd gnggqlsmf
//
LOCUS       WP_010661728             227 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Brucella].
ACCESSION   WP_010661728
VERSION     WP_010661728.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..227
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25743
     Region          18..227
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mdeiqktgqa dngsqafrrt alhdmlvnhl rdmiiegqle pgtrlhegql geqlgvsrtp
       61 lreaikylas eglvelvpsr gavvkrfsaa dvrdmltvlr tleelagkla celatdkeia
      121 evrslhdemi erykhadrlq yyklnqqihl aivrlaqnpt ladihqmlqt rlkrirfvgh
      181 egaekwaaav sehremieal eardatrlse vlgrhltkaw ervrdsm
//
LOCUS       WP_010661676             155 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Brucella anthropi].
ACCESSION   WP_010661676
VERSION     WP_010661676.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..155
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=17272
     Region          7..146
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mtcplfvgir sedfdtaael rklehgrtdi gaivtftglc rdesgtlsal elehypgmae
       61 aeitriarqa ierwpitalt iihryglikp genivlvaaa sshrhaafea asflmdymkt
      121 dapfwkrehl adgsvggwvs skeedekire rwkqs
//
LOCUS       WP_010661743             435 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Brucella].
ACCESSION   WP_010661743
VERSION     WP_010661743.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47380
     Region          21..427
                     /region_name="MFS_KgtP"
                     /note="Alpha-ketoglutarate permease of the Major
                     Facilitator Superfamily of transporters; cd17367"
                     /db_xref="CDD:340925"
     Site            order(31..32,35..36,39,77,135..136,138..140,143,163,
                     166..167,170,252,255..256,259..261,264,292,296,349..350,
                     354,358,374,377..378,381..382,385)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340925"
ORIGIN      
        1 mvsitserse vqstnsrlks iiggstgnlv ewfdwyvyaa falyfaphff psesqtaqlm
       61 saaavfavgf vmrpigawim giyadrkgrk aglalsvtlm cagsliialt pdyqtiglaa
      121 pallvlarlm qglsvggeyg asatylsema gkdrrgffss fqyvtlisgq llailllivl
      181 qstmetpale awgwripffi gallavvvfw lrrglaetes fknaktkdtp ksgfwtlikh
      241 hpketalvml ltaggtlafy aysiymqkfl vntsgfsrev asqinavtlf vfmclqpiag
      301 alsdrigrkp lmiafgaagv lftypifttl eqtrdpitag llvmgaliiv tgytsinavv
      361 kaelfpahir algvalpyal antlfggtae yvalsfkngg wergfywyvt imigislivy
      421 lrmrdtskds miked
//
LOCUS       WP_010661807             111 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Brucella anthropi].
ACCESSION   WP_010661807
VERSION     WP_010661807.1
KEYWORDS    RefSeq.
SOURCE      Brucella anthropi (Ochrobactrum anthropi)
  ORGANISM  Brucella anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Brucella anthropi"
                     /db_xref="taxon:529"
     Protein         1..111
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12053
     Region          7..108
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 mekrivegve vhrssgnvfa dlglpdaekl kiktglviei rkamrargln qqeaakrmgi
       61 pqpkvsgmmr gdftnlserk lmdclnrlgy dieitvkpaa alvghltlav a
//
LOCUS       WP_010661933             427 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Marinilabilia salmonicolor].
ACCESSION   WP_010661933
VERSION     WP_010661933.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..427
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47057
     Region          1..427
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtfkdlelie pilrslkekg ytqptpiqeq sipillggkd llgcaqtgtg ktaafsipil
       61 qniylnssad nqsrrrrkpr lkalivtptr elaiqigesl tdygkytgir nivifggvkq
      121 gaqtqslqrg tdilvatpgr lldlisqgfi slreieyfvl deadrmldmg fihdvrkiin
      181 llpakrqslf fsatmapeiv klsgkilggn pgkvtitpkq ntaekvdqsi yyvdkksksr
      241 llvhlmeenp edstlvfsrt khgadkivki lkkaginala ihgnksqgar qkalgdfksg
      301 easvlvatdi aargidvsgl grvinydlpn ipetyvhrig rtgranaegt alsfcdveek
      361 pylkdiqkli nqripvvdgh pflpqvetgt eekvvekpsg irkkssfksq ssvnryrkqk
      421 rnrnsgn
//
LOCUS       WP_010661972             286 aa            linear   BCT 01-JAN-2025
DEFINITION  glycine betaine ABC transporter substrate-binding protein
            [Marinilabilia salmonicolor].
ACCESSION   WP_010661972
VERSION     WP_010661972.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..286
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32522
     Region          30..281
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(38,40,85,113,143,147..148,193)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mikknfrnti ilffviallg atgckkkkee vviyyanwie gvamtkitel aledvgipvk
       61 tmllspgpvf talargdgdf fleawlpqth rdywerfgdk idrvgmnfdy astglvvpgy
      121 veidsitqln ehkekfngki igvgsgagvy rdtekaikdy glefdqltss gpamvasikn
      181 aaakkewivv tgwkphykwa kydlkyledp kgiypseksy ivtrkgftde rpgfkeflgn
      241 fyfteetmsg lmlllqkedd vdaagriwyk dnkeliqswm peewlk
//
LOCUS       WP_010661973             231 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Marinilabilia salmonicolor].
ACCESSION   WP_010661973
VERSION     WP_010661973.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..231
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25981
     Region          2..229
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mitlenvvkk yngnvvlaid nltfqqgdiv gvvgnngagk ttmfsaildl iqlseghien
       61 nqqrvnesee wkkftssyld ekflidyltp deyfnlvgsl kgyapgdiqe fiagfseffn
      121 geidnkrkyi rslskgnqqk igivaslign pqivlldepf snldptsqyr lrqiikdfqq
      181 qnnctfliss hdlnhvaeac trivilekgk vvddvktsde tmlrlenyfa i
//
LOCUS       WP_010662017             235 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662017
VERSION     WP_010662017.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..235
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25997
     Region          21..230
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mkrsqeqvnv eeidlksfgi fngltdaeie slsqslvcts hkrgsiiyde gsringsyiv
       61 aggvlkiykt gfdgkeqiir fakggdligf rsivsdelac ttarviqdav lcyvpgdtit
      121 sfikgnpefa malmrltcre lgesnkfltd iaqktvrerl aevllllmdt fdldeehtlk
      181 isltreelan mvgtatesvi rllsefkadn lielngrkik llnipkliki gnvyv
//
LOCUS       WP_010662071             134 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Marinilabilia salmonicolor].
ACCESSION   WP_010662071
VERSION     WP_010662071.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..134
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=15135
     Region          8..125
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mtekrtaili ceddrlmaei aeqvlsddtc elkivengar aidelkkkay dlvitdaimp
       61 ernglevtsf irrhqrldtp vlmlsgisdl ryvreakekg vndflskpfs aerlrrkvsq
      121 llkknlfvss glvv
//
LOCUS       WP_010662018             138 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662018
VERSION     WP_010662018.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..138
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=15466
     Region          9..135
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mktsldlnwt gnmsfetemn ghkvvldadp svggenkgir pkplmllala gctgmdvvsi
       61 lkkmrvqled fnvtvesnmt eehpkhydkm hviytfkgkd lpkdkiekav slseekycgv
      121 sevykkamel tteiried
//
LOCUS       WP_010662147             157 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Marinilabilia salmonicolor].
ACCESSION   WP_010662147
VERSION     WP_010662147.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..157
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=17768
     Region          1..148
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mnsyltfkvv devfavhvsh vmeireyekp kpvpqkmefi agliefrdev iplintglkf
       61 nlgaveasqn svivilnlhk eeeeddyrva vmadavsdvl emeegelksi hqeykpgyva
      121 gtyskddafv fvldpdkvft rneviemdki ltaakeq
//
LOCUS       WP_010662002             277 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662002
VERSION     WP_010662002.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..277
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=31176
     Region          10..271
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 msigtspfgg ltpvvknlii invlfyvasl vlfstfgiqi erylglhlpt aeafnpaqfv
       61 tymflhayys pttgiifahl ffnmfalfmf grmletvwgp krfllyymvt gvgaalihil
      121 tqyievapml daiahdmnna spqalksfln kalpaainne ftrlinenpe nlqaivneym
      181 vkyrdlylns fvtvgasgsv fgillafgml fpntqlmllf ppipikakyf viiygaielf
      241 mgvqnfsmdn vahwahlggm lfgfilikyw knkgfyy
//
LOCUS       WP_010662163             343 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662163
VERSION     WP_010662163.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..343
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38306
     Region          1..343
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mkkrilvfrf salgdvamtv pvlwsfldky pdheiwfvsr pfakdlvapl prvhffpvdl
       61 kqnhkglpgl yglfrelkkm gpweavvdlh svlrthvlts lfaitgtkva kidkgrsekk
      121 kltrkdnkvf kalpttadry rqtfgkaglp felqnfpgkt lygkdsldsk cppwgnlggs
      181 pllvgiapfa khqwkmwpee kmlellklld ergvsvilfg gpgeeqkkle gwvanlgmaq
      241 tfagkltmse elelmsqlni mvsmdsanmh laslsgirvv siwgathpya gfmgygqsqa
      301 davqvnldcr pcsvfgnipc hrgdfacmer itadmvleri lei
//
LOCUS       WP_010662170             458 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662170
VERSION     WP_010662170.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..458
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51323
     Region          129..458
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkfghlklrg llcaicllwg ttillaqped tlsftieqai eyasvhayqk isseydvasa
       61 kkkiwetias glpqvdfsaq ynhsidvpvs llpaeivped mrppgigagd kipvsfgtay
      121 dgsyslsvsq mifngsyfvg lqatqvfldl trhqaaktei eirdavakac flvlsadenl
      181 kafeenlnvn ktllretqal yengfrksmd vsqlklmvre sekqileikr nkdvalavlr
      241 fsmgldeeqp vkltedftsl srkatngevk ksgwspeehi dyklastnve seklqlnnir
      301 vqylpkinaf ytyqktgygd dwnifgdewy ksqfvglsvs vpvfssgmrn aqalqqklaw
      361 kksknirtqt mqqiktqglt altdynsaid qyeiasesrm laldiyektk trfsngmtgs
      421 feltqqqgqy iqaqinhvra alavlnsrna ylkatgkl
//
LOCUS       WP_010662181             234 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662181
VERSION     WP_010662181.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..234
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=26322
     Region          5..233
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mpdlfrkylf giaalvfpei crgcgewpga grtglcrrce semprtwfek vpgnpveqmf
       61 wgrakiefat slffyrkgem lqqiihqlky krdknagvyl grlagrvllk ealaekidci
      121 vpvplhpkkq rirgynqsqi iargigeitk hpvnsesvir tvhsasqtrr gryerwqnve
      181 gifkvlhphl fqnkhvlild dvittgatie alcaafshvs gvrisvltig iaag
//
LOCUS       WP_010662199             370 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662199
VERSION     WP_010662199.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..370
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42319
     Region          18..360
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 makyiyeydn wpaftwndkk ivgtlgkvrh lqgkifgqms algfslkeet ilstltldvl
       61 ksseiegefl nkeqvrssia kklgfdnagi vhvdkhvegv vemmldatqr ydktldhkrv
      121 fgwhaslfpt gwsgihridt gsyrdgemqv gsgpmgkeki hfqappanvv ekemnaflnw
      181 fntesdidgv lkaaiahfwf iiihpfddgn griaraisdm llarseessq rfyslsnqil
      241 teknnyyeil qkvqhstgdi tdwiewflnc lyralenteg tlkrvlkksd fwdrhkatnl
      301 nsrqrlmlnk lfdgfdgklk sskwakiakc sadtalrdik dliekgilkq eksggrstny
      361 elteewniys
//
LOCUS       WP_010661962             451 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramate--L-alanine ligase [Marinilabilia
            salmonicolor].
ACCESSION   WP_010661962
VERSION     WP_010661962.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Sangshetti,J.N., Joshi,S.S., Patil,R.H., Moloney,M.G. and
            Shinde,D.B.
  TITLE     Mur Ligase Inhibitors as Anti-bacterials: A Comprehensive Review
  JOURNAL   Curr Pharm Des 23 (21), 3164-3196 (2017)
   PUBMED   28201974
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..451
                     /product="UDP-N-acetylmuramate--L-alanine ligase"
                     /EC_number="6.3.2.8"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008763 - UDP-N-acetylmuramate-L-alanine
                     ligase activity [Evidence IEA]"
                     /GO_process="GO:0007049 - cell cycle [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=49900
     Region          1..440
                     /region_name="MurC"
                     /note="UDP-N-acetylmuramate-alanine ligase MurC and
                     related ligases, MurC/Mpl family [Cell
                     wall/membrane/envelope biogenesis]; COG0773"
                     /db_xref="CDD:440536"
ORIGIN      
        1 mrvhfiaigg samhnlaial hkkgfhvtgs ddkifepsks rlqnhgllpa sdgwspdnis
       61 edldavilgm harsdnpell kaqelnlkvy sypeylyeqt knkrrvviag shgkttitsm
      121 llhvlkqtgr kfdfmvgani kgfdtmvels desgiavfeg deylsspidr rpkflwykpq
      181 ialvtgvawd hinvfpaeev ynhqfelfaq sidpggsfiy yqqdpvlqti akehpelnvl
      241 pyneveasse ggetlvacdg ekfalkifgh hnfqnlagal lvakelgvse kdflksmrcf
      301 egaarrlqil sekedasvfy dfahapskvk atvaavkdqf pqrnllavve lhtfsslnre
      361 flpqykgama aadeavvffn pevvahkkle eitttdveqa faqkglkvft dgdklhqfla
      421 gqrlknsnll lmtsgnfagi dvnalagevl g
//
LOCUS       WP_010662229             686 aa            linear   BCT 01-JAN-2025
DEFINITION  fibronectin type III domain-containing protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662229
VERSION     WP_010662229.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Bloom,L. and Calabro,V.
  TITLE     FN3: a new protein scaffold reaches the clinic
  JOURNAL   Drug Discov Today 14 (19-20), 949-955 (2009)
   PUBMED   19576999
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Koide,A., Bailey,C.W., Huang,X. and Koide,S.
  TITLE     The fibronectin type III domain as a scaffold for novel binding
            proteins
  JOURNAL   J Mol Biol 284 (4), 1141-1151 (1998)
   PUBMED   9837732
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Potts,J.R. and Campbell,I.D.
  TITLE     Structure and function of fibronectin modules
  JOURNAL   Matrix Biol 15 (5), 313-20 (1996)
   PUBMED   8981327
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465549
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..686
                     /product="fibronectin type III domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=77449
     Region          <144..>276
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          242..>680
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          <512..>673
                     /region_name="COG4733"
                     /note="Phage-related protein, tail protein J [Mobilome:
                     prophages, transposons]"
                     /db_xref="CDD:443767"
ORIGIN      
        1 mrciiltilf gfipflavaq enqsfglfsk feegkvylki qplegsawyl gksngyvier
       61 rdvgsesafq kitespllpl pagemealsg dfpfvgelka ilydmetgaq vdetnfaave
      121 akeeelegrl flhfylsams eaaseasglq fvdhsaeagr syeyrvriag edqysnqkvv
      181 ntfrettyti pelnltgldk avrinwyhks fkkkyiayrl ersengqdwd ylgsspivyn
      241 rrvsedsedl esgyiyegds lsanyqpyyy rltamdffgy sagpgqrydv mgrdleppvq
      301 psdveagysp regmyitwdy pdgarvddld gffigtgasp egpfeplnkk vlppdtrsfv
      361 hsepnqggrn fyivtaidts gnykhslpvy eiipdslppa sprelagvid ssgvvelhwt
      421 kgeeadlmgy rvfrantrdh eyvqltqepl qdtlytdsis lktltkhvfy kivavdnnfn
      481 hsgfsaplkl yrpdimppva pkikqahwgd gtvrvtwvpg tsrdaqadil lrqtnglwde
      541 vgvfedgeva ftdsfpssqe yvqyamlsrd esgllsdtsq vrtvrmvqfy evepvddlna
      601 ifnmenrqve lswnyggnee vyyiifrgde eksirmydts sgekqsfsdk llqagqkysy
      661 avrvkrrdgk tsplsenvev vvpqgn
//
LOCUS       WP_010662236             126 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662236
VERSION     WP_010662236.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..126
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14439
     Region          21..124
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mckeilllfl mvnpmvfsqn hlsaedffdi mdsteqvvil dvriyesfse aripgalyag
       61 ekelllsivc dypkempllv yctygdrskt vlkilkkegf snvyhlkkgf kdwkekgfpv
      121 ddseid
//
LOCUS       WP_010662238             137 aa            linear   BCT 01-JAN-2025
DEFINITION  VanZ family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662238
VERSION     WP_010662238.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..137
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=16204
     Region          1..125
                     /region_name="VanZ"
                     /note="VanZ-like family protein (function unknown)
                     [Function unknown]; COG5652"
                     /db_xref="CDD:444373"
ORIGIN      
        1 mnktiqqlin ykftlitvgi ifflslstse sinkiwfldf phsdkiahmg mygfltlvyl
       61 mertaflrry qatrktrwyy vwwivligai leliqpfmag rekdfldfia ntsgiimayi
      121 afflikkyyn fnktfss
//
LOCUS       WP_010662267             267 aa            linear   BCT 01-JAN-2025
DEFINITION  undecaprenyl-diphosphate phosphatase [Marinilabilia salmonicolor].
ACCESSION   WP_010662267
VERSION     WP_010662267.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..267
                     /product="undecaprenyl-diphosphate phosphatase"
                     /EC_number="3.6.1.27"
                     /GO_function="GO:0050380 - undecaprenyl-diphosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28879
     Region          1..265
                     /region_name="UppP"
                     /note="Undecaprenyl pyrophosphate phosphatase [Lipid
                     transport and metabolism]; COG1968"
                     /db_xref="CDD:441571"
ORIGIN      
        1 mdwiealilg ivqglteflp vsssghleig kqllgietpd slrftvvvhg atvlstlvvf
       61 rkdivelfsg lfkfqwneet kyiakiafsm ipigivglff kdtveeifnt gsmlllvglm
      121 llitasflaf syykksgdrd itfrdaliig iaqtfavlpg isrsgatiat gliignkrte
      181 varfsflmvl vpiigentld llksdvpqav tgneigalvm lagfvaafvs gllacqwmie
      241 ivkrgkliyf alycavvgal aiggfvw
//
LOCUS       WP_010662299             414 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Marinilabilia salmonicolor].
ACCESSION   WP_010662299
VERSION     WP_010662299.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..414
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45983
     Region          28..246
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          149..414
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mtthissggf ksivkiawrn lwrnrkrtli tvssiffgvi fsalmgsmqe gsyqkmienv
       61 arfyaghaqi qqkdypdnqs innsfiasds lvkrlnnteg inmvvprles falassgnqt
      121 egilvlgvnp dqedqmtgls dkivegtyfd gpsrllagke laenlgispg dtlvmisqgl
      181 hgvsafgkyp vaglfshpnp elnrqliylp ldearyffqa snrvtslalv gksqksidka
      241 ipeikknleq dqilrtwqem fpailqqies dratalimkl ilyliigfgi lgtvvmlmae
      301 rqhelsvmva vgmyrsklal mllleilwmg vmgvvagfig slpvigwfan hpvpisgqag
      361 ewmknigfep ymffawdvgv fleqmlvvfi ltllisfypf vrafkispiv glrn
//
LOCUS       WP_010662301             194 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662301
VERSION     WP_010662301.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22123
     Region          4..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgkrnnkttr rteileksla lfatkgyhtt ttaeiakaag iakgtlfnyf eskehllrsl
       61 vfetlmelad midpnhdgiv tqdeffgvih ksrkwivdnp qflslyfsmv sqpavfdlfk
      121 aeimqqmspy meklatffqk egipdgyaev rfflamldgi gihyaidpkn fpidqiegki
      181 inyyqgrmnr nvss
//
LOCUS       WP_010662332             152 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662332
VERSION     WP_010662332.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790656
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..152
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17687
     Region          4..151
                     /region_name="SRPBCC"
                     /note="Ligand-binding SRPBCC domain [General function
                     prediction only]; COG4276"
                     /db_xref="CDD:443417"
ORIGIN      
        1 mgtyrlhvrq kikaskdkvw dfissprnlk iitpehmgfd iitpglpekm yagmmieyqv
       61 qalpgyktrw lteitqvqpg dffideqrsg pyklwhhqhh lapdengtim tdivhyippf
      121 gllgdlanql iikrqlnaif eyrrialerk fp
//
LOCUS       WP_010662423             444 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662423
VERSION     WP_010662423.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..444
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50000
     Region          28..438
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrniaailml pmllafteah aqqpekwslk dcieyakdnn lsikqqslnt eyqqnvyeqk
       61 kldripsvng svgyqlsfgr vlddtsfeit dqttqfgrfs lgasvplfqg fslhnqinrd
      121 kanwqasrke leaakndlal nitslylqvl fdkellqvae eqykvakeqv entkklvdag
      181 rvaegnllei ksqaarealt vtqmannltm sllnlaqald leetgnfdvv ipeipelqqn
      241 tltppsdlfv qavdlmpeie asefnleser yalkaaqgql ypsinmdagw ntsvtkkest
      301 vefdfgkhfn dnatqyvglt lripvfngla arnnvkntql sirsaqhdle kekqtlrkei
      361 qqayadaqaa ylkynsaqta vdsyeeslry tekkyavglv spvdysvart dylkaqsdfl
      421 qskyeyvlrt kvldfytgap lsld
//
LOCUS       WP_010662366             247 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662366
VERSION     WP_010662366.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..247
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26989
     Region          3..245
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgkiiafinq kggvgktttt asvasgmaqs glktlaidld aqcnlttsfg itdfkvntyn
       61 tlkgqieldp ikldehltil pasvdlsafe lemsaepgke yllkellepi ldqydyilld
      121 cspnlglvsi naltaadlyi ipllphhlsi qgltklleit dkvkkrlnpn lemggivltq
      181 ynkrkvlhrd iaqvvkehfg qkllntvire nislaeapss gtdifqyapk sngaedylil
      241 tkeiinl
//
LOCUS       WP_010662426             416 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Marinilabilia salmonicolor].
ACCESSION   WP_010662426
VERSION     WP_010662426.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 416)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..416
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46201
     Region          3..416
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mfnslqeifs tlkqnklrai mtgfsvawgi fmlilllgsg nglqngmenn frgtaknalw
       61 iwsrqtqvsy dglqagrriq ftdedydmlv nhfkddisdi sgrfrlwgsg tvtykneygd
      121 yslegvmpef kniqivdleh gryinkldiq qfrkvaiisv pvkkalfkee dpigkyihid
      181 kvpfkvvgtf inperrddeq iyipvktaqr vfngsnklne lavatnaltv aenkrveeai
      241 rttlmkkhri apddkqalgi wntlehfkqa qgvftgirif vwvigimtii agivgvsnim
      301 iilvkertke lgirkaigat pwsvirlvls esvfittlsg ffglvagmgl maaismvlqs
      361 aaqsnpsies tfynpsanls vavsalvvli vagliagyvp arrasaikpi ealhde
//
LOCUS       WP_010662446             298 aa            linear   BCT 01-JAN-2025
DEFINITION  glycine betaine ABC transporter substrate-binding protein
            [Marinilabilia salmonicolor].
ACCESSION   WP_010662446
VERSION     WP_010662446.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..298
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34281
     Region          40..288
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(47,49,95,123,149,153..154,199)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mkrtisnmis lmlsgivisg imvscnytkp sqeeedkrvv klnytdwtes vaitmmaatv
       61 leekmgyeve lkltdvesay qevagqqadf fpdawlphtq rqyfekhkne idtigivfqs
      121 pktglvvpdy skyvsitdlt gdtipivgid agagimtstd raikhyklnn rlltgsddqm
      181 tfqmtdsikr rreivvtgwe phwifsrhdv rfledpdnif ptdehiyvvg nkksieehph
      241 aaeffrrmkl tdkqfnslid qvkmatdpvn gihqwmeknk fivnkwvkdl qperlkvm
//
LOCUS       WP_010662463             202 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662463
VERSION     WP_010662463.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23237
     Region          8..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mknkvldldr imnlyfrygv knltmddvaq elgiskrtly qqvttknelv dmvlndqfsk
       61 yreavssivd kedgsirkly cvykliadff kpltpvfvys lnkmssklae elhrkyndfi
      121 veifgrivde geeegiflvr fkddfarlva gylfqtnekg avlqmaeidl nnafylqtsg
      181 vctdhgrkvl nqlmdnpkll ta
//
LOCUS       WP_010662465             192 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Marinilabilia salmonicolor].
ACCESSION   WP_010662465
VERSION     WP_010662465.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..192
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=22124
     Region          3..192
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mkniliingh pdkisfchsl aisykagces qnanctlvnl adlhfdpilh ygyrqrtele
       61 pdlvqmqeai lkadhlvfvy ptwwgtypal lkgffdrvfl pgfafkyren slfwdkyfkg
      121 ktarlivtmd tpkwyysliy kspghnslrk gilefcgikp vrilafgpvk nsddkkrekw
      181 lsqvtklgae lk
//
LOCUS       WP_010662467             397 aa            linear   BCT 01-JAN-2025
DEFINITION  saccharopine dehydrogenase family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662467
VERSION     WP_010662467.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..397
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44583
     Region          28..391
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mgkvliigag gvgtvvahkm asipevfsei ilasrtkskc daiaekiggn riqtaqvdad
       61 nvpelvelin sykpdlvvnv alpyqdltim dacletgvsy ldtanyepke eakfeykwqw
      121 ayqekfkeag ltailgcgfd pgvtsiftay aakhhfdelh fldivdcnag dhgkpfatnf
      181 npeinirevt qkgkywengq wkltepheih kplnypeigp kesyliyhee leslvknfpt
      241 lkrarfwmtf gqeylthlrv iqnigmagie pvkfngvdiv pieflkavlp npgdlgenyk
      301 gqtsigcrik glkdgkekty yiynncdhee ayketgtqav syttgvpati gammflkglw
      361 kepgvfnvee fnpdpfleel nkrglpwheq hnvdlel
//
LOCUS       WP_010662517             257 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662517
VERSION     WP_010662517.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..257
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29049
     Region          50..144
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 msnentsihd feikliceyy sllerqgpgs pevtkkalsf vdkltehski adlgcgtggq
       61 tmvlaqnapg tvtgldlfpk fidlfnqnaq klnlqdrvtg mvgsmdklpf qqesldliws
      121 egaiynigfe tglktwkpfl kkggyvavse aswftnerpe eidafwqday pgidtipgnm
      181 qkmqdsgyip iasfilpedc widhfykpqv raekiflnkn agnktaidfi anqkhetely
      241 ykykkfygya fyigkki
//
LOCUS       WP_010662549             573 aa            linear   BCT 01-JAN-2025
DEFINITION  terminase large subunit [Marinilabilia salmonicolor].
ACCESSION   WP_010662549
VERSION     WP_010662549.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..573
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64954
     Region          20..560
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mkplrlikal pefqdevirr afqyekdvqs gkqiagkdik kavkrsiklr kkysysekef
       61 rrvaslfyym yipvddrptq flpapwqcwi llnlftiinp angkrvhtea lvfvsrksgk
      121 tmfgaalsli fltkyggmqa ecfgaatvqk qakqlmdyak vivrnspslk srieayrdel
      181 hyddggsmht lmqlseqqae radgsnpsfc lydeahafkn dalkevvvtg mgarpnplfl
      241 tvttagfftv gyplftqvel akkvlsgeie ddstfyaiys ldseeeaknd dikilekanp
      301 glgtavspdr lkamrdkall lpsswknflv kncnifqttt edpfisdehf tkccqevple
      361 qlkgarawig ldlsqsvdlt aftvlvehpd tkmlhtipyh ffpgkqenkv vrangvdlte
      421 wieqgyiieh eeridledvy qklleaislf dvqmigydpy hawdllaklq anldlahlei
      481 vpvsqsittm stptkyleel visqdinlgl npvlrycnsn arikhsptsn lirvtkdeql
      541 npidsiisti valavymqte fdtlthlmnk net
//
LOCUS       WP_010662564             247 aa            linear   BCT 01-JAN-2025
DEFINITION  KilA-N domain-containing protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662564
VERSION     WP_010662564.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Iyer,L.M., Koonin,E.V. and Aravind,L.
  TITLE     Extensive domain shuffling in transcription regulators of DNA
            viruses and implications for the origin of fungal APSES
            transcription factors
  JOURNAL   Genome Biol 3 (3), RESEARCH0012 (2002)
   PUBMED   11897024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..247
                     /product="KilA-N domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28286
     Region          120..214
                     /region_name="KilA-N"
                     /note="KilA-N domain; pfam04383"
                     /db_xref="CDD:367917"
ORIGIN      
        1 msyfskanfk rhtlfyyqsi ifeiiesgek fpvdldevwg llyshkhkav kalkddvmft
       61 eghdyqtinq kvereigstt vikymlttsc leyfiakkvr pvfdvyrnei tfqlgngdtm
      121 inltevarsf pnknltniln skelieylqv lenksdsklq icsfsesqyi tvkkgapntg
      181 ggtwvhqrva lrvaqklspd fsvwvdekle ellttgksti tpilklrvkk igvcpknyrs
      241 aphkkte
//
LOCUS       WP_010662576             413 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Marinilabilia salmonicolor].
ACCESSION   WP_010662576
VERSION     WP_010662576.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..413
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=47001
     Region          128..413
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mryhlaflwv lvllvgiidw flwrivmtek trsgwrrwlg isglivlpvl fisgffyfgt
       61 qipdasshev ynafstfliv fllvylpkvf flliygigri pdaiprkpar qperhyprit
      121 rakflsqvgi iiatapfvsl lfgvlkgrya fytrhvklif pnlptsfdgf rivqisdlhl
      181 gsfgsnrepm keavelinae kpdlvlftgd lvnnfagetr gweeilgkis asmgkysilg
      241 nhdygdystw pseqrkaanf ksivasnrrl gfqllrnesv tlkkngesva lsgvenwghp
      301 pfpqygdlen awnqtngesf kilmshdpdh wdaevvgrkk ydltlaghth gmqfgfeigk
      361 ynwspakykf krwaglyqvg rqflyvnrgl gylgmparvg mppeitvftl kkg
//
LOCUS       WP_010662599            1055 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662599
VERSION     WP_010662599.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..1055
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=118393
     Region          3..1026
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mrrlietfvr ypfyanlfiv vilvsgifgf lqlkksffpe retrniyvtv typgaspkem
       61 eegitvrieq airglvgike instsrenft rvniettgey didevlqevk navdgissmp
      121 vdaerpivfk rrsttpairl glygeadmlr lktlaqried dflasglmsq iniggypale
      181 iaveikeevl lryglthtdi snaisrnnrd vsggqlrsdd qyliirsrsr tvdpdeiady
      241 vvtadpngrl irirdlgkvf lqfsetpsga wlngnralyl svdklitedl eaisdfvhny
      301 aeefnrthdd aeliatfdfl dllnsrlhll yknggfglll viiilaifls frlsmwvawg
      361 ipssflgmfl vagmygvtin mislfgmilv vgilvddgiv vaenifshfe kgksprkaav
      421 dgtlevlpav itsvsttiia fvplmliegn memmgemafv vvaslafsli eaalvlpahi
      481 gsphilqrkk eavnfgnrfr drleryilwm rnrlygrsla filrhrhial avpltlllvt
      541 iglfgggfis stffpnippd sfnvnvaftp gegekqtyey lmdfekavwe vndklmeeyn
      601 dtanfvnyty lvmgssfdgd esgshaghia vnlrnlegse isafdiatrv reyigavpaa
      661 dkfsvagrnr wgepvsislm gdnleeldqa rdflleelqd ipeltdvvdn eapgaqevri
      721 klkpkayylg ldmftimnqv rnaffgaqaq rlqqgkdeir vwvryppger eeigqledmk
      781 iktpqgeypl telvtynler gpvaiqrfng kremrvdadl vdpyepvppi lervsneimp
      841 qiqakypgvs yfyqgqqkya aesqneiaky flpafgiimv limfhfrsfg qgaivlvmip
      901 lgwlgaawgh aihgiplsml svwgmvalsg vivndavvfl qkynqlleeg lsvknaafea
      961 glarfrpivl ttltttlgly piiletsrqa qflipmamal aygilfgtaf iliffpvvim
     1021 alndvrvlmk wlftgrrpsp eevekvnvlk nrkld
//
LOCUS       WP_010662624             325 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662624
VERSION     WP_010662624.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..325
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36056
     Region          2..323
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkkkinwgii gcgnvteyks gpafnkvegs klvavmrrda elardyahrh rvpkwysdad
       61 dlindkdvna iyvatppssh amyaikamka gkpvyvekpm aatfeqcqem navsketgvp
      121 lfvayyrrtl pgfrkvktll edgtigrpll vnimlvrpat aaesdkdspi wrvqpdvagg
      181 gifydlashq mdfldflfgp vkkvsglarn fghlynaedt vvaqmefeng vlgsgtwsfv
      241 sdnsskrdvi eiigtkgrie fstfghepvl lfkerdflef pyinpeniqy nlisnvvdai
      301 rgdavgvstg etaartnlvm ekivy
//
LOCUS       WP_010662633              65 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin
            [Marinilabilia salmonicolor].
ACCESSION   WP_010662633
VERSION     WP_010662633.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 65)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..65
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=7347
     Region          2..>52
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mtnkavedlc giwdytfnnw selqadkyys lllevyqdia nnpesgknye eitkellglk
       61 aknaa
//
LOCUS       WP_010662662             418 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662662
VERSION     WP_010662662.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..418
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46707
     Region          315..416
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(319..320,353..354,357,361..362,365,407,411)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mkkillfaml cfliggfvnv qsqikdpeev vkkkgtsrtn kkvddgidkg ldkieeglgg
       61 lfgkkkkkkq petpadsrsn apsrdvqges gepvsspqnq sptmawskfd fvpgdviife
      121 dnqeneenge fpskwdlkeg nveiakygdd yvinfattnq clitplmdeq gdylpekftl
      181 efdayfsefc ttyniflydi itqkrpssmp fvvvranhvs vegfggtdtg lessdyplwk
      241 hisisfnvra lkvyfgenrl cnipnlraqp tgitvrsrqc hagkqalikn iriargskkl
      301 ydrvvtdgki vttgirfdsg katikpeseg ilkkiynlma dhtdlnfsve ghtdnvgeee
      361 fnmelsekra qsvknelvkr gisadrltik glgeskplha nntpegkann rrvefvkk
//
LOCUS       WP_010662649             624 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Marinilabilia salmonicolor].
ACCESSION   WP_010662649
VERSION     WP_010662649.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..624
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=71737
     Region          63..221
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          301..624
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkllinktis iflgvlllgl lpacedfldr qedeamtfek iwknrstvre ywrntmsflp
       61 ddandfnfsp wlgasdegtv tynrdfrwin fgswnptsvp yermthyykg irecnvflan
      121 vdrtsdplvs eeeiqewkvq trfarayyyf lmmrnygpvf ligdeeldft atteqlerpr
      181 ntwdecvnyv vsemddlagk lpeewqsssd yglatrgaal avisrlklys artlfngnel
      241 ysgitnpdgt rlfpafngek wadaahaaka vidlgiyeln regngnpyed wmgitnehwn
      301 seiiwstgyk srysmgvhtv ptgvpgtayg gvgptqqqvd ayamqngryp itgydedgtp
      361 ivdntsgypa defakeqftn pafdagynta sddnenmwpv lfkdreprfy mtvfwsdsyw
      421 khgdrhtlis fakggngnks hdypksgyim hrfydhslps hsgqwgnivf ptfrlgeiyl
      481 nfieavleck kngisipvay eteamslwad lrdragmssi tdaypgaste qlidlirker
      541 rvelafenhr yfdtrtwmia eetdggpmyg mninaeaesg tdtpdlfwqr sifetrvfqp
      601 nhylypfsqr eidrnseliq nygw
//
LOCUS       WP_010662666              86 aa            linear   BCT 01-JAN-2025
DEFINITION  LemA family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662666
VERSION     WP_010662666.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..86
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=9642
     Region          <1..81
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mvavenypdl nasqnflqlq aawneaeeqi saarrsfnaa vttfnnkvet flsnimagim
       61 gykrrtlfei pdverlnvna kklfds
//
LOCUS       WP_010662713             486 aa            linear   BCT 01-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662713
VERSION     WP_010662713.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..486
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=53736
     Region          4..486
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mnvvddffrk sarldkdvlv ssrekisyre laqnvftlsl wfrenfdqgt pvllvspnnv
       61 ffvtvylaim kggcvcvpvn psvepdgfsf vkektrapya flhssvasrl npegiyadek
      121 etlewilnhq ktdyktgpam ppdslaqiif tsgstavpkg vmlthenlma ntssilkylk
      181 lciddtmmvv lpffycygls llhthlkvgg tlvlnnnfmf lgsvlnelkk yrctgfagvp
      241 shfqillrks dsfrknhfpd lryvtqaggk lhkafilefn qvfpeinffv mygqteatar
      301 lsclspsmlp pkagsigkgi pgvqlkvvde tghpvapget geiiasgkni mkgyfedeea
      361 tnatirngwl htgdlgtvdn dgfiylsark keivkvggkr vspkeieevi vdmagvvdct
      421 vegmehpvlg ealkatvvrs pqsdfseedv rafcskrlap ykiptevvfk dqmevsstgk
      481 kikgvl
//
LOCUS       WP_010662742             436 aa            linear   BCT 01-JAN-2025
DEFINITION  phenylacetate--CoA ligase family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662742
VERSION     WP_010662742.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 436)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..436
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49508
     Region          5..432
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 meisiwnrhf etmprepmrt lqserlrevv ervyfnvpyy rakmqekgvg pehiqsvddl
       61 qklpfttkqd lrdnypfglf alpmseiirl hassgttgrp tvvgysrrdi avwsevmart
      121 ltaagvtnkd fiqiaygygl ftgglglhyg gekvgasvip isggntrkql qlmndfgstv
      181 lactpsyasy laeaidesdi sredlklrvg ifgaepwtdn mrreiekklk ikafdiygls
      241 eiigpgvsfd ceyqnglhin edhfipeiid petleplpeg elgelvfttv tkeglpiiry
      301 rtrdltrlhy dtcrcgrtlv rmdkctgrsd dmliirgvnl fpsqiesvll emdettphyl
      361 lvvdrinnld tlelhveved rfyqdkisel qnlgkkiknq iestiglsvn vklvepktie
      421 rsegkakrvi dkrklk
//
LOCUS       WP_010662783             206 aa            linear   BCT 01-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662783
VERSION     WP_010662783.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..206
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22339
     Region          4..202
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 meidiiiwld yigtmvfais gvltagtkrl dlfgamfigv vtaigggtir dlllgvtpvt
       61 wlqgygylia ifsgfaitlv fkkfvarmrr tlflfdtigi gvftiiglek alnlgvnpav
      121 avimgmtsav vggvirdtlt ndlplifhke iyatacitga lfylffnwln lpstlnellt
      181 vgiiiairll sirfnlvipv fktpes
//
LOCUS       WP_010662831             600 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662831
VERSION     WP_010662831.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..600
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=67170
     Region          162..585
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mgrlrnlrer iniflfdirt nffrvmnvls iiaglagiyf iihffgfspd nvttadlifq
       61 lhrvldffll qfcfrvffdf npkkflreni wegfimllil sesivyfifg kawlfqvsll
      121 aglsvqgyfi lvqsifwvvv lretgresmn mrklhispga flalsflili ltgtvllkmp
      181 emtystiswv dalftsasas cvtglivqdt atfftfrgql iimllfqlgg lnmltiatfi
      241 gsfyrksgsl ytssilkdvl dtehigsltg ilrkvifysl sfeiagavll yflwgnqvgf
      301 qdsveriffs vfhsvsafnn agfslftngl feapvrfqyg aqlvimvliv vgglgfivlq
      361 dvftnpayrq rknilwrklt vnsrvvltit fwmlvsgail ffafeynntl kdhslagkiv
      421 asffqsattr tagfntvdts ilttptllff mlfmfvgasp gstgggiktt tfavalkaaw
      481 anirgrehve vykktirwas vnktyaiiav altflfifti llaitnpgfs frellfeqis
      541 amgtvgltlg itgdlsvagk iilvvsmfvg rigsltmvvi fsrrimsgay rypnaklmig
//
LOCUS       WP_010662855             213 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Marinilabilia salmonicolor].
ACCESSION   WP_010662855
VERSION     WP_010662855.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23413
     Region          1..203
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mywstlldgm lvgfsaslpl gpigvliiqr tlqngrtsgl lsgfgaamsd tiyaiiagfs
       61 lsyivtfiea qilwiqlggv ivltglgiki frtnpvaqlr rqkagkhslv sdfvstfllt
      121 lsnplaiflf iaffagfrvl kseyglvghl iiisgvflga avwwtmltsv vglfrskinl
      181 rrlfwinkia gltiivlvva aflfwlirey fyi
//
LOCUS       WP_010662897             207 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Marinilabilia salmonicolor].
ACCESSION   WP_010662897
VERSION     WP_010662897.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..207
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23064
     Region          52..130
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
     Region          151..>203
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiklltgi llfcflsvan fsaaqsgeva qevdkdakfk gspriiasfh ekymnypdda
       61 rlemlegtve ieaivttdgk lmepeiavgv dplldsealr lvrlmqewkp akkdgqevns
      121 rvripvkfsl sdeerafmqt lrnngltdkm plfviddkva kayievphyn vksvrvlkge
      181 kaleqygpda kngvviittk rgtppvr
//
LOCUS       WP_010662937             591 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF262 domain-containing protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662937
VERSION     WP_010662937.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..591
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=70182
     Region          4..509
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 mehktsfkti neflfqkdki fvipnyqrgy kwavkidgkp savekfcddi inadqeqpyf
       61 lqgitvaeed dkiiiidgqq rtttlyfmlc llnynsikni nlkydireks kefiknikdd
      121 nfdylnfdpe dscqdvhyfk kainqikskl enfenkkkee iynfllekvt llyiiidndk
      181 atktftmmng skasmlkeel vkaemlrkvs lpvreektvt tsiddnlhel keiisidwet
      241 nalrsryare wdkwlywwnr edvkdffnte kplgllldfy yrtkpeiiet ikdkntkfsf
      301 dnfkkllsng dneekkktkl vfkelrdlqk sfedvfnipk ihnnlrlalf csnnsedkfn
      361 iidhflqkkn eenykddytk wrlvgathrq itranslred eetkeakaee alkhlsgpyv
      421 ylyakdlalk qllrlnieed nklfnekgrk fdfsiidnqs lehifpkskv yhkvpneegk
      481 ekyqdgnnin ldiaeiqnnp eylnrfdfea gasehcignl vlldknensk fnnrpflekk
      541 iiyfdvskgf ksrnllhsis vfsnsqwkik eiqvqqkafi egfkkdynik l
//
LOCUS       WP_010662911             306 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Marinilabilia salmonicolor].
ACCESSION   WP_010662911
VERSION     WP_010662911.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..306
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34711
     Region          50..243
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16282"
                     /db_xref="CDD:293840"
     Site            order(95,97,99..100,176..177,195,237)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293840"
     Site            order(95,97,99,176,195,237)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
ORIGIN      
        1 mnpgnlhryf illiffffsv cnwvyaqnam lntkeinqia dkfyllsqyg cnivvmagpe
       61 glllvdsgtk eyafktdsvv stisdssiky vlnthfhfdh vggnmklset gatiianeet
      121 rkrmlsewni peiqgmkypk vlpysdkylp vicfedslkl ffnneivqai sypnahsdcd
      181 viyyfqasni ihagdlffsn gfpvidiyyg gtiagyirai dsilelcnek tiiipghgvi
      241 snrqklndyr nmlveskiri fklikegktl deviaanptk dllkegeswi pinifvntvy
      301 qdlskk
//
LOCUS       WP_010662992             762 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Marinilabilia salmonicolor].
ACCESSION   WP_010662992
VERSION     WP_010662992.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..762
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=86659
     Region          5..760
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 msilkkttlf liciflsinl ieaqentpvd yvsttvgtss kyelstgnty paiarpwgmn
       61 fwvpqtgrmg sgwvytytad kikgfkqthq pspwmndygq fsimpltgrl tfdedkrasw
      121 fshkaevakp hyykvhlgdh ditteitpte raamfrftfp esddsyvivd afdrgsyiki
      181 ipeenkiigy ttrnsggvpr nfknyfvvvf dkpfeyyata sdydirkget eirenhsggi
      241 igfstqkgev vharvassfi sheqaminlk elgsdnfgti vrkgeerwne vlgritiede
      301 ntdnlrtfys clyrsvlfpr nlseidangn lihyspyngk vlpgymftdt gfwdtfrclf
      361 pllnllypse nekmqeglvn aykesgflpe waspghrnim vgnnsasvva dayikglrgy
      421 dietlweavk hgannvhphv gasgrtgyql ynkygyipnd agvnqnvart leyayddwti
      481 yqlgkaldrp eeeikiyaqr amnyknlfnp knqlmsgrak dgsfsehfdp tdwsrdfteg
      541 nswhyswsvf hdpqglislm ggydafnnml dsvflvpgse gidsrgiihe mremqvmnmg
      601 qyahgnqpiq hmvylynyag qpwkaqywar eimdklysat pdgycgdedn gqtsawfvcs
      661 algfypvcpa seqyvlgspl fdsvtislen getitikakn ndatsryvss lkvnnkkhkk
      721 nylihrelmk gskiefemsd spnkqrgtse dafpysfsnd lp
//
LOCUS       WP_010663077             271 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Marinilabilia
            salmonicolor].
ACCESSION   WP_010663077
VERSION     WP_010663077.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..271
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31381
     Region          90..184
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mqkgqisnii rslrlirfad rvryvfqlik nrkinrkfkv anpevglppd yliyesfqin
       61 yhkyfaesrg vakwvvekfr pyvcrdngni ldwgcgpgrv irhlpdlldg qwschgtdyn
      121 sksigwcrkn lpgiefnnnn ldaellypnd ffdviyglsv fthlsaakhh ewfeelnrvl
      181 kpggvmlftt qgqnfreklt pdeckrfdag elivrgkvke ghrtysafhp dlfmlemfan
      241 anvevldhev psplagrslp qdlwiirkpv l
//
LOCUS       WP_010663081             504 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Marinilabilia salmonicolor].
ACCESSION   WP_010663081
VERSION     WP_010663081.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..504
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55748
     Region          7..504
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mntpsqkhpq glwvlfftem werfsyygmr allvlyltst ivnggfayae nhaleiygif
       61 tglvyltpii ggiladrlmg qrkaiiiggi imalgqaala yseyvvnsgi slapealqel
      121 reywlfiglg lliigngffk pnistmvgrl yadgdprkds aftifymgin lgaflaplla
      181 gwlgesigwa wgfgsvsvgm vlgtiwfwlq qeklgtigfg pkrsfqteta klngtdwlhi
      241 lgwslgiiaf iylfvktwwt lpeeattwii rivaivsita iayiiikntt gktewsriga
      301 ilvfcffnif fwsgfeqagg tfnlfardft drmigsfeik aswfqsvnai mivglapvfs
      361 mlwvwlgrrn pntpvkfglg lallslgfvv myaadssasg snlvspmwlv mvyllhtmge
      421 lclspiglsm isklsppkit slmmglwfas talanylaga lrgilenylp dmnlflflvi
      481 ssgsaalllf lispwlkkmm rgid
//
LOCUS       WP_010663103             421 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010663103
VERSION     WP_010663103.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..421
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=47778
     Region          4..421
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 meylpiiiat ilfsaffsgs emaflsankl lielnrrknp riarlidrfl rkpgmfitti
       61 lignnialvv ygiymgqlfe pmiaryfssd failllqtli stliilitae flpkilfrln
      121 pvftlnmfsi pltlfygtff pisrltvgas nfllkkfgns teaistedlv igrldfnhll
      181 eehqeqnatd ssvpqevkfl knaldfssvk irectiprtd leaidaeesi enlrqkfids
      241 ghskilvfke nidnivgyih vselfkhprk lkniinpisi vpetmtankl leiftkehrs
      301 ialvvdefgg tagivtledi leeifgeidd ehdisdlvek qvddqkyhls arfevdylne
      361 kypldlpvsd eyetlagmil nfnesiptig eeikipgftv rildatsski elvelikqte
      421 e
//
LOCUS       WP_010663088             270 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010663088
VERSION     WP_010663088.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..270
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28647
     Region          22..267
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mltkkgntyt isqitenekm eitdaiilia aglaagvint fagsgslitl pllmfmglpp
       61 avangtnrig vvvqnlvatr nflqqkelqp kkewsliipt lfgsllgalv aveinediln
      121 yfiggllvvm ffvillkpaa wikgqasqvk ttksriinsi ifffigvygg fiqagvglfl
      181 laglvlsagy nliranavkv lmvlsftiva livfisagqi awsyglllaa gnavgawfas
      241 knaskigtkn iryillavvl isglkvlgvf
//
LOCUS       WP_010663111             399 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010663111
VERSION     WP_010663111.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..399
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=43725
     Region          1..383
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mssfvrkyik gdqtiwvivv flalvslltv ysatgslayk tqggnttyfm fkqltfllmg
       61 igvivvvhhi pykyfvifsv palyisiaml gltlvsgqnl neasrwftvp gigisfqpse
      121 maklalivyv arvlaqhqrd dgptegafwp imihagivcl lifpenlsts vllagvvmlm
      181 mflgrvpfky lfftgftgla ivslvlilam ndvvlidrae twaarverfm edenqedeyg
      241 sdyqltqski aiatggmigk gpgnseqrnf lphpysdfif aiiaeefgff gavavviayf
      301 fllgrigviv nsskrtfpaf mvlglglmlv iqafvnmgvs vgifpvtgqp lplvsmggts
      361 ilftcfglga iltvsrynqq ekarekaaea rlakteqen
//
LOCUS       WP_010663131             148 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Marinilabilia salmonicolor].
ACCESSION   WP_010663131
VERSION     WP_010663131.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..148
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16292
     Region          7..144
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mekidftdqy fmkqaylear ealrkdevpv gavvvsegti israhnltet lndvtahaem
       61 laitsaseal ggkylnnctl yvtlepctmc agalnwsqig rivygadddk rgykrmtpsp
      121 lhprtevigg vmkqecgelv kqfftgkr
//
LOCUS       WP_010663178             143 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Marinilabilia salmonicolor].
ACCESSION   WP_010663178
VERSION     WP_010663178.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..143
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16087
     Region          1..134
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mtaseildhh kvkkttpria liqvlqessg pqseneirdv mgelydratf yrsvqtltya
       61 giihrivadn vmvkyalnnc ekghhhqvdh ahfycrkchn lfclksikvq slnlpdgfvd
      121 eehdlvirgi cnqcgdsvtv gdv
//
LOCUS       WP_010663224             519 aa            linear   BCT 01-JAN-2025
DEFINITION  M28 family metallopeptidase [Marinilabilia salmonicolor].
ACCESSION   WP_010663224
VERSION     WP_010663224.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..519
                     /product="M28 family metallopeptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0008235 - metalloexopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=57980
     Region          309..514
                     /region_name="Iap"
                     /note="Zn-dependent amino- or carboxypeptidase, M28 family
                     [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]; COG2234"
                     /db_xref="CDD:441835"
ORIGIN      
        1 mktlsfitfl flfstqyays qntyeknkai esisanelmt dieflssdll egreagkrga
       61 riaalyiasr fkqlglkpfn stsdlnnttd qyiqkvplvw snveeacmvl kkgqqdirfa
      121 petdfnppvt dysfningkv vfagyglgvk tkeglknkil lrakgytgmr dtlskgyqqy
      181 nslsereltn iknsfageag vsvilefdpe nptfpvltgn ekkdyaekel skrssgiykr
      241 svrrsgtels vnppvfkvsh rivnalfpnw eemlseynpi dkrkrslpts isgievsvev
      301 ketpftcgnv igeiegknkd eiivigahyd hlgmydgyiy ngaddnasgv agvialakaf
      361 tksgaipekt lifaawtaee rglhgsthfv ntfndtekik yyhnydmigr ssnpeepdsa
      421 vsflytkswe hakkitmenn kganinlnir wgamedptgg sdnapfakke ipimwfhtgg
      481 hpdyhgpydh sgkidqakie kiiklsflni rdlafgknq
//
LOCUS       WP_010663232             163 aa            linear   BCT 01-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Marinilabilia salmonicolor].
ACCESSION   WP_010663232
VERSION     WP_010663232.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..163
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=17792
     Region          2..118
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 minkvilvgn vgkdpdvryf dnnkgvanft lattergftt rdgrqipert dwhnvtvrrg
       61 lvkvaesyik kgtqlyvegk lrtrsyeqdg vtkyvtevia dtvkllgrks dnpavddnsy
      121 sgnsgaqptp dsgqsmapqn qssgnegfsa gddsneqedd lpf
//
LOCUS       WP_010663397             331 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent glycerol-3-phosphate dehydrogenase [Marinilabilia
            salmonicolor].
ACCESSION   WP_010663397
VERSION     WP_010663397.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..331
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=37054
     Region          6..328
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
ORIGIN      
        1 mdeestigii gsgswataia kmvmnnsdrl nwyfreqehi drfrkmdhnp nyltsvdfdt
       61 dqiffstdin eivensdvli favpsaflke sleslrtplk dkfvvsaikg lvpdenliig
      121 sffnkhyevp idsiavisgp chaeevaler lsyltiacqd ikkarifasr lacsyikttv
      181 iddiygteys avlknvmaia agichglgyg dnfqavlisn giqeikrfvd tvhpitrdik
      241 ssaylgdllv taysqfsrnr tfgnmlgkgy svksaqleml miaegyyavk siveinkkyk
      301 vnmpiteavh niiyekispa ieiklltdql r
//
LOCUS       WP_010663412             411 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Marinilabilia salmonicolor].
ACCESSION   WP_010663412
VERSION     WP_010663412.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..411
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43018
     Region          7..411
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 meeitkqvse itvsldmlwv liaaamvmfm qpgfamveag fsrakntani lmknfldfsv
       61 gslmfwligf simfgtdlgg figmpdlffs gsygndvdya ilifqtvfaa taativsgav
      121 aertefkayi lasffitavi ypisghwvwg ggwlselgfh dfagstvvhs vggwlglvga
      181 atvgprlgky ngkrkaipgh sltigalgvf ilwfgwfgfn pgsqlaasgl dnisavasif
      241 vttnlsaaag tvtamiiswm rykrpslgls lngalaglva itagcdivsp ggaviigvia
      301 givlifgvei ldklriddpv gavtvhgfsg avgtimvgll atdgglfygg gasllgvqal
      361 gvfsvaawal amgfilfrti kstvglrvpk rveeegldiy ehgetaydnl t
//
LOCUS       WP_010663582             134 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Marinilabilia salmonicolor].
ACCESSION   WP_010663582
VERSION     WP_010663582.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14436104
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..134
                     /product="response regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14968
     Region          19..128
                     /region_name="REC_hyHK_CKI1_RcsC-like"
                     /note="phosphoacceptor receiver (REC) domain of hybrid
                     sensor histidine kinases/response regulators similar to
                     Arabidopsis thaliana CKI1 and Escherichia coli RcsC;
                     cd17546"
                     /db_xref="CDD:381099"
     Site            order(25,27..28,30..31,34..35,38,96,118,120..121)
                     /site_type="other"
                     /note="Hpt domain binding site [polypeptide binding]"
                     /db_xref="CDD:381099"
ORIGIN      
        1 msdsnlsdal nqdwgdkvil vvedvdtnki ffdaalrrts akilwakdgq qaidlfkenn
       61 vdlvlmdlql pvmdgytatr eikkinpdip viaqtahvms gerekcmeag cddylakpir
      121 lqilietlsr flns
//
LOCUS       WP_010663585             717 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Marinilabilia salmonicolor].
ACCESSION   WP_010663585
VERSION     WP_010663585.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..717
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78892
     Region          27..112
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          94..656
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mssnvkslil avsffvylqp vlsqivvsgh vtdkrtgegl pganvyvkds ydgtitdekg
       61 lykleiqnsg eiilifsfvg yqsvekslsg tdnatidvql sesitslnav titagsfeag
      121 dkkraavmdp mdiyttagsl gdigtalktl pgtqvaaddg rllvrggdas etrvlmdgvl
      181 aakpyyskvp dlptrgrfsp slfegtffst ggysaefgqa lssvlvlesq dvateeltsv
      241 slmsiggela ntwvgdnrsf satggyfnfg pynslvknhm dwedhveavn anisyrqqgd
      301 kgslfkffas gdyggqsfrv pdgtggdlmi dedggniyan styhrsitdk tlmklgasyt
      361 fddqdfragi hnqqtgegvs eakvklisqi ngrfkltygg awqrtsfdet ykqsesgfsi
      421 nanfsdnlys afseaewrln srlafrpglr yeystqsnek alspraamaf aagknttvsl
      481 awghffqtaq sdflkynrdi kmqksehfiv glqsgslatr lfrteayfkd ysglitgeyn
      541 dfgefvpman qgsgyakgid ffyrdktlie nldfwvsysy idserkfmdy hkkvtpefia
      601 phtfslvakq fvspirsqvg ltwmwnsgrp yhipgddnfm ahtspnysdv ganisyltsl
      661 fgqftivhls isnvlgreni lgyrrvslsg dsenasliti kpdvkqfifl gvfisin
//
LOCUS       WP_010663621             415 aa            linear   BCT 01-JAN-2025
DEFINITION  M48 family metallopeptidase [Marinilabilia salmonicolor].
ACCESSION   WP_010663621
VERSION     WP_010663621.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Bode,W., Grams,F., Reinemer,P., Gomis-Ruth,F.X., Baumann,U.,
            McKay,D.B. and Stocker,W.
  TITLE     The metzincin-superfamily of zinc-peptidases
  JOURNAL   Adv Exp Med Biol 389, 1-11 (1996)
   PUBMED   8860988
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Stocker,W. and Bode,W.
  TITLE     Structural features of a superfamily of zinc-endopeptidases: the
            metzincins
  JOURNAL   Curr Opin Struct Biol 5 (3), 383-390 (1995)
   PUBMED   7583637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..415
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47638
     Region          10..411
                     /region_name="M48A_Zmpste24p_like"
                     /note="Peptidase M48 subfamily A, a type 1 CaaX
                     endopeptidase; cd07343"
                     /db_xref="CDD:320702"
     Site            order(277..278,281,355,359,399)
                     /site_type="active"
                     /db_xref="CDD:320702"
     Site            order(277,281,355,399)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320702"
ORIGIN      
        1 mqthtllfff iitillldav wgwileelnr kswadkvper lsdfypqekf ekqkqyrkvn
       61 hrfgkisstf slvvlliflw fhgfarvdel vqqltthwlw rplfffgvvg lasmligipf
      121 slyetfviee kfgfnkttpk tfildqikgi figaiiggil lgliiwfyef agrwfwlyaw
      181 igllafmiff skfyttlilp lfnkqtplee gelrsaiekm sqkagftlen vfvmdgskrs
      241 tkanaffsgf gknkrivlfd tlirdletde ivavlaheig hfrlkhivrs tvlgvlqtgi
      301 mlfllgwfvn epalsealga skpvfhigli gfgilyspvs slsglgmtif srrneyqada
      361 faakyarpea lqtalkkisa nalsnptphp wyvffnyshp pllqrleald kkvrr
//
LOCUS       WP_010663649             793 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Marinilabilia salmonicolor].
ACCESSION   WP_010663649
VERSION     WP_010663649.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..793
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86979
     Region          37..121
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          108..737
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mrtryilpii slfliisgit tatasgeqpi kppsatlegq itnngepipy atvqikstmi
       61 gtattdegnf amsapegsht ivvralgykp vekevqiseg qthslhmeie edvlgleqiv
      121 vtadrnsekr kessvivntl nnamleavqt anlseglays pglrienncg ncganslrmn
      181 gldgpysqil ingrpifsgl aavyglelmp snmierievv rgggsalygs naiagtvnvi
      241 trepvtnqys isaqtsqigs mvedadqgsd qqinfnatls gkenknglal ygslrkrtsf
      301 danddgfsel seldnttiga qwslrtgyks klvtdffhid enrrggdsfd lpyhealiae
      361 atehkintas aswhlftgan qelnvymagq dikrdsyyga gkaldaygnt hdlsysggvq
      421 ykilnpglni itgvevnggn lldkklgyre fiwdeetmnv vaenvpsrti adqesmvggv
      481 faqlekkine lsisgglrld hytiedfvtg sensnnvlsp ritmlyglts pfqvrasyak
      541 gyrapqifde dlhietsdsr qvihendpdl kqetshsftg slsytieran snlellaeff
      601 htklqdpfan eigtpdafgk viytrineee gatvqgvnle akwapsasfd lnagftiqts
      661 eygapqdfne trflrtpdny gfftinwnpi dhwefatngi ytgkmlvpyf gpladdpdtg
      721 llkesdpffd waakvtycle tnvgdfdffv gaknilnnyq sdfdsgaerd pgyiygpvnp
      781 rtiyaglkis nif
//
LOCUS       WP_010663676             423 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A [Marinilabilia
            salmonicolor].
ACCESSION   WP_010663676
VERSION     WP_010663676.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..423
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47500
     Region          1..423
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msgypplaer mrpqslehyi gqkhlvgega vlyqmvssgr issiilwgpp gvgkttlari
       61 ianqlerpfy tlsavnsgvk dvreaiekar karffnsasp ilfideihrf sksqqdsllg
      121 aveegvvtlv gattenpsfe vispllsrcq vyvlkplene dlmvlfnrif sedivlkhrp
      181 vklkeeealf rfaggdarkf lniielitna fkedeeivit nenvtrqlqq npaqydknge
      241 mhydiisafi ksirgsdpda avywlarmve ggedpkfiar rliisasedv glanpnalll
      301 atnafeaikm vgwpeariil sevtiylats pksnsaymai nqaqevvrnt gnlpvplhlr
      361 naptklmkkm dygkqykyph syennfiaqd ylpdelkntn lftpqnnpqe skigermnkl
      421 wgk
//
LOCUS       WP_010663678             268 aa            linear   BCT 01-JAN-2025
DEFINITION  M48 family metallopeptidase [Marinilabilia salmonicolor].
ACCESSION   WP_010663678
VERSION     WP_010663678.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..268
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29953
     Region          67..261
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(138..139,142,201,205,244)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(138,142,201,244)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mkntfkitvf avfltffgys cstvpitgrk qinalpesem lamsltqyee flktnrvsed
       61 ksqtelvkrv ggriaaavee yfsdhgmkdr iedfawefnl vedetpnawc mpggkvvvys
      121 gilpitktet glavvmghei ahavarhgne rmsqqmgiql ggtvlsiaid ekpeqtksif
      181 maaygvgsqv afslpysrlh eseadqlgli fmamagynpe eavdfwqrms aqggqkppef
      241 lsthpsdetr irklreflpe akkyykkn
//
LOCUS       WP_010663695             482 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Marinilabilia salmonicolor].
ACCESSION   WP_010663695
VERSION     WP_010663695.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..482
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54041
     Region          7..474
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mnairiaked kvpffqkiaf gsghlanqlf paalgvfmvv lvmslgmnpi lagllgalpr
       61 lidaltdpvm gfisdntksr wgrrkpyill gsviagvafm imwqlnpens elynffyfli
      121 vslffyigyt ifatpliglg yemtpdyner trlmavsqfm gqiawmiapw fwviiynqsl
      181 fdsapegari laiwvgglcm ilgimpalfn kemivpekdk mkrlsmsema anfkhflsgi
      241 kktlknkpfi rlcgatflif ngfqtiaqfa ffiivyylfs gdkaaagnwp awfgtisala
      301 taflvipvvt kisekvgkkn afiiatlisv igyslkwwgf npenpwlmfm pipflsfgig
      361 glftlmmsmt advcdldelk ngerreamfg avywwmvklg nalaillsgi vlhyvgfnen
      421 vdvqtadtiv nlriadiaip iftalmailv ifpyditekk aneirealia rrgkvhhqde
      481 en
//
LOCUS       WP_010663704             275 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010663704
VERSION     WP_010663704.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..275
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30327
     Region          12..275
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 meqfkewfsn peqildialk yggqlllail tlviglwvis kivkgmkkmf eakgfdaslq
       61 sflisltgiv lkimlvisvv tmlgvemtsf vailaaagla igmalsgtlq nfaggvmili
      121 frpfkvgdyi tseghsgtvk eiqifhtiln tpdkktiilp ngpvsngstv nystepvrrv
      181 dftfgigynd didkakevim sviekderil kdpepfigvi nlgessvdlv trvwanaady
      241 wgiffdmqet vkkefdrqgv sipfpqrdvh lfqak
//
LOCUS       WP_010663714             966 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010663714
VERSION     WP_010663714.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 966)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 966)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 966)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..966
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..966
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=111491
     Region          152..964
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mrffleqlad yhlqkyltdi sefcfvfpsr ragvffrqyl ndktpkpvfs peiltindlf
       61 gkleprpvsd nislifklyd syrevmdkdi tlddfipwge mcladfddid kyladpeqlf
      121 rnladqkald ddfshldddq veairtfwss fdpeklsrlq ksflevwekm pelyrhfner
      181 ldrdneayeg kmfrltaqki qdktvgevpy khivfaglna lnncekrlln ylkikgiatf
      241 fwdypqwime apvqssdqgl irgeheaarf iksnildfpm padwdnpqhd gpekitiata
      301 andlgqtqia aeflnqippq nnagpdkeda phaktalvla dealmlpaih aipeawdkin
      361 vtlgyplknt payglvetlm tlqqsmrttr qgktwfyhrh llgllrhqyi ttimgkegrq
      421 lvnkliaanq vfieksnipa hdltdrllkk tnttedltey lknvlqmvyq hlkknpeanl
      481 erefvyhlyl tikrlgeils aqtekitpet whrlfrklad fqtvpfrgep lsglqvmgil
      541 etrvldfdnl vilsmnegvf phtappnsfi pynlrkgfgl ptidnqdsif ayyfyrlihr
      601 aknvtlawas sdakgqagem srflhqlyye ypgvvqndty iqsvgtkmap eifsekneev
      661 kkqlseyfkd garalspsal styiecplrf yfkylagake aediseeldp rifgnlfhqt
      721 vealyqplln qvvtpeiine iakpdkiatt lekifaknvp firqdksvfv dlqgknslvf
      781 evlmryltgf fksekqnapf tlkglesnih mdfitpagkt irlggnidrl dekkgitrvi
      841 dyktgqgdnk iskfedlfdt skhskikatf qtllyslmve nrgtppekiq pgvvwmrklf
      901 tdtdtslwlq qgrqqkspit lalakdeyqd glgqlldelf dekipfrqtt heknceycvy
      961 reiclk
//
LOCUS       WP_010663729             762 aa            linear   BCT 01-JAN-2025
DEFINITION  AAA family ATPase [Marinilabilia salmonicolor].
ACCESSION   WP_010663729
VERSION     WP_010663729.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 762)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 762)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 762)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 762)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 762)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..762
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=88083
     Region          5..746
                     /region_name="RloC"
                     /note="Wobble nucleotide-excising tRNase [Translation,
                     ribosomal structure and biogenesis]; COG4694"
                     /db_xref="CDD:443729"
ORIGIN      
        1 madkkittli kcqniapien lnreiksssl kmgvfanngs gktflsrlfr ltenkgkial
       61 dennqsptdk lltfgkqngd fsfkvidknn nikddfnisi kkgqattipe tkylyhtfnq
      121 dyveqniqvl gyekdseieg filgkvnidl kddednlaki ekegkelseq vekeidsyvk
      181 knlsniqnik rlrefaylrp keifqgiekn lfpvskglde lfsdynkiks vpenlldiga
      241 ierinidfni lngikenlnk efslsslaen fkqkikskqt fiekgmslls etesntcpfc
      301 eqklqenain lisnytkyln dteaktikqf nentewlsnl iaslksient nsyrinsyne
      361 yktkyipssa keelgilkvk aaqqaiqsyi diieeklkdi skpilvensi ieniekhqtl
      421 lnktidsnnk kikslnakkn qigeenktvr keickcayny lvethktnik tishlreqwk
      481 tldlqikkkk eqqkvskrek vastiktvln yffsdkytld eetfrlvfyk talekdqard
      541 vlsegekniv afayymgdth lkiereddye klffiiddpi ssmdfthvyt lcgvirdisq
      601 iidklkntrl fifthnndfm rvltannivd kklllkkgel kdfnnnltvp yinhlmdvyn
      661 varkdenash ttansirhii etltkfqkid iskdgiaeyi ksnipndsks ftlindlshg
      721 gwrseqspit eddykevcet iikhiekdfc gqieyckkii eq
//
LOCUS       WP_010663743             258 aa            linear   BCT 01-JAN-2025
DEFINITION  ion transporter [Marinilabilia salmonicolor].
ACCESSION   WP_010663743
VERSION     WP_010663743.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..258
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=29323
     Region          9..223
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mfkrfflnen filgviilns itillgafdn lspaqtkfit tidnvitvif viemvvkime
       61 fkiggyfssn wnkldcllvl lsipaliswi fdlslsslsf flifrvlrvf ksfrflkfvp
      121 gitdlikgvq ralktsvvii lgfciyifii gifstylfqn iapehfsnpl tsfysifkif
      181 tvegwyeipe qitantdgtv sffsklyfvf ilvtggifgl slvnsifvea mlsdntddis
      241 qkidkledkl dnylrnkg
//
LOCUS       WP_010663744             198 aa            linear   BCT 01-JAN-2025
DEFINITION  fibronectin type III domain-containing protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010663744
VERSION     WP_010663744.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Bloom,L. and Calabro,V.
  TITLE     FN3: a new protein scaffold reaches the clinic
  JOURNAL   Drug Discov Today 14 (19-20), 949-955 (2009)
   PUBMED   19576999
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Koide,A., Bailey,C.W., Huang,X. and Koide,S.
  TITLE     The fibronectin type III domain as a scaffold for novel binding
            proteins
  JOURNAL   J Mol Biol 284 (4), 1141-1151 (1998)
   PUBMED   9837732
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Potts,J.R. and Campbell,I.D.
  TITLE     Structure and function of fibronectin modules
  JOURNAL   Matrix Biol 15 (5), 313-20 (1996)
   PUBMED   8981327
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10637183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..198
                     /product="fibronectin type III domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=22110
     Region          27..91
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
ORIGIN      
        1 mrklilalvi stflvsgcsd dettrvniei sedvvasngf tinwepleda lyydvmitpd
       61 vweqstmvsn etsitfdnll adteytvlie agssleqeti igegsinitt eavrqefvgt
      121 weynystlve syvlngdgtg kyiydgdesd iiwsagasef afkllnengg gfyyyyeysf
      181 nsdntiltld gtnyflqe
//
LOCUS       WP_010663759             169 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Marinilabilia salmonicolor].
ACCESSION   WP_010663759
VERSION     WP_010663759.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..169
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20362
     Region          5..166
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mktsqrqeke fasflekykr liskvsgiyc hnpeerkdli qeiiiqlwra ypkydkkfsp
       61 atwtyriafn vsishlrkrt srsrireayk nemewldfap pphderlekl yhfidllkpm
      121 dkaiimlyle eyankeiari tglsvsnist rklriketlr tyfekekth
//
LOCUS       WP_010663829             561 aa            linear   BCT 01-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Marinilabilia salmonicolor].
ACCESSION   WP_010663829
VERSION     WP_010663829.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..561
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=64374
     Region          63..508
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          280..561
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkrtiiyfaa vlvvlfsgck dsfleqtpqg vldesqvtsp deidklviaa ysmlgndhyd
       61 vpfslwpygs vrsddaykgg rdeadiddfh fyeisenmrl dagptdgmwf nlyvgisrtn
      121 aalrvlnsvt eeqykqkaer tgelrfirgh fyfllkvlfk nvpyidetvp aedyetisnt
      181 alsndeswsr iaddfryaye ntpkqqdevg rvtsyaaasy larvllyqay qqdaqhnvtg
      241 vdqamlnevl qlteyvmgsp ytlepdfann fihgsyengp eaifsiqfsh ddgtfhgrln
      301 fsdvlatpqg lgccdfhkps hnlvnafktq nglpafdsyn depydegihs vdprlyhtva
      361 ipgypfkynd nqiyeeswnr npgiygvyas lkenvdpesd afinidpfyg nsknriiiry
      421 advllmraea lielnredea lplineirar aqvstpkiey apnlqtalyq dgvncdwtnd
      481 farkalrwer rlefamegyr ffdlvrwgva dsvlneyyes eaqrityyen gdfdknkdey
      541 lpiplqqinf skglydqnps y
//
LOCUS       WP_010663146             226 aa            linear   BCT 01-JAN-2025
DEFINITION  2'-5' RNA ligase family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010663146
VERSION     WP_010663146.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..226
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26538
     Region          43..226
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 melfqhynal yrkavheind erlvvdsmmd sesderrgit llirpddqvk eevsrflnvl
       61 kdvepdqyyy pesdfhitvm sliscydgfh ydridlsrya evvkesiadv gtmgfifkgi
      121 taspscimvq gfptgtglni lrdrlrknfr ntdlqqsldk ryklqtahst vvrfreplan
      181 kkrflkvlea yrdyrfgtfr adslemvfnd wyqktelvek lhtfsl
//
LOCUS       WP_010663954              81 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl carrier protein [Marinilabilia salmonicolor].
ACCESSION   WP_010663954
VERSION     WP_010663954.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..81
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9152
     Region          1..77
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mkesvknfia etsftdpaki qddtmlfeeg ifdsmgllsl isfleesfgi qtddvdlmed
       61 nfknlnaiee yikrkksysa v
//
LOCUS       WP_010664070             293 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Marinilabilia salmonicolor].
ACCESSION   WP_010664070
VERSION     WP_010664070.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..293
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33592
     Region          5..222
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 meniiecrhl thyygdrciy edlnfaiakg rivgllgkng tgktttinil ngylqpksge
       61 crmfgqkagr lspsvkqkva llleghvqys fmniaqiekf yasfyplwdk vpfwelmnkl
      121 kiapkqrisr mscgqrsqva lgiilaqnad llilddfsmg ldpgyrrlfv dylseyahae
      181 dktvfvtshi iqdmerlidd cmildygkll lqqpvdrfld sfkryrmtss lapnwekmpv
      241 vhpekirnkm efysdagrqt ivqnleeqgf easdlqeesl tleeafiglt gky
//
LOCUS       WP_010664147             439 aa            linear   BCT 01-JAN-2025
DEFINITION  permease [Marinilabilia salmonicolor].
ACCESSION   WP_010664147
VERSION     WP_010664147.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..439
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=47738
     Region          43..439
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 meikkelkil gwiiavflfa ffmpldsarf qeaimatfdl tkwyaqehvi lcllpaffia
       61 gviavfvsqg avmkyfgaka kkwvaytvas vsgtilavcs ctilplfssi hkrgaglgpa
      121 iaflysgpai nilaiiltar ilgiemgiar iigavvfavv igsamsliyr keekvkreeq
      181 lnfpdvpeer pmwqtafhff tlvlilvfan wgkpgddvts ggfywlwank wyitsffsil
      241 lvfslifilk lrwqyvalgv iataasaflt tsplvpmvvg iaalsiitlt dkkhdenrew
      301 tmsawdftkq impllaigvv tagfllgsth ddtamagiip eswitslvgg nslfsnffas
      361 ivgafmyfat ltevpilqgl maagmgkgpa lalllagpsl slpnmlvirg vmgtqktlvy
      421 iglvvvmatv sgllfgtfy
//
LOCUS       WP_010664177             228 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Marinilabilia
            salmonicolor].
ACCESSION   WP_010664177
VERSION     WP_010664177.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..228
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25812
     Region          17..225
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpdkintesi fdsaacfqgl ypeeleklsd sktrvqylkg enifkqgafs phvtyvlsgl
       61 vrvylqtghn rqlnirmagp gdflsfssvf gettynysal avkdawvcmi ekdalrnllq
      121 nnadfalriv srncrnekql ldvignlsyk qmrgklasal lylssesfmq eqvfqhltrq
      181 diadfaaist estikflkef esegivelkk kdieiknikk levisrns
//
LOCUS       WP_010664111              79 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl carrier protein [Marinilabilia salmonicolor].
ACCESSION   WP_010664111
VERSION     WP_010664111.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..79
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9178
     Region          1..79
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mnakeirrnl ykvfrmtgip rnvidekasl tddlfmddvd macflfylet rfkvnvknee
       61 mthlqsvgst inylqqhca
//
LOCUS       WP_010664183             292 aa            linear   BCT 01-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010664183
VERSION     WP_010664183.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..292
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31826
     Region          1..284
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mkdkknialv lssggakgia higaieelqr qgynitsvsg ssigaviggl lamgrledyt
       61 hwiktldrks vwglmdfsft sngllkgerv fdrmkefipd idieemtlpf tavasdilne
      121 keivfdkgsf yraarasiai pamftpvkyd gtflvdggil npipiehvrr rdndllvvvn
      181 lygekqpkae lvdesqkeke khgegglfaa fsnlvatgdk kslgyisllt issaamihkl
      241 akmnidrfkp dlvidipads astfdfhrsd ellklgadat akaiyaktqe ag
//
LOCUS       WP_010664248             445 aa            linear   BCT 01-JAN-2025
DEFINITION  flippase [Marinilabilia salmonicolor].
ACCESSION   WP_010664248
VERSION     WP_010664248.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..445
                     /product="flippase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50173
     Region          20..393
                     /region_name="MATE_Wzx_like"
                     /note="Wzx, a subfamily of the multidrug and toxic
                     compound extrusion (MATE)-like proteins; cd13128"
                     /db_xref="CDD:240533"
ORIGIN      
        1 mriisfitkk lkftgnkekv ainvswavlg kvvnilsslf igilvarylg pedfglmsyv
       61 msyvaifqvl atfgleniei relakedsdv pkimgtsfii rmilafttii aifvtliifk
      121 tdqqtktlvl ifsttlifst tkiirnyfts ivqneyvvkt eisrtiigat ikilllsina
      181 pliyfimass fdlflvatgf iisfnkkigl klpwkfdkwy aiylikqsfp lllsasavvi
      241 yqkidqvmik qmmdnvsvgq ysvasriiei gifipvivsq tiapllvkkl hkckdayikk
      301 rqqymsiivw ggilisliif ilskpavtil fgsqyldaip vlkilswkva lmglfnfsaq
      361 iiiiegihkf vavrnifacf tsvllnyfli phygiigssi asisaffisg ylahlfipgy
      421 rfifyiqtks lavgwkqffn ikslk
//
LOCUS       WP_010664277             823 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Marinilabilia
            salmonicolor].
ACCESSION   WP_010664277
VERSION     WP_010664277.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..823
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=90710
     Region          1..816
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mdflnlkesv kscvqiakgf areygngayy pahllkalmh kdiglkgfis slgkdtgyle
       61 ewaevriddl pkgkadgevg adesiaavfe eadnvrlkwg lleinpvcvv talarpgigf
      121 sidelksfpl reqeihdsvi adkdlnvsfa mndedggnlg gnsmasllky cidrnadiqk
      181 qgvapvverd seirmmmeil grhsrpnvli tgdsgvgkta lveglisgiv ekkapsfllg
      241 atvyeldtgs lvagatykge vedrlkgiik dlrkserail fiddihvlld pkqgnsgavg
      301 ilkpelsrgd ltiigttsvd eyrkiiepdq afsrrfevle lnepdldtas rmvnavvgry
      361 eafheinvag esvpecvsla qryvkdrklp daaidlldrt msavkminet aegniqnlfe
      421 qievvesnkk kqppqkvsel klinasmqnl lgpvlmgelt gnqdtddlds yvewldylqq
      481 sltvlqkyae ngvdvitahe iaavissktg ipigkiqage kerllnmedt lrrrvvgqds
      541 alkslvdail esrsgmnrag qpigsffllg ptgtgktela kalaealfnd ekamirfdms
      601 efkeehsaal lygappgyvg yeeggmlvnk irqqpysvvl fdeiekahas lydiflqimd
      661 egklhdrlgk egdfsnaivl ftsnvgsqwl meqkdagnqp tttqlmevmg qyfrpeflgr
      721 lseilpfspi tddillkifd iqfksitdtl edkgigivls dearkilahk gftpkygarq
      781 vngvirnfir rpvsrklisg ilkkgdtlev nldedeelvw sis
//
LOCUS       WP_010664279             261 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Marinilabilia salmonicolor].
ACCESSION   WP_010664279
VERSION     WP_010664279.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..261
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29096
     Region          3..252
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mqemidiriw dlllgfsilv ipffifsyyr vklnrdlivs vlrmivqlfl vavylewife
       61 knnawinaaw vlimvvvggg tvvkrvgipw kqfllpflia glismaiidg fflglviktg
      121 yffdaryfvp isgmvlgnsl nhnivgltaf fkglhkdrel yyflltnsgs srlalrpfiq
      181 dalikglnpl latmsvigli slpgmmtgqi lggaspavai kyqvmimlai fvgctltlvl
      241 silfskrmaf demgnvreka p
//
LOCUS       WP_010664298             653 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Marinilabilia salmonicolor].
ACCESSION   WP_010664298
VERSION     WP_010664298.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..653
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=71582
     Region          6..>61
                     /region_name="COG4192"
                     /note="Signal transduction histidine kinase regulating
                     phosphoglycerate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443346"
     Region          106..586
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnwrdlsiss kirgsiaavv vltllmggft lyslfeigsg vndlsekyip tvneaslvdq
       61 nwrkltevtr sydfsaqpyf devfdryytq mmvalnnlie megegarsse fselkkkmea
      121 yaamyedyse aqksasnhre lmrmageelv dlsgnyrtnv ryqqfinral glwgvvqakd
      181 ytreavaldt elskartlqt dinaaylsga vtatlndfvs saisfiehyq karfaevkry
      241 elgkeimwdt raiadmgqgd ikgmgnqsar ivdniqtlvi aalivlllvg lilalllpns
      301 ianpiiqgvg laekvaagnl svrfdtnrkd evgrlgvald nmvknlrvii gditegtrem
      361 veastslsre stelaegase qasaaeevss smeemhaniq qntdnarete tiarkaaedm
      421 nssneitera aefleqitsk isvigdiafq tnilalnaav eaaragiegr gfavvaaevr
      481 klaersqqaa ndinkvsgmt inssresrem llaltpeiek tagliqeisv asleqvtgve
      541 qinnalqqln qvtqrnasns eeinsaalri eklserlera isvfslseen rkkdvnesgt
      601 pavseesdka tkvekeeega ncsvsqsqlk akakgktpdf dlggfgsddy ekf
//
LOCUS       WP_010664302             481 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010664302
VERSION     WP_010664302.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..481
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53761
     Region          153..477
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mpdsmkiiky itpialvlis sfaasaqvel nqqkcremal dysrqikise nrheqallsg
       61 kiaraqhlpk lsasglyfyk pdpleysleg gylptytpgq ngemqpnvqm npntgqpvtg
      121 pdgnpvfnmy ammpdmnlni gmegvttagv qleqpvylgg kiraanklag tgiemskkqm
      181 dlkkseviss vdaayfqyla vkekkkaane ykvlldslea tieatnregm strnellkvq
      241 vkrneaillk qkansglqla amnlcriigl pletelhide teetelpdir padgnnpsdr
      301 peyqllndai avkqhqekla raemlpqigi sagysylggl eingqgtdem afsamasvki
      361 pifkwfeern rlskaqlete varmeleene kllqldiara rfnleesftr leltekaleq
      421 aqenletsqs lfeegmeplv dlleaqvqwq karseyidae tslklmhtyy lkatgrlsvk
      481 k
//
LOCUS       WP_010664404             247 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010664404
VERSION     WP_010664404.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..247
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26915
     Region          3..245
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgkiiafinq kggvgktttt asvvagmahl glrtlaidld aqcnlttsfg vtdfrantyn
       61 tlkgelglep tkidehlail pssvdlsafe lemsaepgke yllkellepv ldqydyilld
      121 cspnlglvsi naltaadlyi ipllphhlsi qgltklleit dkvkkrlnpg lkmggivltq
      181 ynnrkvlhrd iaqvvqehfg qklfktvire nislaeapss gidifqyapk sngaedylsl
      241 tkeiinl
//
LOCUS       WP_010664432             158 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Marinilabilia salmonicolor].
ACCESSION   WP_010664432
VERSION     WP_010664432.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..158
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18442
     Region          9..148
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 msrpsnketv kqifteylqk nghrktpery aildeiysre ghfdieslyi fmknknyrvs
       61 ratlyntidl lldcklvikh qfgkniaqfe kafeskqhdh lictncgkvt efcdpsiqiv
      121 ldnasknlef tvahhslyvy gtckecrekq eknqnkns
//
LOCUS       WP_010664480             121 aa            linear   BCT 01-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010664480
VERSION     WP_010664480.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..121
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=13752
     Region          1..118
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mivlfdgfcv lcsgfarwlk rqysgniqlk amqsdggqel lklygysvdn pdevvvvdqq
       61 vsysgasavl yilkhggrls rflyfllrmi pnswikglyr lvannrykwf grrasctviq
      121 d
//
LOCUS       WP_010664490             235 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Marinilabilia
            salmonicolor].
ACCESSION   WP_010664490
VERSION     WP_010664490.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..235
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25939
     Region          1..231
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mfkfqqftvi qenaamkvgt dgvllgawtp vdlqpakild agtgtglval mlaqrtrnam
       61 idaveiddaa cvdarinfea spwndrlnly haslqdfaen sassydlivs nppffsgsmk
      121 necsrkatar hdvsltaedl legvnkllsv dgvfslilpv ydyesfrlka acsgmyeqkr
      181 lmvhpnpgkp akrvlsvwtr kqvnlpiies ldveesrhky tpgfknivsg fylaf
//
LOCUS       WP_010664525             111 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Marinilabilia salmonicolor].
ACCESSION   WP_010664525
VERSION     WP_010664525.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..111
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13047
     Region          13..109
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(14..16,30,47..49)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mpykepkiek lyysigevas ifdvntslir fwekefdiik phknkkgnrl ftqkdidnfh
       61 lifhlvkerg mtlkgaqkkl kenkegtenn fevvkrlkdi rallvdikdn i
//
LOCUS       WP_010664544             270 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide biosynthesis/export family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010664544
VERSION     WP_010664544.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..270
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29936
     Region          54..243
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mytnpdflkk tfnsairiag llliisgaig cqsprkmvyl knasgqdttm vyhqpdkkyr
       61 isyddilfvr iltgnpeisa lynnapttgf stsmtseadq yingftvnee gkiklpvlgs
      121 levkgltlqe vekhiqamad qylidatviv rllnfkvtvl gevtrpgvys hyndnmtile
      181 aigkagdvtd lgdkrnimvi rtvpegrttf eidltqkdlm tspafflkpn dviyvkpsgs
      241 kafqinlptm smilssvtti ivllqyfdnq
//
LOCUS       WP_010664541             207 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Marinilabilia
            salmonicolor].
ACCESSION   WP_010664541
VERSION     WP_010664541.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..207
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23413
     Region          24..192
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mqldintili iiisaisifa fsrpeildkl kfnawqvvhr keyhrilsyg lvhgswmhll
       61 inmfvlwsfg ravlyyfdma fdggtviryl ilfvsaigvs tlstlnkekn nphynavgas
      121 gavsavvfts ilfnpynpil lfgiipipgi ifgvlyiiys kymagknvdn ighdahyyga
      181 iyglifplfy epklalhffn elisfnf
//
LOCUS       WP_010664583             634 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Marinilabilia salmonicolor].
ACCESSION   WP_010664583
VERSION     WP_010664583.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..634
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70543
     Region          72..628
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 myfrfsvfcv llvlatnvla qdffqedpvk lkevrvtsqr lhdygvgatv srpdstlvkl
       61 hrsgslssll sntsgvslkt ygpgglasls irggssshta vlwnglniqs pmnggvnlsv
      121 mpvhffdnve vqhggsgtlf gsgavsgvih lsgddllrke nsleaslskg sfglgsagas
      181 iktgssrfas rlsifgqkad ndfpytntsr ighpeetqtn agvtqygvlq enqwrisdks
      241 llttgfwyqd ydkdlqtlmt srrpdetnqr denfmasvny kyygqkstln vkqglirnkv
      301 lysdpdmadp qadnnslswi neaeykyrlg kyhsvnvgvn ytyelarsdg ymgdiirnrm
      361 aafasgrygl ssgrgavvls freemsdadi qpvvfslgve hplwnsiqlk gnisknyrip
      421 nlndlywked gyakgnpdli aesgwsgdvg vdflfnrgif atrlsaayfa srtediivwl
      481 pqdgskwmpq nkkigetdgi evgveltgtt eksrisarvf ytyvnsmlfs ddeyndrqmv
      541 ytpennvnal vgysrgafya tlsgrftder yydhsntlda ysiwdtslgy kfrfsgvrad
      601 csfkinnitn tdyqvvawya mplrnylfsi dlti
//
LOCUS       WP_010664576             256 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Marinilabilia salmonicolor].
ACCESSION   WP_010664576
VERSION     WP_010664576.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..256
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29517
     Region          1..254
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 midthshiyl pefdqdrhev vekalsagve kilmpnidgq svrpmlavee mypdycysmm
       61 glhptsvkgd feeqlaniqy wlgqryfiai geigidlywd ktwereqrvv frkqaewake
      121 qgipivihvr eafeavfqel dkvcddrlkg vfhsfsgnkd qlhkaleypg fmlgingivt
      181 fknarldevl krapsdrimt etdapylapv pfrgkrnqpa ymkntlekla eiygvtsdem
      241 dlittrnark lfaidh
//
LOCUS       WP_010664608             236 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Marinilabilia salmonicolor].
ACCESSION   WP_010664608
VERSION     WP_010664608.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25842
     Region          3..227
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mdtavihied lkkhyevgtq vvkalngvsl siekgeyvai mgpsgsgkst lmnligaldt
       61 ptsgryilng tdvshmsddq laeirnreig fvfqtfnllp rysaldnvvl pliyagvkke
      121 erydkgrqal dnvglaermt hkpnelsggq rqrvavaral vnkpslilad eptgnldskt
      181 svdimrlfee ihnagntivl vtheediaqh akriirlrdg vvesdeavek ilssev
//
LOCUS       WP_010664644             333 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 5 protein [Marinilabilia salmonicolor].
ACCESSION   WP_010664644
VERSION     WP_010664644.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Schroeder,H.R., Yeager,F.M., Boguslaski,R.C. and Vogelhut,P.O.
  TITLE     Immunoassay for serum thyroxine monitored by chemiluminescence
  JOURNAL   J Immunol Methods 25 (3), 275-282 (1979)
   PUBMED   762437
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..333
                     /product="glycoside hydrolase family 5 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=37985
     Region          47..309
                     /region_name="BglC"
                     /note="Aryl-phospho-beta-D-glucosidase BglC, GH1 family
                     [Carbohydrate transport and metabolism]; COG2730"
                     /db_xref="CDD:442036"
ORIGIN      
        1 mkkrltflcl gllvvslmts aqdnpfsris vegknfvneq gevvvfkgln iadpdrleke
       61 gqwkadifde vaawganivr lpvhpaawre rgqeeylgll dqgiewakaa glyviidwhs
      121 ignlrtglfq nemydtsire tyrfwytisr ryknepaval yeifneptty ngelgtltwg
      181 qwsnimvdvi svirannpha vplvagfnwa ydltpvmnep lpveniayvs hpypqkreqp
      241 wvpqwerdfg fvadnypvia tevgymypdq kgahipclgd etygetltgy ftekgisyvv
      301 wvfdpgwspq likdwdytpt rageffkgvm sgk
//
LOCUS       WP_010664726             377 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 5 protein [Marinilabilia salmonicolor].
ACCESSION   WP_010664726
VERSION     WP_010664726.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Schroeder,H.R., Yeager,F.M., Boguslaski,R.C. and Vogelhut,P.O.
  TITLE     Immunoassay for serum thyroxine monitored by chemiluminescence
  JOURNAL   J Immunol Methods 25 (3), 275-282 (1979)
   PUBMED   762437
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..377
                     /product="glycoside hydrolase family 5 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=43332
     Region          36..369
                     /region_name="BglC"
                     /note="Aryl-phospho-beta-D-glucosidase BglC, GH1 family
                     [Carbohydrate transport and metabolism]; COG2730"
                     /db_xref="CDD:442036"
ORIGIN      
        1 mkyivnlvvl lfvlfqtsgc gvsseskttq ktcseftiqr gvnlshwlsq tdrkgderas
       61 fmneedfkki agfgydhvrl pmdevhlwde egvkdtaafe lvhnaikwsk englriiadl
      121 hvvrshyfna dvrplwndpe aqddfvdmwm qisnelsdyp ndllayelln eavaddsedw
      181 nnlvaktmta lrkkepnrmv vigsnrwqsv ntfdelkipe ndsciilsfh fysphvfthy
      241 qapwsskvgf ydgpvhypgh piheedlagy dssqikslta ddafynreyl eeriqepief
      301 akkrglqlyc gefgcypttp ledrvqwysd vtavfekndi awanwdykgg fgvvdgetge
      361 prikilnalt gykekdn
//
LOCUS       WP_010664799             293 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Marinilabilia
            salmonicolor].
ACCESSION   WP_010664799
VERSION     WP_010664799.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..293
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31044
     Region          1..283
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mshthhhvts grafaigitl nivfvgvevf yglvanssal ladaghnasd vlglffawga
       61 frlanrkpkg kytyglqrst ilssilnavl lfiavffiak daivklddpq pvggtsvmiv
      121 agigvvinti tallfvkgqk hdlnikgafl hmaadaavsv gvvvagllin ttgyqwidpv
      181 vsfviiavvl ygtwglfvds vnlaldavpk niniaevrna lnncpgvqda hdlhvwalst
      241 nqtaisvhlv vpaggsddfl akvqqmlddq fnishatiqv etnvdngiec nha
//
LOCUS       WP_010664850             242 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Marinilabilia salmonicolor].
ACCESSION   WP_010664850
VERSION     WP_010664850.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..242
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26933
     Region          43..240
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mikliyiiil syflaggigf ylinrhkplq varksytkfg vyfiiinllf fsivinplff
       61 kyitfviigg gmmelfslhq sagyknkgif lislliftal syglfnfsll nkelilfsfl
      121 tlsifdsfsq itgqlwgrqk ivpkisphkt wegliggtlv alfsaillnk lfsgpltell
      181 iiatgiivfa fagdlaaswy krifhakdys nlipghggll drfdsllagg awvalsawil
      241 ni
//
LOCUS       WP_010664802             156 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Marinilabilia salmonicolor].
ACCESSION   WP_010664802
VERSION     WP_010664802.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..156
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17398
     Region          1..136
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mnahkeymkm aadlarenvl kgggpfsavi vkdgeviatg cnrvtdkhdp tahaeieair
       61 katkklsthd lsgcsiyasc epcpmclgai ywarldqlff gntrkdaasi gfddefiyhe
      121 lekpidqrsi ptqqivteni khafehwaki ddkqey
//
LOCUS       WP_010664851             260 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010664851
VERSION     WP_010664851.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..260
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26777
     Region          42..259
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mtffstiepi yyllplagli vglfgtilgg gggffflpil tliigapaqt avitslvatl
       61 picivgaamh yrkgnldirt gsafaivgil gafagaaian yiapqllkti fgiyavgigg
      121 lmfmnvkqrp saktnkkgkp mnylkkpayg flagmitgtf gtsgtapvla glfaarlpvk
      181 mvigtslfvl vvntsfaaga hflmgqidlt lvalltagsi pgallgpvil sniktdnses
      241 sikyvyaavm vligilmiia
//
LOCUS       WP_010664861             170 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Marinilabilia salmonicolor].
ACCESSION   WP_010664861
VERSION     WP_010664861.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..170
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19901
     Region          6..>32
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mnkehrgvvt qfdvtknygf ikedltgksy ffqydrneqi lwarqtkelp mtcphkddvv
       61 tfslrtsdnk dhdyqachlt fienptiesi kermargikf ygrisysksr yfindiktgi
      121 ifpviilpee kaltdfnqld tnpimeyfln knnnpsnvfa klkltkenvl
//
LOCUS       WP_010664891             361 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010664891
VERSION     WP_010664891.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..361
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41572
     Region          14..315
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mtpeqitsqf aikgtvegik pfgtglintt ykvktqedeh pnyllqiinh qifqnvpelt
       61 rnikrvtdhl rekleaqgid didrrvltpv etlegegfyk daegqywrmf lfiegarsyd
      121 qltntkqana ggrafgqfqr mvsdlpgdpl ypiipgfhnt emrinnfker vekdpvgrlk
      181 evkeevdflm erseeykkiv qmgkegkipe rivhqdtkfn nvlldendev lcvidldtvm
      241 pgyvcydigd airngantgk eddpdldrvs inmdlyegfi kgflqetkei ltpaeketla
      301 fgaklltyeq avrflddyid gdnyyktesp khnlirtraq ikllksmeen wdamqkiveq
      361 q
//
LOCUS       WP_010665012             105 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Marinilabilia salmonicolor].
ACCESSION   WP_010665012
VERSION     WP_010665012.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..105
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /note="This anti-anti-sigma factor, or anti-sigma factor
                     antagonist, belongs to a family that includes
                     characterized members SpoIIAA, RsbV, RsfA, and RsfB."
                     /calculated_mol_wt=11714
     Region          24..104
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(24,26..28,34,57,59..61,63..65,68..69,91,95..96,98)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            60
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mmdtllkvtr ennkitgtlv dtdrlnatia tgvkeqlnkn fddseicftl slqnikfids
       61 tgigvlisal ktarqhngef yltdvnkevm dllalmkldk vfdfk
//
LOCUS       WP_010664903             502 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010664903
VERSION     WP_010664903.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..502
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56265
     Region          54..345
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mvdigrrkfv ktaavagagl tivpgsvlgr rfghvppsdk lniagigigg mgrnnlrnms
       61 genivalcdv dwnyagktfk dypkaerfkd wrkmfekmgd sidavmvatp dhthagitah
      121 amtlgkhvyt qkplthsvye srllsklakk ygvatqmgnq gnsyvdirrv cewiwsgaig
      181 evtevhawtd rpiwpqglqr pvekmnvpgt ldwdlflgpa kyrpyhssyt pwnwrgwwdf
      241 gtgalgdmac hvldpvfwal klkyptkveg sstlvniesa phaeiveytf paresmpnvn
      301 mpevkvtwyd ggllprrpie lldgevlgkd sgggllfvgt kgkimtsyyg mnptllpysk
      361 mddfeepkpv lrripgseng pwsgaherdw irackepads rletsanfay sgplnemvvm
      421 gvlavrlqgl nrildwdgen mrftnisdsd klkivtkdkf evidgdpkfq reyaefnaks
      481 maeewvkhty rngwslpnmp vd
//
LOCUS       WP_010665036             284 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF3822 family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010665036
VERSION     WP_010665036.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19234307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..284
                     /product="DUF3822 family protein"
                     /calculated_mol_wt=32429
     Region          20..281
                     /region_name="ASKHA_ATPase_BT3980-like"
                     /note="ATPase-like domain of DUF3822 family proteins;
                     cd24013"
                     /db_xref="CDD:466863"
ORIGIN      
        1 mipdlsvvde tydttitssy flsiqasldg fsfctldpvr nkyvqfrhfa fknltpeelp
       61 eiaeqifrdn ellnlpykkv fvlipspvst lvpsglfqpd eahkwlsfth qipsgndiah
      121 tnmkmadact iftiperlks lfkrqfpepl ffhqyvpmte tklavsrpgn sksqviinvq
      181 nrffdlvvle knnlrlcntf eingeddliy ftlfvfeqlq ispstaevlf ighhpssdai
      241 kqklgkylkh ikqpglpsgf qysylfrdip ghqfhnlfsl agcv
//
LOCUS       WP_010665037             179 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmD family RNA methyltransferase [Marinilabilia salmonicolor].
ACCESSION   WP_010665037
VERSION     WP_010665037.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002368
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..179
                     /product="RsmD family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0031167 - rRNA methylation [Evidence IEA]"
                     /calculated_mol_wt=20220
     Region          1..179
                     /region_name="RsmD"
                     /note="16S rRNA G966 N2-methylase RsmD [Translation,
                     ribosomal structure and biogenesis]; COG0742"
                     /db_xref="CDD:440505"
ORIGIN      
        1 mrvvsgklkg rrfsppasfk arpttdqare slfnilnnli sfedqevldl fggtgaisye
       61 fasrraisvt tveksfphfk fikttseafg lsgiikivka dvfkylqken kayslifadp
      121 pfslphlkel psiiikskal qssgifileh gpdnnfedhp nfwqqrnygk vnfsffqhk
//
LOCUS       WP_010665089             351 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010665089
VERSION     WP_010665089.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..351
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39698
     Region          4..258
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mvtsdkirfa ivglgrigkr haamiqenpe aelcavcdvr sadetgwedg dipyfndysr
       61 mldaledchv vnictpnglh asqavkaleq rkhvvvekpm altrleaesi ihkalqvsrq
      121 vftvmqnrys ppsvwlkevm ekkllgqiyf vqlncfwnrd dryyknngwh gtaeldggtl
      181 ftqfshfidi lywlfgdvtd ihadfndfah qhstdfedsg svmfnfvngg mgninfstav
      241 wdrnlestit iigekgtikv agqymnevve cnvrdyqmpa lqpsapandy ggykgsaanh
      301 hfiidnviqt lrektfvttn aleglkvvdi ieriyhhrkn ksfkayvsat n
//
LOCUS       WP_010665105             306 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010665105
VERSION     WP_010665105.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..306
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34186
     Region          13..293
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mnelftsafw skllessidw ainelpglii liialtvmlr vvtfsvsrlk killkraand
       61 qstdsletek rintltgiil gavriilftv fiimmlskfs idvgpliasa gilglaigfg
      121 aqelvrdyis gffmlledqi rtgdvaiing tgglvekiel rtislrdfng tvhifqngki
      181 stlanmtkew samvfdigva ykedvdqvmq imkdvgddlq ndpefgtnil epieifgldk
      241 fadsalvika rlktrpitqw stgreyrrrl kiafdkqnie ipfphttvyw geeinplkls
      301 vdqkgk
//
LOCUS       WP_010665112             453 aa            linear   BCT 01-JAN-2025
DEFINITION  S41 family peptidase [Marinilabilia salmonicolor].
ACCESSION   WP_010665112
VERSION     WP_010665112.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..453
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52441
     Region          <135..443
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mkiflfevvi cflflscssn vfvreqyisy eekqdtvltg eridlfinri kkyhpysfds
       61 lggrgideli ekigksfptq kmndaelvfq arklmdfinh edphfriipv frkfpelkyk
      121 tasitvppfr glcindsllv yspydeglkr gdliksindi pvkeylhyyy rdryvdvgnl
      181 vwyfnyrvyp rykidfirnd eensviiegm pypnylvkgg pfcegkiipg yslgyfkire
      241 fennryilkk frklvdemte kgysdliidl rentggsgnd lnlffsffsd kdslhylkna
      301 karvskitkd ygfdesqygq vlslpsekvf hsfaldsslf vpnlkvyvli srttgsiaas
      361 fanicqyngi gtlvgeqlap nalkygevas gefldnpfaf stiqydeytk akdgivrpdi
      421 pipyiareym kggdpvlekl leylkdeklv ffq
//
LOCUS       WP_010665129             218 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Marinilabilia salmonicolor].
ACCESSION   WP_010665129
VERSION     WP_010665129.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..218
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25052
     Region          8..215
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 mkesteiins tiryvkaelt gaegghdwfh tyrvwkmacr isekedcnql vvelaallhd
       61 iadskfndgd eeagprnaaf flselnvage vaehvvkiir hisfkggnhq qefrsteldi
      121 vqdadrldai gaigiartfn yggyknremy npeikpnlnm tkeeyknsta ptinhfyekl
      181 lllkdrmntr tgsaiaeqrh qymerflnef ydewegrl
//
LOCUS       WP_010665151             597 aa            linear   BCT 01-JAN-2025
DEFINITION  V-type ATP synthase subunit A [Marinilabilia salmonicolor].
ACCESSION   WP_010665151
VERSION     WP_010665151.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF003220.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK04192
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..597
                     /product="V-type ATP synthase subunit A"
                     /EC_number="7.1.2.2"
                     /calculated_mol_wt=67093
     Region          6..585
                     /region_name="NtpA"
                     /note="Archaeal/vacuolar-type H+-ATPase catalytic subunit
                     A/Vma1 [Energy production and conversion]; COG1155"
                     /db_xref="CDD:440769"
ORIGIN      
        1 mekndkttgt vsgiianlvv vdvdgpvgqn eicfiahgke rlmaevikvt gdqayvqvfe
       61 strglrpgsk vdfeghmlev tlgpgmlsrn ydglqndldk megvflkrgd ytdplnreqk
      121 wsfkpllekg aeviagdwlg eveenqmphr imvpfklegv ytiksivgeg eytvdeeiav
      181 iedkdgnsvs vnmvqkwpvk vpikthkekp rpfklletgv rcidtlnpit eggtgfipgp
      241 fgtgktvlqh aiskqaeadi viiaacgera nevveifkef pelddprtgr klierttiia
      301 ntsnmpvaar easvytamtl geyyramglk vllmadstsr waqalremsn rleelpgpda
      361 fpmdlsaiis nfysragyvy lnndktgsit figtvspagg nlkepvtent rkaarcfygl
      421 sqdradskry paidpidsys kyleypelqk slqknmgehw ldnvlkakdi lfsgkeadeq
      481 inilgddgvp idfhqrfwka elidfvvlqq dafdkidast plerqkymle kvlniadtaf
      541 efknfeqvgd ffkrlinqlk qmnysefese kfktfekele emlrefavet keeaqav
//
LOCUS       WP_010665185             411 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010665185
VERSION     WP_010665185.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..411
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46843
     Region          24..409
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrskqliliv glvflgltgs iaqsledyfr taaennpglq akyktfeaal qkvpqvsslp
       61 dptftfgyfi spvetrlgpq eakfslsqmf pwfgtlkare daatlaaeak fqefvdarnq
      121 lyyevaaayy plyklsewkq ierenleiln sykeiatrnf engkgamvdv lrvdimlkda
      181 stnleilnqe ekplltrfnk mlnrsaeekv tievvektdt mtvhlnkdsl meqhpvlkkl
      241 elmrqsseae etaarkngyp nlglgldyvv vggptdmqve dsgrdvimpm isvsipifrk
      301 kynsavkeaq lkqeslalqk nqftnnlisk yesvwfdink qeqlirlydq qidetrralk
      361 llttayansg kdfeeilrmq qellkyekkk vdaiskykta varmdyvlga p
//
LOCUS       WP_010665198             271 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Marinilabilia salmonicolor].
ACCESSION   WP_010665198
VERSION     WP_010665198.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..271
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=31215
     Region          1..137
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          169..266
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
ORIGIN      
        1 mrrvllltdf seiarnaaiy alkmfekeqa hfellniydv efsgspyimq vkeemaeesm
       61 rglrkelsll hakfpnarie lasrfgamte vlkkeindye peiiilgckg esalehfllg
      121 staleiikhv hfpmlvvpke arfeapdkia fatdlkdvdi skmvgplthl ikaynsellf
      181 lnvleeeyin rieaeekiaa hfpgiklsfh fidnegdlck silkfmdend atlltlirhh
      241 hsffqrifnp hiikkmvrhp hhpmlilheq g
//
LOCUS       WP_010665217             428 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010665217
VERSION     WP_010665217.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..428
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48247
     Region          7..>44
                     /region_name="DUF1501"
                     /note="Protein of unknown function (DUF1501); cl19855"
                     /db_xref="CDD:473233"
     Region          44..314
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mqdkiqsrre flkkmaltgs vatlaaspwl safaqssaag knpsdrvrla vigtgsrgkq
       61 llrllfeitq ssnleiaalc dvyqphlqet demckeqnmn pvlysnyeel lnkeevdgvi
      121 iatplhqhah itidamnagi hvfceksmar tldttkamyd ahkatgkilq ighqrlfnpv
      181 ylegmqrihn gdlgklgqir aywhrnndwr rpvpnnsiem erfinwrlyk eysaglltel
      241 mshqiqvanw alqktpvsvt gtgsivywkd grevndnval iysyddgtqf vydsmtsnkk
      301 ygleeqimgh kgtiefetnr yytetpppap gilqllndme sgffgkvmig daswvpetav
      361 kyngepiien tdfydtalql eafakyirag kapealireg ynasiwtmlg eiaietgekl
      421 tladkyri
//
LOCUS       WP_010665235             272 aa            linear   BCT 01-JAN-2025
DEFINITION  XRE family transcriptional regulator [Marinilabilia salmonicolor].
ACCESSION   WP_010665235
VERSION     WP_010665235.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..272
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30469
     Region          1..63
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          105..232
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 myfafnlrll rkrkgltqgd lasalgikrp tlnnyenkvs gppldvltsl adyfglsmdt
       61 lvrvdlgklt nfqlkdlegg ndvyvrgsrl rvltstvgpd neenielvpe kakagyltgf
      121 sdpeyisslp vfrlpfldqq kkyrtfqisg dsmlpvpsga witgefildw htikdgdacv
      181 vltrddgisf kiiqneikek gsvkcvslnp lyepydlave eireiwrfvh yispelpqgk
      241 vevehlmrsi shiqsdvgel kehllkggah ea
//
LOCUS       WP_010665307             737 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Marinilabilia salmonicolor].
ACCESSION   WP_010665307
VERSION     WP_010665307.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..737
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=83584
     Region          1..737
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mkkslflisi plmlllfils cqprqreaet rltdyvnpfm gtdgpgntyp gatvpfgmvq
       61 lspdigysgw driagyfypd siitgfshlh ltgtgagdly dilltpvnsr avkttsengn
      121 rpystfshdn ehaepgyyqv flqdyginae ltstqrtgih nytfpkdehs gflldlgysl
      181 nwdrpvmtsi evednqtisg yrmssgwaad qrvwfvakfs kpienttlfl dgeevegrev
      241 kgthtkidlr fstkeqeevm vkvgissagr egalaaiese apqwdfasyr kqasdiwene
      301 lskikvesdn evwkktfytt lyqsmlaptl ysdvngyykg adgeihqaeg yqkydtfslw
      361 dtfraahply timhpdrvpd mvqsllshyr etgllpvwsm qgnetnmmig yhavpvivda
      421 wfkgiggfdp eeafeacksn amsddhgike yrelgyvpls ddhenwsvsk tleyayddwc
      481 iamfakdlgk tedyeyyler asnwknhfdp etgfmrprha dgrfishfdp keytdhfces
      541 ngwhyfwfvp hdieglrdkl gserfshrld smftyepeas ddlpifstgm igqyahgnep
      601 shhvaylyny tgeswktqer vrqiltemyq pepaghcgne dcgqmsawyv lssmgvypvn
      661 padgiyhigs plwrkatisl pgdknftisa pgvsetakyv asvtlngekl snpwihhsdi
      721 vaggtlvlem tdepntn
//
LOCUS       WP_010665327             412 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Marinilabilia salmonicolor].
ACCESSION   WP_010665327
VERSION     WP_010665327.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..412
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44274
     Region          16..399
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 msllliigii ifsgfllgel aarislpkis gyiiagilln pqvlgvvphs fietgdplvn
       61 islavitfhi ggslsfdkir kegknylimt laesllayll vfllvfltvq yvfnlfdsiy
      121 lalafsmlla slaaptdpsa tlavieeyka sgpvsssvlg iaafddimgi ilftlslasa
      181 rilmgggdts mleslghlfy evggavflga afgfllnmls syfkketega livlilailv
      241 tcygtatyig vdellstlal gvvvinynkq rkeifgller yteelifvif ftlsglhldi
      301 sllsgnsvli lvfiaarflg kytgiwasss flptprqvqk ytaggllpqg giviglallv
      361 skeeafrtfs tlimtvvigt aiihelfgpv isklslknag eikderrnee ds
//
LOCUS       WP_010665339             319 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Marinilabilia salmonicolor].
ACCESSION   WP_010665339
VERSION     WP_010665339.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..319
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=34808
     Region          1..317
                     /region_name="PRK14299"
                     /note="chaperone protein DnaJ; Provisional"
                     /db_xref="CDD:237667"
ORIGIN      
        1 mqyknyyktl gvsknatqde ikkayrklav kyhpdknpdd ketenkfkei neayevlkdp
       61 ekrkkydqlg snwkqyenag yggaqgsgfg gfdwsqfggq pgsgrsysfg gdmgdvfgss
      121 ggfsdffnmf fggmggagtt gfggsraakg qdlkadlels vseayhgatr ilnvdgrklr
      181 vnikpgaymg qelrikgkga pgpgggqngd iylrikiqsd tefridgrni ikevpvdfft
      241 aalggkvrvn tpggvvnvti pkgtqpgrtf rlkgkgmpas rqeggfgdll lrlkvtvpdn
      301 lspeeetlvk qwrelrkrk
//
LOCUS       WP_010665406             288 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010665406
VERSION     WP_010665406.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..288
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=31784
     Region          1..276
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mqktiigvdl ggtnmragrv yrdnmeqvak nlvpktdnpe mvyeelrkti kavwtphisg
       61 igigvpgivd yqtgvifdiq nipswkevpl gqmlqeefkv pvyinndanc faagerffga
      121 gkqfddftgl iigtglgagi iknghllqdq ncgsgefgmi pyldhsyehy csgrffehqg
      181 hlsgkeaaql akqnnpkate lfskfghhlg naiktiifav dpaaiilggs vsgsyrffek
      241 tlkeelatfp yarsirnlki ilsqipdiai lgaaalyyeq eqfrnhnq
//
LOCUS       WP_010665477             384 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010665477
VERSION     WP_010665477.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..384
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=44633
     Region          13..177
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mkkvsnnelk qllsngiien idltsndlti pefshnsfkg cilknvtfse nssalklltn
       61 vsfedgklid vcfansilfk vdfrnsslen csfdnnskvl eptitkvnfa kvkmshcrfk
      121 nsvitwsdfr yaeienstfq gatidfcdfy rayfhkinif kksqisnssf nftlfdgnmf
      181 rrenikshri lqeqknkykk fleewkengp girqtddkkh wepdnlqdel demyqhaeni
      241 yrnligswis ngfvidanwa yikakrmerk vlkgmmkrek nvfkksiyff krftngfvdf
      301 afgygesvyk vlrtyvliil lftvflylfi pldnvgtsil wsfknmiaqt pddiknstsf
      361 iillisviqs tlgvlltgif gfim
//
LOCUS       WP_010665489             325 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Marinilabilia salmonicolor].
ACCESSION   WP_010665489
VERSION     WP_010665489.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..325
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36426
     Region          80..279
                     /region_name="BD-FAE"
                     /note="pfam20434"
                     /db_xref="CDD:466583"
ORIGIN      
        1 mkklflltll iiiasnvspq psvipvdttf tvhsalnkik niypiarivn eplpdgvtey
       61 rdiayttled teygdrnlhl dlfrpeggkk lpalimihgg gwssgnksme iplarqiasr
      121 gyvtitieyq lspealypaa vhnikaalrw trahakeydi dpekiaisgs saggqlaalv
      181 gltpgvpkfe gdqgykeypt dvqailvvdg smnflaplsl nkprkrnsad vvwldgfyye
      241 kpkvwkeasp lyyagknspp mlflnsgypr fhagqdelig ilsrhfiyne vhtfhvkvhp
      301 fwlfhpwfnp tveymsnfld ktlkk
//
LOCUS       WP_010665530             411 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Marinilabilia salmonicolor].
ACCESSION   WP_010665530
VERSION     WP_010665530.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..411
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46796
     Region          10..411
                     /region_name="YdhJ"
                     /note="HD superfamily phosphohydrolase [General function
                     prediction only]; COG1078"
                     /db_xref="CDD:440696"
ORIGIN      
        1 mktaphynqr kivndpvhgf isipdnilfe liehpyfqrl rrikqlglts lvypgavhtr
       61 fqhtlgafyl mgtavnvlrd kgheisdres isahaailmh dlghgpfsha leqtliesld
      121 hedislllme rlnqhfdgql saaidifkgn tdklflhqlv ssqldvdrld ylkrdsffsg
      181 vsegvigsdr iikmleiknn elvvegkgiy siekflvarr lmywqvylhk talvaekmli
      241 nvlkrakkla lqgkdvpapp fletflknrf ckddfknnlq ilndftmldd ndimgalklw
      301 qknndkvlai lsscildrkl frievadtpf speiidalke kqkdamklss eeldyfvftd
      361 hvsnstyktg geniniiykd gstkdislas dmldhtalsk pvskyilcyp k
//
LOCUS       WP_010665519             406 aa            linear   BCT 01-JAN-2025
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme [Marinilabilia
            salmonicolor].
ACCESSION   WP_010665519
VERSION     WP_010665519.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 406)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..406
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=44698
     Region          4..404
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mafdirkird dfpilhqdvn gkplvyldna attqkplsvi daeagvykti nsnihrgvhh
       61 lsnvcteafe dvrkktadfl nagssdevif trgttesvnl lsssfgetfl gqgdeiilte
      121 mehhsnivpw qllaqrqgvv ikvvpvtdeg eldmqaftel lnektrlvav thisnvlgti
      181 npvkemivla haagvpvmvd gaqaihhvpv dvqkldcdfy vfsghkmyap tgvgvlygkr
      241 kwleqmnpyq gggemidkvs fsgttfndlp ykfeagtpny agviglgaai dylknlgtka
      301 vweyehelfe yavkqmrevp girfvgqaqn htsvisfllg dshpfdvgtl ldklgfalrt
      361 ghhcaqplmd rfgipgtvra sfafyntree tdslvdalkr vammlg
//
LOCUS       WP_010665602             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010665602
VERSION     WP_010665602.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..233
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=25563
     Region          30..227
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mnifmmmqaa gqavaegael aegeekvtid lielvmqggw imiplfllsf iaiyifiery
       61 laikrasred ksfmnrikdy ihegkiesal alcesndnpv srmiakgitr igrplndvnt
      121 aienvgnlev srlekglpvl atvaggapmi gftgtvigmi ksfwemsnag snievdmlag
      181 giytalvttv tglivgiiay faynwlvarv ekvvfkmear tmefmdllne pvr
//
LOCUS       WP_010665626             951 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Marinilabilia salmonicolor].
ACCESSION   WP_010665626
VERSION     WP_010665626.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..951
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=105348
     Region          8..523
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          467..943
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mgnnkttlqr frqqlngilp asrvytdaly tltkgtdagf yrlipdmvik veseyemvgv
       61 lqlcslynip vtfksggtsl sgqtitnsvl idtgdgfsdf kispdgkyas fqsgisggla
      121 narlapyghk lgpspasins ariggivsnn asgasygiry nsyntvesmr mvladgtvld
      181 tgdlesrrcf eethsdmlsq ltalsksaks neavrqkiqh kfelkntcgy gvnslidfed
      241 pidvlqhlmv gsegtlgfis evsfktvrey glkatsmvff kniksaceai lplrgcsvsa
      301 aelmdrnalr svenksgmpp vlktldeevv allvetsaee edllnirmke iekalsffdt
      361 vypvefttdk deynrlwkvr kglftsaaas rpkgtaciie dlafradvlg dalvdlkkli
      421 eefgyegyvi wghlldgnih fvmmpdfnnr sgveryrqfm ealvklvvhk ydgslkaehg
      481 tgrnmapfvr eewgediydl mkkikevvdp rgilnpgvii nddpeihlkn lkplpvahdl
      541 idnciecgfc eincpsrgit ltprqrivay remhrlsleg kdkdrlselk krynydgdat
      601 catdglcela cpvdintgkl ikdlrfdgns stgnkvaswi anhmssvtls grfvlgvvgg
      661 ahrvlgtkvm sgvssflfkv sghriplwnp hmphggpsfs vyesnghdlt edtvvyfptc
      721 inrtmgksvd ygkemtvvek trqllekagf nvvfpeglkn lccgmafdsk gfkeqglrka
      781 reldqallka sqngkypvyc dmspcllrmk etlsseldly epvefilkyf pdrlhfkkln
      841 kkiaihttcs stkmgleskl lqvaqmcaee vivpdevgcc gwagdrgfth pelnasalkp
      901 lrrqlpddve cgystsrtce iglslhsgis yksivylvde atqiykkgfl d
//
LOCUS       WP_010665698             384 aa            linear   BCT 01-JAN-2025
DEFINITION  LptF/LptG family permease [Acetobacter aceti].
ACCESSION   WP_010665698
VERSION     WP_010665698.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Owens,T.W., Taylor,R.J., Pahil,K.S., Bertani,B.R., Ruiz,N.,
            Kruse,A.C. and Kahne,D.
  TITLE     Structural basis of unidirectional export of lipopolysaccharide to
            the cell surface
  JOURNAL   Nature 567 (7749), 550-553 (2019)
   PUBMED   30894747
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..384
                     /product="LptF/LptG family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42010
     Region          10..376
                     /region_name="LptF"
                     /note="Lipopolysaccharide export LptBFGC system, permease
                     protein LptF [Cell wall/membrane/envelope biogenesis, Cell
                     motility]; COG0795"
                     /db_xref="CDD:440558"
ORIGIN      
        1 mrlapfgsyt ryllraylqq vgsilavlwl valtidilpq igplldnasd hpvrvvlwfc
       61 vlrspwlivp lipfatflgv lateylqtrs gtriliwnsg rspleclvpv lllglmlgat
      121 dtmldawagp asmaiqtrdk lgrdgqrldr sqasdfqwis vtdgllrtkv vqvdgvvllr
      181 elsffhfegp eklvellhak earqetgsfl whatdglfwg taeddrsnal itgniltegg
      241 fskafseidl hlpvdtlwls vigmepqyvp faivralasg sahgydpavy rtreqavfad
      301 tllviamavt asvlstvllt gintltnvtk illigyaahs terafvlfge ngalsaflaa
      361 wsvpvllvag tvlflrtyrg aewa
//
LOCUS       WP_010665766             737 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Acetobacter aceti].
ACCESSION   WP_010665766
VERSION     WP_010665766.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..737
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80758
     Region          77..706
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mftpghkhal lcsvftlgfi vsvsplsvfs araatfdltp akslsrvspk ssqtkvsaek
       61 datgqtkiva hadeniivna irlrdrtnpd ttslfrhslg fssysaggvs alpvlngmad
      121 drvativdgm riasacpnhm npalsyvdpd svataqaiag itpvsiggds tggsivverr
      181 dplfaehgkl lvtghvrgdy rsngggsgas gtitvandtw slrytgsyah asnyrtggsn
      241 srqvrstsyl sfnhavtagf hkdnhlasvt fgqqdipyeg fpnqymdmtn nrstyvngky
      301 kgdfdwgnle araywqrvdh vmnmmndkgg htattgmpmn tdsrsvgysl katillapkh
      361 tltlgsefeh nglndwwppl tgsmmmgpnt fhninnghrd rlghyaewna qwlprlstll
      421 gfrsdlimmn tgqiapyswt gmmsmadama aqkfnassrg rtdtnfdvta lvrwhpldsl
      481 sieggyarkt rspnlyerys waqggmatsm igwfgdgngy vgnlnlspev antasftvtw
      541 hdptddgwev kvqpyytyth nyinvvrigs lsnglsqlqf vnhnaqsygi nssararlwk
      601 teaygtgeir anlnwvrgqd lqnhsglyhq mptngtvgly etyqnwtgri ettlvkskst
      661 vdwvrneprt pgyvllglgg syrwrnflld asienicnqk yylplggmsl gdykatgims
      721 plqgmgrsfn vsltasf
//
LOCUS       WP_010665768             186 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2147 domain-containing protein [Acetobacter aceti].
ACCESSION   WP_010665768
VERSION     WP_010665768.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Barison,N., Cendron,L., Loconte,V., Proctor,E.A., Dokholyan,N.V.
            and Zanotti,G.
  TITLE     Protein HP1028 from the human pathogen Helicobacter pylori belongs
            to the lipocalin family
  JOURNAL   Acta Crystallogr D Biol Crystallogr 69 (Pt 8), 1387-1394 (2013)
   PUBMED   23897462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..186
                     /product="DUF2147 domain-containing protein"
                     /calculated_mol_wt=19856
     Region          27..173
                     /region_name="COG4731"
                     /note="Uncharacterized conserved protein, DUF2147 family
                     [Function unknown]"
                     /db_xref="CDD:443765"
ORIGIN      
        1 mkyvtadlpp etpgrslsai tvgkaavrli laafvgfaap avtasvhaae pssaaipqda
       61 simgmwlsek hdgifriapc gdsvcgtlig lsygpkepmp rakdgraecn lvmltgfrpm
      121 eddpgrwegk ildpdagnly haqiwspkpd ilklrgyilv pvfgetqtws ryhgtigpec
      181 rmpanp
//
LOCUS       WP_010665771             266 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Acetobacter aceti].
ACCESSION   WP_010665771
VERSION     WP_010665771.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..266
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=29216
     Region          12..252
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mtlltgrfgr airatgrfal dlvlpptcss cgeevdqphs lcpacfvrmh pigeprcdqc
       61 gvplpasthl grdarcvsce lhpppwskar aayvydegsr dlilslkyad rtqnaiilar
      121 qmnragrdil eradwlipvp vhwrrllerk ynqaallara vsrlssvpvf vdalqrprat
      181 srlasfsaee rakemqdair irprnaetir gkrvvlvddi lttgstaaac tqallsagve
      241 tvcllaaart tpdthddisr pdlsed
//
LOCUS       WP_010665776             337 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ferritin-like domain-containing protein
            [Acetobacter].
ACCESSION   WP_010665776
VERSION     WP_010665776.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter
  ORGANISM  Acetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acetobacter"
                     /db_xref="taxon:434"
     Protein         1..337
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38400
     Region          <51..142
                     /region_name="YhjR"
                     /note="Rubrerythrin, includes spore coat protein YhjR
                     [Inorganic ion transport and metabolism]; COG1633"
                     /db_xref="CDD:441240"
     Region          90..215
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(98,128,131,204,207)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mtaladiytr lpdsiddlpp ppnaeaveqa dyrarhwsss ipgplkpgsp ehkramadmf
       61 retfnpyrps vinwpklepd alrrvtslpi wdiavqtegk arlrmaayar middpdikda
      121 isrnaweenr hkevlsklve aygiemapep pyvepkdvew aylvtgfsec vdsffafgmf
      181 rvaqtsgffp aelietfepv mqeecrhill fanwlawyra vmpawkrpwf elkvlavwgf
      241 liyerlglvh svdangeeht qdnnftvtgt kdmtsqditl adfmqlclte narrfsgydp
      301 rllrpklapn iaktilfvlr lfgrkphdle agapvaa
//
LOCUS       WP_010665786             728 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Acetobacter aceti].
ACCESSION   WP_010665786
VERSION     WP_010665786.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..728
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80273
     Region          46..720
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mpalpgiplf likrvpflsh lrpirqpget rnnafrwlya ptpaalgfav rttvaammal
       61 viamwmeldd pqwaamtvwi vaqgsrgesl sksrwrivgt aigvimsitl isafpqypwl
      121 ffpalaiwlg vccalatlvh nfrsyalvla gyttaiialg avnnpenvfm vamsratyii
      181 lgitcealla glfahnlaat arsnirtklr saltsvseai ssllegnqaa lirsrtlfgp
      241 llsindqief sevemgphgh egdharaala avsvllsrgl gmtvrlqsld raqpvfdqta
      301 lltrtfletv pprldtdenv elvrhdlsll raecrqrivd alteeiaigd rtakdpripg
      361 lldqrilhna ldellaeldi alaefkasht vipgdhfrfr lqshrdwrea ayngvraaaa
      421 tvasallwei tawptglgfv tfvtlvcglf atrenpvlat tnflkggiwa avvsfflvfl
      481 liprmseyem liaamfipsv agglaarnas talhaaaytl llpnfvhtwn qgrwneigwf
      541 nstgavllgv afavaifrlv lpfnaaderw rmrrtmlqdl rtlaaaqpip ltqdwtgrni
      601 drfarvirha gptpsptieg ylqgtlaamt iglniirlrn vqarnqlppq arqavqatln
      661 rmsqftgkyn rasttarrat ailrqiegre enittrielt raiaylivvs heldanrvfl
      721 daskrfkv
//
LOCUS       WP_010665798             242 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Acetobacter aceti].
ACCESSION   WP_010665798
VERSION     WP_010665798.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..242
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26388
     Region          4..232
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtrdpkliqs veraavilei iaqqggaapl rqiaalagir kttahnilqt lnslgyvrrr
       61 tgdmryylgs rilnlariag ndsatrtklr pvletiahkt dqtvwlavps gdeaayldiv
      121 dfrnpdrasv hapfrekleg savglvflaf ipgmarrlth sltdaatssa ieeieavrar
      181 gyaldlenyh pgihgvaipw rengevlasl cvtgpaaelp qqklvqmawm mmklqtdsvq
      241 pc
//
LOCUS       WP_010665869             264 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acetobacter aceti].
ACCESSION   WP_010665869
VERSION     WP_010665869.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..264
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28741
     Region          1..255
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msdmtslvrv qdaglshdgg knfifrhvdl eieegqfvav lgpsgvgkst llrvimglia
       61 ptegtttlst areqqtgsrr salvfqdarl mpwrtvrgnv elgleglgls rserhqraed
      121 slelvklsae asrwprqlsg gqrqrvgvar altvnpdlll mdepfgalda itrknlqtel
      181 laiwqktrkt vlfvthdide allladriiv lagkpasvrg dlkvgkrprd psspglrala
      241 grlrsliage edpgdtpywq aaei
//
LOCUS       WP_010665879             169 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Acetobacter aceti].
ACCESSION   WP_010665879
VERSION     WP_010665879.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..169
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17721
     Region          <10..165
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          15..44
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          47..77
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(48,52..53,56..58,60..61,65,68,77,79,81,85..86,
                     89..91,93..94,98,101,110,112,114,118..119,122..124,
                     126..127,131,134,143)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          79..110
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          112..143
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mpehegetfd qaeietlfle aardgqtdlv refiaaglsp dvtndkgytp lilaayngra
       61 dtvkqllesg asvdktdakg atalagvafk gdrpiaeili ahgaavdavn svgrtplmfa
      121 vmfgrtdmvr ylleagadpd qkdgegqsar emavaqghpd lltlfgiss
//
LOCUS       WP_010665545             408 aa            linear   BCT 01-JAN-2025
DEFINITION  alanine dehydrogenase [Marinilabilia salmonicolor].
ACCESSION   WP_010665545
VERSION     WP_010665545.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Usha,V., Jayaraman,R., Toro,J.C., Hoffner,S.E. and Das,K.S.
  TITLE     Glycine and alanine dehydrogenase activities are catalyzed by the
            same protein in Mycobacterium smegmatis: upregulation of both
            activities under microaerophilic adaptation
  JOURNAL   Can J Microbiol 48 (1), 7-13 (2002)
   PUBMED   11888165
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Siranosian,K.J., Ireton,K. and Grossman,A.D.
  TITLE     Alanine dehydrogenase (ald) is required for normal sporulation in
            Bacillus subtilis
  JOURNAL   J Bacteriol 175 (21), 6789-6796 (1993)
   PUBMED   8226620
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..408
                     /product="alanine dehydrogenase"
                     /EC_number="1.4.1.1"
                     /GO_function="GO:0000286 - alanine dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0042853 - L-alanine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43903
     Region          35..407
                     /region_name="Ald"
                     /note="Alanine dehydrogenase (includes sporulation protein
                     SpoVN) [Amino acid transport and metabolism]; COG0686"
                     /db_xref="CDD:440450"
ORIGIN      
        1 mgdlgkkasy yfamnqagla pkeelmeigr kqksmsfgip rereegenri pltpqgvell
       61 tangheiive sgagnaanyy dhdfseagak ivtnhedpfr cdvvlkvapp deeergllsp
      121 gqllisllyl asqnrdsiqq lmhkkvnala yellkdesdc ypvvrsmsei egytaimias
      181 eylsnskegk gvllggitgi spaevvviga gtagefavra alglgcqvkv fdnsyrnlre
      241 lernvgqrlf tsvlhpqvls kalrsadavi gsiryfdpqs gflisdeqva gmkpgsiivd
      301 lnmgnggcle avggkggksp vtihhgviyh rvhnlasrva rtssialsni fapvllrlam
      361 aggidqlimq dvgvshglyl ykgiltsyrv gerlnlpskd igllmaaf
//
LOCUS       WP_010665910             130 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Acetobacter].
ACCESSION   WP_010665910
VERSION     WP_010665910.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter
  ORGANISM  Acetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163535
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Acetobacter"
                     /db_xref="taxon:434"
     Protein         1..130
                     /product="VOC family protein"
                     /calculated_mol_wt=14265
     Region          5..128
                     /region_name="GLOD5"
                     /note="Human glyoxalase domain-containing protein 5 and
                     similar proteins; cd07253"
                     /db_xref="CDD:319916"
     Site            order(5..12,29..30,46..50,68..79,84..85,88,97,104..107,
                     116,119..120,122,124,128)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319916"
ORIGIN      
        1 mrftvdrldh vvltvrdiev saswyqrvlg mereeygrhn rtalkfggqk inlrpegmeg
       61 wetaqfascg tndlcfiaav asedviehlk gcgvkvvegp varlgalgpv tsvychdpdq
      121 nlieiasyqg
//
LOCUS       WP_010665940             322 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Acetobacter aceti].
ACCESSION   WP_010665940
VERSION     WP_010665940.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..322
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34677
     Region          84..292
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mtetdlrqfv dpelrplldr lgpasldiss lpearakrqp ppgmkdnlpa lttarlipgm
       61 pdepdvrili iepaavsekl rpamlhihgg gfvmgtpdsm tptlrrwave ldcvivsvdy
      121 rlapehpfpa pledcyaall wlaenasdln idakrigvag esaggglaag lalltrqrgg
      181 palvfqnlqy pmlddrtvla kpdipgcgaf lwtpemnvfg wksylgtepg gegispfaap
      241 arasslhdlp ptyigvgsid lflpedlsya mrlmqagvpv elevfpgafh afeldpragv
      301 tirssvrrld amkramlplc sd
//
LOCUS       WP_010665978             620 aa            linear   BCT 01-JAN-2025
DEFINITION  M3 family oligoendopeptidase [Acetobacter aceti].
ACCESSION   WP_010665978
VERSION     WP_010665978.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..620
                     /product="M3 family oligoendopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=69199
     Region          82..611
                     /region_name="M3B_PepF"
                     /note="Peptidase family M3B, oligopeptidase F (PepF);
                     cd09610"
                     /db_xref="CDD:341073"
     Site            order(414..415,418,441,538,545,549)
                     /site_type="active"
                     /db_xref="CDD:341073"
ORIGIN      
        1 mvdqapfphp harlrplsaq vslsanttss rpstdmsppr wdlsdlytsp dspavkadld
       61 raaaeakafa gqykgtiasl sgadlakaie tcqtineilg kvgsfaslsf sadmtdpetg
      121 kfsqavreci sdisadllff tlelntieed vleaklssss tlahwrpflr dhrmfrphql
      181 pddieqvlle ksvtgasawc rlfdeqital rvsldgremp lgealnqmsd qdrsrreaag
      241 kavgkalegd irlfslvtnt lakdkaisdk mrryprpesy rnvsnmvede vvdalvsavt
      301 ndfprlshry yglkakwlgl dklehwdrna plpgmrekdi pwtdakaivq qayekfdpal
      361 geivseffdk pwidaapvpg kspgafahpv vpsvhpyvlm nyrgrtrdvm tlahelghgv
      421 hqklaakqgy flsstpltla etasvfgeml tfqylldaek dpvqkrllla akvedmlntv
      481 vrqiafyqfe srvhharreg ellpeqigai wrdvqteslg pafnftpeyd tywayvphfv
      541 htpfyvyaya fgdclvnaly gvyqqgkpgf rekyramlea ggtkrhsell apfgldasdp
      601 afwrkgldvi sgfidqlkea
//
LOCUS       WP_010666056             396 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu [Acetobacter aceti].
ACCESSION   WP_010666056
VERSION     WP_010666056.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     gene            1..396
                     /gene="tuf"
     Protein         1..396
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43026
     Region          1..396
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makakfernk phcnigtigh vdhgktslta aitktlaktg gaefkaydmi daapeerarg
       61 itistahvey etakrhyahv dcpghadyvk nmitgaaqmd gailvvsaad gpmpqtrehi
      121 llarqvgvpa lvvflnkvdq vddpellelv emevrellss yqfpgdeipv ikgsalvtle
      181 dgdpeigenr vkdlmdavds yipqperpvd rpflmpiedv fsisgrgtvv tgrvergvvn
      241 tgdeveivgi rpttkttvtg vemfrklldr geagdnigal lrgtkredve rgqvlakpgs
      301 itphkkfkae ayiltkeegg rhtpfftnyr pqfyfrttdv tgvvhlpegt emvmpgdnia
      361 mdveliapia mdeglrfair eggrtvgagv vasite
//
LOCUS       WP_010666180             318 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Acetobacter aceti].
ACCESSION   WP_010666180
VERSION     WP_010666180.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34647
     Region          83..291
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpknvvnpef lpvlakmpsf dglsdrslpe vreifltsvr lmegrpspdv dtreeyvpgl
       61 nkapdvrvlv ysprkaapna pamvyihggg lisghpevdd pkcqilanrl gmhifsvdyr
      121 lapevkypga iedcyavlkw vnenaarlgi nrdkvvvage saggglsaal almardrgey
      181 klacqiliyp mlddrtaikr dpapafgeyv wtrsankyaw qcylgdavgd dktpdyaaag
      241 ratnlaglpp tfigvgsmdl flcedldyat rlmaagvpve vfvvpgayhv fdmfvpdaal
      301 skrfmdaycd vikrtlai
//
LOCUS       WP_010666188             260 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Acetobacter aceti].
ACCESSION   WP_010666188
VERSION     WP_010666188.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..260
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26794
     Region          33..257
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mqtnmshval eilsgvpvgf tlgliggggs ilavplmvyl vgvkdphvai gtsalavavn
       61 alaglvqhar sgtvqwrcaa vfapcgmiga iggawlgkam dgqrllllfa flmigvgvtm
      121 lrgrretdce ktsyapkniv kiasfgagtg llsgffgigg gflivpglma sthmpiinav
      181 stslvavaaf glsaalsyll sgyidwslat ffilggiigt ysgsycakvl ckkgcqltti
      241 fssiiftvav ymiwrgfqtl
//
LOCUS       WP_010666225             349 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Acetobacter aceti].
ACCESSION   WP_010666225
VERSION     WP_010666225.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..349
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38044
     Region          16..346
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mqdtissiqy srhgqaghit ldrpknlnai dramaeaime alaqwqddps vqrilidsss
       61 skafcaggdi kslyrtiqde gpkaahtnmv ipyqamqmia dypkpiitlm dgitmgggig
      121 lgaharyrvv tersvlampe nligltpdag gswllaqapr pyglrlaltg grmagaqavt
      181 mgfadylvss eklealkaal lsdtapedvi lqryaatdlt pladafprti stvydvedmg
      241 pheglpvlls rleasdedwa ktdlttlrsl cpfslhvtwr mqqklhatha scddafalet
      301 qlvlhmisrp dfsegvrarv idkdnaprws patlsevked avehcfkvq
//
LOCUS       WP_010666409             309 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Acetobacter aceti].
ACCESSION   WP_010666409
VERSION     WP_010666409.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..309
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33861
     Region          <36..294
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 msdtdhsnga ngsqktrkgl fsffsrkkdq gvrhsiaalv qeaadagegg dkapeldrqe
       61 ralianvlrl retsaddvmv pradivampa dislddalam mrrenhsrmp vyrgqlddiv
      121 gmihvkdlia yvgtseafnl etllrqplmi apqmpvldll lmmrqrqvhl alvideyggi
      181 dgvvtiedlv etivgdisde hdepsvaliv erpdgsfdvd arcpvetfee qigpiltdse
      241 reaeietigg lvfrlaghvp trgevlnhes gfvfrildad arhirkvrvr kpteiqappa
      301 gtgaenses
//
LOCUS       WP_010666509             337 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acetobacter aceti].
ACCESSION   WP_010666509
VERSION     WP_010666509.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..337
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36309
     Region          7..324
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 magdaplldv rdlcvsfrsg grdvpiienv sftvcereil givgesgsgk svtamaimrl
       61 iddpgvslrg svrfrgqelt tlpqkafrhi rgreiamifq dpmtaftpvy tigwqideai
      121 rvhervskse arartvrllg dmgvpdpert anryphqlsg glrqramiam alscnpalli
      181 adepttaldv tvqaqildll rnlrtdygsa vmlithdmgv vaetcdhvmv lysgrvaerg
      241 pasavfeqpa hpytaallds ippltgprpv rlpsiagapp aplerpsgca faprchyahd
      301 acvtlpplvr faeqdvacvl ptegkalptr llhgaea
//
LOCUS       WP_010666562             104 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Acetobacter aceti].
ACCESSION   WP_010666562
VERSION     WP_010666562.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..104
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11642
     Region          8..98
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mpdttqhvtv vasfhvkeeh ldailpvmta citasrleat nlfytcrrdl ndplhfvfie
       61 qwqsvaaihe hekqphflam kaafekgmeg spmvtmledv safs
//
LOCUS       WP_010666568             401 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Acetobacter].
ACCESSION   WP_010666568
VERSION     WP_010666568.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter
  ORGANISM  Acetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 401)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10588955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Acetobacter"
                     /db_xref="taxon:434"
     Protein         1..401
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43481
     Region          18..206
                     /region_name="AAA_16"
                     /note="AAA ATPase domain; pfam13191"
                     /db_xref="CDD:433025"
     Region          <152..367
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
ORIGIN      
        1 mdpvrnpyvp gagasppela gredlftqag ivlqralagk sarsfiatgl rgvgktvvla
       61 rveqlaksag yltcfveaee ekplgvtlap hlrrmmleld rlgavteqvk rglrvlksfa
      121 sglriqsvlg fsitldvepe hgtadtgdlt idlpdmlsal gqaaqsrhtg valfideiqn
      181 lseadlsali mamhrvmreg lpivlvgagl phlvsligqa ksyaerlfef pvlgplspte
      241 cadalrtpaa renvdftpea vaevvritrg ypyflqeway hawnvahgdh ilkgdidvat
      301 evsltsldgg ffrmryarlt prereycqam aelgegshrs geiaehmgsr tqavapvrat
      361 lirkgmvysp ahgetaftvp lfenylhrir tmgtdpadsd d
//
LOCUS       WP_010666679             301 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Acetobacter aceti].
ACCESSION   WP_010666679
VERSION     WP_010666679.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32835
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 msrptlnelt lfaavathcs frkaadelgv srsslshair sleqtlgvcl lnrttrsval
       61 teagrrlrtg lepvlsgldd aldavadarg apagtlrina nkgaaelflr mivprfmtly
      121 pqveldlvve gqlvdivedg fdagirlaea vpqdmigvpl ggevrfvtva spaylahhas
      181 lqtphdlrlh hcirqrlpgg kryrweftrh genmtfdvpg vltlndsdlm veaagkdlgv
      241 ayvpesfarr lladgrlvtv ldawcppcpg lmlyyprnrh vpsalralin lmketnrkls
      301 g
//
LOCUS       WP_010666709             273 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Acetobacter aceti].
ACCESSION   WP_010666709
VERSION     WP_010666709.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..273
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28770
     Region          7..255
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mtarkklige liaecvavfi iilfgdsvaa mytlydpspy ktaywgvciv wglgvtiaiy
       61 atgavsgtha npavtvalai yrgfswakva pycaaqilgg flgagvvytm fspviehfai
      121 shgldrlhdg aaagvffthp gefvtplhsf vvetiltaml vfgifaitye hntmapeans
      181 galiigllva aigasagyld awainpardf gprlfcyfag wgpqalpspg nywwvpilgp
      241 isggvigagf yrtliqpfmp rpavaassie tsv
//
LOCUS       WP_010666716             750 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Acetobacter aceti].
ACCESSION   WP_010666716
VERSION     WP_010666716.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..750
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82825
     Region          60..736
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mnrpvhpvtf llvaspllfs rhvltpahaa etgtttatpv tahpsaktep vkavtatrde
       61 hiivtahldk qraslqpstg asvyhftrad ieripggdna plnavllqap gvaqdsygqi
      121 hirgdhnevq frldgialpe glsvfgqtlm trfahsmslt tgalpseygf lqagviditt
      181 kngtsdsggn asiyggardy ffpslqyggh ngkwdyfata dfvhnrvgie nptpdfnaih
      241 dlsnqyhflg hlrytadent risfiagvsn aqyelpnnpg qqrqfanpsf lnsalsqqvy
      301 gsvdsaslhe qqkeitdfgm lslqkemgkv slqtsaiary sslgyspdpl gdlvyngiaq
      361 haqrsvfssg nqtdltwraa pkhtvrfgfq ayvertisks datvytqsgt dedgnaefdg
      421 qtqsihdgtg rtgwiyglya qdewrpfknl tinyglrfdg vdeythskqv sprinivwtp
      481 wrggtfhagy sryftpppfe lvggtqldky antsgappnf qntmvkaerd hyfdagfaqe
      541 ilphwhasfd ayvklarnmi degqfgspii lsafnykrgq vngyevttdy shgpftvygn
      601 fswsraigkn ivsaqwnmsp ddlayisnhw vhvdhdqrwt asaggsytaf rktghptrls
      661 atmvygsglr edsvipngas lpqyvtfnlg ivqsfdnlfh tpflkrtelr ldvtnlfdrr
      721 ymlrsgsgig vgapqyglrr tiltgisqrf
//
LOCUS       WP_010666779             382 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Acetobacter aceti].
ACCESSION   WP_010666779
VERSION     WP_010666779.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..382
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40748
     Region          42..376
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 msqsglpphd ddhvhlppcp veditleqrq aarraqwkar eilalaivai ttytihgfls
       61 alawgvvfav atwplyrkiq arwprlaqga llpalctagm allflipmlf vgleaaneaq
      121 nvlglmkhar nagvpvpvwv srlpfganav vkwwnshlsd psaaaeffss fdarglamtk
      181 tvgsqvvhrg tlfffsiltl fflykdgdti mrectvasrr afgrrgelig hqiiasihgt
      241 vaglvlvgvg egiimgviyf ltgvphpvll ggataiaami pfcamipvgl aatlllvdgg
      301 tmsavavfai gavviftadh fvrpgliggs tqlpflwvll givggaetwg llglflgpaa
      361 matlhllwrn wsrergvalp eg
//
LOCUS       WP_010666845             153 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Acetobacter aceti].
ACCESSION   WP_010666845
VERSION     WP_010666845.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..153
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16323
     Region          4..152
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mtdirtriae etktamkagq kervttlrmi gakikdadia argqgkeals ddditstlrs
       61 mvksrqesvk myleggredl aekeqheiev ireflppemd eaalkaavea aiaeagastm
      121 kdmgkvmgal kakfgasldl granglvkaa lsa
//
LOCUS       WP_010666854             458 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Acetobacter aceti].
ACCESSION   WP_010666854
VERSION     WP_010666854.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..458
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=49624
     Region          31..446
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 markaegrgr rrphsrqtpa taidptprry riealgvsgd gigrltdagv qqatpvfipy
       61 tapgdevlar stgkdratiq eicvaaperv tppcslfgtc ggcslqhlsa ewilkwktte
      121 vltglhragv vdlppaasfq tpsasrrrad lavkrkhdgv ilglhrrggd vvdltecsll
      181 hpdivkllpa lrtamerldl frreadlvin lldsgpdlll asdappstad riklaafcks
      241 hcisrlcwke kasqenpeil vqlapsviaf dgvaieppsg aflqasrege tairtavlda
      301 lppstgrkak iielyagcgt ltfglsthar veayeghpga vealtrasag rnitphlrdl
      361 nkqpveakel ssalavvldp phagaglqmd dildarprvi iyvscnpril yrdterllka
      421 gyridaltii dqflwsaete vvcrfshssk krektnnk
//
LOCUS       WP_010666889             133 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Acetobacter].
ACCESSION   WP_010666889
VERSION     WP_010666889.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter
  ORGANISM  Acetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Acetobacter"
                     /db_xref="taxon:434"
     Protein         1..133
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13904
     Region          9..129
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mlsneikeps geltirviam psntnaagdv fggwvmsqmd laagsaagmr aagsktvtva
       61 idgvsflapm avgdelsvyt dilkvgrtsm tigvqawrrv rqsherqlvt hgkfvfvavg
      121 ednrpmeipa aag
//
LOCUS       WP_010666904             417 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA recombination protein RmuC [Acetobacter aceti].
ACCESSION   WP_010666904
VERSION     WP_010666904.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..417
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46002
     Region          87..406
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 miptsagspe tglwigllvc acliiafllf ivlryrstsg gesdsdllar lyvlvereag
       61 vrhaeaeqqr irlaeteral igrveqmrae lmervahlsg algkdqaear amqsealrem
      121 aeasalqlna irgavteqlh aaverqmqts fqrvleqfsa mqkamgevsa mtaqigdlkr
      181 lfgnvktrgg wgeaqlrail edvlppgtfe anrrlgqgre vvefvvrmpv rgsnppvlai
      241 dskfpteaye rlldavaqdd kdaergsrra lentvkmear kiaskyivpp etvefavlyl
      301 ptdglyaeva rapglideig rtyrvlimgp slmpallrti hlgyvtlsle ertdtiarll
      361 gatrqemlkm dgvleklsrn aqsmsstied arqrtrvvar qlrsldttdd ggeevll
//
LOCUS       WP_010666988             263 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Acetobacter aceti].
ACCESSION   WP_010666988
VERSION     WP_010666988.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..263
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29043
     Region          4..259
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mtglidthch ldhfseeemp glldrakefg legmvtigtr lsrqseqkal trysrpdlsi
       61 wcaigthpdh vmeeppmdad aivklaedpe vvaigesgld yfhgaeevrp tqqasfrehv
      121 haarltglpl aihtrqaded masilreete trgafpfllh cfasgpelak talelggyls
      181 fsgivtfpkc qelrdiaasv pldrifvetd spflapvprr gkrnepgyta ytaavvaqtr
      241 gmeeqafiea ttanfhrlft rah
//
LOCUS       WP_010667039             349 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Acetobacter aceti].
ACCESSION   WP_010667039
VERSION     WP_010667039.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..349
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37570
     Region          95..349
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 maessllpga gwltgvaadg adglrgrtmt astgqlsaat piigdfpiss tqesmehasl
       61 svgeaaadrh vddweqggpd ddpavshsrl rlaladigeg lrlwrlavsl gwldiklqfr
      121 gsrvgplwlt lgtavmigsm ggiysnlfhi vlkdylpyla ismilwqigi agvtqdacsc
      181 finaassira trlpfslqal rvlvrnglmf gynivvpigv ylifgllpgp valfavpgll
      241 iwalnafafc lllgsvaary rdippivasi vqvafyvtpi iwsakqlgak gwwlifnpfy
      301 plleivrqpl tgempsisvw svaiglsvll wlsslfvfsr sraqlafwi
//
LOCUS       WP_010667097             165 aa            linear   BCT 01-JAN-2025
DEFINITION  CinA family protein [Acetobacter aceti].
ACCESSION   WP_010667097
VERSION     WP_010667097.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..165
                     /product="CinA family protein"
                     /calculated_mol_wt=16429
     Region          14..161
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mtailpaevl eksatvleql kaaglmvvta esctgglvag altahagssa avaggfvtys
       61 namkqaalgv pedmlaqrga vseqvarsma egalahapga diavsltgva gpdggseakp
      121 vglvwfglkr agkppltqkq ifggnrtevr aqavlhalqm iqdsl
//
LOCUS       WP_010667128             142 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Acetobacter aceti].
ACCESSION   WP_010667128
VERSION     WP_010667128.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..142
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15759
     Region          1..139
                     /region_name="CFF1"
                     /note="Predicted sugar epimerase, cupin superfamily
                     [General function prediction only]; COG3542"
                     /db_xref="CDD:442763"
ORIGIN      
        1 mnaqdiitql glaphpeggw yretwrdrhf ghdergcasl iyyllergqr shwhkidase
       61 iwlhqgggtl rlhtwsggev ttcclgqdla dgevlqacve pgewqaadtd adwvlvscmv
      121 apgfmfsefe mappgwapgh pe
//
LOCUS       WP_010667258             452 aa            linear   BCT 01-JAN-2025
DEFINITION  TldD/PmbA family protein [Acetobacter aceti].
ACCESSION   WP_010667258
VERSION     WP_010667258.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..452
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47341
     Region          12..451
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mtdstptqap ldlacelael arkkgadaad aicvgstslg vsvrngvtde lersettdlg
       61 lrvfvgkrsa iiststldrg rfdglvdqal amahvlpedg yaglpegipl igrltensld
      121 lvdtteptae ellarartte eaghavkgvt nsagasatwg rslvalassa gvagyyertr
      181 nsvsmsalag qgtgmqrdwd fhstvylsdl edsavigeka grnavarlnp tqprtgtmpv
      241 vyaprvsngl lghltgaing aaiargtsfl kekmgqrvfa pgirvlddph rkrglrskpf
      301 dgecvacepl elvadgvlqh wlldcrsarq lglttngras rgtssppspg vsnlyfapgs
      361 vspaeliadi aegvyvtemm gssingltgd ysrgasgfmi rngqlaepia eftvagnlld
      421 mfgrlqvadd lsfrfgsdap tiridamsia gn
//
LOCUS       WP_010667316             419 aa            linear   BCT 01-JAN-2025
DEFINITION  M20 family metallo-hydrolase [Acetobacter aceti].
ACCESSION   WP_010667316
VERSION     WP_010667316.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..419
                     /product="M20 family metallo-hydrolase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45209
     Region          17..411
                     /region_name="M20_bAS"
                     /note="M20 Peptidase beta-alanine synthase, an
                     amidohydrolase; cd03884"
                     /db_xref="CDD:349880"
     Site            order(89,100..101,134..135,142,196,199,219,221,294,
                     362..363,388)
                     /site_type="active"
                     /db_xref="CDD:349880"
     Site            order(199..202,205..206,221,232..236,238,241,245..246,
                     248..250,252..254,256..257,259..260,267..274,278..279,
                     281..284,292,294,361)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349880"
ORIGIN      
        1 msqsvkgsnl rvdgnalwvd lmetaqyggt pkggirrltl tdedrqvrdw fvrtctdlgc
       61 evsfdsmgnl farrpgldna lppitmgshl dtqptggkfd gilgvlggls vlralhnsgy
      121 ttrhpievin wtneegsrfs ppmmcsgvfa gifteaevld krdragirfg deldtigyrg
      181 kepcgqhpis ayfelhieqg pileaedkti givtgiqgar wyevtvrgkd ahagstpmpl
      241 rhdalvasag mimavsevak ahgpsavgtv gllenrpnss nvvpgevfft idirdpddav
      301 vlqmeqelrg klekiaqens veleivqiwd apavhfdkac vgmveeaate hgysarrivs
      361 gpghdagyva kvaptamifv pckdglshne eesilqqdae mganvllaav lkadqtfdq
//
LOCUS       WP_010667319             226 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acetobacter aceti].
ACCESSION   WP_010667319
VERSION     WP_010667319.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23947
     Region          3..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mgetvlalrd itrsyvsgde tlhvlrgvnf elragetval vapsgtgkst llhiaglldh
       61 pdggvievag rdagrlpdkd rtaircseig fvyqfhhlla eftarenval pqmiagtsps
      121 vsrrraeell gvfglghrln hlpgklsgge qqrvaiaral anapsvllad eptgnldvst
      181 adivfdellr vvrgsavgal iathneelaa rmdrvvtlrd gilveg
//
LOCUS       WP_010667322             239 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Acetobacter aceti].
ACCESSION   WP_010667322
VERSION     WP_010667322.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..239
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=26269
     Region          12..202
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mrfcklpgyf allhyldtll shygygvigv vimlesmglp lpaesmlita slysaathkl
       61 siwgiviagv sgaimgdnlg yligrelgfr flhrfgkyig lsadrlllgr yifrqhggmv
      121 vffgrfiavl rvfiallaga nrmhwrafll hnalgglcwa ggyslgayyl ghevmkvsgp
      181 vawgfagiat lagvsvflfl kkneqrliaq ameaakndre ltfgmekell rdgeqqndk
//
LOCUS       WP_010667451             594 aa            linear   BCT 01-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Acetobacter aceti].
ACCESSION   WP_010667451
VERSION     WP_010667451.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..594
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64892
     Region          66..594
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mrpvpfgrpv lgglllsglf slhsalaapa gaeppaggfg nmplpagpgs aqdqfqryqq
       61 rqqdlnmlpp pdnstqilne pkestssthc vevksisieg adhlspgdrh tiiqryagrc
      121 lttgdlnhal ddvngsylaq gnvtsraylp eqslssghlr ivviegkiag flfegieprl
      181 hevaafpgmr dhilnlrdle qgldqmnrlp swsarmkiap gknpgetqvr ilqpapgifh
      241 gqvwadnngq petgretgha mlraddalgl ldmwsveydh slvgdagrrn tqyisangsi
      301 pfgkwtvfgg wwmsndvyhl qsmgedyrfa gkrkdfrfgv srevlrnqig vttlqafyel
      361 ksfsstldrt rletqsarqg svvaqasesl kawggiwyit lgmrfgvrgv gthsnfpdpg
      421 aadphtqyvk ptldidgykp lpfsllwhts ihgeystenq ftsqqlqlgg pytvrgflsq
      481 mlvgndglym rndlsypltg agmsdhcgay rgfcrlfveg tevygildvg mtragyrsnt
      541 lppalkggni agagigfrkt rgpifwmani thsiargplp qegwiagfqa gvrf
//
LOCUS       WP_010667456             253 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acetobacter aceti].
ACCESSION   WP_010667456
VERSION     WP_010667456.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27512
     Region          4..251
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 magidvtnls isfplyhgda rslkktmkga mngkttssrf arddrnrimv qalshinfsl
       61 kpgerlglig rngagkttll ralsgiyepv egrvlvrgrv gtlldtslgm dlelsgreni
      121 rlrglffgls neaireveqd vesfadlgaf mdlplktyss gmslrlafgl ataimpeili
      181 mdewfmagda tfiqraegri aglvegaeil visshmpsiv ekwctrvlwm eqgkivmdgs
      241 padvlpvyld ags
//
LOCUS       WP_010667457             299 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Acetobacter aceti].
ACCESSION   WP_010667457
VERSION     WP_010667457.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..299
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33572
     Region          53..299
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mtseptgvae pitdephvaa elaargdvpv mdlqpergta highalndlf gsfrlfrlgw
       61 tlgwldikmr yrgsllgpfw vtfstiilva amgvlyatll htdlkaylpf lcfslvlway
      121 lsgivtdgcs vftstvnlih sirmpftvhv mrvmvrnllt flhsvgvivv lfvffgimpt
      181 lnwslpagif lwfadlyalt lllgvlgarf rdmppiaani mqilffvtpi lwkpdliymg
      241 rqymlldpcy plieivrgpf mglpvrpsiw laavvysvvl wcvsfllfar lrgrlaywv
//
LOCUS       WP_010667535             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cell division ATP-binding protein FtsE [Acetobacter].
ACCESSION   WP_010667535
VERSION     WP_010667535.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter
  ORGANISM  Acetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Hung,L.W., Wang,I.X., Nikaido,K., Liu,P.Q., Ames,G.F. and Kim,S.H.
  TITLE     Crystal structure of the ATP-binding subunit of an ABC transporter
  JOURNAL   Nature 396 (6712), 703-707 (1998)
   PUBMED   9872322
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Acetobacter"
                     /db_xref="taxon:434"
     Protein         1..224
                     /product="cell division ATP-binding protein FtsE"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=24736
     Region          1..224
                     /region_name="FtsE"
                     /note="Cell division ATPase FtsE [Cell cycle control, cell
                     division, chromosome partitioning]; COG2884"
                     /db_xref="CDD:442130"
ORIGIN      
        1 mirlrdvswh hgtlphegqa tlrnislaip qggfrwllgp sgagkstllr llhmealprs
       61 gdmeilgtei gsrskrstla rlrqrigmih qdfrlmptls vadnialplr lqkrmegeia
      121 qevdalldwl glverkkarp velsggeqqr taiaravimr psllladept naledsqaar
      181 vigmlrelsd lgttvivath ndtlvqrfpa palqlrqgrl fsde
//
LOCUS       WP_010667539             406 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Acetobacter aceti].
ACCESSION   WP_010667539
VERSION     WP_010667539.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..406
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43956
     Region          23..406
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mpsstaassh tstnqksaen sgfsslklnp allarlgkag ledptpiqka aipallsghd
       61 aeilaptgtg ktacyllpll dyllrkkknt aliivptrel arqvtemgtl latrpelepf
      121 avyggtkddp dreydappet arlivatpgr lldmlrterv esascrflvl degdrlmtge
      181 frdemlgila llprdrqtvl vsatgsqetm taagqflykp vriepakdek psirqavlfv
      241 dkaakpaaae allrrhpdrs aivfastrde adlltkqfrk rglkvvglhg gltqparnta
      301 ieafssgkat ilvatdiaar gldveqvgqv inmsppelpd nylhrigrtg ragrmgwaat
      361 lcsaeerktm rkvestlglk lvalpvpals rdttpsrdtp qrsrrr
//
LOCUS       WP_010667594             311 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Acetobacter aceti].
ACCESSION   WP_010667594
VERSION     WP_010667594.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..311
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33638
     Region          1..295
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mrilfitatr lgdavistgl lnyliqahpd arftvvcgpv aaglfqrmpq ldrvivmakr
       61 pydlhwfdlw kqcvgtrwdl vvdlrgsais lllrtrarri mrggrrpgar iahvgdvlsl
      121 sppplpvvwt seedralagt iliendiiaf gptanwagkv wpaqyfvelw sclarifpnr
      181 klavfygpge aersmaapvl aipgaidagg rftlaetaam lqrcalfign dsglmhlaaa
      241 aqtptlglfg psrsseyaps gvhaewiaap gpegaapisg lkpeqvlerl lsmmsgreet
      301 scsslenqel t
//
LOCUS       WP_010667613             264 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Acetobacter aceti].
ACCESSION   WP_010667613
VERSION     WP_010667613.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..264
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28496
     Region          19..259
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 magpdnsgpa icvetvlcae sisksfdsnk vlngvsltve rgdlisiigp sgcgkstflr
       61 clnfleipde gtvtiaddsi rrsggpwkas dealahrlra hvgmvfqsfn lfphrtvldn
      121 vmlaprvvkk vspavaeaea rellakvgle aaclrypvtl sggqqqraai aralamrpdv
      181 mlydeptsal dprvaeevle vmraldregm tqivvthdms faraasdriv fmdggeiiei
      241 gdpdemydnp rdprtrrfll gasa
//
LOCUS       WP_010667663             102 aa            linear   BCT 01-JAN-2025
DEFINITION  HPr family phosphocarrier protein [Acetobacter aceti].
ACCESSION   WP_010667663
VERSION     WP_010667663.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..102
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=10164
     Region          7..94
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 measemmltr avtivnakgl harasakfva eaekwnaevt vtygsevvsa csimglmllg
       61 agvgatitls atgvqageal ealdalvasg fgedtetdaa vs
//
LOCUS       WP_010667725             282 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Acetobacter aceti].
ACCESSION   WP_010667725
VERSION     WP_010667725.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..282
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30492
     Region          203..278
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 msafivtrha gsgdlsfieq eeyrlrlekr renirwgasl lvvtglslgv lwavthmprv
       61 empvdapppa aiaidlaplp aatptpqtdt ppgpqqtqaq pvpepeplpe ltappspapn
      121 ppvplpkmek phpvrkkvkt pivpqklqpv klppalenta ppssaappse aaaaptsaas
      181 ssrashekvt wqgqllaqle rfkrypaeaq skrqegtpll ffsmdrkghv lsarlrkssg
      241 yelldqetla lvrraeplpp ppdsvpgepl mltvpvdfyv he
//
LOCUS       WP_010667782             406 aa            linear   BCT 01-JAN-2025
DEFINITION  YncE family protein [Acetobacter aceti].
ACCESSION   WP_010667782
VERSION     WP_010667782.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..406
                     /product="YncE family protein"
                     /calculated_mol_wt=43183
     Region          8..330
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          137..374
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mtknrfltga avvvlfgaas laparaqtap sqaasdaarl vpaataaavq tipgmppvin
       61 asniysearp gnlnpevakd pariyvpnlr sndvyvidpa tmkvvdrfpv gkspqhvvps
      121 wdlrtlwatn naegttagsl tpidprtgkp gapipvddpy nmyftpdgks aivvaearkr
      181 ldfrdphsmq mqgsveapec rginhagfsi dgryaiftce fggmlakvdt vnrqligylk
      241 lskggmpqdi ltapngktfy vadmhadgvf ivdgdtfket gfiptgvgth giypsrdakf
      301 myvanrgshk vhgprhskeg svsvidfvtn qvvktwpipg ggspdmgnvs edgkllwlsg
      361 rfddvvyaid tttgamtsip vgaephglav wpqpgrysvg htgimr
//
LOCUS       WP_010667741             310 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Acetobacter
            aceti].
ACCESSION   WP_010667741
VERSION     WP_010667741.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..310
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33188
     Region          13..296
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 msesegqtie rrknliawvs lgislvalgl kyaawsvsgs ialksdalet vinvaaaigg
       61 lwaihlaerp addnhtyghy kaeylsaiie samvlvtall iaresyegfv hpqnvgapwf
      121 glalngvata vnlawgltml rigrrirspa lvaggqhvls dvwtgfglva glalipltgw
      181 hwldpaiaal iavnvlrvgw emlrqsvsgl mdeapdsatl aklneviaek avgaleahdi
      241 rirevgaitf iefhlvvpgt mtvavvhdic drieaglrne lgrcvinihv epehkaknsg
      301 ivlahatrcy
//
LOCUS       WP_010667814             544 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Acetobacter aceti].
ACCESSION   WP_010667814
VERSION     WP_010667814.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..544
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60649
     Region          7..544
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mssenlsadv vivgsgvags sianelvrag isvivleagp rvdrqhfven frnlenkpsy
       61 qepfpsvpwa phppdqrtpn eylhttgpda eayqqvylrm iggttwhwag cawrylpsdf
      121 elktrfgqgr dwalkyddle pfyyqaevmm gvcgpdpave dlgsprkqpy pmdalpisya
      181 aqqfrklise ktpwrvvhep qarntrpydn rptceghnnc mpicpigamy ngsysvydae
      241 aagakfipna vvykierdpa nklvtavhyl dpdkgshrvt gkyfviaahc ietaklllva
      301 adeksptgva nssdqvgrnm mdhtgvqvtf isgdkalwpg rgpletnvid nfrdgewrke
      361 rgaylvhmvd dnqvdlatqm aiakgyvgre leerirylaa htvrlfshne alpdpdnrlt
      421 lsktrkdvlg iphpdvyykl peytvrsceh trkvfrelig lmhgtdeqwt pgyfpqdhps
      481 gstimgvdpk dsvvdghcrt hdhenlfias ssvfstvgtg nitltvsala lrvadtlkke
      541 lnha
//
LOCUS       WP_010667971             304 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acetobacter aceti].
ACCESSION   WP_010667971
VERSION     WP_010667971.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=34243
     Region          25..275
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtehqlpdyr tlpadvaerm eqikqrdcvl eidhvgkvfa qkrhqtvale diefgvhrre
       61 fvcvvgpsgc gkstlirila gleetttgri lvdgkpvngp gpdrgmvfqk ytlfpwldvc
      121 rnvmfgiemg gteraearrq amqwlqvvgl ehfatsfphq lsggmqqrva iaralaarpr
      181 vllmdesfsa ldaetrlkmq nylmeiwrki ditivfithd ldeaiyladr ilvlkprpgr
      241 veevievpls rprraaqmms deflatkahl eglirsfgdn aeetdegadd ftmplltlvt
      301 dkae
//
LOCUS       WP_010668040             355 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Acetobacter aceti].
ACCESSION   WP_010668040
VERSION     WP_010668040.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..355
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37598
     Region          4..338
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mnaerlisgl lilgvaygcv vvtapflsai lwaailtfvt wpillrlrry mgpitaavcm
       61 allsticivv piagitskvl tdapqvlsdl tdtflpnlrl ppvppwlskl plagaeatha
      121 wdqagkdlsh igqslrpyag diaqsvlsvl mqlangglhl amalfiafff wlsgdslgrt
      181 irqlisrvag rhadrilriv ggtvrgtvyg llgtaivqgv ltgvgffivr vpepvlfgtl
      241 aaflsvlpig aplvwvpaav wlavsdhlwr giflalygvi lisgadhiir pifiargaql
      301 pylltligvi ggvlefgglg iflgpvllav gyilivefaa grvadlphds ktset
//
LOCUS       WP_010668060             237 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Acetobacter aceti].
ACCESSION   WP_010668060
VERSION     WP_010668060.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..237
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25307
     Region          4..233
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mntssltlvg fgpdgwgkll viaagltlia alcsfaiggl lgtagaalkl sstpilrwig
       61 tfyttvlrgi peilvvylfy fggslalihl mhlagfpgff slpsfvigvi aiglvsgayq
      121 teayrsaylr ldrgqieagk acgmsrpvll wrviapqtlr falpalgniw qsvlketall
      181 siiglvellr qstiasgatr qpllfygtaa llyllmgqlt gfgirsvekr lgrcwer
//
LOCUS       WP_010668105             357 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Acetobacter aceti].
ACCESSION   WP_010668105
VERSION     WP_010668105.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..357
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39182
     Region          4..338
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,224,293,313,315..317)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,172,175,177,224,231,293,313,
                     315..316)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,172,175,177,316)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            177
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mpslfepiel gsiyaknril mapltrargt rehvptpima eyyaqragag liiseatgis
       61 reglgwpyap glwsqeqvea wkpitaavha kggkivaqlw hmgrmvhssv tgqqpvscsa
      121 tkapealhty dgkqapevar pltkediari lndyenaarn alqagfdgvq ihaangylid
      181 eflrdgtnhr sdeyggspen rirflrevte rviatigadk tsvrlspngd tqgcidshpe
      241 qvfvpaakll ndldiaflel repgpngtfg ktdqpklhgp irkvfrkplv lnqdytreea
      301 ietvatgvad aiafgrpfla npdlvhrled nlplnkddir twysqgaegy tdyplaq
//
LOCUS       WP_010668167             112 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF736 domain-containing protein [Acetobacteraceae].
ACCESSION   WP_010668167
VERSION     WP_010668167.1
KEYWORDS    RefSeq.
SOURCE      Acetobacteraceae
  ORGANISM  Acetobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Acetobacteraceae"
                     /db_xref="taxon:433"
     Protein         1..112
                     /product="DUF736 domain-containing protein"
                     /calculated_mol_wt=12215
     Region          1..109
                     /region_name="COG5489"
                     /note="Uncharacterized conserved protein, DUF736 family
                     [Function unknown]"
                     /db_xref="CDD:444240"
ORIGIN      
        1 maqigtftrt adgfagrlrt laldveltiv patssdaeha pdyrvhlgda dagpeigaaw
       61 krtgekagty lslvlddpml aqpiranlfq sdrqgrafhl vwsrpvkrdd rr
//
LOCUS       WP_010668252             213 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Acetobacter aceti].
ACCESSION   WP_010668252
VERSION     WP_010668252.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10136841
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..213
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24209
     Region          40..168
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 msvtietltg esllsvvpdl arlritifre wpylydgnla yeekylhaym qspgtavvva
       61 kdgdrvvgas tclplkdema cirapfeerg lspkdffyfg esvllesyrg qgigvrffee
      121 rerharsasd apfavfcavr rwktdprrpe naqsladfwm krgfmplpgv fchldwkepg
      181 vpgqrdhlld fhikplrgdp ipeallqkdq ded
//
LOCUS       WP_010667522             395 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P) transhydrogenase subunit alpha [Acetobacter aceti].
ACCESSION   WP_010667522
VERSION     WP_010667522.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Bhakta,T., Whitehead,S.J., Snaith,J.S., Dafforn,T.R., Wilkie,J.,
            Rajesh,S., White,S.A. and Jackson,J.B.
  TITLE     Structures of the dI2dIII1 complex of proton-translocating
            transhydrogenase with bound, inactive analogues of NADH and NADPH
            reveal active site geometries
  JOURNAL   Biochemistry 46 (11), 3304-3318 (2007)
   PUBMED   17323922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..395
                     /product="NAD(P) transhydrogenase subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=41107
     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 mslniaaire reqgerrval iplvaqriqh lgcttalete agsasfypda syknttiqsd
       61 vgtllasadi vlavnpptpd miarmrsgsi lisfiygrth pdvvkalqaq kitcfameqi
      121 prisraqamd alssqatlag yyavllgtvh mpkilpmmtt avgslraaqv lvmglgvagl
      181 qalatagrlg avtegydvrp etkeeahslg akfvetgvda tgqggyarel tadekikvkg
      241 vlsdhiarad livttaavpg rkaprlidae qiskmkpgsv iidmgaeggg ncegtvagqs
      301 vqvgptllvg pvnlpsclse qaselyskni lnllqqiikd gklsldmtde viaktlvthd
      361 gkitndavre avegpaptta papppgaapt tgskg
//
LOCUS       WP_010668596             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Acetobacteraceae].
ACCESSION   WP_010668596
VERSION     WP_010668596.1
KEYWORDS    RefSeq.
SOURCE      Acetobacteraceae
  ORGANISM  Acetobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Acetobacteraceae"
                     /db_xref="taxon:433"
     Protein         1..308
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33444
     Region          <17..308
                     /region_name="bifunc_ST_SDO"
                     /note="bifunctional sulfur transferase/dioxygenase Blh;
                     NF040641"
                     /db_xref="CDD:468609"
ORIGIN      
        1 msdsaletai aqvekvergq apapvvrsff deatftathv vhdpatrqaa vidsvldyea
       61 asgrtshtta qkvvdyvrae glevqwqlet hahadhlsaa pwlqaqlggk laigaeivrv
      121 qsvfgkifna gtefardgsq fdrlfhdgdr faiggieaia lhvpghtpad mafvigdaaf
      181 igdtlfmpdy gtaradfpgg earqlfrsir rlmalpdatr vflchdykap grdhfawett
      241 igaerrdnih vhdgvgedaf aamrtardat lslpnlimps vqvnmrggrm pepesngtry
      301 ikipidal
//
LOCUS       WP_010668728             179 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Acetobacter aceti].
ACCESSION   WP_010668728
VERSION     WP_010668728.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..179
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19738
     Region          2..173
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mivlrhcqse fnrlftatrk dpgiadppls ekgekqaeel vqalvgegir hiivspytra
       61 lqtaepiara lnitptinpl ireraafscd igsppaalal nwpeldfsgl demwwssaie
      121 speaveeraa lfraemaasp mwrdtlvvsh wafllaftrs svengswfrl dptvppais
//
LOCUS       WP_010668905             121 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADH-quinone oxidoreductase subunit A [Acetobacter].
ACCESSION   WP_010668905
VERSION     WP_010668905.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter
  ORGANISM  Acetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012780
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Acetobacter"
                     /db_xref="taxon:434"
     Protein         1..121
                     /product="NADH-quinone oxidoreductase subunit A"
                     /EC_number="1.6.5.9"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=13520
     Region          1..121
                     /region_name="PRK06602"
                     /note="NADH:ubiquinone oxidoreductase subunit A;
                     Validated"
                     /db_xref="CDD:180638"
ORIGIN      
        1 mpsvindylp vlifgilavv iagamlgasl vcghqkpyae kltayecgfe afddarrrfd
       61 vrfylvsilf iifdlevafl fpwavslsri gfygflsmmg flgvlgigfl yewrkgaldw
      121 d
//
LOCUS       WP_010669028             357 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Acetobacter aceti].
ACCESSION   WP_010669028
VERSION     WP_010669028.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..357
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39361
     Region          119..329
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlkiemlter lsarkfsgsf trdkpdltsr lllrglhaas qrrrkhrqtl kapqaapvip
       61 htvsaaslay irrltnrpsf pmrlsalplk rvidlrvpga aelrparlyi pygkvrgvvl
      121 flhgggfvhc glnshhgicc rlarasgaav lsfdyslape hkfpaavedv waafnwlase
      181 awrwggavav agdsaggtla avlcqkvrea hrsganpspp apvmqvlyyp atlgreetps
      241 rekfahgyfl tkammewygs qyassdedll npdfapalqk dlsglpsawi mtaecdplrd
      301 egalygrrla eagnvvsytc vrgtlhgflq fypmmrkarw vlhqsgralr avfrark
//
LOCUS       WP_010669078             772 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Acetobacter aceti].
ACCESSION   WP_010669078
VERSION     WP_010669078.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 772)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..772
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84623
     Region          78..757
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mksyflrhss rllatvpayi vlptlpclll astsslaata ttvtgsqpvd akhvaagrtr
       61 tlstqhhpka iahkgeaeqi rvtrsraqrh lstpgtvnvi sgkelrslhl espkdiaaft
      121 pgvtatnavs gsapifsirg vglddyvgtn mggigiyldg vfapfpvfyt gqmldidsva
      181 tekgpqgfdm grsttggsin iqsvkpsdkf ggyaewgyss yntnrgrfai ntpitskisn
      241 rlafnyvngd gwqkdintgk rygaqdllai rnltkfevdd tssvllnlhy trdkgtstsp
      301 qdlgpvskgd tglhpaanav sagntsgqrn enggglsvny tkefnfgtfs sttaidfyrr
      361 ddtdnydgsa lhisdyrwnd taivqshdmh lrmklakifh ltvgvfesyd kidgdytslr
      421 lqsssainln nhfsqqnlst gvyvntvtni tkkldfiasg rfsydergfn ggsrysaias
      481 dsprlfapyy aqvgdaltgv narheyhrft grvglrykia pdtyaygtis ngykagsyfa
      541 apvlaagald yvkpenliay eigiksslfh nklmvegslf dyeyhnrqtl ffapitptan
      601 sltlgtipra rtrggelstt lhnlvpnldl rgsfayldar akspvnying lsldppvtrn
      661 sslpfsprfs wsavtrynin vdryrvtlqa sytwkdnmwa algdnnakts kisslglrme
      721 fgpqtgkwna avyvdnlqnr kgntysftgs dnnriqyiqs prwigcelhy nf
//
LOCUS       WP_010669131              91 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HU family DNA-binding protein [Acetobacteraceae].
ACCESSION   WP_010669131
VERSION     WP_010669131.1
KEYWORDS    RefSeq.
SOURCE      Acetobacteraceae
  ORGANISM  Acetobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Acetobacteraceae"
                     /db_xref="taxon:433"
     Protein         1..91
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9555
     Region          1..91
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mkiadlvdhi atttdtsktd trkvldalve amttaakagd eitlpnfgkf kvrevaareg
       61 rnpatgatiq iaasrklaft pakalkdsln d
//
LOCUS       WP_010669142             454 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Acetobacter aceti].
ACCESSION   WP_010669142
VERSION     WP_010669142.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..454
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49865
     Region          8..421
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mtrsrstfns ifrnvsmltl griltalcsf vymafavral glsdfgllil ihslamtgst
       61 lsrlqtwqtl irfgsdaffd ddmgrfrqvv ffcirldgls avvalaislv vvilyapsvg
      121 wthhertlal lyacvapfmy tgwchgvlrl agkfrlvpit dgftafgkmc gvllayalhl
      181 gvgwflfiwa aavlfdygly tafalsilrk rtsfdyfeaf rhwrwkgegl waftrgvsln
      241 qtlasasthv atlivgkqig taeaavfrvc rqiasgivtp aqlispvlyp elvkmrdrqd
      301 waglrkvtls ifgiliaisa flilltavag shifrallhv hvphtsfyit mmllaaifsl
      361 livpleplli vtgqlrlivr trvlvtllyf palylltrsf hltgaclatl assaavflsc
      421 lagavifsrr lgrsgqpgpe gapdqpepaq eggr
//
LOCUS       WP_010669727             239 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pantoea agglomerans].
ACCESSION   WP_010669727
VERSION     WP_010669727.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..239
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25461
     Region          1..236
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 misllsfgpe gwgrlilsat lttlllsfaa llvgavvgsg vaaaklsphr avrwagegys
       61 vifrgipell viylfyfggs glitqigqlf gadgfieapp fligalaigl isgsyqagvy
      121 raarlalakg eieaavaigm prwrirqril lpqvaryalp glsnvwqmsl kdsalvsvtg
      181 ivelmrasqi aagstrdyfs fylvggacyl lltllsnraf lraesrlgra wqsrtaaqh
//
LOCUS       WP_010669730             210 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Pantoea agglomerans].
ACCESSION   WP_010669730
VERSION     WP_010669730.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..210
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22888
     Region          14..193
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mtrkrysyqp raghglphdp lnaiigprpi gwissvsssg qhnlapysff ncfnyhppii
       61 gfassgwkds vrniaetkef vwnlatrpla eamnessasl padqdefafa gltplaasqv
      121 saslvaespv nfecrltqli qlqdasgnli dswlvlgesv aihideslle egiyqtakae
      181 pilraggpsa yygiseaqrf dlvrpdarrr
//
LOCUS       WP_010669784             209 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TfoX/Sxy family DNA transformation protein [Pantoea].
ACCESSION   WP_010669784
VERSION     WP_010669784.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006898
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..209
                     /product="TfoX/Sxy family DNA transformation protein"
                     /calculated_mol_wt=23474
     Region          1..114
                     /region_name="TfoX"
                     /note="Transcriptional regulator of competence genes,
                     TfoX/Sxy family [Transcription]; COG3070"
                     /db_xref="CDD:442304"
     Region          117..193
                     /region_name="TfoX_C"
                     /note="TfoX C-terminal domain; pfam04994"
                     /db_xref="CDD:461512"
ORIGIN      
        1 mkkvnpvver srarlaplgt iesrtqfggy alavesvvfa linkdelylr aseplreylt
       61 drplqplifr krgklvslny frvdealwrd pdhllalsaa sletaqlelq drqssprlkd
      121 lpnlsvrmem mlyeagvmsv nhlyqmgakq cwlklkainq hvgfqtllal qgaitghhaa
      181 alpqatrael nawfqrtlls npnlrngeg
//
LOCUS       WP_010669883             376 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Pantoea agglomerans].
ACCESSION   WP_010669883
VERSION     WP_010669883.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..376
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42696
     Region          86..352
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 menwlssrrf hslffnqelw lnsaivvvst lviywilrtl irfisnrial ysehrhvrat
       61 ailveilrst sqtlllifsl lialkfvdlp aswsvtiahg wflalivqla lwldcgirlw
      121 lksllrdplh vrnpvttvil gillrvvvwi mmflailsnm ginitalvas lgvggiaial
      181 aiqtvlsdvf aslaigfdkp fehgdfivfg diagsiehig lkttrlrsls geqivcsnti
      241 llqqtihnyk rmqqrrivfk fgisyatpse qvreisplvk eiiqgvettr fdrahflafe
      301 dskltfevvy fvldadynky mdiqqeinlq lmaaleerni rfafpirqve fsggnlppvd
      361 lvavqndgde vrrmtr
//
LOCUS       WP_010669885             699 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pantoea].
ACCESSION   WP_010669885
VERSION     WP_010669885.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..699
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77256
     Region          3..699
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mklslslkgy vplctlalta palsyaadmv vtaqpqedst sptqgylatt sqgatksdrp
       61 littpqsisv vtrqqmqdqg altlnqalgy ssgvftnfgg aatrydtial rgfhggdvdn
      121 tfldgmrlms dggsfnglqv dnafleridv ikgpssalyg qtvpgglvnm vtkrpqfsee
      181 ghiqlqagsn attgtmfdyt naindqwafr ltgvtrnsdt qydhtreeky almpqlmwqp
      241 dedthlilka ylqkdpsggy hgsvpgdgsl tehngyklsn gfyegnsdld qfkrreqiys
      301 fdfahrfndv wsfsstgsys hsnvdldqvy qigwdsvnpd llnryysger sslsawstdn
      361 rlqaefgtge lehrvtlgae yhrykneita aggsanqlna rtgeqvgdmp dytwadktrr
      421 yyqtglylqd emkldrwhld lsgrydriva nnsgsdrrqd dhisgraall yafdngispy
      481 vswsqaitpt altdpnnnll kpttaeqyea gvkyqpvgtr dlysvavydl tqkdvanrdv
      541 ltatytpsgk vhsqgielea rnqltprlst vasytlnhlr fkesvdgndg htpyvtpnsm
      601 aalwghyqfd yglsagagvr yigkqwadne nttrvpsvtl fdasvradlg vwnsslkgaw
      661 vqvnannltd rtyvagcygt gycywgaers vmatvgydf
//
LOCUS       WP_010668104             326 aa            linear   BCT 01-JAN-2025
DEFINITION  retropepsin-like aspartic protease [Acetobacter aceti].
ACCESSION   WP_010668104
VERSION     WP_010668104.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of aspartic peptidases, and those of unknown catalytic
            mechanism
  JOURNAL   Methods Enzymol 248, 105-120 (1995)
   PUBMED   7674916
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Rao,J.K., Erickson,J.W. and Wlodawer,A.
  TITLE     Structural and evolutionary relationships between retroviral and
            eucaryotic aspartic proteinases
  JOURNAL   Biochemistry 30 (19), 4663-4671 (1991)
   PUBMED   1851433
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Davies,D.R.
  TITLE     The structure and function of the aspartic proteinases
  JOURNAL   Annu Rev Biophys Biophys Chem 19, 189-215 (1990)
   PUBMED   2194475
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..326
                     /product="retropepsin-like aspartic protease"
                     /EC_number="3.4.23.-"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34535
     Region          45..140
                     /region_name="Asp_protease_2"
                     /note="Aspartyl protease; pfam13650"
                     /db_xref="CDD:433378"
     Site            order(59,61,63,88..90,135)
                     /site_type="active"
                     /note="inhibitor binding site [active]"
                     /db_xref="CDD:133137"
     Site            59..61
                     /site_type="active"
                     /note="catalytic motif [active]"
                     /db_xref="CDD:133137"
     Site            59
                     /site_type="active"
                     /note="Catalytic residue [active]"
                     /db_xref="CDD:133137"
     Site            order(88..91,95..98)
                     /site_type="active"
                     /note="Active site flap [active]"
                     /db_xref="CDD:133137"
     Region          <182..302
                     /region_name="COG3577"
                     /note="Predicted aspartyl protease [General function
                     prediction only]"
                     /db_xref="CDD:442797"
ORIGIN      
        1 mmrlrslltg lalqafavsa afaapcpltp imeaplrndl gflsapvtva grtvsfivdt
       61 gsegslispw farfmklped pnalthvsgt ggsggvvpnv iipslqvgst gfgpvsmplg
      121 flpsrpnitp pvegllggdv laqdvleida phgrvamwna pgrktdacsv eppflpgvew
      181 qsleaekrgh rivlhvqldg heltalldsg arsrilsrrt aeamglteeq latdpggtta
      241 gvdgkesvyr whkfhsltig qetehnpvlt vspvseqsvd mllgsdwfaa hhvwifyrqg
      301 rifaakipvr pktgsgkpap ngsash
//
LOCUS       WP_010670043             666 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Pantoea agglomerans].
ACCESSION   WP_010670043
VERSION     WP_010670043.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..666
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75144
     Region          21..659
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mnfqwlawdq lpwikanagq wryalrnaia mclalsiaya ldldepywam tsaavisfpt
       61 vggaiskslg rivgslmgas aalliaghtl nepwlftfai agwlalctgi anhyqnnvay
      121 afslagytaa iiafssvnit ditslwtiaq arvcevisgi lcaglmmmvl pstsdgetli
      181 tslkqmharl lehavlllqp sasetirtah envisliltm nllriqafws hyrfrrqnnv
      241 lnyvlhqqlr ltsvlsslrr mllnwtdape alfealqqll aelakpacdk yrlaqilrsv
      301 tpaadgdyrq rafcqrlryf cwmylnvqrw irlldradad trfqpppvpa lardsdsaea
      361 gwsalrtfcv ivlgcafwin tqwssgaaal tltaiacvly asspspggsv tlllktllwl
      421 fafsfvmkfg lmvqisqlwq fllflfpllv tlqlfklqqk qragmwgqfi vfmgsfiavt
      481 npptfdyqdf fndniakvcg vllawlafqi lrpssdarrs rrhiralrla fldqlrqrpr
      541 lsesrfesqi yhrisqlshs rdeqarvwll rwgvvllncs hivwqlrewr agsaalmgfr
      601 dhclqdlqqi issrgvrhss ldrmltelee titallales neaselagii wrlrcslaql
      661 kqavpe
//
LOCUS       WP_010670049             382 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Pantoea agglomerans].
ACCESSION   WP_010670049
VERSION     WP_010670049.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..382
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39174
     Region          6..340
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mrspialalt gfsliavtyg marfswglml paisaeipfn pqqagmlsac sfvaycltil
       61 taaaladryg trltallasl sataglllla casstlllaa glfiaglsag laspalaaav
      121 sdripaagqp rintlinagt sagiiltvvi lsvlpggwra acllfallsl acvlpvmrvl
      181 sghaasrptr vrhwhqrlyr rsmhrlmsia lisglvsaaw wsfgsallrq hvgvdeetar
      241 llwliaggag ivgaatgpva arirlkgvyr lslcgmavpl lvlawsrges tglaiavacc
      301 gagyvtlsgv llvwgarata edpatgvgil ffmlavgqva gsllfgqlya slgastaltl
      361 fafsallllf iapaqnsses gk
//
LOCUS       WP_010670050             179 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator [Pantoea].
ACCESSION   WP_010670050
VERSION     WP_010670050.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..179
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19576
     Region          1..149
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkrndiiqa aerlfythgf hatstdnicr eagvstrtly hhfasrealt aavldareqr
       61 fmadllppqq pdaiahlfrv lgewtaanga rgcfflkawg eyaerdsela aqalafratm
      121 rayitlcvth lrgaenksls daiwilfega ittalitgpa aaqqaaqvvs qllqnratg
//
LOCUS       WP_010670159             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: inositol monophosphatase family protein [Pantoea].
ACCESSION   WP_010670159
VERSION     WP_010670159.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..264
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28209
     Region          8..261
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 meshdeimar lalaeavare ggatalsyfn rretlvvetk ydlqdvvsia dreveqlias
       61 rirdafpadg flgeesglqv gesdytwvvd pidgtspfln gmpswcvsva vlrgdvpvig
      121 vifaptyqec yvaalgqgat lnghrlqvdp trtlqnhvtg fgansyvspq qvgeivaall
      181 saggnfirig sgalmlawva agrvvgyyep ymhawdclag yclvkeaggw yhpfntegdr
      241 itkgaqvlav apgaeadlrr iagl
//
LOCUS       WP_010670150             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fimbrial protein [Pantoea].
ACCESSION   WP_010670150
VERSION     WP_010670150.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..181
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=17930
     Region          10..181
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mntkfrtlnl avlisaglvs asvfaasdnt infqgevtte tcsvsvngnn aspvvllptv
       61 stsdlaasga tagdttftvg vsgcagdsts atkistvfvg nnvsaagnls ntgtaknvev
      121 qildpkdavv nltsgytgsg dltlqtgets gsatysaryy asgtptagtv taslqyavty
      181 q
//
LOCUS       WP_010670160             353 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pantoea].
ACCESSION   WP_010670160
VERSION     WP_010670160.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38173
     Region          5..353
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mttinagsvv fehvakrfag ftavpdlslt vepgtlvtll gpsgcgkttt lrllaglehp
       61 tagriliggk dvthlpaner dvamvfqsya lfphmnaidn ilygllssgm nkreaqdrar
      121 eglklvgles qgqrlpsels ggqqqriava ralvlepqvl lldeplsnld erlrrrvrtd
      181 irdlqqrlgf tavyvthdqe ealavsdkii vmkegdiaqq gapetlyhsp nsvfiadfmg
      241 eanilpceve eadtddalvr lgnqrfrvrg agaktgsaql avrpqfitls gdgqgalqge
      301 vihstwlgdh ieyevatelg alfiidpqme qrlplattvg vnfkpqglal iar
//
LOCUS       WP_010670239             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YoaK family protein [Pantoea].
ACCESSION   WP_010670239
VERSION     WP_010670239.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..243
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25737
     Region          37..228
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mlistesars nsadtrlact laaaagalnt aafeivgffs anmtgnvsll sdhlakanlg
       61 pglfflsivl lfiagsmfst liinaghrrn irtiyafvil iegsalialg vienhfppqs
      121 pgvvlimsls flmglqnavv trisnarvrt thisgtatdi gielamlfev lrrtaspkea
      181 plylsrlrlh cltllsflag giagiglyrl lsydfllpvg fgliclalna iftkpakqqg
      241 ami
//
LOCUS       WP_010670165             607 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Pantoea agglomerans].
ACCESSION   WP_010670165
VERSION     WP_010670165.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..607
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=67932
     Region          20..604
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 menpifhspv rkegfaglgd yaaigegrsv aliapdgsid wwcapnldak plfdrlldag
       61 lggyfqivpr apyqvsrryr dnsnvletrf etrdgtvllt esinstlagr lpwcelarri
      121 egvsgevela itlrfgtaae trspwvadne kgkvfhiaei mamlrtsedi qitelddeqv
      181 catlrtyags rslcallvte keplavpple aidqrietsh tgwtswvesl syegsyptlv
      241 krsalslkfl wysptgalaa aattslpegi ggeknydyry awvrdaclii kafvylgale
      301 dckaafswls qtimrhgvrl racyalngde vpaeryppls gyqnsqpvrv gnnardqlql
      361 smygdmlvta qhfieaghvl dittsrmlge lanccadhwr qkdcgiwelp elqhythskm
      421 acwmaldrav alaesqhiep twlgrwqrer drirdwiesh cwseqqqayl fyagsddrld
      481 aslalvhsyg navnpqrils tyrairqklg dgsamlyrys gvreeestfl acafwlveaw
      541 aeigetdeae qamqeilttl nghgnvdifn emydvrsqsw rgnmpqglsh lalicaaqal
      601 sesqapa
//
LOCUS       WP_010670178             458 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleobase:cation symporter-2 family protein
            [Pantoea].
ACCESSION   WP_010670178
VERSION     WP_010670178.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..458
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47647
     Region          26..441
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mshshekgll yglearigpa paffaalqhl lasvvgiitp pliigsvlgl qayipylism
       61 slfvsglgtf mqarrfygig agmiclqgts faflgvilsg glmvkgrggs peeimamlfg
      121 cnlvaalipi lisrcvgslr kvltpvvtgt vitligisli kvsitdwagg hnatdfgspg
      181 nlalgaltll vivalnrsrn rwarlvavva giavgcvaaa ltghlqlnva pesnwlvlpa
      241 ffrfgfafdw tiflpialvs viavieavgd ltanclisqq pitgkpfqqr lqggivadgl
      301 scvlaavfsa fpnttfaqnn gviqmtgvas ryvgmllgim lallglfpfi gsllqqippp
      361 vlggativmf gsvvaagirv mtqtplgrre mlivaiafgi glgveavpdv lkqfpplins
      421 lfghavttgg ilaivlnmvl pdeapvveev eaetltes
//
LOCUS       WP_010670288             161 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pantoea agglomerans].
ACCESSION   WP_010670288
VERSION     WP_010670288.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..161
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17691
     Region          10..149
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mlvtlilqgi tmikveksdp fsseshrlie mlsaelaait gdngksnftt qamgddkalw
       61 alaknsqgka vgcgairpft qniaelkrmf sdrsesgigg alltfleksa kemgyievrl
      121 etrhinyrav nfymkngyvp ienyglyigr aeaicfskal r
//
LOCUS       WP_010670311             320 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Pantoea agglomerans].
ACCESSION   WP_010670311
VERSION     WP_010670311.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..320
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=34821
     Region          15..304
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mltdarvyay savlmgspil lklfddnqtl agqvfrlikq qenrftvnrg asevmainha
       61 agqhpvvvsq pvfdliacah avsllpdslf nlaigplvkc wkigfqghhv psetelqari
      121 altnphdvil ddasrsvmla rpgmeidlga iakgyiadvv qaflrqqqvs salinlggnv
      181 qtvgappeea gwaiglkkpf geadeligvi gvnnrsvvts giyeryfeld gvcyhhildp
      241 rsgypldndl lsvtvisdrs ldgdiyttll yglgveqgia claeqpgiea ifvtrdrqvi
      301 cssqrhfsfq lldtdyrlvh
//
LOCUS       WP_010670329             140 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Pantoea].
ACCESSION   WP_010670329
VERSION     WP_010670329.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..140
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14948
     Region          29..129
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mnnaitqspr inaglfflrl tgsllllqvh glpkilhfse eltriedpfg lgpmmsllpa
       61 ivaevicpif iilgwgsria clpiiavllv amlvvhpgws laegqfgwll liifttlalt
      121 gpggwrigav khqgvrhgag
//
LOCUS       WP_010670460             477 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Pantoea agglomerans].
ACCESSION   WP_010670460
VERSION     WP_010670460.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..477
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49654
     Region          21..465
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,147,
                     150..151,154,279,282..283,286..288,291,319,323,376..377,
                     381,385,401,404..405,408..409,412)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 maialpdsft prlqhwslal lafaqliysl dinivfvalp eigaglgfse htlqwvvsay
       61 tvccggflll ggraadlmgq rrvfigalwl yalsslaggf awspvvivia ralqgigaal
      121 lfpatlslin rlfeegpsrn ralaiwggag asgltlgsla ggiltsacgw pavffvnvvl
      181 aaiaifaaff vlpkdrfrne rrsfdfpgal tvtvgstllv yalvqgpedg wltgqvllsl
      241 glamvclltf taievgshdp lmpvrlfrnr slvtgmvitf iymgtfgalp yfltvmfqsi
      301 mgysalqtgl sfiipslaif agtqigarla nrlpvrtvll agfltgiagt lalvpaafsd
      361 asyasilpgl visgtgqgiv wtamwiasgs gvthneqgia sgmasttlnv gnavgialli
      421 afsgsggenl qqqtsvssle nalqlafyla aagqvagllv srllprkaat glsaeit
//
LOCUS       WP_010670554             706 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pantoea agglomerans].
ACCESSION   WP_010670554
VERSION     WP_010670554.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..706
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78200
     Region          26..706
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mknkdsrypa rhpalvvaic ssimlpqvna atdsapdmtv tadassegny sasqssvask
       61 mptarideaq svsvvtqqql ddyqasslad amrfvsgvte antlagtedg fvrrgfgsna
      121 dgsiyrdgir ssqglnfdat tervevlkgs ssllygiqnp ggiinvvskk pqyswhssvs
      181 gryaseggga gtldvtgplg ngfafrliae kqnqdywrnf gseehtllap slqwygeqas
      241 flisyadyry dipydrgtaf idgkpidigy kdrlddkanh awghnktlna hydwqfndew
      301 rtrltlgwnq rrydnnevrv tavnassgvv trradanrgf nhktkylswd llgnpeilgm
      361 qhalvvgtdy emnqtyrahq yqgkvnrqfn yftpeydlls pvtdastens aaannlnrih
      421 srslyakdsi slspdwivvl ggryqhyeqr asrgfnpqve tlndegnkfl pqagliyklt
      481 pdlsfytsvs ksftpstdvd degnvgkpeq gtswevgskw qlspklfatv alyridekam
      541 slningstra idkarstgae felngeiapg wdlsanysyd qaeivndrvn pdnngnrlqn
      601 aprhagalyl shemqisslp gsfrlgggar yvgsragdpd nsftlpdyvv adsfvawnnr
      661 lfgektqlrl ninnlfnqhy ysssggnlrv regetrnlmv qarvef
//
LOCUS       WP_010670599            1020 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pantoea agglomerans].
ACCESSION   WP_010670599
VERSION     WP_010670599.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..1020
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112414
     Region          1..1015
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mriqehfldk piriwmvill lgvggiyall nigrledplf tiksavivth ypgasaqqve
       61 eevtlplena lqrlpsldnv tsisgnglsq itvnihtryl adqlpqiwde lrrrvgdaar
      121 qfppgvqapl vnddfgdvyg yffvihgkdf tnselrnyad qlrrdlvlvp gvakvavagv
      181 eqeeirials askmtaygmt pqrvadllsr nnsvasagtl rvdsesirfh ptgelqtldd
      241 lanlpilpag npqnvhlrdi atltrgvtdn paniyfadge aalaigisfa pgvnvidvgd
      301 alsarmahyq qdtpagislk vfynqahevk qsvdgfilnf lmalaivvgt lllfmglrsg
      361 mviaaslaln vlgtllimyl fklelqrvsl galiislsml vdnaivvveg vkidhqrghp
      421 lqqaiarmvr rtalpllgat viailafapi glsqdstgey ckslfqvlli slmlswvtal
      481 tltpvfinws ekrrstaqpe qtepstpyqg ivfrlyrqal ggllrfrltt ltvmvallal
      541 slygftlvkq nffpssstpv fftdlwlpyg tdihytanta adiarfinqd pevaatvttv
      601 gqgalrftlt ydaarqysnf aqimvrvkdg rqldalalkt eayieqnfpq vnqrikriqf
      661 gsasdsaial rvigpdpevl rhigsqldai fladgstfpv rndwqerskv irpvysalrg
      721 qelgidkrdi dqalrmnfsg davgifrdgs rlmpvmlypa deerqsvdhi eniqlwsaal
      781 qhfvplsnvi sdfrlewenp limrrdrtrv ltvqtdpdpa sgltsaqvva rvqpqidqlk
      841 lpagyrlewg gelessreaq sgllsslpvg flamfiitml mfnslrdava iwitvplali
      901 gvtcgflftg ipfgfmalig llslsgmlir ngivlieeir lfrqekslql aiidaatsrl
      961 rpilltaftt vlgllpllrd vffqsmavvi ifglgfatvl tllvlpviyr cfhgreahge
//
LOCUS       WP_010670613             248 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Pantoea agglomerans].
ACCESSION   WP_010670613
VERSION     WP_010670613.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..248
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26179
     Region          3..197
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mkigvigtgn iggtlarkls eaghkvkian srgvdgvrgf ageinaeptd irgavtdvea
       61 vilsiplpal sslpdglfdh lpshvpvidt snyypglrda pitaldngqt esewvqeqig
      121 hpvvkafnni ladsladlgq pqgsrgrlav avagdhpdav qtamslvndt gfdpvfsgti
      181 aeswrqqpct pcyccdweap vmlralalar kgegqarlpq lyasfatlgd apshqdiien
      241 nrainwpv
//
LOCUS       WP_010670627             187 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pantoea agglomerans].
ACCESSION   WP_010670627
VERSION     WP_010670627.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..187
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20524
     Region          4..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msvntreail qaarkiaqsq gynglnfrdl aqdvgikaas iyyyfpgkae lgiavarryw
       61 edgalalemi esespspida lrrfpeifrr sleaenrlcl gsfmgaekdt lppemnaeiq
      121 kfadvniawl nkllvaakvc dsgesesrar aiftaiagaq liarsrsdis lfdslvdsyr
      181 afgplpe
//
LOCUS       WP_010670628             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein [Pantoea].
ACCESSION   WP_010670628
VERSION     WP_010670628.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..233
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26421
     Region          5..226
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtaklqlfts psafpnpqrl rlfmhekgia dqfaetiydm spggeqrgwr hlnmnpwget
       61 ptleladgsy isetaaivry ldqeypgrki mgetaleqgl dnmwdnrvwv hilyrivtaf
      121 hvlhtglgfk leltkneawg ehcrkealah aalvnrhlsd grewllggda ptfsditlat
      181 aiafskfpvn atplderfef ldaywqrwtk rpafqaayad rnsgipelds par
//
LOCUS       WP_010670635             300 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pantoea agglomerans].
ACCESSION   WP_010670635
VERSION     WP_010670635.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32792
     Region          1..60
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          88..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(105..106,108..109,112,116,118..124,217..219,
                     222..224,230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mddvaiflav frgqgfraaa ktlglapstv seritalevs lgvplfirtt rsvtpteagr
       61 mladrmapll semrsvmndv assqrevrgl lrlnvtgavm vdilpplleq fldrhpllrv
      121 eimvddrlvd ataegcdagi rygehlards vavpvgprrq rlalaaapdy lasrglpvhp
      181 talaehhcir lkyssgalip weferngetv svnpagrlti gvngasgaie lakkgqgiia
      241 vfenwlqpcf ttgelqpvlp dwwpefegpw lyfpsrfmsa plrafvdflk evqsmpepld
//
LOCUS       WP_010670658             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [Pantoea].
ACCESSION   WP_010670658
VERSION     WP_010670658.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..247
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26314
     Region          5..244
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mnylqqktai itgassgiga atarelarhg vnivaaaldq ngldtlvrqi eaeggravgl
       61 vtdvtrleet qalvkfasdt fgsidilinn aglmlfssws dvaweewnkm vdvnikgyln
      121 aiasvlpvml kknegqilnm asvaghqvda gagvysatkf fvhamtesmr kdlgvnngir
      181 vntispgvin tgwadkvgdp qgrkvaqeln klaispqdva navvyalnqp qnvtvndliv
      241 sptrqnw
//
LOCUS       WP_010670684             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator [Pantoea].
ACCESSION   WP_010670684
VERSION     WP_010670684.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..182
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19838
     Region          5..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkvskeqvre nrnrivetas elfrergydg vgvaelmsaa glthggfykh fgskadllae
       61 amncgfaqsa ektqgvsrek fveyylsrqh rddmakgcvm salgtdaarq sesiretfaa
      121 gierqlavle teqvtradli ntlaqlvgal mlsracpdns gladeilevc rtrlispdac
      181 kd
//
LOCUS       WP_010670724             322 aa            linear   BCT 01-JAN-2025
DEFINITION  HesA/MoeB/ThiF family protein [Pantoea agglomerans].
ACCESSION   WP_010670724
VERSION     WP_010670724.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..322
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34247
     Region          1..237
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 meryqrqtml peigeagqqr lsrakvlvvg agglsatllp llagagvgfi rlydsdrvel
       61 hnlhrqtlfg vddvgqqkvf caqralaqrn pdcrveahph alsasqlpqa legidlvvga
      121 adnfaityql sdacypaglp licasvlgrk gyvggfcgga pgyralfpkl ptasgncnta
      181 gvmgpavatl gamqaqmals vllkltpspl gcmihcdfvd whirqfrfdd apepdapgtp
      241 fidramlmed dcivelrsle eapvsvadrv vrilpqqlva wqppvdqrvv lvcasgmraa
      301 qaaenlaarg itrlalvaan tl
//
LOCUS       WP_010670742             344 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methionine ABC transporter ATP-binding protein
            [Pantoea].
ACCESSION   WP_010670742
VERSION     WP_010670742.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..344
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37799
     Region          6..338
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 msqvaiafrh vsktfarnga evqalkeinl rinqgdifgv igtsgagkst llrlinhlet
       61 pttgsvevqg ealqgiskkr liqvkkqigm ifqhfnllna rtvfhnvaip lilqgrdkdf
      121 iatrvaella fvnlsdkahs ypdelsggqk qrvgiarala tnpaillcde atsaldpqtt
      181 vqillllqei nqrygitivl ithemsvvqk icnrmavmeq griveqgdvl slfaepqqsv
      241 sasfvqsvih drlpqqtlal lsqhpavdvl rlefvgstaq qpiinrlire hevevnilfa
      301 smtevqrtil gfmivqikge parreaaiqf liatgvkisd vrtl
//
LOCUS       WP_010670747             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methionine ABC transporter ATP-binding protein
            [Pantoea].
ACCESSION   WP_010670747
VERSION     WP_010670747.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..262
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=28398
     Region          1..>254
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 miklshlskq ypgasapald disltieegt ifgilgrsga gkstllrcln rlesptsgli
       61 eidgqdlaam slaqlrqqrq qmgmifqhfn llhsrnvqdn vdlaleiagv paaerrerva
      121 sllklvglas faaawpsqls ggqkqrvgia ralaarpryl lcdeatsald petttsildl
      181 ladiqqqlni tivlithema vvkricdgaa llengqlves gslsqimgre egrlrkmllk
      241 dgeadrafie kyqrealtrc va
//
LOCUS       WP_010670750             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-dependent oxidoreductase [Pantoea].
ACCESSION   WP_010670750
VERSION     WP_010670750.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..200
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=22348
     Region          2..191
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mhalivtshp nqdahthrva dqlaqgiiat ghhtaekaal aaegfdprft lsdhrhfngl
       61 aptppdvlae qqrldradal vlvypvywws fpaqlkgwid rvfiagwafd eqdghlvkrl
      121 ghlpvhlvai gaadtrtflr rgyfasmrnq idhgifdycg apvvtselll sgdegypesh
      181 yqlahqlgqr lfahqekhdr
//
LOCUS       WP_010671076             165 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CinA family protein [Pantoea].
ACCESSION   WP_010671076
VERSION     WP_010671076.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..165
                     /product="CinA family protein"
                     /calculated_mol_wt=17362
     Region          5..159
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 maksldqtae qlgnillssg lhlataesct aglismtlaa vensgdfyts gfvtysenak
       61 irllgvrpdt lkqhtavseq taremvqgac arsgepvgls itgyagpdgg edgtpagtiw
      121 fgwvlpdgrd eaechqfsgd pksvmeqgtq faleglikrl qradr
//
LOCUS       WP_010671107             355 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pantoea agglomerans].
ACCESSION   WP_010671107
VERSION     WP_010671107.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..355
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38700
     Region          1..355
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 maaisltgls kafgaqpvld aislqinqge fvavlgpsgc gkttllrlla gfetldsgei
       61 higerqvaad glhlppeare lgvvfqnyal wphmtvaenv gyslkvngva raerelrttq
      121 altlvgldrf adrrpadlsg gqrqrvalar clvarptlvl ldeplanldv hlratmeeef
      181 rrfhrhsgat llyithdqre amaladrivv lehgrvmqfa spqtlwrepa nemvatfide
      241 grvlpvsdie pldpgqatat lcglrvllrc sphqrplphg kasfhsvsfh laaegerqfa
      301 arveriifrg gyhqinlrpl nqpdvslslt lndaallavd dtvgvavddg wilpa
//
LOCUS       WP_010671117             168 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Pantoea].
ACCESSION   WP_010671117
VERSION     WP_010671117.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..168
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18298
     Region          1..152
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 maaytrlmdg lyllcmliaa valmimvtvi pigifaryvm ngalswpepv aiicmiiftf
       61 igapvglrag thicvsmvtd rlsparqrlm lrvsdllmii tclvifqasy slceamwvqt
      121 laslpavtyg emylpipiga iftllfvver lltgdqsqrp ivtlggth
//
LOCUS       WP_010671118             428 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Pantoea].
ACCESSION   WP_010671118
VERSION     WP_010671118.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..428
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45877
     Region          1..426
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mdaliligsl lvllmvgfpv afavglsafi gawwidlple avviqvtngi nkfslltipf
       61 filagaimae ggiarrlvnf ayifvgfirg glslvnivas tffgaisgss vadtasigsv
      121 mipqmeekgy prdfaaavta sgsvqavltp pshnsviysl atggmvtiss lfvagifpgl
      181 llggclmimc lgfahkrgyp kgeripfrqa lkiffdafwg lftvviimgg ilsgiftase
      241 saaiaciwaf fvtmfiyrdf kwnqlhillf rtiktvtivm vliafaagfg avmtfmqlpt
      301 iiteaftsls dnkyvilmci nilllvvgtl mdmaplilil tpvllpvata lgvdpvhfgm
      361 imltnlgigl itppvgtvlf vasavskqki eqvvramlpf ygmlfivlml ityipaislw
      421 lprlmgvm
//
LOCUS       WP_010671160             333 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pantoea].
ACCESSION   WP_010671160
VERSION     WP_010671160.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..333
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34742
     Region          9..333
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mssketslnl taspwrhqlf dflykwgmll tvviliaafg lasdsflepn niinilrsia
       61 ivtviaigvs isltvggfdl svgstaslan alvislfvwy gfgtttaill tlalctlvgl
      121 fnaflivilr ipdmlatlat lfviqgvamt ysfggsiten mvlpsgdmae gtipaafgll
      181 gqvptiviim lvvtvaaqla lsltkhgrrm yalggnpeaa rlsgirttry rvlayviasl
      241 laglggilla srigssqvna gsgylmdava aawigfslag sgkpnalgtl vgavilgvlq
      301 nglvmlsvpy yamdiikglv lalalaityi qrr
//
LOCUS       WP_010671182             334 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphotransferase enzyme family protein [Pantoea].
ACCESSION   WP_010671182
VERSION     WP_010671182.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..334
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37553
     Region          18..326
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 msakqydnlt dsqltlmaqq alacypaalq gqlsllcrse natfllqaag rryalrlhrg
       61 dyhqkadivs ellwlnalre tgimvpeavp dkegetvltl rlpeggeryv vlfhwidgem
      121 pttdvdpraf qqlgqitarl hqhskqwqpp agfqriiwdh htmtsaeshw grwqdapnln
      181 padhgvveqa isqvgaamtq fgkgsdrygl ihadlrltnl llhkgetrvi dfddcglgwy
      241 lhdlaaaisf vehhprapew idhwirgyeq vahisdaema mlpalliqrr iqltawvgsh
      301 aetemarslg sawashsvrl crrylegeql pvgv
//
LOCUS       WP_010671213             153 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator [Pantoea].
ACCESSION   WP_010671213
VERSION     WP_010671213.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17147
     Region          1..140
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mldktdlkll sllqhdctls lqaladavnl tttpcwkrlk kleddgiira rvalldgdki
       61 glsltafmfv ktqqhsrdwy qafvsvvssm pevmafyrma geydyllriq vadmksydaf
      121 ykrlvngvpg lidvtssfam eeikyttalp vap
//
LOCUS       WP_010671249             299 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pantoea].
ACCESSION   WP_010671249
VERSION     WP_010671249.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33384
     Region          7..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(110..111,113..114,117,121,123..129,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mnnaiynqir ifqsiaregn issaarklei tppsvskalk lleahighpl fvrttrriel
       61 tdagqqlleq tsaavaslek slesirdqnq epsglvritl srfayllvlk pamaafcqqy
      121 pgiqleisvy dgtvniider fdlgirfgdi leggvvarpl mkpfreglya ssaylaafgi
      181 paspsdlhqh rligyrfitn nrilplildh hgeqltvemp gqlmsndiev madgirnglg
      241 igrlfepvhn lqpdkeafip vmerywktyp pvylyypksa gktkrvktli dfllkhtag
//
LOCUS       WP_010671252             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [Pantoea].
ACCESSION   WP_010671252
VERSION     WP_010671252.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..240
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27019
     Region          34..110
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
     Region          138..222
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mnnitaltlt llmagpasaa alteptnrvi nlhemeikag kngqydevar dnitrslaeq
       61 pgtlamyslk hkenahqaym ieiyaseeay qqhlssepyr sfitrapdli gqkkstvlep
      121 qflgdkpfvq nketinnlvi vdvkpadqqa frdivlpema eslkvepgvl amyaatdakn
      181 ryrwffyeiy asdaayqqhr etphfrdyir ltaemtdrke aipvvpallk nrgalnafvn
//
LOCUS       WP_010671259             407 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Pantoea].
ACCESSION   WP_010671259
VERSION     WP_010671259.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..407
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43836
     Region          10..357
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mrfkglnigf fililaiatl gffevlspyf spilwaaila vifhplktyl rvrmgerngl
       61 aalitllcic livftplaii asslvvetna vyhklqtnsa qfpavfadll qhlprwakhy
      121 laennldnae qiqqklssfa lkggqyvags afiigkgtfs ftvgfgvmly llffllkdgs
      181 ylvhlileal plstyvkhhl mvkfaavara tvkgtvvvgi vqgilgglaf wftgidgsll
      241 wgalmaflsl ipavgsaiiw vpaaifffat galwkglflv gffvvivglv dnilrpllvg
      301 kdtkmpdyli liatlggmei ygingfvigp viaalfiacw nllsgrdnre nieaideefi
      361 eegkkqsdta aeaaaeaaaa sadaaaeter kvaalaasek etaekka
//
LOCUS       WP_010671418             299 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Pantoea agglomerans].
ACCESSION   WP_010671418
VERSION     WP_010671418.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..299
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=34974
     Region          63..>114
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 manyfyedvf rraikdlesf ykkeysynik vnysdnlrqh asiigkndns tirfsndcck
       61 qgvndskdlf vallivchel ahylnhhnyf ssiedednrv ieawadnfgs kifmvlityg
      121 vnttnlcktf nvpndageri dligcafekl ctmfynnesk kyhyrmermm hicagissfl
      181 qfywgrfdlq ltidiylrly sssgmykiik adhisfplsn dnfdkvidih fplqnnqpai
      241 tlglkkmyrk yidtafvkdv standykrvf yqtaiaqadn cecpvnmkef feeklkhls
//
LOCUS       WP_010671462             443 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pantoea].
ACCESSION   WP_010671462
VERSION     WP_010671462.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..443
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47461
     Region          23..430
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,82,140..141,143..145,148,168,
                     171..172,175,258,261..262,265..267,270,302,306,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mqasltdtld kqqdptpvns rskvviaslv gtaieffdfy iyataavivf phiffpqgda
       61 tvatlqslat faiafiarpi gsavfghfgd rvgrkatlva slltmgistv vigllpgyet
      121 igvmapllla larfgqglgl ggewggaall atenapakkr alygsfpqlg apigfffang
      181 tflllswllt deqfmqwgwr vpfilsavlv liglyvrvsl hespvfakvq kekkqvrvpi
      241 aallskhlta tilgtfimla tytlfyimtv ysmsygttaa paglgiprns mlwmlmlavi
      301 gfgvmvpiag lladrfgrrk tmititlmii afsflfpaml gsgsqalvma flllglsimg
      361 ltfgpmgall pelfptevry tgasfsynls silgasvapy iatwlnahyg lqavglylas
      421 mavltliall acketrnqtl ydv
//
LOCUS       WP_010671475             300 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pantoea agglomerans].
ACCESSION   WP_010671475
VERSION     WP_010671475.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32553
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..296
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,224,241,275)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdilglistf irvvengsia aaarakgmsp aavsqslsrl eahlgvrlls rttrsmilte
       61 ngkryfekvr hiphdielas qaaanetkpq gplciattaa fgryvlaplm pafkasfpdi
      121 dielistdrn vdhrlegvdv sirieaqlnd qliarkiasl pfifcaapay ldragtpqtp
      181 gelsqhaclv fryptdrrfl pwtfmvngqp vnaklnpsfi sddidiiari avngggiarl
      241 asfvaqplid sgllrplaws ghsgesties lpmniyacvt ersalnskvr tfiefladai
//
LOCUS       WP_010671489             374 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pantoea agglomerans].
ACCESSION   WP_010671489
VERSION     WP_010671489.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..374
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42965
     Region          1..373
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mslihltsla eipaaewdal lpddqpflrh aflltleqsg svrleagwqp dhllwreegv
       61 traalpgyrk ghsqgeyvfd hawadasqra giryypkwlg aipfspvsga rllgetaaaa
      121 qllsalpesl lqqglsgahi nftdaqanql ladqpdwlsr lgcqyhwhnr gyrdfqdfld
      181 slmsrkrkql rkereqvmqs gfefdrylgy qlredqwdfv ytcyantyav rgqrpyltrd
      241 ffsllaermp qnivvviarl qqqpaamafy lrdsnalygr ywgclaefdr lhfetcfyqg
      301 mdlaldeglt rfdagaqgeh klvrgfepqi thswhyllhp glrdavadfl vqeregvrgw
      361 aeeardalpy rrgd
//
LOCUS       WP_010671578             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Pantoea].
ACCESSION   WP_010671578
VERSION     WP_010671578.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..200
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21688
     Region          1..199
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 melslflsml gflwvaaitp gpnnmlltas ganfgfmrti plmigimigm qvmllmvafg
       61 vgglillyps lhlvlkiags lyllwlawki atasyeklet dqapdapmpf wqggllqlin
      121 pkawlmalga vasfslagda yrhsvmaisi gmflvnlvsg viwmgfgami grilrsrraw
      181 kifnlamgll taacvlliwh
//
LOCUS       WP_010671602             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar kinase [Pantoea].
ACCESSION   WP_010671602
VERSION     WP_010671602.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..321
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34648
     Region          14..309
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(45..46,49,101,116,118,147,180,269,272,308)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(238,243,259,269..271,274,296,300)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mtthhtmhhn gpldvvtige amamfiaret gdlaaaetfv kraagaelnv atglarlglk
       61 vgwvsrigdd afgrficqql ekegidharv tvdkryptgf qlkskvddgs dplveyfrkg
      121 saashlsvdd fdadyfgsar hlhlsgvaaa lsesslellk htakemrarg ktisfdpnlr
      181 pvlwrseeem rkqlnllaey adwvlpgeke gliltgyrqp eaiadfyldk gvkavviktg
      241 cdgawyktaq geqgqveaik vdnvvdtvga gdgfavgvis allegqslpq airrgnkigs
      301 maiqvigdse glptrqqlgd v
//
LOCUS       WP_010671617             310 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Pantoea agglomerans].
ACCESSION   WP_010671617
VERSION     WP_010671617.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..310
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34204
     Region          3..293
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mthtvwflil pgvmaldltg paetlklage hftlryigpq pevvcstgmt iggieplpdq
       61 lpagsllvvp gvydsqvcya tpqagearew lmrqhaalra qtfmlvcvcs gallaaqagm
      121 lddvlctthh dviarlkaaa prarvqenrv fvgheniwts agitagidla lhlinqlcdt
      181 qtalavarem vvwfrragdd pqlspwlryr nhmhpaihra qdlmiahpeh gwtltelagr
      241 thvssrhlar lfrqhlgisv reyheqlrvg varqrqqqge saekaalaag fssarqlrra
      301 rqreadqltk
//
LOCUS       WP_010671798             792 aa            linear   BCT 01-JAN-2025
DEFINITION  beta-N-acetylhexosaminidase [Pantoea agglomerans].
ACCESSION   WP_010671798
VERSION     WP_010671798.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 792)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 792)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 792)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 792)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..792
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88006
     Region          19..603
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mwlprsllll llpalspial asplplmpwp qqveqpasgg tliltpqltl qisgdhlaga
       61 earwlerisn qtgwpllpat qpvaaptiri viakavdplp lpdsdesyql qvdgdgillt
      121 apsrfgamrg metllqliqn gaqgttipyv tihdhprfpw rgvlidtarh fmpvetlkrq
      181 idgiaaarmn vfhwhltddq gwrfasshyp qlqqkasdgn yysqqqmrei vkyatdrgvr
      241 vvpeldmpgh asalavampe lisapgpwqm ergwgvfkpl ldpsneqvyq vidtlvgema
      301 aifpdpwlhi ggdevdptqw ndspaiqqfm rdhdlkdaha lqayfnqrve kileahhrqm
      361 vgwdeiahpd lprsiliqsw qgqdalsala kenyrgilst gfyldqpqpa syhyrnevtp
      421 qglngqdrlr pgdqaqswsf tmprlkgspv kgsftliqge pgwrgfidfd gkarrmvsqi
      481 nwlstrqvrf svdswmgpfq pvftlqqnal kgyaevgnvr ypttgqrlaq tpagiapalp
      541 tpeqvqqnll ggeaalwaen insqiidtkl wprafvvaer lwsaqdvtnt dsmysrlaam
      601 drwssvsvgt lqhaqteqqm mrlasghdia plrvlaevle paqyytrqhl kfqaghydyh
      661 eplnrladvl paeseavrql eqqvavlian rnnpaaasav raplqrwqan tsavlpiina
      721 satlkplaqs vqqiealsam glalvnayvr nqafgaseva emratldaaa evqdetvial
      781 vrpletllra fq
//
LOCUS       WP_010671874             162 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DinB family protein [Pantoea].
ACCESSION   WP_010671874
VERSION     WP_010671874.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..162
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18374
     Region          9..149
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 mdkstlvtll kfkrwidaet lkavkgises ayaekrhlml rlmnhihvvd mifranisgq
       61 qhgytalntp etpsvdelei kmddctnwyi rrvssmspad lretikfsfv dggegqmtat
      121 dmlnhmlfhg tyhrgavgwl isecegvppk dvltvflrdh nh
//
LOCUS       WP_010671933             148 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Pantoea].
ACCESSION   WP_010671933
VERSION     WP_010671933.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..148
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16314
     Region          5..129
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 msndtgfthl alqvrdleks vdfyqryagm qvihqrkpgi peaqkvawls dltrpfalvl
       61 vqsdnnedtp lgpfghigva cssreeidek valarlegvl rrdaqqsgvp vgywaffadp
      121 dgntlelsyg qqigleiita rntqslnk
//
LOCUS       WP_010672025             364 aa            linear   BCT 01-JAN-2025
DEFINITION  YncE family protein [Pantoea agglomerans].
ACCESSION   WP_010672025
VERSION     WP_010672025.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..364
                     /product="YncE family protein"
                     /calculated_mol_wt=39465
     Region          <88..273
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          159..192
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          197..235
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          243..280
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          285..323
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mkalfsprta altlamvttf sltacqmpak kvdasapvvm qpsspdnliq relgeglyem
       61 aylpaknaly vasaqgfkdi sggmiyrlda stlqstgagh fdlknfglis apdgsalyat
      121 ntldggiski dpdngkvlkr lmfdeknekg mpygtreifl hdgllyvggv gdpgviwvvd
      181 aktltlktri knagkwvtgi ifspvsdriy aangsgeilv inprnnkieq rltagdgqey
      241 lflnmaedpa tgrlfvtdns kakntlvfde rsgkvikrln lgdslgikfn gkrneiyisq
      301 reskkvlqld gtayevknsw sfdshpnsll vspdgqtlfv tlkqgfnddh ssqgldgvar
      361 itlq
//
LOCUS       WP_010672040             469 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pantoea].
ACCESSION   WP_010672040
VERSION     WP_010672040.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..469
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51783
     Region          38..456
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(48..49,52..53,56,96,146..147,149..151,154,174,
                     177..178,181,292,295..296,299..301,304,331,335,384..385,
                     389,393,409,412..413,416..417,420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mttistslpp mhassaarns laarvdalps saglwrfitl lalggffely dlfetgyist
       61 gllsagvfht gaagvlgfsd qaafasatfl glffgaslla pyadrfgrrl tfmcallwyg
      121 lfsllmafqq saemiilfrf lvgiglgvel vtidtylsew vpthlrsraf afsffvqfls
      181 vpavalmsww lipqtlfsle gwrwvviaga vcslviwlvr rnlpesarwl aqqgrhqeah
      241 qvlstmeqrc gipagpafsa ddaaaqlpkr grfseiwspa yrkrtlmlvv mnffqaigff
      301 gfgnwlpall sgrgatvths llyaffitla yplgslicsr yadklenkwq ivlsslmtvv
      361 fgtlfafqtq pvllilcgfl itwsnawltf sfhayqteif pthiraravg fcysfsrlst
      421 vfssiligvi lqyagtpgvi tfivlsmvmv mlsvgiygpk trgidleni
//
LOCUS       WP_010672052             449 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Pantoea].
ACCESSION   WP_010672052
VERSION     WP_010672052.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..449
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45990
     Region          9..444
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mstesrpasg kldawfsisa rgssvrqeil aglttflamv ysvivvpgml gkagfpptav
       61 fvatclvasf gsiimglwan lpmaigcais ltaftafslv lgqhisvpva lgavflmgll
      121 ftlisvtgir awilrnlpmg vahgtgvgig lfllliaadg vglivknpap glpvalghft
      181 tfpvmmtllg laaiiglekr rmpggilmti iaisllglif dpavsykglf alpslrdasg
      241 esllfsldim gamqpvvlps vlalvmtavf datgtirava gqanlldkqg qiinggralt
      301 sdsvsslfag lvgaspaavy iesaagtaag gktgltaivv gllflailfm splaylvpay
      361 atapalmyvg llmlsnvakv dfndfvdams glltaviivl tcnivtgimi gfaslvvgrl
      421 fagewrklnv gtviiaialv afyaggwai
//
LOCUS       WP_010672098             394 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NupC/NupG family nucleoside CNT transporter
            [Pantoea].
ACCESSION   WP_010672098
VERSION     WP_010672098.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..394
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42386
     Region          4..394
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 maailhflla lvvifalall vshdrkqirl rfivqlivve aalgwfflhs agglalvgsf
       61 agffetllgf aaqgtefvfg gmskqglafi flgvlcpivf isaligilqh wrilplliri
      121 fgtllsking mgklesfnav stlilgqsen fiaykgilgd ipprrlytma atamstvsls
      181 ivgaymsmie pkyvvaalll nmfstfiils iinpmksqde qpialdklhe eqsffemlge
      241 yilagfkvam iilamligfi aliaavnalf aavfgysfqq llgylfypla wligipkada
      301 lqaasimatk lvanefvami elqkvaagms arglgilsvf lvsfanfasi givagaikgl
      361 nekqgnvvsr fgwklvygst lvsllsaafa glfi
//
LOCUS       WP_010672193             377 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ROK family protein [Pantoea].
ACCESSION   WP_010672193
VERSION     WP_010672193.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..377
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=41049
     Region          <9..59
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          87..371
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mktngkgpal lrlnnqkrvm tqlrklrvts rqdlaetltl skntvsliid dlleqgliee
       61 lgpvsvasag rpkigitlrp eklksagimv ernvihwrvc dyfsqvlaek tlrtdtsnpt
      121 rllaelamlc relmksypdl lgiglgfpgi vdprrgwmhi slplewqdvd llgalskhvs
      181 lpirimnnvk aaallavqlr glsvesghfy lrisegigga lvqhgevftg hswtageagh
      241 lvvqpdgprc scgrrgclea lvsqpavkqq laqrqpglsw qnrdsaprvv devmaqaggy
      301 lgaalsqiml llnpatiiid cpwnasevfc kavrttahgn alaftaahtl lhfpeqridp
      361 anglalavle qseqrmi
//
LOCUS       WP_010672238            1041 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Aeromonas caviae].
ACCESSION   WP_010672238
VERSION     WP_010672238.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1041)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1041)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1041)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1041)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..1041
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=115519
     Region          1..1032
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 maflseaave qalmeqlggl gysiereedi gpdghrpere shdevvlkrr fedavsrlnp
       61 glpldarqda irkvtqselp slleenrrlh klmtegvdve yyaddgtlta gkvalidfeh
      121 peqndwlavs qfvvingqnn rrpdvvvfvn glplgvielk apgsagahll gafnqlqtyk
      181 kqitalfntn allvtsdgia arvgslsadl erfmpwrttd gtdvapkgap elstliegvf
      241 vhrrlldllc hftvfgetgs glakiiagyh qfhavrhavn stvtasspqg nqrvgviwht
      301 qgsgksllma fyagqlvkhp amanptlvvl tdrndlddql fstfamcrdl irqtpvqaes
      361 redlqkvlsr asggvifttl qkfgeiaepl ttrrnvvvia deahrsqygf kakvdaktge
      421 isygfakymr dalpnasfig ftgtpieadd vntpavfgny idiydisrav edgatvpiyy
      481 esrlarield eeekpkidae vnelteeese adqerfkkkw stvealvgsd krlalvakdm
      541 vahfedrvaa ldgkamvvcm srricvklyd eivklrpdwh saddnagavk ivmtgaasdp
      601 qewqqhignk arrdllakra rdpkdplklv ivrdmwltgf dapcmhtmyv dkpmqghglm
      661 qaiarvnrvf rdkpaglivd yigiaqnlks alqqyskndq entgvdeaqa iavmmekyev
      721 vrdmyhgydy vsamsgtpqe rlammagaie wildlqqkla akektkegkk nahrryqdav
      781 lalskafala sasdeareir eevgffqair aalvksstgs gvtqqerela iqqivsravv
      841 steivdilaa agikspdisi lsdeflaevq qmekknlale alrklindgi rsrskanvvq
      901 tkafserled avaryhanai ttaevlqeli qlakdiraar qrgeeqglse deiafydala
      961 enesaiqmmg ddklkliahe llmslrenvs vdwahresar armrvmvkri lrkygyppdl
     1021 qdtavqtvlq qaealssgws r
//
LOCUS       WP_010672282             244 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Aeromonas].
ACCESSION   WP_010672282
VERSION     WP_010672282.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..244
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26591
     Region          1..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 minltglska ydgnqvlngi dlevkkgeiv viigpsgtgk stllrclnll etpdagrlvi
       61 ddlavdlaka sdqqaielrk rasfvfqnya lfanktaldn iaeglitvwk qpkaearata
      121 lgilkdigla ekqdaypasl sggqqqrvgi gramaahskv ilfdeptsal dpewvdevlg
      181 lmkqlarqhq tmvvvtheie fardvadrvi fmeggriveq gppdqilvdp qdprtreflr
      241 kvlk
//
LOCUS       WP_010672290             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Aeromonas].
ACCESSION   WP_010672290
VERSION     WP_010672290.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..256
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27951
     Region          1..240
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mkitqvrnat llihyagtrf lidpmlapkg sypgfegman shlrnplvel plpmatllev
       61 davivthdhl dhwddvakak iprhlplfvq hqkdadtmrg cgfedvrllg evgefagirl
      121 qqtegrhgsd timallgdrl gevsgvvfsh paektlylag dtvwnaqveq alhrhqpevv
      181 vlncgdaqvt glgaiimgke dvaavyqaap qatliashme avnhallsrr elrhyldsqg
      241 maarvrvped gdtmvl
//
LOCUS       WP_010672332             594 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Aeromonas caviae].
ACCESSION   WP_010672332
VERSION     WP_010672332.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..594
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=67428
     Region          52..>276
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(130..131,133,167,170..171,174..175,177..178,205,
                     210..211,214..215,218)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          155..199
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          181..>576
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
     Region          204..234
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          244..270
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          431..578
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(464,507)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(469,472..473,477,481,503,505..508)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(499,526)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 malallwmtq lqaapsllke aelqaardpv gylqrldasp qqdmelfyar slaqaalgry
       61 pqaqrdnara rglanaqqet lrlldfrlqq ialtldadtp dqalelltql wpavrhhprq
      121 vsewhalngl alyrtqqmke ailelktayh lkqkepgsil stlqcgrllm tlgnlyadln
      181 lyreaetyyq dalgqmvqln epnsqaiira nmarlyidmg qparasqlld tllatpslsp
      241 hyraivlgyq amvfnaradw hsawrsleea qaiydrldsp qaasrlteir artllgrgek
      301 qlalqllmeh taplsmdgra mqarlladlg rypeaygamt rymqyykqhf nqtlsqhaaa
      361 fqvemdlars easnralqqe nenkrqqlly qqsaryyqll llvllavali llglttrrlh
      421 rssrhlykla tfdqltgmpn rrallerlgq qwlhetpltl liididhfkq indkhghqag
      481 dqairqlare lkswapdqql igrwggeefl vamtqdgatc wrraeqlrsr iaylaaphmt
      541 isigvaerst qddslsqlih radmamyqak rqgrnqtvla qspnlspela cnva
//
LOCUS       WP_010672434             665 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LTA synthase family protein [Aeromonas].
ACCESSION   WP_010672434
VERSION     WP_010672434.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..665
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=74697
     Region          17..606
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 myqtrlkrll sliwfhliwl tlllmaarfs mfhafvepaq ladkgddllr mwatglrydl
       61 riagmavapf lllglglagw skgwgylwrs lplwlgttaf ivasvaigny fyyqtyhnhi
      121 dvfafglvdd dtravlanlw qdypvikggi aatlfalppv wfsyrvrsmt qrpwpdalfc
      181 gilvlsvilv aiaargsvgt fplrrgnaqv sdltvlnklt pnglmaidwa ikdhqddivf
      241 ekvdaaekik llgatglnsl tgrtpvntwl annkphvvms lmesfgsnml aldeqskndl
      301 lgslrepfrq dfvfkrfvse gngtapslaa lffhspmenl shssaqskvl tgtpffiykq
      361 agyrvifisp gnmmwrnlvn ylpvqgvdal ydqnaliemy pesvkemtdw gvpdeyayql
      421 aekllkdaqq plfisiltvt nhppyvvpsh yvpqpvavtd gvrrhaedgq idqlnilrty
      481 qyaadalgrf vadikesalg shtliaasgd hqmrrvkayy paeqmldrav pfylyvpkai
      541 ldrvpwrfes arpgshkdif ptlyafslsd vpyqalggrn llapqddptr afgynetvwi
      601 dangaypltg npvrylwvpg eswylgeavq pidevqrqrm qaypallrwq lnarvagvia
      661 ddeie
//
LOCUS       WP_010672473             372 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Aeromonas].
ACCESSION   WP_010672473
VERSION     WP_010672473.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 372)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..372
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39575
     Region          5..355
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 msqarvpawi svgvlpavni llaflvsail fyyldispie aaeimwygaf gtgegigftl
       61 yyatgfiftg lavavafhag lfniggegqa yigglgvglv clllgdvlpf alllplaiia
      121 gglfgaawaf ipawlqakrg shivittimf nfiaaslmay llvdvfkppg smateskvfa
      181 vaswlpkmse laagfgiamp nsplnisffw alicaalvwv fiwhtrwgye irsvgasqsa
      241 sayagisypk vvilamvisg mlagffalnv lqgelhqikl nfvegfgftg iavalmgrnh
      301 pvgviiasll fgflyqggae lsfefgvdrn ivvvlqglvi lfcgalehml rprieqayla
      361 fanrpaaqvk ga
//
LOCUS       WP_010672488             212 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Aeromonas].
ACCESSION   WP_010672488
VERSION     WP_010672488.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22397
     Region          1..204
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mftslfltlg lvhlvalasp gpdfalilrt slhrptalga algialaill hatlsltgis
       61 lliasqpwlf lavklvgaly lgwlgwgalk aawqgsgdla lraggerpgw rkgvksglat
      121 nllnpkamlf fmgllaamvt pqvdgltrgl lilelfllsl vwfsalawsl stpraqhllg
      181 riqrplnlmt gllfgavsls ilvdlqghwp aa
//
LOCUS       WP_010672643             357 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: porin [Aeromonas].
ACCESSION   WP_010672643
VERSION     WP_010672643.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..357
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38444
     Region          4..357
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkqsmlalai palfavgaaq aaviyqaddg snvdlygrlg fnvsdkkngn sqgdfdgrig
       61 ftarqtvndq vavigmaqyq vnaaeyannv qknssdltar yvwagidgge wgkvtggrvs
      121 sglimftdig dvfaasdvsm arqaskvdst avqvfrqdgt lqyqntlgnl dvslayilgn
      181 gtsdldygyn galrytfdlg aagklapvia yqqskaaqtd askvdpdadq yrfsgigary
      241 tlgslmlgal yakdqvsyrn graesedkvw eltavydisq kwaaragyrh ldndggdgms
      301 lrdttlelqy kltprsslys ayvfrdgedg ladntitsfg gssnsesfyh lglryef
//
LOCUS       WP_010672779             667 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Aeromonas].
ACCESSION   WP_010672779
VERSION     WP_010672779.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..667
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73973
     Region          19..662
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mipslwrqtp wgkanggqwr yalrnalamc lslwlafvlq ldspywamts aavvsfptvg
       61 gviskslgrv vgsligamaa vmitglgigd pwlfsllial wlggctyisn hhqnnvsygf
      121 alagytaaii afscvnltdp qhifdiaqar vsevivgilc gglmmmilps fsdgetllds
      181 lgksqtrlle haqllwlget gadvrtaheg vigqiltlnv lriqavwshh rlrrhnqlln
      241 yllhrqlrmv slisglrrml qhwpedavdp tpmlaavlre lgqggcdklr iarlmapfva
      301 rsgddyrcqa fwlrlrhfcw sylecqrwle rlarhdgqew papprhsslt shtdgleaay
      361 nggrtflcvm lgctfwihsq wdagaaaltl laiccvlysa tpapakgaqt mlkaivllsf
      421 icfgvkfglm iriddfwifc allfpalitl qllklqrpqg aalwgqlivl lgsflaitnp
      481 psydylafvn sslaqalgvm saglafqllr pssdrrksrr lmhrlrrdfv dqlapaphqs
      541 egefesrvyh avsqlsqsqd qgarlwvlrw gvvllncshi vwqlrlwrsr dpalylvrdg
      601 clrclkgilt eggvqhetlg rtlaeldris lglgehadpa aralaglvwr lhcslsqlvq
      661 alpgept
//
LOCUS       WP_010672924             188 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Aeromonas].
ACCESSION   WP_010672924
VERSION     WP_010672924.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20340
     Region          1..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrsaeydrda vlrnameafr akgyakttmq elvaatglhp gslyaafgnk rglllaavdh
       61 yvaekgalrr rclaqpspla glhafleqvv ddalqgscll trtlmelaeq deelhlrfka
      121 iygeleqdla gqlalakaqg elakegdipt ltaflqvhiq glvtfaqchp drpllagvva
      181 rmmsalra
//
LOCUS       WP_010672905             198 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Aeromonas caviae].
ACCESSION   WP_010672905
VERSION     WP_010672905.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..198
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21765
     Region          1..198
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtiewyatlf gfalltcgtp gpnnlmltas ganfgvrrtl phligvavgq pvlqlvlalg
       61 fyplferwpl lklslqvlgs lyllwlawri vvagapgdpa srarpltlle glgfqflnpk
      121 awmmgisais lfslpgsdyw psmwgimsvf pmagfpvcfa wvmfghqlsr winsdkgwrr
      181 lngslgalta lcvvmlwy
//
LOCUS       WP_010672937             491 aa            linear   BCT 01-JAN-2025
DEFINITION  GGDEF domain-containing protein [Aeromonas caviae].
ACCESSION   WP_010672937
VERSION     WP_010672937.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 491)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..491
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55793
     Region          227..474
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 maasllrflp rrwltrlgwl clalmglglv cnytylrirh dmalitakqp nlfevfyqra
       61 rilapeklaa fidnssikmp ifsengdata yaygydlptl krlavipvlp panqmllayq
      121 yvisnpevln lyafyddrrm lgmvaskgml psqllpintd lsdiepwthy fgcaffaath
      181 vpcstdeawv sglytdtftg lqaitlyfpf iyyepaikdy ryglkgidia vdrafkevlr
      241 pfehlnptrt vlsfeevepc rpfhlclstp lmrtkagsdl ylkwsyrygd faravlygpa
      301 fkiylivmll lmltgrslvt rlrtlaqtdh ltrlprrdil neallqehdy lmildidnfk
      361 svndthghgv gdlalvafaa hlktnirkgd vairwggeef ivlfkgmddd nmmhhsaarl
      421 lerplripel ptpitfsagv trirdyltvt eavqladdll yhvkqhgkrn iayyqgqtic
      481 lvrdpgadsa p
//
LOCUS       WP_010673025             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Aeromonas].
ACCESSION   WP_010673025
VERSION     WP_010673025.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..262
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29109
     Region          3..254
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 melidthchl dfpvfdadre alltrwrqlg vgeyiipavg eenwgrvmal agrhddiryg
       61 lgihpwyvgk qprdaltrle tllasrprgl vavgecgldl rshvsqegqv emfeaqvrla
      121 mahalplivh svrandtvak ilrrftppqg gvihafsgsl hqaevfwqlg frlgiggvis
      181 yeranktrea irqmpleall letdapdmpl qgqqgevntp aslptiarll aqlrqqpled
      241 visvlhdstr rlfppgnhei ni
//
LOCUS       WP_010673065             398 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NupC/NupG family nucleoside CNT transporter
            [Aeromonas].
ACCESSION   WP_010673065
VERSION     WP_010673065.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..398
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41275
     Region          1..397
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 miallgilsi lalaalcsdn rrriplrtvg falclqvlfa alvlwlpagq qvlngvsesv
       61 ssvigygqeg iaflfgdlak fklgfifafn vlpviiffsa liailyhigl mpkviallgg
      121 glqkllgtgr aeslsatani fvgmveaplv vkpylsrmsd sqffavmscg lasvaggtlv
      181 gyasigvelk yliaaafmsa paglamakil vppaaqekdh hedveiprat nvieaaadga
      241 maglniavav gatllafvgv iallngllgw agdlvglels fqiilgwlfa pvswligvpw
      301 dqaqaagali gtkivinefv afialvqdqt lnesskaivt falcgfanis smailigglg
      361 amvperksfi arygmraila gvlanlmsas laglflal
//
LOCUS       WP_010673149              96 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Aeromonas].
ACCESSION   WP_010673149
VERSION     WP_010673149.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..96
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10618
     Region          7..>85
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mitstkerra fqrmvinapv tlfqhqqvle gvcrdlsang mgvevnkhef dlaqpirvsl
       61 atssnllppf eaqarivrvl eeedglllal eflslt
//
LOCUS       WP_010673155             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Aeromonas].
ACCESSION   WP_010673155
VERSION     WP_010673155.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23336
     Region          12..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mekrrpgrpv grsdirdkll aaarerflnt pyskvttrei aelagsnlam ihyyfgskeg
       61 lykavlgdva epleqawhde ssnrsltdll ntyyqvmapn seltsaissa lstekspgrd
      121 fvlsrlldrq lpqfdalles mrsngqladn ldpemlkisf lsmmwqpfvm kdlyeqvfgl
      181 tvdehfmsrl aahncrlmen glrgaln
//
LOCUS       WP_010673181             658 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Aeromonas caviae].
ACCESSION   WP_010673181
VERSION     WP_010673181.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..658
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=70823
     Region          128..656
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkisskllls fcfinlliil ssalvyhqlg riegsqdall aqalpalqrd easqkaliat
       61 vsslraylil gkdpaqgdri kqeweeawha ierqrftpdl tralkdfkga qsqvwalaht
      121 eenlpahtlm lleagplaes aldqlqsfan eevatpqatl pgdrrlllkq vgdaynslgn
      181 alsalrdfli sgekeyldky rdyyqfhqqr vaelkqqdan fteaqkglwt lfeemsapfa
      241 elvgqviekr qapdwdranh lmateiepal trladqlatq vthtraevdk magemaaasq
      301 tihrtlllat tsvillgtlv allfsrrltr diaslvkrag lvadgrlpvt plpvlrqdel
      361 ggltgsinrm saqlrelvge iqgavgqveg agrevgqttn aivddlasqn qrldavaaai
      421 eqmsvstrdv agniadaaga arqteqqare geqalarmgt tmaqigamia qanqamtqls
      481 sqseqvgrvt eviatiaeqt nllalnaaie aarageqgrg favvadevrq lasrtsastm
      541 einqtiasiq qqtretadtv gsgtllveqg rgavasvtet lesmatlvqd lsgqlaaiat
      601 ateqqsraaq evagtveeia glshqssehg qqgeqiaarl tretgrltsa isrfelda
//
LOCUS       WP_010673217             280 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: lytic transglycosylase domain-containing protein
            [Aeromonas].
ACCESSION   WP_010673217
VERSION     WP_010673217.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..280
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30797
     Region          43..72
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          54..265
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mkkrlwgwgl lillattsha dpfrqapkam salrqgaame qgnprqaiah yctaanlgnp
       61 eayyrigrll argpqgirna rsanaylama mrlgnqqaar yynervgnap lgtcgigggg
      121 gapwvrpstp fdqerylarq sqakqklavm irqaaqrhkv dpqlalaiai aesnlnstav
      181 spkqaqgvmq lipetqarfg vtrpfdaqqn irgamiylkw lekqfgpdwv risaaynage
      241 qavlrhggvp pyqetqeyvq rvlyysgqdp dkparrsspr
//
LOCUS       WP_010673283             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methylated-DNA--[protein]-cysteine
            S-methyltransferase [Aeromonas].
ACCESSION   WP_010673283
VERSION     WP_010673283.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..158
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17206
     Region          1..156
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mirydmmptd qgellvaide rglvhvdfla glrplpdmsd wrqdgealap flaefrdyfa
       61 grlqrftlpl aprgtafqqa vwqalcdipy getrsygdia raigkpnavr avgaangrnp
      121 lsiiipchrv igqngsltgy agglpikqal ltlerasr
//
LOCUS       WP_010673300             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Aeromonas].
ACCESSION   WP_010673300
VERSION     WP_010673300.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..264
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28686
     Region          1..252
                     /region_name="trans_reg_YgbI"
                     /note="DNA-binding transcriptional repressor YgbI;
                     NF040890"
                     /db_xref="CDD:468826"
ORIGIN      
        1 mipverqqri lqllaergvv siveltdwlq vshmtirrdi qkleeqgrvl svsggvslsq
       61 riksepshaa krslmqgakl aiarlaaaqv segstvylda gttslelare lalredlmiv
      121 tndfmvcayl iehgrcrlyh tggqvirenq scageatahf lrnlhldiaf lsasswdsqg
      181 istpseqkvp vkravvesaa trilicdssk ygkvgtfnvv swdaidqvit deqlpqsare
      241 alaqhgvrvt maplaslvas aeqg
//
LOCUS       WP_010673421             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Aeromonas].
ACCESSION   WP_010673421
VERSION     WP_010673421.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33059
     Region          8..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,223..228,
                     234..235,237..238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtlsrtdlae lavfaavarh rsfskaalel gvsasalsha lkglesrlav rllnrstrav
       61 vpteagerll aqvlptlgql eaalaeltrh agepvgrlrl capraaiqev lapvlidylv
      121 ryprmqveve elelmprlie dgydaalfyg dllpqemisv plgpqqrylv vgspdylarr
      181 gtprhpsdlr qhdcigyrlt phhhyrwafa akgelleiev tgplttstpa lylgaaeagl
      241 glaychegev fdalasgrlv svlddwspsf agfnlfypgr hqlgqglral idmlkeyhri
      301 r
//
LOCUS       WP_010673426             575 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Aeromonas].
ACCESSION   WP_010673426
VERSION     WP_010673426.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..575
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62974
     Region          7..489
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mttlmsthsl qmsaghlplf dhlelgirag drlgligang cgkstllall agertpqagr
       61 ivqaaacrce fvaqqlpael stlstravll dalgndpaae wqvdkllael qleaqatlpv
      121 salsggqhsr lqigrallrq pnlllldeps nhldlpallw leqfllgwrg afvlvshdgr
      181 lldsvtdqtl ilrdgqlhrf alpcsqaraa laaedeqarl rradeqkeid rlsasskrla
      241 iwgrehdnek lvrqaksmek riarlqeeqs qvaalapwrl elrgvslpad tllrlealdv
      301 spapalppll raeglwlrag drvallgang tgkssllrqc wrelaaqslq agwychpgas
      361 iayydqslqq laddatlsda lyplaplpev trrqalirag fpyvrhgqqv htlsggerar
      421 llflalslgs hhmiwldept nhldlagkee ladaiaafpg gvllvshdre lierscnrfw
      481 likdgriqea hcaerayael lgdapllqag spaqsgdpqt aaatgddeea llarwyelda
      541 llaadlarkp rhqtprlqqq wrdelarlae rlgfa
//
LOCUS       WP_010673432             386 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: patatin-like phospholipase family protein
            [Aeromonas].
ACCESSION   WP_010673432
VERSION     WP_010673432.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..386
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43199
     Region          1..366
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 marpntalll tgggaraayq vgalkavael yprnigipfp ilcgtsagal nitalacyas
       61 cfhlgvrkle wvwrrfethh ifdfhpcqll wrtlyqgsag litpqsnraf hlfdnaplrr
      121 lldqlidyhr iddnilygsl eaiaitasdy ddglsttffq graehqpwer arrrglrtll
      181 tsdhllassa lpfvfpatpi gdrvygdgsi hqlsplspai hlgaerillv tldsphrenp
      241 tprqghltss niashllntv fsdtlnsdle rlgrinqtls liparersrl klrqvetcvi
      301 rpsqdldlia leylprlptq lrrllrvlgv ngeessslas flmfdpgycq rliklgyqda
      361 ldhrqrieaf ldlpgsgrqq qfreea
//
LOCUS       WP_010673433             285 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Aeromonas].
ACCESSION   WP_010673433
VERSION     WP_010673433.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..285
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31004
     Region          63..278
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 msskiyfntr rfspsklllg lgtrlhhvla pthakrtask llltpqratr gvaaptglve
       61 qaihtsegtl msyrlgqgpv wllmhgwsgs asqfyplmsh iaaqgytala ydhpahgrse
      121 gnrghlprfv rafdeilerv gpvqgviths mggavtlssr hpaidalpll lispvldyvp
      181 qlygmvarsg ysirlfdavv keieheyqhp lstvdplgrl arrsgaaliv hdeedrfaph
      241 rdslraaqdg rtrlvstrgl ghgrilaspp afaafdqlsq tplan
//
LOCUS       WP_010673434             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Aeromonas].
ACCESSION   WP_010673434
VERSION     WP_010673434.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22061
     Region          1..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mskgrltrdt ilqtafeqas qqglesltig slatacemsk sglfahfqsr dnlqiavlth
       61 saevfrervi qpvrqqgyat qqekllallq awlawnqsfa grcmfldawt saqegevqqa
      121 arelvrfwld ylarqvvqgq argewrsdld pwravyrlyg lylgdqvfha lalsedparh
      181 fwpeveqllt swr
//
LOCUS       WP_010673435             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor [Aeromonas].
ACCESSION   WP_010673435
VERSION     WP_010673435.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..214
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23265
     Region          7..122
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
     Region          149..204
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mdsqftivia ddhplfrgal yqavhmaidd arlleadsid slshlldehp dvdlllldlk
       61 mpgangfegl aylrghhpdl pivvvsased paiiqqvlrl galgfipksv pmkelvsaln
      121 tviggdnwvp egislhpeps egpdfatkla sltpqqykvl imlrdgslnk qiawelnvse
      181 atikahitai frklgvknrt qavialqqmd ikds
//
LOCUS       WP_010673439             123 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GtrA family protein [Aeromonas].
ACCESSION   WP_010673439
VERSION     WP_010673439.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..123
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13455
     Region          7..123
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 misreefwrl vrfgfvggga tlvdlgtsia lfhtwpaise hlvttlafav afwfsffghr
       61 yitfqkqgaa skfllvalfs lavrnlilsg llfaglsgll pvviatltvt vltyvlsriw
      121 vfa
//
LOCUS       WP_010673477             241 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: copper homeostasis protein CutC [Aeromonas].
ACCESSION   WP_010673477
VERSION     WP_010673477.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..241
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25220
     Region          1..241
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mtrleicidn leslftaqaa gadrielcsa lglggltpsy gfmqqvarha tipvyamirp
       61 ragdfcfgeg efdimlqdia avraaglqgv vvglldedgr vpegklrqlv eaagplgvtf
      121 hraidlssdw rldletivaa gcerilssgh aptalaglet lqamhqalag raslmpgagv
      181 nadnvrtiie ftgvnevhms gmgwrggmvp hgvnmgtsdd grvnitdgak vaavralldr
      241 a
//
LOCUS       WP_010673594             674 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BCCT family transporter [Aeromonas].
ACCESSION   WP_010673594
VERSION     WP_010673594.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..674
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73971
     Region          14..488
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mnaprpprct lslpifipgl lfilallaic slapeaaarf fgsgqswiaq hfswfyvlvv
       61 gmflilllvi afshfgnirl gpddarpefs ftswlamlfa agmgiglmyf gvgepmshfv
      121 sppqatpltq vaareamvtt ffhwgfhawa iyaivglvla yfgfrynlpl tirsglypif
      181 kekihgplgh avdvfalvgt ifgiattlgy gvmqlsagit rltgmdtsge lfrfgligvv
      241 ialagisavt gldkgvkrls elnlflaivl llfvlvagpt qyllgalsen ignyvsslsq
      301 ltfrtftyse trqagwfgnw tllywawwis wspfvglfia risrgrtlre filgvlfvpt
      361 afnllwmtvf gnaaiwasqh eggtslidsv gnidtllfnf fdllpgadit salavilisv
      421 ffvtsadsga fvidniatqg kegspvwqrl fwalllgvta gtlmstggla alqsmtliaa
      481 lpfafimvll clglcrglva dkehsarrls patdfwngkq wrtrmdhllr psteqearaf
      541 vdkvalpalt alsqefaarg itsrveedgp dqchllvpqq grrdfcygvr iearpapafn
      601 pleaahnhdp earifepity fadgragydi qyltrdelsa dvlrqyeryl vlsqdegqdl
      661 lssapehtqp tqge
//
LOCUS       WP_010673611             246 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dienelactone hydrolase family protein [Aeromonas].
ACCESSION   WP_010673611
VERSION     WP_010673611.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..246
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25803
     Region          28..241
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mkrawilall glmgsgaaea gavryevegk pfegyylagt dkdaplvvlv hdwdglngye
       61 ikraemlval gysvfavdlf gagvrpgtve dkkrltgaly qdrtrmrsll qgglaeagrq
      121 ggrldnaval gycfggaavl elarsgadlk gvvsvhggle tpagqdykea kgqllvqhgs
      181 adeavslgqf aalvaelesa gvkheatsys gaphafsvfg sdnyradada kswqrftgfl
      241 kevtgs
//
LOCUS       WP_010673643             385 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Aeromonas].
ACCESSION   WP_010673643
VERSION     WP_010673643.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 385)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..385
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41463
     Region          117..371
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mihtptllli slainlmsgl imlfihslkp grgnflywsl saflfslsil llslgvlggh
       61 palgirvggl vslmsillll agfcalyera whpravgggv avllllylgl sslapvrivl
      121 almesmlylw caclivslgr qqkrvlhava liyllhftil lsqggllllg veermgdggw
      181 ldliffmhmv ltigsvlllp lvayveteea llalserdpl tgvlnrrglf rhgegttpgq
      241 trcvvvldid hfkrvndqfg hgcgdeviry vagvlvaevr kddlvgrigg eefaiimggv
      301 sgqmardicd rirrqietgs rqgaclpceg vtvsmgvvca saeadlalml tkadaamyrv
      361 keagrngvhl afepalprlv esseg
//
LOCUS       WP_010673670             141 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein [Aeromonas].
ACCESSION   WP_010673670
VERSION     WP_010673670.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..141
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15659
     Region          39..141
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msllpsrtsl fddlfhdmas gfyirplhgd plpgqikldl resgddylll aelpgvaked
       61 ihvdvhgklv tlkaeirqfd sqskderalr seryygsvsr svelpvevsp eqvsarfdng
      121 iltlrlpkqa aspaphripi e
//
LOCUS       WP_010673636             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: siderophore-interacting protein [Aeromonas].
ACCESSION   WP_010673636
VERSION     WP_010673636.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..268
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=29642
     Region          1..256
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 msqpapanrp rlltvkhvqd vsphlrricl tspelvdypf scggahvkim lprpdqreiv
       61 lptptdkgpr wldpaqkpvi rtftirafrr ealeldidfa lhgeagpasr falhakpgdr
      121 laisgpggpd pmlqtaehyy magdltalpa isamvevmpa halghiallv phqddvqdls
      181 lpagvdlrwf vgnpeqaatl vahftaqpmv aegsyfwfgg eeslvvplrr hvrraldaer
      241 qrvyavpywr sgkdedayhq drhavmds
//
LOCUS       WP_010673686             453 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Aeromonas].
ACCESSION   WP_010673686
VERSION     WP_010673686.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..453
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48359
     Region          17..388
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(24..25,28..29,32,65,115..116,118..120,123,145,
                     148..149,152,221,224..225,228..230,233,260,264,308..309,
                     313,317,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 mndftmtrge rratwalgsv fslrmlgmfm vlpvlttygm slagaseali glaigiygmt
       61 qalfqipfgl lsdkvgrkpl ivggllmfal gsviaalsda iwgvivgral qgsgaisaav
      121 mallsdltre qnrtkamafi gvsfgitfai amvtgplith alglsglfwl iallalaaia
      181 mvlwvvptpa ahlqnresam vrgsfrtvlt nprllklnlg ilcvhtllms sfvalpplle
      241 raglprdsqw qaylvtmlia fvsvvpfiiy aekhrqmkrv flgcvvvmla aelvlwqsgq
      301 qlwgllaglq lffigfnvme allpsliske sppgykgtam gvystsqflg vaiggslggl
      361 lyslgggplv fggcaalala wlgvsltmae ppyvsslriv lpegveatpa leqriraceg
      421 vsdvllvree hslyvkvdsk rltrsdlerl vsf
//
LOCUS       WP_010673740             446 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TldD/PmbA family protein [Aeromonas].
ACCESSION   WP_010673740
VERSION     WP_010673740.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..446
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48048
     Region          6..445
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 msqldmnqll arlleqvadl gaeadvianq ekafslkadk gelseykvts sqqigirlik
       61 egrvgiayse sldasaldam vqdaldagrf akvdpdqrit vqqsrlitdc aeihqadtta
      121 veekialtlr lesdmlalpd vtgapyngff egesrlwlan sqgslcehqe fsvgchssal
      181 ieregrqsmh yqgqyarrfd elesqplirq ihavadgllm geavpsgrys vifsthcfas
      241 lfgcfqsals gkwaqqginp wrdklgqsva srwltlesra ympggmkika fdgegaatsd
      301 llligegelk tllhnsatar hfgvtsngaa arsarsaldv aprhlvfglg phgeaevqsg
      361 eylelvkldg lhsgadavsg dfsfgasgfl crngervapv rgitvagnfy rllgeleavg
      421 nqlhhddgkd fyaplirfgg lsiagk
//
LOCUS       WP_010673742             466 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TldD/PmbA family protein [Aeromonas].
ACCESSION   WP_010673742
VERSION     WP_010673742.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..466
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49776
     Region          10..464
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mtsfsllapa iardvldhal algadfaelf vehkrrsqls llssqienis ggldfgigvr
       61 lcyghkvlyg ytnladrnel lrivtllaak drrdpvvtat afdftrltdr npialplsad
      121 klleqkiayl hamdaaarae sdkvsqfsgn vlgweqevei fnsegvqvsd rrhynrimaq
      181 tialdggeqs vgyeapgamk gwehaesidp relaltatrq alvklgaapc psgklpvime
      241 sgfggvifhe acghlletts vakkasvfhd kmgqlianpa vsavdeglqg nawgsinvdd
      301 egmatqhtql ikdgvltgfl vdrmgalrtg yartgsgrre sykfapasrm rntyiepgny
      361 slddmlatve hgiyakrmgg gsvqpgtgef nfnvqeayli eggritrplk satligtgpq
      421 vlkeismvgr dlalsagmcg svsgsipasv gqpplkvdsi lvggna
//
LOCUS       WP_010673808             225 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycerophosphodiester phosphodiesterase [Aeromonas].
ACCESSION   WP_010673808
VERSION     WP_010673808.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..225
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24440
     Region          1..224
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mqiiahrgas dlapentlka mslaldlgak aieldvqwad gelwvfhdrr lerctngqgv
       61 ltgqsreyla sldagdgeri ptlwqvmalv agrcelhiel kgahtaepva altrraeael
      121 gftqahwivs sfhhpellrf kglrpeirig almaslpldg aafaetlgaw slncdvdfvd
      181 etlvadahrr glkilvytvd evsdgsalas mgvdgiftnr pdrfs
//
LOCUS       WP_010673840             306 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Aeromonas].
ACCESSION   WP_010673840
VERSION     WP_010673840.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..306
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33352
     Region          78..283
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mekqlepaia amvadfiaag rpkasqlswq arrdgylasa llggereevg aieewqadhh
       61 aircyrpadk pdpaypvliy fhggcfvsgd fethdrqmrm lcnrastlif avhtrlapeh
      121 typaahddal aatraimaev ekwhgdparl aiagdsaggh lalvttlrlk aasaplpkal
      181 lllypmldal cesqsyrdlg ddylitrdml esgfhaylgs lppshpeasp lhhpalsglp
      241 pthivtaeyd plrdegealy gklvqagvda tcqrqhgvih gyfqlaaisp aarqlidqia
      301 mmlrrl
//
LOCUS       WP_010673872             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Aeromonas].
ACCESSION   WP_010673872
VERSION     WP_010673872.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..190
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20758
     Region          4..129
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,67..68,71)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(66,110..111,113..114,118)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(72,77..78,106,109..110,113..114,117,120)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95..97,106..107,110..111,114,118,121,125)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95,111,114,118,121,125)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(119,125..126)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          141..178
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(142..144,174..175,177..178)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mgqvigyarv ssvgqsldvq ldkltkagce rvyqekvsgt stdgreqlae llryvregdd
       61 vvitkldrlg rsladlldit eqleakgvtl rvldqnletm taqgklmftm lgafaefeta
      121 lrkerqmegi akakaagkyt grpksideda ikatlleggk slreiatlhg vsratvhrls
      181 trmredgels
//
LOCUS       WP_010673884             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Aeromonas].
ACCESSION   WP_010673884
VERSION     WP_010673884.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..267
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29943
     Region          14..253
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          171..252
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mstpllqlnh yfgirqqplr rvliyaptli wvqqgrkqlw wreqrlsfdk eswllipagh
       61 rltfvnqpeq gtfrsqaltl lapppaewla espldllkpp airvtsalaf cfdlvttmaq
      121 rqlcetaqtq llqgfygelr eagglgllfp attmtlgerl arylsvepgl dhrletvath
      181 famsraslvr klaaegrsfr qvltqvrlgh altllqqglt plqtalacgy dspgrfaarf
      241 keefgltphq ylrtcpgsha arqvger
//
LOCUS       WP_010673885             177 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YbhB/YbcL family Raf kinase inhibitor-like protein
            [Aeromonas].
ACCESSION   WP_010673885
VERSION     WP_010673885.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..177
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=18648
     Region          22..175
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrspiipllp lfclaalpag amtlkstdir egepmdkifs fngfgcsgen rspqlswqsl
       61 pagtqsvait aydpdaptgs gwwhwlvvnl pasqselpsn asgklkqgle lgtdygtqgy
      121 ggpcppaghg mhryqftvwa lpkalevkan tppamvgyml nslalgkatl tatfttp
//
LOCUS       WP_010673940             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Aeromonas].
ACCESSION   WP_010673940
VERSION     WP_010673940.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..264
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29625
     Region          1..251
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mivwtvanqk ggvgktttvv slagilaqrg qrvllidtdp hasltsyldf dsdrlegtly
       61 elfqaakpsa elvnrmtlkt rfenisllpa sitlatldrv mgnregmglv lkrallrvqd
      121 qfdyvlidcp pvlgvmmvna laacdrilvp vqteflalkg lermmktfei mqrskrekfr
      181 ytiiptmfdk rtraslmtlq sikeqygeav wnavipidtk frdaslvhip psiyapgsrg
      241 tyayetllnh ldalerqrtq evmp
//
LOCUS       WP_010673956             403 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RsmB/NOP family class I SAM-dependent RNA
            methyltransferase [Aeromonas].
ACCESSION   WP_010673956
VERSION     WP_010673956.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..403
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=44918
     Region          <123..403
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mlkspllprf gdlvvaivdd vlgqgltldr ayarhfsgie lkpqeqaria lvtgdllrrl
       61 slycfltgiq vrqaeknvwp llhswhafhk idqpnhptld rfneeafrrr lteakknpvl
      121 mdgcpawlek lgseqlgdaw paeraalawm pkrylrvntl kctrdelqam lakehvttvp
      181 vdgvetalqv tsdaalfrtq afadgcfeqq dagsqlvaaa ldvkpgmrvi dacagaggkt
      241 lhlaammqgk grllamdvee wklenlkqra rragahnvet rvitssktvk rlkesadrvl
      301 ldvpcsglgv lkrnpdakwr dtaerlpvlv alqeeilqry sqmvkvggll vyatcsilpe
      361 enrqqvdkfl aanehfrlig dhnvspaetg fdgfymarle ria
//
LOCUS       WP_010674078              85 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Aeromonas].
ACCESSION   WP_010674078
VERSION     WP_010674078.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 85)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..85
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=9545
     Region          3..83
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 msdilhqadq qqfvctvdgk lsrlayrrld atkvdaystq vppelrgqgi adklarrfyd
       61 wtlsegltiv pscsyidvwl rrnag
//
LOCUS       WP_010674082             196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Aeromonas].
ACCESSION   WP_010674082
VERSION     WP_010674082.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21406
     Region          2..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mretmtdkrr qildaalalc aedglqgaat ariakaagva ngtlfhhfps kevliqslyq
       61 diklrlgaai teadaalplq eqarhywhqa mgwmqahpre lrfvlgffhs pllarplrsq
      121 ilaetlhflp sllargqasg elmsappalm levcqgqfla caslfvdqpe lgedphwqes
      181 aftlfwsais ggshap
//
LOCUS       WP_010674118             191 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Aeromonas].
ACCESSION   WP_010674118
VERSION     WP_010674118.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..191
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21599
     Region          39..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mrievkpdra yawfirpffw lqkrnygqvl ipgkcwgrsp rlfaavatly gvinrkrspi
       61 dpvlrslvtv rvsqlnwcrf cvdinamtlv kragssdkve alarwrdspl fdereravld
      121 yaeamtgldg vsdeqaarlk pwfdddalve ltgliafqnm sakfnaaldi apqgfcqlpv
      181 qperhldkgq g
//
LOCUS       WP_010674201             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Aeromonas].
ACCESSION   WP_010674201
VERSION     WP_010674201.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..155
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17270
     Region          1..144
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 msareltlqf laepadvnfg gkvhggmvmk widqagyaca agwcggyavt vyvggirflr
       61 piqigqlvev hakvihtgtt smhlavdvys rhptdperrk tthciiifva mdehgkptpv
      121 pqwqpvsesd lqlqqyakkl malreeldke mrqhm
//
LOCUS       WP_010674269             246 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Aeromonas].
ACCESSION   WP_010674269
VERSION     WP_010674269.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..246
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26805
     Region          1..246
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mfdlkgyets llegawitle valaslllal vlgmlgalak lspykwargi aaayttvirg
       61 ipdlvlmmll ffggqvling ictwvneayn nhllasnpnq ewvsllpdyi dispfaagva
      121 tigfifgaym tetfrgaila vdkgeleaar afgmrasqvf vrilfpqmmr halpgfgnnw
      181 lvllkttalv siiglddmvr kaslaagstq qpftfymava liflvftavs tsalkwaerh
      241 yaiktr
//
LOCUS       WP_010674309             543 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Aeromonas].
ACCESSION   WP_010674309
VERSION     WP_010674309.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..543
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58204
     Region          12..542
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 msykhlsigk kiaavfavia vinavfglfl atelrdirdr vlnftdstlp svlsvdnlly
       61 dvsyvrraqf allmvedavd rqvrrariqe slgkvqqvmd ayeatvgaeh erqafnrvkq
      121 qwlqylgavn qvdallfqgs rdearealfr snglytelel avralvkvnl gfveenrgsl
      181 lgsvtmvmtf avvsiatlli fmgvmtwflt rqiclplqav vaqanaialg dlthrldrqh
      241 igqdelgmla saslkmqdnl rglieevaaa vtqlgaaiee vsavseqssq giqsqqqeia
      301 qvatamaqmk atvadvagnt evasesassa nalarrgsqd vqgaldaitr vagemeqagn
      361 lvselekesa qinlvvdvir giadqtnlla lnaaieaara geqgrgfavv adevrtlagr
      421 tqastgeiva iietlqaran raksvtgqsc emirqcvsqs ertsagirqi eeavaqiadm
      481 aiqiasacge qdavsdelgr nvarindssn evatgadhta kaclelsqla aglrqsmgrf
      541 rla
//
LOCUS       WP_010674326             411 aa            linear   BCT 01-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Aeromonas caviae].
ACCESSION   WP_010674326
VERSION     WP_010674326.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12112208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..411
                     /product="HD-GYP domain-containing protein"
                     /calculated_mol_wt=45710
     Region          3..126
                     /region_name="DUF3391"
                     /note="Domain of unknown function (DUF3391); pfam11871"
                     /db_xref="CDD:432148"
     Region          <96..337
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 maliqasieq lrvghyihlp tgwtshpfmf nafkikdqqq ldiirhldlt llmvdpdksd
       61 lpvepllrae pvpslemsdt gdtapssegp tfdekafrrs lriadkafgq slsdlrdalg
      121 alnlkpdegl antaqivrst aarlaehqgp lglhlirnqn tdtllqhsls vafiamlvar
      181 elgmnpveie etglaglihd igelripsqi iqkrgelska eqnflnmhpq yglvmlnqlq
      241 afeprireva ylhherldgs gfplgikgdk ipplarligl vdhydellhp rsglnppgps
      301 qvigqlykls qkkfeqtqvr llikvlgvyp pgslvrlddd alalvlstep smplrpkvlp
      361 ylkgqrpegv amidlredar sivaplrqee lddaqraffg lgrrvcyyfa f
//
LOCUS       WP_010674334             309 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TerC family protein [unclassified Aeromonas].
ACCESSION   WP_010674334
VERSION     WP_010674334.1
KEYWORDS    RefSeq.
SOURCE      unclassified Aeromonas
  ORGANISM  unclassified Aeromonas
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="unclassified Aeromonas"
                     /db_xref="taxon:257493"
     Protein         1..309
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=34512
     Region          1..306
                     /region_name="R_switched_Alx"
                     /note="integral membrane protein, TerC family; TIGR03718"
                     /db_xref="CDD:274743"
ORIGIN      
        1 mwtgffsivl vllwidirfv gggkahkvsl keagiwsliw vsvallfnla iwlwldhsag
       61 reianqkgle fltgylieka lavdnvfvwl mlfgyfaipa elqrrvllyg vlgaivmrag
      121 mvfagswlie qfhwilylfg afllltgakm lwaadkepdl ennallgwmr rrfkvtetle
      181 gekffvwrdg vryatpllli lvlvevsdli favdsipaif avttdpfivl tsnifaimgl
      241 ramyfllagv adrfallkyg lalilmfigv kmllldifki ptgialgvva lillasmgls
      301 llmtrkkaa
//
LOCUS       WP_010674451             309 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit alpha/FixB
            family protein [Aeromonas].
ACCESSION   WP_010674451
VERSION     WP_010674451.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..309
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32090
     Region          2..309
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 msvlviaehh qgriadnlaq lvtaagrlgg evhllllgqg lteageqaaa ltgvnrvlla
       61 ehpmlaegln dgvdrllaev ardyqhclma assqgkdllp rvaarlgvem iaevtgiegp
      121 dtflrpiyag naiarvassa pvkvltvrpt afakagsgee ralmeslpva evrcrtrlie
      181 rravrsarpe lgaarvvvsg gralgskehf alidaladkl gaavgasraa vdagyvsndl
      241 qvgqtgkvva pelyiavgis gaiqhlagmk eskvivaink daeapifqva dyglvgdlft
      301 llpeltakl
//
LOCUS       WP_010674594             503 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [Aeromonas].
ACCESSION   WP_010674594
VERSION     WP_010674594.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..503
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54080
     Region          11..487
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(68,70,74,77,81,114,117..118,127..134,139,142,145,
                     238,242,245,248,250,423,425..426,428..429,432,435..436,
                     438,440..443,452,456,458,472,479..484,486..487)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(154..157,165,180,183,213,230..233,236,254..256,288,
                     388,390,416)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(157,254,285,288)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 msqhhtqygd lplyiggeac psasdewiev tdpadqhlla rvpkatsaei elavraahda
       61 yllwrevpap erarvmfnyq hllkvhhdel atllaqetgk nladakgdvw rgievveqac
      121 giasqtlget mgnvarrvdg hswvqplgvc vgitpfnfpa miplwmfpla vacgngfvlk
      181 pseqdpltpm rlaelfteag aprgilsvvh ggaeqvdall ahpdvkavsf vgsarvgghv
      241 yrsatsqlkr aqcfvgaknh mvimpdanka qvlgnlvgag vgaagqrcma isvavfvgsa
      301 rewipelaae fakvkpgvwh dpeaaygpli speakvrveg lieagiaega eclldgrfcd
      361 vpgypvgnwv gptlfrgvtp emriykeeif gpvlaclevg sldealalin anpygngtsl
      421 ftgcgaaark frhevavgqv ginvpipvpl pffsftgwrg sfygdlhayg kqavrfytet
      481 ktvterwfde dipsgpnmti qlr
//
LOCUS       WP_010674626             292 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Aeromonas].
ACCESSION   WP_010674626
VERSION     WP_010674626.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..292
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31862
     Region          11..266
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtqqwqrias rltdvggipv araipvkerr tigpwcfldh igptrfapga pgmdvgphph
       61 ialqtftwml egeilhrdsl gskqvirpgq vnlmtagrgi ahteesvpnq pdlhaaqlwi
      121 alpeadqhtp prfdhyptlp rwqqgeitlt lligehgsrr aptlhfspil gldlhapegg
      181 eitlpldpaf ehglfplage tivagealap eqllylppgn revaltlrpg arllliggep
      241 lpkplqiwwn fvsvdkeair taaadwesgh prfgevtgyq gprlkapplt gl
//
LOCUS       WP_010674674             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Aeromonas].
ACCESSION   WP_010674674
VERSION     WP_010674674.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28439
     Region          1..249
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mleisrlsls lgqqtllrdl sltlhpgqvh viigpngtgk tslmrtlfge ltpdsgdirl
       61 gdqsarqmtq arwrqqfgym pqniqleldl svievvvlgr ldslsmrlad edilaagral
      121 qalgiahlad rplyslsggq rqmvlfaqvl lrdprimmld epvsaldlhh qmqlmehlcq
      181 qtreqqwitl vvlhdlnlaa qfadqlivla ggdlqafgpp arvldaalie rlyqvpveis
      241 hdqhgipflr tlrkts
//
LOCUS       WP_010674711             293 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Aeromonas].
ACCESSION   WP_010674711
VERSION     WP_010674711.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31402
     Region          12..283
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkrvigiysa prqhwvgdgf pvrslfsyqt hgralspfll ldragpahfe padhargvge
       61 hphrgfetvt ivyegevahr dstgqggiig pgdvqwmtaa agimhdefhs qgftrrggtl
      121 dmvqlwvnlp akhkmstpgy qgitsdtipq lslkegdvrv riiagndagl qqgevagpar
      181 tfspmniwdl rlkggasvvl pavagwnsal vvlkgsliin gqerageaql vlldpngeef
      241 mleaegeasl lllsgepide pivgygpfvm nseaeihqai ddfnsgrfav iap
//
LOCUS       WP_010674796             416 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator [Aeromonas].
ACCESSION   WP_010674796
VERSION     WP_010674796.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..416
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=45981
     Region          120..230
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 miitdeelma llesddsqep tfypvsvyal davshlavkg aglpayanlh rtrpdagwqw
       61 eglfaagaia lfdpashqga dylphllapg agiyrlsdpw leglqareqg wrawlaqcqi
      121 llledhpfqg aciqqeiqgl glpchwvqdg egclkaleeg gvrllicdls laeqdaisll
      181 mshpqyhhsg lpiillsahd qtlidgarrl lhdagfnvla alakplqsdd llrllkmlyl
      241 gpqrqrrlgg lkrtvrswqg eargqlglla daasctlpiw lslsglsphw eplklwleqh
      301 greaseltlv ihrrdhllsq adrfalvlqa slagarlall ldhaqhlpfd lierlplqsl
      361 llgqhllpel eamaadslla rfiqrsrelg ialylddpfn lqdaaqwqdr gvagrw
//
LOCUS       WP_010674904             423 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YeaH/YhbH family protein [Aeromonas].
ACCESSION   WP_010674904
VERSION     WP_010674904.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11148708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..423
                     /product="YeaH/YhbH family protein"
                     /calculated_mol_wt=48746
     Region          13..421
                     /region_name="DUF444"
                     /note="Protein of unknown function (DUF444); pfam04285"
                     /db_xref="CDD:427839"
ORIGIN      
        1 mahfidrrln gknksavnrq rfirrykkqi kqavsdavsk rsiqdvdkge sisiptkdig
       61 ephfhqghgg kremvhpgnd qfvsgdkidr pkgggggqgs gegqasdqge gvddfvfqis
      121 kdeyldllfe dlelprlqkt qlnqlmemkt yragytsngv paninvvrsl qnslarrmal
      181 qagkkrqlre leerlaqlac epndhfaema qlekeirelk rridavpfid tfdlkfnnfv
      241 krpvpssqav mfclmdvsgs mdqatkemak rfyillylfl srtyknvevv yirhhtqake
      301 vdeheffysq etggtivssa lkmmndiine rypanqwniy aaqasdgdnw addspqcrei
      361 lmrdimprvr yysyieittr ahqtlwheye avaeqyahfa mehirkvedi ypvfrelfkk
      421 qaa
//
LOCUS       WP_010674953             212 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [Aeromonas].
ACCESSION   WP_010674953
VERSION     WP_010674953.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..212
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=22169
     Region          2..212
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mkialigasg fvgsailqea vsrghqvtai vrdvskvaah pqvtavavda qdsqalakvl
       61 kghdrvisay npgwsatdiy dqylkgasai vaaandagsw llvvggagsl eiapgvqlvd
      121 tpefpaewkq galaardglt alrrettldw rfvsppvfle pgekrggyrl gtdqvlfsge
      181 qpagitvgdl adgvlnevqa pahlrqrftl gy
//
LOCUS       WP_010675022             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Aeromonas].
ACCESSION   WP_010675022
VERSION     WP_010675022.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..201
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22242
     Region          30..201
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mennkmatsl wqrgtrallt ltlllgltgc gmntiptlde qvkaswgqve nqyqrradli
       61 pnlvatvkgy asheqetlka vtdararvgs vqvsdpsqlk afeaaqeqls salsrlmvvv
      121 erypdlkadq qfltlqaqle gtenriavar rdyieavrqf nteirtfpgv iwskllysdl
      181 eakptfsakp gadeapkvsf q
//
LOCUS       WP_010675079             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Aeromonas].
ACCESSION   WP_010675079
VERSION     WP_010675079.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..161
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17723
     Region          5..159
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mrpvknricl wydgdaeeaa rfyaslfpds avgavhrapa dypagkkgdv ltvefrvmgi
       61 pclglnggpg vrhnwafsfq vatqdqaetd rywhaiidhg gqasecgwcq dkwgiswqit
      121 pqvlieaisd pdpeaarraf eammqmdkid iatieaarqg e
//
LOCUS       WP_010675092             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein [Aeromonas].
ACCESSION   WP_010675092
VERSION     WP_010675092.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..220
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24940
     Region          1..201
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mielytaatp ngfkvsiale elglpykvip ldfstmeqkk peflainpng ripaivdrdn
       61 gdfavfesga iliylaektg kllpqdpkrr sqaiqwlmfq mggvgpmmgq anvfyryfpe
      121 kipaaieryq kegrrlfevl dghlahheyl adeysiadia twpwvrihdw sgisieglvh
      181 lqawmarmea rpacqkgiti pprnespedq vkraqqmvtr
//
LOCUS       WP_010675093             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein [Aeromonas].
ACCESSION   WP_010675093
VERSION     WP_010675093.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..202
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23148
     Region          1..202
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkvyelrrap narrvrmfla ekgiemeyqq vdlgagenla pafltknpag ripvlelddg
       61 tclsetlaic ryfeelhpep nlfgctaler atiemwsrfi efnlwlpigm afrhitgfyk
      121 drervfpewg eeckqqaqiw fdkldarlae vpyiagerft iadilalcti dfgkvvglri
      181 tpeqphlqdw hdrvsarssa qa
//
LOCUS       WP_010675112             369 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkene reductase [Aeromonas].
ACCESSION   WP_010675112
VERSION     WP_010675112.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..369
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39525
     Region          5..347
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,234,301,321,323..325)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,182,185,187,234,241,301,321,
                     323..324)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,182,185,187,324)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            187
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mhhdplfcpl rlgqlhlanr ivmppmtrsr asqpgdvana mmatyyaqra gagliisegt
       61 qidplgkgya wtpgihsaeq vagwkqvtna vhaeggimfa qlwhvgrvth pdniggaqpl
      121 sssaiqakgv kvfvdngsda pgfvetvtpr amtqadidav vgqfrqaarn ameagfdgie
      181 lhaangylin qfldsesntr tdgyggslen rlrflkevte avcdeigpdr vgvrlapltt
      241 lngtvdanpq etylaaarll gqlgvvylhv aeadwddapl maesfkqglr dafpntliya
      301 gkydgerara aieagwadmi gfgrpfvanp dlpnrlrhgh pfaphdpatl fgggekgltd
      361 ypvygaera
//
LOCUS       WP_010675116             122 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Aeromonas].
ACCESSION   WP_010675116
VERSION     WP_010675116.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..122
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13731
     Region          10..117
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mkslndwill dkhtvsptpl mpaperirag tpsqtawnhy sdpsqqfhvg fwacepgcwa
       61 vhyteheycq mlegeavihd eqggrlhlkp gvqfvipagf vgqwetltpc rklyvifepd
      121 as
//
LOCUS       WP_010675174             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: O-methyltransferase [Aeromonas].
ACCESSION   WP_010675174
VERSION     WP_010675174.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..192
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21451
     Region          33..192
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 maleqlkrel erfgeqndga qhsrgskmln itrdtgella vlvqtrgaqa vleigtsngy
       61 stlwlaeavk rlggrvttie ldegkrtmaa tnferagltp wieqlageag sllpclptag
      121 yqlifldser rhyqawwpei qrllaprgll vvdnaished emrewmaqvr rdpdfltslv
      181 pvgkgewlvv rl
//
LOCUS       WP_010675180             216 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Aeromonas].
ACCESSION   WP_010675180
VERSION     WP_010675180.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..216
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23721
     Region          19..216
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mqdmllaiwh qdfdqliqmq aigllvtclv vilflessfv flplpgdslv llagglvgmg
       61 vlgpevtlly lplaagigsv laywqgqalh gtrfmghver mipegslpra srlldrygfw
      121 amfvsrfipf vrvltpmlmg vsrlhllrva vasfasaflw slvlsmvgkm vmatpvfahh
      181 qelltkcllv tsfglfviav aaigmrllkr pskrvr
//
LOCUS       WP_010675249             459 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkaline phosphatase [Aeromonas].
ACCESSION   WP_010675249
VERSION     WP_010675249.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..459
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47788
     Region          5..459
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mnitmkktlv ctallgtlgg lsqahaadak nvilfigdgm gptvltatrl fkvgeegdle
       61 mmklpqsari ktfshdaqtt dsapsmaayt tgvkmnnevi amssdtrava pskdangnkg
      121 innctsdngs pvptllelak aagksvgavt ttelthatpa atyshichrd aayaiaeqav
      181 pggagfnqal gdgvdvlmgg ganhwtpysa snkggradgr dltaeltarg yryvttkdel
      241 savnsgkvlg lfstkshldy eldrvakgaa stqpslsemt akaidllsqn sqgyflmveg
      301 gridhalhat nakrsltdav aldeavktal gkvdlsdtli vvtadhdhtm tingysakgn
      361 kvldlvknad gstqndadgk pfttlvfgng pnrqdqrptl tsdevmaddy lqetgvklgs
      421 ethgggdvml faggagssqf kgtldntrvf gklrealgl
//
LOCUS       WP_010675318            1286 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Aeromonas caviae].
ACCESSION   WP_010675318
VERSION     WP_010675318.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 1286)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1286)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1286
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..1286
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=143181
     Region          <212..766
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          601..1267
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 msaftlssdc hallcelqlq raastrylqd tlhgqhsltd tlnrlerlgl irqrteqqws
       61 ltaegtltli lavrsgacsm pdwrrgpsvt gqevaqgvvl elclgeagqi payyqsaell
      121 slldlpdahr llpgsspawq tlllehfalq tlldaepeas wplaslvtpc apalaarvea
      181 latewewlcg pltgevtthw pslqqlaare deqplaerlq ralgqwqvqg gagswprmfs
      241 allwlgwlqq adpvqgseqr kkwqrslgng splladllgq wagdrhgqav glfdtlqlpl
      301 eelhwgylwl dlcalarhge qspqvtilhk wdlshlleae prhrlmafcq dllrlllgqg
      361 avraplhslr aspldedeeg aqgeegkapa saswlnwlqg lgrssgvrkp qerlvwllha
      421 egpeleckiq kqstkgewta grrvdpalls tqyanlldea dwalvrtlqr nmgklpreaw
      481 rpladhprlf nakgqklqla isapllqivp eegahdpaaq gagmkallsp aaaargahiv
      541 plaqdlwqli ltpqalldrl paleaipalp pagldelqrt ldaipdlpwh sqvaglkgna
      601 elapwpgips vqldwqegql vvqlvtregd lpplplgkge amvrqgirey hywqrdlaae
      661 kaeaqrlrnq lpiglpgnew kldgeqaltl vnalpelvda gvvvhwhqds arlksldeaa
      721 lslrierrqd wfqvegalal dehqildlrl ilrqltpgqr tvqldektsl mlsdklverl
      781 tmlgamldte qrinnklayp larllsavtt agddawhdlq qewqqeveca pelltalrdy
      841 qkegvrwmat lahhgfgacl addmglgktl qalmvlrmrq hlgpalvvvp ksvvtnwqee
      901 varfapelev vvfehpaera tliqeakagq iilvnygmlg slsqalksrh wasmvldeaq
      961 qiknagtqra kllfqldgdf rlalsgtpie nhlgelwslf tfinpgllgs lsefkrrfgk
     1021 avkdprhmam lravispfil rrlkqqvlte lpdkteiihh islspeerql yeatrrevvq
     1081 qvqsadgral mhvlsgltrl rrlccspqlv mpewsqtssk ldeamnllee aidgghrvlv
     1141 fsqfvdllsl lrsrieqrqw dycyldggcs aksrqesilr frheavplfl islkaggtgl
     1201 nltqadtvlh ldpwwnpave dqasdrahrm gqtqpvtvyr lvceqtveek ivalhdekra
     1261 ladgllsgqs evkgldvesl rallms
//
LOCUS       WP_010675377             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Aeromonas].
ACCESSION   WP_010675377
VERSION     WP_010675377.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..197
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22082
     Region          91..184
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mdkhqlltde elamlrdlgn dediatsqyl rgplplplqs llqrakpltl eariagyqlr
       61 fplhctqaee ghaelriaap titelgsphl rawrldekav lctedaeyev yslslggliv
      121 aglpdafakg dplggylrie dlpplamtgt lvrhvdanph rhdwavqfrl gkedqeqlrd
      181 wlfqrhqdaf vqayqgd
//
LOCUS       WP_010673810             444 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MATE family efflux transporter [Aeromonas].
ACCESSION   WP_010673810
VERSION     WP_010673810.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Kaatz,G.W., DeMarco,C.E. and Seo,S.M.
  TITLE     MepR, a repressor of the Staphylococcus aureus MATE family
            multidrug efflux pump MepA, is a substrate-responsive regulatory
            protein
  JOURNAL   Antimicrob Agents Chemother 50 (4), 1276-1281 (2006)
   PUBMED   16569840
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..444
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47695
     Region          10..432
                     /region_name="MATE_MepA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Streptococcus
                     aureus MepA; cd13143"
                     /db_xref="CDD:240548"
ORIGIN      
        1 mssvdlgtap lsrlflryvt ptvaamlvtg iyvtidgifv ghilgqdgla gmmlaypica
       61 vlyavgalig mgssslasfy lgkgeqarar hivgnalvmv liasallafi girygkamlv
      121 wmgaqgvifd agfaylqwya wlgvfavlsm aftallrndg rpglttwilv gggvlnvlld
      181 yllmavipwg lagaaiatml sqavtgglcl whfftprsql rirwdtlvpd wrlmgetlrl
      241 gvssflmyly lsvvlalhnk allsvgtslh vaaygvisys eaffylifeg iamgiqpias
      301 fnagagnwsr vlrvrnlalg vtmavalcgm iplylwpeav vylfagdnaa llpvaslgiw
      361 lyfwglpmeg lllvgatyfq ainrariasl ltggklvlig gflwgfsslw gvagvwlalp
      421 tcstllvlvm wrvmnregrq hsaa
//
LOCUS       WP_010675457             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Aeromonas].
ACCESSION   WP_010675457
VERSION     WP_010675457.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15739
     Region          3..141
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mptiksllcp vdfsemsrav ldyavfmant hqaelklvhv vdqlhgfdsy kilhmtaiei
       61 themerqaks qlkelvaclp ipakfevrfg raadeivlqa kedkvdlvvm gshgrsgish
      121 llvgsvaesv vrhapcpvlv vrk
//
LOCUS       WP_010675551             468 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Aeromonas].
ACCESSION   WP_010675551
VERSION     WP_010675551.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13387252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..468
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51226
     Region          <18..242
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
     Region          132..454
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mtakfikslc pcllgvvlgs aqaqtvsfte awsrviqqdd glaaeqagve raqqlreaak
       61 amylpkvdvg asythldqpm eldmldlnpi anhpefgkvl gpvmqalnls psdfvtpltk
      121 qnvvtssvkm lwplftggri daaqdirqaq vseaeqllvl kqqstfesls qtyfgvvlaa
      181 qvvqtkqeie qglahhldha kkleaqgqia kverlsaqsa ydraridtqk arrsleiaql
      241 alghmlklkq aepntalfin egmpalspfv eetlsvhpgl klltakkeqa qgmiklekgk
      301 yapelflfgn ynlyeddsiv skttpdwlvg vgvsmplvsr dgrsetvqaa ksaelqvnll
      361 qaktrqdlel lvektwreaa qgleeyhsls stqalaeenv rlrdkafgqg lstsldvvda
      421 qtqlagvktq raaaayqyvi slarllalsg qmnsfnqyqh gqaievns
//
LOCUS       WP_010675618             147 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GatB/YqeY domain-containing protein [Aeromonas].
ACCESSION   WP_010675618
VERSION     WP_010675618.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..147
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16039
     Region          1..147
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslkdqlkdq qklamlakdk prlgairllm aeikqrevdt rvelndeeil avvtkmvkqr
       61 rdsisqfeaa grqdladkes aeivvlqefl pqqltadeia alieqaites gaavmadmgk
      121 vmavlkpkiq gradvgavsa qvktrla
//
LOCUS       WP_010675588             415 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Aeromonas].
ACCESSION   WP_010675588
VERSION     WP_010675588.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 415)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..415
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44413
     Region          16..228
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          137..411
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mlklalqslw arrltagltl lavaisvtll lgvervrsqa rdsfantvsg tdlivgarsg
       61 qvnlllysvf rignptnnvg wdsyqaikar pgiawtipls lgdshkgfrv lgtngdyfth
      121 lkygkqqalv lregrpfetp feavlgaqva eklgyhldqs iviahgagnt sfsqhdnmpf
      181 kvvgilaptg tpidrtihvp lagieaihlg wdtgrhsknv tpeqamaqdl tpktitafmv
      241 glsnrilafq lqrsvntypr eplmailpga alqelwglms vaetalsvia gfvvvaglig
      301 mlttllagln errrelailr slgagpahlf lllaleamal ttagialgva alylgqglas
      361 pwllshyglq mslglpsaye wqllglvwla gmvigllpaa rayryslsdg msirv
//
LOCUS       WP_010675697             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Aeromonas].
ACCESSION   WP_010675697
VERSION     WP_010675697.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..155
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17133
     Region          2..155
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 mseysatisw qrgehepfvd qrysrahewa fdggvrvpas ssphvvplpy svaehvdpee
       61 afvaalssch mltflwlaak agyrvesyrd eavgimakng qgrlamtrvt lrprvifgge
      121 qepaladleq lhhqaheecf iansvntvvt teivi
//
LOCUS       WP_010675715             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Aeromonas].
ACCESSION   WP_010675715
VERSION     WP_010675715.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29574
     Region          57..261
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          200..256
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mppspatdtl sltaavdalh gsgfpaalvr liqqqvafdc alllgvglrp vylydnlhhq
       61 rallfdrylt rhfsqdpfmq aleqglgagv wtlaqvsrgr ldpeyrhhfy qatgwqeevg
      121 lilpvrgglt lmlflgrldk rsslsrdela rlealfplvh slcrqhwree tprlarspar
      181 sdgtdlkgav eqaiasvggd qltrrerqva glllqgldte aiadalgigs gtvknhrkhl
      241 yaklnlhsra elfsfflnhl itapagapp
//
LOCUS       WP_010675737             421 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: inorganic phosphate transporter [Aeromonas].
ACCESSION   WP_010675737
VERSION     WP_010675737.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10475700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..421
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43446
     Region          27..409
                     /region_name="PHO4"
                     /note="Phosphate transporter family; pfam01384"
                     /db_xref="CDD:460184"
ORIGIN      
        1 mdiianygtt lvlvaalfgf lmawgigand vanamgtsvg tksltirqai iiamifefag
       61 aylaggevta tirsgiidsn afadtpdllv lgmiasllaa glwlilasyf gwpvstthsi
      121 igaivgfavv sigpeavqwn kfggivgswi itpaisgiia yfmfisvqkl ifntdnpldn
      181 akryvpfymf ltslviclvt ikkglthvgl hlsngegvll svaisiavaf agwiyirgqq
      241 ynpkddskmh fanvekvfgi lmiitacama fahgsndvan aigplsavas ivaaggeigg
      301 sshiawwilp lggigivigl atmgekvmat vgtgithltp srgfaaqlat aatvviasgt
      361 glpisttqtl vgavmgvgla rgiaalnlgv lrnivvswvi tlpagailai aifyvlqacf
      421 s
//
LOCUS       WP_010675783              64 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [Aeromonas].
ACCESSION   WP_010675783
VERSION     WP_010675783.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 64)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 64)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..64
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6581
     Region          1..64
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mtieltvtgm scggcaaslq kallaqpsvr tatvdfasrq avieselska elialikarg
       61 fqve
//
LOCUS       WP_010675789             152 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Aeromonas].
ACCESSION   WP_010675789
VERSION     WP_010675789.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..152
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17241
     Region          3..140
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtdkfdllil aelqqdarlp tpelahrvgl sapacyrrvr alresglier evalvapstm
       61 gwpitmlvlv tlerdhgriv demiaslqre pevmdlwyvt geqdfvlqva ardmqsyeqf
      121 trrvlhardq vrsfktlvvm gqhkrcsall pg
//
LOCUS       WP_010675809             636 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Aeromonas].
ACCESSION   WP_010675809
VERSION     WP_010675809.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..636
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=68657
     Region          107..636
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mfasltlkqk ilatvilava lscllvgyfs qrsaqqlied rmfeqelpnl tqrigkeiek
       61 dltsvanaar qlandrfvld wvergmpkeq esilinqlkd mtsqyglvta sfadrqsaay
      121 ynqdgflril nheqdnwfyd ytksrqdlml sifresngev klfvnfqqld grglaglaks
      181 ldsmvsmlan frigdsgfvf mtdgsgkvkl hpdaaridrd nltqlasgss tnllnkqpfa
      241 atraevdgqp vilassyipl ldwylvaqvp eaeiyaeldr arlhmvlvsl aiavgmgllg
      301 vllagsvsrp lnelarlfre lgsgdgdlth rlkvdgrdel aqvatgfnnf vakihgsieq
      361 vasnsrqlaa tanevaakaq ltqhnctaqr drtvqvatai hemgatvsei agnaslaadv
      421 akqaneqada gaqvvaqarh givglsgeie qvagviesla sqtdsigsil dtirsiseqt
      481 nllalnaaie aarageqgrg favvadevrn lasrsaasta eiqgminslq eqsaravsam
      541 aqgrnqslrv vtqadeanga ldqitghitq isdmniqvat ateeqssvvg einrnvedin
      601 qltmetadia hqltessrsl qqlsgeldkl vgnfrl
//
LOCUS       WP_010675893             805 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S8 family peptidase [Aeromonas].
ACCESSION   WP_010675893
VERSION     WP_010675893.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10141191
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..805
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=89768
     Region          256..571
                     /region_name="Peptidases_S8_Subtilisin_like_2"
                     /note="Peptidase S8 family domain in Subtilisin-like
                     proteins; cd04847"
                     /db_xref="CDD:173793"
     Site            order(261,293,351,366,402,537)
                     /site_type="active"
                     /db_xref="CDD:173793"
     Site            order(261,293,537)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173793"
ORIGIN      
        1 matykhlsit reildnqrrt knpprfvtrt dlrghgqkln ayfatavgqa rkqigssvda
       61 pfvlklkyeg altfdkltvh glefisqenk qlcvvfatev glaqfadhld klglldahlt
      121 ykqileaieg ieawsaedrm swaithiglp qdkeykldve lwpvevanhp nriklitafe
      181 rwldgagikr ldkinldsll myrvtvspdq aqlllnhrdv rivdlipatg isvqqlsrdi
      241 ntlpldvpap algasricil dsginsnhpl irpamaesas fvddegeadq aghgtavagv
      301 alygdveacn esnfwqpqfw iyngkvmkkc phtgnavyne htldasltra vehfvelgcr
      361 ifnlslgnsn apydgmhvrg layildvlsr rhnilfvvst gnfcgsespa ipanswrdey
      421 peyllaeqss iidpapamsa ltvgsiarhn atldaqrhpe isqlspasen qpspftrhgp
      481 svkgafkpdl vaiggnlacp mriqdgqwrq vdkglgvltf nhefigntif kevsgtslaa
      541 pyithlagrl lneypessan llramlvnra elpnevastf skqiqddykk nkntynreva
      601 rdvagygvvn egdlfrssdh avvliseqti ekdscqffel plpadflrks kgtreltvtl
      661 ayspavrttr aeylatqisy rlvkgaslde vqrhfnqknk adtetrndda qsnrnisaqq
      721 rsrgtvqssr wtfkkrnpde kwfvvvirqd rewnhpdvld aepyalvvtv adrenenaql
      781 ytqiqaliaq qtvvrqqaar lqtrn
//
LOCUS       WP_010675909             130 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Aeromonas].
ACCESSION   WP_010675909
VERSION     WP_010675909.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..130
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13663
     Region          1..130
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mdkmkdvall vgrvllalmf vmagwgkigg yagtqgymea mgvpgfmlpl villelgggl
       61 aimlglftrs lsvllagftl maafifhyqp aeqmqmlmfm knvsvaggfl alaaagagaf
      121 sldarlgkhw
//
LOCUS       WP_010675918             258 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Aeromonas caviae].
ACCESSION   WP_010675918
VERSION     WP_010675918.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..258
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28693
     Region          30..256
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mhdltprwpr wvlgalvatl llpllatfly sistrwgatl lpdgftldwy lklwgdprfl
       61 aafgrsllvc fatlllgtlv lvptvlvvay yfprldpwmn llillpfavp pvvssvgllq
      121 iyadgvlpii gtpwiligtw ftvvlpfmyr alanslqgvp lqdlmdaahl lgassarafl
      181 lvvipclrkg llaalflsls fllgefvfan mlvgtryetl qvylynmrat sghftsalvm
      241 syflltlllt waanrfhr
//
LOCUS       WP_010675934             234 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [Aeromonas].
ACCESSION   WP_010675934
VERSION     WP_010675934.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..234
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25096
     Region          9..231
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mnelratral isggasgigl aiaealasqg velilasrrl glleqeaarl earygvrvma
       61 laldvcdgdq vrdgharire rlgpvdllin nsgvgsdhlv qdlpesewdr vmdtcakgtf
      121 lltraclpdm lanrhgtvin iasqaarhgy arasvycaak favlgfaral reevqhqgir
      181 vhtlcpglvq vpppacaadr kpgwlqvedl aeavlytlrq pphvqldeig mtgi
//
LOCUS       WP_010676033             306 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Aeromonas].
ACCESSION   WP_010676033
VERSION     WP_010676033.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32979
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..293
                     /region_name="PBP2_DntR_like_1"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     similar to DntR, which is involved in the catabolism of
                     dinitrotoluene; contains the type 2 periplasmic binding
                     fold; cd08460"
                     /db_xref="CDD:176149"
     Site            order(101,103..104,108,166,203,268)
                     /site_type="other"
                     /note="putative substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:176149"
     Site            order(102,105..106,109..110,113..114,116..117,120..121,
                     123..127,129,192,220..224,227..228,231..232,235,249)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176149"
ORIGIN      
        1 mtpdfnllit ldalleegsv agaarrlgls asamsralar lrettgdpll vragrglipt
       61 praqilrdev arlvqetrav lrpqqevdpa slertfrlrs sdgfveavgp allarlavea
      121 pgvrlhflak pdkesgplrr geldfetgvi gattapelrt qalfqdhfva vvhpdhplcd
      181 gtltvaryaa arhvlvsrrg qphspideil agqgrrrtit tlvpgfatal alvresnlva
      241 tvphlhcasl lgdlvtlplp falpgirval lwhpsqdadp ghrwlralir dtcarppyht
      301 gatdtp
//
LOCUS       WP_010676453             280 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Bacillus timonensis].
ACCESSION   WP_010676453
VERSION     WP_010676453.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..280
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30670
     Region          1..279
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkllyvlli gllaftlaac gsndnadkgt dtkeaegnke livgasavph aqvleqakpl
       61 lkekgidlki evftdyilpn valhekelda nyfqtpgyld lqlkdnpdfd fvsiaeihke
      121 pigiyskkyk nlnelpdgak iimsnsfsdh grilpifere gliklkegvg dqarvedive
      181 npknldfsnl ieakllasaf qngegdavvi ntnyaleggv nieedgiafe gedvvpanlv
      241 vvnkgdedre eikalvevlk seeiqkfiee eyagavisvk
//
LOCUS       WP_010676455             341 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Bacillus
            timonensis].
ACCESSION   WP_010676455
VERSION     WP_010676455.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..341
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37936
     Region          1..338
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mitlknvkki yqtktnsvta vnnvdlqine geifgiigys gagksslirl lngletpteg
       61 tvsvaghdit sikgkalrda rkeismifqh fnllwsrtvr enisfpleia nvpktkrdqr
      121 vteliklvgl egredaypsq lsggqkqrvg iaralannpk vllcdeatsa ldpqttdsil
      181 dllvdinerl gltivlithe mhvirkichr vavmengkfv eqgrvldvfk kpqanitkrf
      241 vqqvtepeet ketiehlldr fpngkvvqlt fvgedaekpl ithlirdfkv evnilqgkis
      301 qtqngsygtl fihlagdine vtsaiefirq qrveaevien a
//
LOCUS       WP_010676458             101 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Bacillus timonensis].
ACCESSION   WP_010676458
VERSION     WP_010676458.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..101
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11566
     Region          21..98
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(28,31)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkewnandin tqlitedefw lylytpmcgt cqvaskmimv vdellpnvli gksdlnylpq
       61 kaiewqiesv pcllhvkdgk vsqkfyafhs vpylvevltk q
//
LOCUS       WP_010676481             456 aa            linear   BCT 01-JAN-2025
DEFINITION  S8 family peptidase [Bacillus timonensis].
ACCESSION   WP_010676481
VERSION     WP_010676481.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..456
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=50051
     Region          168..428
                     /region_name="Peptidases_S8_Thermitase_like"
                     /note="Peptidase S8 family domain in Thermitase-like
                     proteins; cd07484"
                     /db_xref="CDD:173810"
     Site            order(204,237,300..301,388,391)
                     /site_type="active"
                     /db_xref="CDD:173810"
     Site            order(204,237,391)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173810"
ORIGIN      
        1 mwnkkriaiv alaitigltl fvsfslfdng aqdkskmsst pnapiqlgne tidtspqimn
       61 vdsihlynkv qkqldtheei dvidhngkdk shyhhhqviv dfkkhltqae inqiekdidg
      121 kllrkldsty ifesdnmktp emisyfdkrk dvefaepnyi lmqnqqhpnd llyndfqwnl
      181 rmidsengwg itqgsdkvki aivdtgvdld hpdlvnrisg gynilkdnnv pdddnghgth
      241 vagiiasqtn nhqgtagltw fnpimpvkvm gadgygstfd iargiiwatd hgadvinlsl
      301 gnyqgskllk qavdyayrhd vvmvaasgnd nssqpsypsa ypqvlsvaav dlngekadfs
      361 nygdyidiaa pgvtipstyi deqyaalsgt smaaphvaal aalmrsinpn lsnkeimdii
      421 kgtsldlgka gkdiyfgegl idivqalqqa kqgkas
//
LOCUS       WP_010676489             321 aa            linear   BCT 01-JAN-2025
DEFINITION  ring-cleaving dioxygenase [Bacillus timonensis].
ACCESSION   WP_010676489
VERSION     WP_010676489.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10327061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..321
                     /product="ring-cleaving dioxygenase"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35581
     Region          5..129
                     /region_name="VOC"
                     /note="vicinal oxygen chelate (VOC) family; cl14632"
                     /db_xref="CDD:472697"
     Region          156..319
                     /region_name="PcpA_C_like"
                     /note="C-terminal domain of Sphingobium chlorophenolicum
                     2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and
                     similar proteins; cd08347"
                     /db_xref="CDD:319935"
ORIGIN      
        1 mqliglhhvs lltgkaernf efytkilglr likktvnqdn tqsyhlfygd akgnpgteit
       61 ffdipglgrt hpgvssisst slrvkttdsl hfwkqrladf gisseeitkr agrdtlafqd
      121 fegtrlilvg dngeagiaan epwviegipt ehailglgpv tltvstadpt ikiitdvmgf
      181 rkvgsypslt gdfpdvlvfa tgeggtgael hietrpdlpk erlgrggvhh vafripnede
      241 yeqwftkikq trlpnsgkvd ryyfkalyfr epngilfels tdtpgfdvde pletlgerla
      301 lppflepkrs eieanlrple i
//
LOCUS       WP_010675974             217 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: protein-methionine-sulfoxide reductase heme-binding
            subunit MsrQ [Aeromonas].
ACCESSION   WP_010675974
VERSION     WP_010675974.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Gennaris,A., Ezraty,B., Henry,C., Agrebi,R., Vergnes,A., Oheix,E.,
            Bos,J., Leverrier,P., Espinosa,L., Szewczyk,J., Vertommen,D.,
            Iranzo,O., Collet,J.F. and Barras,F.
  TITLE     Repairing oxidized proteins in the bacterial envelope using
            respiratory chain electrons
  JOURNAL   Nature 528 (7582), 409-412 (2015)
   PUBMED   26641313
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..217
                     /product="protein-methionine-sulfoxide reductase
                     heme-binding subunit MsrQ"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016679 - oxidoreductase activity, acting
                     on diphenols and related substances as donors [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /calculated_mol_wt=24280
     Region          3..207
                     /region_name="PRK05419"
                     /note="protein-methionine-sulfoxide reductase heme-binding
                     subunit MsrQ"
                     /db_xref="CDD:235452"
ORIGIN      
        1 mtprlktahi nglralvhlg slgfllwlgy avpagllggd pvqglthylg kgalhllllt
       61 llvsplakrw rqgqliklrr plglwcaawa slhfmvwlgl dlqfdwglig gelvkrsyiv
      121 vgmvalllll alsitsipal lrrmgpawqk lhnwiygval lvpihywwsv ksgwqepliy
      181 lvlacallwp rrekllrpwr rraqvagrga aqqpsrp
//
LOCUS       WP_010676528             258 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Bacillus timonensis].
ACCESSION   WP_010676528
VERSION     WP_010676528.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..258
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28172
     Region          12..252
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mdtiqyisnd qhigivylnr ppynplssqv ynelftlfee lekdsevrai iltgkgdraf
       61 aagadinemv nldgvdmmem srisrlaydk iesiskpvia avnglalggg celalacdfr
      121 igspttkfgl peinlgiipg gggtqrlprl igqakakell yfgemidaek alevglvnkv
      181 vesenvldea iewaeklaqk prvamkmlkt sinrgkevdl qaaldletac fgnafasqdr
      241 vegmrsfvek rkpqfvgk
//
LOCUS       WP_010676529             285 aa            linear   BCT 01-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Bacillus
            timonensis].
ACCESSION   WP_010676529
VERSION     WP_010676529.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..285
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=31211
     Region          2..283
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mefnqigvig sgtmggaiah qaaicgfnvv lvdvdqrfld saqarmeklm drsiskgklt
       61 eddksailsr iklttsmadv gdcdavieai iedldakkei fqqldeilkp galiasntss
      121 msitvlasst nrpeqvagmh ffnppqvmkl vevirgykts detvsafkel aiamkkepie
      181 vkkdvpgfiv nrilipqfie airlveegva tpedidkavt lglnypmgpf tlqdyagvdi
      241 glhvmdyfye efkdqrfaap ltlrnlvrag rvgkkagagw ydynn
//
LOCUS       WP_010676585             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Bacillus timonensis].
ACCESSION   WP_010676585
VERSION     WP_010676585.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34411
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdnitieelk ilkrvmetnn itqtatelyi nqstiskmik rvenqnniqi fnrkrgfslt
       61 negeifysyi mdllktwksl ehhiseqntn yiskihiglp piigsflfpk iitsfidtyp
      121 fieniiyesg glkieedllk gdidvgfavl ptknsslksh iiyqdvfvic vsekhvlaky
      181 deidfvdlkn erficfsndf mihqyflkmc eisafepnii lnssqwdlii elvgvnfgis
      241 iipriliskf egknikeiki skpklpweig iiysdanyls iaaknfieia kktyypli
//
LOCUS       WP_010676601             263 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus timonensis].
ACCESSION   WP_010676601
VERSION     WP_010676601.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..263
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29161
     Region          3..249
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mklqvenlny slneksiied mnlhvsegef igiigpngsg kstllkniyr arkpdsgvvf
       61 idgdnidkmn skkvamkigv vgqeqvipfd fkveeiiamg rspykgfftg dsakdkeiva
      121 naikhigmtd mekrnysnls ggekqrvllg rvlaqqtdll lldeptnhld iqhqlqifdl
      181 ikglgvtvis aihdlnlaal ycdrlyvvkd grmlragtpe evltpesiye iygvrtdvni
      241 hpatkkvtvt ylpvsllypd eae
//
LOCUS       WP_010676605             151 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Bacillus timonensis].
ACCESSION   WP_010676605
VERSION     WP_010676605.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 151)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..151
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16548
     Region          7..136
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04677"
                     /db_xref="CDD:467560"
ORIGIN      
        1 mgyiedlrki vgsrplnlvg tavgvlnqkg eillqqrlng vwgvpggfle lgestedagr
       61 revleetglq igklelvgvf sgkehfvtlp ngdefypiti ayvtkeilgg elevnkeegl
      121 daqffglyql peninplipn vlhtylqtrk v
//
LOCUS       WP_010676686             413 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bacillus timonensis].
ACCESSION   WP_010676686
VERSION     WP_010676686.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..413
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45181
     Region          25..392
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(25..26,29,61,111..112,114..116,119,139,142..143,146,
                     226,229..230,233..235,238,262,266,319..320,324,328,344,
                     347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mkqiigkwkf pallltglgl sslgdfvylv ainllvlkmt gsaaavaalw vvgpitsilv
       61 ngwsgsiidr snkkkimivt diiravavai ipilpsiwmi yavlfvinvs ksfftptstt
      121 yitvlipkeq rktfnsirsl vssgafitgp aiagmlfvvg sleiaiysna ilfaisaili
      181 aclpnldsgq tqtteklqfk klkedwkevi rfgkkevfvm tiyfsfivfd iftmamdsqe
      241 vvftqrvigl teveysllis vtgigyaagg llvifisrfl sirtligtgl fmlatgyfiy
      301 siassftiaa tgfiilgfff afsntgfttf yqnnvpvemm grvtsiisvl qsavsvvfll
      361 figimgdllp lrytivtlsv ismvlaiivi ilvaqksrkv yfvenqsqki met
//
LOCUS       WP_010675204              75 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FeoA family protein [Aeromonas].
ACCESSION   WP_010675204
VERSION     WP_010675204.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Gomez-Garzon,C., Barrick,J.E. and Payne,S.M.
  TITLE     Disentangling the Evolutionary History of Feo, the Major Ferrous
            Iron Transport System in Bacteria
  JOURNAL   mBio 13 (1), e0351221 (2022)
   PUBMED   35012344
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Lau,C.K., Krewulak,K.D. and Vogel,H.J.
  TITLE     Bacterial ferrous iron transport: the Feo system
  JOURNAL   FEMS Microbiol Rev 40 (2), 273-298 (2016)
   PUBMED   26684538
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Su,Y.C., Chin,K.H., Hung,H.C., Shen,G.H., Wang,A.H. and Chou,S.H.
  TITLE     Structure of Stenotrophomonas maltophilia FeoA complexed with zinc:
            a unique prokaryotic SH3-domain protein that possibly acts as a
            bacterial ferrous iron-transport activating factor
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 6), 636-642
            (2010)
   PUBMED   20516589
REFERENCE   4  (residues 1 to 75)
  AUTHORS   Kammler,M., Schon,C. and Hantke,K.
  TITLE     Characterization of the ferrous iron uptake system of Escherichia
            coli
  JOURNAL   J Bacteriol 175 (19), 6212-6219 (1993)
   PUBMED   8407793
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10512799
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..75
                     /product="FeoA family protein"
                     /GO_function="GO:0046914 - transition metal ion binding
                     [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=8234
     Region          1..74
                     /region_name="FeoA"
                     /note="FeoA domain; pfam04023"
                     /db_xref="CDD:461133"
ORIGIN      
        1 mvltelspgq sarithmnhl gralrrklmv mgllpqteil ylraaplgdp lqiqcqgicl
       61 smqrslaqqi evepv
//
LOCUS       WP_010676364             494 aa            linear   BCT 01-JAN-2025
DEFINITION  aldehyde dehydrogenase family protein [Bacillus timonensis].
ACCESSION   WP_010676364
VERSION     WP_010676364.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..494
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=53471
     Region          21..489
                     /region_name="ALDH_F1-2_Ald2-like"
                     /note="ALDH subfamily: ALDH families 1and 2, including
                     10-formyltetrahydrofolate dehydrogenase, NAD+-dependent
                     retinal dehydrogenase 1 and related proteins; cd07091"
                     /db_xref="CDD:143410"
     Site            order(164..165,167..168,191,194,223..224,228..229,
                     242..245,248,251..252,266..268,300,397,399,425,463)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143410"
     Site            order(168,266,297,300)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143410"
ORIGIN      
        1 msqlifalre kvesflqgtk klyingefve sasgktfesy npatgevlat vseagpedid
       61 ravkaarkaf degpwskmta aqrsrimykl adlmelhkde laqletldng kpiretsnad
      121 iplaiehmry yagwstkivg qtipvngpff nytrheavgv vgqiipwnfp llmamwklga
      181 alatgctvvl kpaeqtplsa lylaelmeea gfpagvvniv pgfgetagqp lvdhplvnki
      241 aftgstevgk gimerasksl krvtlelggk spniilpdad lskaipgaln gvmfnqgqvc
      301 cagsrvfiqk kqfdnvvadm ashaekikqg aglhsdteig plvsieqqnr vlgyiekgln
      361 egaelvvggq kpfeegyfvs ptifanvkde mtiakeeifg pvisampydd ldeliarann
      421 seyglaagvw tqdvakahyi annlragtvw vncynafdaa spfggykqsg igremgsyal
      481 nnytevksvw iamn
//
LOCUS       WP_010676690             143 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Bacillus timonensis].
ACCESSION   WP_010676690
VERSION     WP_010676690.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167397
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..143
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16334
     Region          1..128
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cd07812"
                     /db_xref="CDD:176854"
     Site            order(1,3,5,14..16,18..19,34,40,42,44,46,62,64,66,73,75,
                     90..91,93,95,101,103,105,107,121..125,127..128)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176854"
ORIGIN      
        1 mkqsvvikap itavfetiak anlrekwfpn vtsirysnps ddmktgasfq lmaeegkekv
       61 llngrnkdfi qpsvfafele sqtyrmafsy hlqqqgeltv veqefetkyy rtvmnvidkl
      121 fksstkqtge lvltslkvfc ear
//
LOCUS       WP_010676713             275 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Bacillus timonensis].
ACCESSION   WP_010676713
VERSION     WP_010676713.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Grant Pearce,F., Hudson,A.O., Loomes,K. and Dobson,R.C.J.
  TITLE     Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and
            Evolution
  JOURNAL   Subcell Biochem 83, 271-289 (2017)
   PUBMED   28271480
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Laber,B., Gomis-Ruth,F.X., Romao,M.J. and Huber,R.
  TITLE     Escherichia coli dihydrodipicolinate synthase. Identification of
            the active site and crystallization
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 691-695 (1992)
   PUBMED   1463470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..275
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0009436 - glyoxylate catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31049
     Region          9..272
                     /region_name="DHDPS-like"
                     /note="Dihydrodipicolinate synthase family; cd00408"
                     /db_xref="CDD:188630"
     Site            order(9,41,44..46,136,164)
                     /site_type="inhibition"
                     /note="inhibitor site"
                     /db_xref="CDD:188630"
     Site            order(41,44..46,136,164,206)
                     /site_type="active"
                     /db_xref="CDD:188630"
     Site            order(45,50..51,84..85,109..110,117,121,270..271)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188630"
     Site            164
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188630"
ORIGIN      
        1 mltenihiav ptaffedesl niqgtighir dlykqgirsv lvsgttgeqh slslpekiel
       61 inglereeel vtnmeiifgv ssvrqkeaee lakkihhtki agimlgfppy iiptqeealv
      121 ytrriihlsh kptilynnpr rtgfdlseqs iiqlskidsv vgikdagnke kvtrikhdlg
      181 rndfyfyagg evdleekisy gynrlssmag nvfpteisqw lqkmlmkqki skpeieqiek
      241 mmeqvyqgna ivnlkkilnq kgvpmgtcrs pignr
//
LOCUS       WP_010676720             407 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bacillus timonensis].
ACCESSION   WP_010676720
VERSION     WP_010676720.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..407
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45281
     Region          11..390
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(21..22,25..26,29,61,116..117,119..121,124,144,
                     147..148,151,225,228..229,232..234,237,261,265,317..318,
                     322,326,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msssilknrs fvfiwvgnai selggafgtf snsiliyqlt nstmalgsmw llyfipslil
       61 qlfigpfidr wsrkwtmifs qwmrgliflv plaalglgnl epwhiyavqi ivglitpiyt
      121 panqaitpti vskdqlstan ayrdgtvrlm tflapimggf vveylgvtyt lifvsavlfi
      181 sgilllfiqe trvshnvrrt wveqfvdgis yffkqpiivw lgiflafvqf gvgvtmvitl
      241 pyvtdelsgs iteygyfmas fplgyvigsl ivgkftyksr rvimlgalvi ggltfislgm
      301 nhsiifalft eviagiamaf fsvqnitifq qtvpdhlmgk vssvrlfiir gamplgvfvg
      361 sflgeiwgir pmyfligsvi ctmsllgifl pyfrfidani eekslpn
//
LOCUS       WP_010676762             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MOSC domain-containing protein [Bacillus timonensis].
ACCESSION   WP_010676762
VERSION     WP_010676762.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12233312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..218
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24697
     Region          26..173
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
     Region          171..213
                     /region_name="3-alpha"
                     /note="3-alpha domain; pfam03475"
                     /db_xref="CDD:460938"
ORIGIN      
        1 mtiemknfsi glpkkmtygk neevitgirk qaveeafltk dgfrgdgvad lkhhggpdra
       61 vciypyehys lwqneflvql plptfgenlt ltnmeekdvc igdvfqvgea vmqitqgrip
      121 cstitkrtnn pyllkmmvqt gftgylarvl kegtvrkdsp itlvernpnq vsileaneiy
      181 fkrprdvegi nkilavdela dewkdmlner larltarq
//
LOCUS       WP_010676763             168 aa            linear   BCT 01-JAN-2025
DEFINITION  HXXEE domain-containing protein [Bacillus timonensis].
ACCESSION   WP_010676763
VERSION     WP_010676763.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10618834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..168
                     /product="HXXEE domain-containing protein"
                     /calculated_mol_wt=19053
     Region          14..125
                     /region_name="HXXEE"
                     /note="Protein of unknown function with HXXEE motif;
                     pfam13787"
                     /db_xref="CDD:433480"
ORIGIN      
        1 mmkqsrfhly lilfpllyli hdieeiltve kfliehsdii pfrvttleft vaflllwvla
       61 svgcyqafqg rkflgmkpgt ylsflvpgvi lanavghilp clifkeyvpg iitsifilvp
      121 ysfftarfli tmgevtvkkq ityfvigfaa qmplaflahi vssnivkw
//
LOCUS       WP_010676798             248 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Bacillus
            timonensis].
ACCESSION   WP_010676798
VERSION     WP_010676798.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..248
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27818
     Region          3..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 maiidisnlk ksygqvevlr kisfevnknd vvaiigpsgs gkstllrslv yleevnggsi
       61 rvdgedlvkd gvyskpqkik qitskmgmvf qhfnlfphlt vkenlelapk lvrkesplei
      121 qkrseellek iglanwatsy pstlsggqkq rvaiaralmm npeillfdep tsaldpelte
      181 evlqvmkkla eeqmtmivvt hemgfakeva nkvifmdkge iiesghpdel flhpqhertk
      241 sflyrnlk
//
LOCUS       WP_010676815             645 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Bacillus timonensis].
ACCESSION   WP_010676815
VERSION     WP_010676815.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 645)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 645)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 645)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..645
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72762
     Region          59..180
                     /region_name="FtsX"
                     /note="FtsX-like permease family; pfam02687"
                     /db_xref="CDD:460652"
ORIGIN      
        1 msfkslifrn lvkniknyyl yvfalifsva lyfafvtlqy dpsmdemegt vkggaaikaa
       61 svmligivmv flvyantlfi krrgkeiglf qlvgiskgkt fwilsvenmi lyfgsmmigi
      121 flgfvssklv mmillkiigi eevaglrfst ealvqtvivf vaiyvvimvl nalfikrqqi
      181 lslfhttstt edrkrkvsvl evimgilgla liifgyylst elfsgqfkmm eqmftimvvi
      241 lasviigtyf fykgsirfif nlirkkdngy lsvnkvlsls simfrmksns vlltvittvs
      301 alslgllslt yisyysaeka ageavvndfs ipneerakqf temldakqig ftrteielmt
      361 aktdlsnvle ieqtdmldlt apmtvvsdrf vedidvgend svfvnsnaal qafftfkegt
      421 ftmsgktksf elnfikyenk rliplrltgg gfpvavidds iyqqlvadad pevenefpvy
      481 igvdiekrse lkeanqifnd ldlgqwaghe sqldsftmqk vnmglmmfiv gflgltflit
      541 sgcilyfkqm degeeekgny tilrklgftr ndlvngikak qlfnfgipli vglchsyfav
      601 ksgwfffgte lwtpmiivmv fytllysifg ilsvmyykkl ikeal
//
LOCUS       WP_010676819             376 aa            linear   BCT 01-JAN-2025
DEFINITION  Ger(x)C family spore germination protein [Bacillus timonensis].
ACCESSION   WP_010676819
VERSION     WP_010676819.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Cooper,G.R. and Moir,A.
  TITLE     Amino acid residues in the GerAB protein important in the function
            and assembly of the alanine spore germination receptor of Bacillus
            subtilis 168
  JOURNAL   J Bacteriol 193 (9), 2261-2267 (2011)
   PUBMED   21378181
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Li,Y., Setlow,B., Setlow,P. and Hao,B.
  TITLE     Crystal structure of the GerBC component of a Bacillus subtilis
            spore germinant receptor
  JOURNAL   J Mol Biol 402 (1), 8-16 (2010)
   PUBMED   20654628
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Hudson,K.D., Corfe,B.M., Kemp,E.H., Feavers,I.M., Coote,P.J. and
            Moir,A.
  TITLE     Localization of GerAA and GerAC germination proteins in the
            Bacillus subtilis spore
  JOURNAL   J Bacteriol 183 (14), 4317-4322 (2001)
   PUBMED   11418573
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..376
                     /product="Ger(x)C family spore germination protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=43045
     Region          1..366
                     /region_name="GerAC"
                     /note="Spore germination receptor GerABC, GerC subunit
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG5903"
                     /db_xref="CDD:444605"
ORIGIN      
        1 mkrwfeifmi lpllmmltsc gyqvpledtt ivfilgidld ednnlifyes spvfnkgakv
       61 qtetyqtkad tirdskkyfd tvesgevsga kiqvlllgkk vvehedwfpi ldtlyrnsnf
      121 slntrvvvve gnvsdvinye pksnaylvmy lknvidknhk rtrtakgtlq llhseiydkg
      181 vtpalshvkk dkrvevtgtv llndrgkyvd sldlsestlf lflknnqkhp isyttitipt
      241 dkedgifhkh dlsfevtnvk skiktsydmd kvtfdvkvsm silileslls mdmksneeki
      301 keiieerlks eyeklfkkiq shkidpigfg vyarayeyeh fkkvqdnwge alsqaninis
      361 veveikgmgt vnetsk
//
LOCUS       WP_010676833             175 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Bacillus timonensis].
ACCESSION   WP_010676833
VERSION     WP_010676833.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..175
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20518
     Region          4..171
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msyssaeeai lqlqkgdkea leviynvyka plyqfvfryt nneqlsidlv qdtfeklqhk
       61 fhqfdpekgk lktylyqiay ntmmtrlrrq nvfrtllpil aerhphhens dekltvqaai
      121 qslsedlrai vlltyyhdlt qkeistilhi pvgtvksklh ralkklreel evned
//
LOCUS       WP_010676824             386 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Bacillus timonensis].
ACCESSION   WP_010676824
VERSION     WP_010676824.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..386
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43424
     Region          1..385
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkkinvgmig ykfmgkahsh ayrdlpmffp ntlhpemkvi cgrnlngvae aakqfgweey
       61 ttdwrsllqr ddidlidina psdvhkeiai aaaqagkhvf cekplaltlk dsremlqvvn
      121 aagvkhmigf nyrfapavml akklidegrl gdiyhfraff lqdwlidpnf plawrlqkdi
      181 agsgshgdlg ahlidmahyl iggidevigm netfikerpi ptnmtglsat gnknaekgev
      241 tvddatlfma rfangalgtf eatrfasghr stnsfeings kgsvifdfer mnelqvyftd
      301 dredvqgfrr vlatdpahaf aenwwppght igyehtfihe ivelmesfre drlpvpnfnd
      361 gvkcqevlea veqsietrqw ikvsdv
//
LOCUS       WP_010676845             141 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Bacillus timonensis].
ACCESSION   WP_010676845
VERSION     WP_010676845.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..141
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16305
     Region          4..138
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mqeekmaeli pflkerglri tpqrtlilqt flslkghptv ddihrhlpqi slatiynnvk
       61 lfvslrilke lpygnglsky elanqpnhyh ilcescgdii dfnypaltqi ehvacklthf
      121 kiyshqmevy glcqscqkkr r
//
LOCUS       WP_010676857             646 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Bacillus timonensis].
ACCESSION   WP_010676857
VERSION     WP_010676857.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..646
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=73889
     Region          8..>271
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
     Region          313..338
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(314..315,318..319,321,345,348..349,352..353,
                     355..356,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          321..605
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          343..373
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          382..409
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          461..494
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          551..582
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          587..620
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mikigsfidd ryeilkeigr ggmsivylam dnrlnkslvv kdirkrdnsn nellinslvv
       61 eanmlkkldh galpkiydii esegdiyvvm dyvegeslkq klkrekiisa klvinwakql
      121 aevlhylhtr kphpiiyrdm kpdnimltpe gkiklidfgi arefkdeslt dttnlgtkty
      181 aapeqlsgkr tdartdiysl gltlyqlitg ksladppyev rpirqwdptl peglehiilk
      241 ctqaepenry qtceellydl qninkltagy rkkmmkrlyl fllpavlclg fsttsvlgyq
      301 gmqneqfqdy mglvnessis liegndteai kllekaikvd kgrasayinl ldvyinrndv
      361 dtglskiesy vndeygnihk nsevlfklgm tyfdlkrdyp valkyfkqvd ekkipdasyy
      421 itlattlggm nidyeqfstn liefekfndn lpnnakkvdn ynslaniyis ykgqiadant
      481 kaitvvqkaq evlelapdeq lqlkyeiefe qklaqafysr gvnsedqvaa rddfeqaidh
      541 ynnllelnvq nkeevmvdig viyqemgeqs qaveqfegil keypkslnay vklgnllldi
      601 eqgkqedqrn yskakevfnk ggqlegaqnd eaykklsrrm gnlnir
//
LOCUS       WP_010676900              78 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl carrier protein [Bacillus timonensis].
ACCESSION   WP_010676900
VERSION     WP_010676900.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..78
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=8805
     Region          1..75
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mdiqeflkif aedivmlepe dvtpdtilde ledwdslaii slnvaldehf gftlnqeeik
       61 nlesvsdilt iinkksni
//
LOCUS       WP_010676925             280 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Bacillus timonensis].
ACCESSION   WP_010676925
VERSION     WP_010676925.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..280
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=31015
     Region          1..278
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mktaivtdst ayipkelree lnihmiplsv vfgeesyree vditaeafyd elkarkdlpt
       61 tsqppigefv elfeklgqen daiisihlss gisgtyqgai tagdmvegvr vyafdseisc
      121 ivqgfyalea aemanegkpv eeivarldei kksvrayfmv ddltnlqrgg rlssaaafvg
      181 sllqvkpilc fedkvivpfe kirtrkkaln rvfelfdeda skgvpmraal ihgnieveak
      241 elkaelekky phvefllsyf gpvigthlge gaiglgwymk
//
LOCUS       WP_010677007             299 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Bacillus timonensis].
ACCESSION   WP_010677007
VERSION     WP_010677007.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..299
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32477
     Region          1..299
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mdlllivipa flifaagfig qrllkidiks istfslylll pflafdtfyt nelnadylym
       61 fiftvllavl ligvtfligk ivkadrphms alqlgsvfpn sgnygapval fafgsmgfdy
      121 aviimvihaf iinslgifia slgsssptgp keafirlirm pvlygaivgi lfqlfhiaip
      181 ptiidgismv geasipvvml ilgmqlaeik pqkfnlkyvs tvsalrmvis pllavalvql
      241 mpvnetiqhv fillaampva anttilavqf dckpelisft tlvttllsli tipfvlyll
//
LOCUS       WP_010677008             330 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Bacillus timonensis].
ACCESSION   WP_010677008
VERSION     WP_010677008.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..330
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36552
     Region          18..242
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mskvkvgfvg vggiagvhle nisqnshaki vavcdiveen arkkglqyna afytdldvml
       61 eketldavfv cvppfahwdi eekivsrgih llvekplgld ietvkrkekv ikesgvicav
      121 gyclryldtv akakeylkdk kiamvrgyyi tsfvqtpwyr emsksggqlv eqsthtldlm
      181 rylagdiesv yanmslqvls dipnidipdv ssvnmtftsg tvghldssit qsdhrsgiei
      241 lgkdfrleld gttltivekd stiiykskvd fyqeqdrrfi eavmkgktel ilsdyedgak
      301 tlaatlaank snevglpikl tsltnnrvtl
//
LOCUS       WP_010677012             325 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Bacillus timonensis].
ACCESSION   WP_010677012
VERSION     WP_010677012.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..325
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=34134
     Region          7..314
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 meqtedlaig ldiggtkila almskngevl skcqtdtkkg keqfgdlllt tinvlinean
       61 iektrikgig iatagvidsk kkeilfasnl glsnfpiglf lesklglpvq lyndanaaav
      121 gewmwgagkg kqnliyitvs tgigagiisn dnlltgmtds agefghisih fdgplcpcgn
      181 kgclenyasg taiakkaher iqggavsqyl svdtvitavd vcnaaergdp fsidlleevg
      241 eylglgiinl ihlfnteavi lgggvmngak filpaiqrtv qkhgiasmvd kakidrshlg
      301 ndacvmgatg lffkestqna allik
//
LOCUS       WP_010677085             350 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Bacillus
            timonensis].
ACCESSION   WP_010677085
VERSION     WP_010677085.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..350
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39278
     Region          1..336
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 miqleninkv fklgktevsa lknvnihvek geifgvigfs gagkstllrm vnllekpttg
       61 difingknll ilsekelret rkkigiifqq fnllssynvf dniaeilrin rvpkqeikrk
      121 vkklltlvgl edkaeqypaq lsggqkqrvg iaralamdpe illcdeatsa ldpqttdsil
      181 ellldinkkl gltiilithe mevikktcdr vavmdkgevi eqgtvldifs nprhvttknf
      241 lrnlyedtit ddvverlqkr ghsyilrlaf rgesayepvl nkiasnysvv tnivhgsity
      301 lkgvplgill vhlsgdedkv eqaitylkdv vyhveinlel nkkykeamvl
//
LOCUS       WP_010677118             178 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerol-3-phosphate responsive antiterminator [Bacillus
            timonensis].
ACCESSION   WP_010677118
VERSION     WP_010677118.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..178
                     /product="glycerol-3-phosphate responsive antiterminator"
                     /calculated_mol_wt=20045
     Region          2..177
                     /region_name="GlpP"
                     /note="Glycerol-3-phosphate responsive antiterminator
                     (mRNA-binding) [Transcription]; COG1954"
                     /db_xref="CDD:441557"
ORIGIN      
        1 mnqsilpast tmkefedflk skyeigifte ihiaqlknin kmaglhgkkm iyhvdmvhgi
       61 ksdeyateyi cqefqpygli stkssviqka kqkgvcaiqr mflidthale ksykliaknk
      121 pdyievlpga mpwmikevke rlnipvlagg lirtkeevqn aldagatait tskrelwv
//
LOCUS       WP_010677165             149 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Bacillus timonensis].
ACCESSION   WP_010677165
VERSION     WP_010677165.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..149
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16654
     Region          1..138
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkidetdkki lelltinarm syvdigkelg lsrvsirerv nqliekgvie kfsvvinsek
       61 vgkgvsaffe vdcepaslvr vaetlannps vascyqmtgp stlhmhvlve dfaklekfin
      121 eelysldgit rveshillrr fksrtglkl
//
LOCUS       WP_010677248             433 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Bacillus timonensis].
ACCESSION   WP_010677248
VERSION     WP_010677248.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..433
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45774
     Region          2..433
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mfklselntn vkkevlagit tfltmvyvvv vnpvilsdag vpfqqvflat iiatvvgtlw
       61 malfanypia iapgmglnaf faysvvgane nityetafaa vfvagiifvi lsltpfrekl
      121 ieaippnlkh gitagiglfi afiglrltgi itahptnlvt lgnlhspsvl lalvglaitl
      181 illarninga lffgmiitgi iayltgqlef kegfvntpsl pegliianpl taigdviqyg
      241 lyavvfsfll vtifdttgtm igvaeqaglm kgnvmprarq alladsigtt vgamfgtspt
      301 sayiesstgv aaggrtglts vtvsilfila affgplvsav sgiaaitapt liivgslmmg
      361 sikdirwnei deafpaflii lsmpltssia tgialgfisy plmkvvrgkw revhplvylf
      421 avlffyqlaf lph
//
LOCUS       WP_010677303             157 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Bacillus timonensis].
ACCESSION   WP_010677303
VERSION     WP_010677303.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..157
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18576
     Region          1..157
                     /region_name="COG5628"
                     /note="Predicted acetyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:444356"
ORIGIN      
        1 mdiqiqaisk reeevlhnlm qfyiyeftky mdsirindsg lfgrfnldvy wtddnhhayf
       61 vrvdsllagf vlvqsqteke pnsieeffim rgyegkgigs fvaeqifamf pgrwqvrqse
      121 knerartfwr siiskctkgn feerldernc siqefii
//
LOCUS       WP_010677343             233 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase family protein [Bacillus timonensis].
ACCESSION   WP_010677343
VERSION     WP_010677343.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10065661
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..233
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=26962
     Region          6..217
                     /region_name="MPP_PPP_family"
                     /note="phosphoprotein phosphatases of the
                     metallophosphatase superfamily, metallophosphatase domain;
                     cd00144"
                     /db_xref="CDD:277316"
     Site            order(9,11,38,42,67..68,149,168,187)
                     /site_type="active"
                     /db_xref="CDD:277316"
     Site            order(9,11,38,67,149,187)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277316"
ORIGIN      
        1 mkrmlaisdi hgdidkferl lelvqyddki dqllllgdyv drgpnsravi nkvielrnkg
       61 aialignhek mmleafrads msvkrwfyng giktlqnygy hiekddakyw ytteempnll
      121 qinkeirphl etlkefpyyy etdthifvha gvhpetples tdphllvwir eefhngyage
      181 ktvvfghtpt kylhksnemy fgnnnivgid ggcayggrly cfdatnsqif yve
//
LOCUS       WP_010677346             286 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Bacillus timonensis].
ACCESSION   WP_010677346
VERSION     WP_010677346.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..286
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31059
     Region          40..271
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mldilsfnwe allikvgiiv lkiigifiaf iivkkignkv idrtftrlqe kqnvsigrah
       61 tlqklmenvl sytlififva slfsifnisv asliagagiv glaigfgaqg lvsdvvtgff
      121 lllekqidvn dyvtigaidg vveavglrtt qirgfdgtlh yipnrditsv snhsrgnmra
      181 lvdigiayge didkaitvmq evcdqiaadn pvivegpnvi gvqalgasdv vlrviakten
      241 gehwgverql rkaikeafda ngieipfphq vtihrngenp ekmvqs
//
LOCUS       WP_010677399             412 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Bacillus timonensis].
ACCESSION   WP_010677399
VERSION     WP_010677399.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..412
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44229
     Region          121..409
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mgyydqdysn qrnrrqggrg swflsgliga iigallvlfl lptlskyhll pyeenaaree
       61 lnglddveek apatgrsvqq ninvnvttev tsavnrvsea vvgivnlqqt nfwseeatta
      121 gtgsgvvykk gngkafvvtn hhviegasdl evslsdgsrv kgrllgsdiw tdlavieida
      181 dhvkkiaqfg nsdninlgep viaignplgl efsgsvtqgi isglnrtipv dinqdgvpdw
      241 nadvmqtdaa inpgnsggal vnikgevigi nsmkiaqeav egiglsipit sakpiiedle
      301 mygevkrpfm gvgqlkalse issyhreqtl hlpndvtegv avlevlsntp asnaglreld
      361 viveldgeki ssvielrkhl yneksvgdkm evtfyrggek qkaiiqlare sl
//
LOCUS       WP_010677467             338 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus timonensis].
ACCESSION   WP_010677467
VERSION     WP_010677467.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..338
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37561
     Region          5..321
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 maekiievkg lrtsfftdeg eipavdhvnf yikegeilgv vgesgcgksv tslsimglvp
       61 sppgkivdge ivfngeniak fsekkmrqir gndiamifqe pmtslnpllt ignqmiegik
      121 ihmkwdkkks raraievmkr vglpraeelm deyphqlsgg mrqrvmiama macnpkllia
      181 depttaldvt iqsqilklmk klnaelntai mlithdlgvv aqicervvvm yagkiveega
      241 vssifknpkh pytkgllksv pdirnknerl ysipgnvprp gsikngcrfa ercefafdrc
      301 fsdtpelyev ddkghrvrcf lqskeeesnh dtaftsss
//
LOCUS       WP_010677487             500 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bacillus timonensis].
ACCESSION   WP_010677487
VERSION     WP_010677487.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..500
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54214
     Region          39..482
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 msnktidngq syhtarlwqi gfftlnntss nlhlfalgfv tyyatgvagl avmlvstllm
       61 aarlfdglid paigyiidkt egkfgkfspl ivvgnvisag tiitiysvth llpesmqflf
      121 ftamlivnki gyslqtsvtk aaqtvltndp kqrpifsifd gvfnaviftg gqiyvssyli
      181 gkyggftlpl ftelnivali lsavfaalai rgiwskdkke yyglgeettk ttlreywgvi
      241 kgnrplqlls isasfdklgm sifgysvvgv mlfgillgdy slsgtiglit lvpgllitfl
      301 vvivarkvgl rksyiiscwi ailaftglia lftlidptsi slsdigvttv lflilyavar
      361 afagvpstfv ipmiadvsdy ethksgryvp gmmgtifsfi dqlvsslapt ivgfvvgfig
      421 ykekfpevge alttplfytt lllafglpal clvvslvamk fykldakrme eiqkgisekk
      481 rkgngdfppt pftpdsgiak
//
LOCUS       WP_010677503             160 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter small permease [Bacillus timonensis].
ACCESSION   WP_010677503
VERSION     WP_010677503.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..160
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=17787
     Region          1..148
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mnkvkqildk vlivfsslll vsmvvlstwq vlsryvfnis spgteeltry mliwfgltsa
       61 ayvfgakkhi gilfirekfs pkvqlqieyi tdviilltaa ilmvyggiki vvltsaqtaa
      121 atgismgvvy aailfsgici viyqfhslms ykerkrevil
//
LOCUS       WP_010677504             431 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Bacillus timonensis].
ACCESSION   WP_010677504
VERSION     WP_010677504.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..431
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45576
     Region          5..431
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 metvaaiilf atffflllfg apiaiaiils svftflfvlp fdvailtsaq rmvtgidnft
       61 mlaiplfvls givmnnggia frlvnfakvl vgklpgalah tnavgnmlfg sisgssvasa
      121 aamgrimtpm qtnqgyklty saavniasap tgliippssv livyslvsgg tsvaalfmag
      181 yipgilwgia vmvvayfmak kekypvsslp nmkdifyiiv saipsllliv iviggivagi
      241 ftategaava viysvllsmi ykslklkdlp gifietieit gmilflitas alfslvmsym
      301 rlpeaisgal lsitdnqtgi iliiifilli vgtfmditpa vliftpiflp vaknfgmdpv
      361 hfgmilcfgl cignmtppvg salfvgcsva kvkieevvpt llpyfgivil vlllvafipq
      421 lslflprlfg l
//
LOCUS       WP_010677544             398 aa            linear   BCT 01-JAN-2025
DEFINITION  thiolase family protein [Bacillus timonensis].
ACCESSION   WP_010677544
VERSION     WP_010677544.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 398)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..398
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42241
     Region          1..398
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mreaviidav rtpigklngs ltsvrpddla ghvikqlmar vdldsslied vlfgcanqag
       61 ednrnvarmg lllaglpvsi pgvtvnrlcg sgleavnqaa aaiksglgdv fiaggtesmt
      121 rapyvmmkph vtnprgnqtl hdtmlgwrlv npvmnemypp islgetaenv aekygisree
      181 qdalalasqq kaalaiqsgr fndeivpiei pqrkatvlfk qdeharpett letlsklkpv
      241 frkngtvtag nssgindgas ailvmekela erlglkpiar vvtsavsgvh pdymgigpvp
      301 atkkalqrag ltvedldlie ineafaaqsv acikeldldm dkvnvnggai alghplgcsg
      361 srivttlvhe mqkrdvrygl atmcigvgqg iatiiekm
//
LOCUS       WP_010677586             422 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Bacillus timonensis].
ACCESSION   WP_010677586
VERSION     WP_010677586.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..422
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44833
     Region          1..421
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mawllfgili vlffinvpia valglssmiv lmiqdnvplm vivqkmftst dsftlmavpf
       61 filagklmev ggiskrlvdf amtivgrmhg glaivsvvtc mffaaisgsg aattaavgai
      121 mipamvqkgy dksfstaiqa aggtigvmip psvpmilfgv iagasisdlf iagilpgilv
      181 gvslivvayf isrkrgygke ekssirdvft sfnrailail mpviilggiy ggvftpteas
      241 vvaavyglvv glfiykeikw kdlpevfiss avtsavimfi iacasifgfi ltreqiplqi
      301 tnallefssn piivliiini illiigtfle tsaaiiimap illpvtnavg idpvhfgvim
      361 vvnlaigfit ppvginlfva snianlrlek vvraiipfli mlivdiiiis fvpeislffl
      421 dk
//
LOCUS       WP_010677595             565 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Bacillus timonensis].
ACCESSION   WP_010677595
VERSION     WP_010677595.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..565
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=61188
     Region          <160..565
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkrtlttqlg iiiivvifvs mfitsvsnyw vsyektyeaa gieavgcani ttglinpidi
       61 eaiidgdknp aelnelldwt tnhksifegq yilslegeil aldsnmqkqg fkagdqfyid
      121 knvlktiqet khphyseiyk fggmkritgy apifkdhdpn keiiainaid fdakivtert
      181 vdavkdsfil gllpmliacl itifiirrkt kpltllinna qevaegdltv rqieiknkde
      241 igdlatafnr mtnnlrelin qvsyttnnva asaeqltass eqttdatkqi avtmhevaag
      301 vdrqvqsiee tsqtvqemsi gvgqiagnaq rvsasvtdta ekaseggesi rtaesqmnsi
      361 nhtfselsel ikglgnrsee igkiievits iasqtnllal naaieaarag ehgrgfavva
      421 devrklaeqs agsssqisel ildiqnetnk avaameaate evisgigiih tagtnfdqie
      481 esikevtsqi qevsaavqqm aagseqmvhs mrlisevaee skagtqevsa steeqmasmd
      541 eisssassla nmaeelqgiv nkfki
//
LOCUS       WP_010677615             442 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bacillus timonensis].
ACCESSION   WP_010677615
VERSION     WP_010677615.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48168
     Region          23..431
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(36..37,40..41,44,83,141..142,144..146,149,169,
                     172..173,176,259,262..263,266..268,271,299,303,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mstapviqed intenkgfsk ehrkvglasf igttiewydf ylygtaaalv fpalffptfd
       61 plygtlaafg syaagfiarp lgsavfghfg dkigrkkmlt lslllmglat flmglipsyq
      121 tiglmaplli sllrivqgfa vggewgsavv mavehapkgk rglygsfpqm gvpaglllst
      181 fvfsmvnnsm pndaflawgw ripfllsail viiglwirlr vsespvfeem aekkqleekp
      241 vltvlrtqrk plfltigmkl vqnatfyiys vfvltylvgt vnvdrsigln avmissvvgf
      301 vtmplwsyls dkigrkpvyl ggtiattlfi fpffllmdtg svlwitigiv lglnvihdsv
      361 ygpqavyyse lfgskvrlsg asigyqvgai laggfsplia twllakydgq slpiilylva
      421 lgvisiiatl faretyrdsl tq
//
LOCUS       WP_010677674             541 aa            linear   BCT 01-JAN-2025
DEFINITION  amidohydrolase [Bacillus timonensis].
ACCESSION   WP_010677674
VERSION     WP_010677674.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..541
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59752
     Region          2..536
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mkadivfmng evvtvdddns vvesvavkgn hiiavgsnqe iqeyishetn vidlhgksvl
       61 pgfidahlhl tiygtnllgv sciephiqsl edlftdlqkk aeetpkgqwv rawgfneskl
      121 kenrfptrqe ldkvstdhpi viirtcnhts iansraleia gitedtvnpd ggiigrdkng
      181 altgaliena hmqlfeyasy tdeeirkgmk lasdefiqag vtsihdagay gdgaeslrim
      241 qqaikkkeiq vrvyaiigsl tnshefverv vkagpisglg ddyfkigpak lftdgssvgp
      301 tiatrepysh nsndygityy sqdelnrilg eahkkgfqit ahaqgdrave mvldciekal
      361 eehpridhrh rvehagissa dlqnrmqklg vipipnpvfm yvngdkyley yadrvnvmyp
      421 lrdfidkgii aaigsdapvt fvnpllgiha avnrkswkdq lvgenqridv ieairaytyn
      481 gayasfeeak kgsievgkla dlvvldssil haeseklkdi kveltmvdgd ivfqskqlit
      541 k
//
LOCUS       WP_010677681             811 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Bacillus timonensis].
ACCESSION   WP_010677681
VERSION     WP_010677681.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 811)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 811)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 811)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..811
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86716
     Region          12..81
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          80..809
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msteateask lkeasiqitg mtcaacatri ekglnkmegv eqasvnlale kssikydslk
       61 lseadfekki ealgygvvkq kaefditgmt caacatriek glnrmegvat anvnlaleka
      121 tiefnpsevt vgdiiakvek lgygahqkqe dkeqvdyrek hikdqqrkfi isailslpll
      181 wtmvghfsft sflyvpdflm npwiqlilat pvqfiigkqf yvgaykalrn gsanmdvlva
      241 mgtsaayfys vyqaivtagt hhmphlyfet savlitlill gklfearakg rsseaikklm
      301 glqaktavvv rdgvekevpl eevvigdtil vkpgekipvd geviegttav desmltgesl
      361 pvdktsgdvl ygstinkngf ikmkatkvgr dtalaqiikv vedaqgskap iqrladqisg
      421 ifvpivvgia iltflvwiiw vspgeftpal evliailvia cpcalglatp tsimagsgra
      481 aeygilfkgg ehleqtqgid tvvvdktgtv thgkpvltdv lvaegqdeek flsligaaek
      541 qsehplaqai vegieekgiv lgnvqffeai pgygviatvs gqgvvigtrk lmqqygieie
      601 tvlpemekle thgktamlag ingkyaglva vadtikdtsk eavsrlhdmg iqvimmtgdn
      661 ertaqaigke vgvdsviaev lpegkaeevk klqqqgkkva mvgdgindap alatadigma
      721 igtgtdvame aaditlirgd lnsiadailm srktmrnikq nlfwafaynt igipiaaagl
      781 lapwvagaam afssvsvvln alrlqrvkln k
//
LOCUS       WP_010677698             563 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Bacillus timonensis].
ACCESSION   WP_010677698
VERSION     WP_010677698.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..563
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60786
     Region          13..562
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkmtigrklf tgflsvllil iatvtigyve itsvqhtyde lindkakklv mikeldsaik
       61 qeqvglrgyl ligdeialkd fedshskfle tskslhdiit qpkakellqe ldtiedeyyq
      121 fsdkvfqlkd enkvdeytsl iaidgraivk dfnqsieefm kyqqdlldkg nietsekvks
      181 tkniililgv lsllvglsia tyigriiskp vvaisknaek iasgdlsvde ikvknkdeig
      241 elansfnqma kslreviqqv glnadqvaas aeqltasseq tndatkqiae tmqqvasgvd
      301 kqvksidets qtvnematgv qqiagsaqqv tssalettek asegrqsikt vvnqmssind
      361 tftelsgvvk glgqrsveig qiievitgia dqtnllalna aieaarageh grgfavvade
      421 vrklaeqsat ssnqiaqlil aiqnetnkav etmevateev vsgiglvnta gtaftqieds
      481 itdvttqiqe vsaavqqmaa gteqmvqsmq liteiaeesg sgtqevsaat eeqlasmdei
      541 sasagalahm aedlqevisk fkm
//
LOCUS       WP_010677701             296 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Bacillus
            timonensis].
ACCESSION   WP_010677701
VERSION     WP_010677701.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..296
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32330
     Region          11..291
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 meqryqdlkl gergailsia vyillsllkl iigyiadsea lkadglnntt divasvavli
       61 glklsqkpad ddhpyghwka etvssliasl immvvgvqvl fgaassvfsg nhespdmiaa
      121 wtgfisafim ylvykynkkl akkvkshavm aaakdnlsda wvsigtaigi lgsqlglpwl
      181 dpvtafivgl licktgwdif resshyltdg fdikdleeyk qtilnvtgvl evkdikgrty
      241 gnsnvvdvvi svpnhlditq aheistrvev tlikehnvqd vhvhvepvrd dklims
//
LOCUS       WP_010677715             246 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Bacillus
            timonensis].
ACCESSION   WP_010677715
VERSION     WP_010677715.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..246
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27550
     Region          4..241
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mekiidiqhv nksfgthevl kdinfsvnkg evvsiigssg sgkstllrci nllekpsggq
       61 iiyqgenild nkhdvttyrr hlgmvfqqfn lfnnhnvlsn cvvgqikvlk rskeeaekia
      121 mkylkvvgmd kyinakpkql sggqkqrvai aralsmepdv mlfdeptsal dpemvgevlk
      181 vmkelaesgl tmlivtheme fakdvsdrvv fmdkgviaee gspehifnhp tqertreflk
      241 rtlvhs
//
LOCUS       WP_010677759             425 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter large permease [Bacillus timonensis].
ACCESSION   WP_010677759
VERSION     WP_010677759.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..425
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45388
     Region          1..423
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 msifllvlff ilmflgipia tslgisvvaa vllftdvpls lviqsmfssm nsfllvsvpl
       61 filaglimee ggvadrlfgf aqslvgwmtg glghvnvias lifagmagss vadiagtgrm
      121 qinamvkkgy plsysaaltl itamlasiip psilmivaas tagvsigaal igglvpgiii
      181 siifmlfnhy yskkhnygir ekfdwnyfkr etitslpall apvvllagil sgiftpteaa
      241 aicvlytlii svfiyrklsf krlpnlmlkt anmsgtilfi avtakaaswv feydglpsri
      301 aaviggises piiimlilfv fllivgmfmd ataaifilvp ilmpaiiavg idpvyfvvfm
      361 vvalsfglvt ppvgvclyat snitglsier lskdsmpwfg vtmiallvli fipqiitvpl
      421 twfdl
//
LOCUS       WP_010677760             168 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter small permease [Bacillus timonensis].
ACCESSION   WP_010677760
VERSION     WP_010677760.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..168
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18736
     Region          15..157
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mvnhnenkpa tifmilnrit dvlagistaa islvvlwqvf grvlgipapw teevtrflfi
       61 wlvflgigig frkvesarvt illqyapkfi kklsvwiyai asvgffifmt fygfelvtqq
      121 iniheksaal lfpmwiigls vpvsgllgif ntvqsliydk eiiekggv
//
LOCUS       WP_010677798             387 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bacillus timonensis].
ACCESSION   WP_010677798
VERSION     WP_010677798.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..387
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42820
     Region          8..373
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(15..16,19..20,23,55,105..106,108..110,113,133,
                     136..137,140,213,216..217,220..222,225,249,253,303..304,
                     308,312,328,331..332,335..336,339)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mklrfwilvs ivavsgfsqg mllpliavif ensglsstln glnatalyig ilfvspfmey
       61 plrkygykpi ilfggllvav slalfplwks fwfwfvlrll igigdhslhf gtqtwitsfs
      121 penkrgrnis lyglffgigf atgplltplv kisetlpfil ssvlcligwf flfllknefp
      181 etdmgvnsfk etidrfskaw kyawvaflpp maygflessl ngsfpvyglr idlnvtfvsi
      241 lltsfaigsi itqlplgils dkfgrrnilm ivlflgflmf tiasllehsh vglwlcitfa
      301 gmavgstfsl gisymtdlmp ktllptgnll cgiffsigsl vgpfigglfi qffedisffn
      361 vigsilllif lvisvfgtkt atktven
//
LOCUS       WP_010677825             346 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Bacillus timonensis].
ACCESSION   WP_010677825
VERSION     WP_010677825.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..346
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39347
     Region          124..339
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstikrqmiv gicvsvtlfv lahvivfmaf planwgslwq tefmdlpyii laisfsligg
       61 lvfgimsgvl wrkqllsvsd aiyqieqgra ipeipenqti eistiwerik kvqahiaeqt
      121 klsqklanek aedqekriqk ivseernrla relhdsvsqq lfaasmmmsa inesrprtda
      181 reakqfklve emihqsqlem ralllhlrpv alkgktlqeg iqelivelaq kvpvtiekki
      241 edfridkgve dhlfrilqes lsntlrhaka nqlevllikr dhfiilrivd dgigfdveqa
      301 ktgsyglqnm yeraveiggt mrivsikekg trievkvpll egeend
//
LOCUS       WP_010677854             202 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Bacillus timonensis].
ACCESSION   WP_010677854
VERSION     WP_010677854.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..202
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22111
     Region          11..190
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 misidptris erdnyklmig siiprpiafv tsttktgtln gapfsyfniv ssdpplisls
       61 iqrkdgdmkd tarniiegke fvvhivdesn vekinktaas lppneseiel aeltpvestr
      121 ikvpgikeak iriecvleks ielggqampg cdllignvvq fhidealfsk grinqeklga
      181 vsrlagnyya kvgnifeier pk
//
LOCUS       WP_010677871             143 aa            linear   BCT 01-JAN-2025
DEFINITION  GAF domain-containing protein [Bacillus timonensis].
ACCESSION   WP_010677871
VERSION     WP_010677871.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..143
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=15832
     Region          <7..>132
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
ORIGIN      
        1 meaiqveieq klhdlctnts sdfsafanvd qgsqtirwey ahgftnnryk nmvirpgkgl
       61 sgsvvrfgtt mvldidtpnr qrtrlqypim laenlvsava vpvqmngkvg gvlligsrte
      121 vkytteqvel lkktaseite ikk
//
LOCUS       WP_010677890             292 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus timonensis].
ACCESSION   WP_010677890
VERSION     WP_010677890.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..292
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33082
     Region          4..218
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mniieiqnlt kmygksrgie disfhveege ifgfigpnga gksttirtml sliyptsgsa
       61 kifgkdsiqf ssdikkeigy lpsevfyydn mkvkdllnys asfykkdctk rmkelaeime
      121 ldltrkiddl slgnkkkvgi vqgllhepkl vildeptsgl dplmqqrffe lleeenkkgv
      181 tilfsshils evqrlcnrva iikegkivtv ekistlkenn fkrfsvetah pidnnyfsip
      241 gvnhlsskei tflfkgnint vmekiagiei tnlsvtepdl eeifmhyyek ea
//
LOCUS       WP_010677925             317 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Bacillus timonensis].
ACCESSION   WP_010677925
VERSION     WP_010677925.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..317
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34482
     Region          2..294
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(33..34,37,89,103,105,134,167,254,257,293)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(224,229,244,254..256,259,281,285)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mdvvtigetm vmftpqsspl mryaesfikr yggaesnvai glarlghkvg wiskvgndef
       61 gkgmisfirg egvdvsqvkt dshaptglyf kevksghnvt vqyyrngsaa shltprdldp
      121 dyikqakflh itgitpalsd scyqtvkrai siakengvqv ifdpnvrkkl wseekarevl
      181 velttladiv lpgleegtfm fgetdyvkig krfletgpkl vimkdgkkga yvfkedcyel
      241 ipgfevdevi dpvgagdgfa agfisgllsg ftveksveig navgahvvqi pgdfeglpsq
      301 welkqflnsg attdvlr
//
LOCUS       WP_010677959             217 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Bacillus timonensis].
ACCESSION   WP_010677959
VERSION     WP_010677959.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24610
     Region          17..183
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mskenlldai ieqsklskkp tekqqkiaet aikmfaekgy antstseiak aagvaegtif
       61 rhygtkdnll lsvilpflke alpgmaenvf kevlteetph frdflkglfk nriefvienr
      121 eifqiivkei lytdslrqei apffadsvvk rinqaielfk ergeikdipt ntllklimtt
      181 fggflvthfv llptnekmdv dyeaenlvcf mvdgirn
//
LOCUS       WP_010677976             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bacillus timonensis].
ACCESSION   WP_010677976
VERSION     WP_010677976.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..429
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46300
     Region          7..413
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(20..21,24..25,28,67,125..126,128..130,133,153,
                     156..157,160,242,245..246,249..251,254,282,286,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mqtkvekkvl iaslvgssie wfdyflygtv aalvfntaff hsedptvglm layasfalsf
       61 firplggvif shigdkigrk ktlvltlslm ggatvlmgfl ptyeqigvia pillillrli
      121 qgiglggewg galllaveya pkgkrgffgs vpqmgvtvgl llgtialslm sllpeaafms
      181 wgwrvpfils allvifglwi rkgieetpsf kkvqekgeva ripfletmrs hwkevlisig
      241 akvvetapfy ifgtfivfya ttqlgfsrta tlnavtiati vttilipimg glsdkigrkr
      301 lyvggtilmm vyafpyfwll hqgsvallii atvlglgiiw apitavlgtm fseifksnvr
      361 ytgitlgyqi gaalaggtap lvatallaaf nysyvpvaly iiltsaisll avaairdrks
      421 edldneeia
//
LOCUS       WP_010678045             144 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Bacillus timonensis].
ACCESSION   WP_010678045
VERSION     WP_010678045.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..144
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=16979
     Region          40..139
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mkmdqfknmn dwrkqwdhff gdefwsgfap ffdnphsqln lyqgenellv vlslpglakv
       61 edveifvnhq tlevrgkinl nfkgfdiiqe gifqgkfere iqlpytvkee rikasykrgl
      121 llihlhkqip ddsrkkvevl dkdk
//
LOCUS       WP_010678055             150 aa            linear   BCT 01-JAN-2025
DEFINITION  VanZ family protein [Bacillus timonensis].
ACCESSION   WP_010678055
VERSION     WP_010678055.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..150
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=17205
     Region          1..127
                     /region_name="VanZ"
                     /note="VanZ-like family protein (function unknown)
                     [Function unknown]; COG5652"
                     /db_xref="CDD:444373"
ORIGIN      
        1 mqlfiirfil rflpviymvw iwlqsshfnp sklegihvqi gipiylllga aleighlfqf
       61 ailyallvma fltfgklslk ieillfaiav lygvldeihq fyvpfrsfsi tdlikdgigv
      121 ivvsyiihkk yfnneqsrlg rllrgitvlh
//
LOCUS       WP_010678082             295 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Bacillus timonensis].
ACCESSION   WP_010678082
VERSION     WP_010678082.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..295
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34374
     Region          1..208
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkkltiftpt ynrayclhtc yeslikqttk efiwliiddg stdnteeivk qwkqeniiei
       61 ryhwqenqgm hgahntayel idtelnvcid sddfmpenav etilsfwnkh gsdkvsgiig
      121 ldsdstgkli gsmlpsdlkt sslfnlyhkl gvtgdkklvy rteltrnypy pifederyvg
      181 laykyykldr dyemllmnev lccveylpdg ssmnmlsqyr knprgwafyr kelmklpfvs
      241 qsfkfrqaih yvssnllikn ysflketpsk flttlaipfg illsfyvqqk tksvi
//
LOCUS       WP_010678121             264 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF92 domain-containing protein [Bacillus timonensis].
ACCESSION   WP_010678121
VERSION     WP_010678121.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487781
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..264
                     /product="DUF92 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=27809
     Region          9..252
                     /region_name="DUF92"
                     /note="Integral membrane protein DUF92; pfam01940"
                     /db_xref="CDD:460391"
ORIGIN      
        1 mislfiqila sivvavlgyk lkslsfsgai gtiivgsavs igygfrglll lgvffasssl
       61 wskckagnkd nlqnkvakge qrdivqvian ggvatltglm yawtglnfwl lffvgsiaaa
      121 nadtwaseig tlskrkpill tsmkrvdagt sgavsvlgtm agflgsllis fisflvwpei
      181 svilfvglti vgfcgnlidt iigatfqvay kcgvcgiete ksvhclkett yskgirfcnn
      241 dvvnflsill asgigtffls lleg
//
LOCUS       WP_010678167             323 aa            linear   BCT 01-JAN-2025
DEFINITION  PhoH family protein [Bacillus timonensis].
ACCESSION   WP_010678167
VERSION     WP_010678167.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..323
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=35815
     Region          11..322
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 msedlvmskh qlenpnealv lfgnndlhlk rmeeelnvsi itrgealhvs gdptnvqlve
       61 eilekllsvi rkgirvserd viyciqmakg gkldsfeely deeitktakg ksirvkthgq
      121 rqyvaaikqh dlvfgigpag tgktflavvm avnalkngqv kriiltrpav eageslgflp
      181 gdlkekvdpy lrplydglhd vlgvehterl mergtieiap laymrgrtld dafvildeaq
      241 nttlaqmkmf ltrlgfgskm vitgdisqid lprgvksglh evmhilkdvy gsafiyleqs
      301 dvvrhplvar iieayeqaea gqs
//
LOCUS       WP_010678173             148 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Bacillus timonensis].
ACCESSION   WP_010678173
VERSION     WP_010678173.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..148
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16454
     Region          1..148
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 msllerlnnd mktamknkek dklsvirmvk aalqnegikl gtgelseeae ltvltrelkq
       61 rkdslrefsn agredlvnkv qteieilevy lpkqlseeel veivketvqe vnasskadmg
      121 kvmaaimpkv kgkadgslin klvqqqls
//
LOCUS       WP_010678225             216 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Bacillus timonensis].
ACCESSION   WP_010678225
VERSION     WP_010678225.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..216
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24560
     Region          36..213
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mlsskitnyl eallpkrdev ieeiehyahe nnvpimelvg ietmlqilri srpkqileig
       61 taigysairm aqalpgtkiv tierdqerye kaleniertg tssqihvifg dalevfdevk
      121 nhgefdcifi daakgqyrhf fdiyekclsk dglivtdnvl fkglvaeeqi eskrirnlvt
      181 kiksynewli khpdyqttil pvgdgvalsk krgvke
//
LOCUS       WP_010678244             306 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus timonensis].
ACCESSION   WP_010678244
VERSION     WP_010678244.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..306
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33734
     Region          5..220
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mqpvlqlknv kktigkkdii kgitfdvypg evfgflgpng agktttirml vglmsitdge
       61 viikgtniak nfeqavqhig givenpemyk fltgyqnllh yarmvkgvtk erilevtelv
      121 glgkrindkv ktyslgmrqr lgvaqallhn psilildept ngldpagire vrdyvrklar
      181 eeglavivss hllsememmc drigiiqngk lvgvqkvtef vneeasirvq fqvdyvekal
      241 silsteysal evvqtdkgie iltdqemipk inaslvknei qvygimqlsk sledrflevt
      301 ggsgig
//
LOCUS       WP_010678250             186 aa            linear   BCT 01-JAN-2025
DEFINITION  SH3 domain-containing protein [Bacillus timonensis].
ACCESSION   WP_010678250
VERSION     WP_010678250.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..186
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19818
     Region          28..156
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 mlhkilkfgl afilaivfsi ttnpglptna etfaiidtpi lnvregpgls yarnaqvkqg
       61 ekytiidkkg dwvklqlssg ktgwvaswli kenqsnpkpt vssstvvstv dglrlrsgpg
      121 tnfqvigsln kgteagfiea nnnwtkisln ghigwvssqf vaakqtsgss nskpgsnast
      181 skkqeq
//
LOCUS       WP_010678298             402 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Bacillus timonensis].
ACCESSION   WP_010678298
VERSION     WP_010678298.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..402
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=45261
     Region          2..402
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mpmfqyegrd rygrkktgkv ssisqrqaiv qlreqgvavk siqemkgily kevslgakkv
       61 ktkdfviyir qfstllkagi svvdctrils qqttnkllqq alteivegle egnpfselae
      121 rhrkvfppff tnmlkageag gnldeildrl atyyekqykt iqkvksamty piflgissig
      181 ivifllatvv ptftdmfesf gselppvtrf vinvgdfvqs fwyliilfgl lvyfgilyar
      241 rnkrskyyld yfllkipvig kvfqqaalar mtrtlaslfs ssvpilqais iveriienev
      301 makvlrdsri slesgqslat pmqkhwvfpp mvshmivvge ksgsldiild kvadyyeaev
      361 dqiteqlksl iepimialla vvvgtivgsi aipmfdifnk iq
//
LOCUS       WP_010678502             259 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus timonensis].
ACCESSION   WP_010678502
VERSION     WP_010678502.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..259
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28979
     Region          1..250
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mgflsvkdih hvyftkdqat taledislti kegefisllg psgcgkttll siiagllkpt
       61 ygevlidgkt iekaksdigy mlqqdylfpw ktieenilvg lqimnqetdq tikkalalle
      121 eiglngveks ypkqlsggmr qraalvrtla tnpkilllde pfsaldfqtk lkledlvsdt
      181 lkeyhktail vthdigeaia msdriyllsk gpgkitkvft ipeclrnetp fdarqhpeys
      241 nifqqiweel dkletnpeh
//
LOCUS       WP_010678533             194 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pantoea agglomerans].
ACCESSION   WP_010678533
VERSION     WP_010678533.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21013
     Region          4..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mekqsskaht rrrildeaar vmretgtegi gvsalmkrvg lthggfyahf tsreelveev
       61 lkhmfaeadt lkpaesvtqp aqqladfids ylseahrnap aqgcplaalv sevahlpqpt
      121 rqifaqgfna mhaglaqilr elrlpdaeal assmlaemvg alalaracpd aeqasqmlqr
      181 srdalkqrtl evaa
//
LOCUS       WP_010678552             168 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Streptomyces sp. SA3_actF].
ACCESSION   WP_010678552
VERSION     WP_010678552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SA3_actF
  ORGANISM  Streptomyces sp. SA3_actF
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Streptomyces sp. SA3_actF"
                     /db_xref="taxon:682181"
     Protein         1..168
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=17666
     Region          1..140
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 msafpsgvgv vtaldenavp rgmtcsslas valdpavlvv clraggptsd avlgsgrftl
       61 nllhedardv sdlfasqrpd rfervvwrlp lgasgphlte aalatadctv vravpfgdht
      121 avfghvtrva htdtaaplly grrryarwsa aaaapeprrt egeprvrp
//
LOCUS       WP_010678648             822 aa            linear   BCT 01-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Pseudomonas sp. S9].
ACCESSION   WP_010678648
VERSION     WP_010678648.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..822
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=88237
     Region          1..819
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mssaantlaa vdpvevatsp vfdsgflrgm gqdidlsrfa kagivvpgty tlditlngke
       61 rirqdvrvtd vegnqhfcfs tadakrwgar leqlpdqeqv arvlasdcve vqalipgasf
      121 smdvaelsgt lsipqayagr vkrgyvdpte wdegitaail gyhgnvfrne rdgadtttdy
      181 svninaglnv sgwrlrhngn yrdsddgpse yssqnsyaqt didmlqsqlt lgeyftpgsd
      241 fdsipftgiq lasddsmlpe sergfapivr gtaetnakvt isqngnvvye tsvapgafvi
      301 ddlyatgyag dlevtvtead greksfivpf aavvqmlrpg ssrfniasgn yrddnledep
      361 wftqatyrrg isnkltaygg gilaedyssa lagaafatpi gavafdatft rakglptigs
      421 gedaiggdln gqsyrisysk lldatrtnfs laayrfssee flsfgdfarl renadsaslr
      481 ernrfqvnis qplgdygdfn ftgltrnywg dqsnsttfql gygkgfswgy mnltasremq
      541 dgenndtyml sasiplgsga rrpmltttat ldddnnnsir snlsgsagey gemnygvyas
      601 rsetnnesdn tyggnlnyrt satqlgasys hgddykqysg satgtvvvhs ggvvfsperg
      661 etmallvaeg apgaeitsgq gnrldgngea lkagltpyrh npvgisprgl pvdvelqtts
      721 qnvvprrgav vrldyatisg kplllrvqnp evpfgasvvd adnksvamvg qggliflrge
      781 hqglkvvwgq ssqescqlny qvpadeqgdn pyvqveasca hg
//
LOCUS       WP_010678731             342 aa            linear   BCT 01-JAN-2025
DEFINITION  CapA family protein [Leptospira interrogans].
ACCESSION   WP_010678731
VERSION     WP_010678731.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..342
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=37678
     Region          20..323
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mrqifilsvl flfsfgllgd sktikikavg dmvpgtnfpq plniqdprsf lfgkvesylk
       61 gadllfgnfe stltdypnts kdtsrkmifa frtppayakv lkevgfdils iannhsldfh
      121 eqgfvdtqkn lsdvgirytg kkgmitymnv kdisvawigf shlkshnnvn eigegvalvk
      181 eakkkaqlvf isfhggaegg palhvknqme rfygeyrgnl vefshslida gadlvighgp
      241 hlvramelyk grliayslgn fmgyralssr givsyslvle vevdsqgkfv kgkilplqld
      301 sasipeydpe kktidlmkkl tkedfpgkgp kiaddgtilp gt
//
LOCUS       WP_010678875             196 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Leptospira interrogans].
ACCESSION   WP_010678875
VERSION     WP_010678875.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..196
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21962
     Region          119..195
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 meqpnstiti vkksrlrrwi dryrmeffls vsfllqifil ffwytpsiqf drldrlvdev
       61 afvdnlviqe pnvgevaddg efevtdtikk kedpriagaq daiisgatap vdltpnitpd
      121 ypdearsagi tgtstlevii aengqvlrvr svgkslgfgl deaaieafyk kryspsildg
      181 rpitvkvlip vrfsly
//
LOCUS       WP_010679070             165 aa            linear   BCT 01-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Leptospira interrogans].
ACCESSION   WP_010679070
VERSION     WP_010679070.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..165
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=18943
     Region          29..145
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(59,62)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mwnlrliflf vffllfscsl sreesilyql slydldknsv slkeykgkvl lldiwaswce
       61 pckdavpvle klakdlngkn gvllgintep elskeehlna akefgmtypf fvdrdftlin
      121 qykvegqpal ivfsqsgtll kiqygirekd ypklranfsn wfsap
//
LOCUS       WP_010679123             201 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Leptospira interrogans].
ACCESSION   WP_010679123
VERSION     WP_010679123.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Ko,T.P., Lin,J.J., Hu,C.Y., Hsu,Y.H., Wang,A.H. and Liaw,S.H.
  TITLE     Crystal structure of yeast cytosine deaminase. Insights into enzyme
            mechanism and evolution
  JOURNAL   J Biol Chem 278 (21), 19111-19117 (2003)
   PUBMED   12637534
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Carter,C.W. Jr.
  TITLE     The nucleoside deaminases for cytidine and adenosine: structure,
            transition state stabilization, mechanism, and evolution
  JOURNAL   Biochimie 77 (1-2), 92-98 (1995)
   PUBMED   7599282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..201
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0001882 - nucleoside binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22927
     Region          69..163
                     /region_name="nucleoside_deaminase"
                     /note="Nucleoside deaminases include adenosine, guanine
                     and cytosine deaminases. These enzymes are Zn dependent
                     and catalyze the deamination of nucleosides. The zinc ion
                     in the active site plays a central role in the proposed
                     catalytic mechanism, activating a...; cd01285"
                     /db_xref="CDD:238612"
     Site            order(76,92,103..105,133,136)
                     /site_type="active"
                     /note="nucleoside/Zn binding site [active]"
                     /db_xref="CDD:238612"
     Site            order(101,106,110,134..135,138..139,142..143)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238612"
     Site            order(103..105,132..133,136)
                     /site_type="active"
                     /note="catalytic motif [active]"
                     /db_xref="CDD:238612"
ORIGIN      
        1 mskspsdqnl sgkksdsdqk kvkteflisk siesdsiafq lstkedsvik tdskilsdfl
       61 nklenlvtrd reeipsftri yhkekliset fnevekksds sfhseilcir nakeklktry
      121 ladcmlitsl epclmcagti llsripkvvy llpakqgegi sslsiemiys rnffpelfci
      181 pteisknafk sffkvrrkkf n
//
LOCUS       WP_010679143             222 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Leptospira interrogans].
ACCESSION   WP_010679143
VERSION     WP_010679143.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..222
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25850
     Region          107..205
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mtfrlskeei ekqirsmlse gltgtvndff swirmdtirk fkdepdlent ivenilesfv
       61 essyvkrskf nskefhihpd viqdkkfppk ecytllgkit fqpmqyvrsr fefflknqgt
      121 pedlvvdlci gvleavenav kygdgtevev eyyidpsqtl fiqiinnlke lnleqdierg
      181 kfsstatlmr gmmvmqklfd eldleilenk kqaqfnakkk ls
//
LOCUS       WP_010679151             197 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Leptospira
            interrogans].
ACCESSION   WP_010679151
VERSION     WP_010679151.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..197
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22223
     Region          2..189
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mitllicllt fgmsvwcfas eeklykfilt pyrlernkny ytlftsgfih adwmhlifnm
       61 vsfysfgknl emtvgpirfi lfylgtilit sviswrknld nphystlgas ggicgvlfat
      121 ilfypslsly mmfipipipg avyavlyliy tyfssksgaa dginhdahlw galcgiafal
      181 llepmilsrv frnilgn
//
LOCUS       WP_010679156             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Leptospira interrogans].
ACCESSION   WP_010679156
VERSION     WP_010679156.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870074
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..321
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35985
     Region          11..229
                     /region_name="ST1585-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Sulfolobus
                     tokodaii ST1585 protein; MBL-fold metallo hydrolase
                     domain; cd07726"
                     /db_xref="CDD:293812"
     Site            order(71,73,75..76,160..161,179,229)
                     /site_type="active"
                     /db_xref="CDD:293812"
ORIGIN      
        1 mlsyekevfp glytidcdyi spgiacayli vengeaafve nntnhsipil leelqkvgrk
       61 pedvkyiiit hvhldhaggt gllakycpna tilahpkaak hlinperliq ssiqvygeen
      121 fkklygeilp vpqervkcpe dgeeiqwgnr ifkfyytrgh anhhfciyds lsngiftgds
      181 fglgykdfav gkepilypst tptdfdseea ihtvdkilst gankaylthf gvwknlesga
      241 rqmkrglyam qgilsseeks nlegkalles ctekvrdylk gellaqgivl gerekmilel
      301 dskinaqglv fqierkkrnk i
//
LOCUS       WP_010679210             277 aa            linear   BCT 01-JAN-2025
DEFINITION  undecaprenyl-diphosphate phosphatase [Leptospira interrogans].
ACCESSION   WP_010679210
VERSION     WP_010679210.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..277
                     /product="undecaprenyl-diphosphate phosphatase"
                     /EC_number="3.6.1.27"
                     /GO_function="GO:0050380 - undecaprenyl-diphosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=31254
     Region          4..273
                     /region_name="UppP"
                     /note="Undecaprenyl pyrophosphate phosphatase [Lipid
                     transport and metabolism]; COG1968"
                     /db_xref="CDD:441571"
ORIGIN      
        1 mnpylnaflr siieaitefl pvsstghlfl fssffpfyge nvefddlfdi fiqsgailsv
       61 lflyrekfks qivssfryil kqnsdsegfh fliqicigaf piliagfiak efldtikarp
      121 dlleilsgaw ifggvlilva ewyfhqrpee kkpigfkdsi ligifqcmal ipgmsrsaat
      181 iitarflgkd tkssaefsff lavpvllaag iyklikyrsi lngntipvlm fgflvsfllc
      241 tlvirwflry iqkhsfsvfg vyrillgvgv lvltkli
//
LOCUS       WP_010679283             380 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Leptospira interrogans].
ACCESSION   WP_010679283
VERSION     WP_010679283.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..380
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43133
     Region          65..166
                     /region_name="F5_F8_type_C"
                     /note="F5/8 type C domain; pfam00754"
                     /db_xref="CDD:459925"
     Region          <181..357
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mfnqfyfckl eylilriffi isfastsavs apiaygnlgs evdfidfgrw itapfsysvs
       61 ssfsaeyggf nlfdsdpnth wysanrsgse wvivdfgskr lingleitvp ifrkeravkk
      121 yeiqvlirdd wrtiltnqnv elhnfhklgn idasvlriyf pdstnhevvi sdlklflnqk
      181 llngieprlr gysfpvpdgl isnfdsqlpn aprtyrngvh kgidiykkke ldgqirnlnf
      241 qdeiispadg iviradhsys pmtlsdyeyh ttqsqkgtvt yvekdfggrq vwidhghgvm
      301 tsfnhlssih knikvgekvk qgesigtvgn sglleeakni sdnihlhfei wvdgeflgng
      361 lppaqvrkll qfffkrngvd
//
LOCUS       WP_010679341             550 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Leptospira
            interrogans].
ACCESSION   WP_010679341
VERSION     WP_010679341.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..550
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62590
     Region          2..>71
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Region          39..550
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 mptnkklssl ktrssgnses siydllvigg gitgahvlwd stlrgmksvl lekndyasgt
       61 sqatskmihg glrylknlel glvreslrer atlaritpqa vqtmgilvpl ysnldrivlk
      121 fgmilydals ydrntnickd rliprydfls keqtllespt ieheklkgay lyydylninp
      181 erhtcefifs arergaeakn ytevvsitrs nnslytiiak drisgkeivy ktravinaag
      241 pwadfieslv gveidkhlvr skgihvvtrk iggdkilvtk kkdgthlfvi pwrnktiigt
      301 tdteyadhpd hfrvtkkdie ellseinnsf gytnltlkdv dfyygglrpl vedsgeggst
      361 yntsrkteii dhrdlgfpgf ftamggkytt srgvaeevvn kvadylpknf rvcetslvpp
      421 stgnysdlvs likdlqkkfs kfngelietl afrygsqsyr ilekskpeee fyilqngekf
      481 yesevkfitn redirfatdf ffrrsgvgvp glleeqemnr lfrslgrhlg wnqnqirqei
      541 ktvkdrykiy
//
LOCUS       WP_010679440             166 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Leptospira interrogans].
ACCESSION   WP_010679440
VERSION     WP_010679440.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..166
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19449
     Region          1..157
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdalyreysg kifdflykys senpeiamdl mqdtflnffr kysdtdidqe qairllytia
       61 rnrsinysrk fstvkesgns emqefqeqkl sfvrkaelkd leerllvcld eleedekyal
      121 ilrfmedynl ttiaeimnis vstasrlivk atakvteiae kknlkp
//
LOCUS       WP_010679571             129 aa            linear   BCT 01-JAN-2025
DEFINITION  HIT family protein [Leptospira interrogans].
ACCESSION   WP_010679571
VERSION     WP_010679571.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..129
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15124
     Region          <37..123
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 msdcticnfh qfcdsseila rfgefsvrhs eqekklkgyl yieprshwts yldwsqesfl
       61 dfgkalefat nwiyknhspv kiytvtvsem vphmhfhlip rysddlkgid yiklalqgkl
      121 ledqsirdl
//
LOCUS       WP_010679579             730 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Leptospira interrogans].
ACCESSION   WP_010679579
VERSION     WP_010679579.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..730
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83673
     Region          23..715
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkeedkktse kengimvqgk kdkrdieifk tpssisrfne qdildkgisr tndidkqvpn
       61 faiidsgarn ftyynirgmr stlfsdpsvg livdgvplvd nvalntelfa ldsievhrgs
      121 qatvfaknfq ggvieintkk pnnmpqgrfm vdwgnykkke ysffynmpli knklyisisg
      181 kstqrngyln nvsgfnypnn lvsdipievh kthpdgrrgk sgrlrlfwtp lenlevdlqt
      241 naesfddgsl nivnylaskt errkslvkgc vvspevcdkn irtyinrtka vrkvfwdyeg
      301 vsnttgktys ssityklpka ifktvssirk meidplivdg dftrspviks eyiehsttrt
      361 hetsiesknk keplqfkigt lfyhkisdke fiqerlmqay tynvlkglna pakeihhsrv
      421 vdksfsffth nsytfwekft ltlgarietq rigighsrda rgvlfdnpyg dvrilsphyv
      481 rndsyrynvs riifdykpie slmifiglsr gyknggfstv vnqpslaafk peindtlevg
      541 ikskyfnetl gmnlayfyte tadfhvirai siaeainlna ekvtirgaem eaylkphksl
      601 qlgflagyte gifnkfydri ldtnfdgkhv hfipqydvvs ylqyrsspgl ffryefqvvg
      661 kmyfaadnti ysnpytitnl kigyeeerls aylycnninn eyyftsyidg tfqavpgapr
      721 tygfivnyki
//
LOCUS       WP_010679694             712 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Leptospira interrogans].
ACCESSION   WP_010679694
VERSION     WP_010679694.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 712)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 712)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 712)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..712
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79669
     Region          262..697
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mtnvknhsrf sayylgqwif gigtilvivs ffgnyyykek nidrlidnih wtvsylcaaa
       61 lawlgcfsve aagiyrfrfw falgltanal gqlswaiqvy fnyymtptps dflfpwvapc
      121 fiigysiivi ecdrnkirva aldalglita vltfslalyl pqregvgiaq llplinhpvs
      181 fltaaalgil lipvlrlqpn kswlsfivgm ggsgfcwllw nalfiveipp dgtvlnagfs
      241 istlilgygv wtwepklngh piwgrrfeaa lrllplfevv assvtivlag tlsglpegvr
      301 ivawtgttiv vliasvrqtl lvkemtdaeq eirlvnegle eivakrteel rtvnqylisk
      361 neqviraian lknaqkqlvr sekmavlgql vagiahelnt plgaivssne aiqlvlsnsw
      421 egllrnysdf tedekviwek lfskgitlre fydtreertk rkkiaillnd fgfseatrla
      481 diltdlgihp dyvlenfkyl sqkerlllia qnalslsgla rasftiekaa ekaslviqal
      541 keyayrdrse tamspvdvrk qletvltlyy skyktqveiv rempetsyvq gnaesltqvw
      601 tnlignalys mgykgkieis ckrvsttwev aikdsgagie esikdrifep ffttkpsgag
      661 tglgldicrr iiedhngkiy fetskegttf fvilpasepv lqkletqisk nq
//
LOCUS       WP_010679888             444 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Fusobacterium
            gonidiaformans].
ACCESSION   WP_010679888
VERSION     WP_010679888.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..444
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48576
     Region          10..439
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mkrdkkqmsp srklilgfll viivgvfllm lpfslkegks lsplealftv vsavcvtgls
       61 vvdvaevfsp vgdailiafi qigglgvmtf ssivfllagq kmtlytrill keernansvg
      121 eilnfvrlml ltvfiiesig avilmhefrk impyeqavyy gifhsisafc nagfslfsnn
      181 lenfrgnpvi sltisyliil ggmgfaiins fimmirkgvs rftltsklai qismiltfgg
      241 ailffllefs nsatlfplpw sekiiasifq svtlrtagfn tiplanlrsa tvfmaciwml
      301 igaspgstgg giktttlgvi lfyvigiirg kehveifnrr ldwdvmnkal allvvslsyi
      361 alvillllvi epfsmekivf evvsafgtvg ltmgitpylt vtsklliivt mfigrlgpmt
      421 ialalgekkk karvqypked ilig
//
LOCUS       WP_010679966             502 aa            linear   BCT 01-JAN-2025
DEFINITION  S8 family peptidase [Fusobacterium gonidiaformans].
ACCESSION   WP_010679966
VERSION     WP_010679966.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10141191
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..502
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=58528
     Region          105..364
                     /region_name="Peptidases_S8_Subtilisin_like_2"
                     /note="Peptidase S8 family domain in Subtilisin-like
                     proteins; cd04847"
                     /db_xref="CDD:173793"
     Site            order(111,140,190,207,242,330)
                     /site_type="active"
                     /db_xref="CDD:173793"
     Site            order(111,140,330)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173793"
ORIGIN      
        1 mteykkhyki klkkqntkke kdlqeerwek flkeknisye kkeffpgyei ykvgelsetl
       61 ekeiqenpei dfikplhryf lnfqtkqiet ekgtilkpkq gekypivgvl dngiapleef
      121 enwlyqdets yckeeiypsh gtfvagvily gdilsqehwc ggrevqifna avvpdfsvyq
      181 leedelyeri ykvisehswi kvwnlaisir fpvekdrisd fgllldylqe kydilicksc
      241 gngnfvengk eagmilqgsd teralvvaac nrdkvvssfs lsgkghkilq kpdiamyggd
      301 vfrneegkrk iegvfsfspe geivssfgts fatarmtria anilfwkens sslflkammv
      361 haargyekys lgygcslsse eiyqeyqnsi leegslveee sflfyfsnhk ivatltsdvv
      421 ldyhqeeeyi lediswrify qgreitgenq lgnfeyfssl kklecemkee ngevkivlfr
      481 rkkrkktqen keklqycllw kk
//
LOCUS       WP_010679979             504 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Fusobacterium
            gonidiaformans].
ACCESSION   WP_010679979
VERSION     WP_010679979.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 504)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..504
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56439
     Region          44..503
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mkkvftlllg llavlfvacg ekqsntegqe kvvvvsqgak pksldpymyn eipglavtrq
       61 fydslfkked dgsitpllae syeyktptel witlrqgvkf hngdiltvdd vlfsfqrmke
      121 tpasaimisd iekveavddk tfkiilkqss apllfslshp ltsilnkkyv eehqgniste
      181 pmgtgpykfv swgdgekiem aafddyfrgr akvdkvifre iiedssrlaa letgeidiay
      241 dmtaidsgti eakdnlvlis epttaveyic lnnqkspfdn klfrkaldya idrqsivdsv
      301 ymgrakitns ivnpnvfgfy dglnkftfdp ekakeliaes giknpkftls inegsdrqqa
      361 aqiiqanlrd vgidmqiqil ewgtylqsta egkfeaflgg wmsgtsdadi vlfplldtks
      421 fgsagnrary snpafdklve darseldvek rkelykeaql ilqedtpmti myaknknigv
      481 nkrikgfiyd ptnvhslytl eiae
//
LOCUS       WP_010679993             153 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Fusobacterium gonidiaformans].
ACCESSION   WP_010679993
VERSION     WP_010679993.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12134272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..153
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18792
     Region          5..134
                     /region_name="Acetyltransf_3"
                     /note="Acetyltransferase (GNAT) domain; pfam13302"
                     /db_xref="CDD:379112"
     Site            order(81..83,93..94)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 mniklrkmee rdiptiyqyi hkkyvkkyye keeekqwqah rnwycfvlns nsyffyiier
       61 eqefigtvry eleeekaivs iyireeyrnq gyaklalles iscllkevev egifahilqe
      121 necsqqvflh cgfqkykkev ywkeikvred rng
//
LOCUS       WP_010680001             300 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Fusobacterium gonidiaformans].
ACCESSION   WP_010680001
VERSION     WP_010680001.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..300
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=32861
     Region          5..279
                     /region_name="ASKHA_NBD_ROK_FnNanK-like"
                     /note="nucleotide-binding domain (NBD) of Fusobacterium
                     nucleatum N-acetylmannosamine kinase and similar proteins;
                     cd24068"
                     /db_xref="CDD:466918"
ORIGIN      
        1 mkqdkiiavd iggtnikyal vsfrgeilss gdipteaskg ieillskldn iiqtflteei
       61 lgiaisatgq idyyqgkvvg gnpiipgwig celvkileek yhlpcvlend vncaalgeaw
      121 lgagkgqkdf lcltigtgig ggiilnhdly rgasavagef gklylqnkee vyekyasmsa
      181 lvkkvetktg ehwngkkifd vywqgektiv slvdewihdi teglkvllyl wnpsciilgg
      241 avthqgeafq kkieeelqkq itpnylecle fkfanlgnha gllgaaflll dktkqeevkq
//
LOCUS       WP_010680006             237 aa            linear   BCT 01-JAN-2025
DEFINITION  vWA domain-containing protein [Fusobacterium gonidiaformans].
ACCESSION   WP_010680006
VERSION     WP_010680006.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..237
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=26985
     Region          27..220
                     /region_name="TerY"
                     /note="Uncharacterized conserved protein YegL, contains
                     vWA domain of TerY type [Function unknown]; COG4245"
                     /db_xref="CDD:443387"
ORIGIN      
        1 mkkillgill afslvacang ttkkevkakn ielvfildrs gsmfglekdt iggynsmlqk
       61 qkeqtgdvfv ttvlfddyye mlyhhknike lpnmtekeyf vrgstalyda igktivnvdr
      121 eqelaekkvd qvlfiittdg menasqefta kqvraliekq kkekkweflf lganidaeet
      181 aaqfgiskek avnyhadslg tqknykvlge avlqmrsgqq lkkewkqeie edyksrk
//
LOCUS       WP_010680063             227 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Fusobacterium gonidiaformans].
ACCESSION   WP_010680063
VERSION     WP_010680063.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..227
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25676
     Region          5..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnkfilelkh lekyyqetgt klhiirdlsf niekgefvti lgrsgsgkst llnliglldr
       61 adageiilgg kllssmneie knklrneflg fvfqfhyllp eftalenvml pamlakklkk
      121 eeiekraiel lisvglgerl qhkpnqlsgg ekqrvaiara linqpkllla deptgnldee
      181 tsetifkifk einekygqti ivvthsrela kissrqiylk kgmleei
//
LOCUS       WP_010680067             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Fusobacterium].
ACCESSION   WP_010680067
VERSION     WP_010680067.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..228
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26052
     Region          14..225
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mevsleeikk ievfhgitkk siekiqktae iislpqnkyl ytdkqnldyi yfvlsgkvvi
       61 skgnehgesr iifllssgam inqpfmrnnt saieciafen srilritfsd fatilsqdyk
      121 lckncmifme nrirrlyrql knsvsinldk klaaklyrlg iehgsssqee gmtkinlnit
      181 itclakmlgc qreslsramk slnsrkivkm igrsiyvdme aaknlfkn
//
LOCUS       WP_010680125             348 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Fusobacterium].
ACCESSION   WP_010680125
VERSION     WP_010680125.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..348
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39439
     Region          13..347
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 metnilhqvv gnvgqiilnr pkklnaldra svrelreile kfakdsevcf vilrsnieka
       61 fcaggdllsd kkileeegle amvdelraey alasqithfd kpilvylngi tmgggagisv
      121 gadirivtet tqwampemri glfpdvalsy yfarmqaglg eylaitsnsi qaedclwagv
      181 adykiqsgdy tslekellam dwygiekeei lkkiqkkveq ysspkcignl ekrskelkqy
      241 ftkssfkevf qsleqekets dfarsildsl nknstlsmai twellkrakk lsleecyqld
      301 lvlirsyfqg kdifegirai liektkdpkw eyknidgipt evvlsyfn
//
LOCUS       WP_010680172             317 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Fusobacterium gonidiaformans].
ACCESSION   WP_010680172
VERSION     WP_010680172.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..317
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33638
     Region          1..315
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mkyyagvdlg gtntkigicd aegkivssss iktdsirgvd dtlfriwtei qrqvleqkie
       61 kenlqgigig ipgpvknqsv vgffanfpwe kninlqekme kisgvttkld ndvnviaqge
      121 aifgaarghr ssitvalgtg igggifidgk lisgmtgagg evghmklvpd gklcgcgqkg
      181 cfeayasatg mirealsrly vnkqnalydk fqgnyeklea kdifeaaaag difsqeivdy
      241 eaeylamgig nllniinpev ivlgggiala keqilvpiqt kiskyaleit lenleiktgv
      301 lgneagilga aalfivs
//
LOCUS       WP_010680177             318 aa            linear   BCT 01-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Fusobacterium gonidiaformans].
ACCESSION   WP_010680177
VERSION     WP_010680177.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..318
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=36424
     Region          19..98
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(20,32..33,35..36,38..39,42..43,45,52..59,61)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          87..303
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mrrivenyey qvgeedqgkr ldlflkeqlp eatrsylekl itegyvlcne kvitkngrkl
       61 kgkeviqlai peeekmeiva enipldivye dkyllvvnkq anmvvhpalg nysgtlvnal
      121 lyyckenlsd mngvirpgiv hrldkdttgl iivaknnqvh sklalmfqek tirktyvaiv
      181 kgrfseekke grletlitrd skdrkkmtvs qiqgkkaisn yrvlldgdkh slvevkietg
      241 rthqirvhmk ylnhpilgdi vygqedtkck rqmlhayrle fihpiteeai clegklpedf
      301 ieagkrvfdg kdvgtvli
//
LOCUS       WP_010680231             378 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein
            [Fusobacterium].
ACCESSION   WP_010680231
VERSION     WP_010680231.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..378
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40580
     Region          1..378
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mayliseeaq dlladvkkfc enevkeqcke ydvtgewpke iydkaieqgy halevpeefg
       61 gpglsrvdva alleemaiad agfattisas glgmkpvlis gsqeqkqrva dlileggfga
      121 fcltepgags dasagkttav kdgdsyilng rkcfitngav asfycitamt dktkgvkgis
      181 mflveagtpg lstgnhenkm girtsntcdv vledcripas alvgkegegf aiamktldqa
      241 rtwmgciatg iaqrgineai aygkeriqfg kpviknqalq fkiadmeikt etarqmvaha
      301 ltkmdlglpf akesaiakcy agdiamevas eaiqvfggyg ysreypvekl irdakifqif
      361 egtneiqriv iannvigr
//
LOCUS       WP_010680337             274 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Fusobacterium
            gonidiaformans].
ACCESSION   WP_010680337
VERSION     WP_010680337.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10178918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..274
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006308 - DNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=32056
     Region          24..265
                     /region_name="MnuA_DNase1-like"
                     /note="Mycoplasma pulmonis MnuA nuclease-like; cd10283"
                     /db_xref="CDD:197338"
     Site            order(28..29,31,56,94,123,143,182,184,223..224,259..260)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197338"
     Site            order(28,56,94,143,182,184,224,259..260)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197338"
     Site            order(28,56,259)
                     /site_type="other"
                     /note="putative Mg binding site IVb [ion binding]"
                     /db_xref="CDD:197338"
     Site            order(30,143,182,184,260)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197338"
     Site            order(31,94,123,143,182,184,223,260)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:197338"
     Site            order(182,224,260)
                     /site_type="other"
                     /note="putative Mg binding site IVa [ion binding]"
                     /db_xref="CDD:197338"
ORIGIN      
        1 mkffyqcllf lclsiasfaq eayiasfnvl klgespkdfe tmaktiehfd lvgleevitp
       61 eglerlvksl nkytnhtwdy hispfpvgtr kykeyyayvw kkdrvtflss egfypdrekl
      121 firepyganf qigkfdftfv lqhavygkse terraeafql vkvyryfqdr nkkendilig
      181 gdfnlsafde afsslyedkd qiiygvdpri kttigmkkma nsydniflsk kyteeftgks
      241 gaidftnrqy kvmrnkvsdh lpvfiivnid rddd
//
LOCUS       WP_010680353             528 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Fusobacterium gonidiaformans].
ACCESSION   WP_010680353
VERSION     WP_010680353.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..528
                     /product="DEAD/DEAH box helicase"
                     /calculated_mol_wt=59677
     Region          10..419
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          453..522
                     /region_name="RRM_DbpA"
                     /note="RNA recognition motif (RRM) found in the DbpA
                     subfamily of prokaryotic DEAD-box rRNA helicases; cd12252"
                     /db_xref="CDD:409698"
     Site            order(460,465..468,470..472,474..475,481,484..487,
                     516..517,520)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409698"
ORIGIN      
        1 mekketlkef relgigekll kalskkgyet ptpiqsltip alltgekdii gqaqtgtgkt
       61 aafalpilen iehqdkiqgi vltptrelal qvaeemnslg sskkikiipv yggqsidiqr
      121 kllrngadii vgtpgrvidf ierkflrlqd lkyfildead emlnmgflee vekileatne
      181 dkrmlffsat mpneilkvak khmkdyeila vkarelttdl tdqiyfevne rdkfealcri
      241 idlaedfygi vfcrtktdvn evvgrlndrg ydaeglhgdi gqnyrevtlk rfkakkinil
      301 vatdvaargi dvndlshvin yaipqeaesy vhrigrtgra gkegtaitfi tpqeyrrllq
      361 iqkivkteir keevpevkdv iqakkfqiqk dideilgege ydkfkklaqd llkkeeaeni
      421 vasllklaye dvldesnyne isstksvggg karlfvalgr kdgmtakklv ekvmkvakvq
      481 dkkirnvevy eafsfitvpf keaeiiidsf karqkgkkpl iekaksqk
//
LOCUS       WP_010680442             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Fusobacterium].
ACCESSION   WP_010680442
VERSION     WP_010680442.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..161
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18230
     Region          3..148
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mrdllkkfel ylgsvfisvt vvvvimnvft ryflkftyfw teevavgcfv wtiflgtaaa
       61 yrergligve aivvllpkkv rkvvefftfl llviisaimf yfsltyvmgs skitsaleis
      121 ysyinsgivl sfalmtiysv ifavqcfkem itgkdckeie g
//
LOCUS       WP_010680487             229 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Fusobacterium gonidiaformans].
ACCESSION   WP_010680487
VERSION     WP_010680487.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..229
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25793
     Region          3..222
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mkilvtgats gigkavverl lqegnqvtgv grdfqkypie hvcyqkyscd frkmaemetl
       61 lrivareewd vvilvaglgy fapheeihfs kiqemvqvnl ssammivqat lrnlkkkrgq
      121 iifvssvtat kaspmgaays atkagishfa tslweevrky gvrvsviepd mtktdfyehn
      181 sfdvgeeadn yllaeevvda iffllsqrqg mnirrievqp qrhkitrkg
//
LOCUS       WP_010680523             214 aa            linear   BCT 01-JAN-2025
DEFINITION  precorrin-8X methylmutase [Fusobacterium gonidiaformans].
ACCESSION   WP_010680523
VERSION     WP_010680523.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..214
                     /product="precorrin-8X methylmutase"
                     /calculated_mol_wt=23637
     Region          3..206
                     /region_name="CobH"
                     /note="Precorrin-8X methylmutase CbiC/CobH [Coenzyme
                     transport and metabolism]; COG2082"
                     /db_xref="CDD:441685"
ORIGIN      
        1 mayikvpgdi ekrsfeiiee emgekihqfs eqelpivkri ihtsadfeyg dliefqnnai
       61 qsgieslrkg ckiycdtnmi vnglskpams kfacsayclv sdkevieeak kegltrsivg
      121 irkaakdket kifiignapt alyqlkemie rgeierpalv igvpvgfvga aeskeafksl
      181 dvpyitingr kggstigvgi lhgilyqiyk regf
//
LOCUS       WP_010680532             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Fusobacterium gonidiaformans].
ACCESSION   WP_010680532
VERSION     WP_010680532.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..389
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44413
     Region          20..315
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mkniialvwg esslkissil yssvitayll qigltnykig ilwsiilfvq micdyptggf
       61 adkygrlkif migmifmgts ifmmvsgngf llylgaiilg igesqvsgtl fpwfvhtlke
      121 kgvseeerke silkvnaqsq yitnflgili gflifpfdlk yktiliiagc vyilnglliy
      181 lffkdnrsde rdllkigkrs iaifcqdqkl wlyglamtlh yifysihlfi wqpkanalgi
      241 legklafvqs ifligmalsg fivkhinikt yfiyflasil ipislvyiyd ssnlkaylsf
      301 mfilslsngl ivplifgsmh ffipddvrss vvslmsslss illvffqaii gkildqhnfw
      361 ylsffcffig ilyicciyfi ykwrirnek
//
LOCUS       WP_010680533             208 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Fusobacterium gonidiaformans].
ACCESSION   WP_010680533
VERSION     WP_010680533.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..208
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24062
     Region          40..206
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mleilnninq ylyhkieetd pilleleaya kehkvpiitk evaeylkmml qikkchnale
       61 igtaigysgi yiarqitgql ttieideerf eeakvnfkka disnvvqilg datekikeiq
      121 enfdfifida skgqyqkffe dsypklnqgg lifidnilfr gyvceenypk rfktlvkkld
      181 efisylyksh nfvllpfgdg igivrksk
//
LOCUS       WP_010680541             266 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(+)/NADH kinase [Fusobacterium gonidiaformans].
ACCESSION   WP_010680541
VERSION     WP_010680541.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..266
                     /product="NAD(+)/NADH kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006741 - NADP biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0019674 - NAD metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=30000
     Region          3..262
                     /region_name="NadK"
                     /note="NAD kinase [Coenzyme transport and metabolism];
                     COG0061"
                     /db_xref="CDD:439831"
ORIGIN      
        1 mkkkvylyyn dgkeiaqely ekslpffqer gieimtkere neadfyvvig gdgtlltafk
       61 kfarvdipvi ainaghlgfl teikkedmfq eyqnflegks qtqkrhflkv kiggktyral
      121 nevvitresv vknmvklkvf sedsfvnhyk gdgliiatpt gstayslsag gpivgvpmkv
      181 yiltpiaphn lntrplvmdg ssplsvslie eekayciidg nneklldgnd rveisyseet
      241 lhlvvpknrd yysvireklk wgdnlc
//
LOCUS       WP_010680577             178 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Fusobacterium gonidiaformans].
ACCESSION   WP_010680577
VERSION     WP_010680577.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 178)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..178
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20539
     Region          41..167
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mkfkhkerke ifrndvvtvy nenlvlpngk evswtftgkk evvailaltk kqtvimveqy
       61 rpairrefle ipaglvekne lpleaakrel eeetgyqaes wtkicsyfgs agvsdgeyhl
      121 flakelkkth qhldedeflt vreipleeis iydlqdpksi iafqyyllss sccedtnk
//
LOCUS       WP_010680598             438 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Fusobacterium gonidiaformans].
ACCESSION   WP_010680598
VERSION     WP_010680598.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..438
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47863
     Region          15..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkydlvvvgg gpgglaaaie akkngiesil vierakelgg ilqqcihngf glhefkeelt
       61 gpeyagrfid qllemnieyk ldtmvldvtd kkevhainsk dgymlieaka ivfsmgcrer
      121 trgaisipgd rpagvftaga aqryinmegy mvgkrvvilg sgdiglimar rltlegaevl
      181 avaelmpfsg gltrnivqcl edyniplyls htvidiqgkd rvqkvilakv denrqpipgt
      241 eieyecdtll lsvglipend isrktgvemd rrtngpivne mmetsvpgif acgnvvhvhd
      301 lvdfvsgear kagkaaakyi kgevsegeyi flkngngisy tvpqkvrmvn vdnslevfmr
      361 vnrifkdvkl evkageevlm slkknhmapg emerimipka klevaqgkei vvevvegrqi
      421 iactsydnct eeavggak
//
LOCUS       WP_010680629             124 aa            linear   BCT 01-JAN-2025
DEFINITION  YegP family protein [Fusobacterium gonidiaformans].
ACCESSION   WP_010680629
VERSION     WP_010680629.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..124
                     /product="YegP family protein"
                     /calculated_mol_wt=13496
     Region          1..57
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
     Region          67..122
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
ORIGIN      
        1 mgkfivketk tgikfdllak nneviatsev ykakascmng iksvmtnsai atiedqtken
       61 tpkeknpkfe vykdkagefr frlkakngqi iatsegykak ascmngiesv kknasgapie
      121 elnk
//
LOCUS       WP_010680661             474 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Fusobacterium gonidiaformans].
ACCESSION   WP_010680661
VERSION     WP_010680661.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..474
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=55245
     Region          1..377
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mkiavayvrv stnkqdirgs klgqeqeikn yaskegyniv affddtehgd ianrvglddl
       61 kkylrmndsv kyvivyhsdr ftrgfqngiq dlffldglgi klvsvmegiq niegnydslp
      121 tivrmlgaqv ekdkmvqkvt tamyqyaeta rylggsifpw fsvekgyidg krckivvqnk
      181 dtwdfyrrff ltmiqsksik staekfglnl ntvqswlvvp elmgkrsygk kgkidklhnk
      241 grrqdylite kivfpalltk eeydkllylr hrhriqvred ikiylysqvl ycgcggkfeg
      301 nfirkigkeg kgtlyyrcsk cgkrinakkl erdlidricn dsrlqmlnev efrladlfde
      361 kteyekqini lrekekrvih lvtdgitsmd vveaelralk kqrdhfhsli nkidktiqee
      421 akkeitedni nmlkelltln lpdddfrisl keiinliirr itigntdnki yitf
//
LOCUS       WP_010680719             141 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Fusobacterium
            gonidiaformans].
ACCESSION   WP_010680719
VERSION     WP_010680719.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..141
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16433
     Region          4..136
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mniridnvge ylkehgikps yqrmrifqyl ldyhnhptvd viykalcpei ptlskttvyn
       61 tlnlfvekki vnviiieene trydlvstth ghfkcqecga vydvelkntp fqaesllegc
      121 qveeehfyfk gickncmekk h
//
LOCUS       WP_010680749             274 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Fusobacterium gonidiaformans].
ACCESSION   WP_010680749
VERSION     WP_010680749.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..274
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30615
     Region          1..270
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mksriivali gipilifvil fggipllift nfvvgigtwe fyrmiehsgr rvhkyvgmla
       61 slalpnyifw tqgqkvegei ailvfamvlm flervftnri ehasteignt vlgliyvsyf
      121 fshilkwsfw dnggqlilll qimvwscdsf ayfigisigr kifkrgftei spkksiegsl
      181 ggilctilaa ylllkyftlf laqtqeelli fslilgvgvs laaqigdlve slfkrecgik
      241 dsgkilaghg gildrfdsmi fvlpimyyim gavl
//
LOCUS       WP_010680777             258 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Fusobacterium gonidiaformans].
ACCESSION   WP_010680777
VERSION     WP_010680777.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..258
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29166
     Region          4..254
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(7..11,41..42,185,207..209,211..212)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mkwiisdldg tllnndrtvg ektilgvqnl lkkgypfvia tgrgfasant ireklgvpiy
       61 mvcnngasiy spkgelifen yipvemvkkv taclekyrvd yrgffqdyyf mpsygkedmk
      121 rieykavile kdedfqilek ilvvdpntdl lrkiqkelqe evgeeltitl sssecldins
      181 kncskaagie kvatylqlhl qdaiafgdse ndfamlasvg kavsmkgtya aqekdyevte
      241 ftnhedgvir hlekyikf
//
LOCUS       WP_010680793             210 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Fusobacterium gonidiaformans].
ACCESSION   WP_010680793
VERSION     WP_010680793.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..210
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=24331
     Region          2..136
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(7,9,66..67,70)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            9
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(65,117..118,120..121,125)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(71,76..77,113,116..117,120..121,124,127)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94..96,113..114,117..118,121,125,128,132)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94,118,121,125,128,132)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(126,132..133)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 miygyiriss ktqneerqii alkdagvssd nifidresgk nfnraswqkl maklvvgdtl
       61 iikeldrmgr nnkemkenfe liknkgcfle flenpllstr nksqieieli qplilhllgy
      121 faekerdkil trqkegydsl dtdekgrkis kkknkvvgrp skienlsleq kryieawiqg
      181 nikisdcikn trigktslfk ikklrrakiv
//
LOCUS       WP_010680808             478 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Fusobacterium gonidiaformans].
ACCESSION   WP_010680808
VERSION     WP_010680808.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..478
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55244
     Region          2..>82
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          50..456
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkrkwnlffc llfltscssv nkeasensll qelqnkeket qeilkeqkls leeairlake
       61 rnlelkmkel ekeiasidkr iafgnflpki safytrsfwe eplsaqidlp sslgkfpmig
      121 pllpkeihgr lldqnysvyg mqasmpifap atwflysark kgedihslvf dltekmitvk
      181 viqqyywila lkseekqlqa slqsaeqllh ntkialetqs ildwqyqkae vyykqkklal
      241 eenrrdlkia nmnllltlnl spfseiyled anlstkkpll nyeevvyqsl lhsqaleiqn
      301 kmievekekv kislsrflpi vglqgfygeh sfslltsphy lfgilggvfs vfngfqdisa
      361 yqkakieqqk aiikreqlml qtiaettnvy qklqssleeq eiaqgnlkae ngkfyqkeme
      421 kkvgmidels ylqalqsyee arslnakaey qsavlqeild mlmeqgrfvk iregekne
//
LOCUS       WP_010680864             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TlyA family RNA methyltransferase [Fusobacterium].
ACCESSION   WP_010680864
VERSION     WP_010680864.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..267
                     /product="TlyA family RNA methyltransferase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30331
     Region          3..244
                     /region_name="YqxC"
                     /note="Predicted rRNA methylase YqxC, contains S4 and FtsJ
                     domains [Translation, ribosomal structure and biogenesis];
                     COG1189"
                     /db_xref="CDD:440802"
ORIGIN      
        1 mkerldqilw kygyvdsiek akrlimlgav ivneqridka gtlfkyseem nirvkgqenp
       61 yvsrggfklk kaidhfacsf qgkrvldiga stggftdcsl qegaayvyal dvgtnqlawk
      121 lrkdpkvksi eqchvkdlnw dildqesvdy ivmdvsfisv cgifrylypf leengkllll
      181 ikpqfevekh flekgivyer kahqevlerv ieiakengff lqnieispil ggkgnveyis
      241 cfskqqtsav lelesileka kemgglk
//
LOCUS       WP_010680929            1051 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Acetivibrio
            cellulolyticus].
ACCESSION   WP_010680929
VERSION     WP_010680929.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1051)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1051)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1051)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1051)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..1051
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=122060
     Region          1..1043
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 msreteynem yisqipalev lskigyivlp fekaeamrgn lynvilkdil yeklkeinhf
       61 eykskchkfs eknikqaiqd ldealtdglm ktnekiydsl llgrsyaekl pdvdgtrsfd
      121 inyidwkkpe nnifhvveef sveredgqgn arpdivlfin gipfavieck kasisisqgi
      181 sqmlrnqgkg yipqlfkfiq ivmatnknet qyattgtpkk fwsvwkedek sveykwfeke
      241 lgkavtdrip ttqdknivsl fhpnrvlqli ryfnlydkni kkiaryqqyf aikeiiktve
      301 emdkngnrqs gviwhtqgsg ksltmvmlar yllsemaevh pqllvitdri eldsqihktf
      361 nhsrlkaera tsgknlveli nnngadiits lvhkfdtasr hqepvksrni fvlideshrt
      421 qygelhikmk kvfpnscylg ftgtplmkkd kstmnkfgsr mihqytikng vddgaivplf
      481 yegrlveqtv nrnaidrrie mitrnlnekq aeelknkwsk feaiasseqr irliaddiyv
      541 hykqfykgty akailatask sdairyqeaf eefedvstav visppdqreg yeevdeepkd
      601 rvlkfwrkmt eeysdpdkye ehvksefvdg delevlivvd klltgfdapr atilyidkpm
      661 kdhtllqaia rvnrlyegkd fglivdyrgl iaeldsamkt ysgaglenfd gkdleralvd
      721 vistlgklre sysnvvaifk avknksdkee yeliledevi rndfynelse fgrylgiale
      781 sehvynaige kdillykkef kfyqelrasv klrysdtidh keyepkmrnl mdtyiaaedv
      841 iqitapvdil deeefeeelm rldskrakad airtrmtkri nakwdenpay yktfaqriee
      901 iikaykekri seadylerin avkrdfrkgy setvypekik hnthaqafyg vikdiledet
      961 scdagvsggi nepgriynye dilaelatdi dividkhskv dwhdnpdvhn risqeidgll
     1021 yiakkkhfpd lsykqidkli eniktvalrr y
//
LOCUS       WP_010681038              73 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF378 domain-containing protein [Acetivibrio cellulolyticus].
ACCESSION   WP_010681038
VERSION     WP_010681038.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..73
                     /product="DUF378 domain-containing protein"
                     /calculated_mol_wt=7798
     Region          6..72
                     /region_name="YuzA"
                     /note="Uncharacterized membrane protein YuzA, DUF378
                     family [Function unknown]; COG2155"
                     /db_xref="CDD:441758"
ORIGIN      
        1 msrtpldrla lvlvvigaln wllvglfqyd lvaglfggtg tflsrtiysi vglaglysis
       61 llfreaptvr dkv
//
LOCUS       WP_010681067             569 aa            linear   BCT 01-JAN-2025
DEFINITION  vWA domain-containing protein [Acetivibrio cellulolyticus].
ACCESSION   WP_010681067
VERSION     WP_010681067.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10646251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..569
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=62761
     Region          78..346
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
     Region          330..565
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
ORIGIN      
        1 mrrqfrnilc ilvstivcil sgcsvtekpd tpdtekkvpq gaielklmig ndkqwifdev
       61 qkildqkavk vngksiyist ekagtgeame kvitkgadyv gwmpassthi lwanerwyan
      121 gntkpivded yttvflsptv iamqeslaki mgypnkkigw qdiyalstaa dgwgmygkai
      181 lnpvrfahth paksnsglna liaaeyafsg kkkglsiddv ktnssklkql eqtivhyges
      241 tsllqkkive kgpsfiqyav lyeymvasmn vnspgkdklv aiypsegtiw gdvcftkvls
      301 dnitedqska ldevkkills kdlqtkgmne yffrpadssi plsnaisvqn gvnpsepqtt
      361 lelpgidvin gilndwqtnm kkranvlfvi dtsgsmsgep idnarsaiqn lfnkeaqekn
      421 ytsiddedti slmtfntdvs dvytvkgkdi semsvvidsl sasgnthlyd avdkaitehq
      481 alkqsesekk idiivvlsdg adtnsqiqfs qlesmlkqke gnlpviitig ygnvdkdvle
      541 sisdktggky yegnpdtikk vfeeiktff
//
LOCUS       WP_010681079             259 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Acetivibrio cellulolyticus].
ACCESSION   WP_010681079
VERSION     WP_010681079.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..259
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29373
     Region          2..254
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mlfdthahyd dekfiedrfd viekahssgv syiinastdi ksckeslafa qkyeyvyaav
       61 gihpheldgv ddstlaklle fakedkvvai geigldyyyd tapreiqqhw fsqqidlare
      121 lrlpiivhdr dahqdsvdii kaqkasevgg vfhcysgsve makelincnf yisvggsltf
      181 knakklvevv rcipmerlli etdcpyltpe phrgkrndss yvrfvaekva eirqmdfeev
      241 aeatlrnake lfkikapgy
//
LOCUS       WP_010681256             238 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Acetivibrio cellulolyticus].
ACCESSION   WP_010681256
VERSION     WP_010681256.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..238
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=26600
     Region          10..238
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mpnsrpiigi sagfdysenr lfinngyiea irlagglpvl lpvtndtell khiigrfdgf
       61 llsggsdvda rfwgepnytf ggeisplrde pelfiareai aadkpilgic rgcqvmniam
      121 ggtiyqdiya qqvgkeiykh sqnapkwypt hdifiekdtk vfkahqeeii rvnsfhhqav
      181 kdvapgfivs srcgdgives iehisckfav gvqwhpelmw ekdntylkif vkfvalck
//
LOCUS       WP_010681309             224 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Acetivibrio cellulolyticus].
ACCESSION   WP_010681309
VERSION     WP_010681309.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..224
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24718
     Region          1..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnkiielkgv sksfelantk vkvleninle ieegefisim gpsgsgkstl lyliggldka
       61 segailvngv emrklsdnle skirrndmgf ifqaynlidn ltleenillp allegkkkka
      121 vlrkaeelmd ivgilhrrnh tpkelsggeq qrtaiarali ndpdilfade pignldsksg
      181 tevlellgki nkergitilm vthseestry gnriirlkdg riia
//
LOCUS       WP_010681327             253 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [Acetivibrio cellulolyticus].
ACCESSION   WP_010681327
VERSION     WP_010681327.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..253
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=28473
     Region          6..159
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mnisklfrrf waycfdimiv cginsgilll tkvldtnntl naalqelrtv fskgilvnil
       61 ngqayyialf flsygllfli yeiiflsskl satpgklilr levacgnkvn ffkvftrsll
      121 kviatlvfpl tfiaflisac thtkqtlhdk lantyvitvn tsnrgttphm slneffeemt
      181 srglrmyseq kalaeeiygs pvidpaksne taslvgilvl vfsiilnlsl lsysypdikn
      241 yvqdftlyyt qkl
//
LOCUS       WP_010681346             255 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Acetivibrio
            cellulolyticus].
ACCESSION   WP_010681346
VERSION     WP_010681346.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..255
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29224
     Region          <128..173
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 mlkrstkyly rnmlkyvgir kkfccicnka vvgflpyege fknfsftelk ivgsdvrnfm
       61 cphcrcidre rhlflyakkl dliskmsnak ilhfapekni skiineikps kyikadlypt
      121 spdiqkidml sipfedntfd fvianhvleh vsdvsialke lnrilkiggl gvlqtpyssv
      181 lqntfsdpgi ssdsarlnly gqedhvrvfg ndifqiitsn gfksrvcthh eilydidpiq
      241 ygvnvleplf lfeki
//
LOCUS       WP_010681414             560 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ShlB/FhaC/HecB family hemolysin secretion/activation
            protein [Pectobacterium].
ACCESSION   WP_010681414
VERSION     WP_010681414.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..560
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61887
     Region          21..553
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mcktlsfisl iflslssstf aataisptdr dalelqqksl leqakqqrls lensttltip
       61 tvtaptvkda vcfpiqnivf hdaeslstkd raavqrryqn rcldlatihn vvrettntyl
      121 nrgfvtsqay lqeqdlsngt liisvsegki eairmegetp laikmafpgl egrilnlrdi
      181 eqgmeqlnrl psqqvtidiq pgkqagssiv ylkrtthsrp vtlslstdns gqkstgreql
      241 sthltfdnpl rladrwwlta srdsafshsy gskalsggms lpygywtlgy qyawndffqp
      301 ipigssayry egqsnthrls lnrtlyrdgk qklaldgals rrrtenrmag erlevssptv
      361 ssaslglsys ttlvggyftl npmlshgvrs wgatddtken sglprsefrk fsvsssyfyp
      421 lapslyflts lygqttpdnl ytservslgg eysvrgfkeq tltgnrgfyw rnelnwqftt
      481 lpflgdialt taldsgwiag kagkvdggnm tgasvglsas srwvsqsvsl gvplhfpndl
      541 hpdnavvywq vslpvtaffn
//
LOCUS       WP_010681434             403 aa            linear   BCT 01-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Pectobacterium
            brasiliense].
ACCESSION   WP_010681434
VERSION     WP_010681434.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium brasiliense
  ORGANISM  Pectobacterium brasiliense
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pectobacterium brasiliense"
                     /db_xref="taxon:180957"
     Protein         1..403
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41807
     Region          1..392
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mpasfalkdv tfstliagfv avlvgytssa aiifqaaeaa gasamqiggw lsmlgiaqgl
       61 asislslyyr apilaawstp gaallvtslp gtslneaigv flfasalifi cgitglfarl
      121 mnvipqaisa amlagillrf gadaflslqq dfwlafamcv tyllsrrllp rfaivltlla
      181 glllalfrgq iavsdsplvf avpelitphf swasllgvgi pffivtmasq napgvatlka
      241 agyqvpispl itvtaliali ltpfggfsvc iaaitaaicm gpdvhpdpkk rylaaiaagg
      301 fyllagvfgg sigqlftalp qplihaiagl allstisgsl yralldeqqr daavvtflit
      361 asgltlwgig aafwgliggm mtwlvlsggk rrhadgirnt ger
//
LOCUS       WP_010681492             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pectobacterium brasiliense].
ACCESSION   WP_010681492
VERSION     WP_010681492.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium brasiliense
  ORGANISM  Pectobacterium brasiliense
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pectobacterium brasiliense"
                     /db_xref="taxon:180957"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32780
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like_7"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08476"
                     /db_xref="CDD:176165"
     Site            order(100,104,143,157,159,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176165"
     Site            order(101..102,106..107,109..110,113,117,119..125,186,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176165"
ORIGIN      
        1 mdslngfvvf vqvaetrsfv aagrllgvsa savgksiarl eeklgvrlfh rstrsitlta
       61 egslflarsr rilaeieaae lelsqtsavp rgrlrvslpl vsslvlpvlg dfmhkypeie
      121 ldldftdrmv dvieegfdav vrtgdpvdsr ltarrlgtfr flvvaapeyl aqsgcpqtpa
      181 dlmqhaclhy rfpnsgklep walrlppgep elplptsmic nnietrvcfa lqglgiaylp
      241 dfsirellae gqlqpiltdy versgvfyvl wpsskhpspk vralvdflca rvfpasdt
//
LOCUS       WP_010681529             392 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter permease [Pectobacterium brasiliense].
ACCESSION   WP_010681529
VERSION     WP_010681529.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium brasiliense
  ORGANISM  Pectobacterium brasiliense
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Pectobacterium brasiliense"
                     /db_xref="taxon:180957"
     Protein         1..392
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43228
     Region          3..392
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mlqrptvkgd lsltnpavra wlyqivvvia vlavaayllh ntvtnlsqrg itsgfdflnk
       61 sagfgivqhl idyqqgdtya riflvglfnt llvsalcivf asilgftvgl arlsdnwllr
      121 kisnvyieif rnippllqif fwyfavlrnl pgprqsisaf dvaflsnrgf ylpspewgpg
      181 aaafflslii tlvvtwgvfr rnqryhastg qprrtwpltl glllvlcals hlifgpafhw
      241 dmpelkgfnf rggmvlipel aaltvalsvy tssfiaeiir sgiqsvshgq heaarslglp
      301 npvtlrkvil pqalrviipp ltsqylnivk nsslaaaigy pdmvslfagt vlnqtgqaie
      361 tiaitmsvyl iisllisllm nlynrkialv er
//
LOCUS       WP_010681546             252 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pectobacterium brasiliense].
ACCESSION   WP_010681546
VERSION     WP_010681546.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium brasiliense
  ORGANISM  Pectobacterium brasiliense
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Pectobacterium brasiliense"
                     /db_xref="taxon:180957"
     Protein         1..252
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26665
     Region          8..252
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtgssiatlq avsvgygrtv vnhdisfslp sgqitcllgt ngsgkttlmr tllglipafs
       61 gqihiaekpi aawsaralaq vaayvpqahd spfafrvldm vlmgchprls lfstpgkrei
      121 asaeavlsql gilslsqrsy atlsggerqr vliaralvqq palmvmdepa asldfgnqir
      181 llahikrlke ssiavlmsth hpqharavad nvvllhpgag teqgtpdall tptklaalyg
      241 vqeadihahf rt
//
LOCUS       WP_010681609             327 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Pectobacterium].
ACCESSION   WP_010681609
VERSION     WP_010681609.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..327
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35574
     Region          38..291
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(53,136,138,140..141,168,223,244,247,260,262,291)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mkllkplall lvscafvpaf tqaqdiaqik tqpgyyrmml gqfeitalsd gtntmpmdkl
       61 lqrtppekit ellaekaltp qvetsinayl vntgkhlili dtgngkqsnp tvgkvlpnli
      121 aagykpeqvd tvlmthlhgd hfgglvqdnk lsypnatvyv sqpetdfwls pdnlknapen
      181 rksafqrvqs tfdvirkenk lktfpaqqtt llpgvtaips pghtpghtsf liesegkkll
      241 awgdiihaea vqmslpatti sfdsnmdqat esrnkalada asqgywvaga hlpfpgighv
      301 gtrlerngtt ngyrwlpany svaglkn
//
LOCUS       WP_010681612             519 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pectobacterium].
ACCESSION   WP_010681612
VERSION     WP_010681612.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..519
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57555
     Region          1..468
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mktrkiglan ylaygsgdfl gagttaltaa wllyfyttfc gltpieatfi famarvldav
       61 vsplmgfltd nfgstwlgkr fgrrkffill gipfvfsysf mwvgdmsywy ylltyllfdi
      121 vytmvlvpye tlvpemtddf kqktkfsgar ialaqlsail aaflpgillg yfgkdnaisf
      181 fysslvfsvi calvltlvyf ftwerprdqm seaslraeke rqsltlgqsl krlnvelvst
      241 lririfrqhl gmylggyiaq dvfnavftyy vvfvlmqspt masslmgtma ilqfiavigm
      301 iplcirfgpa psyrlvvclf gvsalsyavl wysglhdtfs llllisalag igrgginyvp
      361 wntytyiadv devitaqrre gifagimtlt rkasqagavm lvgvvlqlsg fvsgqsvqap
      421 gvshtilmil sfgtvgvlal gflvslrfkl nlqthsvlre etlkmreagr pvpenitpqa
      481 ratvemlagm pyeslwgnnn igylnrhkgd kpvthatqs
//
LOCUS       WP_010681632             194 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Pectobacterium brasiliense].
ACCESSION   WP_010681632
VERSION     WP_010681632.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium brasiliense
  ORGANISM  Pectobacterium brasiliense
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10536250
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Pectobacterium brasiliense"
                     /db_xref="taxon:180957"
     Protein         1..194
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22136
     Region          19..181
                     /region_name="Ser_hydrolase"
                     /note="Serine hydrolase; pfam06821"
                     /db_xref="CDD:399658"
ORIGIN      
        1 mqtteierrl tevsqkltmv lvpglrdsdd ehwqshwerr fphwhrirqr ewyqadldrw
       61 vlairrelsv ctqpviligh sfgalaschv vqqgqegiag vmlvapaepm rfeiddriqa
      121 aplsvptltf ashndplmsf traqywahaw dselvdvgea ghinaeagfg pweygltrla
      181 efsetlinrp vsik
//
LOCUS       WP_010681677             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Pectobacterium].
ACCESSION   WP_010681677
VERSION     WP_010681677.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 269)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..269
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29477
     Region          4..266
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mrlkkliplm lalgisqaya adsgkeitig vspgpygdmv tkaikpemvk kgyevkvref
       61 sdyiqpnlal snksidanlf qnrryldrfs adkglklaev itvptasmgf ysnkvrslde
      121 lkagdivtlp ndpsnlarsl dflqkyglik inpditptka slrditenpk glvfkpleaa
      181 qlpralggvt gslinanfai saglnlsdai qldvlpedlk nmivvraeda dkpfaqdlka
      241 avqspefaaf fedknsmfha fqkpewmkk
//
LOCUS       WP_010681807             244 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Leuconostoc
            lactis].
ACCESSION   WP_010681807
VERSION     WP_010681807.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc lactis
  ORGANISM  Leuconostoc lactis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Leuconostoc lactis"
                     /db_xref="taxon:1246"
     Protein         1..244
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26517
     Region          1..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mitvknlvqq ygdrraldqv sttfpaeqtt vilgpsgsgk stllrtlnll aqptsgtlai
       61 geqtldlgqp ltaskllavr qhfgmvfqek alfthltvlk nltqgpikvk gipadqataq
      121 anslltqfdm aalaprypyq lsggqqqrva ilralamqpd yllldeptsa ldpeleaqvl
      181 rvlrdladqk ksmvivthnl afaqavadki ifmedgkigy dgpsagffqa hdpriqrfln
      241 amtf
//
LOCUS       WP_010681860             285 aa            linear   BCT 01-JAN-2025
DEFINITION  carbon-nitrogen hydrolase family protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010681860
VERSION     WP_010681860.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..285
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30394
     Region          7..270
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(45,99,116,120,132,157..158,160..161,182)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(45,116,157)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(117..118,138..140,158,161..165,167..168,190..191,
                     194..195,197..199,201..202,232,263..264,267..268,270)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mpesrftaac vqmrsgrnpe anrdaavagv reaagrgaaf vqtpemtslv ersrerlfae
       61 vtteaqdrtl aavrevaret gvvvqigsia vrsgdkianr ayligsdgdv vasydklhlf
      121 dvdlpsgerw resatytgga cavvaptpwa mlglticydi rfpglyrala eagaeiltap
      181 acftrqtgea hwhvlqrara ietgsfvisa aqgglhedgr etfghsvivd pwgrvladag
      241 gsepcvilae idvaqvadar aripslqhgr pftvervgpk iqaaq
//
LOCUS       WP_010681897             480 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010681897
VERSION     WP_010681897.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..480
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50484
     Region          1..396
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 maviaafvln aglnfvlgll iakllgpadf grfalattga ivlntvlfew lrlsatrfys
       61 grvrvdepwi rhgldraylr igllllaaaa lcgafgfagg adgreavlcg tglaalgigv
      121 fdyhaalara rfdgklylgl vavknvlsfa lmaaaawwlp qpawvlaaag vsqllavvll
      181 rhplrdprta ferprltatw gvfaryglpl iaantayqcl afvnrgaiag qagfaeagyf
      241 alaadvtars fmtlgtaldl llfqlavqae eqhgrvaaea qvaenagtvf allapcavgf
      301 wavlpalqgl vvpeayrgpf etysvalmpg lfclsmmfya lnpvfqirrr tfpvvaaalv
      361 gltvngagll vlpdqaggig valaqtvglt aaalwlgwra ltgterlqlp wteigvaala
      421 caamglvlap frhlppvtal avlvpagmal ygalvwlfdi aglrrqvlar lrpgravvae
//
LOCUS       WP_010681160             252 aa            linear   BCT 01-JAN-2025
DEFINITION  imidazole glycerol phosphate synthase subunit HisF [Acetivibrio
            cellulolyticus].
ACCESSION   WP_010681160
VERSION     WP_010681160.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     Enzymes with molecular tunnels
  JOURNAL   Acc Chem Res 36 (7), 539-548 (2003)
   PUBMED   12859215
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Myers,R.S., Jensen,J.R., Deras,I.L., Smith,J.L. and Davisson,V.J.
  TITLE     Substrate-induced changes in the ammonia channel for imidazole
            glycerol phosphate synthase
  JOURNAL   Biochemistry 42 (23), 7013-7022 (2003)
   PUBMED   12795596
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Fani,R., Mori,E., Tamburini,E. and Lazcano,A.
  TITLE     Evolution of the structure and chromosomal distribution of
            histidine biosynthetic genes
  JOURNAL   Orig Life Evol Biosph 28 (4-6), 555-570 (1998)
   PUBMED   9742729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785016
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     gene            1..252
                     /gene="hisF"
     Protein         1..252
                     /product="imidazole glycerol phosphate synthase subunit
                     HisF"
                     /EC_number="4.3.2.10"
                     /GO_function="GO:0000107 - imidazoleglycerol-phosphate
                     synthase activity [Evidence IEA]"
                     /GO_process="GO:0000105 - L-histidine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27319
     Region          4..252
                     /region_name="HisF"
                     /note="Imidazole glycerol phosphate synthase subunit HisF
                     [Amino acid transport and metabolism]; COG0107"
                     /db_xref="CDD:439877"
ORIGIN      
        1 mkniriisrl dvkgpnlvkg ihleglrkig dpnefsksyy fggideiiyi divaslynrn
       61 nltdiviktt kdvfipitvg ggirsvndar dvlragadkv aintaaikrp elvkevaemf
      121 gsqcmvlsie akktasgkwe ayydngrekt gidvvewakr gyelgageil ltsidmegte
      181 kgfdlglvka vsevvpipvi asggagntnd ikkvietgka davavasilh ynrteigimk
      241 kelhsteinv rl
//
LOCUS       WP_010681929             158 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Methylobacterium mesophilicum].
ACCESSION   WP_010681929
VERSION     WP_010681929.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 158)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..158
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16380
     Region          19..145
                     /region_name="NUDIX_ADPRase"
                     /note="ADP-ribose pyrophosphatase; cd04673"
                     /db_xref="CDD:467557"
ORIGIN      
        1 mtadapaads rlfparpfvg asiavirgdr vllaaranep mrgvwtlpgg lveageslae
       61 aalrelseev glsaavvgvl ppteiivrde agrarhhyvv hphaalwqgg epvagpealg
      121 trwatlaeva tlpttpglid tlraafarta lqdreata
//
LOCUS       WP_010682144             294 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Methylobacterium mesophilicum].
ACCESSION   WP_010682144
VERSION     WP_010682144.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..294
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32089
     Region          <4..284
                     /region_name="bifunc_ST_SDO"
                     /note="bifunctional sulfur transferase/dioxygenase Blh;
                     NF040641"
                     /db_xref="CDD:468609"
ORIGIN      
        1 mtepviraff deptntvsyi vadpdtkqaa fidpvldydh sggsvdtrsv eamlkaared
       61 gftvvwtlet hahadhlsgs pyvkaktgak igigehikev qkifrpvfna tdlktdgsdf
      121 drlfvdgeaf aignlavevl ytpghtpadi cyhigghvfv gdtlfmpdfg taradfpggd
      181 vrtlyrsirk lltlppetvl hmchdykapg rdvyawettv geqrernvhv kegvseeeft
      241 amrtardatl aaprlllpsi qvniragkfp paeangvhyl tipvklkgga elgv
//
LOCUS       WP_010682128             129 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010682128
VERSION     WP_010682128.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..129
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=13921
     Region          32..126
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(53,56)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mttrrfllga laaapllfgt atnaaeavft pdafeaaqka gkpilvhvta pwctvcaaqk
       61 pilakleaqp rfkdlqvfdv dfdsrkdvlk rfgvttqstl itfkdeketg rsvgdtqpew
      121 iegavekal
//
LOCUS       WP_010682202             290 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease
            [Methylobacterium mesophilicum].
ACCESSION   WP_010682202
VERSION     WP_010682202.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..290
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=29813
     Region          1..288
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mneliqhlvn alilggtyal lgigltlifg imnvvnfthg alytvgayvm ylavsalgln
       61 fflalpvaiv gglllgaaie lvllrpfrgs didttmlvmi gagiilqsgt lwtfggvaka
      121 ipapfpeapl qigpvsvswl rlfvlgaala lialtyalin rtklglamra afqdadtaal
      181 mgvdvrriyt atfalgssla aaagallgpv yvvfpqmggl aelkafaivi lgglgnvtga
      241 aiggfilala eelgagyvss gyrdamgfli iiavllykpt glfakaerig
//
LOCUS       WP_010682208             316 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682208
VERSION     WP_010682208.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 316)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..316
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33703
     Region          8..298
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mirrrtllag fgaglvagpl sgaraqstpv tirmgslkli hsiapsfyer ftpagvtvev
       61 vpfespteck navvtksvdf gtfgiaaatl gaaagepivv iastcnrgma viakkdsdir
      121 aikdlrgkrv aiwpgstqev fvlermrmeg lsvkditpvr vsfsemhial argdvdayvg
      181 aepgpgvsla sgvgqlveyp ygtemgalnm vfgahrdtla erpdlvrtml eihrkatdfa
      241 agdrnamiam avaklgqkrq alelsapnve ltwrlgpdev rqagayaqhm lalkqikrlp
      301 eagfidtrfv damgra
//
LOCUS       WP_010682339             728 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682339
VERSION     WP_010682339.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..728
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=77346
     Region          74..688
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 makgrgriep nfdvpegrtr drgeldlrls redrpgsgdr vakrsggaaq rpakaparna
       61 grsksagrgr rrrswlgrlv yatvvlglwg viglagliay hasqlppidq lavpkrppni
      121 ailasdgsll anrgetggrv vsirelppyl prafvaiedr rfyqhfgvdp vgilraigqn
      181 ltrrgvaqgg stltqqlakn lfltpersas rkiqeailal wlehkytkde ilelylnrvy
      241 fgagaygvea aaqryfgkpa kevslaqaam lgglvqapsr lapnrnlpaa qaraaqvlaa
      301 mqdlgfvpaq dvkvalaqpa kpanargggs anyvadlvmd vlddyvgkfd tditvqttvd
      361 tglqaaaera lteelnakga rfnvaqgavv smrpdgaira liggrdyaqs qfnrattakr
      421 qpgssfkpfv ylaavehgat pdtvredapi rignwapeny shryegavtl rtalaqslnt
      481 vavrlgqevg pkavvqtaqr lgitsplqan gsialgtsev tllemvgayg afanggtgvi
      541 pyvvtavkga dgkvlykrad sglgrvmsad adgmmnammh etfvsgtgkk adipgwdlag
      601 ksgttqdyrd awfigfsgsl vtgvwlgndd geltkkvsgg nlpaeiwkty mtqalkgqnp
      661 vplpglnrwr rapettasva sagpgappgi lgqifgepea paprpaapar raqkddrnfi
      721 eklfgige
//
LOCUS       WP_010682346             276 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Methylobacterium mesophilicum].
ACCESSION   WP_010682346
VERSION     WP_010682346.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..276
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28799
     Region          50..246
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mrlliglgla iglvygaala vlalnqhrfl ypgafrtpvn latpegvaai tvvtedrerl
       61 halwrppapg cavvvsfhgn gsypephadr faagpwragg wgvlapayrg ypgstgmpse
      121 dglirdglaa vaaaaerapg spillhghsl gaavaiavae rvpaiglyle apfdsmthvv
      181 rlhvplvpsw flrdtyrsdr riragaapvl iiqgrddgiv paklalalsr aagprarfev
      241 ipgdhvsilg vrdhdaealf rggldaactg aeaavr
//
LOCUS       WP_010682358             382 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Methylobacterium mesophilicum].
ACCESSION   WP_010682358
VERSION     WP_010682358.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..382
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40058
     Region          40..373
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mlvernsgap pgriigqddr dsrvpgrdre daratvveaa iriglaaalv yacgriifpl
       61 hevliwsail svmlyplhar llsrigdrws alligfvggt iitvptiavv tsagstiytf
      121 lsdvqnqtla lppppnwvar aplvgprlae awalaaanap lalarygsml krpvawllsa
      181 vrglatseis fvlsfaiaav viaygesaak fsrtflsrtt gneargsqla alivatirsv
      241 algivgvavi qalllgagff aiglpaagll tlatfflciv qvpallltlp iiayvfatea
      301 trpaviflaw tigaglsdni lkpfllgrgm qvpmpviltg viggliahgl lglfvgpvll
      361 atgyvllvew irrdeinagm pp
//
LOCUS       WP_010682411             711 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682411
VERSION     WP_010682411.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 711)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 711)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 711)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10833107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..711
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71952
     Region          17..78
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(22..24,27)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          111..707
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Site            order(408..412,559..560,586,604..605,608..609)
                     /site_type="active"
                     /db_xref="CDD:319763"
ORIGIN      
        1 msdattlert eipatrlrvs gmdcascaak vetavrrlpg iervevsvat etltvmhgpa
       61 tsvgtivatv rglgygaedp daaatgadap dkpwwqapka llafacgaav asayvlglav
      121 pvterwffla amlvglvpva rralsaarhg tpfsiemlmt vaavgatlig ateeaatvmf
      181 lflvgevleg vaagrarasi rgltglvpdt allerdgate rvtaaslrig gtvlvrpgdr
      241 ipadgtvidg estvdeatvt gesvprpkav gdavfagtvn gdgairvrvt aaardntiar
      301 vvrlveeaqe akapterlid rfakaytpav vavaalvala pplvagaaws ewvykglail
      361 ligcpcalvi stpaaiaaal sagarrgllv kggavlerla avtkvafdkt gtltegkpvv
      421 tdvvafgrtg rdvlslagal eggsshplak avlakaaevg apvppasgtr alggkgvegk
      481 vgrldlflgs preaaarctf tpeqearvsa lqgegktlsv llsngavagl lamrdeprad
      541 akegvdrlas agigavmltg dnartarava galgiearae llpedkqriv relragglvv
      601 akvgdginda palaaadvgi amggaadaal eaadaavlhg rvadvarmve larrtlanir
      661 aniaialglk avflvttvlg vtglwpaila dtgatvlvta nalrllnpsl d
//
LOCUS       WP_010682429              70 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [Methylobacterium].
ACCESSION   WP_010682429
VERSION     WP_010682429.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 70)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 70)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..70
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6942
     Region          1..66
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 myrfkvskmg cggcaksvtr avlgiepdaq vevdlgaklv tvsgsggpad riaravtaag
       61 ypaepvhala
//
LOCUS       WP_010682418            1082 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Methylobacterium].
ACCESSION   WP_010682418
VERSION     WP_010682418.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..1082
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=115775
     Region          1..1065
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miskildfsv hqrwlvllls llaaafggya vtrlpidavp ditnnqvqin ttapslspvd
       61 iekqvtypve talagikgle ytrslsrngf sqvtavfaek ldiyfarqqv aerlsqvkre
      121 lppgaepamg pistglgeiy mwsihyakpg erkvsaggkp gwqpdgsylt pegqrlrtel
      181 eqtaylrtvq dwiirpqirt vpgvagvdgi ggfekqyhvq pdpnklasld lsfsdvaral
      241 dsnnanqgar yledngegyv vraagrledm ddignvvvat rggvpvrikd iaevrigrdl
      301 rtgsgsedgq evvvgtalml igensrtvaa avdarmdqir kslppgievq tvldrtrlve
      361 atvktvaknl segaalvivi lfmllgnira avitalvipv amlmtmsgmv earisanlms
      421 lgaldfgliv dgaviitena lrhlaerqha lgrgldieer letvrasaee mikpslygqa
      481 iiilvyvpll tftgvegkmf epmaltviia lvsafvlslt fvpaliaivi sgkvtetdnl
      541 iiralkavyr pvlaaavrgp fafigaalll lvgasllftr lgtefipqld eksialnatr
      601 ipstsltqsq tmqlnvekvv skfpqvayvf sktgtaevas dpmppnssdt fvmlrpqeew
      661 pdpslskadl qeqiekavga lagnvyefsq piqlrfnell agtrgdlavk vfgeefepml
      721 kaanavatvl kgvegaedvk veqaaglpfl eikinkpeaa ryglstgaiq evigaaiggr
      781 dagvvfegdr rfpivvrltd kvredreale nipvplppgp ngrassvllk qvasfqvteg
      841 pnqisrengk rrvvvtanvr grdigslvae aqakvgsqvq lppgyyvtwg gqfenlasak
      901 qrllvvvpvc ffliflllys algsprdall vfsavplalt ggivalwlrg mpvsvpaavg
      961 fialsgvavl nglvmltfik qlvaegrpkr eailegamtr lrpvamtalv aslgfvpmai
     1021 atetgaeiqr platvviggl isatlltlvv lpalyarfgk aepakvngrq peaasphlka
     1081 ae
//
LOCUS       WP_010680772             365 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA polymerase III subunit beta [Fusobacterium gonidiaformans].
ACCESSION   WP_010680772
VERSION     WP_010680772.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Fernandez-Leiro,R., Conrad,J., Yang,J.C., Freund,S.M., Scheres,S.H.
            and Lamers,M.H.
  TITLE     Self-correcting mismatches during high-fidelity DNA replication
  JOURNAL   Nat Struct Mol Biol 24 (2), 140-143 (2017)
   PUBMED   28067916
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Paschall,C.O., Thompson,J.A., Marzahn,M.R., Chiraniya,A.,
            Hayner,J.N., O'Donnell,M., Robbins,A.H., McKenna,R. and Bloom,L.B.
  TITLE     The Escherichia coli clamp loader can actively pry open the
            beta-sliding clamp
  JOURNAL   J Biol Chem 286 (49), 42704-42714 (2011)
   PUBMED   21971175
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Georgescu,R.E., Kim,S.S., Yurieva,O., Kuriyan,J., Kong,X.P. and
            O'Donnell,M.
  TITLE     Structure of a sliding clamp on DNA
  JOURNAL   Cell 132 (1), 43-54 (2008)
   PUBMED   18191219
REFERENCE   4  (residues 1 to 365)
  AUTHORS   O'Donnell,M., Jeruzalmi,D. and Kuriyan,J.
  TITLE     Clamp loader structure predicts the architecture of DNA polymerase
            III holoenzyme and RFC
  JOURNAL   Curr Biol 11 (22), R935-R946 (2001)
   PUBMED   11719243
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Herendeen,D.R. and Kelly,T.J.
  TITLE     DNA polymerase III: running rings around the fork
  JOURNAL   Cell 84 (1), 5-8 (1996)
   PUBMED   8548826
REFERENCE   6  (residues 1 to 365)
  AUTHORS   O'Donnell,M., Kuriyan,J., Kong,X.P., Stukenberg,P.T. and Onrust,R.
  TITLE     The sliding clamp of DNA polymerase III holoenzyme encircles DNA
  JOURNAL   Mol Biol Cell 3 (9), 953-957 (1992)
   PUBMED   1358275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..365
                     /product="DNA polymerase III subunit beta"
                     /EC_number="2.7.7.7"
                     /GO_component="GO:0009360 - DNA polymerase III complex
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=41497
     Region          1..362
                     /region_name="DnaN"
                     /note="DNA polymerase III sliding clamp (beta) subunit,
                     PCNA homolog [Replication, recombination and repair];
                     COG0592"
                     /db_xref="CDD:440357"
ORIGIN      
        1 mkfkikreef isvlsdytsi lkensikpil salfmevken elvfmgssie mdyrkqiqce
       61 gmeegavafk palvleyikl leeewltvek ldgflkiang efaileeeny pkivelasms
      121 llqiqgnefa kyletvkfsa sqtpenlaln cirvvfgkek infvstdsyr llylekkiga
      181 qferaislpl eavnviikll kektevisle lsgenllllw egtyfscrlt avpypnfqgi
      241 lnqnffdkkm efcledlkaa mkrvitvakt sidakyggtf dfkgkqlvvk avttgraktq
      301 qkvammkegd dfiaslncky lsefldtisk nviiygknss smfrvmeegn eeliyilmpl
      361 alrev
//
LOCUS       WP_010680935             422 aa            linear   BCT 01-JAN-2025
DEFINITION  serpin family protein [Acetivibrio cellulolyticus].
ACCESSION   WP_010680935
VERSION     WP_010680935.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Huntington,J.A.
  TITLE     Serpin structure, function and dysfunction
  JOURNAL   J Thromb Haemost 9 Suppl 1, 26-34 (2011)
   PUBMED   21781239
REFERENCE   2  (residues 1 to 422)
  AUTHORS   van Gent,D., Sharp,P., Morgan,K. and Kalsheker,N.
  TITLE     Serpins: structure, function and molecular evolution
  JOURNAL   Int J Biochem Cell Biol 35 (11), 1536-1547 (2003)
   PUBMED   12824063
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Gettins,P.G.
  TITLE     Serpin structure, mechanism, and function
  JOURNAL   Chem Rev 102 (12), 4751-4804 (2002)
   PUBMED   12475206
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Silverman,G.A., Bird,P.I., Carrell,R.W., Church,F.C.,
            Coughlin,P.B., Gettins,P.G., Irving,J.A., Lomas,D.A., Luke,C.J.,
            Moyer,R.W., Pemberton,P.A., Remold-O'Donnell,E., Salvesen,G.S.,
            Travis,J. and Whisstock,J.C.
  TITLE     The serpins are an expanding superfamily of structurally similar
            but functionally diverse proteins. Evolution, mechanism of
            inhibition, novel functions, and a revised nomenclature
  JOURNAL   J Biol Chem 276 (36), 33293-33296 (2001)
   PUBMED   11435447
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Irving,J.A., Pike,R.N., Lesk,A.M. and Whisstock,J.C.
  TITLE     Phylogeny of the serpin superfamily: implications of patterns of
            amino acid conservation for structure and function
  JOURNAL   Genome Res 10 (12), 1845-1864 (2000)
   PUBMED   11116082
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Carrell,R.W., Pemberton,P.A. and Boswell,D.R.
  TITLE     The serpins: evolution and adaptation in a family of protease
            inhibitors
  JOURNAL   Cold Spring Harb Symp Quant Biol 52, 527-535 (1987)
   PUBMED   3502621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14444449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..422
                     /product="serpin family protein"
                     /GO_function="GO:0004867 - serine-type endopeptidase
                     inhibitor activity [Evidence IEA]"
                     /calculated_mol_wt=46802
     Region          56..420
                     /region_name="serpin_tengpin-like"
                     /note="serpin tengpin and similar proteins; cd19589"
                     /db_xref="CDD:381055"
     Site            order(372..386,391..400)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381055"
ORIGIN      
        1 mkflnrpkry lnsllifvlp ialianltgc svsvkaddlm sgispnkvsg katddkfitn
       61 vsqfsielfk ksisdkensl isplsvlial smtangaage tlsqmekalg mdipikdlne
      121 ylytyvnnlp sednsklnia nsiwfrdnkg sftvnkdflq knsdyynaai yksafdsqtv
      181 kdinnwtkks tdnmidkvid ridgdtvmfl inavafdakw envytkenil kdnftsidgk
      241 vqnidfmcss epkyigddka sgfikpyind kysfvallpn eninindyia tltgksfqnt
      301 iksaqdifvs aylpkfsyny siklndalkn lgiqkafspe qatlgklgks segnifigdv
      361 fhktfisvde lgtkagavtk veikcesvgm vektiklnrp fvyaiidntt nlpvfigtvm
      421 sl
//
LOCUS       WP_010682456             175 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: arsenate reductase ArsC [Methylobacterium].
ACCESSION   WP_010682456
VERSION     WP_010682456.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..175
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=18578
     Region          7..143
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(12,14..19,112,114)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mpeptynvlf lctgnsarsi laeamlnkdg ggrfraysag sqpkgephpl alqvlresdy
       61 pteglrsksw defaapgapv ldfvftvcdn aageacpywp gqpvtahcgi edpavaegse
      121 merkrafvta qrylrnriaa fvalplgsld pvalsskvre igqlagatsa rpeva
//
LOCUS       WP_010682472             169 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Methylobacterium].
ACCESSION   WP_010682472
VERSION     WP_010682472.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..169
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=18690
     Region          2..158
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mddiayliep qipalrryav allrdreaad dlvqdtlera lsawsgcrrd gdfrawlfti
       61 ernlflgavr rrgrrgvdvg aesleqvpdp gidpeaamga rdvlagldtl peeqrsvlll
      121 vavedlsyae aaqvlgvplg tvmsrlsrar trmrsfletg rtsvlrrvk
//
LOCUS       WP_010682475             116 aa            linear   BCT 01-JAN-2025
DEFINITION  YidH family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010682475
VERSION     WP_010682475.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..116
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=12421
     Region          2..115
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 mppnaprvrl aedrtvlaae rtfvawlrtg laflgiglaa qrflrevlav wplkvlsltl
       61 iacaltsfag avwrdraira rlahseipmm prlltigiaa lliaiaglaa tallwa
//
LOCUS       WP_010682516             353 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682516
VERSION     WP_010682516.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..353
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38422
     Region          36..>123
                     /region_name="CE4_SF"
                     /note="Catalytic NodB homology domain of the carbohydrate
                     esterase 4 superfamily; cl15692"
                     /db_xref="CDD:472828"
     Region          96..324
                     /region_name="CE4_Mlr8448_like_5s"
                     /note="Putative catalytic NodB homology domain of
                     Mesorhizobium loti Mlr8448 protein and its bacterial
                     homologs; cd10968"
                     /db_xref="CDD:213025"
     Site            order(103..104,235,239,275..277)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213025"
ORIGIN      
        1 mlssrtkhri fasgfraiqa vgadrwlapa arglgviltf hhvspdpvpa fapnrllsit
       61 pdfldltlre ldargfevig ldevprrlaa pdygppfaal tfddgyrdnv vharpvlarh
      121 gvpwtlfvts afadqrgrlw wleleraivr ldrvritigs rsldlparsp qekaiafdvi
      181 yrdlrggdee lllariadlc rqagftpgal aadlclswde mralardpav tfgahtvshp
      241 mlakheaava areiaegrdr ieaelgrpvr hlsypvgdpg sagprefala samgfdtavt
      301 trpghlfadh aghlhalprv svngchqsra alagllsgvp flawnrgrrl nva
//
LOCUS       WP_010682542             151 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator [Methylobacterium mesophilicum].
ACCESSION   WP_010682542
VERSION     WP_010682542.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..151
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=15826
     Region          7..131
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 msdsvqpgqk pvilvvedqp derflaatll edtgftviea etadralail ndradevsvv
       61 fsdvrtpgpi ggfelariig vtwprvrvll tsgdagdqps dlrvsatfip kpwraedila
      121 wveqaagrps gaagpsvigp ggkiitpgle t
//
LOCUS       WP_010682632             613 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682632
VERSION     WP_010682632.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 613)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..613
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65761
     Region          1..558
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msallsirdl avafrtetgp fealhglsld vprgrtlalv gesgsgksvt aqailrilpp
       61 saaitrgqil fadgqaetdi arlpaegpam rairglriam ifqepmtcls plhtigdqig
      121 ealrihtgad rkeadartqe alarvgfpdp hralrtypfe lsgglrqram iamalilkpa
      181 llvadeptta ldvttqaqil allarlqaet gmaillithd lgvvaniahd vavlyrgrlv
      241 esgprdtvmr apghaylral lhavprfdma pgerltpirp araeippara laplagpllq
      301 vegvsktftl ragrlwqkpr lvhavsdvsl slkagqtlgl vgesgsgktt vskmimrale
      361 pdsgrilfdd gsgpqdvhal sgdalfafrr tvqfvfqdpy asldprmtvr qilsepmeih
      421 gvpaaerrer cralmamvgl epaglaryph afsggqrqri giaralaakp rllvldepvs
      481 aldvsvqaqi lnllkdlqaa lglsylivsh nlavidymad tisvmcrgri veeapraalf
      541 rrpvhpytra llaavpdpsl dhpldfaavt gdqndptrwa ppyrlgpdea gtmraiesgh
      601 rvrlggaqaa eaa
//
LOCUS       WP_010682676             228 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682676
VERSION     WP_010682676.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..228
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25413
     Region          16..220
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 marlgtipff kdpgielstf eprchwrrfd enevlvdfdd istdvyfias gevrilnrtq
       61 sgkevilgem rggaffgela aidgigrsan vtaltrgdvc vvpaavfrqm vfaseviadr
      121 lfrllakrvr elntrlmeha lldlkhrlya ellrlsvpra gasgervvsp ppyhhvlaar
      181 igcrreqvtr eftamaaegl vdrtrgalvl rrpdllearv aealreds
//
LOCUS       WP_010682703             415 aa            linear   BCT 01-JAN-2025
DEFINITION  NupC/NupG family nucleoside CNT transporter [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682703
VERSION     WP_010682703.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..415
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42320
     Region          22..415
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mldrlthagl slllllavaa lfstnrrais prvvltgial qvglgalvlf lpagqaalra
       61 aadgvvtvls ygdrgtaflf gglvepkmfe lfggsgfila lrvlpqilyv saligvlyhl
      121 gvmqtlargl gavlrrilgt spiesfsavi tiaigqseia valrpflavl tgaelfavms
      181 sgaastagsi lagyaalgvp mtyllaasvm aipggllyak ilmpsteptr itttrvefge
      241 traaniieaa adgtqkglvv avsvgamlia fvglialadg lfgavgglvg ypgasfegvl
      301 gwglaplawl lgvpwehatl vgaaigqkla fneflayanl sptlkagtld prsqaivcfa
      361 lcgfanfasi aiqlaslasl vperrsevar yglrailagt lsnltsaaia glfva
//
LOCUS       WP_010682722             367 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682722
VERSION     WP_010682722.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..367
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39813
     Region          181..365
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mpslirdpva rlrddleagf qqdleeavfd aarwpdlier asrasgsega lllrsdrmgl
       61 daihtpsldd aaqryfgegw yredyrlrgl pfmrtrgiav dqdfttpeei arlpfyqdll
      121 asrglrwfag igfevkgrlw clslqrtvaq gpyepheqer latlspllrr aglltaivek
      181 arlagltqaf evieraalvl dsegralrwn eafgallgtd lklaggrlva edpeaarhle
      241 alarpygrpp fsavaverrd appmvlhvvp lvgpsrglfa ggctlllarv pgaatvpaaa
      301 llqvayrltp aearlaqals ggmslaeaas ryaitaatar sqlkaifakt gatrqsdlvr
      361 lvtglar
//
LOCUS       WP_010682725             208 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF2147 domain-containing protein [Methylobacterium mesophilicum].
ACCESSION   WP_010682725
VERSION     WP_010682725.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Barison,N., Cendron,L., Loconte,V., Proctor,E.A., Dokholyan,N.V.
            and Zanotti,G.
  TITLE     Protein HP1028 from the human pathogen Helicobacter pylori belongs
            to the lipocalin family
  JOURNAL   Acta Crystallogr D Biol Crystallogr 69 (Pt 8), 1387-1394 (2013)
   PUBMED   23897462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..208
                     /product="DUF2147 domain-containing protein"
                     /calculated_mol_wt=21684
     Region          30..152
                     /region_name="COG4731"
                     /note="Uncharacterized conserved protein, DUF2147 family
                     [Function unknown]"
                     /db_xref="CDD:443765"
ORIGIN      
        1 mrfssigrrv aplavlaaaa lagpahaatp tdpsgtylte dgrarvrlek cgtagdrlcg
       61 yvvwlkvpln ekgepridfk npdpkkqtrp slghqlimgl kpnadahyeg kiynsedgks
      121 ydvtiwtdkp geltvrgcli aflcksqtwn kvtdlapgql agptngpsgp hsdpefagpa
      181 aatagarpta kagakpapkp aaappaqe
//
LOCUS       WP_010682764             379 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Methylobacterium mesophilicum].
ACCESSION   WP_010682764
VERSION     WP_010682764.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..379
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41714
     Region          8..362
                     /region_name="BcsL"
                     /note="Acetyltransferase involved in cellulose
                     biosynthesis, CelD/BcsL family [Cell motility]; COG5653"
                     /db_xref="CDD:444374"
ORIGIN      
        1 mqdrmqerfe tirtaerlae vgpawsdlwa rsgalifqsh awisawwasa adrdrrtlai
       61 alawrgqdli gvmplatvrr kgfrvlewaa kdcsdfgdal lapeadrdlv rrmwrhagrt
      121 ggfdlaylnr llpeaaartl lepasggirl hlnhrdeanw rvrgpwktgq awfdaqskkt
      181 rqnyrrgqkf mgergllafr llgleeplgp vldrlttfkr awlathalas tafydegsqa
      241 lpamvrvlae tgllhafvle cggevvavsi nfvqagtmma fvttydpave rgspgmvlmm
      301 dyimwsidrg lhtvdflcgd egfkgrfgtq nltlasmmga rtplglaarv adsvghaarr
      361 rfggtapqsg gapaaevaa
//
LOCUS       WP_010682754             247 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682754
VERSION     WP_010682754.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..247
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25226
     Region          5..241
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 maepdaflgg llrlhqpprg ahragtdavl larllpvsag drvcdigagt gavglacaal
       61 arglqptlve rdpmlaelar anaalngida rvivadvlap aaerraagls pdaldvvltn
      121 ppffaagshr asphpgraaa htfaegsldl wiractgilr pggrlglihr adalpaalda
      181 lkgrygavai rpvhargdtp airvliaair gsraaprllp glvlhepdgg ftpeadalhr
      241 gapwpla
//
LOCUS       WP_010682820             356 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682820
VERSION     WP_010682820.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..356
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=36898
     Region          2..353
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mtplgaeiaa lirqtgpigv drymalclgh pvhgyyrtrd plgvrgdftt apeisqmfge
       61 ligawsgyvh glmgrpdplv lvelgpgrgt lmadalralr aaapgvrvap hlvetspvlr
      121 aaqeralagt gaiwhaevet lppgpsvvva neffdclpvr qferrptgwh erqvglgpag
      181 glafglspep tpgleaagpv galmsvptag lalirglsqr lcaaggalla idyghvrpgf
      241 gdtlqalsgh syadplaapg qadlthhvdf aalaqaarve gadvhgpveq rdflfalgll
      301 araerlqsra teaqapeigr atarltepgv rgmgslfkvl avsgpglgpl pgfpnt
//
LOCUS       WP_010682835             301 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682835
VERSION     WP_010682835.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..301
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32082
     Region          133..301
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mrhavyglpp vdlaevpgda vqlsplipga erledlsens ldsatvlapp gtverryvla
       61 qmlralgpgg rmvalapkdr ggtrlakelt tfgcaaadqp rrhhrictae rppslaglae
      121 aidegaprhv dnlalctqpg ifswdrldpg talllanlpt lkgrgadfgc glgilsravl
      181 rsdavatltl veidrravem arlnvadpra tihwadvrtp gvvpdhldfv vtnppfhegg
      241 sedpslgraf iaraaevlrp ggtlwlvana hlpyeaslre afrhvavavq aggfrvyear
      301 r
//
LOCUS       WP_010682872             353 aa            linear   BCT 01-JAN-2025
DEFINITION  lactonase family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010682872
VERSION     WP_010682872.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..353
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37079
     Region          10..353
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mpdtahaplg lafvgcftte rrrargrgid iyrvgggles wshlgrvegl tnpsflvtdp
       61 gravlytvqg dgaeasafaa dasgalralg gadtggtnsv hqaldpdgrf livanyasgs
      121 valmpvrayg glepashvlp lpgetgphrt eqacahphhv vlspdgrhal vpdkgldrvf
      181 vlrregeqla ivsetamrpg agprhiafhp srplaflvne ldsslatcrw dpasgtltpl
      241 hlaptlppdy fgastaaaiv itrdgrfvya snrgqdgiar frvdiagrld pagwtqaggr
      301 dprfmvlapd gehllvaneq gdslvefaid ptsgdltrtg srpslspcti afl
//
LOCUS       WP_010682965             133 aa            linear   BCT 01-JAN-2025
DEFINITION  tautomerase family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010682965
VERSION     WP_010682965.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..133
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=14015
     Region          2..60
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
     Region          68..122
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mpfinvkvag rtlaksqver lqagitsqms lilhkvgplv gvlveavpla gwsvgghpva
       61 caaqvdaiis aetntaeeka rfiaetnqll kdvlgtalae vsyvvihevp kdswgydgrt
      121 qadraqrrps tas
//
LOCUS       WP_010682930            1053 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682930
VERSION     WP_010682930.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..1053
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=109501
     Region          17..1043
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mteppgaagr ggpqaflvgf avrlprvvla lacavlafgl yvlagarydv fpefappivt
       61 iqteapglds eqvevlvtqp vevaigglpg letlrstsiq glsvinaafk pgsdvdrirq
      121 rvnerlaala grmpdgvatp amtpltsstl tvllvgltae ardamdlrhv aewtvrrrlq
      181 avpgiaqvsi yggavralqv qvrpddlirf qiglndvlta arkatgvrga gfvdtpnqrv
      241 llrsegqslt pealgrtvlh ndggasvvls dvatvtaape paisaalvdg kpgvllmvga
      301 qvgvdtravt arleaalael rpvldregit lradlfrpas fvdvatgnvi qalafggvlv
      361 vivllvflad wraalisaaa iplsliaaal alqawgesln tmtlgglala igevvddavi
      421 gvenvarrlr aargerparv vlaamlevrt svayatlavl lmflpvlslt gvagrlfgpl
      481 alayiaavva sllvaltvtp alallllggr margeaappr eppvvrwsra aylrllagis
      541 rvprlamlgs llvtlagaai lptlgavflp dlreghmilh mvavpgtslq esqrlsallt
      601 gdlkgitgvr avaaqigrae agedtagphy seihidlqpg ldgaaqrsve sairdliagf
      661 pgaafslktf lterieetvs gftalvvvnv vgsdldriea aarsvarela evkgardvqq
      721 aspaglpqvt valrpvdlrh wgldpvevle avrtayqgdv vgqayrgnav fnvlvildag
      781 vrsrlsavgd lplrapggry vrlsqiadvy esagryqvqh lgaqrvqavt anvagrdmag
      841 fvaaakrkia kevrlpegvy vtfsgaaeaq eaarrdllih aglagfgivv llaivtgsaa
      901 nlmlvlvnlp fafvggvaaa altggvlslg sivgfvtlag islrnsvmmi ahyeqmvird
      961 glpwnaataa egaadrmvpi lmtslvtglg llplalgage pgreiegpma liilgglvts
     1021 tvlnllilpv lalrfarfrs eepgdraftp arp
//
LOCUS       WP_010682997             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Methylobacterium].
ACCESSION   WP_010682997
VERSION     WP_010682997.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..290
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30127
     Region          1..290
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 meillqlias gvavgmiyaa iafgyqltfa tsktlnfgqg ealalgalfg ltlvpfvgyw
       61 lmiplvlvfg falgavverl gvrpavkiks eygwimatia lgiifknvae niwgrddlkf
      121 psplpetalq vggvrilpme llivagallm mlaveifnrk siwgkavvat sndidaaglm
      181 gintqkvitl sysisamtaa fagvlvapvt ltgatmgsvl alkafavaii gglesglgvi
      241 vgglilgvae tltgfyistg ykdvpglill lvvlsirpvg lfgkavikkv
//
LOCUS       WP_010683019             129 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Methylobacterium mesophilicum].
ACCESSION   WP_010683019
VERSION     WP_010683019.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..129
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13862
     Region          20..119
                     /region_name="cupin_HNL-like"
                     /note="Granulicella tundricola hydroxynitrile lyase
                     (GtHNL) and related proteins, cupin domain; cd02233"
                     /db_xref="CDD:380361"
     Site            order(29..30,59,61,82,84,86..87,106,108,110)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380361"
ORIGIN      
        1 mqifhgrets aksesrgptf tgqvwadpvm qstggvminn vfftpgartf whahaqgqil
       61 qvtagkgwic vagqkaqpir agdtvwipad erhwhgaaad syllhtaisl gktdwqdevi
      121 eadyagata
//
LOCUS       WP_010683008             234 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Methylobacterium
            mesophilicum].
ACCESSION   WP_010683008
VERSION     WP_010683008.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..234
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25840
     Region          13..233
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 makeararpn legvasadrv ltvltafrrg ddalelsela rrtalvksti mrlcislekf
       61 nlierlddgr yrlgveaari gsvyqqsfal eerivpvler laaesletas fyirrgnqrl
      121 clfradspsp lrmnvrpgdm rpmdesaiar vlrtfsdrra sdraamevpl yssgitdphv
      181 asvampvfgt eqrligalal sgpssrltie qaeilkprlr eaaerlssel gaql
//
LOCUS       WP_010683024             290 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Methylobacterium mesophilicum].
ACCESSION   WP_010683024
VERSION     WP_010683024.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..290
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29708
     Region          5..286
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 meqrtigvvg lgmmgdpmsr clakaghalr lldadagrtd alardlgata ltrenaagld
       61 llitmlpnsa iveavlldeg wadalpagat vidmsssepv rsralgetla gkglgyldap
      121 vsggvrravd gtlailvgge adllarwrpv leamgssvlh igpagsghaa kalnnfvsaa
      181 gllatvealh vaqrfgiape amtdvlnass grsntsenkv kqfmlsgsfa sgfslklmdk
      241 dlgiagalaq svdyplgfgr hcietwhaia ggvgptadht emyrllaeva
//
LOCUS       WP_010683059             335 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010683059
VERSION     WP_010683059.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..335
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35866
     Region          6..331
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msavrrigli gagwvaqhhl agwatlrgra vvvaiadpsa errmdraqaf dipntyadag
       61 amldagglda idvaapravh aelvrlaaer glpilcqkpl aptlaearal vaavegrarl
      121 mvhenwrfra yyreaaawlr agcigqpfaa rlelvtsgtl pdeaglfpal erqpfmrdea
      181 rmlvaevlih hldtlrlllg plrvvacats rtcsdlaged taliqlagpd gvavqvfatf
      241 aahgappasl drleilgrdg airlqgaels mtgreprtrt fdlaaaytds yaaaiahfid
      301 rlddgapfet apadnletlr lvedcyrlag raear
//
LOCUS       WP_010683098             146 aa            linear   BCT 01-JAN-2025
DEFINITION  CsbD family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010683098
VERSION     WP_010683098.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..146
                     /product="CsbD family protein"
                     /calculated_mol_wt=15569
     Region          3..66
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mvdtdritga arelggkvqg avgdltgskr dslegrarea agqaenlygr akdtvrdtgd
       61 rirdaagdvi gsgdiedryv raersvrraa deaydyaeda yergghylrr gtrevshqva
      121 eyplasllia glagfglgll vsakrd
//
LOCUS       WP_010683153             356 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Methylobacterium
            mesophilicum].
ACCESSION   WP_010683153
VERSION     WP_010683153.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..356
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39698
     Region          61..329
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mttrhkiagv krfwsakagk tyyyhrasga rihsepgtaa fvsevdrlnq awkakavakn
       61 tlghliaeyr ktpeylrlkp itkadyervl imfekaggmp lsaitraqvf twrnqafakh
      121 krrfanyvvq vlsrmlgvgv nlglletnpa lrvekirkat gekhrnrpwt sdereavlsa
      181 apiqlkapla fmrylgarlg dvrtmpaaay qdgmitfrtg kgdvevcvpc paplaaildq
      241 rlpsrthlfv tsegtpwtdg gwnaswrklr trledagkvr pgltahglrh svatdlrelg
      301 ktdreiadil gqrttyatpv yhrtadmkrs narvmgelhg ddrsdeksns vanlps
//
LOCUS       WP_010683312             294 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Methylobacterium mesophilicum].
ACCESSION   WP_010683312
VERSION     WP_010683312.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..294
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31920
     Region          12..293
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mdkiigsehr askddvslfl wrkrgqdglg sgwppvvlvh gssmsalptf dlsvpnhpdy
       61 smmdwlarrg hdvwtldheg ygrstitggn sdvacgvadl eaatdlirdv tgtrsvsiyg
      121 lssgalraag faqafpdrve rlvldafvwt gkgaptlakr regvatfraq nrrpidlafi
      181 egiflrdkpg ttapevarac aeaqmslgns vptgtyldmt trlplanper ilaptlivrg
      241 ehdgiatldd ivaffqrlpt gdkriavlpd vahctplgim rhrmwtamae fiei
//
LOCUS       WP_010683330             588 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010683330
VERSION     WP_010683330.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..588
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=64713
     Region          1..578
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mskpiesyal igdgetaalv grdgsidwlc wpdfdddacl callgtnrng rwsiaprgav
       61 ldtarryrgd tmiletvmkt tdgavritdf mpiretlsav vriveglagt valdidlspr
      121 fdygalapww eareggaasv agrhrltlra svpvsvdvrg vkaafrlreg erhtfvltrt
      181 dawdsdaphl dvdaalgatq ahwerwisgf dptrtrwaaa vkrslltlka ltharsggll
      241 aapttslpev paggmnwdyr yswlrdstft lgaflnagfk aeatawrdwl lraiaddpdn
      301 lrimyradgs rhlpewtvda lpgyrearpv rvgnaastqk qldvygevld tlalarrvgi
      361 aatdhqcvve rrlaehlaqv wqdrdagiwe srgepkryty skamcwvgfd rvlrhcdlpg
      421 elratlaecr dkvraevcre gwnvglgtft qsygshdlda sllllplvgf leateprmaa
      481 tierirgdld qnglirrmra kgdgedegaf lpcslwmadc lrlqgrpela edylervlgv
      541 andvgllsee ydvpgrcltg nfpqalthlg vvntalslcg pvvdrggg
//
LOCUS       WP_010683439             449 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Methylobacterium mesophilicum].
ACCESSION   WP_010683439
VERSION     WP_010683439.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..449
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46525
     Region          17..443
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mtdgtrdpat ppsrraglle rtfrlaehgt svrtevlagl ttfltmayiv fvnpsilaea
       61 gmprgavfva tclvaalgsl imglyanypi alapgmglna yftyvivqgl gftwqaalga
      121 vfisglcfla vtltglrali vdgiprsmri aitvgiglfl aiialknagv vaaspatfvt
      181 lgdlhkpetv lavigfliva vlsarkvraa lltsiltvta lsfvfagntf qgvvalppsl
      241 aptflaldvs galsaglmnv ilvlflvelf datgtlmgva sraglltddr lprlnralma
      301 dsaavfagsl lgtssttayl esasgveqgg rtgltaatva alfvaclffa plaaavpaya
      361 tapalfyvac lmlrelvald wddlteaipa cvtallmpft ysiatgvslg fiiyavlkll
      421 tgrarevkpv vwviavvfly klvetggah
//
LOCUS       WP_010683590             113 aa            linear   BCT 01-JAN-2025
DEFINITION  circadian clock KaiB family protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010683590
VERSION     WP_010683590.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..113
                     /product="circadian clock KaiB family protein"
                     /GO_process="GO:0048511 - rhythmic process [Evidence IEA]"
                     /calculated_mol_wt=12353
     Region          21..92
                     /region_name="KaiB_like"
                     /note="KaiB-like family; composed of the circadian clock
                     proteins, KaiB and the N-terminal KaiB-like sensory domain
                     of SasA. KaiB is an essential protein in maintaining
                     circadian rhythm. It was originally discovered from the
                     cyanobacterium Synechococcus as part...; cd02978"
                     /db_xref="CDD:239276"
     Site            order(22,41,44..45,69,72,74,78,81..82,85..86)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:239276"
     Site            order(62,65..68,71..73,75,78)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239276"
ORIGIN      
        1 mnattpdepa qetdpdgdpg hyhlrlyvag qtnkslaamt nlkrfceehl agrydievid
       61 lmknpqlaag dqilaiptlv rrlpsplkri igdlsntekv lvgldirpka dqp
//
LOCUS       WP_010683604             260 aa            linear   BCT 01-JAN-2025
DEFINITION  YdcF family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010683604
VERSION     WP_010683604.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..260
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28728
     Region          38..228
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mlrasdplst divgwawhew grpgrtlsgr apqprgrial wtcgagacfg alaliagfli
       61 fvgalarher tpldradgiv altggaqrig daidllaggy grrllitgvn ertsrdeiar
      121 lnptqralia ccvdldyrar ntignaietr rwmrahrfst vavvtsnyhm prtlveldha
      181 lqdsdrvlph pvvteafdad rwwqspiaak lvaseyvkfl aswvrtrfea dpersraail
      241 igrrkpvkmv aeplmmrgvd
//
LOCUS       WP_010683661             824 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Methylobacterium
            mesophilicum].
ACCESSION   WP_010683661
VERSION     WP_010683661.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457611
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..824
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83317
     Region          6..>47
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          72..141
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          161..806
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(453,455,761)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(497..499,562,578..580,610,650..652,672,675,678,697,
                     700)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(762,790,794)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mpdpvtltlp vegmscascv grveralrsl pgvrdvavnl athraslvlg gaarpadaaa
       61 alaevgypvp etetllaieg mscascvgrv ervlaavpgv tgasvnlaar ratirhpegv
      121 vstddlvaav aaagyearsl eaadpadpaa rqdqegralr rdliaaalls tpvvvldmgg
      181 hvlgrlhggs atavvqavla tlvlagpgrr fflrgvpgll rghpdmnalv algagaayly
      241 slvstlapal lpadaahlyf easvlivtli llgrtleara rgrtgqaiar lmdlapktar
      301 vlrgdaeaqv plaglrigdl vrvrpgerva adgvvvsgtg hvdesmvtge pvpvhkgpgd
      361 rmvggtlngr gsldlrvdav gsatvlaqia amveraqggk lpiqalvdrv tgrfvpvvig
      421 iagvtflawl vlapapalgt alvnavavli iacpcamgla tptaimvgtg raagrgvlfr
      481 dgaalqrlrd vrvvaldktg tltegrprvt divtargvpe edalalaagl esrsehplag
      541 avvaaardrg lrapeadgfe alegfgvtgw vagravalga pryldrlgia adpdlaarae
      601 rlagegrtpi hlaldgrhaa vlaladpvka gareavaslk arglavamvt gddprtaasv
      661 arslgiddva agvlpggkve avqrfraahg pvafvgdgin dapalaeadv glaigtgtdi
      721 avdsadvvlm sgsldslvea lalsravman irqnlfwafa ynaalipvaa gvlvpfggpt
      781 lspilaagam afssvfvlgn alrlrraggg spppkaaalk prpa
//
LOCUS       WP_010683686             381 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Methylobacterium mesophilicum].
ACCESSION   WP_010683686
VERSION     WP_010683686.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..381
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40589
     Region          54..375
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mqpmikpgtp pvpvetplpq nqgpsqelpp herarsqgaa rvllvlalsa lglwilhefl
       61 palawavvla ialwplytrl errfppgkhn illptlmtva valvflapla vlgiqaarea
      121 hdvaefvrna eangipapdf lqhlpygapq atawwndnlg haqagsdllr rfennsviga
      181 srnvgreivh rivlfgfslv alfflfrdwr tvrdqsltac hrlfgprger varqmvasvh
      241 gtvdglvlvg lgegfvlgiv yyfagvphpv llgaftavaa mipfgaavai aiaalllvaa
      301 gsakaalvva aaglvvtfva dhfirpalig gttklpflwv llgilggvet fgllglfvgp
      361 avmaalvllw refteghdqt a
//
LOCUS       WP_010683737             433 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpP1/FadL family transporter [Methylobacterium mesophilicum].
ACCESSION   WP_010683737
VERSION     WP_010683737.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..433
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45468
     Region          6..418
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mraamlaata vilcagqaha gafgireqst qaqglsyaga asgsggvssi fwnpatitmn
       61 pgfvseqnlt figlsseirp apgtnpafag lggsgdigqg avvpagatsy qlsdrlwlgl
      121 stgapfglvt kprdvwagev ygrssrifsl afnpvigfkv newlalaagp nieyfrltlr
      181 qalpipgisp vvypsgflkg eswgvgftag atitprdgtv lgigyrssvh hdidgsigvp
      241 llalaplagq vraklntpdk lsvgltqait pvarvnlgfe wdnwsrlgtv givsktlglp
      301 vnnlplnykd gytyaigaey dasanltlrt gfayetspid fsnrsvrlpd gdryiasvga
      361 syrwnqqltl nlayshffld rsrilagigr dynvgniafa gvvdssadvv svgfryvfga
      421 pqapapapii rky
//
LOCUS       WP_010683754             460 aa            linear   BCT 01-JAN-2025
DEFINITION  2-hydroxycarboxylate transporter family protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010683754
VERSION     WP_010683754.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..460
                     /product="2-hydroxycarboxylate transporter family protein"
                     /calculated_mol_wt=48035
     Region          31..458
                     /region_name="CitS"
                     /note="Na+/citrate or Na+/malate symporter [Energy
                     production and conversion]; COG3493"
                     /db_xref="CDD:442716"
ORIGIN      
        1 mtstattrsa pppaesraae agaarfwpdr wwrlvdakig iiplpvylil ailigvlvqe
       61 geikpdgptm iavlvmggft caeigkripv lknigagaif atfipsalvy yalvppqmvk
      121 aitdftkftn flyiyiatii vgsilgmdrd vlikgflkif aplavgsvaa alvgtlvgtl
      181 lglgpyktff fivvpimagg vgegaiplsi gyaailgmqq gvvfaqvlpp vmlgsltaii
      241 lsgtlnyvgk qyphltgegr lqpdsegiks sdaqakseaa rgqidpatig aagltaitly
      301 llgvmahhmv glpapvamlf lavfaklasa vsphlqaggf vvykfvqvsm typllfaigv
      361 altpwnelma aftlvnliti vstvvtlmvt gffvgrwlgm ypietaivna chsgqggtgd
      421 vailtaanrm almpfaqiat riggaltvtg tiiamkwiga
//
LOCUS       WP_010683763             557 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010683763
VERSION     WP_010683763.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..557
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58201
     Region          2..550
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mavfntiksr lvillallgt lllasdligq walsrsnrsl qavysdrvvp lgqflairda
       61 ydtivdasrt vreaaadpad atrqieagla sikqqwatyl tshltpeekg laaameaqig
      121 rnavivadil erlrtrnldg yaaahlalnh mmaptaaalv qlrslqlret qieyeqaqas
      181 aslarlvlii llaaacvail fglhavlarv trpldratvl mgrlasgdls vtvtgverrd
      241 eigamiravq vfkeamiakr aadeaaaven aakmhraarl davtlrfeat isamtrslad
      301 aasemettae amagiagaat qqaatvagaa vqtsgnvqtv asateemats vqeiveqvtr
      361 saeiadrave ramrtgitvr hlattaeria afvdviagia rqtnllalna tieaaragqh
      421 gkgfavvade vkalaeqaer atgeigarig eiqaatdeav gdiegigrii gemssyatav
      481 aaamdeqgaa treitrnvqe aargteqvtr siagvsdgas ragaaaaqvl qaaqglsrqa
      541 atltqevsvf lgdikaa
//
LOCUS       WP_010683783             257 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010683783
VERSION     WP_010683783.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26359
     Region          2..254
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mllqvqdlaf gygaravgtd vsfdldagev lcllgpnggg kttlfktllg llparggrir
       61 ldgtdlsrls rravartaaa vpqahaayfp ftvrevvvmg rasrigpfsa pgpadeaaae
      121 aalvtlgirh laekiyteis ggerqlalia ralsgaprll imdeptasld fgnqarvlgq
      181 vrrlaragia vmfsthdpgh alacadrvla lhggglvacg ppaatvtpal lrliygidvv
      241 vaplpgipap vcapvia
//
LOCUS       WP_010683789             383 aa            linear   BCT 01-JAN-2025
DEFINITION  AAA family ATPase [Methylobacterium mesophilicum].
ACCESSION   WP_010683789
VERSION     WP_010683789.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 383)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 383)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..383
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41243
     Region          1..375
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mltvrevsvs gyrslrrigf pvddlsvfvg gngtgktnly ralellqaaa rgtltrdlaa
       61 eggmnsahwa grrrqgepar irlsatlrdd rtgqdftyav eiglvpqaga eiygaafrhe
      121 pqikterlsv rtggrtavil drdgrsgfvr dadgrkqslg idllatetal gsarvatgqp
      181 eiafvrlamt awrfhhgfrt daesplrrpc lavttptlas dgsdlaavfa tlvhirqdtn
      241 dldeavdgaf pgarlivpep greasfgvtf pdfhgrvfaa selsdgtlrf lalagallgy
      301 rlppfialne petslhpdlm dplarliara aartqvwlvt hserladgva ehggarprtv
      361 lkrdgetwie glrlsgsfgd ead
//
LOCUS       WP_010683893             257 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Methylobacterium
            mesophilicum].
ACCESSION   WP_010683893
VERSION     WP_010683893.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..257
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28170
     Region          14..224
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpnprarklq ryiplsdadk lwlsdvlgpg rqiaartdii hegddpravn vildgwacry
       61 rqlldgrrqi vafllpgdlc dphvfllkem dhtisaitpv llgqisgaam qamtarspql
      121 dlavhrevla taavqrewtv slgcrtgier lahlfcelha rlaavgladd ntcpmpitqn
      181 dladamgqts vhinrtlqem rsaglitlrr rsltihdpta laqlghfdra ylhltvdyps
      241 apfpartvgs lsigndv
//
LOCUS       WP_010683969             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Methylobacterium mesophilicum].
ACCESSION   WP_010683969
VERSION     WP_010683969.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48725
     Region          25..446
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(39..40,43..44,47,79,129..130,132..134,137,157,
                     160..161,164,276,279..280,283..285,288,316,320,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mqrvaaeggl ertvaaeagr ttrfrwvlmi lvfgiytlas adranvgivl pfvkaefgmt
       61 nteagavisl ffvgysvaqi psgflvrrfg vrstfpifml ltslftgllg tagsafamka
      121 nrlalglaea plpvailsml nrwfppqekg tavgiflaaa kfgpvlvppi gaviittfgw
      181 pyvfyfcalp givfsllwyg lvtddpgrnr fvsegeanhi qagqrtapga eaaavaaepr
      241 wigrldrlvr arvvrpiata retfasphiw glaagyflms giitvilswl ptylvtvkhf
      301 simnvgfvss apfvggvlgn lvggwfsdri vakrrkptil ististvfmm yalvhapndp
      361 ptlaallmlt gfllnlgysa ftvypagltt keayplavsv vntggqagaa llpfvtgvil
      421 dhfdwdrvfl flgsaslval tvmltiidpv errag
//
LOCUS       WP_010684189             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Methylobacterium
            mesophilicum].
ACCESSION   WP_010684189
VERSION     WP_010684189.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32243
     Region          9..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..291
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(110..111,113..114,117,121,123..129,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 meridflglq aflsianwgs fnraaaslnl sqaalshrlk kledelgvrl varttrqvtl
       61 tpagvellps aqrivdelsq ifgtlrrqgr esqdvvrfgc lptiaghhlp vilqgfsaah
      121 pgvlvrvldq sataiiervr ageaefgiti msaqhydldi tpihqeafvl vcradhalar
      181 akvvtwsdld reilikigeq tgnnlliaag lggryadvtw tyevhrvata igmvrgglga
      241 tvvprlafqa adegkivavp lrapsiarti givtrrnhtl spvaeslarm iqayfnal
//
LOCUS       WP_010684025             314 aa            linear   BCT 01-JAN-2025
DEFINITION  site-specific tyrosine recombinase XerD [Methylobacterium
            mesophilicum].
ACCESSION   WP_010684025
VERSION     WP_010684025.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Spiers,A.J. and Sherratt,D.J.
  TITLE     C-terminal interactions between the XerC and XerD site-specific
            recombinases
  JOURNAL   Mol Microbiol 32 (5), 1031-1042 (1999)
   PUBMED   10361305
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Cornet,F., Hallet,B. and Sherratt,D.J.
  TITLE     Xer recombination in Escherichia coli. Site-specific DNA
            topoisomerase activity of the XerC and XerD recombinases
  JOURNAL   J Biol Chem 272 (35), 21927-21931 (1997)
   PUBMED   9268326
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..314
                     /product="site-specific tyrosine recombinase XerD"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007049 - cell cycle [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=33906
     Region          18..311
                     /region_name="xerD"
                     /note="tyrosine recombinase; PRK00283"
                     /db_xref="CDD:234713"
     Site            order(167..168,236,238,258,293)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271175"
     Site            order(167,258,261,284,293)
                     /site_type="active"
                     /db_xref="CDD:271175"
ORIGIN      
        1 mtavqgsdeg shapssevad yldmlaaerg aglntlsayr rdlddylgfl arsgidlpev
       61 dagtlraflv dlearglkas saarrlscvr gfhkflyaeg fadadpsvav sgprrgrslp
      121 kilsvaevdr llgvaqaeas aerapgaarr arrmvcllel lyatglrvse lvalpraaga
      181 trerylfikg kggrerlvpl teaarsamaa hletvpedsa wlfpadsesg hltrqafard
      241 lkavalqadl rpdrisphvl rhafashllq ngadlrivqe llghadistt qiythvlder
      301 lkamvrdlhp lmdg
//
LOCUS       WP_010684206             780 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Methylobacterium
            mesophilicum].
ACCESSION   WP_010684206
VERSION     WP_010684206.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..780
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84231
     Region          24..780
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrsigepaa srafvpvrrl vrvslissts lltlgtgala qpapvtdvel selsvmgetr
       61 grtlngdlyg aggangavpg yvasrstvgt ktdtpileta qsvsvigrqq iedqnaltin
      121 qalrftpsvt teqrggagst rleqfyirgf tapifldnma lptnrdafpt vdpyrlervd
      181 iikgpasvly gqsgpgglvn lvskvpqfvr hgeifvqggg fsevrggfdi ggpiesdipg
      241 fadqfayrvi glgwngdgpa vttkverafi npsitwrpst dtsltiiany qrdpfsgfyg
      301 gfpavgtvfa rnfgngifgr lpvnfydgdr niersdrtqa sieylfdhri tetlrfhsag
      361 rylrsegdyr svfttfgdvn gpytsgpiig rsvggtqvdi eaytmdnnvi adfdtgpiah
      421 tallgvdhrt fstrsvtgpf pattslnala pnhelpiafp aftatarida qqtgvyfqdq
      481 akfdrfiltl ggrydtarqt gptrtfapng ltiqdvpaea ftgrasllyl fdsgvapyvs
      541 yseafepivn grifdtafgs agrvpdpias nqyeagikyq ppgtdilltt affdirrsna
      601 ttsdpvnpgf fvqtgevgvq gvefearatl aeglsliggf slldirnird tgfttndltr
      661 rqvplqglrp vqvpdttasl fvdyrftdgp llglglgggv rylgpswgdp antfqvpesv
      721 lvdavasydm khldprltgl tgqiniqnll deryvtgcft ysgcyyglpr tvyatlryrw
//
LOCUS       WP_010684255             247 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Methylobacterium mesophilicum].
ACCESSION   WP_010684255
VERSION     WP_010684255.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..247
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24992
     Region          47..243
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mrwgpvllkl allvllgafl iapeafaglf rpfapgdtpp iyvqtplltl ainhlllvaa
       61 ataaasllgv gfavvatrpa grdvlpfara vanlgqtfpp vavlalavpv vgfgtvptli
      121 alilygllpv fetaltglgg ldpalmeaar gtgmtdrqrl vavelplalp milsgirvsa
      181 vfglatatlg stvaastlge aivsglltgn tayvlqgglt vaamailida gfqnlqlraa
      241 rragfps
//
LOCUS       WP_010684277             311 aa            linear   BCT 01-JAN-2025
DEFINITION  ring-cleaving dioxygenase [Methylobacterium mesophilicum].
ACCESSION   WP_010684277
VERSION     WP_010684277.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10327061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..311
                     /product="ring-cleaving dioxygenase"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32945
     Region          5..128
                     /region_name="VOC"
                     /note="vicinal oxygen chelate (VOC) family; cl14632"
                     /db_xref="CDD:472697"
     Region          155..308
                     /region_name="PcpA_C_like"
                     /note="C-terminal domain of Sphingobium chlorophenolicum
                     2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and
                     similar proteins; cd08347"
                     /db_xref="CDD:319935"
ORIGIN      
        1 mvqtglhhvt afsgpalrnl dfhtrilglr lvkktvnfdd pgtyhlyygd aagrpgtilt
       61 ffpiehaapg rvgigetqet afrvprasig wwthrliekg vaheplvqvf geptlrfrdp
      121 dgmmlalvgv dpgaddagte gwassevpae hairglhgvt llldkaepta ailtevlglg
      181 evaregnlir fagsaaiggl vtvravggfl rgrpgagsvh hiafraadda aqaamgeala
      241 arglhateqr drqyfrsiyf repggvlfei atdapgfavd epvealgsal klpaglephr
      301 aeieavlpkv a
//
LOCUS       WP_010684278             210 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Methylobacterium mesophilicum].
ACCESSION   WP_010684278
VERSION     WP_010684278.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..210
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21650
     Region          32..205
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtqeslgfvh hfepgadaar pllllhgtgg gehdlvplgr mvapdaalla prgavtengm
       61 prffrrlaeg vfdeadlrrr tgdlaafvae ardryglgap lalgfsngan iaasllmlrp
      121 gvlagavlir pmvpfaeppa adlggrpvli lsgamdpivp aenarrlaaq ltaagaaveh
      181 rilptghgls qadvslasaw lrnaalsraa
//
LOCUS       WP_010684410             144 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010684410
VERSION     WP_010684410.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..144
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16258
     Region          42..117
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mnasphnlsr qqvmalleer dtlleqvrql eealapaail prswrltste erllcalrav
       61 gpnvlhhera mlalygmlde apqqkildvl vckirrklme aqaqirieti wgrgwrlspe
      121 scarfdalvg edrvrwaaqg rava
//
LOCUS       WP_010684605             296 aa            linear   BCT 01-JAN-2025
DEFINITION  ketopantoate reductase family protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010684605
VERSION     WP_010684605.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..296
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29882
     Region          13..295
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mnvavvgaga vgcyygflla raghavtlig rpalveavra dglvlegsek taavpvratv
       61 dgdgvagadl vlvcvksgdt eaagamiaah lepsatilsl qngvdnaerl adllgravvp
      121 vavyvatama gpgrvrhngr gdlilgasea sdriaaalta agapttvsgr aldalwgkli
      181 mncaynalsa ltqlpygrlv qgegvvaamt dvvqecvtva eaagvsvapd ifdsvmalst
      241 amadqrssta qdlargrpse idhlngyvvr kgaalgiptp anrmlhtlvk lveqkg
//
LOCUS       WP_010684610             657 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Methylobacterium mesophilicum].
ACCESSION   WP_010684610
VERSION     WP_010684610.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..657
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69788
     Region          20..372
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 msedpvtaqr lreglpviva laslllvvat maalylgrei lvpvtlaill sfvlvpavrm
       61 lrrlrvprap avllvvvivf galfgigsli aseasqlaad lprytlvmrt kikdlrgata
      121 gtgtlsriad mvqdlsatlq pppaaeikge pgspthpitv eltpvrasvi dtlqtfagpv
      181 lhplattgli liftifillq redlrnraik laggsgdlrr ttaaiddats rlsrfflaql
      241 alniafgvvi gfglwiigvp sptlfgvlaa ilrfvpyiga aisallplil aaavdpgwsm
      301 viataalflv vepicghvie pllyghstgl spvavilaat iwtflwgpig lvlatpltvc
      361 lvvlgrhvqr lwyldvllgd qpalsppeif yqrmlagdpv eaidqgwqfl keralvtyyd
      421 evalagllla qedlsrgtld rerqaevgta irtvvdrlgt apvarrprrg sgrgpdteta
      481 aalaavgpdr qvagivlsre dlapgwrset pvlcvssrgp fdeaatlmls qilarhglas
      541 qilsmaaira gerpenpegl alicfsylep vslsqirftv rqaraavpgv rilvgfwrer
      601 dpatldrlrr atsadflvts lnealsavlg acretapart spapaaalpg partaaa
//
LOCUS       WP_010684643             323 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010684643
VERSION     WP_010684643.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..323
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33768
     Region          1..322
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,214,
                     236..237,239..240,261..263,313,315,317)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mrallctrld gpehleiaer pdpvpgpgqa lvrirlaaln ffdtlivagr yqvkpplpfs
       61 pggegvgvve algegssgva vgdrvivhag hgccaeliav darkltpvpd avpdeqaagl
      121 titygtslha lanrarlqpg ewlavlgasg gvglaavelg rligarviac asseeklava
      181 rahgaeatlv ydpatlkdel raisgggvdv vydavgdaya epalralgwr grylvigfaa
      241 gaiprlplnl mllkeldvqg vhwgafldre peahqadqrq llgwvaegel takvhgvypl
      301 tefpeafgll trraavgkvl lrp
//
LOCUS       WP_010684678             127 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF423 domain-containing protein [Methylobacterium mesophilicum].
ACCESSION   WP_010684678
VERSION     WP_010684678.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..127
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=12612
     Region          6..125
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mrlsgfdral vaiaclagll gvalsaaaah ipgadslkta aqfllfhapa ilalaglgaa
       61 glvraglarv aaallvlgli lfcgdlgvrt wlqrplfpma aptggfalmg gwlvgflcal
      121 vparrga
//
LOCUS       WP_010684685             243 aa            linear   BCT 01-JAN-2025
DEFINITION  M48 family metallopeptidase [Methylobacterium mesophilicum].
ACCESSION   WP_010684685
VERSION     WP_010684685.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..243
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27300
     Region          11..241
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mplallrrpd pdhlevqhag vslrialrrr ptarritlrv saatgevvit lpsrtainta
       61 qlfaarhsgw iaarlarvpa rvvfepgasv pvrgvahrle lrgtrggvra egdgedavls
      121 vacepahvar rireflvrea rrdlteaver yvdrlgerpt ritlrdtrsr wgsctarrel
      181 nfswrlilap pmvldylvah emahlremnh sprfwellhg lcsevdaaea wlkrhgaslh
      241 ryg
//
LOCUS       WP_010684697             534 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010684697
VERSION     WP_010684697.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 534)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..534
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57157
     Region          1..529
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msepvvrird ltialpkgad rphavedlnl dlesgkilcv vgesgsgksm sayaltgllp
       61 ralkptagti lfegrdlltl depawrslrg rriamvfqep mtalnpvmri gdqiaemfea
      121 hdlltrserr aravalakev glpnpeeavr ayphqlsggq rqramiamal alepsvlvad
      181 epttaldvtt qaqilrlird lqqkrgmsvl fithdfgvva eiadhvavlq rgrlvesgta
      241 eavlrtpqap ytkallaavp sltppprspv daapvalsvs glsktysgrs glfgkprvva
      301 avkevsfdvr rgetlgivge sgsgksttar lairliepdg gtvrlgdldy talgkaalrd
      361 krsriqmifq dpfaslnprr tveqiitagp iahgvpaaea rerarsllgl vgldpkaaar
      421 ypnafsggqr qrigiarala mepdvlvade avsaldvsvq rqvldlledl kqrlslamlf
      481 ithdlrvaat icdriavmhr gavvemrgta elfaapehay trsllaavpg ahas
//
LOCUS       WP_010684720             438 aa            linear   BCT 01-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010684720
VERSION     WP_010684720.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..438
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47591
     Region          5..435
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mpeveatpyw ldgnfapvqe eitsfaleve gaippdlsgl yarnganprd ghsghwflgd
       61 gmihgvalrd graewyrnrw vrtprfegra sgnpldlrgs vantsvvtha grtfalvena
      121 lpmrigpele tlgyedfggr latpftahpk icpetgelhf fgysplppyl tyhvadaggt
      181 lvhsaalplp apvmmhdfal trghvvfmdl pvvfdmtlal rgtmpfawsd ahaprlgvlp
      241 rgagaealrw vavepgyvfh vgnayeeadg tlvldvawyp elwrggpsas rfeparlrrw
      301 rvapgadraq etdlddrpve fpriderrtg lahgvlyavq tgagpsgdet gdgalvrydl
      361 argrdathvf aggipsefah vpggpgegwl mgfvydrvrg asdlvileas emaaepvarv
      421 rlprrvpqgf hgtwipda
//
LOCUS       WP_010684789             290 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Methylobacterium mesophilicum].
ACCESSION   WP_010684789
VERSION     WP_010684789.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..290
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30563
     Region          167..288
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msrpspstsp salagirdvl vgtavegere gassaigygl tlakaagahl tvqsaswrls
       61 gddawlgdfd degvavidrr ldalarsiaq rsagdaaqag vicmtetpsl pypeivsrlt
      121 erarlhdltv ldigarafdl dremiekalf hsgrpviavp pghdaftvrr imvawdgsaq
      181 aaraandalp flraaeavei vsvgteaeih aevpgaefap hlarhgvnat vndlprgesv
      241 aatlraqagl fradmivmga yrhsptreyf lggvtrsflr gspaplflah
//
LOCUS       WP_010684993             177 aa            linear   BCT 01-JAN-2025
DEFINITION  Dps family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010684993
VERSION     WP_010684993.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..177
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=20027
     Region          17..171
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 makakpssrf esarlntptd ldpndvkkia egltilssdl falyiktknf hwhmsgphfr
       61 dyhllldeqs eqifgiidav nerarkiggt vlrslgqaks ltrvpdndae yvsplemlke
      121 lrddnkalta hmrelhgvtd eaddvattsq leewidqsee rtwflyeitr datdsgh
//
LOCUS       WP_010685022             428 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Methylobacterium mesophilicum].
ACCESSION   WP_010685022
VERSION     WP_010685022.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..428
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=45423
     Region          5..412
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 msesvaivgl gyvglplala fgrsrptvgy erdaakvaay ragldpagev saaafraaah
       61 lsvtddparl seadviivtv ptpvdaaqcp dfelltqasa lvgqnmrpgt tvvfestvyp
      121 gateevcipv lerssglrwk sdffvgyspe rinpgdvehs lgkvvkvvsg dtpetlarlr
      181 alygtivdag lhaaasirva eaakvientq rdlnialmne lslifdkldl dtlevleaag
      241 tkwnflpfrp glvgghcigv dpyylthkaa migyhpqvil agrrindsma ahvargtvkr
      301 ivrrgggagn arvivlgltf kencadlrns kvadlvrela efgcavsvhd prasaaeaaa
      361 eygialvgwd alpedadavv iavphqdyae mapeaitarl kpgglvvdvk slhdraafar
      421 lgyevwrl
//
LOCUS       WP_010685034             106 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Methylobacterium mesophilicum].
ACCESSION   WP_010685034
VERSION     WP_010685034.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..106
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=11374
     Region          <27..97
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
ORIGIN      
        1 mkhhrlddmk ggwflgdfap caarssdaev gvkryaagar edkhfhkiat eltvivsgtv
       61 rmfdqvwqag diitvepgda tafealtdav tvvvktpsvp sdkypa
//
LOCUS       WP_010685076             254 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685076
VERSION     WP_010685076.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..254
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27696
     Region          8..252
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 maiavrrile gqeigkafgs hrvldavdlt lheqevvcvi gpsgsgkttl lrclallaap
       61 drgrvlmhdr vvaggqpnrt varaaravrp digmvfqhfn lwphmsvlan vieapmrvrg
      121 ltrdeavara eallakvgls dkrdaypgrl sggqqqrvai aralamrpav llfdeptsal
      181 dpelrrevlt vmrdlagegm tmmvvthemg faervgsrvv fmdggriiee gepnaffaap
      241 rtdrarrfla qfed
//
LOCUS       WP_010685079             508 aa            linear   BCT 01-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685079
VERSION     WP_010685079.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..508
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=53303
     Region          6..495
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 migtaltdla hgfevalqpt nflacfagvl lgnivgvlpg mgvmaaisil lpltfamppv
       61 aailmlsgif ygaqyggaic sillnlpchp phavtcldgy pltkqgkggt algitmmggf
      121 fgasfgivmm iffapllvra alkfgpadvc slmllgllag stlargsalk giamttlgll
      181 lgifgtdvts gferftfglp eladgveiva lalglfgiae flksvnkvep lrggasvrlr
      241 dmrpsgadlk rsalpilrgt ligslcslip gtgptiasfv ayaaekkisr tperfgrgai
      301 egvaapetat hssvqgdfip tmslgipgda vmalllaalt iqgitpgpll isqhpdifwg
      361 liasfwvgni llmglnvpli giwvklltip yrylypsalf fvcigvysts sslfhvgevl
      421 vigifgylll ilgfhpapil lgfvlgprfe enfrramlls qgdltvfver pisaaflavc
      481 aililgqlyl rwrrrgalvp dgpivmeg
//
LOCUS       WP_010685083             297 aa            linear   BCT 01-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685083
VERSION     WP_010685083.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..297
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30932
     Region          82..293
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mrlvtfssdg aeraglllgd asgpddtvvd lahpalqpal agcppqvldl irsgladaaa
       61 rlrahaipea aqlplrsvrl raplprpgri fgiahnyvda laergaphpa epflfmkepw
      121 tvigpgepvv lppgiggcty eaeiaavigr rahgvraeda lnhvcaygvf ndvsaselir
      181 rdgfgpgkni atfgpfgpyl atsdevpdpq slriglsidg vslqdsttar mlfsvadlva
      241 hlsrqtvlep gdviatgtpa giaalrqppa wirpgstmta wveglgslis piveegp
//
LOCUS       WP_010685086             238 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685086
VERSION     WP_010685086.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..238
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25943
     Region          4..220
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mrhverlplw dqayaelrta mlggrfepge rillrevaae lgisltpvrd avnrliaehv
       61 lergssgqgg gavvprmnve rfdelltirc dlegraaara aeraapgdlg vldallaemk
      121 tlirqqklda yldlhrrfhf elyalarmpi leglieniwl rcgpvltyvi pdyvllekgs
      181 dlhtaalsal rtgdaeaaaa airqdireag ryiagladaa gliedpaasr rprahaas
//
LOCUS       WP_010685090             439 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Methylobacterium mesophilicum].
ACCESSION   WP_010685090
VERSION     WP_010685090.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46837
     Region          21..423
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,153,
                     156..157,160,256,259..260,263..265,268,295,299,349..350,
                     354,358,374,377..378,381..382,385)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtstsdetps eieratmrrv tlrimpllml gflvafidrv nvgfaalqmn adaglsasvf
       61 glgaglffva yflfevpsnl mlerfgarlw larimitwgl isaatalvvg pisfcalrfl
      121 lgaaeagfyp gvifyltrwf pkayrarvia lfavavplsn fvgsplsaal lgldgwlglr
      181 gwqlmsivea apavvlgllv lrflpegphr apwldeaqrg wltgrleaer aeqplvrpsv
      241 wriirdrrvl aaglifagsv gasaclsiwq pqifksyglt tmeigllnsv pfgiaaglmv
      301 lwarrsdrtg erawhvagpq altalclaaa laahgfwptv ailflailgt yavkgpfwal
      361 vtewlppgas aagiaqinai gnlgafigty lmgvikdasg syalgllpla lvtaigaala
      421 lglsrtrppl ipilpgera
//
LOCUS       WP_010685103             541 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-binding protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685103
VERSION     WP_010685103.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..541
                     /product="thiamine pyrophosphate-binding protein"
                     /GO_component="GO:0005948 - acetolactate synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0009097 - isoleucine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009099 - L-valine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56100
     Region          2..538
                     /region_name="IlvB"
                     /note="Acetolactate synthase large subunit or other
                     thiamine pyrophosphate-requiring enzyme [Amino acid
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0028"
                     /db_xref="CDD:439799"
ORIGIN      
        1 mqtlrgadiv artlealgvt riftlsgnhi mpvfdallet gislvhtrqe aacvhiadaw
       61 grltgevgva lvtggqghtn gaaalttala aespvlllsg haglselgrg afqelaqadi
      121 arpmtkaawt agsvaalgpd larafriare grpgpvhlsl pvdlldtavp aasvripdra
      181 aaairvaepa pdlvadllaa lagaerplia cgpalcdasg raamatleet lglpvvgmes
      241 prgvndpalg afaevlartd llvllgkpld ftlrfgaapa lapdcrfalv dpdpallara
      301 padrlavsgl adprpvlaal taratalprr dawhresraa layrppawad fhgtgqrlhp
      361 velcravdaf lerhpdgtli cdggeigqwp qalvrggrrl ingvsgtiga sipfalaaal
      421 erpgapvvav lgdgtfgfhm aefdtavryr ipfiavvgnd arwnaehqiq lrsygpgrtr
      481 hcdllptryd avvqalggfg alvteaadlp aaleaahasg lpacvnvmie svpapmirrp
      541 g
//
LOCUS       WP_010685116             336 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685116
VERSION     WP_010685116.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..336
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35896
     Region          10..333
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mstgvsgtpl lsienlqvhf rtpdgvnrav dgvsfaiqsg etlaivgesg cgksvtsmsi
       61 lrllpeppar iagaikfegr nlldlpnsam rkirgndisv ifqepmtsln pvltvgrqig
      121 etlrlhqglg rreaearave mltlvgipep krrvreyphq lsggmrqrvm iaialacspk
      181 lliadeptta ldvtiqaqil dlmrdlkarv gaaimlithd lgvvaevadr vvvmyagrkv
      241 eeapvrdlfr aprhpytrgl mgavpklgav ehgadarlae ipgmvpslkg riegcvfagr
      301 cpevtdlcra yapalepkap ghlaachyap kdalaa
//
LOCUS       WP_010685141             557 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Methylobacterium mesophilicum].
ACCESSION   WP_010685141
VERSION     WP_010685141.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60337
     Region          18..378
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          451..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 malperesmd fdvvvvgagp aglatairlk qraaeigeei svvvvekgse vgahilsgav
       61 idpigldrll pewrtdperp lktevqrdef mmltknsgit lpnvffpklm snhgnfvgsl
      121 snvckylgvq aealgveiyp gfpasevlfd engavagiat gdlgigksgd prddytrgme
      181 lrgkytvfge gargnltkgl iqrfelnrhs dhfkyglgvk elwqlapgkf epglvqhtmg
      241 wplpnkaggg swlyhfddhl lsvgfvthln yenptlspfe efqrfkthpm iaetfegakr
      301 igygaraime ggwqsvpklv fpggclvgcs agfvnvprik gshnavlsgm qaadaiadal
      361 kagragdelt ayeagwrdsp igqdlkavrn vkplwskygt lvgvglggid mwattilgas
      421 pfgtlahgkp dhaclkplse vtpivypkpd gkltfdrlss vylsntnhee dqpphlkvrd
      481 lelqkrsehd ifggpsgryc pagvyewved asasdgvryq inaqncvhck tcdikdpnen
      541 idwvtpegpg gpnypnm
//
LOCUS       WP_010685221             343 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685221
VERSION     WP_010685221.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..343
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35365
     Region          35..328
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 maghdhahgg hahgehvhge hvhgehahgg pshgshahgg lgghahapkn fgpafaigit
       61 lntvfvvvea iygylsnsms lvadaghnls dvlglaaawi aailvrrrat arftygyrgs
      121 silaalfnav flliamgavm wealvrlvhp epvagttvmv vagigilvng vtawlfasga
      181 kgdinirgaf lhmaadaais agvvvaglvi qltglvwldp avslgvaglv vwatwgllrd
      241 svamsldavp peispaavtg flrerpgvad lhdlhiwpms ttsvaltvhl vmedghqahr
      301 apgngflnet aeglrarfgi ghatlqieea ggpacrlard caa
//
LOCUS       WP_010685247             281 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Methylobacterium mesophilicum].
ACCESSION   WP_010685247
VERSION     WP_010685247.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..281
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29823
     Region          64..281
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mtepldprlt parpevadir lrgqvaaarf vaatprrvma paaplhraps peagldteal
       61 lgdavalyde adgfafvqlv rdgyvgyvpa aclgpaepep thrvtalrtf lypepdlkrp
      121 vrahlslgar lvvtgqsgsy letpggyvfa ahcapvahre pdhvataarl igtpylwggr
      181 tslgldcsgl vqlcldaagl pcprdadmqe rdlgrplpld lsglrrgdlv fwrghvglmr
      241 dpetlihang hhmavaaepl agavariean sfgavtgirr l
//
LOCUS       WP_010685370             268 aa            linear   BCT 01-JAN-2025
DEFINITION  creatininase family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010685370
VERSION     WP_010685370.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..268
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=27935
     Region          5..261
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mavrlwsdlt tgdfsgrdmr rviavlpvaa veqhgphlpl stdcdiaegy larvralaps
       61 egppdpdvll lpvqavgksd ehdafpgtls ldtgtalaaw tgigaavhra gcrklvivss
      121 hggnsalidl vaaelrarfg mvavttawar fgypdglfpd aeiahgihag gietalmlal
      181 rpdlvrtdri adfpprtlam artlthlrag rpaafawkag dlhpsgamgd arlgtaeagr
      241 aaldhgaraf lallrevdaf eldgsgpa
//
LOCUS       WP_010685425              99 aa            linear   BCT 01-JAN-2025
DEFINITION  PilZ domain-containing protein [Methylobacterium mesophilicum].
ACCESSION   WP_010685425
VERSION     WP_010685425.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..99
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10924
     Region          3..>77
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mferrsyprt rlnetgsisv dehrslpciv ydrsaggirv alpdaeivpe hfvlsidasn
       61 eflvcravwr kaeeigattd espilhmdgl gltralels
//
LOCUS       WP_010685445             195 aa            linear   BCT 01-JAN-2025
DEFINITION  PAS domain-containing protein [Methylobacterium mesophilicum].
ACCESSION   WP_010685445
VERSION     WP_010685445.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12091914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..195
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=20855
     Site            order(40,45,67..70,96,101)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(59,68,76,79..80,108,110)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          <65..127
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
ORIGIN      
        1 mrineidgya enadrlraal dascvvgawe wdhvggvvvy dagaallltg ksdladrpin
       61 gpmalaavhp edmtwlmdhm lravsssglv laeyrvfkad gsvrwllsrg rthrsadgqp
      121 qrshgilmdi teirdggdry vlgkpltgvd pleravdlal alkdtltddm paevrtaael
      181 vllglgrtia gtvad
//
LOCUS       WP_010685447             858 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Methylobacterium mesophilicum].
ACCESSION   WP_010685447
VERSION     WP_010685447.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 858)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 858)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 858)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 858)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 858)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..858
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89856
     Region          12..857
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mhgtiarpdp aprripltlr lalrelragl rgfavflaci algvaaiagv asisrslsdg
       61 lgregrrilg gdlaynlinr eatdterqal aregrldvva slramavags gdaalvelka
      121 vdpatypaag dlatdppgrl adllaerdgv pgaladpall trldvkvgdr ialaghpvai
      181 rgtivsepdk iaggigfgpr lmiseptlra tglvqpgsln rwsyrillps gtpdadldaa
      241 qariraatpe agweirsrsn adprfaksie rftqfltlvg ltalivggvg vgnavhafve
      301 rkrpsiatlk svgapgsqvv alyltqvmli aglgtgigla igaslpflld alfaadlplp
      361 lnptlapgel alaaayglit afafaitplg rahdvpvsgl frdtvdparv sprwryriwl
      421 avsltalval svatafdrrv alifiaaaai afgllhlval glmalarrlp hprwpaprma
      481 lanlhrpgal tpaivlslgl gvtllvtlsl idvnvrrtis atlparapnl ffldipsrda
      541 arfrdflaga apngkiedvp mmrgrivaln gvparkirpp edaawvldgd rgityadtvp
      601 dgssltegaw wsaeqgakpl vsfeadlarq lglklgdtvt vnvlgrdlta tifnlrrvew
      661 rnlginfvmv fspgtfrgap hsdlatltlp ggtdaatenh ilrdvaktfp svsavrvkda
      721 ldaigdlvgr lvlairgasa vavlaslfvl agaiaaghra rlydavvlkv lgasrsrlla
      781 ayaieyaalg latalfglma gtlagwviva kvmhldfrld lsgalvaava avalaillgl
      841 agtwrilgqk papylrqi
//
LOCUS       WP_010685462             510 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Methylobacterium mesophilicum].
ACCESSION   WP_010685462
VERSION     WP_010685462.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..510
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55105
     Region          1..430
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          <403..>498
                     /region_name="PRK12495"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:183558"
ORIGIN      
        1 mpfsdlglse kvlnaveaag yteptpiqae aiphvlarrd vlgiaqtgtg ktaaftlpml
       61 tllengrara rmprtlilep trelaaqvve nfdrygtnhk lnvaliiggv sfadqdaklm
      121 rgtdvliatp grlldhferg kllltgvell videadrmld mgfipdieri akmvpftrqt
      181 lffsatmppe ierladmflh npqrvevarp astattitqr lvatgpeghs krerlrdlir
      241 geaelkngii fcnrkrdvam lqkslvshgf daaalhgdmd qrarttalda frsgdtallv
      301 asdvaargld ipavshvfnf dvphhpedyv hrigrtgrag rsgtaytlvs pddsrslgai
      361 ealigqpvpw ldgdlstvae gsgetgtrhr grsgegrrgg rsakgtgrgd aksdvkrdvk
      421 ddakgdvkre aradgeaadr prarrgsast aqraearpas prgearaasr petgreergr
      481 raepdgetpv glgshvpafl lrpvlakkek
//
LOCUS       WP_010685584             218 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685584
VERSION     WP_010685584.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549439
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..218
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23506
     Region          53..151
                     /region_name="Methyltransf_12"
                     /note="Methyltransferase domain; pfam08242"
                     /db_xref="CDD:400515"
     Site            order(55..61,79..80,103..104,121)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 matdtqagqa iynprtlqiy dlvvlrlsnp liwrcptari ldlydrhagl ahldvgvgtg
       61 wyldrcrfps sapriglmdl nadslafaaq riaryrpety rvdvlgapas giapfdsigm
      121 tyllhclpga iaekakafdt vrpcladggv vfgatilsgg vpvtgaaral mrvynrkgvf
      181 snaadtlpdl rtaleqrfrs veitvvgcva lfvardpr
//
LOCUS       WP_010685641             230 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010685641
VERSION     WP_010685641.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..230
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25213
     Region          15..169
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mtdphvtiep silylgtpvv listqnedgt anlapmssaw wlgwrcmlgl qtasqtpqnm
       61 irtgqcvlnl aspkqadavn rlarltgtke ipvlkrklgy ayeprkfeva gltplpshtv
      121 aaprvlecpi qleavvaarh gimdddpqva glisafevri trvhvhpdll meghenridp
      181 akwqplimnf qklygvspae ivpsrlaeid elayrmpdvd rargeadlaa
//
LOCUS       WP_010685672             185 aa            linear   BCT 01-JAN-2025
DEFINITION  GbsR/MarR family transcriptional regulator [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685672
VERSION     WP_010685672.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 185)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 185)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 185)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..185
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20557
     Region          8..168
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mteisdrsni lptaverfvl hwgdlggqwg vnrsvaqiha llylserplt aediagtlgi
       61 arsnvstslr ellgwnlirr vpvmgerrdh yvaetdlwem vtriaagrke reidpaiaal
      121 racvaeadad palgavakrr lramldftet merwygqmln vprgtlakli rlggrivkfl
      181 pakte
//
LOCUS       WP_010685679             277 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685679
VERSION     WP_010685679.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..277
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28744
     Region          25..269
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mpsrlaiala vilssgpvga agapmrvvsm nlcadelvlr ladrdqvlav tylardprgs
       61 tvaseavglp vtrglteevv alkpdlviag afttrttvgm lkrvgapvle lgvpadldgv
      121 raqirqvaav lghpergevm vasldarlaa ivpatrplra lvmrpnaftv apgglgdali
      181 raaglvnvsa eigrdrfgqv pleaaalanp dlivvnegap gwpsladtll hhpvfqtlar
      241 ahrtvdipnr fwtcpgpqva evvarlaeaa narvsrp
//
LOCUS       WP_010685743             234 aa            linear   BCT 01-JAN-2025
DEFINITION  YoaK family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010685743
VERSION     WP_010685743.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..234
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23462
     Region          2..226
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mrsqntssst ftgaalafva gfvdaaafia ltglftahvt gnfvligael vatsagvlak
       61 llalpvfiaa vasarvltlm lkrqggdslp wlltielgll aafglcgalw splgaadgtp
      121 aisvgmfava amgvqngigr lclghlaptt vmtvsvsqav idatdltlgt aenfdltrtr
      181 flsvlpavaa faagalcgaf giahlafgcv vlplavlssl ivltmkpaem nakt
//
LOCUS       WP_010685769             472 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685769
VERSION     WP_010685769.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..472
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51297
     Region          6..447
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mlanvdalll arwqfgftva fhivfpafsi glasylavle glwlatgrqv fidlfrywik
       61 ifaigfamgv vsglvmsyqf gtnwsvyadk tgpvlgplma yevlsaffle agflgvmlfg
      121 mskvgprlhf latlmvaigt ffsafwilsv nswmqtpqgh tvnaagqfvp adwwaivfnp
      181 sfpyrlvhmv laaylttalv vgavgawhll rdranegart mfsmamwmla vvapiqilag
      241 dahglntleh qpakvmameg hfqshpdgap lilfglpdqa agtvryavev pklsslilkh
      301 glneplkgld svprenwppv pvvfwsfrvm vslgmlmlll gclsllarfk gklyqwaalh
      361 rfalamgpag fvavvagwit tevgrqpftv ygllrtaesa splhapavaa sltafvlvyf
      421 avfgmgilyi lhlmaksphr gehgiepgap irtagitpap svdldrtlhp ae
//
LOCUS       WP_010685818             427 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Methylobacterium mesophilicum].
ACCESSION   WP_010685818
VERSION     WP_010685818.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..427
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46773
     Region          13..400
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mkhapgptpe sptltvralp glkeigaadw dacafspetl aggdethnpf lshaflsale
       61 dsgcvsrrtg wlplhvsver dgqrlgvvpc ylkshsqgey vfdhgwaday eraggsyypk
      121 lqvsvpftpv tgprfliapg adpdeatagl vaglralrge tkassihvtf mreaewdrag
      181 aagfllrtdq qfhwendgya tfddflaala srkrktirke rrdalapgit vehltgaait
      241 eahwdafydf ytdtgsrkwg rpylnrrffs lltermadrv llvmakrdga yiagainlig
      301 dtalygrnwg ciedhpflhf evcyyqaidf aiargltrve agaqgehkla rgyrpvlmrs
      361 ahdiadpalr ravadylqre rahvaeavdv ldtltpfrrt dsgsacapaa tpspdtppas
      421 ppesset
//
LOCUS       WP_010685864             354 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein
            [Methylobacterium mesophilicum].
ACCESSION   WP_010685864
VERSION     WP_010685864.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Sinha,S.C. and Sprang,S.R.
  TITLE     Structures, mechanism, regulation and evolution of class III
            nucleotidyl cyclases
  JOURNAL   Rev Physiol Biochem Pharmacol 157, 105-140 (2006)
   PUBMED   17236651
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..354
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016849 - phosphorus-oxygen lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0032555 - purine ribonucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=38855
     Region          154..334
                     /region_name="CHD"
                     /note="cyclase homology domain; cd07302"
                     /db_xref="CDD:143636"
     Site            order(159,161..166,201,203..205,208,272..274,278..279,
                     282..283,323)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(161,205)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(166,178,181..182,185,189,201..202,260,263,273..276,
                     279,323)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
ORIGIN      
        1 mrfrppwffl vaptlgalag lmygaifevg pltgaairga iigtpimlye rrlllprlre
       61 rirglatplf llatvaiyia mivignavas tilnrlfrfm ysernamlmt dtgllyalgi
      121 saivvfvfrv rdligpgvfa nlligryhrp iseeriflfl dvtgstrfad rygdraaqay
      181 lgqvfnalal pvsrtrgsid dyigdlalvt wtmerglrda aclrcvfdfa arlnaeaesw
      241 rsrfgqvpef raalhcgpvv taeiglerhk iayfgdvvnt tarletlsks lgvhvlvsad
      301 lldrigqlpd dleaedlgah tlrgreealv vaavrhrtpv pfpaaaprra avtg
//
LOCUS       WP_010685941             426 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Methylobacterium
            mesophilicum].
ACCESSION   WP_010685941
VERSION     WP_010685941.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..426
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=45464
     Region          4..405
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 madrariviv gggvagieva tslgrggrad vtladrslsh vwkpmlhtfa agtaradrqk
       61 vdffaqarrn sfrfqpgtlv gidrqakrvr laveaaegrp eidrpydllv laigsrandf
      121 gtpgvaehcl tiddlteaeh fhdqlrchll arldrgsmle iaivgggatg velaaelkha
      181 inllsaygsp dlprrlrltl iesgarllpa fpekvsraaa rtlsdlavev rtnamvtgad
      241 vdgfslkdgs ripaglkvwa agvkapdvla gldglersrt gqlvvgpdlr tsrdpailal
      301 gdctslddpq sgkpvpataq aarqqaqhla rhlgralarg gsvatdlppf ryvekgaivs
      361 ladfngwgtl grytfgggrl nglsarlthd llyrqhqigl ygpvrgtmtw llddldhlis
      421 ppvrld
//
LOCUS       WP_010686061             367 aa            linear   BCT 01-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010686061
VERSION     WP_010686061.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..367
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39570
     Region          100..334
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mtrllipall lagclassar aadaqagpda lepvlhsdsl vfngitrakd grvfspfqrq
       61 skgkgielge wrdgkpvafp deawnawkqg ddpakafvav nairigpegd lwvvdkgapg
      121 mgeaplpggp klvqidlatn tvrkvyplqa attdrsfidd frfngrnvyl tdagqpgllv
      181 ldldtgglrr vldghwstia qrpltgqgrv lrddkgkllf ihadqlevsp dgktfyyqac
      241 tgplysietr ylddanlsda erakhvtlfa atvatggtai dadgtiyasd tdglrilkil
      301 pdgtmstlve dprlvwvdam wideqgglwi paaqmnrtpt mnggeasavk fpttiyrmqi
      361 gakplrn
//
LOCUS       WP_010686071             214 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010686071
VERSION     WP_010686071.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..214
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22531
     Region          3..204
                     /region_name="ParA_partition"
                     /note="ParA family partition ATPase; NF041546"
                     /db_xref="CDD:469431"
ORIGIN      
        1 mdvlaiatqk ggtgkttvsv nlavaaaegg rrvaaldldp qgslagwatr readdpavdh
       61 lglerigqlp eilaalerqg ydlvvldsag alnpaayfal raaslvlipa rptlldllat
      121 eptlralagi gladrvalll sqcptqgqar aatyaerlrr wgylaepplt qrvdyqdall
      181 ggqgvteyap dgkaageira lwawteqrlk escp
//
LOCUS       WP_010686151             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010686151
VERSION     WP_010686151.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..243
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24614
     Region          1..241
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mtspflgefl gtmtlivlgd gvvagallkh skgenagwia itagwafavl agvfvanatg
       61 sadahinpav tvagavssgd ysklatyipa qmlgafvgav ivwlhylphw gatqdpglkl
      121 acfctgpair daksnwlsei iatfflilti salvtttlgs agaipravap ymvgmlvwgi
      181 glslggttgy ainpardlgp rvahavlpia gkgssdwsya lipvaapmvg avlaglfvra
      241 lgi
//
LOCUS       WP_010686158             202 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Methylobacterium mesophilicum].
ACCESSION   WP_010686158
VERSION     WP_010686158.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..202
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=20292
     Region          38..198
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mesrpraegs rppgrperdl raeraaalar rgnaavrsea gvehlvclck derfgvpmaa
       61 vaqvlpmrpc tpvpgavpal vglvalsgri vgvlslaral grpdaatdpd agaghlvvlr
      121 gaqahpqapa svpvqarsla favdrvlgia raagtapass ggpdagglgn eaasgyapga
      181 agdsrpdfvv idlprllrra lp
//
LOCUS       WP_010686159             557 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010686159
VERSION     WP_010686159.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..557
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58997
     Region          26..556
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mtlsigrril lgffavtvvi valgfyalaq igavrdtada ivrrdmavlr qlddlgnear
       61 dlgllrrnav iamltqaqgr qarsedilaa wrqtadrieg rltaiaqlas eyqassasse
      121 raaawdrvaa aaadvqsafg evrtlgeaqf aaiakqdaaa vesrndditr lqapflggik
      181 tlrtlldggm avgqraaqav yersrlsiyl tlaasvllal lvtwlisrav vrpletvmrf
      241 vervgdgdls gqlearrqde vgrlagtlna mvsglsdlar tnraatadln aaaaeirasa
      301 qeqaasveqq faavqetaat vdeithsgaq iskratevia taqataqtsr qglravsdta
      361 kameaireqa eavagnivsl sektqtigdi igtvndiser thllalnaai eaaaagesgl
      421 sfavvasemk lladqakaat gqvrgllgei qrgintsvml teeavkraaa gktrsdttqr
      481 tieeitarve envqtfqqiv astnqqqlgi eqvmgalqni rqasqqtaag trqveaasan
      541 ltelaqalma laeryrh
//
LOCUS       WP_010686166             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Methylobacterium mesophilicum].
ACCESSION   WP_010686166
VERSION     WP_010686166.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..290
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30558
     Region          13..263
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(28,112,114,116..117,144,195,216,219,232,234,263)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mtgskplpgv lrwnlgdltv talndgwfqa sldlvtgisk eeagrlqvag frteqpkitl
       61 naflitgpgl tptlidtgyg dlapaptlgr agaalastgv kpeeigtvlv shlhpdhvgg
      121 lvkdgaaryp naeivlhade aahwlpdeal akapeaakpy fegarkslap yagkvrehrg
      181 gevlpgitav hlpghtpghc gfrivsggqa lmmwtdvvhl paiqfknpea gvgfdvdgdq
      241 aretrkrild evarertlia gghlefpalg yvdrdgagys fvpvlwvgge
//
LOCUS       WP_010686198             731 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Methylobacterium mesophilicum].
ACCESSION   WP_010686198
VERSION     WP_010686198.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..731
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77225
     Region          51..>189
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          195..731
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mlnarrpnpl pvrpsrrgll agagalvvaf rfdpkparaa sgpnladvka qpnafvriga
       61 ddtvtvvikh ldmgqgnttg latiladelg adwakvrtef apadaalynn tlmgpiqgtg
      121 gstavanswf qlrkagaaar emlmaeaafr wkvpvseitv adgvvrhaps grqarfgela
      181 ssaaslpvps eprlkdpsew rligqkiprl dsvaktngta vysldirrpn qvtavvarap
      241 rfgatvtsfd ataarkvagv ldvvqvptgv aviardtwaa mkgrealtva wddstaetrs
      301 sdailaeyre rakgpgltas ergdpqaalk gaakvieaef tfpylahaam eplnatieka
      361 adggydvyag fqfqtveqat maailgvtpd rvrlhsnwag gsfgrratpt adylaeaatv
      421 lkasgekapv hlvwtreddm aggyyrptvl hkvragidgr gavvgwdhvm vgksimiasp
      481 feamivkngi dattvegasd tpyalpayrf gvhngregvp vlwwrsvght htahvmevmi
      541 delahaanvd pvayrlsllt qaprlagvlk laaekagwsa kpkdqgrglg vavhesfgsy
      601 vamvadvtaq eaavrvnriv aavdvgvavn pdviraqveg avgfalsavl rnritlkdgq
      661 vqehnfdaye ptrmsemptv evhivpsrva ptgigepgvp vlgpsianav faatgrrlrs
      721 lpldlssvkg a
//
LOCUS       WP_010686184             373 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Methylobacterium mesophilicum].
ACCESSION   WP_010686184
VERSION     WP_010686184.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..373
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40359
     Region          53..366
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 madrraqtdp ngaregkgpt gglarrhvig alaagaavaa tpapaaapss rltmeefrlp
       61 wsepgveiyv rnkrpagidr fpgdrillyv hgstypssta fdlplggmsa mdylaglgfd
      121 vycvdlpgyg lsgrpaamda ppddnpplmr tpdaakvvgq vvdfirkrrg vekidlmgws
      181 wgtstmglyt sthndsvnrl vlyapqwlar tpgliggggk vgayrtvnrd sararwltgv
      241 pedrqadlip agwldqwada tfatdsagak rsppvlrapn gtvadkdayw aagkplydpd
      301 eirvpvliih aewdadlpsy qaqeyftklt hapykrfvel gegthtvmme knrmqflhev
      361 gaflteadpq aln
//
LOCUS       WP_010686204             210 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Methylobacterium
            mesophilicum].
ACCESSION   WP_010686204
VERSION     WP_010686204.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..210
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23159
     Region          15..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mslddtthli aeecapdtrs rilatadtyf reigyqkttv adiartlkms panvyrffds
       61 kkaineavle rligeseavi seiadrpgld aterlvaaie tlhrdctrrc etfprlhemi
      121 eaamveswev crhhvarita gferiiregv argafeaadp aeaaacihta iarythpllv
      181 gsstlqpvpp vevmtafllr slaprtggrr
//
LOCUS       WP_010686217             296 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Methylobacterium
            mesophilicum].
ACCESSION   WP_010686217
VERSION     WP_010686217.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..296
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32118
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mfdfsqlrcf aavaeelhfg raaarlnmtq pplsrqvqvl erildvqlle rtsrsvrlta
       61 agrsflpeaq rilrlaesat httrqvaagr agvlklgfta asaydflprl vaafrqalpd
      121 vtlalremvt kdqleellag ridaalvrpp vthpdltair amaeplvval pagnalaarg
      181 tlvprdlade dliayapnea hyfhdlvqel laeaelrprv vqqltqihsi lalvrsglgi
      241 alvpaaaehl rlegvvfral alpdprpael ilawrrnada pllaqlvsil ealpsa
//
LOCUS       WP_010686230             400 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Methylobacterium
            mesophilicum].
ACCESSION   WP_010686230
VERSION     WP_010686230.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..400
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43429
     Region          1..400
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,207,236,238..239,247)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,200,245..247,276,279)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            239
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 malladvlsr vkpsativmt qkardlkasg vdvislsvge pdfdtpehik qaaieaihrn
       61 etryppvsgi vplreaivrk fkrengldyk vsqtivgtgg kqvlynafla tlnpgdevvi
      121 prpywvsype mvglcggtpv fadtdmahgf klqaeeldrv ltpktkwivl nspsnpsgaa
      181 ysraemkalt dvllrypdvh iltddiyehl tygdfefvtp aqvepqller tltmngvskg
      241 yamtgwrigy aagpeklika mdfvqgqqts gastiaqwaa vaaldgpqdh latfraafqg
      301 rrdlvvsmln qtngltcptp egafyvypsc aaligkkteg gktietdedf vmellqaegv
      361 aavhgsafgl gpnlrisyat snavleeacr riqrfcgslr
//
LOCUS       WP_010686224             171 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Methylobacterium].
ACCESSION   WP_010686224
VERSION     WP_010686224.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..171
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18584
     Region          1..138
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdaidlkila llqtdatlsi aaigervgls qtpcwkriqk leadgvidrr vavldpvklg
       61 lgltvfvsie tadhsqewlq rfaatvsamp evlefyrmag dvdymlrvvv admqaydsfy
      121 khliavlplk nvtsrfamek vksttalplp appkngrhlp gtapvlavvg e
//
LOCUS       WP_010686285             364 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Methylobacterium mesophilicum].
ACCESSION   WP_010686285
VERSION     WP_010686285.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..364
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38918
     Region          4..337
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,225,294,314,316..318)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,173,176,178,225,232,294,314,
                     316..317)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,173,176,178,317)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mpslldpiri gaieaknrif mapltrgrgt rehvptpima eyyaqragag lilteatgis
       61 qeglgwpyap giwsdaqvda wrpivkavhd rggkivcqiw hmgrlvhpdf lggakpvsss
      121 attapdqaht yagkkpyaea ralevaeipr lladyehata nalaagfdgv qihaangyli
      181 deflrdgtnh rtdryggaie nrvrllrevt eavakvagpe rtgvrlspng aiqgcndsnp
      241 eplfvaaaqa ladvgiafle mrepgpdgtf gkadhppiap amrrvfrnpm ilnadydgts
      301 gqkvldagea daisfgrtfi anpdlvaria kgaplnkdna atwysqgpeg yidyptlade
      361 praa
//
LOCUS       WP_010686323             316 aa            linear   BCT 01-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010686323
VERSION     WP_010686323.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..316
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=33342
     Region          4..284
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mteiaivggg lmghgialvl alhghavrit dtapetrarv palmasalet lreagaapeg
       61 wdadrlarav rveaelepav agaglvieai tenpeakral fadldrlcpa dailasntsy
      121 ldvfplipda rqaralilhw ytppyivdlv dvvpgpgtdp avvaamadlv rglgkvpivl
      181 krfipgyian riqqaisaev frlldegvad pkdiddaiih glalripilg hlakadftgl
      241 eltqralang syapppprtr setldalcaa grtgvmagqg yfdwggrapa dlfrerdrkl
      301 lalkaamagi grmegt
//
LOCUS       WP_010686331             352 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010686331
VERSION     WP_010686331.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..352
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38363
     Region          39..289
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(44,47..49,52,63,65,97,116..119,216,218,220..221,223,
                     234..235,238,253..254,257)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(44,48,52,63,65,97,116..119,216,220..221,223,
                     234..235)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(47..49,216,218,221,235,238,253..254,257)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 msdadvfsgv kpveprhrid etklaawmeg hvrgfagplt vqqfrggqsn ptyrldtpaq
       61 ayvlrrkpfg qllpsahave refrvigaly gegfpvprpf alcedseiig aafyvmeavd
      121 gavhwdgalp gldpharhrh yagmiatlar lhaidpeaag lsdygrpgny farqvdrwtr
      181 qyraaedgrl edverliawl prtvpeqqga cvvhgdyrld nlifsrdggv savldwelst
      241 lgdpladfsy llmqwelpad grsglggldl salgiptrde avalycraad rknlpaldwy
      301 faynlfrlvg ilqgvaarak agnaasehaa amaarvpkla aaawgfaera ga
//
LOCUS       WP_010686337             423 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Methylobacterium
            mesophilicum].
ACCESSION   WP_010686337
VERSION     WP_010686337.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..423
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43903
     Region          7..405
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 maqtsgrvli vgaglaalrg aealretgfs gtltivgdep yhpydrppls khvltgatpa
       61 dattlpgshg ldadwqlgsa avrldraaha vhladgrslp ydrlliatgt rarpwpnphe
      121 grlagvftlr grddaralrq alaagprrvl vigggfigce vaslcrqlgl pvtlvepgpt
      181 plarvlgrtv ggfigaiheg hgvelrcgse vewledeggr lvrahlvdgg ridadlavia
      241 lgavrntewl dgsglsadpg gvdcdadgrv ldtegrpdph itaagdvarf phplyegrrv
      301 alehwshava qgvhagrlla gtpsngpyga lptfwstqgd lvvksaglte gadtvaitqg
      361 dpaagrfval ygragrciaa vsvdsarwlp ayaelvaaga pfpprgtatd rpkgieifep
      421 gfp
//
LOCUS       WP_010686435             266 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Methylobacterium mesophilicum].
ACCESSION   WP_010686435
VERSION     WP_010686435.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..266
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28566
     Region          2..257
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mlidshchld fpdfaadlpd viarakaagv agmltistrv akadtyraia eahaevwyti
       61 gthphgaaee pdvaagtiad iaeanprcvg igeagldyhy adaapeavqe rvlrahieas
      121 rraglpliih ardaddhmer vltdemgrsp fravlhcfss grrlaeagve lglfvsfsgi
      181 vtfrrshdlr diarrvpldr ilvetdapfl apephrgrtn epaytadtar slaetlglsa
      241 ediarittan ffalfdkaag trpsaa
//
LOCUS       WP_010686443             166 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010686443
VERSION     WP_010686443.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..166
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17966
     Region          5..160
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mtrdklttcl wfdhgearka aefyaatfpd shvgtpmnap sdypggsaga eltvaftvlg
       61 rafvglnggp afkanqavsf mvltedqaet drywdalvsr ggaesqcgwc tdrwgfswqi
      121 tprallrans hpdraaarra feammtmrki diarieaair gdsada
//
LOCUS       WP_010686466             437 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein
            [Methylobacterium mesophilicum].
ACCESSION   WP_010686466
VERSION     WP_010686466.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..437
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=45394
     Region          34..390
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 masgsagnpt laalqsarsp aegraepgsd daavlramqa ggglrllglr vvivlvllma
       61 aqaydgslha lshwfilgly glgtvwfglr ergggpaana yswagtglna glavyviieh
      121 mmagggaglg adavsrlpaf llllqtglsm rvaqtlvfcg lvtvcwsaaf lvglvhpdlf
      181 pnadtfptaq itglatfmaa gllvidgmir lraavaralr mehertqlar fvpdtvaldl
      241 aaedgdsglg ihrrhaclmi ldirgfsrls rehppeamvk allavraaaq aavaeqgglv
      301 dkyigdavlv qfvldrpdaq araalacals irdriaalna erareglftv rvvvalhagd
      361 llvgvfddgv raeytvlgpa mnalarietq akaaeialaa sgdfmdlleg tlpvgiravp
      421 vpqavlpgpl tlfaiae
//
LOCUS       WP_010686528             266 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010686528
VERSION     WP_010686528.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..266
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=27517
     Region          58..244
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mrrlalsfml aalaagpaaa eqdlllgadm aspamtkaem sradveamik aadgkpidlh
       61 dkalsgldls glnlrgvnlr tarlnkanlr gadlsganle qawflkadls gaklagakmf
      121 gitardanfs gadlsrsmpi gdfkganmsg atlvdldgga diknqsmglm ravftsvnls
      181 ganlkganlg rsrleyadle dadltdvvlm gsdlsgadlt gatiagadfk nvdvsgarli
      241 dlkgqaeakd waervnvdra itqaih
//
LOCUS       WP_010686595             328 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Methylobacterium mesophilicum].
ACCESSION   WP_010686595
VERSION     WP_010686595.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..328
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35751
     Region          148..289
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mrdesrdear vrlavagsre aplirvaelg tpdaaveail araealtaqd tgvqriavaa
       61 dpetagrlla lgaarrvgdg ieilpgllwq caarwlpdar ppfpalyiat egrrhplrpe
      121 tpagtvyarv ipwlertlsf rtltepgdva lfsawmndpr vaavwqetgs ldahatyigr
      181 lqsdagtlpl lgcldgtpfg yfelywares rlgplyesdp ydrgwhvaig daavrgrsyl
      241 sawlpslmhy lfldeprtqr ivgepradha qqirnlhasg fatvatidfp hkraalvals
      301 rehfvrdrlw vpgaaaadaa prppavpa
//
LOCUS       WP_010686597             257 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Methylobacterium mesophilicum].
ACCESSION   WP_010686597
VERSION     WP_010686597.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..257
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26875
     Region          175..247
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mraldltfda lreahvaslt gslidgvehg pggagyvwsr gipdptlnfa ygvsrpdqfa
       61 wagaaalgra rapaflarda eevallrglf epavhypasw mvarslpars agddpvavqa
      121 tpapgpvfeg vfanlsddpa vrthlrrtyl palraarvrp gvaplhlvlr daagpaacas
      181 lylrgdtagl ynvstrfdrq rrglgaavtt aalreararg avqvflqcpa ggaiealyar
      241 agfrtvcapt llctspp
//
LOCUS       WP_010686658             181 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Methylobacterium mesophilicum].
ACCESSION   WP_010686658
VERSION     WP_010686658.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..181
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=19465
     Region          10..170
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 msaaieikdl slrvngaavg pipvpvgtsl ldvlhewlgl tgsrmgcgqg ichactvmle
       61 eaagpreira citgahwfeg rsirtvegha rtapdgtvvl spvqqafiet fafqcgyctp
      121 gfvtgasvli erlrrepirr devervvtea ldrhicrctg yvryhqavrd lvlatpglvt
      181 a
//
LOCUS       WP_010686711             405 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Methylobacterium mesophilicum].
ACCESSION   WP_010686711
VERSION     WP_010686711.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41936
     Region          22..361
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mpdaptlttq rasfaqagps nvlrlaiaqa lagansvvvf stgaivgnml apskvlatlp
       61 isifvvgmaa cslpagsiar rygrgaafmc gtscgvlvgl lstlailtad fwlfsaamff
      121 ggayaavvfs frfaaaecvp perrpralst vmaggifagv igpqlvthtm nlwppylfaa
      181 tflaqaavaa laavvlagvr lprpaadvld ggrplarila qprfiiavvc gsvsyllmnf
      241 vmtaaplamh lcghaqadan lglqwhviam ygpsfftgrl itrfgaprvv aagltltgaa
      301 avvglagvdv ahfwlalill gfgwnfgfvg asamvlechr peertrvqsv ndfivfgmva
      361 vgsfssggll tsygwdtvlw vsfvplalaa salvlmsvrg arrla
//
LOCUS       WP_010686759             299 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Methylobacterium
            mesophilicum].
ACCESSION   WP_010686759
VERSION     WP_010686759.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32291
     Region          6..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,220,237,265)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     214..218,225..226,229)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mndqsdleif arvvrtsslt qagselglsv avvskrlkrl eerlavrllh rttrrvaptd
       61 vgaafferia pivdaiaeae slvsqtasra rgtlrvtaps sfgrlhivph lraffalhpd
      121 lvlnlelsdd fesivergyd lairvgales sgltavrlap vrrvlcarpa yldaagrper
      181 lddlrghvcl atenqnpwrl vgpegpctvg asgplrthsn evvreavigg lgialrstwd
      241 vhaelrdgrl evvlpaytaa asagifavyp srafvpaktr afiaflkqty rssgawaeg
//
LOCUS       WP_010686782             311 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Methylobacterium mesophilicum].
ACCESSION   WP_010686782
VERSION     WP_010686782.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..311
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32608
     Region          2..292
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(27..28,31,83,97,99,131,165,253,256,292)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(220,225,243,253..255,258,280,284)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mrvacigecm velserpdgs largfggdtl ntalylarlg vavdyvtalg ddvwsdemaa
       61 swgqegiglg avrrmpgrmp glyiirtdpa gersfhywrd raaardlftg pdaagtraal
      121 atydlvyvsg islslygagg raalgetlsa lrarggrvaf dtnyrprgwp drdearttfr
      181 aalaqadlif asvedldwlf getgedevlr hrgraeivlk asgrsgpvar vlhgasdtav
      241 pagpvervvd ttaagdsfaa gylaarlagl apeaaageah rlagavighr gaviprdamp
      301 amafrppdpa a
//
LOCUS       WP_010686831             562 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-binding protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010686831
VERSION     WP_010686831.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..562
                     /product="thiamine pyrophosphate-binding protein"
                     /GO_component="GO:0005948 - acetolactate synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0009097 - isoleucine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009099 - L-valine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58562
     Region          11..559
                     /region_name="IlvB"
                     /note="Acetolactate synthase large subunit or other
                     thiamine pyrophosphate-requiring enzyme [Amino acid
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0028"
                     /db_xref="CDD:439799"
ORIGIN      
        1 mpietveaag rrrgadllve vlrsegvryi fgnpgttelp lidalteapd iayilalqea
       61 tavamadgya qgarrpafln lhtagglgha mgglvnsqvs gtplvvtagq qdlrhaltdp
      121 llmgdlvaia dpvmkwarev tspdqipill rrafhdagaa psgpvflslp mdvmeamsav
      181 pagetstidq ravagsldrl aeklaaiapg rlaliagdei dasdasaqmv aladllaapv
      241 ygsswpahip fptahplwag nlptradaia dilgrydavf alggkslitv lysdvsavpp
      301 gvqvfqlsad vrdlgrtyat clstvgdira sldallplla prladraeaf aqlrsqavtv
      361 raerraklaa aadaafedpv iaplvaarev aravgaetti vdeapatlth lrtfldspsa
      421 hqyaamrggv lgwgmpaavg fslgldrapv vcvvgdgaam yspqalwtaa heklpvtfvv
      481 innaeynilk tfmkgqahya svranrfiam dltdprvdfl alaasmgvpa rrvtaatdia
      541 paieagirsg ganlvevvvr at
//
LOCUS       WP_010686840             343 aa            linear   BCT 01-JAN-2025
DEFINITION  YncE family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010686840
VERSION     WP_010686840.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..343
                     /product="YncE family protein"
                     /calculated_mol_wt=33964
     Region          90..300
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          233..268
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
ORIGIN      
        1 msaartaagg ppgigrgatl aallatlsaf lgsagaqela vvsqqgarvs riaagalsaa
       61 vavapapavv aadaggrlyv shpdghaitv vepdgalrrl pfagqafgla vepdgraiyv
      121 gdwsgnrvar lsaatgavea avdvgrdpag lvlgadgrly vaeresrsvg iidtgrmerv
      181 aslpvgdgpf alahdpvrqr lyvanvrsnd vtvidaaaar vlgrvtvgas pygvavsgdg
      241 arvlvtnqha asvsvidaaa lsvvatvpvg rypegvallg trayvanwfs ddvsvidlds
      301 qramgripva egprtivalp pagtsagpaa gaaagtaaeg rsr
//
LOCUS       WP_010686946             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Methylobacterium].
ACCESSION   WP_010686946
VERSION     WP_010686946.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..218
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23947
     Region          3..209
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 mpeviftgpa grlegryqap kkrgapiaii lhphpqfggt mnnqivynlf ytfanrgfaa
       61 lrfnfrgvgr sqgsfdhgsg elsdaaaald wvqsvnpeak scwiagvsfg swigmqllmr
      121 rpeiegfisi aamanrydft flapcpssgl fvhgsedrva parevmpvie kvktqkgvii
      181 ehqmveganh ffdgkveelt qtvdtyldkr lgkreeaa
//
LOCUS       WP_010687282             227 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Methylobacterium
            mesophilicum].
ACCESSION   WP_010687282
VERSION     WP_010687282.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..227
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24629
     Region          17..221
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mskgssfgpl lrvnplfadl gpeaidclae mattrilrsg evlfqvgdpg dtlygirrge
       61 irietgteag rrivlnslga gdlfgeiall dgrertadav aavasevfvl rrsdllaylr
      121 repdvairli gllcsriryi agqmnelatl slgarlarrl tvlaedfgne iqisqeqlga
      181 fvggtresvn rqlqvwrrag yidlrrgcvv lldakaltrm aqepsca
//
LOCUS       WP_010687445             223 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Methylobacterium mesophilicum].
ACCESSION   WP_010687445
VERSION     WP_010687445.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..223
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23980
     Region          67..223
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 msrsastlae priaslldsl faqaetsspl saigdlsade rtrlmgsstg yrdfysrlkd
       61 mplavsretg rllymlarsc rartvvefgt sfglstlhla aalrdngggr lvtcefepsk
      121 vvraranlme agladlvefr egdalqtlgl dlpdavdlvl ldgakglype vlslvesrlr
      181 pgalvvadna dhspdylarv rapsrgylsv rfaedvelsm rlg
//
LOCUS       WP_010687494             410 aa            linear   BCT 01-JAN-2025
DEFINITION  amidase [Methylobacterium mesophilicum].
ACCESSION   WP_010687494
VERSION     WP_010687494.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..410
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41980
     Region          2..406
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mlslldlrar iaagtltpgg aidlcraaia arepdlhalv tldaapaipd sgplagiavg
       61 vkdiidsagl ptqmgstiye gwtprgdaav vsrlkqlgav alakttttaf assdptatvn
      121 phdpghtpgg ssagsaaavg agmlplalgt qtagsvirpa sycgcaavkp sfrliptvgv
      181 ktyswaldtv glfaagvadv ahalalvtgc peieradags apriglvrqd fagapapeae
      241 aalvrarqaa eragarvndl alpeelaqaw erhnliqhye grlalaweyd tqadalppla
      301 rahldagaai spaqyddarr hghharrvlk glfadydail tfsasgpapa tlastgdprf
      361 nqlwtlmgvp cvnvpvpghr lpvgvqvigr fgddgralav arliedglrg
//
LOCUS       WP_010687516             563 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010687516
VERSION     WP_010687516.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..563
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58502
     Region          48..556
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mlrlsnikil pklvaviali saivggciwy aqsrmttidd gysrfivnea aavaevrrln
       61 rlivelnygv yriiaetapd qisaandtfe mtvpklqali palrahaptf setidtqaar
      121 ierylrdvie vrrlgtanqn adaialvhsa idpvfsglla dgnrladeik aymeknsdtp
      181 tdqtnatrrt liaisaigml agllaavfia tvgitrpldr lvsvlqrraq geidagikea
      241 arrdeigavg kavegikamv arkaaeeaev krqadeaaaa erkrtmlela dgferavggi
      301 vgmvsssate lqataqtmta sasqtasqst tvaaaaeeas anvqtvaaaa eelgtsvqei
      361 grqvlgsadl aqtavgeade tqhlvqalsq aatrigdmvg lisniagqtn llalnatiea
      421 arageagrgf avvaaevkel aqqtaratee isqqigqiqg vtgqavsaid viaarirein
      481 gvattiaaav eeqgaatqei vrnvsqaatg teqvtsnigg vakaseetga aaaqvlgaag
      541 alsrqsehlg aevsrflgkv raa
//
LOCUS       WP_010687558             152 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Methylobacterium mesophilicum].
ACCESSION   WP_010687558
VERSION     WP_010687558.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 152)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..152
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /calculated_mol_wt=17510
     Region          14..143
                     /region_name="NUDIX_DIPP2_like_Nudt4"
                     /note="diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase
                     type 2 and similar proteins; cd04666"
                     /db_xref="CDD:467551"
ORIGIN      
        1 mkkllrkaqa kplkqvaalp frvgadgrle vllitsrdtg rwiipkgwpm igrkahraae
       61 reayeeaglq griaaspvgr yryekrldhg lalpckvrvf plrvevqher wperhqrtlr
      121 wfrpeeaarl vhedelqrll kgfaapdrdg ra
//
LOCUS       WP_010687650             132 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010687650
VERSION     WP_010687650.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..132
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13758
     Region          14..109
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 maqgsdrrri gdvvlrgllt avflaaagmk faavsfeveg farfgyplwf myvvgalqll
       61 gavllwtrgc valgagllav lmvgavgshl lagdpalmpl pafvllills giayarrael
      121 lqpsagaemr ra
//
LOCUS       WP_010687564             444 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Methylobacterium mesophilicum].
ACCESSION   WP_010687564
VERSION     WP_010687564.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..444
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47450
     Region          24..427
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(37..38,41..42,45,77,127..128,130..132,135,155,
                     158..159,162,261,264..265,268..270,273,300,304,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtglatgspd eaalersamr rigwrlvpfl ilayfvsfld rvnvgfaaiq mnhdvglsat
       61 vfgwgagiff lgyflmeips nlmlerfgar lwiarimatw glisaamalv qgpwsfiglr
      121 fllglaeagf fpgvilylty wfpsayrari igvfmisipi ssflgspisg allnvtgfgl
      181 agwqwlfile glpavllava vlwllpdgpr daawlppaer dwlerqlqae aarntrrgqp
      241 akpplreils drrlllfaai yfgstassyg lsfwtpqivk sfglgnvetg llnsipygfa
      301 svamilwgrh sdktaerrwh lalsflvlal glaggtvltg lgpvvaaltv aavgvymlkg
      361 pfwalateqm ppataaasia ainavgnlgg flgpyligai kdgtgsftls lvplvlfali
      421 saglslvpgr tprpdpgapr psta
//
LOCUS       WP_010687763             398 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Leuconostoc gelidum].
ACCESSION   WP_010687763
VERSION     WP_010687763.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc gelidum
  ORGANISM  Leuconostoc gelidum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc; Leuconostoc gelidum group.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Leuconostoc gelidum"
                     /db_xref="taxon:1244"
     Protein         1..398
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41514
     Region          1..393
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mntgdlawvl issalvwlmt pglalfyggl gekrnllhtm fvpiliigia tlvwfvvgys
       61 lafggsgnvi gnfnhmfmtn vsftkstknl tipdgafalf qgmfpiitaa iitgsvigrv
      121 rikamivfit lwlifiyspl ahmvwgggll aqlgaidfag gtvvhissgv tglvlalmig
      181 hrhhdkhipv rpsyvligga llwvgwfgfn sgsalaangt avlalvntwl asavsvltwg
      241 iaeykrhgra tlagitsggv aglvaitpaa gfvapwaavi mglvagfigf agitfvknsf
      301 gyddtldafg ihgiggavga iltavfadks iggvagving dvsllwkqlv ailftiafaa
      361 igtfilakit efiaaplrlt aseeaqgydn ilhdltle
//
LOCUS       WP_010687782             626 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Leuconostoc gelidum].
ACCESSION   WP_010687782
VERSION     WP_010687782.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc gelidum
  ORGANISM  Leuconostoc gelidum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc; Leuconostoc gelidum group.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Leuconostoc gelidum"
                     /db_xref="taxon:1244"
     Protein         1..626
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70448
     Region          6..528
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          556..622
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mkqfrvdnlk stygekvlfn disflmtegd rigligvngs gktsllnais gvnladsgki
       61 fkqndysigy ltqnptlddn alvmdailsg dqpvfktirq yqyalqqfge qptnikvaqn
      121 fedaqnamdr deawtteaqv kailtqlhmp dlqrqigels ggqrkrvgla qilieapdll
      181 ildeptnhld fdsiawleky lanykgvvla vthdryflda vttrifelsf gdlyeykgny
      241 qdymigksqr veqskvadhk qqqlykqela wmrksarart tkqtarenaf selesqmgnl
      301 kldddvavnl gqqrlgkkvi vidnasikfd dkiilknfnl riaagdrigi tgengagkst
      361 flnaiagrlp vtsgvielge tvkmayytqs teeipddkrv iaylsdvaes vtdkngnqvs
      421 vselleqflf ppfmhgtlir klsggekrrl yllklllqqp nvllldeptn dldigtltvl
      481 edflsgfsga vitvshdryf ldkianqlym fqgqgvvery dglfsqylie haddrlkvse
      541 kisvskskpv tiqkkkltyn ekkewetied diakletrlg aipddmakng tdyvklgdlq
      601 kesdkleael dkkmdrweyl sdivag
//
LOCUS       WP_010687801             483 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar porter family MFS transporter [Leuconostoc gelidum].
ACCESSION   WP_010687801
VERSION     WP_010687801.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc gelidum
  ORGANISM  Leuconostoc gelidum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc; Leuconostoc gelidum group.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Leuconostoc gelidum"
                     /db_xref="taxon:1244"
     Protein         1..483
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51890
     Region          11..450
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(23,143,146,150,265..266,270..271,274..275,366,
                     370..371,375,398..399,402)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 mnherhlstn fvyffgalgg llfgydtgvi sgamlfigke lgiksgsfqd gfitasvllg
       61 aiigaavigp lsdrlgrkkl lliasiiflt galgsgigin ytilvvsrvi lgiavgaasa
      121 liptylaels padkrggigt lfqlmimtgi ffayvsnewl spngflglke nvgwhwmlgl
      181 aaipaallff gglrlpespr flvrngklde akrvlsqmnp naklveeemh diqlqanips
      241 ggfkelfgvm arpvlimalg laifqqvmgc ntvlyyapki fisagfsehf alqshivigl
      301 fnvvvtaiav kimdkidrkk mltygaigmg vslllmstam lvlqagngnl gswvcvislt
      361 lyiaffsatw gpamwvmige afplnirglg nsfgavinwt anfavsqtfp mlliaftpan
      421 avnsegkgia klfliygalc fvaiwfiakf tietrnrsle sieaglrska hakmpynhks
      481 sll
//
LOCUS       WP_010687802             346 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leuconostoc gelidum].
ACCESSION   WP_010687802
VERSION     WP_010687802.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc gelidum
  ORGANISM  Leuconostoc gelidum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc; Leuconostoc gelidum group.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Leuconostoc gelidum"
                     /db_xref="taxon:1244"
     Protein         1..346
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38054
     Region          2..339
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mevkfnhvtl typngievlh dmdfdiddgq lvallgpsgg gksttlnlis gllsattgni
       61 yfgdkdvtkq dalergvgmv fqnyalyphm tvldniifpm kmakidkatr kqraldlakl
      121 vrvddqitkk psdlsggqqq rvaiaralak spnillldep lsnldarlrv emreeirriq
      181 ketgvttifv thdqseamhv adkimvlndg riqqydnpqs lyenpnnqfv anfigepaln
      241 visahqlgte vtqlfdgnva tigiraealt nevkepaikm qavvhevlsf grdrqatisv
      301 gehqliatdv ttsalidqem tlfaalsgvy afdkdgqrlp lrgera
//
LOCUS       WP_010687814             184 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leuconostoc gelidum].
ACCESSION   WP_010687814
VERSION     WP_010687814.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc gelidum
  ORGANISM  Leuconostoc gelidum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc; Leuconostoc gelidum group.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12807001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Leuconostoc gelidum"
                     /db_xref="taxon:1244"
     Protein         1..184
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=20504
     Region          2..68
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          7..172
                     /region_name="PRK09943"
                     /note="HTH-type transcriptional regulator PuuR"
                     /db_xref="CDD:182158"
ORIGIN      
        1 migklvgenl kkvrieknmt ldnvaemtgv skptlhniet gktspsidnl wkissglgip
       61 inyffskagi dfelvtqsdl hmidtenigv tiqttfntsv ndnfetfkis lssqaeryse
      121 phvnntieml ivtrgaltiv venvshmihv gelakfnaqv ghqyinqesd dcefycimly
      181 entl
//
LOCUS       WP_010687966             273 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Leuconostoc gelidum].
ACCESSION   WP_010687966
VERSION     WP_010687966.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc gelidum
  ORGANISM  Leuconostoc gelidum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc; Leuconostoc gelidum group.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 273)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Leuconostoc gelidum"
                     /db_xref="taxon:1244"
     Protein         1..273
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31153
     Region          4..264
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mpkskkqrql fylmpyglwl llfviaplil llfqslttqn gqftlhnyal yfssgtyllm
       61 tfnsvwyall itiitlvisy ptayllnqlk qkqfwlllvi lptwinlllk tyafigllsk
      121 tgtvnnfmsl fgivpqqllf snwsfllvaa yieipfmilp ifnslaeinp rleqasrdlg
      181 anrwqtlrrv implsmpgik agiqavfips lslfmitrli ggnrvitlgt aieehflvtq
      241 nwqlgstigi ilivamvitm iftrdrkhsr krg
//
LOCUS       WP_010687967             275 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Leuconostoc gelidum].
ACCESSION   WP_010687967
VERSION     WP_010687967.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc gelidum
  ORGANISM  Leuconostoc gelidum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc; Leuconostoc gelidum group.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Leuconostoc gelidum"
                     /db_xref="taxon:1244"
     Protein         1..275
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30151
     Region          1..261
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 msrkfklgnl ylgsvfvlly lpilflivys fnagdvmqgw agfslkhyse lfsdtrilei
       61 vvstfliall ssllasiigt agalyiynlk htvvknifls lnnillvspd viigasflil
      121 ftvmgfalgf tsvllahiaf sipivvlmvl prlqemnqsi vasakdlgan nwqmisrvil
      181 pvispgilag ffmaftysld dfavtffvtg ngfttlsvei ysrarqgvsl einalstmmf
      241 vvslllvlfy yvistravkn kkrstrlvlp asegl
//
LOCUS       WP_010688032             190 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Ligilactobacillus animalis].
ACCESSION   WP_010688032
VERSION     WP_010688032.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..190
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=20903
     Region          15..190
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 meflqldtgk lissaviktn lgeitlalfp eqapktvenf vtlakngyyd gvifhrvisd
       61 fmiqtgdptg tgmggesiwg eafedefsee lynlrgavsm anagpntngs qffivqnknm
      121 pkriikqltt ypkeivqayr qggtpwldgr htvfgqvisg mevvdkiaka ktgwgdkpkk
      181 eiviknieil
//
LOCUS       WP_010688056             234 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Ligilactobacillus
            animalis].
ACCESSION   WP_010688056
VERSION     WP_010688056.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..234
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=26934
     Region          132..226
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mnlktlgsya wrtikfillg lclilpqqvf slphilpqnf splatniltw gllllgyalv
       61 ivifnwqfkk dqpntdkifq klsnqdinai itgfitlfii kiiygmfmsq fgqtqndqal
      121 qqmfklstna almmflmtai faplceellf rgifmryffp kntvlaiffs glvfgmlhfh
      181 lgdifwtlll yctlgwvlay yykktgkllv simihflnni lpalfmlfsa lftk
//
LOCUS       WP_010688058             286 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GRP family sugar transporter [Ligilactobacillus].
ACCESSION   WP_010688058
VERSION     WP_010688058.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..286
                     /product="GRP family sugar transporter"
                     /calculated_mol_wt=30049
     Region          3..286
                     /region_name="GlcU"
                     /note="Glucose uptake protein GlcU [Carbohydrate transport
                     and metabolism]; COG4975"
                     /db_xref="CDD:444000"
ORIGIN      
        1 mwialipala wgsiglisgk lggnanqqtl gmtwgallfa ivmtvvapgn flannnwqlw
       61 vagilsglfw slgqnqqfha mkavgisktv pistgaqlvt nalagiflfh ewtttrqlsl
      121 gslalvilvv gavltalrdk sansseqned wkkgttalvl stagylgytv vvnllkvdaq
      181 amvlpqalgm vagasmfalg kdafkkesfk niitglvwgt gnlcmfqata miglavsfsl
      241 sqtgivistf gsilllgehk tkkemvyvtv gslmviiggv mlgllk
//
LOCUS       WP_010688109             402 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Ligilactobacillus animalis].
ACCESSION   WP_010688109
VERSION     WP_010688109.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..402
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=43618
     Region          1..388
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mkkvvvlgag yaglqtvhkl qknvkgkaki ilvdkddyhy ettelhevas gtqsalkity
       61 piadivdpav tefiqdevvk ldatkkqvql kqhgmldydy cvlalgfvse tfgikgaken
      121 alemtnikqs laiydhilas mekyketkdk rylqlvvcga gftgielaga laegrpeyak
      181 vagvapsevk itvveaatrl lpmfseklad ygvklveslg iellcgakis evapgeviye
      241 kdgqtnslka etiiwttgvs gspvvgesnl qerrgrvvvt dnltdpnfdd lyilgdvaav
      301 mdkesgrpyp ttaqiatema vyaakdlesq ingnghlstp fvykskgtva svgnthgfgv
      361 igkleikgyp asmmkkmimn kslfeiggfk efiakgrfdl yh
//
LOCUS       WP_010688121             185 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Ligilactobacillus].
ACCESSION   WP_010688121
VERSION     WP_010688121.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..185
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20945
     Region          17..185
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 malivlvviv lllavvyitl ynglqkakvy teeswsqidv qlkrrndlip nlvettkgya
       61 kheketfaev vklrnqlvai pdgdhqakme vsnqlsdtlr sifalsesyp dlkanqeftk
      121 lmeeltnten kiaysrqlfn ssaaafnqkl ltfpsnliak ihhftkvdyl svpeeqkeap
      181 kvsfd
//
LOCUS       WP_010688133             174 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Ligilactobacillus].
ACCESSION   WP_010688133
VERSION     WP_010688133.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..174
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20186
     Region          25..147
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msksqvrkkd alaqallall hheavekitv dqlcreanvh rstfyryfqd kydllhyvfq
       61 tiwleqiden nvvdsmiemi vhdkdifrni sinnsnnsly almidmvaeq ileaslnnrl
      121 hnilwieetv lnatdqklaa dmiagafltl lfkwvdsnyq msstelsdfi khlh
//
LOCUS       WP_010688137             203 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Ligilactobacillus].
ACCESSION   WP_010688137
VERSION     WP_010688137.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..203
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21792
     Region          1..203
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mdttvlteli gqygylgial lialenifpp ipsevvltft gfltltagln vlgaitaati
       61 gavlgavily avghflsver lekilngkig qtlrfkaedl nkatnffqkn gvlalffgrf
      121 vpvvrslisv pagmthykft sfiilttlgt liwntvliiv grmagsawpq ivamietysl
      181 atvivlalaf vgggfyffnr kka
//
LOCUS       WP_010688148             484 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Ligilactobacillus animalis].
ACCESSION   WP_010688148
VERSION     WP_010688148.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..484
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54754
     Region          1..432
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mntlnqnsln qkkytpwlvl tlldfvtiis fenifypfqn qglsvviswi fmlfvyvipy
       61 elivsqlglt fdqqagglas wirrgtgsdl fgyatswmyw vqtipylvdv snsiivsfsw
      121 iilgdatlss hmstftfgll tfviilafil lenifknale ilsligggam fimsmlfvlm
      181 tgyalthgah iatqpfdwsa fkpnfslhyf sttgllifam sgaelaapyi srmknpkrdf
      241 prsmwmlalm tgaltifgtl alavffdann ipndfkmngp yyafkllsqq lgwdnslmyv
      301 favvqsffml aqlavlidaa srvfagdvnq kymptwltkt nkngrpvhsy tltagialvl
      361 lllsgtlpdi nsiynwllnl ngivspyktc lvfvafiavr wqqdkfssdy ifiknrtgal
      421 lvgfwcflft fvcatmgfip qnahfgtkqf thelmmnfff vflifgmgvi lpflrkleik
      481 rkqk
//
LOCUS       WP_010688150             207 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Ligilactobacillus animalis].
ACCESSION   WP_010688150
VERSION     WP_010688150.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18096355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..207
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24093
     Region          2..177
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          123..191
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 meidlrlmra sdydeilkmv ittwdyrswv pkdlvepmae yflsdllqks dyivvvtvdg
       61 kpagicagdv ldytkiqrfc lrkktaalga ilkqtepdsi fekyiqtmal dqelllqskr
      121 efegslnlll vngkyrglgl gkklynnfce ylqkngvrsf ylytddssdy gfyehnglek
      181 lvekrfywde gneetaetyy lygrdfn
//
LOCUS       WP_010688258             375 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Ligilactobacillus animalis].
ACCESSION   WP_010688258
VERSION     WP_010688258.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..375
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43445
     Region          58..367
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msrivkrdkg yfaeftkgag kkryrkqktf qkksdaqdwl vemehsylqg svspradmsf
       61 aeyykqwitm ykspivsant idgyrsshsr issnrlgqik lrdltrddiq iyfnnlnksh
      121 etarkdlnri raclrdafnd giiqrnpsag siniiadpnl tkgnnrkfma ikdfrnlqky
      181 llnssynlld vnrvilfvis qtamrvgecl alkeddidei nctlrvdesw dshhkvlkqp
      241 ktqnsirvlp vsrevmnklt ewvryhrkel fkrgihnknk liflnykskl pmaasintty
      301 krlqqnlglt gvfsthtmrh tiasmmlnsg eislvyisrf lghsnisitq kyyidllpdq
      361 vtnedkkvvk llafa
//
LOCUS       WP_010688295             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Ligilactobacillus
            animalis].
ACCESSION   WP_010688295
VERSION     WP_010688295.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..272
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29789
     Region          1..269
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mrlsekihqn yfsltpaekk vadhflwagt diiyetmndi kqktnvgdat ivrlchklgy
       61 dgfsdlkvev akedyssnvh qtahspyasi etaltktist tlnklnkdvl teaislldqa
      121 qriyifgvgg salssnales mllrvgvraq avtdphyqaq laavtnssdl iiafsltgrt
      181 kdtleplkla knnqakviai ttypaspiat qadlvlqtav ddflnggslv grlsqlligd
      241 vlvyeyeklh aketitarek vvrailnkrk qe
//
LOCUS       WP_010688383             266 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Ligilactobacillus animalis].
ACCESSION   WP_010688383
VERSION     WP_010688383.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..266
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29690
     Region          68..252
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mepknfrnis tgvkaikiia fgewhafkqn kglllsmame plitygllvl slntslgqvk
       61 idnvtvlykq yaltgiltff mttqmsqamy ratidkeygl lalkflngiq pwhylvgmnc
      121 fpiigllfqc fillllglvs egiykvslfl lailvvivsl gfwaslgill stkittyekr
      181 dvvmtlifsp vsyaaptlyv fsddlplivr iltminplty qlqairtvaf gsfdvtvlii
      241 dflltlgmmf iaqcvlckip lklstr
//
LOCUS       WP_010688388             250 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator
            [Ligilactobacillus animalis].
ACCESSION   WP_010688388
VERSION     WP_010688388.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..250
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28192
     Region          1..243
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlkkerllki leivdqqeiv tvnelintlg vsdmtirrdl deldksgkli rlhggaqkia
       61 nieevelsrn qkkeihlvek qevaklaaqk ikpgdtiyig agttleliln yvekpetlrv
      121 vtnslpvfea wqkteaelil vggnyrrhsg efiggltikl ledlkftkaf vgvngvnndn
      181 mmaanteegq aealglnnaq eryvvmdkyk fnrndfynfy slynvdallt nssvapdtle
      241 hyqtytkien
//
LOCUS       WP_010688394             255 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Ligilactobacillus animalis].
ACCESSION   WP_010688394
VERSION     WP_010688394.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..255
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27775
     Region          3..251
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgrvialanq ksgvgkttts vnlaasladl gqkvllidmd aqgnatsgig idkgqikqdi
       61 ydvlvnevel edvilhtkrd kldvvpatir lsgaeielas qfarekrlad alvlirdeyd
      121 filldcppsl glltinaftt cdsilipvqs eyyaleglnq lvntiklvqk hfnptlkieg
      181 vlmtmldsrt nlgnqvvaev knffgdtvyq tviprnikls eapsygmaiv dydqrskgal
      241 dyealakevl atyak
//
LOCUS       WP_010688428             720 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Ligilactobacillus
            animalis].
ACCESSION   WP_010688428
VERSION     WP_010688428.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 720)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 720)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 720)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..720
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80132
     Region          1..>69
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          78..714
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mlcqncqqnq atlhlttnin grqtsidlcp ncyralknqs qlppsldgif qdsfgsdpfa
       61 dffkeinqqn qqrhtpaqep ptkagdngdn gsildkygld ltaqakagqi dpvigrdrei
      121 krvteilnrr tknnpvltge agvgktavve glaqkivdgd vpqkllnkkv irldvvslvq
      181 gtgirgqfeq rmqelmdelk qkqdiilfid eiheivgagn aeggmdagnv lkpalargef
      241 qlvgattlne frtiekdaal arrlqpvqve epskeealai lhglrakyes yhqvaytdea
      301 lesaiqlstr yiqdrylpdk aidlldeags rknlalqafd psevkakitq aqankkaald
      361 qedyekaafy rdqvakleeh ltakpqakse vtaqdmekiv eemtsipvge lkqkeqaqlq
      421 tlaqtlkqnv igqdravdkv arsirrnrig fnksgrpigs flfvgptgvg kteaakqlal
      481 elfgtteami rfdmseymek fsvskligsp pgyvgyeeag qlteqvrrhp yslilldeie
      541 kahpdvmhmf lqilddgrlt dsqgktvsfk dtiiimtsna gsgdpivnvg fgttestpns
      601 vvdkltkyfk peflnrfddi iefnaltken ldqivelmle kvdqtlqeng mslkvstkar
      661 qklvelgydp kmgarplrrt iqdqiedkvt dfyldhpqvk dfyadltddt iviseanvte
//
LOCUS       WP_010688434             242 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ligilactobacillus animalis].
ACCESSION   WP_010688434
VERSION     WP_010688434.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..242
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27016
     Region          1..227
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 makieikyit ksvpllldkk ekhdvknfwe lrgidlavnd geavgvigdn gsgkvalmki
       61 lgqkdkqttg fittkakrsy asctsldpek tglenirqai aqadidefkg nhytngiinf
      121 seigellyrp vkeystgmya rlalsivlfi dpelvildev lspvdrnfyf kavqkiqqlk
      181 dtgvtfivse vrpviietlc eraallqfgv lqdfgattev vrqyeyacew ianltlpekm
      241 tt
//
LOCUS       WP_010688435             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GtrA family protein [Ligilactobacillus].
ACCESSION   WP_010688435
VERSION     WP_010688435.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..145
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16846
     Region          2..136
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mkklyrkyqn ffsytffgtl asainvilfh ilekdlgfny llanclayiv aiiftfvtnk
       61 hwvfaskntt lkqtlqefvs fcnvrlfsfi ldlglmftgv qllalykdla kildqlicgi
      121 lnyffskwfi fkttakilpk evdee
//
LOCUS       WP_010688474             353 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Ligilactobacillus].
ACCESSION   WP_010688474
VERSION     WP_010688474.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..353
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38641
     Region          128..353
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mylalkeikh ekirysliia mvvlisylvf iltslalgla hentyaiksw dfekialnrd
       61 advnlrqsll tkeqinelkl tkneavigqa piivkekgrq klsatfvgle rsqfvyqqlk
      121 assghlpktk qevvvddsfk ndgyklgdkv yfnsqttpyt itgfiknakl nvlpvvygsl
      181 tawselknvg pnfaasgvls kdpdfkvtdp qlqvatqqal idklpgysaq nstftfmiaf
      241 lmiislivia vflyiitiqk lpnyavlrvq giankvliqn tigqsfilvv tgliigallt
      301 latalvipan vpmtfdlkfl slvsvglvlt svlgslipvr ailridpaqa igg
//
LOCUS       WP_010688507             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Ligilactobacillus animalis].
ACCESSION   WP_010688507
VERSION     WP_010688507.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10150691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..397
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44159
     Region          4..379
                     /region_name="MFS_HP1165"
                     /note="HP1165 family MFS efflux transporter; NF040872"
                     /db_xref="CDD:468809"
ORIGIN      
        1 mlqlhkniki fylatilttl aaslphavlt vllfakglsl tqimlvqaty slvilvseyp
       61 sglladlysk kvlflwakvf ligmfllvwl gesfqtmlla wacyglamal esgtldaqli
      121 nelkhqdqsh lvakfisntn rldliglllg gtigswlyys lgikfylvsv sltlvaflav
      181 rygyleantd isqqnlkqsl vaqmvtgfse lkhsrqlrlm ialtiagqff fqahyqlwqa
      241 lflkqgfdke qfyiyyvifq lislgayslp vkldtstikr wylasmlglv gagvflaftv
      301 kmsfllsylv lvfiftlfey fsnvlfsktv spthisslts lrsscgrlas laslllssll
      361 ltylsvksvv llnfglaiia slgviflalk nntvhsk
//
LOCUS       WP_010688485             346 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methionine ABC transporter ATP-binding protein
            [Ligilactobacillus].
ACCESSION   WP_010688485
VERSION     WP_010688485.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..346
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38089
     Region          1..343
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 miefkqvskt fatasgqvda vknvdltina gevygivgfs gagkstlvrm lngletptsg
       61 eviingkrid nlkgkelrdq rkkigiifqh fnllwsrtvl eniefpleli gvakeerhkk
      121 akhladlvgl gerinaypsq lsggqkqrvg iaralatdpd ilisdeatsa ldpqttdevl
      181 dlldeinekl nltiviithe mhvirrladk vavmengqvi eegpvsevft hpkeeltkrf
      241 vsaevdtkqt tdvkqvvanl leknpqgklv elkfhgqqve rpvinelskn fpeleisile
      301 gsihqladkg tigslfvqlv gpveqikeal tlleklevea kviehg
//
LOCUS       WP_010688562             151 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Ligilactobacillus].
ACCESSION   WP_010688562
VERSION     WP_010688562.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..151
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16592
     Region          8..149
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 melikqeyrn ilvpvdgskt aekalerate ialrnkahld ilnvidlkqf svsfggmvda
       61 ngdavyqafe dvegylntlv ervkkqgled vtaharfgsp raviarefpd dhendliimg
      121 ptglnpverl lvgavtdyvt rvakcdviia r
//
LOCUS       WP_010688567             149 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Ligilactobacillus animalis].
ACCESSION   WP_010688567
VERSION     WP_010688567.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..149
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15906
     Region          4..147
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mkhyktilvg ldgstnslsa lekagelaql mdaklvlvtv vkpelqvgfg gpglevntls
       61 akqleekqaq aqkmlteyqa klpgqvkqqa vvvlgdpkvm lsetlpqkyq aelvivgatg
      121 lnkldrfilg stasyvvrnt kadtlvvne
//
LOCUS       WP_010688604             443 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Ligilactobacillus animalis].
ACCESSION   WP_010688604
VERSION     WP_010688604.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..443
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50433
     Region          4..379
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnktfkdfnl kpflnealte igfqaptevq krlipvikkg ksvvgqsqtg sgkthtfllp
       61 ifnaidpavh avqavittps relayqiyga akqlakhset eilvqnyvgg tdklrqiekl
      121 khhqpqivig tpgrildlmr snaldvhnah ylvvdeadmt ldlgflkety aiasalpkdl
      181 qmlvfsatip qklkpflqky mndpvvevve nktvisptid nwllstkgrd kkqliyqllt
      241 mgepylalvf antkertdel ttylrhqglk vakihggiqp rerkrlmrei qnleyqyvva
      301 tdlaargidi egvshvindd lpedleffvh rvgrtgrnnl kgiaitlyvp seeaqieele
      361 kmgvtfvpka lkngeivdsy drnrrqkrrt rqesldpkmi gmvkkakkkr kpgyknkikw
      421 alkrdaqkkr kiarrqerkn qrs
//
LOCUS       WP_010688629             246 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Ligilactobacillus
            animalis].
ACCESSION   WP_010688629
VERSION     WP_010688629.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..246
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26656
     Region          6..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 madlkvdvtn lkknygsnqv lkgidfkvan nevvvligps gsgkstllrc lnkleeptsg
       61 sividghdis dpktnidkar enigmvfqhf nlfnnlsvge nimlapvelg kankdeamtt
      121 akqlletvgl adkfdampas lsggqkqrva iaralamnpd imlfdeptsa ldpemvgdvl
      181 evmkdlakdg mtmvvvthem gfakevadrv vfmaeghvve egrpeaifed pqnertkafl
      241 ekvini
//
LOCUS       WP_010688697             422 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A [Ligilactobacillus
            animalis].
ACCESSION   WP_010688697
VERSION     WP_010688697.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..422
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=46243
     Region          1..421
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mkplayrmrp kkledivgqq hlvapgkila rmvsakllss milygppgtg ktsiasaiag
       61 stkyafrmln aatdskkele mvaeeakisg tvillldeih rltkpkqdfl lphlekgsii
      121 ligattenpy itinpairsr tqifevkplt eadigqaidr altdkenglg eqnvvltgea
      181 rlhltrvthg dlrsalngle lavmstepdd sgvltidlpt ieecvqrkal vqdkdgdahy
      241 dvisafqksi rgsdtdaalh ymarlleagd lpsvirrllt iayediglan pnacahavqa
      301 itaaekiglp eariplaqav ielclspksn saimaidaal advragnygd vpdhlrdahy
      361 qgakklgrgi gykyphdyph gwvkqqylpd klktehyyap kensryekal qeqyerlnkf
      421 ks
//
LOCUS       WP_010688731             527 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Treponema denticola].
ACCESSION   WP_010688731
VERSION     WP_010688731.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 527)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..527
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59624
     Region          54..517
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mnkklmilst vllvifgssf iscngknksn iketkkssad klmvlpigsd psiinplyan
       61 drvsltishv lydplytikn gkilynglae klenssdfla ytlklrhdvt whdgkpfsad
      121 dliytlsvim dekqnakgrf alifgdkvie yrklddytve fklpqvnmsf vqnlssikpi
      181 pkhiymgqan iaesknnanp igngcfkfke qrigetyqve rnnnyygdka lldgivyrvi
      241 pnsnavmval engeinaayi kanqiekyks nenlqivtfs egmvnniffr isnpkisdvr
      301 lrqaisyaid kdkllkgayg gpeyatiafs pfaqetqyyt devekyqyni dkakellkea
      361 kigsislrlm ytsgnpaqek ealliqemlk kinitiellp lergsfiekl lnvknqdfel
      421 alngyvfgdn pdtygalftk nspenfsgyl npeidklfaa avtetnsskr enmykeiqqi
      481 lvkdavqist aymksivvvn kqfknlkean papihmfdyf nkiskde
//
LOCUS       WP_010688738             236 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cell division protein FtsQ/DivIB [Ligilactobacillus].
ACCESSION   WP_010688738
VERSION     WP_010688738.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..236
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=26805
     Region          3..228
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mirlteqrkk alrqqalfpl vffsimtllt lclilpisrv rsvtvdsndk qlrvavikas
       61 glhyyeslfn vwfnaskien kiqnkvglve qatlryvnvn nvvidvkeep qvgyiyrnnk
      121 yykigttgqp lsegtpsvkg sypvfyafkd kaklklavtk vqelptelkk svseihydps
      181 kvnpnrikly mndgneviad lstltkkmey ypqiatkmdq kgivdlevga fsypkn
//
LOCUS       WP_010688750             180 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Ligilactobacillus].
ACCESSION   WP_010688750
VERSION     WP_010688750.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 180)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..180
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20305
     Region          41..177
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mdfeekvtnv ehlfdgkvid ldretvmlpn gkealreivr hhgavgviai tpqdkmvfik
       61 qwrsplgqvt leipagkiep deqnspleta trelneeary taenlelvmp fytspgfade
      121 kiylyhasgl spvttelpqd edeflekvel tlpealkamq eglicdskti mavmfwqlmn
//
LOCUS       WP_010688795             372 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Treponema denticola].
ACCESSION   WP_010688795
VERSION     WP_010688795.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..372
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41559
     Region          8..367
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 myqenkhrlq tisffvllag mlilvgklfl pyasvllwsa viyvlvrply nkilsrmnke
       61 kktfpikkrl lagsfaiitv lvvagvlffv vikifgqgki lvqniqsfle ninnsesgfs
      121 ktdiaaivnr lsmgtvdisn ldlqkeilsl lssssdkilr yatslvknag sfflslvffa
      181 falyffyvdg aylfsllkha ipidnetsnk lfskigeitt nlfkglflvs fyqglasfiv
      241 ylifgvqsal llailtffst flplvgcgli wfpvgvglcf tdglvkglif lvvagsiisf
      301 mdnflrpffl kdrikihpll iffsmlggvs mfsfdgiilg pmivilffti ldmaldieek
      361 kendedsfeh li
//
LOCUS       WP_010688796             395 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: elongation factor Tu [Ligilactobacillus].
ACCESSION   WP_010688796
VERSION     WP_010688796.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     gene            1..395
                     /gene="tuf"
     Protein         1..395
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43281
     Region          1..393
                     /region_name="TufA"
                     /note="Translation elongation factor EF-Tu, a GTPase
                     [Translation, ribosomal structure and biogenesis];
                     COG0050"
                     /db_xref="CDD:439820"
ORIGIN      
        1 makehyertk phvnigtigh vdhgkttlta aitkvlsekg laqaedyasi daapeererg
       61 itintahvey etegrhyahi dapghadyvk nmitgaaqmd gailvvaatd gpmpqtrehi
      121 llarqvgvey ivvflnkcdl vddeelldlv emevrdllse ydfpgddipv irgsalkale
      181 ddedakkkil elmdtvdeyi ptperptdkp flmpvedvft itgrgtvasg ridrgivkvg
      241 deveivglkd dvlkttvtgv emfrktldeg eagdnigall rgvdrtqier gqvlakpgsi
      301 qthkkfkgev yvltkeeggr htpffsnyrp qfyfhttdvt gvielpegve mvmpgdnvtf
      361 sveliapvai ekglkftvre ggrtvgagvv seidd
//
LOCUS       WP_010688933             377 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Treponema denticola].
ACCESSION   WP_010688933
VERSION     WP_010688933.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..377
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43471
     Region          33..367
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mdikdfksgs lkqgykyqyf mpekinhdfs wedpsintll ekasfhlgal nsfsslvpda
       61 dmfiimhifk eavisnrieg trtnieealn eqdnldpekr ndwqevhnyv kamnnaiqel
      121 enlplsnrli knthkillst grgehkspge frisqnwigg ttlsdavfip paheelpell
      181 sdlelflnnt niniphliri aiahyqfeti hpfldgngri grllislylv hskvlqkpll
      241 ylsdffeknk tlyydnltfv rtkndmsqwi kyflegvsqt aensaqtlkk iielktdlek
      301 nkllslgkrt ktaneflyfl fhspvitsta lqkemkitak tanslidafi glnilkertg
      361 ysrnrifvfd kyvelfm
//
LOCUS       WP_010688975             549 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010688975
VERSION     WP_010688975.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 549)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..549
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62187
     Region          1..542
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mpeiilqnlt krwgkfygtd nlnltienns fitllgpsgc gktttlrmia gletptsgki
       61 iidgetvfds ekginipank rkvgflfqny alwpnmtvye nisfglknik elmplcdfei
      121 kriddlkkil necgkaveii idsqtkdkkk gnrldektal iklidnfiis eytaktvlsy
      181 glekaenree kvrsiisgld ekrasllekh kkngfsvngn yelvdekgev ikkirklene
      241 eidlivrrvs rivkigmfmd rypnelsggq qqrvaiartl apgpkvlfmd eplsnldakl
      301 rlemrselqr lhldtkstfi yathdqleam tlatkiclmd ngllqqydap ldiyekpvnl
      361 ftadfignps infieaaget saegdfnlnc leglqfkfkp aqkidykewl lkteaeikkq
      421 rdeeaertkn aekenkilpf kyhiakadea efdlnspapt ekdfiigvrp efikihengk
      481 ltgsiyssmp tgmettvkik vgnllltgvv flnitykige kikfdiegdr imlfsslnqr
      541 lislgclek
//
LOCUS       WP_010688974             241 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [Ligilactobacillus].
ACCESSION   WP_010688974
VERSION     WP_010688974.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..241
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=27119
     Region          1..228
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 maerlqkvma nagvasrras ekmildgrvr vngkvikelg qkvdgndvie vdghlieree
       61 kvyylfykpr gvisaakddk grkvvtdyft dyservypvg rldydtsgll lltndgelan
      121 rlmhprykvn ktyvakvkgi vqndelkqlr vgvrlkdgkk sarakakils ldkksdtsiv
      181 sltihegrnh qvknmlqavg hpvkklkret ygfltlaglt sgqyreltre evkalyelgn
      241 k
//
LOCUS       WP_010689012             166 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase [Ligilactobacillus animalis].
ACCESSION   WP_010689012
VERSION     WP_010689012.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..166
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19158
     Region          1..165
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(5,22,27,57,101,107,120)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(7,14,44..46,64,102..105)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 misfiwaedk ahhigyqgkl pwhlpadlaf fkkqtighpi vmgrktfasf pgllpkrqhv
       61 vlthseelkk eaqtterltv fsdltelktw lsqqseevfv iggaslfnsl qeeverlyvt
      121 kiaaefkgdt lmpeldyskf kvifqedgvv deknhyphtf yiyerk
//
LOCUS       WP_010689133             259 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 32 protein [Ligilactobacillus animalis].
ACCESSION   WP_010689133
VERSION     WP_010689133.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Yoko-o,T., Tsukahara,K., Watanabe,T., Hata-Sugi,N., Yoshimatsu,K.,
            Nagasu,T. and Jigami,Y.
  TITLE     Schizosaccharomyces pombe och1(+) encodes
            alpha-1,6-mannosyltransferase that is involved in outer chain
            elongation of N-linked oligosaccharides
  JOURNAL   FEBS Lett 489 (1), 75-80 (2001)
   PUBMED   11231017
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..259
                     /product="glycosyltransferase family 32 protein"
                     /EC_number="2.4.-.-"
                     /calculated_mol_wt=30447
     Region          1..132
                     /region_name="OCH1"
                     /note="Mannosyltransferase OCH1 or related enzyme [Cell
                     wall/membrane/envelope biogenesis]; COG3774"
                     /db_xref="CDD:442988"
ORIGIN      
        1 mipkiihycw fgqnempkqy rqyiegwkki cpdyeiiewn eenydveqva ytaqaakvgk
       61 wsfvsdylgf dvvyryggiy ldtdvellqt ldhilendaf faieenesga evapglgfga
      121 kknhpllkql rdmyndlefi kadgslntva ipvyttqlle klgfkrqdkl qklgdvtiyp
      181 ttyfapmdfl tgqitlspet isihhysalw qtptnlrhie kmrrinrrfg kkwgmrinfl
      241 wrvwwalerr ikklwgesk
//
LOCUS       WP_010689203             720 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK [Ligilactobacillus animalis].
ACCESSION   WP_010689203
VERSION     WP_010689203.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 720)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..720
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=78326
     Region          22..>240
                     /region_name="PRK08581"
                     /note="amidase domain-containing protein"
                     /db_xref="CDD:236304"
     Region          <135..>213
                     /region_name="ser_rich_anae_1"
                     /note="serine-rich protein; NF033849"
                     /db_xref="CDD:468206"
     Region          <244..717
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mehydgpafy rnngrpatka rvqtkvpakt ektptrtats nqkerlnesp rafsprqvpr
       61 slvadrvvkk rpdydklvrs lkkapedyll fegtvllgtq aidltvkrpl isdstetklp
      121 krptvssqlk tptlasdsqt tssslatses lddstsqayl asstsqlqss vsdthaqsts
      181 qanseaksvs qsqvtselts qveltsevat ksepqkmtgl kaalahessl tqsqpsvtaq
      241 pttpeyepkh yqfpplnllp apvidddpal ddwvasqvqt lnetlkafhv datvsdwtig
      301 ptvtqfeltl grgvkvnkit nlnddlklal aakdirieap ipgkssvgie ipnktsrpvm
      361 lsevlrsdkf qeasspltva lgvdlfgepq itdlqkmphg liagatgsgk svfinsllvs
      421 llykaspsev klvlidpkav emapyhdlph llapvisdak aaaaalkwlv nemeeryqrl
      481 aaagarnlea ynekakaage yglqlpyivv videladlmm aassevqdhi aritqkaraa
      541 gihllvatqr psvdvltgti knniptriaf mvssqvdsrt ildtagaerl lgrgdmlylg
      601 ngsgqptrlq gtyiedevdl vtdfvrqqgk pkyafdpdsl kkravesekq ddllprvldy
      661 ivneetists klqrvfsigy nraaaiiddl eakqyispah gakprkvflt qeglnklrsv
//
LOCUS       WP_010689209             246 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ligilactobacillus animalis].
ACCESSION   WP_010689209
VERSION     WP_010689209.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27075
     Region          3..244
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtlevenlvg gysrvpvlkd vsfevkagel vgliglngag ksttikhiig llrpqkgtit
       61 legvtlktdp kaykqkmayi petpilyeel tlrehielti maygleaksa wqraqkllel
      121 frlenkldwf panfskgmkq kvmivcafit eaklyiidep flgldplatq dlldlidqkk
      181 qagaavlmst hvlstaqeyc drfvmidqgq vtakgdlasl rtqfgdetas latiylkltg
      241 agekha
//
LOCUS       WP_010689211             142 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HIT family protein [Ligilactobacillus].
ACCESSION   WP_010689211
VERSION     WP_010689211.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..142
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15637
     Region          3..138
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mtdcifckii ageipsvtvy eddkvkafld isqatpghtl vvpkkhvadl feydeqlasd
       61 vfsrlpkiar avkasdptik glnivnnnge vayqtvfhsh ihllprysne dgfgmtfadn
      121 sadytpeklq viankiaeqi kd
//
LOCUS       WP_010689377             632 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Treponema denticola].
ACCESSION   WP_010689377
VERSION     WP_010689377.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..632
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71602
     Region          3..397
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mlnkqrkmtw rtylaygaad lygggcffiv ttfamyylvn viglhpvlag lipaigkfwd
       61 avsdpmmgyi adntpqnrfg krrvwflvsi vpialsfiii wvptgiesqa gkfifytiay
      121 iifftvstvs yipyaalsae itkdfsernk lngsrlmfsf iatllgglla qpiidafhgs
      181 mmgyfvmsiv falifalpwi plyfetwelp eeksqkksda kfiknflslf ksrscrihia
      241 myvcsygald ivmslvlfyi vdylnrgsvf iiaqgalllt mmatlpihnr iinkkghkpv
      301 yvaaliifav sivlmsfhtp qtnpvfliln mvlmgigisa nnliphqllp fladidklms
      361 genragtysa amtltrklfl glvimttigf vlsgigyknp vpsvltqkqf keaqnlavkn
      421 nenfeninky yslredgnfh lkymsrstde iitsaykkak knehanplfs ffegkdnfde
      481 ipqdvfenvl ssfdkkdfne idkkflvess ytksgevykk ieprdfytkd dlydlkelld
      541 kidfkysgig qvqkpqqkes tlkgvkisfi implfmilfg iffglkfnvs penhtiilde
      601 lnrleaggkk edadektkqi celligepyg rt
//
LOCUS       WP_010689383             721 aa            linear   BCT 01-JAN-2025
DEFINITION  vWA domain-containing protein [Treponema denticola].
ACCESSION   WP_010689383
VERSION     WP_010689383.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10076759
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..721
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=78310
     Region          28..>147
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cd00198"
                     /db_xref="CDD:238119"
     Site            order(35,106,135)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238119"
ORIGIN      
        1 mfkrvslclf lfvlftpifa qnnvktnaei vilmdtsgti lpyyedinnr vlseindkfv
       61 rkgdtvhvls fnadaryems qkinsekdms rvvsrfllly qlgkssdflt glqyarqygs
      121 nlpdtkekil iiisdgifnp pesspyknyt ddqikneigl lagsirkkgw kvyyvklpyp
      181 adavirgldg kefynpgggy agtgsgssgs qgaggsiggg stsgtsgsts sgggytggst
      241 tsgtsgstss gggyaggstt sgtsgstssg ggyaggssts gtsgtdqggs gntgtgqgsl
      301 tdvskdfkea sgaagselpk dengkftitd naedlplinf pdegleahgn klafsfevtn
      361 nsdedvelyl thividngvn iskipvdsqn tkikasekdv pirvsallpd eykegnynii
      421 mrlefaegkr vlpqvmetsl avfptsfqrl knsnviwfil lglillllli flivfftrrr
      481 gsspssnqvr yaaagsqiny qeedkryphk lseeddhasr lngfnsassn tsiysetknf
      541 agdggsiysa dnldrvasqr qddevlrrrv laasfaakep rgtymspanf fetieikrnk
      601 sgmteiyvln qnrnigrrni hvmkpgtslt lgggktdnfl iflvpfparl aqvrydgqdy
      661 hlailkpkyf pyeksnvvnn cisktvtivs dkgyhvyftf reyenptekl nsiltsikyd
      721 k
//
LOCUS       WP_010689399             355 aa            linear   BCT 01-JAN-2025
DEFINITION  MraY family glycosyltransferase [Treponema denticola].
ACCESSION   WP_010689399
VERSION     WP_010689399.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..355
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=39502
     Region          41..295
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            98..99
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            220..223
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133463"
     Site            order(271,285..288)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 mtaiqfilyi iaipcalsaf fvylailfsk khnlydktgg rkihsgnipr iggvgfgfay
       61 iisslilhfr fpelrllhln ffyialgcll ifimglwddi knwraifkll vqscaaiivl
      121 yggytfkkis fgpigffwym gpetyvitfl wiigitnain lvdgidgqag clgvsvllty
      181 aaiyysigis liiifrvlil afsvvgflff nlsrpsakif mgdcgsqilg fvlailplip
      241 spegyeaagi qfasvilmlp ifdtvaaiwr rvrekrpige gdkfhlhhkl mligfsprga
      301 lsvfmilqli inlfagmaii lqgvralvvl iglilvgllf ftlihyekek iinkk
//
LOCUS       WP_010689448             268 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Treponema denticola].
ACCESSION   WP_010689448
VERSION     WP_010689448.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..268
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31312
     Region          64..145
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 meltmydfer yiqkdqnesr aeqmwdnksk dfyertekkq kqfangfifq fikerqllka
       61 dskvldigcg tgrhlsefaa ytpyltgidi sskmlayaqe klrhipqakl ihgnwmdtft
      121 tenqfdfvfa cmtpaiasid nikrmcmisk kycilertvy ekdsieeeie qllgrklfrl
      181 phndknyvyg vwnilwlmgy cpevlvdkqv rttshsiedy mhgteyndee ktaviqllnt
      241 kaqdgiitae esvvkaiilw dtetklkg
//
LOCUS       WP_010689450             113 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Treponema denticola].
ACCESSION   WP_010689450
VERSION     WP_010689450.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..113
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13259
     Region          11..95
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mninqkskfk hltafilvil aeaprnrrdi ytellqdfpg ftidmstvyr clsslekegl
       61 vtmewelpse gaarkkyait qsgkndlyew kedieirkhn fevflqkfne rkv
//
LOCUS       WP_010689485             404 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Treponema denticola].
ACCESSION   WP_010689485
VERSION     WP_010689485.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..404
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=46174
     Region          2..402
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mqkeivktkk mvfgascias lkdgktvfvp yslpdevlei sivkehknyt egkiekilea
       61 sphrveprcp yfyvcggcnl qtaddeyqhf lrksmaleal dralglykek tvfekpslek
      121 nlfeesvfvn gpdwdyrarf qfyidedgsl slkenkssgs vkikdcpiav pairnllrsn
      181 lkeytpnsri hifsdgekif tqdnakdcev rlagkrikfn plgffqsnle mteklintif
      241 eyaeilssvl dfysgvgtfs lfaydqakei hlvehnkhal ayaqenflin ssssgivrek
      301 kengfpkify haldgknwak tkesklkfdt vfvdpprigi dkealswlcs sgtrqifyis
      361 cdpvtfardt asllvsgykl ekhflfdfyp qthhietlgi frkn
//
LOCUS       WP_010689551             302 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Ligilactobacillus animalis].
ACCESSION   WP_010689551
VERSION     WP_010689551.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34137
     Region          3..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(106..107,109..110,113,117,119..125,219..224,
                     230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mnirdfeyfh qlvkeknfsk vaqifsvsqp tvtlaikrle eefettffir drshkellvt
       61 psgyqfdahl kvilnelaia kkealrakqe kllfglppii gnyffpnivs kliatglieq
      121 letreagsqa llkllldgsl dfcllgslep ltqpalkaet faqasfkiiv skqhplaskk
      181 avyfselkde rfivhnegfi hdkvlkllaq kehfrpdiiy rtnyvhvlks mvasntgiac
      241 ltdiaispnd dfsvlellde qqpkfllsiv tratqvitpa kkqlldilhd tvynspigke
      301 ne
//
LOCUS       WP_010689510             615 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Ligilactobacillus
            animalis].
ACCESSION   WP_010689510
VERSION     WP_010689510.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11550563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..615
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=66015
     Region          12..609
                     /region_name="P-type_ATPase_HM"
                     /note="P-type heavy metal-transporting ATPase; cd02079"
                     /db_xref="CDD:319774"
     Site            order(267,269,573..574,596,600)
                     /site_type="other"
                     /note="putative HM ion binding site [ion binding]"
                     /db_xref="CDD:319774"
     Site            order(311..313,373,389..391,421,462..464,484,487,490,509,
                     512)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319774"
ORIGIN      
        1 mqkfilgkkn hitivsaili iiayvsklgf knepiaiwsl iiasvlgvip iaiqayqalk
       61 vkvvsidvlv tiavigafii knyeesaivt flflfgayle qrtlnktrsa ikeltemape
      121 valkqlknge feeveieevd vgdillvktg akipvdgtvl tgeghineas itgeavpvsk
      181 kkdsgvyagt ilengtlqit adrvgedttf gkiielveea qdskseaerf idrfskyytp
      241 avlglsfivg lisrdielai tilvlgcpga lvigvpvsnv agigngarhs vllkgsevis
      301 dfsrldtmvf dktgtltign pkvadkeiya dnvdevlayl ssvekesdhp lakavveyig
      361 dtksytvekt vvvkgggiva hveghrvavg nvalmeqenv llskkvrgdi arfeengnsl
      421 vltsvdgelk vligirdqir pgvkedlqql kklgvknlvv lsgdnqgtvd lvarelglte
      481 ahghmlpedk sayikalqer gqivafvgdg vndspslala qigiamgsgt dvaietsdvv
      541 lmnsdfsrlp yalgltkata nnmlqniiia vgvvlvllas vffsewmnms igmlvheasi
      601 lvvilnamrl lrykl
//
LOCUS       WP_010689605             245 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Treponema
            denticola].
ACCESSION   WP_010689605
VERSION     WP_010689605.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..245
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26807
     Region          1..207
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mlkveniyks fgslkvlngi sfsadkgevi aiigpsgmgk stllrcinll eepdsgsiei
       61 dgvkftagek ehqtirdlra ktamvfqnyn lfknktviqn imlpmvsakk ntkkeaella
      121 ldllnqigls dkknvypskl sggqqqrvgi aralavnpsv llfdeptssl dpelvnevld
      181 iilalaknhq stmlivthem qfakevadri ifiddgiiik dcspqnmfsl gensrissfi
      241 kklgs
//
LOCUS       WP_010689649             488 aa            linear   BCT 01-JAN-2025
DEFINITION  TldD/PmbA family protein [Treponema denticola].
ACCESSION   WP_010689649
VERSION     WP_010689649.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..488
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53534
     Region          6..485
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 miytseslle aaknavpkae lvtlrihrtr dtffaaqdga fessgysvdq gfmvevlykg
       61 hiaygasqnm tpqgaaeaac qafnaaktas afkiadfdkn vrpytelkye tlrgkktrps
      121 kteifdylfe icnilkvsde vidthayvnl geeviellss ggakilqdfy tigssfgaaa
      181 rrgdiiqrrt yngagartfq ggyeflnfak skveakrvgn eviellgaes cpsdrrtlvl
      241 mpdqmllqih esvghpleid rilgdernfa ggsfikpedi gsfqygsklm nicydptipy
      301 qlatfaadqt gaqakktfii kdgilvcalg slesagrlya gkpvpldkmv anqratswnr
      361 ppidrmanln lepgtssfdq iissiekgii mtsnrswsid dyrnkfqfgc eygqliengk
      421 itktvrdpny rgvsqnfwrn lcavgdkstf hvygtpncgk gepnqvisvg haspvcafsd
      481 vevfgggk
//
LOCUS       WP_010689699             377 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerate kinase [Ligilactobacillus animalis].
ACCESSION   WP_010689699
VERSION     WP_010689699.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..377
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38668
     Region          2..374
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mkiiiapdsf kesmtaseaa qaiyagfkpi fptatyelip ladggegfvd tilntvpgki
       61 ytyqvmgprk qsvtaklavi eagkiallet aaasglqlcn gikdpltats ygtgellkha
      121 ldlgvehiil glggsatndg gagllqalga kfydrshyel plggihlqal ekidisaldp
      181 rlqttkitla sdvaspfigp ngasvvfgpq kgaspnavlq leqaltnfsq vikatcgqdi
      241 attpgagaag giggallaft natltsgvel aialtdleqk ataadilltg egsldsqtkl
      301 gktplgvlra vrsvspdctv iglagkveav aelhqlgfda vfsctpgvin leqalrsgsk
      361 hltqtaneia hllqkfv
//
LOCUS       WP_010689753             289 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Treponema denticola].
ACCESSION   WP_010689753
VERSION     WP_010689753.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..289
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=32296
     Region          20..269
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 mninleqiqt fvkenftlps fisilsflgi ilityiffki iikslkkfte nkvspaiqnl
       61 itkilqytcl avilmtifkk lgininafvg aagiagvaig faaqtsvsni isgffvlaek
      121 afkvgdriql gditgnvesi dfmairvktl dgnivripne vvikgnliny sslpirriet
      181 kisvaygsdm ekvesvlmei pnrvpqilks pepfvfwsay adsgievafy awgknedflv
      241 iknsifklia effeeaeini pfpqmdvyin pertkkepvf yesaenkpi
//
LOCUS       WP_010689780             355 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Treponema
            denticola].
ACCESSION   WP_010689780
VERSION     WP_010689780.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..355
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39410
     Region          <31..116
                     /region_name="PLN03184"
                     /note="chloroplast Hsp70; Provisional"
                     /db_xref="CDD:215618"
     Region          <293..355
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 maskigikla dgtffpilde dalseqslel ttvrddqesv qinlfkqvdg aepeyigsli
       61 vedistgrag dptinlkikl deeknlsaea vdegsgshqs lrvslknlde anlegmdfdf
      121 asldsssgft sgdddyfike sddlsfdesl esqadsqlyd neekpekkkk mplwliiiii
      181 ilcitalvfa illltkkmpf adkdkiasip ekveqvqesk kdvnattsna pkenaaekaa
      241 aeakrkaeee akqkaeakkk aeeeakqkae aeakkkaeee akqkaeakkk aetqqksntn
      301 sngavrykik wgdtlwdlse tyyktpwlyk kiadynkikn pnliiagtyi dippk
//
LOCUS       WP_010689851             435 aa            linear   BCT 01-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Treponema denticola].
ACCESSION   WP_010689851
VERSION     WP_010689851.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11720441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..435
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=47634
     Region          29..>87
                     /region_name="DUF1565"
                     /note="Protein of unknown function (DUF1565); cl23857"
                     /db_xref="CDD:305014"
     Region          189..320
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
ORIGIN      
        1 mkkgiitcll avlvlanlta aeyyvsketg kngnagtkda pfkniekaae kvqpgdkiyv
       61 aegnyygvrd kgfiviqkav eiyggyskdf skrdvlkyrt lvmppassng tgrankamef
      121 dikngegkkl vidgiifdkg lsngyhptkg kpqgvetgml vlppgqgvng geksitteka
      181 ifggsimkcd vliqncvfnn asnfaiqfgg tgnvkilnnv ftanamaace iwgkenkpna
      241 itvefayntv lftwprthaf edmgygfrvm tkvevnihhn iiglsclsav drcridspas
      301 mengrkvlmd nnrffmnkqa dvtlpglgtf eyvwvkdfdd ldrfnsaegn eelkdiaslk
      361 nvlnkaylag flnatykekt dydpnspane frramgmnqt mtvqtdvsmf ankypqddav
      421 klfgavkgfg aqaik
//
LOCUS       WP_010689874             316 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Treponema denticola].
ACCESSION   WP_010689874
VERSION     WP_010689874.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..316
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36026
     Region          <180..313
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mlkkrsfqvl lffcflfalh psgkkevsdi eqngksekal yiislpesgd lgsffnvkfk
       61 aarkiekawi tiydtsekkv qainafpldk tekewaaiaa vavwwksgkw kirthliidg
      121 alfeedrsfe vlerefeeyv mklskknsqi lrdkspkkte qrnrfaevlk vqnleslyfk
      181 gpfampfdak risstfaekr tskypdgkts vsrhwgidyp spigtpifap gtgkvvlaen
      241 rivtgwtlvi ehapavytiy yhlnkihvke gslvkqgeki adigttgfst gphlhwelri
      301 neipadpell lkkelf
//
LOCUS       WP_010689882             738 aa            linear   BCT 01-JAN-2025
DEFINITION  YncE family protein [Treponema denticola].
ACCESSION   WP_010689882
VERSION     WP_010689882.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..738
                     /product="YncE family protein"
                     /calculated_mol_wt=81372
     Region          <163..300
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mykkylflff alilcfslga qnadlpwsev aenqgdqttg gtgqgggtsg snsasqtqpn
       61 tnsstsqqtq aetnasanqq aqsassgnmg aqsseikpee kkinilafaq amtlavandk
      121 alysrnsaar anlpeqdklr sakvvhkfsg gvteimnsgs lpiffaagkd gfvtrysypk
      181 fepdtwqlss mpiqkiavhp kgqlvavyet ngfsihqvsl wdwakkktlf skrlsdsvvs
      241 lswsangtyl fvgnrstdgi tvldskgivq niyqeapgiv flaataster sivtygesgr
      301 lvytdiakkk klkefrtenk lenpnliknf triigykdnn vyvidavtge tvskhqarya
      361 lfaskiqdsv piwiertrrk newcirqgda sssgfyvpgn skitaarhik nhmvigtqdg
      421 siymiglned ssvnlekplt ysdskiddit sdgnilyilk dgkiyvqnsp eekpvpiied
      481 lktnkftfyn ngfllwsdik kgmpishysl dtkslkkiii pketvisvsv yknlflyves
      541 fngvtlvnfd ngkkefvyna pgiqnavqvd dntmliaksa igrsqspvfi intlteetsp
      601 ipmegnlafa leqnasrpns lacflvgtsp spktellhis lnrkntidst fkpilsykee
      661 svdafleisg ndiltnlgns slvhcntssk qarrlsrsyg fpkeavilkk yfislnfgdt
      721 lswyerktga ilktvtie
//
LOCUS       WP_010689906             276 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Ligilactobacillus animalis].
ACCESSION   WP_010689906
VERSION     WP_010689906.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..276
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31189
     Region          5..267
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqqtrskwad lylvlvfifl ylpifylvwy sfnagdtmnd ftgfslrhfs elfsdtrlvi
       61 illntfllaf lsaliatvig tfgalfiyyl rkrrhrntll slnnilivsp dvtigasfli
      121 lfitlgsifs gfslgfwtvl lahvsfsipi vvlmilpklq emndsmitag ydlgannrqi
      181 lkdiilpyls pgiiagyfma ftyslddfav tffvtgngft tlsveiysra rrgvsleina
      241 lstlvflfal vlvvgyyyis kdnqprskkk krgllr
//
LOCUS       WP_010689918             209 aa            linear   BCT 01-JAN-2025
DEFINITION  YoaK family protein [Ligilactobacillus animalis].
ACCESSION   WP_010689918
VERSION     WP_010689918.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..209
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22876
     Region          3..207
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mtgltlafcg gyidaytyvl rehslvagqt gnivflavdi askgltitet rfftfiffil
       61 gifvisflak kldspyvkpl slfpcilacl vigflpvstp dylvvpplaf gvgiqttsfs
      121 kiegipynns fstgnikkgm iawngfffsh sladkhaakl ylaitlafal galcsaelek
      181 lwgihtiwai tvilsavmlr ylyllrhek
//
LOCUS       WP_010689911             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Ligilactobacillus].
ACCESSION   WP_010689911
VERSION     WP_010689911.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29659
     Region          7..258
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mkkyntllav pyflwllffv lapvvlvigy sffdqsghft lanyaeyfgs gkyllmtfns
       61 vwyaflitli tllisyptay fltklkhkdl wllliilptw inlllkayaf igifgvhggl
      121 nsflgffgil pkqllftdfs flivavyiql pfmiiplfna leelppsfia askdlgasst
      181 qtffkvvfpl slngvksgvq avfipslslf mltrliggnr vitlgtaiee hfmvtqnwgk
      241 gatigvvlii amvivmlftg ekkaggk
//
LOCUS       WP_010689932             752 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Ligilactobacillus animalis].
ACCESSION   WP_010689932
VERSION     WP_010689932.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 752)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 752)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..752
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=86226
     Region          1..750
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mkrifeidpw kvvthefkpe ekrlqesmts igneymgmrg mfeetysgdt hkgiylggvw
       61 ypdktrvgww kngypeyfgk vinavdftkv diklngssvd lakdefsdfe laldmkkgil
      121 nrsfivekdg qkfrlnferf vsvaqkelya skitvenlnd teanveiksy idadvfneda
      181 nydekfwnvl aqnvakthms ltaqtipnnf gtpqftteml adhvtdlrpm aaetteksvv
      241 nifagqvaag qivafekrvi vvtsrdydtq ealtqatqtl sqkqaeksfe elkteqaagw
      301 akrwekadve isgnaesqqg irfnlfqlfs tyygddarln igpkgftgek yggatywdte
      361 afavplylal adesvtknll kyrydqlega yhnaqqqglk galypmvtfn giechnewei
      421 tfeeihrngt iayaiynytr ytgdeeyath ngfdvlvgia rfwadrvhys krkgqymihg
      481 vtgpneyenn vnnnwytnml akwclnyane iadkvsaekl aqldlgeaer qkwheiadnm
      541 ylpedqelgi fvqhdtfldk dltpvkdlpe gqlplnqnws wdkilrspyi kqadvlqgiy
      601 yfvedftpeq keknfdfyep ltvhesslsp sihsvlaadl hkedkafemy srtarldldn
      661 ynndtedglh itsmtgswla ivqgfagmrv idgelefapf lpkewdgykf rinfrgrlls
      721 ievdktgski ellkgeplki klngeetelt vk
//
LOCUS       WP_010689950             248 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Treponema denticola].
ACCESSION   WP_010689950
VERSION     WP_010689950.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..248
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28068
     Region          11..183
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mnlektnknl iffiakkefk mmyksssfya aslfflagaa iafigsdswf naglsdlknf
       61 flnmpllfcv vtpmltmssw sdekkqftdk flfslpvsir yivlgkylsl iliwsimlal
      121 slviplsvfs layfdsgsff vsyfsiflfg sgiisislgl savsgkpein fllsfltvlf
      181 ftiiypltrn lnfplllnei isylsfshhf esaarglfds rdlifylilv vlgielnvfi
      241 ltqqrnvr
//
LOCUS       WP_010690027             448 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Treponema denticola].
ACCESSION   WP_010690027
VERSION     WP_010690027.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 448)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..448
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48822
     Region          30..250
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          153..446
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mknlvfikma frflgigsgk tvsnarkslf gavlgigisi iplivvlvvs dgmiqgitsr
       61 tielgtghlq vinmrsissy knaeteknvr slilefdegn fvenawierq gnglvigksg
      121 rsggairave pefftqnira lnlikvisgs lefennksai lgtaiaeklg lkvgdtcrii
      181 tisknekgkt iprvssfkis glvssgyqel dalwvfiple eglkimpmss sltsivvstn
      241 dpfdedkmqa lqlklnsilp esfsiyswad lnrsaftsfk ttknillfim flivlvasan
      301 issaivmlvm errreiailk aagahpssis lafllagllt slggiilgmp lgilaaihin
      361 eifayaekil nhiqnffytf lygtggtgkp leihlldpay yleyipvkln lfdlytiavs
      421 mlilsvvvcl ipavragkek pieimrkl
//
LOCUS       WP_010690037             242 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Ligilactobacillus].
ACCESSION   WP_010690037
VERSION     WP_010690037.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..242
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26493
     Region          2..240
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 miefkgvtkk ydnvialnnl nlvipagkif gflghngagk sttikslvsi lnpdagqiiv
       61 dgkdlaeqrf lvkkmigyvp dspdiflqlt aaeywdmlaa ayeikaseka trikelagsf
      121 gilerqdevm esyshgmrqk aiivgallse pdiwvldepl qgldpqaayd lkemmkkhva
      181 kgktvifsth ildtaqqlcd elailkkgsl iyngtvaell akepgksleq iylelagrke
      241 ge
//
LOCUS       WP_010690079             308 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Ligilactobacillus animalis].
ACCESSION   WP_010690079
VERSION     WP_010690079.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..308
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33392
     Region          1..160
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mkfiaivgtn atksynrkll qfmsshfatq aqievteikd iplfcedyeq tpqsvldlaq
       61 kieasdgvif gtpeydhdip aalksviewl swkvhpltkr pvmivgaslg nlgtvqaqes
      121 lrrildspgl gsfvlpgfqf llgraenafd ekgclidqgt iswleqcfng fihyatalek
      181 lqhaqqaqak nehipttpal kqqeaksalq aldridtttg asetadmsfe eanginfvld
      241 ddtefsfpde qtgasetatk petvteeppa liytedalts asestpapke epvpapaqvd
      301 tttgaseg
//
LOCUS       WP_010690135             449 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Ligilactobacillus animalis].
ACCESSION   WP_010690135
VERSION     WP_010690135.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..449
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47273
     Region          12..445
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mdngqttatk agwlertfhf kelktntkre tvaglttfvs mayilfvnan ilgaagmdkg
       61 avftatalsa iigctlmafl anypigiapg lgdnafftys vvltmgipwq tamagvvvas
      121 iiftllslfk ireividaip hdlklamaag igifiafvgl kgggivvask sslvelgslt
      181 vpttwltifg ffvtallmar rvpgsifigi lattllglvt glipmpdkiv ssipslaptf
      241 gvglanlgni ntpqmlavii vlllvtffdt agtlvglaqq aglmkndkmp rigralmads
      301 fsmlagsvmg ttptaayves sagiavggrt gftslviagm fglslffspl lsvvttevta
      361 paliivgslm aqsmrfinwe kfeialpafl tiiampltsn isygiafgfl vypitmiaag
      421 rrkelnpvvi vlffifiaml yvlnilphn
//
LOCUS       WP_010690155             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Ligilactobacillus].
ACCESSION   WP_010690155
VERSION     WP_010690155.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..268
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29504
     Region          10..197
                     /region_name="YycJ-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Bacillus
                     subtilis YycJ and related proteins; MBL-fold metallo
                     hydrolase domain; cd07733"
                     /db_xref="CDD:293819"
     Site            order(62,64,66..67,127..128,149,197)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293819"
ORIGIN      
        1 mseevglkvs vlasgstgna tyietpkqkl lidaglsgkk ieglmnsigr tlkdvdkllv
       61 thehsdhikg vgvlarrygl dvyanektwe qmapkigqvk teqkhifere tvqtfgdldv
      121 qsfgvshdat dpqfyevhya gksfaivtdt gyvsdrikgi venadgylfe cnhdtemlra
      181 giypwslkqr ilsdqghlsn edganaltsv lgartkriyl ghlsqennvk elahltvqrq
      241 mqakdfgvgq dfllldtdpa qatelavl
//
LOCUS       WP_010690157             434 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Ligilactobacillus animalis].
ACCESSION   WP_010690157
VERSION     WP_010690157.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..434
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44725
     Region          128..418
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mskneqfdge fnevgsnngp tkqpgskqqg lgkvfliglc agvlgggvav ggytlyqnns
       61 tqlasnsqgt tatsnvkvnv stqttkafdt vkdavvsvea yseqqssssl edlfgknsgn
      121 stsqtstseg sgviykksgn tayivtnnhv isgankvevl lnsgkklsat vvghdsvtdl
      181 avlkinakdv kqvasfgnsd nikvgetala igsplgseya tsltqgiisa ksrtinvtns
      241 sgittgqatv iqtdaainpg nsggalvnlq gqviginsmk lsstgssest svegmgfaip
      301 snevvsiinq lvengkvkrp algislvdld yisqsartdt lklpadvtsg vvvmkvdsss
      361 plkdsgiaky dvitsiggkk vtdlatlrqa lyehkigdtv eigyyhegkq qtanvkltle
      421 addsntttss nsne
//
LOCUS       WP_010690174             102 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Treponema
            denticola].
ACCESSION   WP_010690174
VERSION     WP_010690174.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..102
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12097
     Region          4..96
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mkkyilrylp lakqdldgii nyiqnnlqnp iaaentlski esailerldn pedfaiwssk
       61 kqcpypyrri nvgnytvwyv vidnimeirr ilysrryeen li
//
LOCUS       WP_010690182             157 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Ligilactobacillus animalis].
ACCESSION   WP_010690182
VERSION     WP_010690182.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..157
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17425
     Region          5..148
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 malnykrvlv aidgskgsdi aletaidvtk rneahldilr vldlnsleyg gagialdgeq
       61 iyrieqenea yllklreeli ekhgfktdqi nvhirfgnpk ivitedfqse ynidmiivgs
      121 tgksflhriv tgsvashvtr takcdvlvar steenlk
//
LOCUS       WP_010690186             720 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Ligilactobacillus
            animalis].
ACCESSION   WP_010690186
VERSION     WP_010690186.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 720)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 720)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..720
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79334
     Region          79..701
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 marytdpfgd mddifnqlwg nnglssessr yminghevtp eefrqyrqtg rlpnqaqqqa
       61 aaqaqqaamq qqagqqegsv lqklgrnltq daregkldpv igrkkeiqea aeilarrtkn
      121 npvlvgdagv gktavvegla qaivngdvpa aiknkeivsi dissleagtq yrgsfeeniq
      181 nlvnevkeag niilffdeih qilgagstgg dsgskgladi lkpalsrgei svigattqde
      241 yrntilknaa larrfnevvv neptpedtfk ilegirklye dhhnvvlpdd vlkaavdlsv
      301 qyipqrtlpd kaidlvdmta ahlasqhtvt dakqieaeik kakdeqqaaa dkedyeealn
      361 vkakidelea klnsnseaqk vtatvddvaq sverltgipv skmgasdier lrniesrlkg
      421 kvigqdeave avsrairrnr agfddgnrpi gsflfvgptg vgktelakql aydmfgnkda
      481 iirldmseys drtavsklig ttagyvgydd nsntltervr rqpysivlld eiekadpqvi
      541 tlllqvlddg rltdgqgntv nfkntviiat snagfgneal tgdedkdeei mkklapyfrp
      601 eflnrfnavi efshltkedl hhivdlmlad vnhnlakkgl dlevsepake flieqgydea
      661 mgarplrrvi eqqirdkvtd fyldnidvkh leadmkdgvl viaerkddak keepeteakd
//
LOCUS       WP_010690219             310 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Ligilactobacillus animalis].
ACCESSION   WP_010690219
VERSION     WP_010690219.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..310
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35517
     Region          7..191
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(10,12,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(44,97..98)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            96..98
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
     Region          <222..308
                     /region_name="secD"
                     /note="preprotein translocase subunit SecD; Reviewed;
                     PRK08343"
                     /db_xref="CDD:236245"
ORIGIN      
        1 makklsiivp cyfeeesvpl fyeavekvkd klvdveleyw fvndgstdnt lnemqklqik
       61 dpehvhyvsf srnfgkeaal ycglreatgd yvtvmdvdlq dppdmlpeml niiettdydc
      121 vgtrrvdrsg eppirsffar mfyklinkis dteiidgard frlmtrqmvd ailemseynr
      181 fskgifswvg fktkylnyen qervagktsw nfwslfkysi dgivnfsqfp ldiaafvgfi
      241 ssvisglgil fiiaryliqg dptsgwasti cimlfiggiq lfclgivgky igkiftevkd
      301 rpvyiikekk
//
LOCUS       WP_010690227             332 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Ligilactobacillus animalis].
ACCESSION   WP_010690227
VERSION     WP_010690227.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..332
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37254
     Region          1..181
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mplisfiipa ynsektlkra vesvtnsiid qtyevliidd gskdntlila nqlalqnqri
       61 rvltagkgvg harntgikha rgqmiaflda ddhylrsalp kalsqakknp adlqifsfeh
      121 gkhtvdltlp ssnsldvrcr tlekptnymt vwgkffkrsl lidndiyfne eltmsedsef
      181 lirytaaces ittsalvlyh ytidtpsatr sfdtkkiqay lnalniaeef idsqpqvikq
      241 sflsytliqv niiavrliyt lgnpasnkqk raeldkvita pvvkkaleqv tlkqcltphl
      301 lpglflklhl sslaillfkl rskqneqken ns
//
LOCUS       WP_010690248             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Ligilactobacillus].
ACCESSION   WP_010690248
VERSION     WP_010690248.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..248
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27727
     Region          1..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mlrlknvtkt fgtqtalkdi ttafndhett vlvgpsgsgk stllrslnll erpesgtydc
       61 dgieldfakk itkketlavr qktemvfqdy nlfphltvlk nvmegpvhvl kedkqtakkr
      121 alelldkvgl kqkadaypnq lsggqaqrva iarslamrpr yilldeptsa ldpelelevl
      181 kvllelanek qsliivthnl efarhvadki lfiedgqinf sgskddffns ndlrikefis
      241 amtldnln
//
LOCUS       WP_010690301             463 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Ligilactobacillus].
ACCESSION   WP_010690301
VERSION     WP_010690301.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..463
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49911
     Region          18..463
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msikervfkk esldrylsed rkfnktlsak dlismgigav igtgifilpg tvaalhsgpa
       61 itisfviaal vcstaamcya efssalpiag saysfgnvvf geivgwflgw alileymlsv
      121 aavstgfsay fnsllaglgi hlpkaitgpf dpangtfinl pavlivlfia yvlsrglrts
      181 mtinsifvii kiaiiilfll vgmfyvkpan wdpfmpfgtk gvlvgaaqvf faylgfdvva
      241 ssaaevkepa knmprgiigt laictllyil vsivltgmis ytklnvadpv sfalyavkqn
      301 wvagiisvsa lagmftmmvt mvysssrliy sigrdgllpk flgqinektk tpeksmlivt
      361 liialtggff slnqltnlvn igtllafmfv slgvlplrkr kdipnkdgfk vpfypvlpii
      421 sailcavmla qlsletwtaa fvwfaigmvi yfsygikhsk ine
//
LOCUS       WP_010690313             439 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Ligilactobacillus animalis].
ACCESSION   WP_010690313
VERSION     WP_010690313.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..439
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47434
     Region          1..438
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mkkneqvhld rsinlfsala lvigtvigsg iffkqasvls yshsttmall awffggvltl
       61 tsgltiaeig sqmpqtggly iymhnlygkv wgflsgwmqi tvygpaviaa lgsylaillq
      121 affgfpasyt pfvgvlsvvl isgfnflsnr ygsalqivtt lcklvpiaai iifgllfgdq
      181 navgqvlaer sssvagnfgv ailatlfayd gwilianmgg eiknpqkilp laivlglsav
      241 liiyvlvsys ifktmpaemi arygenatph faemafgkig gkilnigiii sivgcmngkv
      301 mtiprimyam aknnelpfsk qlaylnktmh tpmvsisaia viasgmiltv dadrlteici
      361 ftiycfyvmt ffgvfklrkt tprakrpfsi plypltpiva ilgaafvlvs elfsdlsgvv
      421 islvivlcgl piyyyknrv
//
LOCUS       WP_010690348             271 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Ligilactobacillus animalis].
ACCESSION   WP_010690348
VERSION     WP_010690348.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..271
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29938
     Region          21..233
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkyftkkmit plsttaeltg yvpdnspeid lkrkrpavii cpggayrmts dreaeavafk
       61 flgmdlaafv lryscapary pvallelaes vryvrahake faldpnkiii lgmsagghla
      121 aslgtlwtde lfndhgyake mikpngmilc ypvitagefs hsgsfdnlvg kdpklrefls
      181 lekrvtaatp ptfiwhtvad qsvpvensll faqalrkhgi dfemhlypyg rhglslgtkq
      241 takkanyiep avqswislve twlvggnfqp k
//
LOCUS       WP_010690357             545 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Ligilactobacillus].
ACCESSION   WP_010690357
VERSION     WP_010690357.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..545
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59928
     Region          12..458
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mvslievqiv qkrsislfsa tmlalsslig sgwlfgssea asvagpaavi swvigavvig
       61 ivafnyielg vmlpesggms rypqyshgpl vgfiaswanw lslvalipie avaavqymst
      121 wpwawanwtn dfmkngqivg kglivvflfm vvftllnfws vsiltrftnl isvfkiaipl
      181 ltiillmssg fyvenfghtl aefmpngssp vfeattvsgi ilsynafqtv iniggeikdp
      241 qknifraiti sltiatviyi mlqiayigti tptqlathgw sglnfaspfa diaillgihw
      301 lavllyldaf vspfgtgvsf aatsgrtlaa mtlnrripkw lgevdstygn prfaylanfa
      361 vgallvlvfr dwallasvma tatliayatg pvtvmafrkl rpdytrpvhs kmmpviaplt
      421 fviaglaiyw amwpttvqvi faillglpmy myydrkngqi swkrqlksgg wllvylafls
      481 mmsyagskgf ngqdwikypy dfliiivvsl vfyywglasr mpdspdleaa dklnknvrqs
      541 vrqhg
//
LOCUS       WP_010690459             467 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Treponema denticola].
ACCESSION   WP_010690459
VERSION     WP_010690459.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..467
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51268
     Region          21..445
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mlkntdlkky aligtkrfwf lmwglglagq lcwnienqwf ntfvyakiak dssivtlmvi
       61 tsalvttfst flfgtlsdri gsrrrfvsig yivwglttil fgltefvgrg hvgtgakvsv
      121 waavlvilad dfmsffgsmg ndsgynawsn dmttdknrgq vgavlaiqpv igtivgtvlg
      181 glligsenny qrlfwsmglf vigtglislf llkdapdlkp hkegsfgkqf aaifkaegff
      241 shkelmlacv ttavffisfn vyfvhmgnwm iyrmgfdaar mgiiqglsll aaslsvipai
      301 glinksrtpr laafaiilns lglcilslfi kpasvnpdav fslkniplfl svflagtgqi
      361 lvtqsmtmwv kelypetsrg qfegmrilff vltpmiigti ignflvknga gsvvnefgit
      421 enipvesiyv cgavlalcaf iplyfaskly nkrknnepkd sesyekk
//
LOCUS       WP_010690520             921 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Fructobacillus fructosus].
ACCESSION   WP_010690520
VERSION     WP_010690520.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 921)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..921
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=105238
     Region          253..828
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 msllfniitf crpfflfsle sllglffvig fsklsqvksk rdpyfgrrvf qkgspawvsk
       61 nmlfitwfsm vitnffiivy wsfytevvgv nrgsindqfg rvsgeilnyi npfnwatvle
      121 plphityena lvwrivfvaf mivgqigvyr swknikneqa defggasfte pyelkqqyqa
      181 vpdrgetfeg ygsvpaghkf nwnreglkly fatalpkfvp krflkyksse pgakqpnprk
      241 lpgvyfvdsk ptntiinadt ragkgktlve ptidlvargd kdqslivgdl kgelstmtme
      301 lllkhnydvk ianfdnlnys mpinllsqti yyakkgnypk arlkvsqlan tifpsedsda
      361 kskfftngas atfsgltlat lwlmrrendw dkvtianvae mlqvlgttee svssstgeri
      421 lkpsneisfq drpkqknkld mlvdcfriiq qqniekgesd vlldmavsaf nqsgmggset
      481 kgniyasmfs dieiftsdvn vrklttinnf ryssigfprv melqlphyfg nrkaeisfta
      541 ggkeyvdlvi ademgliqya iepklddett fkvsfkhyen tknlqalppd ttltdkyiti
      601 qafkkyrgsg fgsrsrhekd pytgldvidg yqikkidtni esnpvygple isfdysekrt
      661 alfvilppln aqynliamff meqlyqenyd waqrnknkvi nrmhflmdef gnfpkwpkle
      721 tklssalgyn ieftlvlqnl eqlkdvygeq taatiranss nfayiksssq etteeiskal
      781 gnrtitystq gqntadgdnr nrqikeqpll npeqlrnfrp gqmlffraak nndikghlvt
      841 tnpiydygwt gmpasynllq gylnpspela kievdspqry lnlddyridy lnlfdqlyle
      901 thpryaawwn lymnkesggs k
//
LOCUS       WP_010690528             191 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Fructobacillus fructosus].
ACCESSION   WP_010690528
VERSION     WP_010690528.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..191
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=21073
     Region          10..189
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mtdfpqlnls qkdvsavlkt sygdislalf peqapkaven flthakqgdy dqvifhrvin
       61 dfmvqtgdpd gtgrggqsiw gkpfedefsd elfnirgals managpntng sqffivqnkh
      121 fpkqmkpylg rypeaiakvy qeeggtpwld gkhtvfgqvv egmdvldkia aakvnradqp
      181 lkdiviekvi l
//
LOCUS       WP_010690568             252 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010690568
VERSION     WP_010690568.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..252
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27343
     Region          2..242
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mieisnvska ygssktkavd cisvnvknge ifgflgpnga gktttikmit gvlnqdsgsi
       61 ivdgvniaed pmeakrrigy vtdnpelfsq lkaaeylnfi gdvygvsadv rqeriekytk
      121 lfgindalng sigsfshgmk qkllvtgsll sdppvwilde pmvgldpksa fslkeimrer
      181 adagkvvffs thvmevaekl cdrlaiinag kimfegslqe lrekrgenas leklflelvd
      241 dkpsfnlgng ea
//
LOCUS       WP_010689590             651 aa            linear   BCT 01-JAN-2025
DEFINITION  formylglycine-generating enzyme family protein [Treponema
            denticola].
ACCESSION   WP_010689590
VERSION     WP_010689590.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..651
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=72566
     Region          424..648
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mtksdlyskt raavliaaal fallftacpn naggggnfpt vnitvkgdtk vnpltepisv
       61 wagakwrnvk tqvegkvsfk pgfilnswhl gedesapelt dedafytdtt vfvksradlp
      121 plgplqngtn kvkitfavnp aeagqilgpn pisvnkgttw tqleayakaa lkanygfsee
      181 hvewkkdgsv lgstdsfntd vkltahpedr riivtvtgdt evtiaepati tvidgakwqd
      241 vrakalgkvt vkntnfaiaa wkldgesgtv ltddyefkkn dgtsrtvyae tgdrritltv
      301 kygrgfdatk nggtitvydg dtwrsvkaea akkvnipkgi ilqewrrnda sgeiikdgyi
      361 frasdgnsrt ffariradik lkdnkltyya mvngdvteyv ywlcsipevk ggligrdynv
      421 snkerpiyls aywmgktevp qvlyelvmgk npsyhqgdsh lpaegerqel rpvekvswld
      481 ciafcneltr cteglgegqc vytynnkpyt vqdakdkrip yilpwarkgf clptdeewew
      541 aaqggsrrqk ysgtndvngl nsyawyrens eskthevqtk fsndyglhdm sgnvaewcwn
      601 rygntlpesr riirggcfad sessctcdar ttekdydird ifygfrivfh p
//
LOCUS       WP_010690578             246 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Fructobacillus
            fructosus].
ACCESSION   WP_010690578
VERSION     WP_010690578.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..246
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25788
     Region          1..246
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mliilygfli gcfvtliggg gatfylgvlt sslamstema vptslfiavf allsgfltql
       61 klknvdlrig nrlifaaipg iiigtavsrf ipaviyqtai gclltfmgcv vlyknlrkkk
      121 keqvvneksk vallfglisg lmvgfgglsg gsavvaglsi iglpavkatg tttyilwvla
      181 vvglfshlaa gspiswtagl flmaggiags vltplvlrlf dqkklnkfls pmlgfviiyf
      241 glnlif
//
LOCUS       WP_010690644             945 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Treponema denticola].
ACCESSION   WP_010690644
VERSION     WP_010690644.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..945
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=107311
     Region          6..>343
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mrfpitnadk pglrnaqiga iyavasyatl nskdaavivm ptgsgkttvv mmapyllkkn
       61 kvlivtpsam vrnqiandya ylrtlkyvgv fskqtnapii yeakhlystd ynenilradv
      121 viathqvals isesqirqnf dyiiideahh vpaptwqrii knmidipsll vtatpfrldk
      181 keikgktvyn yplsraykdg ifgeimfnpi eegpekdkri aleaerilfn dresgydhfl
      241 mirtdtkdka kkleelykdv tklklerids tmstktvekt ikllkekkld giicvdmlge
      301 gfdfpnlkia aihephksla stlqfigrfa rtnaekigta kfiamnddnl kiennklyss
      361 daawqdmiis mseekiegdl evneilsqft kpenkdelis lnnirpncha kvykvsnfni
      421 ygdfpeelkv geniyrskem nsilgisqis stplwldgds vlnnefglyi vhyqpntklm
      481 fiysqnktea vyeliaesfa ehydkiprde mnrvlaefsd yeffntgmqn rysesgesyr
      541 iyagsntass idettgkmls aghafckvkk dgststigys sgskfwsssy lnipeyikwc
      601 dlfgekisnn klkvktdtny dklpipvril eyetdilfcf ldrkafispc tivyrenlda
      661 kalitditlk vievnknkik fgvqlfdvte vltcdvtgky nsekeefick ngkeeyslae
      721 yfsnnplsfk ttddtvyygq evlkgnlele kydqnricsf nwddmnvdts lecgigingm
      781 isiqdglrny lkqelkfshi ifdhgtgeia dfitfeengd fiyvemyhck amkgktfnss
      841 vddvyevtqq aikssiwvss kamllkkind rvlgakndkf lrgefrtlke ilqsskllqv
      901 kvyvvqpais ksveipnkig tilsagasfi kntgkiqell iigse
//
LOCUS       WP_010690695             658 aa            linear   BCT 01-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Treponema denticola].
ACCESSION   WP_010690695
VERSION     WP_010690695.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..658
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75734
     Region          <172..483
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mktnlyfysq lnylprtaie aeilfavcls kkkaltggkf laredkyskk igvksavltl
       61 vyfyiimivh kcqqsakrkl llnknnlsdv fpltvgsgkt mafenrrgky keigkkvpqa
      121 yrvyvehlfl rsdagdarif skegnmtnkl sttnipgsqg nsypkaeldy nlnyeydpay
      181 ahrlihagtr yyrydangni taekdgpftd eeeftftysy fenedvygtd ygfgldapke
      241 teqanpqdlf ayrrnytwne rnlltkssdr nftvhyryge dgqralkytd egrsetlyfn
      301 nfftihiptq dqnnpqglrv hkhifvgnsr lvtamthtdn ygdneeqkvk ryyyhsdhlg
      361 saqfvtdwkg rqyehieytp ygelwieeva agldklpfrf tgkeldeetg fyyygaryld
      421 pkysrwlsgd palndyipqa pvndeakkhn enlpgmggvf nvvnlhvyhy agnnpvkyvd
      481 pdgkkmvegd yiretnlsfp dmiylwdtnn kkynysksil gwfgigqssi daglmvgewg
      541 nlfrgiakdi agvvgsasti isvitaimpd pegeakqkwd kflasyvddr geaidgtrkd
      601 iklirsrkvt lkkyteqrgp iivfgvkarv kettelsyin kdgkeireli keeiwdey
//
LOCUS       WP_010690635             792 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Fructobacillus fructosus].
ACCESSION   WP_010690635
VERSION     WP_010690635.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 792)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 792)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 792)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 792)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 792)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..792
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=89499
     Region          1..784
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
ORIGIN      
        1 mkieeihivg fgkwtdvtfr fsndfqiiag pneagktslk afiigvffgf prgrradqql
       61 yeprsgaryg grvtiatqkg rfsierldrt qsmltvrsld sgltmpdpek wlqrlfaplt
      121 ekdyrhifsf deaeldqvtn ltgddfeqal ltyakpqtqq flswadqhhq lgqqqfaqgk
      181 ngkrplnman kayralqekq alasqqegqy qnllakrlel eatlaqltde etklqealhd
      241 kqseladwsl yqdvstkkna skelvelpde nrrqaiqele qekrwlekka qeqqealtsi
      301 qqelsdqnqv ppsesvirdt maslaayqse eerivqaiah aghgftrglp qplnqteekl
      361 lqksarlpwt vaflllgasl laalllpgle aglllvvsla llgffwqqks kkralldrfa
      421 plnqaailay qdrlrtiyre qsqlplidkq rqqalqalkk allqsgrlde atlaawsddq
      481 vqdwvkeell dcrhtgktgl nhrlqealrq qaaiakqkeq laerlqeqla pyglaniddf
      541 yerinqqqkq eqllvaqrma tkqlgqgrla tfsklvdtlg qenvanhlqa qlgeyqnkla
      601 slrqsknqqq qliadvsaql tqlvekgslt sisqelanfe sdlkedyvhy laqvlavdvv
      661 krafvgkeds lahqvfeqag aylaqltega yqrillndgs invfdsagql fraielssgt
      721 rdllflairl alstsvhree plplliddal vhldhqrrqa alvllqelat eqqvlfwtfd
      781 egllgpsgir lt
//
LOCUS       WP_010690705             464 aa            linear   BCT 01-JAN-2025
DEFINITION  RHS repeat domain-containing protein, partial [Treponema
            denticola].
ACCESSION   WP_010690705
VERSION     WP_010690705.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         <1..464
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          <65..308
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 gsgktmtfen rrgkykelgk kvpqayrvyv eetflpcdav iarifskddv yginygfgld
       61 apketeqanp qdlfayrrny twnernlltk ssdrnftvhy rygedgqral kytdegrset
      121 lyfnnfftih iptqdqnnpq glrvhkhifv gnsrlvtamt htdnsgdnee qkaksyyyhs
      181 dhlgsaqfvt dwkgrqyehi eytpygelwi eevaagldkl pfrftgkeld eetglyyyga
      241 ryldpkysrw lsgdpalndy ipkapiddea kkhnenlpgm ggiyntinlh vyhyagnnpv
      301 kyidpdgrlt adeetakkie nlgknapgkl ideillklke dgwtivtnee kkevhddlkd
      361 saskdnknmm vsidstpisi ekdfteeekd qielnkkida ipnnnlhkkt feklkrdikp
      421 kditltmiif kvnpydfekk qilgnykeyi didndgnidg ykyk
//
LOCUS       WP_010690710             254 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Fructobacillus fructosus].
ACCESSION   WP_010690710
VERSION     WP_010690710.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..254
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27362
     Region          2..252
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 makiialanq kggvgkttts inlsaalaka gkrvllvdad pqgnassgvg vdkstlesdi
       61 ydvliqdtpv nevilpsstp gldilpttiq lseaevqlvd lpereyrlsk alakvqadyd
      121 yviidnppsl glltinsfta adavlipvqt efyaleglgq lintielvrq glnpdlemag
      181 illtmydgrt nlgkqvseqv rtyfedrvyq tviprsvrls eapsygqaii dfdpkspgar
      241 lytefakevm aqyg
//
LOCUS       WP_010690749             135 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Fructobacillus fructosus].
ACCESSION   WP_010690749
VERSION     WP_010690749.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..135
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15128
     Region          1..131
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mlnplknvlq ehqlkatsqr ltlleymmth dthptaemih qdlpnislat vyntlekfve
       61 kklvviidgi sdgkrhydaa dhphyhvint rtneiidaan ydpaplikaa qaatglkite
      121 ykidlygvdp dskpe
//
LOCUS       WP_010690750            1152 aa            linear   BCT 01-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Treponema denticola].
ACCESSION   WP_010690750
VERSION     WP_010690750.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 1152)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1152
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..1152
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=131585
     Region          <146..1024
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 miffyyckyf nyllfrtaie akilfavcln kkqaltggks lacedkyskk igaesamltl
       61 vyfyiimivh kcqqsakrkl llnknnllev fpltigsgkt mafenrrgky kelgkkvpqa
      121 yrvyvedtfl pcdaviarif skevihdglg risytakege vyidgtentt qtgwnissai
      181 yydragrkte egmpffyggn lesdlknals yeaieqfyel nnfttirngt kyeyddidrn
      241 iltvlpdgnt qkteysidas lqitkatdpl enisiskkda rgnireverl dknnslltka
      301 kyeysvlgem lkaydakdnl lavnydmlgr risleskdtg kkewiydekg rlyaetdsvl
      361 knkaaeirye ydgfdriikt dypfsrdiey kygaprqngt gqivykkdet gethysygnl
      421 neviketrti nrygagtnpe tasfeyrsdy lgrmqsmkyp dgetitytyd kggqlkgvsg
      481 vkttnkgsik ysyvdkilyd ehsqrvyiky gngvetryky dekrrwldsi etknvqtqdv
      541 fqkikynfda vgnvlgyand astyetsqsy tydnlyqlis vegtsnqykg kksfgatpvs
      601 iakykqtfsf daignmkekl sttnipgsqg nsypkaeldy nlnyeydpay ahrlihastr
      661 yyrydangni taekdgpftd eeefvftysy dpetdvygtd ygfgldapke teqanpqdlf
      721 ayrrnyiwne rnlltkssdr nftvhyrygd dgqralkytd egrsetlyfn nfftihiptq
      781 dqnnpqglrv hkhifvgnsr lvtamthtdn sgdneeqkak qyyyhsdhlg saqfvtdwkg
      841 rqyehieytp ygelwieeva agldklpfrf tgkeldeetg lyyygaryld pkysrwlsgd
      901 palndyipqa pvndeakkhn enlpgmggvf ntvnlhvyhy agnnpikyvd pdgekildvs
      961 ttlvqengee dplgkgntti ashgcvltay trianaisai sertlqnans lalkkdiydg
     1021 nnknlifnsp tasklvnsis ilseykmsfy kslnnislne ygseleklsk sedlyaitir
     1081 vsnkygghtv nmnsdgiivd tednytikin ntsekgylps tvvndiitds saiiridifk
     1141 iekvktvpfl pe
//
LOCUS       WP_010690843             250 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Fructobacillus fructosus].
ACCESSION   WP_010690843
VERSION     WP_010690843.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..250
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27152
     Region          1..247
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 maiknkvvii mgatsgmgra talklnkega kvfisgrrke rleeiakeva ypenlkylta
       61 dvsqpqevra vidqaiadfg rvdvlfnnag vmplgqlsdp nydisvwkri fdtnligvln
      121 gikavlpqmq kqqsglvist ssvvghvvmp agaaysaskf gvraimetlr qeenqngirs
      181 aiispgatnt elihsignea ieknlsesfg ndadyslrae dianavaymv dqpehvdvne
      241 miirprkqei
//
LOCUS       WP_010690860             274 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Fructobacillus fructosus].
ACCESSION   WP_010690860
VERSION     WP_010690860.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 274)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..274
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30457
     Region          19..262
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mtkkkmilli vglgilllaf lsfgpkhkts kskvitvata pgpyselfmn gikpilekeg
       61 ytvksknfsn llnadialdn neadlsvdqh saylknfnke kkgvltgiik iptipmglyq
      121 gakkslaalq dgdriavped asnkarayri lsqnglirlk dgvnevtvtq kdiadnpknl
      181 qfteidssti prvkdefdyv vlpgsvayaa kvpakenllk ekvmddyylv ltvnkvnknk
      241 kwvqvvkhay eseefkryfe sknednswvt adks
//
LOCUS       WP_010690921             288 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Fructobacillus fructosus].
ACCESSION   WP_010690921
VERSION     WP_010690921.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..288
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=31388
     Region          16..288
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 miaklekkld hyyyhqfaga vlygvilaia lnyfwkpghi yssgftglaq lidtvtngri
       61 svswgiaaan lpllviaalk lskrfaifta lavllsalfv pvfatktvlt sdplicaifg
      121 gglngmavgt alrfgvgtgg ldiigmlfkm kfhtkvgsin lafnslimig agltygweya
      181 lysiigvvvs ahfidvfytr qqqiqeiivt nkpemmcehi qnkmrrgvti idsahggytg
      241 kdksvlltvv tqhelgdlre aihevdphaf yseskvehtg grffepep
//
LOCUS       WP_010691014             164 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Treponema
            denticola].
ACCESSION   WP_010691014
VERSION     WP_010691014.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..164
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=18843
     Region          41..156
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mhfdkktlrf llefififti fvlppmlnkr dftpppqpeg ffyvlvfilk ivffaayeei
       61 lyriylpyri ksfygenpes fksafavyei lpviffalah rylgpfnvly aaaagiifrs
      121 lyvliqkkss akcsmttasi kaalcvivlh svhngiiyll ifkg
//
LOCUS       WP_010691021             337 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Fructobacillus
            fructosus].
ACCESSION   WP_010691021
VERSION     WP_010691021.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..337
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36439
     Region          24..332
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mstqeeaprq taashgtvqq kenhlhhhgh tqggqpsqkp yligislnli fvlselifak
       61 lahstalfad afhnlsdvla lviawlavlv fgikatrskt ygwhnvsila sifntvlllf
      121 avgtilvegv ndllnpsgih tnglmitvva aigivvnvst allfkasdvp dehghshhhd
      181 qdlnaktayi hllsdagvsi gvilagwlin ltgwqiidpi vslligliil ltawpvmket
      241 vnlaingvpd tidedaiydy lakkegvvsl hdlhiwplst tetaltvhla lsdealrgdh
      301 gqkelhdiet alketfgvsh vtiqiegqqh eencnti
//
LOCUS       WP_010691043             301 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Treponema denticola].
ACCESSION   WP_010691043
VERSION     WP_010691043.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..301
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32793
     Region          24..68
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          <69..136
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          <137..296
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mykknilrpl ffilfsffcf aedivhiiek gdtlysiskk yntpidsilk knnlsdpski
       61 kigqkliipv ensakndkkt naktnleeit hvvqkgdtly alakkfgvkf sdilklngln
      121 ektplkigqi lkipqgksqg taqeqeskap qdgkqektsi tkagsdketq avkpststkq
      181 adskllwpvp askvsylsgk itgvvidsvk gqavkavssg kvvstgphrg fgqvvfvqsk
      241 tkhiyvyggm ekiavkkgdt iavgqklgel gvelltgkar lyfmvydknk pidpakaprg
      301 l
//
LOCUS       WP_010691112             180 aa            linear   BCT 01-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Fructobacillus
            fructosus].
ACCESSION   WP_010691112
VERSION     WP_010691112.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..180
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=19430
     Region          21..172
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 maikstdvvl nnlqeaqnid vtvkglteng ffekknysgi fgieggqdis peiqwgkvpe
       61 gtksivvtmy dpdaptesgf whwaikdipa dvtylaenag sanseklpng aitmpmdarm
      121 nqyvgaapsa gdephpyhiv vtaldvptld ispdstpafm nfnmighela rgyqivyaqi
//
LOCUS       WP_010691052             286 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Treponema
            denticola].
ACCESSION   WP_010691052
VERSION     WP_010691052.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..286
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=34317
     Region          144..238
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mnkkvikdlc flfilyilvf fmlsyvgkfl fknfynyyyt lfvkyngifg illfllfiii
       61 fylfyskdlk iiftykklnf sfvvkgliyl ssimmiyyii yfifdnaflf nffkyfndvl
      121 tgkknitiyd ililekslkp rfepfmligt viigpifeei fyrgllynkl keisnafiav
      181 fissiffall hipgygfnik mfslvldgil ltycyektnn iyvpilvhsi nnffiflfny
      241 vyfyfliviy fiifiiafii liidiikyvk vrktfnevqt dnlaey
//
LOCUS       WP_010691123             227 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Fructobacillus
            fructosus].
ACCESSION   WP_010691123
VERSION     WP_010691123.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..227
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=25994
     Region          125..221
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mairsksfwg valitvslsi lwtglsrafs vfvpakyntm fadantifwh vlapmaltyl
       61 vffllmrrme rlgqvyqqqp liahrgvril faiiviamil fslfnlyqhl hailnhwhhn
      121 slarllfafm stffvgllee svfrgfalte flrrfnepis cllslilfgf whlpniiaga
      181 pviqaslqvf stmiigfgly mavrlsrsiw ggvlmhwlwd falviah
//
LOCUS       WP_010691170             267 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Fructobacillus fructosus].
ACCESSION   WP_010691170
VERSION     WP_010691170.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29216
     Region          2..258
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mkiierfwla fcffllyapi lflavysfns gdamqgfagf swvhyqelwq dtrllqivln
       61 tlilaltssl iataigtiga laiyrterrl lkqtllglnn vllvspdvii gaaflilmta
      121 lglklgfltv llahvafsip ivvlmvlpkl qemnrdlvla asdlgakpte vltkvtlpvi
      181 apgifagffm altyslddfa vtffvtgngf stlavevysr arqgvslein alstimlgla
      241 fvlvlgyyay sqkttsrkat klkekvk
//
LOCUS       WP_010691277             303 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF4097 family beta strand repeat-containing protein [Treponema
            denticola].
ACCESSION   WP_010691277
VERSION     WP_010691277.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..303
                     /product="DUF4097 family beta strand repeat-containing
                     protein"
                     /calculated_mol_wt=34293
     Region          <156..302
                     /region_name="YvlB"
                     /note="Uncharacterized conserved protein YvlB, contains
                     DUF4097 and DUF4098 domains [Function unknown]; COG3595"
                     /db_xref="CDD:442814"
ORIGIN      
        1 mkkniilafa wfclafavia fftnelrrfn rlgykdfmrf giingkfnph tsvlkemqfd
       61 ineihsikas lisedikfip snddkiivki igieenkklp eikkekdall ikafetekkr
      121 fffgwdyshr ieisipsael yiaenagngs aentisafie stssdiriyd itlknlhfks
      181 vsgdvifrns kienqfefnt ksgdirgeaf iygftgtsvs gdfklrflsa pkndstfsst
      241 sgdfsiylpk ditgfscdfn sssgdyknsf tgssaekkiy dvyktdsprl fiktvsgdcr
      301 irs
//
LOCUS       WP_010691341             467 aa            linear   BCT 01-JAN-2025
DEFINITION  leucine-rich repeat domain-containing protein [Treponema
            denticola].
ACCESSION   WP_010691341
VERSION     WP_010691341.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..467
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=50194
     Region          101..453
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          216..236
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          237..257
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          258..278
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          279..299
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          300..320
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          321..341
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          342..362
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          363..383
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 mktcnskika paflgaafvl lialmftack qpasaekpep pappappkha vtfnvegtpp
       61 ngtlkailgt seitsgdkve egkwviftak addgyrvkew kldgnailgh ksntyahkvt
      121 kpaaitgsfe pysvkltlsp dkntvkvkak tkdgsaikve gctvteltsd vettltaigt
      181 kvkligdiie ldcrgeetpg gnrplialda sgctalqkln crfnniteld vqglkdlqel
      241 ycnsntltal dvygltklek lncktnqlta lnvsdctalk elicnsnels tldasgltal
      301 qelncsrnql taldvsglka lqeficndnk ipelnvqglt klqklecggn qlttlnvqgl
      361 tklqeldcas nqlpaldvqg ctalkmlvcf rnklnadafi kifndlptre asdsatavly
      421 mkgtnvtegn ctdfsqpesl kkafdnakda khwkmqkmng afipsdi
//
LOCUS       WP_010691377             299 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Fructobacillus fructosus].
ACCESSION   WP_010691377
VERSION     WP_010691377.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..299
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31457
     Region          1..289
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 msiivssisq gilwavlgva lyltfrilnf admtvegsfp lgastavali ahgtnpflat
       61 iaalfvgala glitgvlytk gkipillagi lvmtaclsin lrimgsanis lldqktifsl
      121 sflqdlpkyf dgvvlglivi tiilgflmwf lqtelgqafi atgdnkvmaa afgiktdqmt
      181 imglmvsnal iafggaviaq nngfadinmg igiivialas iiigevafgd lslnqrlvav
      241 vigsiiyrlv llavlqlgfs tndlnlissi ilaiammipq arkylkldkv lhmggkahd
//
LOCUS       WP_010691423             326 aa            linear   BCT 01-JAN-2025
DEFINITION  ketopantoate reductase family protein [Fructobacillus fructosus].
ACCESSION   WP_010691423
VERSION     WP_010691423.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..326
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36071
     Region          1..316
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkyavvgaga mglryglllq evagksvdfv eptkesldki kgqgnlvyqs rdhedkhpvl
       61 vniyspeeyt gepdvwiffm kqmqlaetle rmaphfkdnq vavgamngmg hieklqsyfk
      121 ddkiiggtam iatilndfgd vdfigkansg asaysnlsge eteatkevme dfqaahlnpt
      181 ysnnfmgtll tkvffnaven siatmfqarm gnllsydqfv ptiakplvde aydaataagi
      241 tlletreeml vqvdyvarev vplhfpsmyq dfvknrptev dyingwiadl aeangvaapt
      301 qrfitnlvhl aeamrefnpp vnqlaq
//
LOCUS       WP_010691434             251 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Fructobacillus fructosus].
ACCESSION   WP_010691434
VERSION     WP_010691434.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..251
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27544
     Region          2..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mplltvdhlk keykskrssq kvlalkdvdf qveegefiai mgesgsgkst llnciatldk
       61 ptaghillkd adlsqlkdkd laafrrdhlg fvfqnfnlld tltvqdniyl plvlakntkg
      121 kekklltlaq qlgiadllhk ypyelsggqq qrvaigrali tkpelllcde ptgaldskna
      181 edilklfsdc hengqtilmv thsslsasha grvlfikdgt vfhqlyrgdk sdqemlvain
      241 damtnllggq a
//
LOCUS       WP_010691457             209 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Fructobacillus fructosus].
ACCESSION   WP_010691457
VERSION     WP_010691457.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..209
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22452
     Region          24..203
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 msektggqqy ftadptaehd yqnfdftllg knlhfqtdag vfskktidfg trvmldaaae
       61 qhfvagkvld lgcgygpvgn avakawgrev dmvdvndral dlaktncqkn gvndltrvfq
      121 ssvydavvdk yalilvnppi ragkvvvtam lqgatkhlvd ggaiiavlqk kqgapsaqkn
      181 leavfndvsv igkkkgyfvl makepketv
//
LOCUS       WP_010691461             160 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Treponema denticola].
ACCESSION   WP_010691461
VERSION     WP_010691461.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..160
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18529
     Region          53..142
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 mktnhptpdn iefkeitpdn wriinslsik eeqknfaasn vtilarafvy rkenakvfav
       61 yhsdkpigli mqrdwidgek ivcimdqfmi dkksqgrglg kaalqkwlsm ieaekkysci
      121 qlcyvegdia akhlyenfgf yeidkdedei imqkdmekdl
//
LOCUS       WP_010691505             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Treponema].
ACCESSION   WP_010691505
VERSION     WP_010691505.1
KEYWORDS    RefSeq.
SOURCE      Treponema
  ORGANISM  Treponema
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Treponema"
                     /db_xref="taxon:157"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28286
     Region          2..250
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mvldisslsf nfgsknilad idlsikdngi vgiigpngsg kstllkciyr vlkpktgtif
       61 idgknindyq fketakkmav vaqhndthfd fnvlemvlig rsphkkfmer dsaedielay
      121 kaleqvnmkd fadrnfssls ggekqriila ralvqntdcl ildeptnhld ikhqlhfmsl
      181 akdlkitvis aihdlniaam ycdkiyalke gqiiasgsvn eviteevikt lydveakiiy
      241 deekkphvif kni
//
LOCUS       WP_010691553             233 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Fructobacillus fructosus].
ACCESSION   WP_010691553
VERSION     WP_010691553.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..233
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=25703
     Region          18..224
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mqenvrgitk enfltsawwa laffamagil llvwrpwati ttvtvdsgni ptetiekqig
       61 lhqgskrydv ylqegflerk lqkanskvsk advslkgqkv titvaekina gfikekghwy
      121 qldsngnkqq vakpdgrgpv ytgfksdsqv kkvaksvssl dkvirddige iqfapdsnnd
      181 sklilvmndg ntvyasqktm aekmryyggi aqsmtqsgii dlqvgsysya ygs
//
LOCUS       WP_010691522             460 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Fructobacillus fructosus].
ACCESSION   WP_010691522
VERSION     WP_010691522.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..460
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51267
     Region          1..451
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 msqenthiee qqlskglqnr hvqliaiggt igtglfmgag nsihfagpgi lavyaiigam
       61 mfimmramge mlyqdpsqpt fiaymtkylg nrvgffarws ywltmiffgm aeltaigkyv
      121 qfwfpsmpew liqiiflval tgvnliaval fgemefwfsm ikviailali vtglmmafgh
      181 fqtpvgtvsf gnvfnhfslv pngwgnfins fqmvmfafvg mefigmtvae tkdprkilpk
      241 ainqipfrvl ffylgalfvi mtiypwkqip ahqspfvmvf elvglkgaaa iinfvvltaa
      301 assfnsilfs tsrnfyslak esrakflqpf tklssrglpa kallfsslis vssavissip
      361 aindafvfvt saatdlflmi yimilwaywe yrksssympn gfllkapkff vplaviffvf
      421 vyvtlffnds svvpaigatv wlvvfgivsy fqpkkavsee
//
LOCUS       WP_010691582             102 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Fructobacillus fructosus].
ACCESSION   WP_010691582
VERSION     WP_010691582.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 102)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..102
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=11683
     Region          1..97
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mairipnrvl eavvlsvlke eplygyaltk kiqlqlpisd sttypilrrl eqkdlvttrs
       61 kvfaervrky yeltdsgqly lkeacadwql fsnqinallg eh
//
LOCUS       WP_010691604             452 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Fructobacillus fructosus].
ACCESSION   WP_010691604
VERSION     WP_010691604.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..452
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50700
     Region          8..405
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mseenqqfgq fnlkpavlaa lkkigfehpt piqskliptv lrggdvvgqs qtgsgkthtf
       61 lvpifnqlkp elqrtqvvit tpsrelaaqi akaartfaea mamekvsive yvggtdkarq
      121 vrqlekhqpq lvvgtpgrla dlvktgalvv nqvktlvvde admtldmgfl pdvdflaaam
      181 pkdlqtlvfs atmpeklkpf lrkylenpsf ttiptsatia dtidnwlist rskdkeevid
      241 qllsifnpyl alifantker vkelakhlrh qglkvaeihg dipprerrrv mkgimnldyq
      301 yvvatdlaar gidiegvshv indgvpgele ffvhrvgrtg rnglsgtavt lygpdeenki
      361 aeleklgivf qnkqikngdi vavkdrkary qrqattkkld pemvgmvkkk kkkvkpgykr
      421 qiknnlkrkq qmdrrieqrq errntrrenk qg
//
LOCUS       WP_010691640             133 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Fructobacillus
            fructosus].
ACCESSION   WP_010691640
VERSION     WP_010691640.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..133
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14826
     Region          39..125
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mqilsfitli ltfflifyav saissnvlar rratvlksda fierqqathg qlidvrekep
       61 fkrshlkgar nmpalslaqg ksglrqdipv fvygdtlana lgvakrlrke gfnrsnlflm
      121 aggfrqfaak qkr
//
LOCUS       WP_010691721             254 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Treponema denticola].
ACCESSION   WP_010691721
VERSION     WP_010691721.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..254
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28575
     Region          1..222
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mvvvtfsslk ggtgkssaai ivsmalksag krvlgidmdi nnsfsfyfle dgnesekkni
       61 ayalqsdnll dfiihtnkgv diipsslrlv dlramstnil krlipslena ydiviidtap
      121 tydnivlnsv nasdyvitpv nysqfdfnss iflgqklrme tehfdkwflf fnghesryde
      181 npeslqnqyr tlftqnevfg skilpvsfpf trnirkfada geiiqskgqt aklhravcdl
      241 csiiideeir pekf
//
LOCUS       WP_010691738             248 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Treponema denticola].
ACCESSION   WP_010691738
VERSION     WP_010691738.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11979130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..248
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27649
     Region          22..97
                     /region_name="ParB_N_Srx"
                     /note="ParB N-terminal domain and sulfiredoxin
                     protein-related families; cl28891"
                     /db_xref="CDD:452888"
     Site            order(34,48,78,81..82)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:319246"
     Region          65..>212
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mtkltalgnv gktsiansga selsvmvpie ninlkdefkn lfplngnmvd titenilsgt
       61 ydksqpihvw kegmilvdgh hrlaaakkag lkeipvfyhy fkdleealay aiklqtdrrn
      121 lsdaellkil qtldqlkqvg rialdsdkks sgksaeitaq kigvsrskve kartvqnkas
      181 eeikkavedg emsinaayni vqneskeiev aiilepytce lemdekqvkr ienflkkeni
      241 kyslvkkl
//
LOCUS       WP_010691769             265 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Fructobacillus
            fructosus].
ACCESSION   WP_010691769
VERSION     WP_010691769.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..265
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=30298
     Region          113..217
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mslfkkrksd kkhhgvlilf lfilgltfyp nyptvislqg tvflcvilsv ilvlfiwlvr
       61 rvtnhekvfa trlsldrker glavvlvlyf lflylmngni qsglnvfrsp mkillscvfi
      121 aigagcfeey fvrgylfnlv qrmlnryqvk qhrltiiavv tsflfcllhl anladepaea
      181 vaqqvvytfa igmifvtlri vsnqiwplai ahflfdlqdn ivqplvvgsw temlvsflps
      241 vilslfllfy ldrsveekqa tvlqp
//
LOCUS       WP_010691871             120 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF805 domain-containing protein [Fructobacillus fructosus].
ACCESSION   WP_010691871
VERSION     WP_010691871.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..120
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=14302
     Region          10..116
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mnkksvvrvy knfwreifnf sgtedrfefw vpffinalfn lvitflvtfi tgktisetnn
       61 vfifiplfff lilfevaels amirrlrdsg rkwyfllvqf ipligelylf illgkpthrn
//
LOCUS       WP_010691934             921 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Fructobacillus fructosus].
ACCESSION   WP_010691934
VERSION     WP_010691934.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 921)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..921
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=105417
     Region          253..828
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 msllsniitf crpfllfsle sllglffvig fsklsqiksk rdpyfgrrvf qkgspawvtk
       61 nilfitwvsv vvtnffivvf wsfyteivgv nrgtindqfg rvsgeilnyi npfnwvtvle
      121 piphltyens lmwrivfvaf mivgqfgvyr swknikneqa defggasfte pyeleqqyqa
      181 vpdrgdtfsg ygsvpaghkf nwnkeglkly fatalpkfip krflkyksse pgakhpnprk
      241 lpgvyfvdsk ptntiinadt ragkgktlve ptidlvarge kdqsliigdl kgelstmtme
      301 llrkhnydvk ianfdnlnys mpinllsqti yyakkgnypk arlkvsqlan tifpsedsda
      361 kskfftngas atfsgltlat lwlmrrendw nkvtianvae mlqvlgttee svssstgerf
      421 lkpsneisfq drpkqknkld mlvdcfriiq qqniekgesd alldmavsaf nqsgmggset
      481 kgniyasmfs dieiftsdvn vrklttinnf ryssigfprv mevqlphyfg nrkaeisfta
      541 ggkeyvdlvi ademgliqya iepklddett fkvnfkhhen tknlqtlppd tilvdksiti
      601 qafkkyrfsg fgsranrekd pytgldvidg yqikkidtni ksnpiygsle infdysekrt
      661 alfvilppln aqynmiamff meqlyqenyd waqrnknkvi nrmhflmdef gnfpkwprle
      721 tklssalgyn ieftlvlqnl eqlkdvygeq taatiranss nfayiksssq etteeiskal
      781 gnrtitystq gqntadvdnr nrqikeqpll npeqlrnfrp gqmlffraak nndlkghlvt
      841 tnpiydygwt gmpasynllq gylspspela kievdspqry lnlddyridy ldlfdhlyle
      901 thpryaawwn lymnkeseds k
//
LOCUS       WP_010691991             102 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Fructobacillus fructosus].
ACCESSION   WP_010691991
VERSION     WP_010691991.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 102)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..102
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11363
     Region          10..89
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 maiiqkpgwf yyekdgerlg evsylkaahn qvlvlnhtyv dpslrgqnia rqlvdavcdl
       61 arsqgqkvqp dcryaaalfk ryqedyadva ledgpkansc si
//
LOCUS       WP_010692015             316 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Fructobacillus fructosus].
ACCESSION   WP_010692015
VERSION     WP_010692015.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..316
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34709
     Region          11..311
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mpatdpglla qisedyylnk lsfgeiseky qvsrylinky lteavktgvv kieiastasr
       61 nsqleqvfke kfpetscyii qddttatate ellsnysanf vikhlekdph ivgmtwgetm
      121 yslidaitsn pldqvkftqf vgenmkynst agsvrivera akkvageflt lpaplylsdd
      181 tirnglyeaa sikrtldvak qmdtiltglg tiaslesiai wnqnlnllfp dvrlgevagm
      241 vygrpyding nilntesdkt vglslntilg vkkrigvvrs kskasaaiga lrgklltdli
      301 mseslayril nqeegi
//
LOCUS       WP_010692046             191 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Fructobacillus fructosus].
ACCESSION   WP_010692046
VERSION     WP_010692046.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 191)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..191
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21450
     Region          41..182
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mveketcvsn dikyegpifk idsrwvklfd gslaqrdvvt rgpavgilpl idedhavfvk
       61 qwrepvqdfv leipagkvda rdhgdiktac reaairelne eirihpgkle afadgfeavg
      121 ftdskialyv atelthldga nqlprdegey ldvvtisyde mtslyeagql ndlktitayf
      181 hwtirrlkng q
//
LOCUS       WP_010692162             177 aa            linear   BCT 01-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Fructobacillus fructosus].
ACCESSION   WP_010692162
VERSION     WP_010692162.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..177
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=19281
     Region          6..170
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mdaftsrvrr tigidglist iigafitiwp eksasfvagm igfaffaigv skllvsirdt
       61 eqgrsnriig iimsilymva glfifldlet atlsllvvvg vftgltwaie gvvqmtiinr
      121 wgsnrvwpfi salisflagl tlvfspffgg lllweflgim llvvgivklv qfatirq
//
LOCUS       WP_010692196             494 aa            linear   BCT 01-JAN-2025
DEFINITION  RHS repeat domain-containing protein, partial [Treponema
            denticola].
ACCESSION   WP_010692196
VERSION     WP_010692196.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         <1..494
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          <1..376
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 agtryyryda ngnitaekdg kfsdkeeltf tysyfaehdv ygvdygfdle ppeddpanle
       61 sggttsttpt ggyrrdytwn ernlliksdd klntviyryg ddgqralkft qqsnsetlyf
      121 nnfysvhqva hepnhehglr vskhifvgns rlvtamthad nngdtteqte kryyyhadhl
      181 qsaqfitnak geqyehieyt pygelwieet apgidklpfr ftgkemdeet glyyygaryl
      241 dpkysrwlsg dpalndyipk apiddeakkh nenlpgmggi yntinlhvyh yagnnpvkyt
      301 dpdgreienl dpsqeaklle niinvagtgf yfennklkfd ssskasgkys qtardiliag
      361 iasskttyvl paspekiqel lpdaygelgf arrvsgepgn tvgvymidvp ttqaaidyln
      421 ntfnctpsea delgfihevl ghaicdmgip gynsktdimk ierkireelg wkgvsrslks
      481 eeadltglff rirk
//
LOCUS       WP_010692126             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Fructobacillus fructosus].
ACCESSION   WP_010692126
VERSION     WP_010692126.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..279
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30829
     Region          26..274
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 msnkskiina lvllvvlvlg yfsfvqpnqk aqktvtigvm aankqddaiw sqvsktaksk
       61 yginlkfkrf tdysqpnkal engdvdlnaf qhyafldayn sknhsnlkai gqtfiapihl
      121 ysksyhqvsd fqdgdtivvp ndasnesral yvlknaglie lssgsnlktt kditknpknl
      181 kikeisadqt artlgdaqgv vvngnyataa glslkdaift eplnkdakmw iniiaarskd
      241 knnktyqevv kafqtkevkq aiheqygdse qaawdknfn
//
LOCUS       WP_010692197             413 aa            linear   BCT 01-JAN-2025
DEFINITION  RHS repeat domain-containing protein, partial [Treponema
            denticola].
ACCESSION   WP_010692197
VERSION     WP_010692197.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..>413
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          <147..376
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mkisycriqp nylfsrtaia reqkqfikia favhlsavis aeryrsdsva lksavsvfvy
       61 fysvlmvhky wqsakrklll nsptdrtfen rwsrykepsk nkaeayrvyv ehlflrsdag
      121 darifskevi hdglgrinyt akegevyidg tdyqtqtgwn vsgavyyded grkkgegqpv
      181 fyggdiqnel sgsssqilly eklnelkhpt syeydglgrv ikttlpdgni qrneylidss
      241 lqitkttdpk eniniskkdi rgnikeverr dknntlltka ryeysvlgem lkaydakdnl
      301 lavnydmlgr rislesldmg rkewnyddkg rleyendsvl rsklasikye ydgldriiki
      361 dypfsedvey eygaagekga gevirkkdet getmysygll nevkvetrti krg
//
LOCUS       WP_010692198             433 aa            linear   BCT 01-JAN-2025
DEFINITION  RHS repeat domain-containing protein, partial [Treponema
            denticola].
ACCESSION   WP_010692198
VERSION     WP_010692198.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         <1..433
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          <106..305
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 ggyrrdytwn ernlliksdd klntviyryg ddgqralkft qqsnsetlyf nnfysvhqva
       61 hepnhehglr vskhifvgns rlvtamthad nhgdtteqte kryyyhadhl qsaqfitnak
      121 geqyehieyt pygelwieet apgidklpfr ftgkeldeet glyyygaryl dpkysrwlsg
      181 dpalgeyipq apvndeakkh nenlpgmggi yntvnlhvyh yagnnpvkyv dpngekildv
      241 sttlvqenge edplgkgntt iashgcvlta ytrianaisa igertlqnan slalkkdiyd
      301 gnnknlifns ptasklvnsi silseykmsf ykslnnisln eygselekls ksedlyaiti
      361 rvsnkygght vnmnsdgiiv dtednytiki nntsekgylp stvvndiitd ssaiiridif
      421 kiekvktvpf lpe
//
LOCUS       WP_010692250            1057 aa            linear   BCT 01-JAN-2025
DEFINITION  RHS repeat domain-containing protein, partial [Treponema
            denticola].
ACCESSION   WP_010692250
VERSION     WP_010692250.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         <1..1057
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          <51..929
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 gsgktmafen rrgkykelgk kvpqayrvyv eetflpcdav iarifskevi hdglgrisyt
       61 akegevyidg tenttqtgwn issaiyydra grkteegmpf fyggnlesdl knalsyeaie
      121 qfyelnnftt irngtkyeyd didrniltvl pdgntqktey sidaslqitk atdplenisi
      181 skkdargnir everldknns lltkakyeys vlgemlkayd akdnllavny dmlgrrisle
      241 skdtgkkewi ydekgrlyae tdsvlknkaa eiryeydgfd riiktdypfs rdieykygap
      301 rqngtgqivy kkdetgethy sygnlnevik etrtinryga gtnpetasfe yrsdylgrmq
      361 smkypdgeti tytydkggql kgvsgvkttn kgsikysyvd kilydehsqr vyikygngve
      421 trykydekrr wldsietknv qtqdvfqkik ynfdavgnvl gyandastye tsqsytydnl
      481 yqlisvegts nqykgkksfg atpvsiakyk qtfsfdaign mkeklsttni pgsqgnsypk
      541 aeldynlnye ydpayahrli hastryyryd angnitaekd gpftdeeefv ftysydpetd
      601 vygtdygfgl dapketeqan pqdlfayrrn yiwnernllt kssdrnftvh yrygddgqra
      661 lkytdegrse tlyfnnffti hiptqdqnnp qglrvhkhif vgnsrlvtam thtdnsgdne
      721 eqkakqyyyh sdhlgsaqfv tdwkgrqyeh ieytpygelw ieevaagldk lpfrftgkel
      781 deetglyyyg aryldpkysr wlsgdpalnd yipqapvnde akkhnenlpg mggvfntvnl
      841 hvyhyagnnp ikyvdpdgek ildvsttlvq engeedplgk gnttiashgc vltaytrian
      901 aisaisertl qnanslalkk diydgnnknl ifnsptaskl vnsisilsey kmsfykslnn
      961 islneygsel eklsksedly aitirvsnky gghtvnmnsd giivdtedny tikinntsek
     1021 gylpstvvnd iitdssaiir idifkiekvk tvpflpe
//
LOCUS       WP_010692292             273 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Treponema denticola].
ACCESSION   WP_010692292
VERSION     WP_010692292.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10470251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..273
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31185
     Region          3..267
                     /region_name="TatD_DNase"
                     /note="TatD related DNase; pfam01026"
                     /db_xref="CDD:425997"
     Site            order(6,8,130,155,205)
                     /site_type="active"
                     /db_xref="CDD:238617"
ORIGIN      
        1 mytdahvhil dtieklnsqn iegpilktfd reiffcasan eagrfeiqek icrensehfi
       61 lsfgihpqcp iedeipylek lltekriaai gecgfdlfde hykstleaqk kvwdvqlnla
      121 qksnlpivvh crkglhlifd dvktlkkvna vifhgwagsv tearsflkkg inayfcigkg
      181 llrgqkaqle taatlekdri ltetdapyms lkeenfsltt dikkvfsila elraksagfl
      241 nydektykny teelkdsife nfkkaynirf dgn
//
LOCUS       WP_010692297             137 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Treponema denticola].
ACCESSION   WP_010692297
VERSION     WP_010692297.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10644999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..137
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=15623
     Region          64..125
                     /region_name="DnaJ"
                     /note="DnaJ molecular chaperone homology domain;
                     smart00271"
                     /db_xref="CDD:197617"
     Site            order(93..95,107,110..111,114..115)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 msknyyndmg nilrdaltsd edpfeaaaqr sngryrtmgg rmerrpppkv dkeairvpvp
       61 pelvedfavl nvlsgvplde ckrswkrlik khhpdvqssp skqaeanvii rrinnsyrki
      121 etwfktgkil sekdlns
//
LOCUS       WP_010692321             281 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Treponema denticola].
ACCESSION   WP_010692321
VERSION     WP_010692321.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..281
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30267
     Region          1..279
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mkgkllsffy ivcgvlmias gihffllpsk lslggatgma lvlskylpls tgallvvvni
       61 flfalgflii gnkfglktvc aslglsgavw lleifvplqg pivsdkflql viavilyggg
      121 vgivlnqyas tggsdifami lqkyfgldlg kgclitdfti tvfagfaygp eialfslvgv
      181 iinglvidst idglnmskyc vintdkpdel crfmvelgrs anvykatgay tkiersviqt
      241 vmsrrdfvkl ksylaandpe afmvvtnahs vfgwhwrrig e
//
LOCUS       WP_010692346             662 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Treponema denticola].
ACCESSION   WP_010692346
VERSION     WP_010692346.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..662
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75659
     Region          2..645
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mnefteglnp eqfkavttin gpvliiagag sgktrvitfr iahmldkgip qsqilaltft
       61 nkaakemadr ikeltgkklq nltvstfhaf gvkvlrshid kigwrsnfsi ydetdrnqli
      121 kecgrelkfs adaldvykvg ilfsnikmgr kdwtnehdsy kalykeyqdg lklynavdfd
      181 dlimlpikif kehpevlaey reryryimvd efqdtstqqy nfmkliadkn icvvgdddqs
      241 iyswrgasfe nirnfekdfp emieikleqn yrstgtilaa angvishnvn rkvkalwsek
      301 dsgrpieifi peneaaeadf isdmilslkq regfkysdfg vliranslsr pleesflevn
      361 ipyrmsggts ffqrkeikdl isylrvvanp dddvnllrii ntprrgigkk tletlsalat
      421 enscsmrtai rlllespped mrgksiedlk efaelisahr tqllsgkgla qkvrkllddi
      481 ayneyliaey qksekaaqfk mmniesflhs mddwennpdn ldgslydyln ritlltrddt
      541 eeekgevnim tihsskglef pvvfiagaed glipharsve endgdveeer rlfyvaitra
      601 qqklfitscr qrrkqggite capspfldei padlvqyhep daqaeeeria difsqmkkkf
      661 si
//
LOCUS       WP_010692396             131 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Treponema denticola].
ACCESSION   WP_010692396
VERSION     WP_010692396.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..131
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15103
     Region          45..121
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mkktcifltf llmvifsasc ntkstenitr mdgsrletil ndeterekyl vidvredyey
       61 kaghvpyain isvqeiesri seisdwkekn vvvicrsgrr srtaaeilvk ygfkkifdad
      121 gvskynykle k
//
LOCUS       WP_010692405             695 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Treponema denticola].
ACCESSION   WP_010692405
VERSION     WP_010692405.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..695
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77944
     Region          4..688
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mdktfvsdle fenqewacli rssdadakii dieipdlpeg fsffsakdiv gknsisflkt
       61 eipvfadeki eyagqavgil tgpdkkklle lsnlfqiktq ylsrpkaqft feeeeknyfd
      121 ypivsresls sgnaeevfek ssqvvystfs fkqryhyhae tacvktnwvd drleihlatq
      181 wpyqvltsvc nvldvpkeki nvvshaeaes ldgriwfpal laaqvsvasf ltkknivief
      241 srqedflytv ktpivmiqhk tsvselgkit amdvsiivds gsfnpfitqm lkqmvvtaag
      301 iyhlpvymis avaiktekgl tglfsgwgds yvssalekhi seiveqldlc piqfrlqnnl
      361 kvgqktitgi kkeedfvfen ilkavcntsd fyrkfyayrl mnksrkdryd gnwrgigvav
      421 gcqynglhil vksgmnysae itltkddkvl vkadptsegl krilkkqiak elevednqiv
      481 flgastdemi ptgaatascg isilpgliek cctgiknqrf rkplpitvsk tyklprskdw
      541 dnetltgnpf isetpgacvi eleldpstyq iivrgiwfac dpgkiyskkm vhrnihktia
      601 navsnisved irennllpsn ykiiatgaip pirdfildse lktrglgela eslvpaayis
      661 alnqiminhk ridflpvfte difnavtkse avded
//
LOCUS       WP_010692425             309 aa            linear   BCT 01-JAN-2025
DEFINITION  SPFH domain-containing protein [Treponema denticola].
ACCESSION   WP_010692425
VERSION     WP_010692425.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..309
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34363
     Region          1..275
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mialyialvi tviilfsiav vvpeqesyvi erlgkysrtl tagfhiltpf idriaykqnl
       61 keealdvdpq vcitadnvqv qvdgilylki fdpvkasygi dnyryavaql akttmrseig
      121 kmeldktfcg reglndnivk aldeasdnwg ikvtryeird itptrtilea merqmraere
      181 kranilsseg kqqsrinisl gkkkeainka mgekqrrinl aegrskaiei tsnataeglr
      241 liadalsqpg grtamgirla enyiqrfehi ikksnvsvyp eniaglaaft diiknagkev
      301 kviqggqna
//
LOCUS       WP_010692426             305 aa            linear   BCT 01-JAN-2025
DEFINITION  SPFH domain-containing protein [Treponema denticola].
ACCESSION   WP_010692426
VERSION     WP_010692426.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..305
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34128
     Region          22..285
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mlnfiipivi aaviaivfiv alfrsirivp hkialiverl gkyhttldag fhilfpfldr
       61 vkykqnlkeq aidvpaqdcf tkdnvqvrid gilylqvfdp ikasygirdy ryatillaqt
      121 tmrsvvgqld lddtfeareq inaqvvkavd easdpwgvkv tryeiqnirv sdsimdamen
      181 qmkaerekra eiarsvgeme tvinlsraay eeavnisege kermineaeg qareivavae
      241 atadgikkia astqiqggme aakltvsqew inalssidek tkiimsadft dikkmtidma
      301 eeiik
//
LOCUS       WP_010692515             371 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Treponema denticola].
ACCESSION   WP_010692515
VERSION     WP_010692515.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..371
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=41095
     Region          35..350
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mfkksifllf lafymllafs cqpaikeysk twlslgtvcr vriltsepkk kveevlekvy
       61 aeltkldsif nantdkisae nnnlkglttv neselerlnk eagifpievs pelyellqis
      121 lmiaeltdga fnpaigplvk lwnigfenet vpsqkeidei lplldyknie lkagnqvflq
      181 kkgmrldlgg iakgyaadki akillehgik dflidlggni lasgknpsgk twktalrnpi
      241 igkqnpvism nlqdaslvts gnyerfiekd giiyhhifds ktgnpvhnnl nassiisess
      301 tladalstss yvlgeektra llqklvtvdf pligkpkmpa cilfykdnsi svfgndgisi
      361 eiidqnffik k
//
LOCUS       WP_010692519             422 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Treponema denticola].
ACCESSION   WP_010692519
VERSION     WP_010692519.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..422
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=48161
     Region          2..402
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mqkeivktkk mvfgascias lkdgktvfvp yslpdevlei sivkehknyt egkiekilea
       61 sphrveprcp yfyvcggcni qtaddeyqhf lrksmaleal dralglykek vvfekpalek
      121 sffektifvs gsdwdyrarf qfyidedgsl slkenkssgs vkikdcpiav pairnllrsn
      181 lkeytpnsri hifsdgekif tqdnakdcev rlagkrikfn plgffqsnle mteklintif
      241 eyaeisssvl dfysgvgtfs lfaydqakei hlvehnkhal ayaqenflin sssneivrek
      301 kengspkify haldgknwak tkesklkfdt vfidpprsgi dkealswlcs sgtrqifyis
      361 cdpvtfardt asllvsgykl ekhflfdfyp qthhietlgi frkdgdnrlc cykpqkiigc
      421 nv
//
LOCUS       WP_010692544             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010692544
VERSION     WP_010692544.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..190
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20438
     Region          29..120
                     /region_name="HTH_GlnR-like"
                     /note="Helix-Turn-Helix DNA binding domain of GlnR-like
                     transcription regulators; cd01105"
                     /db_xref="CDD:133380"
     Site            order(31..33,47,65,68..69)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133380"
     Site            order(81,84,88..89,101,104,108,114,118)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133380"
ORIGIN      
        1 mveeasnraa aaeqgelfpd aalpdelvgy rgpaacqiag ityrqldywa rtklvgpsir
       61 saagsgsqrl ysfkdilvlk vvkrlldtgv slhnirvavd hlrnrgvqdl arltlfsdgt
      121 tvyectsaee vvdllqggqg vfgiavsgam reisgtihdf paeradggel vppvddelsr
      181 rrrdrqaetg
//
LOCUS       WP_010692551             289 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010692551
VERSION     WP_010692551.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..289
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33012
     Region          7..244
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 misddvlkie klkfsigrgk ktfslndisf svprgcvtgl igengagktt lirllldmyl
       61 pesgkiflfg eelkrdniei kekigfvind nffsplytak kagkflagiy tnwnqelyek
      121 ylndfkipps rflaalssgt mqklqiaial shgaellild eplnfldpvs kkefldllrn
      181 fmldenhsil isshqtnele kicdeiifis egkkvfdssl eninknygll kmdekafksl
      241 ysndyigyrk tdyayevlvs dkrnqkftgm vcedasledi myfytrrki
//
LOCUS       WP_010692565              82 aa            linear   BCT 01-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Treponema denticola].
ACCESSION   WP_010692565
VERSION     WP_010692565.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..82
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=8500
     Region          1..65
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mptyeyvcds cghdfevfqr msdepvsvcp ecgkpvrrvi sgglginfrg sgfyvndsss
       61 asktasggcs gcsssscstc kh
//
LOCUS       WP_010692597             305 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Saccharopolyspora spinosa].
ACCESSION   WP_010692597
VERSION     WP_010692597.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..305
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32491
     Region          28..273
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mvgvmssnve dvlvigggaa glnaalvlsr arrrvlvvds grprnapahq vhgfvsrdgt
       61 ppsellaigr eeveryggrv vagdvravrr dddgfevela dgvvrarrvi vatglrdelp
      121 dvpglrerwg rdvlhcpych awevrdqpfg vlgwqpgavh qallarqwsa dlaffaedlg
      181 dedraklvtr gvrivdgevs glvvendelr gvrladgtie alsalfvpar fvpndtvlse
      241 lgcelgddgw vrvdpsglts vpgvwavgnv vdpraqvvna aaggakaaaa vnwdlieadm
      301 levar
//
LOCUS       WP_010692602             255 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Saccharopolyspora spinosa].
ACCESSION   WP_010692602
VERSION     WP_010692602.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..255
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25955
     Region          36..248
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mpsasipvtp algvaialll vaaaavaglg glaryrdvlf aglrgavqll vvslliayiv
       61 rwtalaavfi almfaiaaht agrritsdrt wlwaglpiaa gvapavlvlv vtgavpltgl
      121 vliplvgqli ggalvatala grrlldelqq rrgevdaala lgmvdraarl eiarplagsa
      181 lvpaldqtrt vgtvtlpgaf igmllggatp iqagivqlyv lvallavesv ailvvleiva
      241 rglltrsgth lffrs
//
LOCUS       WP_010692615             244 aa            linear   BCT 01-JAN-2025
DEFINITION  (Fe-S)-binding protein [Saccharopolyspora spinosa].
ACCESSION   WP_010692615
VERSION     WP_010692615.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..244
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26077
     Region          <2..237
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrvalfatcl gdamfpaapk atvqilerig cevefpaaqt ccgqmhtntg yrkqavssvr
       61 tfvdafgdyd avvapsgscv asvrhqhamv adgdkrlsra variapqvhe lseflvdtlg
      121 vtdvgayfph rvtyhptchs arllrvgdkp lrllravrsl elvelpaadq ccgfggtfal
      181 knpdvsvamg adkarhvret daevlcagds sclmhiggll srqrsgiqvm hlaeilaste
      241 gtdr
//
LOCUS       WP_010692676             180 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010692676
VERSION     WP_010692676.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..180
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20135
     Region          1..86
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          92..176
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 msleyailvs lqeragsgye larrfdksig yfwaashqqi yrslkrmvel dwvscdevaq
       61 dkrpdkkvyr vgeagaaela rwlakpvdpp tirnelsvki rgacvgdvdg vveevarhrq
      121 lhsqrlaafr alerrdfpap eglsgqqlhq hlvlrggils eeamvswlde altvlradlg
//
LOCUS       WP_010692690             391 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010692690
VERSION     WP_010692690.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..391
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42617
     Region          7..389
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mkhwndsltd dqkmflrtva dacshfdday wsrheeehcf peeffktmag mgivgmlipe
       61 eygggggsle daalalqtva asgaglngcs gihlsmfgfh plvmhgteel kqrylpqvav
      121 geihiafgvt epnagidtgq vstravrdgn dwritgrkvw mtkagfsdaa lvlartrpte
      181 etkrpidgls lfvvdldrey veaspikkmg rnavasyeva fdglpvpskn lvgeegrgfh
      241 alldglnper vlvaaeaigi giaaverasr yagervtfgq pigqrqgiah pladaymqll
      301 aanhvmldaa rrydtrqpcg lqantakfla gragffaadr avqthggygy aseytverlf
      361 revrltriap ipeemilnfv aeqelglprs y
//
LOCUS       WP_010692708             239 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010692708
VERSION     WP_010692708.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..239
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26720
     Region          1..228
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mstadaaaeq yanlrrlile qqlkpgtlll etalaarfgv srtpvreala rlaqeglitk
       61 qkrgyvvdel speeiievfd vrillectav ekaatdcddf rlahleqlte qldeliatls
      121 taidngdtdk qtaigdeila anvrwhealr agsrnrtlir minqlmdvqk iynplmkvhd
      181 laeiskgqqq hhelvaalrd rdparareim adhltrvrqi rvaefarslh aterrggss
//
LOCUS       WP_010692713              67 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Saccharopolyspora].
ACCESSION   WP_010692713
VERSION     WP_010692713.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora
  ORGANISM  Saccharopolyspora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Saccharopolyspora"
                     /db_xref="taxon:1835"
     Protein         1..67
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7177
     Region          1..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 maqgtvkwfn sekgfgfiap ddggadvfvh ysaidargfr sldedqkvty evtqgpkgpq
       61 asdvriv
//
LOCUS       WP_010692771             454 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Treponema denticola].
ACCESSION   WP_010692771
VERSION     WP_010692771.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..454
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49958
     Region          23..448
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mklkfigqtt aqrrelilta splktliils lpalmmamlq ammpftdglf inrltdhvta
       61 savsfsqpii fivlalgqgl svgataiigq lngrgdides kkvatqifvf sfllgiasip
      121 llfiigtiis ytlkseiapl vfryislycf vmplsfmeai yngiknangk peapffrmii
      181 mliikiignf iflyifrmki dgcvlaslla nmvvaawmfy dlflkknpdk lslknfkfss
      241 ptlkellhvg fpaminyafv ylgfflinre mepygaviln gqsiasnist icfnipgcfs
      301 aavttmvsmn igsenpkkak racllgcits aisgavliav ivpssanlvs mfkpempeig
      361 diavkalhiy tysvigfgic mtiqgafigl gktkiplmlg ilriwllryi filtteryls
      421 yysiywgnlf snltaglvai ililntkwvs gikk
//
LOCUS       WP_010692798             489 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Saccharopolyspora spinosa].
ACCESSION   WP_010692798
VERSION     WP_010692798.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..489
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49364
     Region          21..455
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,144,
                     147..148,151,274,277..278,281..283,286,314,318,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mttavalrsq pgrwilvati lgsgvafldg svvnvalpai grdiggdlsv lqwvldayll
       61 tlsallllgg algdrygrrr vyvlglvlft laslgcglap ggtalivarl lqgvggallv
      121 pgslalinsa irhddrgeav grwagltgms saigpfaggw lvdaaswrwv ffinvpiaaa
      181 allalrhvpe srnpaaagrl dvfgaiavtv glagavyali eiptkgldav sagaavvgvv
      241 alvafpliel rhpdpllpls lfrsaqftga nlttftvyaa lsgalfllsl qlqqsmgypa
      301 laagiatlpi tiimllmsgr vgalaqrtgp rvpmtigpli cavglalmtl avpgstylsg
      361 vlpgvlvfgv glsitvaplt savlasvspd nagvasgvnn aisrlaglla vavlpviagl
      421 shtgagaplg pgfgramlis aamcaaggvl awltidrark vdayplpgvn hacqdpctcq
      481 fgknrdqat
//
LOCUS       WP_010692821             220 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Saccharopolyspora
            spinosa].
ACCESSION   WP_010692821
VERSION     WP_010692821.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23705
     Region          26..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtaaaapnpa skpqdrrhrr tmrthaaiea aalrlfaeqg fahttveqia eaadiaprtf
       61 frhfpskdav lfgepaldae rmrevlasrp asehpmrsla aalldaaera eldraqhlmr
      121 aelldspqda gdyemylikq rsvqdmadlv aersgtgtdd prtvawsivl mscfgsamhs
      181 wlvctdgtpl reilaqvlde tagglaqaad vvgsaikdag
//
LOCUS       WP_010692906             470 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Saccharopolyspora spinosa].
ACCESSION   WP_010692906
VERSION     WP_010692906.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..470
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47090
     Region          5..429
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(12..13,16..17,20,52,102..103,105..107,110,131,
                     134..135,138,253,256..257,260..262,265,293,297,349..350,
                     354,358,374,377..378,381..382,385)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mlvvmcagmf lvlldvtvvn valpsirgsl gvgiagaqwv vdgyalaiag lllvsgmlgd
       61 gfghrrvvla gmvlfgvasl gcalapglgv lvasravqga gaalllpgsm aviagvypds
      121 aararalgvw savsslalpa gpllggalve wggwrlvfal nvpvvlaavv gvrmlvpdlp
      181 gdrgrrvrig vlasavsglt avvfavieag qsgvdvlvla alvvavialw vagrripral
      241 lgnrpflaan svallmnlgm ngtlfvltly lqnlggnspa rtgllllpms vplvllapva
      301 gwmvarfgpr vpmlcgaviv aagsgfwgla spdggyaeva pvlvacgvga gllttsvvaa
      361 avgalgpqrs glasgvnntm rqtgtalgva vfgavagsps apadftaglh qlavvgvllw
      421 lvaitfsvla gnsaqstqra tdrvpaarcg rsrrrrpvlr agrrarsrrg
//
LOCUS       WP_010693039             223 aa            linear   BCT 01-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Saccharopolyspora spinosa].
ACCESSION   WP_010693039
VERSION     WP_010693039.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..223
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=23392
     Region          9..219
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mrrsatltpp llliahgtrd pdgprvierl adaaahrlrv pvhvayvdvi gptvaealse
       61 vdgpvvalpa flaagyhvrt dlpeqitasg redvavsapl gpapeiieam frrlvaagwq
      121 pgsqvvfaaa gssderalsd vraaarmlgr rvgqwltpsy vttaspttae vcgpadyiap
      181 yllapglfhr rlaelpvagv aepigahpdv idliarryrl agg
//
LOCUS       WP_010693023             963 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Saccharopolyspora spinosa].
ACCESSION   WP_010693023
VERSION     WP_010693023.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..963
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=103886
     Region          1..524
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          466..959
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 matsfddlaa elrgalsgpv rfdpgtraly stdasnyrqv pigvvlprte ddvtaavava
       61 rrygvpitgr gagtsiagna vgpglvldfs rhlnrildid perrlarvqp gvvldslrsa
      121 vaghgltfgp dpsthsrctl ggmignnacg thsvawgktv dnvhsldvll adgtrlqlga
      181 tspteldrlc trgdrtgrly qelralreda gdlvrrsfpd ltrrvsgynl dqllpengfh
      241 laralvgteg scavvlgatv qlvpsppvra mtvlgfpdty aaadevprlr gldalaiegl
      301 saelvdvvrq rnpgspalrl lpvgrswllv esggadqgea eaaanriaea mgtraesvih
      361 tvparmaalw kireegsgys trmagserwp gwedaavppe rlgsylrefd allarfgrrg
      421 vtyghygdgc ihvridfdll sspgateyra fleaaadlvv ahggsvsgeh gdgqarsall
      481 srmyppevid aferfktafd pverfktafd pddllnpgqi vrprpvdadl rllvapprlp
      541 srttlalhad sgdlaaatrr cvgmgkclnt tggvmcpsyr atkeekhstr grahllfeml
      601 agrvvrrgwr spevrdaldl clsckgcksd cpvdvdmaty kaeflhhhyr hrvrpashya
      661 mgflplwlrl gqrvpklanr vlagplapvl krlggidarr avpelapqtl qawwsrrrpi
      721 vntttrvvlf pdtftnhfdp qigrdavaal ealghtvemp repvccgltw hstgqlgiar
      781 smarrtahll rpridqglpv vglepsctaf lrndalelap hdpdvaalaa atktfaewve
      841 ptrsqwrrae sgpealvqvh chqhaelgfa adqatldatg trarvldsgc cglagnfgfe
      901 rghydvsiac aeqallpavr aadpgteiva dgfscrtqlr qtsetepvhl atlvaralnv
      961 sgs
//
LOCUS       WP_010693041             271 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Treponema denticola].
ACCESSION   WP_010693041
VERSION     WP_010693041.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..271
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31013
     Region          12..>267
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 midrneeqnf nklseviney nklqisqqld ydkfylysii thstaiegst vteienqllf
       61 degisankpi heqlmnldlk aayeksfela kqhtqitpei lcelsalvmk ntgtvyntig
      121 gtfssakgel kplnvsagrg gksymawqkl pqkleefcvw lnserksiae kdieaqyafs
      181 flthyklvym hpwadgngrm nrllinfvqy eagiipsiik kenraeyiqs lassqekddp
      241 aeflhfmfsh hirnlseqie eyktslemsg s
//
LOCUS       WP_010693056             446 aa            linear   BCT 01-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Saccharopolyspora
            spinosa].
ACCESSION   WP_010693056
VERSION     WP_010693056.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..446
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45747
     Region          19..439
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mrqglgaklg igwklhgdgs tprpgetvap derlswgrtv glgaqhvvam fgatfvfpvl
       61 mgldpnlaim vsgvatilfl livqgkipsy lgssasfvgv vtviragggd sstvtgailv
      121 lglvlsvvgv iihfvgpqvv hrllppavsg avvmligfnl apvvaesywp qdqwialitm
      181 ilvlgcsvll rgfwsriavl iglvagyals wlfdlgfgpi tapnasgvvs thfrldlsgv
      241 adaswfglpt lhapsfdaaa iivvlpvvia liaentghvk aveemtgtkl dgslgraifa
      301 dglastlssa vggpptttya enigvmaatr vystaaywva aivailfglc pkfgaviaat
      361 pggvlggitv vlygmigllg akiwtenrvd lgdpvnlmpl aaglvvgigg vslqitpqfs
      421 lsgialgtvv tllgyhvlrl lvparr
//
LOCUS       WP_010693059             432 aa            linear   BCT 01-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Saccharopolyspora
            spinosa].
ACCESSION   WP_010693059
VERSION     WP_010693059.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..432
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45814
     Region          3..428
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mtsthseltk rhravlpdwl tlyydepidi ergegrhvwd aegnryldff ggilttmtah
       61 alpevtaavs aqagqilhts tlylnrpmie laervaelsg iedprvfftt sgteandtal
      121 llatgyrasn qvlalrnsyh grsfsalavt gnrgwsptsl spvqtayvhg srrrgtplad
      181 lpdeeftaac vsdledvlgq lhgnvaclia epiqgvggfa tppdglfarf kevldrqgil
      241 wisdevqtgw grtgehfwgw qahdangapd ivtfakgign glsvggviar aeimnsvran
      301 sistfggspi taagalanld hllandlqgn aarvgavlre eldgalgrip tvvdvrgkgl
      361 migvelahad gtpapeiate vlesarrrgv ligkggldgn vlrvapplsl teaeareggq
      421 ilvaaleeag rr
//
LOCUS       WP_010693111             283 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Saccharopolyspora spinosa].
ACCESSION   WP_010693111
VERSION     WP_010693111.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..283
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27995
     Region          <79..228
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mtataavttt artsaplgrv lvaelrwvlr rprnllalll laglpvllgt aiavtggpgs
       61 rgggsilaav agnglvlpva alvlaqslll plvvamvaad alageashgt lrglllapvg
      121 rvrlvgikaf gvlvlavlav tvvavsgvlt glvivggdgm vtlsgttlpi gsalgrvala
      181 agwsavqmaa vgavalaiss ltehplvvma atlgglivfg vlgtipaldw lqpvlittdw
      241 savmdvlrdp msgdtlvtgl fragcyllig lsatiarvvt kda
//
LOCUS       WP_010693182             261 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010693182
VERSION     WP_010693182.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..261
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27772
     Region          13..255
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mhnndkivat seprtqtqav dralsmlvll aqrgpsgvte larklgvhks tasrlmtale
       61 khrfveqvgp rgryrlgfgi vrlagataaq ldiagesrpi carlaselrg tvslsvfegg
      121 gatavvqeps ternwiglrv plhatasgkv llasfgfeel edamkqplrr ftthtvtsrg
      181 alladlnrvr argwaaasge fepdlhtvav pvrgpggria galsvsadea hlrpadfqgi
      241 sriltqaaee ihdrlqslag p
//
LOCUS       WP_010693203             204 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Saccharopolyspora spinosa].
ACCESSION   WP_010693203
VERSION     WP_010693203.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..204
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22178
     Region          42..204
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mmtihenddr hlfdaipaid fdaskrlhie lvnaaqregl ldvayrtint pvgelllaat
       61 erglvrvafa rqghdevles laatispril rtpdrlekva rqieqyfsgq rrtfdlpldw
      121 rlsrgfrlnv lshlpdiayg rtasyaevav aagspravra vgtacatnpl pvvvpchrvv
      181 rsdgtsggyv ggveakamln leaa
//
LOCUS       WP_010693207             208 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Saccharopolyspora spinosa].
ACCESSION   WP_010693207
VERSION     WP_010693207.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..208
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=22705
     Region          18..203
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mspaaadttt dagvvigedg larppwaard pllreyydte wgmavrgeqa lferislegf
       61 qaglswatil rkrpafreaf dhfdpdavaa yteddvarll dnsgivrnka kiraaignar
      121 atielraddg leafvwsfkp dttprprtia eipttspesv slskalrrkg fafvgpttmf
      181 almeaigmvd thlvdshrrg tsgiwpqs
//
LOCUS       WP_010693250             312 aa            linear   BCT 01-JAN-2025
DEFINITION  permease [Treponema denticola].
ACCESSION   WP_010693250
VERSION     WP_010693250.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..312
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=34375
     Region          1..289
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mlslitttnt iflsillqaf pfmllgivis silhvfisdn fivkvfpsrh glgfltavfg
       61 glvfpvceca svpvlsglik kgvimpiavt fmlaapilnp isimatlyaf peypmiavyr
      121 iilgivtaat igilllfypk neylkedien dnhcscgcnc edscsashss gqrsfienlk
      181 emllhsgeef fnvgpyfilg alftslirag vpsnffiqfn esnslggili mmlfafifsa
      241 cstsdafiar sfygtfslfs imgflvygpm mdiknifmll sifkkrfvie ltiiitimni
      301 ifisamsfli ki
//
LOCUS       WP_010693263             167 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Saccharopolyspora spinosa].
ACCESSION   WP_010693263
VERSION     WP_010693263.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..167
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17645
     Region          48..142
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(63,65..67,73,96,98..100,102..104,107..108,130,
                     134..135,137)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            99
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 madrsnpeaq grlhmpfaef grtevpaprt ersaedlapk aeklslrttr papgviviea
       61 agildmnsat qfaeavrahl taatrtavld lsglsflstd gvvvlmeagh ralmrqanlv
      121 lvsqnrivdr llgilditdr ftyastadaa isaadatpal gepvsrl
//
LOCUS       WP_010693269             248 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF427 domain-containing protein [Saccharopolyspora spinosa].
ACCESSION   WP_010693269
VERSION     WP_010693269.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..248
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=28133
     Region          115..239
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 mtdntgeqpr iqrspkrvra ylrgrlvadt rgpmlvwehp yyptyylpae dvkatlrptg
       61 etrhidrvgd gdvhdvlvdg tvaegaavrf pdssaapnlv rlewgaldew feedepvyvh
      121 prdpykrvdv lassrhvtvr iggvvvadsh rplvlfetgl ppryylpltd lrtdllrpsd
      181 rrtqcpykgt atywnamidg tehadivwty rapfpesqki aglacfyder veitidgelq
      241 eqprtpfs
//
LOCUS       WP_010693275             605 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Saccharopolyspora spinosa].
ACCESSION   WP_010693275
VERSION     WP_010693275.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..605
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=67585
     Region          11..605
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mtpsqqpsgf lpiadhglig dlrsvalvgt ngtidwyccg rfdgpsvfaa ildadrggsf
       61 elaadvpart kqfyfpdtnv litrffaedg vgeiqdfmpi vddsreagrh rlirrvvcvr
      121 gslpfrarva prldyatcph tlrvegchai fesaslslal tasvpvepdg tdvwsafklh
      181 egevavfald qvggdvmprt cplaeaeref aatvrfwrqw lsasryrgrw remvhrsalt
      241 lklltyaptg aivaapttsl pesiggarnw dyryvwirda afcvyallrl gftaeaeafm
      301 gflskyvdlr hcdssgplqi mygidgrsel pereiphlsg ylgsapvrvg naavhqfqld
      361 iygalidsiy lydkwgapis serwdevvdv vdwvcanwdr pdegvwetrg grknflysrl
      421 mcwvaieram rlanhrglpa diprwrqard tiyrqimkrg wsdkrhafvq hedddvldaa
      481 vlmmplakfv sptdpkwlst ldalgehlvs dslvyrydpq aspdglpgte gtfsicsfwy
      541 vealtragrl eearlafekm ltyanhlgly aeeightgeq lgnfpqafth lalisaafnl
      601 dralg
//
LOCUS       WP_010693320             228 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Saccharopolyspora
            spinosa].
ACCESSION   WP_010693320
VERSION     WP_010693320.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..228
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24140
     Region          12..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprplipnrv gaildaaesl vlrdgfdgvt veriarragi gkgaiyrefg skrelmdall
       61 arcarrlvdq vrqrvveast pvglsaayrl givallddsl ltaaflddea vlgshmpavg
      121 gdryrqrfaw iteyvealhe agslasdaap eaisialssf tigllsassv lgpltrdqla
      181 aaldvvttli ergleslpda gapaandahl lllgrmagqf dadteehr
//
LOCUS       WP_010693344             196 aa            linear   BCT 01-JAN-2025
DEFINITION  DinB family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010693344
VERSION     WP_010693344.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Newton,G.L., Leung,S.S., Wakabayashi,J.I., Rawat,M. and Fahey,R.C.
  TITLE     The DinB superfamily includes novel mycothiol, bacillithiol, and
            glutathione S-transferases
  JOURNAL   Biochemistry 50 (49), 10751-10760 (2011)
   PUBMED   22059487
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Cheo,D.L., Bayles,K.W. and Yasbin,R.E.
  TITLE     Cloning and characterization of DNA damage-inducible promoter
            regions from Bacillus subtilis
  JOURNAL   J Bacteriol 173 (5), 1696-1703 (1991)
   PUBMED   1847907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..196
                     /product="DinB family protein"
                     /calculated_mol_wt=22149
     Region          9..160
                     /region_name="DUF664"
                     /note="Protein of unknown function (DUF664); pfam04978"
                     /db_xref="CDD:428232"
ORIGIN      
        1 maepgpksdl hlylrsarea llwkldglse ydirrpltpt gtnllglikh ltgcelgyfg
       61 itfgrpfdep lpwlthdaep nvdmwatade sreeivglyr rvcahsdati delalddagt
      121 vphwpddrkr itmhrvlvhm iaethrhagh adiirelidg atglrrendn mapgdqgwwq
      181 ayrdrlenva rqadrg
//
LOCUS       WP_010693449              64 aa            linear   BCT 01-JAN-2025
DEFINITION  ferredoxin [Saccharopolyspora spinosa].
ACCESSION   WP_010693449
VERSION     WP_010693449.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..64
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=6599
     Region          1..64
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mkvtidqdkc vasgqcvmaa aevfdqrded gtvvllnanp pvelaadvrq aavlcpalai
       61 tvde
//
LOCUS       WP_010693504             261 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Treponema denticola].
ACCESSION   WP_010693504
VERSION     WP_010693504.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..261
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29827
     Region          1..261
                     /region_name="COG3694"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:442909"
ORIGIN      
        1 mnglklyfky lgillkstmq ykasfflscl gqflltcnsa aalyflfarf qsikgfsfae
       61 vvfcysimql sfaitesyar gfdsfsalii tgdfdrlllr prnlplqvlg skfefsrigr
      121 lliavvlffy girfgnmdws flkvltvffm llggiavfsg lfliyaaisf ftiqslefmn
      181 iftdgartfa sypvsiygnk ilrfctfiip yalfqyypll flfdkyknpa laflpllsfl
      241 flipaylfwr lgvskykstg s
//
LOCUS       WP_010693525             706 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Treponema denticola].
ACCESSION   WP_010693525
VERSION     WP_010693525.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12036995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..706
                     /product="methyl-accepting chemotaxis protein"
                     /calculated_mol_wt=76364
     Region          45..282
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          <295..706
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mvaekiyqke girfsilrkl vfffgmlili ggftmgasal fvarnalmek ieealimkak
       61 dtaeivdgra nallyflegl aripalrdsk ltffekvkal qkdaernkti eyfgvsdkng
      121 iryspdgtsi fvgdrdwyke aikgrnfise plisrttgel qiifsvpiyd dehnilgvfs
      181 aavngldlnn liddiviget ggcyiidasg ttiadkdiel vkrqensikk avsdpelksi
      241 adfeqkalas seaglarfvy egqkeiaays pmktknwkvi isapvheltg slrplkitir
      301 ligisilivs iiltavialt ivkpitstvq alkniadgdg dlrvrlpikr ndeitdlsky
      361 fnktiekign siktvgsgtq emeqignela snmtetasai hqistniegv kqqaltqaas
      421 vtetsatieq iiktiaqlng miesqaasva esssaieqmv gnissitqtl artddaiknl
      481 agataegket lslsntvtqk iseesgglle assviqhias qtnllamnaa ieaahageag
      541 kgfavvadei rklaeesssq gktitstlki lskeienlss ssklaeekfd sifalseqvk
      601 kmseslmlam keqenggrev ltaihninli tsqvndgsae mleggkniav emqkldaltr
      661 vitasmnems agalqineat qevniisqkn kenignlvne verfkv
//
LOCUS       WP_010693577             489 aa            linear   BCT 01-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Treponema denticola].
ACCESSION   WP_010693577
VERSION     WP_010693577.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..489
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=54740
     Region          91..113
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          121..251
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          152..181
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          188..209
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(202..203,206,208..209,241..242,245,248..249,
                     272..273,276,279..280,283,303..304,307,335..336,339,
                     342..343)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          206..341
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          222..251
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          254..284
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          314..344
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mktlkkelnf flkigvlsll filsfavrlg aqeaaqppse nkaaqadekk kkevsefeek
       61 rdiilygigd dilelikrlk adeddrfdad lqkvfaetki pairealfty faekkndclk
      121 adalmllenk ddapqetvrs aisyirelei yegidflrqi lkdeqdeyrd lcisaigkig
      181 kpedavflte lfdsessdde kksliikqni mfaleelhtp eisdflirva edsdensiir
      241 gsaasalgki gnenavpvls elfedkdpvl rtaaikgiag fkdekaksil tqafkdsyyk
      301 vrlqavqsak eekaedavpf ilyrakkdpe nvvklaaiea lshfnnaean ewlidsfnee
      361 rtglsirlki aesllknnfd vifdgvkkaa lkaisdkkqn kfsaelgkvi skvenrgtap
      421 iaeaylnhkd pifksigldm fkrnrypelv slvsliaede kngalsrrak dllqsgntng
      481 sqnnqtgnk
//
LOCUS       WP_010693617             251 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010693617
VERSION     WP_010693617.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..251
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27500
     Region          1..246
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msqtvaraid iigfvsrqhr slgeiaehlg vhkstalrll qtleeggfvr rvsegygmgf
       61 qlialgqlal dqvearslah pvlqelseqy ghtvhlgelv ghqivyvdki dgrgsvamgs
      121 riglpalvht agvakiitay qdhdtraril dgvtferytp ttitdladle kdldvtrdrg
      181 waedngered yincialpvf dargkvthgi sitalravap leelrghidq fraaahrisk
      241 slgwrgdqyg h
//
LOCUS       WP_010693591             180 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Saccharopolyspora spinosa].
ACCESSION   WP_010693591
VERSION     WP_010693591.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..180
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=18915
     Region          3..178
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mitrvvlatd rgeihidade graplsagdf lryvrdgsya gglfqravtp qndngdpvie
       61 ivqaaiaega lprepldhes teqsgiahte gvvslprgrl gtgtaasffi cvadspgldf
      121 ggtrvadgag faafgkvvdg mdvvreihra ptlpdapvey lrgqlladpv eiravhivny
//
LOCUS       WP_010693619             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Saccharopolyspora spinosa].
ACCESSION   WP_010693619
VERSION     WP_010693619.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48037
     Region          17..429
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(30..31,34..35,38,77,135..136,138..140,143,163,
                     166..167,170,257,260..261,264..266,269,297,301,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtpsptsaaa ldsrgtrrvv iassigtvie wydfalyeaa salvfgplff peqsaiggal
       61 asfavfavaf fvrpiggmia ahigdrigrk piliftvtlm gvatvavgll ptyeaigmwa
      121 pillvltrml qgigagaefa gavtavaeya pqnkrafyts faqasvglaf vlstgffavl
      181 aaiprdalln gawripflas vvifgvaifi rrrveetpef ieakseiskp tteptkipll
      241 qaikgsprel tvgilcgsgl nvagylvntf slsyikttle msatvatlgv vaatgssiia
      301 vplfgiladr igrwpvllgg aiftaiympf yfmlldtrqs givvaamvia ygvgqsamlg
      361 sqsaflself etryrftaia asreinvmvl ggttpfiata mvgatngspw pvvlfvvasq
      421 fltivsvlla rrtrripgtg psnlqvrkie sqplt
//
LOCUS       WP_010693664             480 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Treponema denticola].
ACCESSION   WP_010693664
VERSION     WP_010693664.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..480
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51893
     Region          70..480
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mkalqyvrii fmilaiisis fiipigtaiy enetylipsf liptafvfav aavfffflrn
       61 kkvrlsvsgg iilvaaawia agilgaiplc isgvipnfad avfesvsgft ttgatiltnv
      121 eacpmtmhvw rtqmhwlggm givaltvalf pllgvggfql iksettgpdk gkvtakitht
      181 akalwfiylg mtvvqiillm iaglpfleal chtfaslgtg gfstrnasvg afnspsveii
      241 cavfmilagv nfslyfhlft ghpeeffhns elkaylkivf vstvliafsi ypiygiggcl
      301 rqsffqvasv itttgfstad ynawpefakm vlfflmfvgg csgstagsik virwlilqkq
      361 agmeakrlls phgvfgiqln nrpgrkdivy nvagfifcyf llslitalva aadgadllsg
      421 ftaslalign igpgfgrvgp agnfaffssp vkiffsfvml agrlelytmi iyfmpafwkr
//
LOCUS       WP_010693677             180 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Treponema denticola].
ACCESSION   WP_010693677
VERSION     WP_010693677.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..180
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20491
     Region          8..177
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mfngkgilra tsdedfraiy ealmpviykv aynivregdi aedichdsli kmtekkmefp
       61 siddakywli rvtrnaslnh vkrcgrerka yakalkedtr kvdtgeeivl kqesinsvqa
      121 aleklpknlr avlqlkeygs lnykeigsil gisegnvkvr vfrareqltk yigesdvymp
//
LOCUS       WP_010693783             271 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010693783
VERSION     WP_010693783.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..271
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29890
     Region          31..262
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mfgvftfavp gvelgevvrt ssarrlpdvv rsryveiadt laaelaqlpa gsriagehei
       61 aarfevgraa araamqeleq rllvrrvrga gtfvnrridy visqrrapsw hqtvreagae
      121 prsvvrgvrr aslpateaer lerpvgspas llirqyyvdd llhgwsnewi padvlddvei
      181 avhsvesvds ilhqmskvqp vrswcrvsnt lpgpevvagl eiesdrpvwl vesvsldaat
      241 gtpvlcirsw srpdsarivv emdgpyqped e
//
LOCUS       WP_010693803             397 aa            linear   BCT 01-JAN-2025
DEFINITION  OmpA family protein [Treponema denticola].
ACCESSION   WP_010693803
VERSION     WP_010693803.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..397
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44645
     Region          118..323
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 mllssvplta ensqdiqnte qgsdnpaadi sekwysnift sagfqtfipg sllkdytkpk
       61 pgyrialgyt ffrskqhtmp vyletghgvi lgtnplvrsf davpitinaa yeyfpiryls
      121 vgafagigly alqiqhypvv ldiltnklkt shgvdgvlnm gisvgseifn rsvefkaafs
      181 idlllektra vplpsfqmyv rvypidvyay arrknkpspp vlipapepvi iekkievpve
      241 kqlaqfdaiy iyfnsessel dvnakgdikk aaailkehed lfvlfessaa pfgsqkgrlk
      301 veeariasvs gylqkngitq driiynepkd knykkenape edfytryryv kirfvrlqfn
      361 pneganhyqs apanrkpnet nektdkitie kmqgenk
//
LOCUS       WP_010693811             208 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010693811
VERSION     WP_010693811.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..208
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22832
     Region          1..>207
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mekaflqlkn ikkhftekdi sisfelkkgk alallgpsgc gkttvlkiia glvpadsgei
       61 ilngkninht ppgkrgigmv fqdyalfphl nveenifygl vsqgmtkkea rkaivplvel
      121 fhlealqkrk tdllsggekq rvslarslav kpdlilfdep lsaldadlrl hlrkelrakq
      181 eslgytavyv thdkdeaaal adevlymg
//
LOCUS       WP_010693823             128 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Saccharopolyspora
            spinosa].
ACCESSION   WP_010693823
VERSION     WP_010693823.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..128
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13259
     Region          <19..>123
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(23..25,27..28,32,35,44,46,48,52..53,56..58,60..61,
                     65,68,77,79,81,85..86,89..91,93..94,98,101)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          46..77
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          79..108
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mshggltpeq tervvaiamn laragetaql aefvdhglpv dvadqggntl lmlaayhgya
       61 qtvralldrg anpdlrnerd qapiagalfk gadevvavlr eagadldagt ptaraaatmf
      121 grehllad
//
LOCUS       WP_010693851             446 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Saccharopolyspora spinosa].
ACCESSION   WP_010693851
VERSION     WP_010693851.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..446
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48468
     Region          4..402
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mpeprvviig gghvgltlal rlqrkmkpge akvtvidtqp hmtyqpflpe aaagsleprh
       61 vvvplrealr ncevltaqvs gidharqrlt atlgdgkver fgydmlvvvp gsisralpip
      121 glaeqgvgfk tigeaiylrn hvlsrldiaa sttderlrrr lltfvfvggg yagieamael
      181 esmaryairs ypqvsaqemr wvlveamgri mpevsppmse ytkgrleerg ievklnttak
      241 sfvdghvals dgdefdadtv vwtagvkphp mledsdlprd akgrvectar lqvrgthnvf
      301 sagdcaavpd ltssdpdalc spsaqhavrq akvladnila mlrgeqlvny khkyagsvag
      361 lglfqgaaev hgvklkgfpa wllhrgyhlm rmptashkar ilgdwlmelp fprqvvalge
      421 lhdpraefvk aantrglpkp ngrvag
//
LOCUS       WP_010693853             423 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Saccharopolyspora spinosa].
ACCESSION   WP_010693853
VERSION     WP_010693853.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..423
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43083
     Region          33..403
                     /region_name="MFS_MdtG_SLC18_like"
                     /note="bacterial MdtG-like and eukaryotic solute carrier
                     18 (SLC18) family of the Major Facilitator Superfamily of
                     transporters; cd17325"
                     /db_xref="CDD:340883"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,158,
                     161..162,165,237,240..241,245..247,250,278,282,331..332,
                     336,340,357,360..361,364..365,368)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340883"
ORIGIN      
        1 mssssatade tiepvenagd sgigslprei wvlvvgsfiv avgmgivapa lptfatsfgv
       61 gvtaaslvis afalmrlafa pvsgrlvsff gersiyvwgi sivgistaac afagsywqll
      121 ifralggtgs tmftvsaval lvrlapphlr grasgvwats fllgnisgpi iggimvgysl
      181 rlpfvtygia lfvaafigwl mlrkstlaap rtdtgvptmt vgqalrhray raamlsnfsn
      241 gwavygvria lvplfvveal rstqsmagia lsvfalgnaa vlllsgriad krgrkplvli
      301 glavsglata slgvtdsipw flaasliagv gagilnpaqn aavadiigak gkggpvlaaf
      361 qmsadfgail gpliagvlad tmsygaafav tgftavlgll awigapetrp atpprpeptt
      421 eaa
//
LOCUS       WP_010693865             332 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Saccharopolyspora
            spinosa].
ACCESSION   WP_010693865
VERSION     WP_010693865.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..332
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36219
     Region          1..131
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          172..292
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mldevdlalv dalqvnpras wialaevlel apitlarrwq rltdagaawi tvalgnsssk
       61 gatvefacap gtavqvaerl aelphvitvg vttgeyqvfa lvmaptlgai snvllrtlpl
      121 pkevtkvrsh vfgstfggii wrlgvmnrsq aeqvresvgp ppreirpfgv adralflalg
      181 rdgrrsyasl aselnispqa vkrrldrlrq hgdivfrcdm arplagwhtm allwlavpdt
      241 evqrigkslg swpetrhcaa vtsptnlgli vglrslnhld elliriaheh pdakvmdrkl
      301 ilrttkvhgr ilddqgrstr vvpvdpwaal st
//
LOCUS       WP_010693919             555 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010693919
VERSION     WP_010693919.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 555)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..555
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63011
     Region          1..542
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mpeiilqnlt krwgkfygtd nlnltienns fitllgpsgc gktttlrmia gletptsgki
       61 iidgetvfds ekginipank rkvgflfqny alwpnmtvye nisfglknik elmplcdfei
      121 rriddlkkil necgkaveii idsqtkdkkk gnrldektal iklidnfiis eytaktilsy
      181 glekaenree kvkaiisgld ekrasllekh kkngfsvndn yelvdekgev ikkirklene
      241 eidlivrrvs rivkigmfmd rypnelsggq qqrvaiartl apgpkvlfmd eplsnldakl
      301 rlemrselqr lhldtkstfi yvthdqleam tlatkiclmd ngllqqydap ldiyekpvnl
      361 ftadfignps infieaaget sadgdfnlsc laglkfkfkp aqkidykewl lqteteikkq
      421 reeeaertkn aekenkilpf kyhiakadea efdlnspipt ekdfiigvrp efikihengk
      481 ltgsiyssmp tgmettvkik vgnflltgvv flnitykige kikfdiegdr imlfsslnqr
      541 lislgyleke dvesv
//
LOCUS       WP_010693939             165 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010693939
VERSION     WP_010693939.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..165
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=17564
     Region          5..86
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mtelnatsaa llgllhegpk tggqlvaaat erfggffsvt rsqvyrelpa ltdagllrlg
       61 kqgprssqqy aitaagkraf kswlntepgp dnvrsplilr lvysgsltpk qrsglvesar
      121 aqyavkvdea rnaakaatdp yekaaadftv synraiikll dsipd
//
LOCUS       WP_010694018             135 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Saccharopolyspora spinosa].
ACCESSION   WP_010694018
VERSION     WP_010694018.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 135)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..135
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14602
     Region          5..>88
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mircvgaiiy dpsgrlllvk rahepgkgkw slpggrvepg etdhsavqre vreetglsvt
       61 vgalvgrvfr paplgtyeil dyscrsteqn lsagddaada iwadhatfat lerddalteg
      121 lvetlrswds lprne
//
LOCUS       WP_010694050             361 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010694050
VERSION     WP_010694050.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..361
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40793
     Region          3..360
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mkvslkdigk kyegrenfti rhinleiddk efcvilgpsg cgkstllrmi aglnsitege
       61 lifgekivnk vapkdrdiam vfqsyalyph mtvydnmafs lkmkkerkei ihervleaak
      121 ilqisdnlya kpsdisggqr qrvalgramv rrpgvflmde plsnldaklr ehmrvelvrl
      181 hkqlgttsiy vthdqteamt matkivllnk gkiqqvgkpe efynkpanif taefigsptm
      241 nifegkiehg rfitasgvie vfpkeadakv laayegkkvy lgirserfia geneknsfha
      301 kidvievlgk eqllytkldd gtdcimsepg yfkyavdeih nftfdldalh ffdgetteri
      361 n
//
LOCUS       WP_010694079             432 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Treponema denticola].
ACCESSION   WP_010694079
VERSION     WP_010694079.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..432
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48198
     Region          4..411
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mkfelalmii efiallfcaf ffsatetait aitrteykai kksrtkksrr laflierkde
       61 ivsatligtn fvntlssali tafvidtygq qhipaataia tvliiifaei lpkavaayna
      121 veitktflvp lsvvrlflkp fififslmsn fivklvskkq nnqsselsed yletlinisl
      181 adgtfqtgeh elikravrlh elklqsimtk kedivsldin sslenmvsif rktmfsrlpv
      241 ykgekdkiig svhykdilfy rshntemdin kiirralfip ktanifsaik tmsknkrnma
      301 fvideygsta glitiddist aifgsiqdey sktktnplsg mkivdgthil ipgavpiiql
      361 nsilntdfhs dyndtiggli letaeylpke gelitigevd fkvekvetsk iisliadvsk
      421 ltagaqfpka fq
//
LOCUS       WP_010694192             198 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Treponema denticola].
ACCESSION   WP_010694192
VERSION     WP_010694192.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23038
     Region          7..>97
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 makafteqer ieikekilea aldlfhdkgt kalsiaeltk ragiaqgsfy nfwkdkeali
       61 meliayrssq klnyiekkfs nslsdpaefl tdiiyrysvd lmvkmqkqpv yedafkilea
      121 kklnevhrie ilydgfltkl ieyweqngsi kradkkglln afsgsfllcs hyyqfdkdhf
      181 nemlltfisg ivnkyiek
//
LOCUS       WP_010694242             312 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Saccharopolyspora spinosa].
ACCESSION   WP_010694242
VERSION     WP_010694242.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32917
     Region          62..272
                     /region_name="BD-FAE"
                     /note="pfam20434"
                     /db_xref="CDD:466583"
ORIGIN      
        1 mavtlrvlaa clalaavvat gcsresdade arpadvatrd lgaasvqrdl iyaehgtgal
       61 kldlylpeqr etrtplivyv hgggwnagvr tlnadsgspe sltaqrller gyavatvdyr
      121 ltgvaqypaq vvdvadavrw lqqhagqwhl dadriglwga sagghlvsql galagdpekp
      181 gggltgirav vdwfgpvdms aeaqlahpkm qeyaskvvrq llgcmpvecp gkadsaspik
      241 nisgdeppfl iqqgtadslv pidqsldlar dlrrlgvsae lhpyegldhg fgkgphntli
      301 vdtvaafvet hv
//
LOCUS       WP_010694244             499 aa            linear   BCT 01-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Saccharopolyspora spinosa].
ACCESSION   WP_010694244
VERSION     WP_010694244.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..499
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=53318
     Region          6..442
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 maekvllgid igtasskgvl vstdgriiar asrphetshp hpgwvehdae svwwadflel
       61 arelvraaeg reiaglgvsg igpvllpadg dgkplrpail ygvdtratee iaelteefga
      121 deilrrggsa lssqavgpki rwlakheper yqrtemllmc ssylvhrltg ryvldhhsas
      181 qcdplydlqa rdwsadwaqr vapglplpel awptevvgrv taqaaaetgl peglpvtagt
      241 vdawaeatsv gvrepgdvml mygttmffvq vltdvqphpa lwgtcgafpd tytlaagmat
      301 sgavtqwlrg lvdgdfaqlv ekaskvpags rgllllpyfa gertpifdpd argvlagltt
      361 shgraelyra alegigfgvr hnlaamgeag gtarrlvavg ggtqgglwtq ivsditgqeq
      421 qipaetvgaa ygnallaglg tgaavapeaw npvtrtvrpn pehteryngf frhyrdlyds
      481 tvriahflag eqraaderd
//
LOCUS       WP_010694259             347 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Saccharopolyspora spinosa].
ACCESSION   WP_010694259
VERSION     WP_010694259.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..347
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35152
     Region          17..344
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msnqteqrpa esgggvaapa kranvvetlf rfqsffglva vflaavifsp rndgqilflt
       61 sdnlfnivra vseigiiavg ltfviliggi dlsvgsvlgl aavgsavlmv edgfgvwtav
      121 alvllagiaf gllqgtaval lgvqafivtl aglqiargla rmwsggetvq isygdgpgqa
      181 pmlfsllger tfggvvpipa lifavvaiva ilflrgsays rhlyaiggne kaarlsgvpv
      241 nrvkiiafgi agfcaalagi vhagqlnags pndgiayeld giaavvvggt nlaggrgsvi
      301 gtiagalllg ilnnilslns vntdlqllik glvivaaaal qrlrpts
//
LOCUS       WP_010694335             348 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Treponema denticola].
ACCESSION   WP_010694335
VERSION     WP_010694335.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..348
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=39546
     Region          15..344
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mrpfnyyeik nqkwdsgtlg liaaiykeag kqemylkqrp eeleklveia kiqsteasna
       61 iegivttstr ikqlvkektt pknrdeqeia gyrdvlniih esfdaiplsq nyilqlhkil
      121 yshmnnpmag riksvqnyit vtysdnhaet lftplapfet pealdkicee ynrvignmev
      181 epliaipvfi hdflcihpfn dgngrmsrll ttlllyrngf yvgkyislea kiaknkdlyy
      241 dalgraqigw hegkedvvpf ikyllgtvla ayrdfadrfa lveiklpale tvrraalnki
      301 glftkqdire lcpslsissi egglrklvsa gelkkegsgk nicyyrlk
//
LOCUS       WP_010694309             166 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Saccharopolyspora
            spinosa].
ACCESSION   WP_010694309
VERSION     WP_010694309.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..166
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17658
     Region          21..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mapnaeglda ldarllllls deprlgvlec srrlgvargt vqarmdrlvq rgvllgfppe
       61 vdlaamgygl tafavleiaq ghrrlvaeql asidevcevh attgqgdlfv rmvarsnadl
      121 qrvideivgv sgvrrtstsi alstpvaprv rpllerlaad garpes
//
LOCUS       WP_010694364             135 aa            linear   BCT 01-JAN-2025
DEFINITION  RidA family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010694364
VERSION     WP_010694364.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..135
                     /product="RidA family protein"
                     /calculated_mol_wt=14006
     Region          1..128
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mnrrsiyvdg fshenpipaa cqlgglvttg avhgggsgsd pddfparfgd qvaamfdrva
       61 ailtaaggsl ddvlkfsvri sspedrdeln rqwcalfpdp ssrparqvsi gttrphilvq
      121 cevlalvagd gggda
//
LOCUS       WP_010694393             478 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Saccharopolyspora spinosa].
ACCESSION   WP_010694393
VERSION     WP_010694393.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..478
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50064
     Region          2..458
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mianvdalrv eaggravldg vdltigegea vglvgpsgcg kttlalallg hlhdgathvs
       61 gqafvdgrpm lpkppprvrg hligylgqdp glgltpylrv daalklagaa dvsealdrvg
      121 lpgrlarryp hqlsggqqqr valafalars prllvldept aaldvmarae vlaelrrlrd
      181 ngvallwish dhgalgqlvd rtlalrhgri asapepvagv vrrpstqdge pvltataisa
      241 rhgrtqvlrd vdltvhagec lavlgvsgag kstlarclag lhrpasgtta lagttlagdv
      301 rgrsrderar vqlvpqnpae slhprqtvrt allrplkvlr kqqhgvdell aavglpakla
      361 drlpgelsgg qrqrvalara laarpkvlvc deitsaldpr araevlalld dlrrerglai
      421 vfithdaava aaisdrvlvl aegrvlahgg tdellarpdd lpsllalgrp taedpcki
//
LOCUS       WP_010694460             346 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010694460
VERSION     WP_010694460.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..346
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37879
     Region          41..286
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(42..44,47,58,60,92,111..114,212,214,216..217,219,
                     230..231,234,249..250,253)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(42..44,212,214,217,231,234,249..250,253)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(43,47,58,60,92,111..114,212,216..217,219,230..231)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mnaqppagel pgldldrlra hldaerpglv ggpltgefvq ggrsnltyvv gdgahqwvvr
       61 rpplghvlat ahdmtrefrv lsalagtpvp vpethllcqd esglgapfyl meyvpgtvyr
      121 tpqlterlaq qqrvdlawql mdvladlhsi apdavglgef grpegflerq vrrwskqlaa
      181 shsrdidgve elaarlaktv pstprtgivh gdyrldnviv gddqriravl dwematigdp
      241 ltdlgllavy wegfngvern piakgvgpdf gfpaarqlld ryaersgtdl sdmnwyvafg
      301 ffkisvileg ihyrfihnqt vgegfehvga lvaplveqgl atlkev
//
LOCUS       WP_010694476             372 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010694476
VERSION     WP_010694476.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..372
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39078
     Region          5..365
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msapdllyse veedlranvr rllrdrcdwt avlarcetde pydlalwrtl agelglaall
       61 vpeelggaga sarelsvvae eigrsvapvp flsnllttaa lvacagqplv reilpqfidg
      121 sqlctvavgl ttvpygafpq svkadgsals gsvsavvdle vadyvvvpat dadgaalylv
      181 dtsvsgvsra sttpldltrr fgtltldgav geriasgaga erilrqalvt aagllaaeqv
      241 glaeqcleat vayaktryqf grqigsfqav khrladlwtg vssaravarn aadtlargde
      301 eselavaiaq sfcsdlvvra aeehlqlhgg igmtwehsah lylgrakssq lsfgiaethr
      361 qriaeladlp tp
//
LOCUS       WP_010694484             168 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Treponema
            denticola].
ACCESSION   WP_010694484
VERSION     WP_010694484.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..168
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18837
     Region          <50..126
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 mknilkilai malfsfvlts cgtpptpppe ekpapvvvee ptpapepepv veptpepkpi
       61 veeprdvpvk eyvvvegdtl seialkfygt rekayyfpii mainpgkvkh pdkltpktkl
      121 lipdfelfmk hspskmlarp efekcikiye degksgvves lrrrlkef
//
LOCUS       WP_010694500             146 aa            linear   BCT 01-JAN-2025
DEFINITION  roadblock/LC7 domain-containing protein [Saccharopolyspora
            spinosa].
ACCESSION   WP_010694500
VERSION     WP_010694500.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     Dynein light chains of the Roadblock/LC7 group belong to an ancient
            protein superfamily implicated in NTPase regulation
  JOURNAL   Curr Biol 10 (21), R774-R776 (2000)
   PUBMED   11084347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..146
                     /product="roadblock/LC7 domain-containing protein"
                     /calculated_mol_wt=15151
     Region          9..130
                     /region_name="COG2018"
                     /note="Predicted regulator of Ras-like GTPase activity,
                     Roadblock/LC7/MglB family [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441621"
ORIGIN      
        1 mandlpagqt sdlgwllanl lrrvphtrca llastdglkr yyhgleadea dalaawaaaq
       61 sslarnggmr fgagdgvrqv vvefddvvff vsaagpgavl vvlayqdada svlgyeiaql
      121 vkkvpshlat pmrqptaasr agemgg
//
LOCUS       WP_010694520             361 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Treponema
            denticola].
ACCESSION   WP_010694520
VERSION     WP_010694520.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..361
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40921
     Region          <171..359
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mksrklfvfi plivivillf ltaafflfvt iaeyrpktve kadinkgake qllktdealk
       61 vlswnigycg ldaqndffyd ggknvtarsk eavlnnlerv kallkkedcs fnllqeidvk
      121 skrsfyvnqk kalsafftdy dsalalnyda livpapisnp lgrvksgvft lskygiqkae
      181 rlqlpgafsw plktvnlkrc llvseiktdv qgknlyiinl hlsaydaagv lrkqemeflr
      241 nlalkfyneg hwviaggdwn slfpgvekdq lmpyttpeef lewieyspad figkewkwgf
      301 dnsvptvrll ekpyvkgeny ttiidgfics pnveivgvkt tdlnfevsdh hpviaefklm
      361 k
//
LOCUS       WP_010694582             317 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010694582
VERSION     WP_010694582.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..317
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35724
     Region          13..317
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mnnteinlae lpllkienls vsfgsknapq vlqdfnldif egdkiavige tgsgksvmll
       61 avlkllpkna evqgsaffkn rnllnldrra lnsirgkeis yipqgsgnsl npllkvgyqv
      121 gepliihygy skknaekesv nllrkfnlgn eeeravqyph tysggmkqra miamgisaga
      181 hlifadeptk gldsrrlkmv eqafkllkee tyvcvthdln fakniskrlc vmhssysvem
      241 glteevfakp yhpytediir ampenglqyk aksmqrpvye tgcryapnce yafekcrqtp
      301 pmieieknrk vrcwkya
//
LOCUS       WP_010694590             933 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Treponema denticola].
ACCESSION   WP_010694590
VERSION     WP_010694590.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..933
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=101822
     Region          1..346
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          38..63
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(39..40,43..45,47..48,52,55,63,65,67,71..72,75..77,
                     79..80,84,87,96,98,100,104..105,108..110,112..113,117,120,
                     129)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          65..96
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          98..129
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          198..517
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          247..278
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          280..311
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(313,315,319..320,324..326,328..329,333,336,345,347,
                     349,353..354,357..359,362..363,367,370,379,381,383,
                     387..388,391..393,395..396,400,403,412)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          313..345
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          347..379
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          381..412
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          445..477
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          480..510
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          497..781
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          544..574
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(545,549..550,553..555,557..558,562,565,574,576,578,
                     582..583,586..588,590..591,595,602,611,613,615,619..620,
                     623..625,627..628,632,635)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          576..611
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          652..682
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(653,657..658,661..663,665..666,670,673,682,684,686,
                     690..691,694..696,698..699,703,706,715,717,719,723..724,
                     727..729,731..732,734,737,747)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          684..715
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          701..931
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          717..747
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(749,751,755..756,758..760,762..763,767,777,779,781,
                     785..786,790..792,794..795,799,802,811,813,815,819..820,
                     823..825,827..828,832,835,844)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          749..777
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          779..811
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          813..844
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          846..908
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mqniilttkk ifklafilil itanfmsckt apakeetlid likagkseel qerlnssain
       61 mkdeegnsll hiaavknnpi ivrllinmda dieaqnnige tplaaalnns aydavkvlve
      121 ynanifakdn dgekpfdiac knnvpglilt aqtikqkden qdtalhlaak aidkqlteqi
      181 laiappetay nkeklsplgi aynhndaeds aeiasmllla giqpmgkdfa efetaslarn
      241 ysmrfgdget llhifarkgy tgflkflikn kvpidvkdis sstamqeavy ngnteaaill
      301 lqagadpnsr nssgntalhl vmpeasrskl fnelitagan pnlkdnyget plhvaarigm
      361 nddildqllk agadinernk kgqtplilai drnqtqqvdf linhgadiha edksgesafv
      421 rsisaglpmv ehvvteknsa erdsngstpl hlavshrass diiyylvekk slintrnklg
      481 ntplhiaaek nyreageili annadifyan lngdsplkfa mtlregredw minshtigag
      541 dgagntplhl aaewqilpmi pylidkgadi narnannetp lfnavrtdsp eavkallgeg
      601 lskkadldar dflgntilha avrwsayksa dfilrkdtee yvrlinaknl agktvlheaa
      661 kqgeikfini flkakvdvns adetgrspls eavltnqtqa idlllkngas pvqqdmygrt
      721 alheaveise eslilvrnag gnplakdayg ktpfslalnk nirtvdlvlg ndslladtdg
      781 dtplhiavke kvsldyfqri mkkrypvnkr nkngetalll avqnnqkeit rallaggadp
      841 fivnnkgvsa iteifthhtd fvpiaaefsl kqtdtlgegm lhyaakfadv qtlkdllalp
      901 gvkldvknta getpyqvalr wnrneiaell kte
//
LOCUS       WP_010694597             155 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Saccharopolyspora
            spinosa].
ACCESSION   WP_010694597
VERSION     WP_010694597.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..155
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17025
     Region          1..137
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdsidraiis qlrrncrqsn ielaeavglt pspclrrvkr ledegiitgy hasiapaavd
       61 rgfevlveie lkdqspastk kfeaeliahd eviearrmfg spdfrllvat kdlaayeafv
      121 tnklltlpgl gnlqshfpml tiksdppras grprs
//
LOCUS       WP_010694601             332 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Saccharopolyspora spinosa].
ACCESSION   WP_010694601
VERSION     WP_010694601.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..332
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35329
     Region          11..310
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtadadapva vdvsgltlsg prgllvtdva ldirvgeclg lvgesgsgkt lavrsiagll
       61 psgielaagr idtggrrvgm ifqdpmraln ptftirrtmr epliqhhglp rkvadrrale
      121 lmkdvgikda eriagcyphq lsgglrqrvl iaaalacepq illcdeptta ldvttqaiil
      181 dllhglreer klamlfvshd laviskisdr vavmyagqti evgptdevlr sphhaytagl
      241 lrsspsggrp geplfaiegi ppqrhgelvg crfaarcpwa vpectggavp wvgqgdrhia
      301 rcvraddvaa afslrvedgg wprnqeveha vs
//
LOCUS       WP_010694605             510 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Saccharopolyspora
            spinosa].
ACCESSION   WP_010694605
VERSION     WP_010694605.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 510)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..510
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53414
     Region          50..490
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mpllvamval vavvasacag nssndtngat gtpvqggtld vgltiditsl npydgsgdtt
       61 smilanlnaq lfkdydhkvv palaesltrs adgktatvtl rkglkfsdgt pitpedvvfs
      121 ieqakagsay gslykeiits ekasgedkvd ltlvrptpnl eallsfpraa iipanfggks
      181 kseylqkpvg tgpymfisrq pgvsiqlkkn pnywdsgkpy idtldfqvfn nnnaltsafq
      241 aktvqaipfa peasipsltg anivntaaaa temffingrt gplsdvkvrq aismaidrea
      301 ivkglrgpgd kptatfvpas vlgsahpapv kggdieaakq llaassykdg atikviyptg
      361 ddtlantvqa mqaevakigi kfdlqaldqg awvndvlggk yelayqnisa ngttadttmq
      421 ffiasgaygg gwstdvaksa ltkyqtatda agqaaaldef qnwlsaelpv iptvwlrpsl
      481 vlkgsvagyq gldtvtqqal pfeglwlnks
//
LOCUS       WP_010694657             439 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Saccharopolyspora spinosa].
ACCESSION   WP_010694657
VERSION     WP_010694657.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46548
     Region          13..418
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(26..27,30..31,34,73,131..132,134..136,139,159,
                     162..163,166,248,251..252,255..257,260,288,292,344..345,
                     349,353,369,372..373,376..377,380)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mpngtdsrrt hrrraviast vgttiewydf flygtvaalv fpkiffpgss asagvlesfs
       61 tlfvgfaarp vgaaifghyg drigrkatlv ttlllmgiat vligllpgya tlgvaapmll
      121 vvlrimqgig vggewggsvl iamewgsasr rglmasmpql gvplglllst aavgvssavs
      181 gdafeswgwr vpfllsvvli gvglwvrmrv lespdfaevk kqqavekqpv waairkhpke
      241 iltsafvrla eqapfylfit fvltygtkhl emprsellna tlvaaavgli svplfghlsd
      301 rfgrrliygi givctglyaf pyfalldtrs sglvllaivv slivhdimyg pqaaliaesf
      361 gtnirysgag lgyqlasvia ggpapliaaa llqstgtsvg iswyivlcsv islialllmp
      421 rrtvpassds pttsdrlea
//
LOCUS       WP_010694674             251 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleotide exchange factor GrpE [Treponema denticola].
ACCESSION   WP_010694674
VERSION     WP_010694674.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Harrison,C.
  TITLE     GrpE, a nucleotide exchange factor for DnaK
  JOURNAL   Cell Stress Chaperones 8 (3), 218-224 (2003)
   PUBMED   14984054
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087353
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..251
                     /product="nucleotide exchange factor GrpE"
                     /GO_function="GO:0000774 - adenyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0051087 - protein-folding chaperone
                     binding [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=28292
     Region          88..227
                     /region_name="GrpE"
                     /note="nucleotide exchange factor GrpE; cd00446"
                     /db_xref="CDD:271355"
     Region          88..138
                     /region_name="2-helical coiled coil"
                     /note="2-helical coiled coil [structural motif]"
                     /db_xref="CDD:271355"
     Site            order(90,93..94,97..98,100..101,104..106,108,111..112,
                     115..116,119..120,122..123,126..128,130..134,136..137,
                     156..157,159..161,164,171..172)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271355"
     Site            order(106,114,136,139,184,186..187,189..193,209,218,222,
                     224,227)
                     /site_type="other"
                     /note="Hsp70 (ATPase domain) interactions [polypeptide
                     binding]"
                     /db_xref="CDD:271355"
     Region          156..172
                     /region_name="2-helical coiled coil"
                     /note="2-helical coiled coil [structural motif]"
                     /db_xref="CDD:271355"
ORIGIN      
        1 msknhekqad kkqaekedle kdlqpkdesa vkdeqgagcg cktskenpqe draeqnsstg
       61 gkceekpekn ddvlspekri eeleticrdw qdqylrkaad fenyrkrmir ekqeaidyan
      121 snllldlvqv lddfdraida gktqggeaan nafvegvvmi knqmvsmlss kyglsyypak
      181 geafdpnlhe avsmiqspdv keavvgeelq kgyklkervi rhskvmvlmp aekqdekkae
      241 eseaadkkne n
//
LOCUS       WP_010694681             314 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Treponema
            denticola].
ACCESSION   WP_010694681
VERSION     WP_010694681.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..314
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34162
     Region          10..296
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mdsgnriklv riaslislig niiiciaklv igiyanslsv igdgidsatd igisimtlav
       61 sfiigrpsdk khpwghqrae tmaslilafi imiagfqlfi tatgklinvy kgtvtilmph
      121 ifavivtvss iavklllaln qyiigkktgs mmiqanaknm tndvilsasv laglgishff
      181 kapifdavta llvslwimks gielfmelni elmdgntndi lykqlfeavn svegahnphr
      241 arirrmanll didldievda aisiyeghci aekvtsaike kienvydvmv hiepygihnn
      301 eeegfglsek dinn
//
LOCUS       WP_010694698             232 aa            linear   BCT 01-JAN-2025
DEFINITION  response regulator transcription factor [Treponema denticola].
ACCESSION   WP_010694698
VERSION     WP_010694698.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14439489
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..232
                     /product="response regulator transcription factor"
                     /calculated_mol_wt=26597
     Region          7..119
                     /region_name="REC_OmpR_NsrR-like"
                     /note="phosphoacceptor receiver (REC) domain of
                     Streptococcus agalactiae NsrR-like OmpR family response
                     regulators; cd18159"
                     /db_xref="CDD:381143"
     Site            order(37..38,56..66,85,92)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381143"
     Region          138..225
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(156,175..176,194,197,205..206,217,222)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mkqlikiliv eddktiasvl kknleqwnfn vrcaknfsni leefedykps lvlmdiglpa
       61 fngyhwcsei rnksqvpiif lssrndkmdi vmamqmggdd yiekpfdmdv aiakiqavir
      121 rtyqftasmn evgfagtvln lstltlvynn kttlltanei kilkclylaq gefvsrekim
      181 dvlwqnnqfv ddntlsvnit rlrkklenag lfnfienkkg lgyklnehhg nr
//
LOCUS       WP_010694700             253 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010694700
VERSION     WP_010694700.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28373
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 metlldvkni qkiyrsrfsk qgtvalrdvs fsvkknefta imgesgsgkt tllnllatld
       61 kpssgeiflk gepiskikak disafrrnkl gfvfqdynll dqfsvkdnil lplvlsnypi
      121 demnkrllpi aealrildll ekypyeisgg qcqrataara fitkpqlila deptgaldsk
      181 ssdmlletfs qmneagqtii mvthsaraas yakrvlflrd gniyyeiykg dmgqalfrer
      241 ineglfmmnk mds
//
LOCUS       WP_010694752             446 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Treponema denticola].
ACCESSION   WP_010694752
VERSION     WP_010694752.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..446
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=51617
     Region          1..437
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 mkgilkrkid sfltewknta nhlplivkga rqigktesir ffahqnykni veinfalqpe
       61 fkkifdqgfs vnnilknisf irpdsvfekg ntliffdelq alpncatslk sfkedgrydv
      121 icsgslmgis yqeieansvg ykqeyrmysm dfeeflwahg ykepqiediy hylknalplp
      181 nltfnilsec fkdylviggm paivknfieq knfsgslelq rmllndyked iikyaagldk
      241 akilniyrsi piflgkdnkk fkiskvrkna rnrdytgisd wlkdsgivni cyclnfpelp
      301 lkgncnyeny kiyyhdtgll iaalddeaqe dlrknknfnt ykgavfeniv sqmlvcagyn
      361 lffyknekst iemdffirdk dslipvevks ndgatvslkn lihqkqfpdi kygiklsann
      421 igfngefyti pyfltfmlkr flaekn
//
LOCUS       WP_010693786             337 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA-dihydrouridine synthase family protein [Treponema denticola].
ACCESSION   WP_010693786
VERSION     WP_010693786.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Finet,O., Yague-Sanz,C., Kruger,L.K., Tran,P., Migeot,V.,
            Louski,M., Nevers,A., Rougemaille,M., Sun,J., Ernst,F.G.M.,
            Wacheul,L., Wery,M., Morillon,A., Dedon,P., Lafontaine,D.L.J. and
            Hermand,D.
  TITLE     Transcription-wide mapping of dihydrouridine reveals that mRNA
            dihydrouridylation is required for meiotic chromosome segregation
  JOURNAL   Mol Cell 82 (2), 404-419 (2022)
   PUBMED   34798057
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Bou-Nader,C., Bregeon,D., Pecqueur,L., Fontecave,M. and Hamdane,D.
  TITLE     Electrostatic Potential in the tRNA Binding Evolution of
            Dihydrouridine Synthases
  JOURNAL   Biochemistry 57 (37), 5407-5414 (2018)
   PUBMED   30149704
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Xing,F., Martzen,M.R. and Phizicky,E.M.
  TITLE     A conserved family of Saccharomyces cerevisiae synthases effects
            dihydrouridine modification of tRNA
  JOURNAL   RNA 8 (3), 370-381 (2002)
   PUBMED   12003496
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..337
                     /product="tRNA-dihydrouridine synthase family protein"
                     /EC_number="1.3.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0017150 - tRNA dihydrouridine synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /calculated_mol_wt=38034
     Region          2..245
                     /region_name="DUS_like_FMN"
                     /note="Dihydrouridine synthase-like (DUS-like) FMN-binding
                     domain. Members of this family catalyze the reduction of
                     the 5,6-double bond of a uridine residue on tRNA.
                     Dihydrouridine modification of tRNA is widely observed in
                     prokaryotes and eukaryotes, and also...; cd02801"
                     /db_xref="CDD:239200"
     Site            order(6..8,33,62,89,145,175,206,208,230..231)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239200"
     Site            order(62,92..93,145,147,174..175,177..178,207..208,231)
                     /site_type="active"
                     /db_xref="CDD:239200"
     Site            order(92,147,175,177)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239200"
     Site            order(93,145,174,178,207..208)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239200"
ORIGIN      
        1 mnlisapmaa ithsafrrlt acfkepdeyf semihapsai sgggfekwyf ranpspkklv
       61 wqitspdeda aaacvplllq yggfgidlnm gccapqivnt gagfawmkkp lsqaaslvsk
      121 vkkavllyde qkagpqtepi rlsvklrlge eenydrllsf ckmlvlegvd litlhprtqk
      181 qkysrpckhe ytarlasdls vpvygngdin sleslkkvss kypcsgwmig raavqkpwif
      241 yelskgvlkn giaedkdkki eidllktael flsflreeqp qefyltraqr ffaffcdnfs
      301 fahhikskil ncknlddmlh nlsdyleevl edrlirl
//
LOCUS       WP_010694830             317 aa            linear   BCT 01-JAN-2025
DEFINITION  KilA-N domain-containing protein [Treponema denticola].
ACCESSION   WP_010694830
VERSION     WP_010694830.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Iyer,L.M., Koonin,E.V. and Aravind,L.
  TITLE     Extensive domain shuffling in transcription regulators of DNA
            viruses and implications for the origin of fungal APSES
            transcription factors
  JOURNAL   Genome Biol 3 (3), RESEARCH0012 (2002)
   PUBMED   11897024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..317
                     /product="KilA-N domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36522
     Region          58..180
                     /region_name="KilA-N"
                     /note="KilA-N domain; pfam04383"
                     /db_xref="CDD:367917"
ORIGIN      
        1 mdyeiklkke padkngcrmg qnngkqaeie yrtrkrenem aknrkinvqg fdialyesnk
       61 ndyisltdia rykdtehtdd iiknwlrnrn tvellgfwei innpnfkpve fdgfrkqagl
      121 nsfvltpkrw iettnaigiv sksgrnggtf ahqdialefa swisiefkly vikefqrlke
      181 densrlklew nlqrtlakin yhihtdaike slipkevskk qaaliyadea dllntalfgl
      241 takewhernp klsgnirdya gleqlvvlsn lesinallik qglpqserli qlnktaiaqm
      301 ktlvenraik klesknn
//
LOCUS       WP_010694884             721 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Treponema denticola].
ACCESSION   WP_010694884
VERSION     WP_010694884.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12036995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..721
                     /product="methyl-accepting chemotaxis protein"
                     /calculated_mol_wt=77996
     Region          60..297
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          <302..673
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkdkelvvak paakkelvmr ksvsedkifs mgkkllilfa aivvisvstq giigavmskr
       61 ailekvethl kdkatdtadl vdsmvnsfln fvssasrase lrnidasysd kiaylkkkaa
      121 fnpriiefsi tdingkchal dgrifdvndr ewfkralage qfvsepygsk adgtlvntis
      181 vpiydyenri igvlaadtpg tklsedidhi tvgrsgycfi lgktgnaiah rnrelvlnqd
      241 nfqenaktnp alvsianfak qamqsnkpsi gyytfngekn igsyaimqst gwmvivrapv
      301 ndfldtvasl qymmvvtgft llgvalvstf vvtrkmilpl qkvvlalkdi sqgegdltvr
      361 lpvtsndevt llskyfnqti ekignsiksv gtntnnmqfi gdelasnmte tasaveeins
      421 nidnikdqal tqaasvteta atveqiirti kqlnnsietq aasvaessss ieqmvanies
      481 itqtlgksdn iireladata egkgkvstan evtqkiaees gslmeasnvi qhiasqtnll
      541 amnaaieaah ageagkgfav vadeirklae essaqgksit stlknlsgei evlaesartv
      601 egkfnsifnl aenvkemsnt vmeamteqen gskevliair nintvtqevk qgssemlkgg
      661 egiaqemnkl deltrtitdr mnemasgalq innavqevqg itqknkasie gladevmkfk
      721 v
//
LOCUS       WP_010694885             664 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Saccharopolyspora spinosa].
ACCESSION   WP_010694885
VERSION     WP_010694885.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..664
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=72329
     Region          83..420
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 masalhvlkr lvlgrpvrsd rlremllpkr lalpifasdp lssvtyatqe illilslggl
       61 allhltpwva lavvvllavv vasywqvvha ypsgggsyev varnlgrnps lvvaaalmvd
      121 yvmtvavsva agvdnlvsav pslypqrvwi avvvvvlmma mnlrgiresg qafavptylf
      181 vaamgltivv glgqaaaghp pvaesagwdi rpeqldvtgl aliflllraf ssgctaltgv
      241 eaisngvpaf rrpkdvnagr tmiimgvlai glfsgvtala misdvriann pcdligfpad
      301 crstaqrtvi aqvagavfgl dsvlffvvqa gaalilllaa ntafngfpml gsllaqrryl
      361 prqlhtrgdr lahsngivll glvaialiaa fegsvtaliq lyiigvftsf tlsqigmvkh
      421 wnhlladaag aahraryhrs rlvnavgavl tatvlvvvli tkfthgaylv viaipllyfl
      481 mraihrhyrd vrreleperd gitlpsrvha vvlvsmlhkp tlralafara nrpdtltalt
      541 vnvddaethl lrsewerhgi dvplkvvesp yreitrpvvd yikrirregp rdlvcvyipe
      601 yvvghwwenl lhnqsslrlt wrlrfeqgvm vvsvpwqlds shrreidrvh hlpghtrrgi
      661 tppt
//
LOCUS       WP_010694726             392 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010694726
VERSION     WP_010694726.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..392
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43889
     Region          3..240
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mdlfklkqld vgygnsvivg nveielqhgq ilclmgpngs gkstiiktit qhikklggkv
       61 figeediekl snieqakkms vvltdrinph lmtaeeivat gryphtnkfg kmteadymav
      121 ddaikivdge alkhkeflsl sdgekqrimi araicqeadl iildeptsfl dirykidllg
      181 ilrtlarkkn kiiilslhel dlipkiadki ilildkdnyl ygtpeeiisd tsickafdik
      241 ngsyntllgn ielarrdtss kifvvggegk gipvyrllnk yeinfnsgil fendldtpia
      301 ralstkyltq nsfeaisdki fdeaklviek seiiidcgas fnginsrnld likyaeelnk
      361 kilslkerqe yadytycntf sqllktiqsl ng
//
LOCUS       WP_010694938             186 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Saccharopolyspora
            spinosa].
ACCESSION   WP_010694938
VERSION     WP_010694938.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..186
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20252
     Region          10..137
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mlekltpagr rvldvaaelf yrqgihavgv eaiaagagvt kktlyacfgs kdqlltaylv
       61 erdqrwrawl erwvaesagp prekllavfd aleawmdrad frgcgfvnal aeipdpehpa
      121 haviigqkrw mrqyfeelaa aagladpadf vdgalllyeg atvaasagfp davrkarrta
      181 eillka
//
LOCUS       WP_010694854             350 aa            linear   BCT 01-JAN-2025
DEFINITION  formylglycine-generating enzyme family protein [Treponema
            denticola].
ACCESSION   WP_010694854
VERSION     WP_010694854.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..350
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=38343
     Region          82..350
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mkktlvifla vllvsvlsct npflkkmlve ddtvkpdlds fedagdfvki ippangiagv
       61 epdpatlpgn eakwkgvfia grkvklspyk lgktevtykl wkevydwate kgyqfahpgt
      121 kgssgtgndk eqpvtkvswr dcivwcnayt emkmdenecv yrksdstvlk dsrdsagaac
      181 daayvdmkkr gfrlpteaew eyaarwqgsv etnavqygdv wltklysasg atdkwdttet
      241 gevawysgns gsktnpvgkk rknalglhdm sgnvlelcfd wyndnpasnd naytsegivt
      301 dpqgaalgnr rvvrggfcse saknctvglr nhstpygkgd algfrvacrp
//
LOCUS       WP_010694834             226 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Treponema denticola].
ACCESSION   WP_010694834
VERSION     WP_010694834.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..226
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26306
     Region          21..>85
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mlitnmdnyk gkiladkdel ntrakilraa kqefftngfa dtnvraiakk agvttgalyn
       61 lfdnkdcife alvsgvfdef lnimahrdvf daenfgmkts dlsaitelsq rrflrmidff
      121 ydnwdamkli vccskgssye rifdkaiavt eketfqwlkl dgvkmsrrir ffihvmvtsh
      181 fenlkeifyh nlkkseavky vldfnvyhca gwkqywmeqv kglkrl
//
LOCUS       WP_010694939             234 aa            linear   BCT 01-JAN-2025
DEFINITION  pseudouridine synthase [Treponema denticola].
ACCESSION   WP_010694939
VERSION     WP_010694939.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..234
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26388
     Region          3..225
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mideirlqvy larcgvasrr asenlilngr vsvdgkivte lgtkvsgkek icldgkqifp
       61 eaekryilln kpegyvcsla dekdrpiaas llkdtyterl ynigrldmls ggailftndg
      121 dfsakvehps seiekeyevl tvfeypdevl qkflrgvrie gvfykalsae riaknkmriv
      181 liegknreir rvlkffniki kkltrvrigc vhlsglpsgk hrpltyeeik gllg
//
LOCUS       WP_010695008             413 aa            linear   BCT 01-JAN-2025
DEFINITION  thiolase family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010695008
VERSION     WP_010695008.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 413)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..413
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43253
     Region          18..405
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 maapasvpad srsrqavrdv vfvdgvrtpf gkagskgqya qtraddmvvk virellrrhp
       61 elpaeridev aiaattqigd qgltigrsaa llaglpksvp gfaidrmcag amtavttvss
      121 giafgaydva iaggvehmgn hpmgegidpn prfvsdkvvd psalimgsta enlhdrfptl
      181 tkkrtdayaa lsqqrydeal ragkitpdlv avstrskrgw glatadeppr pgttvealsg
      241 lrtpfrphgr vtpgnaagln dgatgcllad adtaaelglp vgmrlvgyaf agvepevmgv
      301 gpvpateral qragltiddi glfeineafa vqvlaflehf giadddprvn pwggaiacgh
      361 plassgvrlm iqlsrhfaeh pevrygittm cigfgmggtv iwenpnynag gar
//
LOCUS       WP_010695097             275 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF169 domain-containing protein [Treponema denticola].
ACCESSION   WP_010695097
VERSION     WP_010695097.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..275
                     /product="DUF169 domain-containing protein"
                     /calculated_mol_wt=30830
     Region          6..231
                     /region_name="COG2043"
                     /note="Uncharacterized conserved protein, DUF169 family
                     [Function unknown]"
                     /db_xref="CDD:441646"
ORIGIN      
        1 menlnvskle kslglkrhii gvqfiyfkse yealdipdyn kktsfcmmvk aamdgdvfka
       61 sannfgckca iealgieeem ecvesgqryf siglyesrav akavtkmicr ikqhafgvvl
      121 gplenmekad vvifmtnayq lmrvvqgysy kfgtpqnitm agnqgvcadl caapfekndm
      181 nfsvlcagtr kmckwgveem gvgvpiqmfa slvdgvintl nyieypehkk eirirldspd
      241 elgividdnl hygkmgkeyv rpseydklky gikte
//
LOCUS       WP_010695098             245 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Treponema
            denticola].
ACCESSION   WP_010695098
VERSION     WP_010695098.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..245
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26838
     Region          1..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mlkveniyks fgslkvlngi sfsadkgevi aiigpsgmgk stllrcinll eepdsgsiei
       61 dgvkftagek khqtirdlra ktamvfqnyn lfknktviqn imlpmvsakk ntkkeaelra
      121 ldllnqigls dkknvypskl sggqqqrvgi aralavnpsv llfdeptssl dpelvnevle
      181 iiltlaknhq stmlivthem qfakevadri ifiddgtiik dsspqsmfsl gensrissfi
      241 kklgs
//
LOCUS       WP_010695110             300 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Treponema denticola].
ACCESSION   WP_010695110
VERSION     WP_010695110.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..300
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33760
     Region          <150..298
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          177..206
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(181..182,185..187,189..190,194,197,206,208,211,
                     215..216,219..221,223..224,228,231,240,242,244,248..249,
                     252..254,256..257,261,264,273)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          208..240
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          242..273
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mnvaifydek kkdaamaikn iiishecdvt lynedeiwkd enlhtprhim knithvlfiy
       61 sknpaaylgf mffsgyatgl nlpvlvlees eklelpknfl rsfvmltiks fesyfevekk
      121 rftenhlkel arakllengy slfipnyvra vknnekeive lfidagfdps qkdslgtpvl
      181 slavrnkcle tlelllekga ainlcaedrn ytalmdaaqv gyieavqall ekkadtniqs
      241 kdgqtalils vgrreadive mlvkhgadyn ikdglgmsal gyaklfgdkk ilslfgeqtn
//
LOCUS       WP_010695199             365 aa            linear   BCT 01-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Treponema denticola].
ACCESSION   WP_010695199
VERSION     WP_010695199.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..365
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40846
     Region          220..337
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(250,253)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mkkfykifmt avvfllitst ifiscskkve ikeptkeeke agwryfkaig fklhrpaffd
       61 tygdnvnads svgeedkktd evvykvylye fasdelneky daivsnkeln rgqkiekiqk
      121 evdpylkpiy klvvlrtpli gtktlaeltg lpnnevirkt keftqvlaia dfnaedlsek
      181 aaeiykdmis qvkpiiptiq ctdpisaeaa miknvkgltf ntvdlegnki tsdilakydv
      241 tminiwatwc ppcraelpei aklyeafkdk scniigitgd vspdeqdalp takeliskag
      301 ckytvvqynd tlkpildnla awpttifvdk kgniiassvn diiigsrdla efteamekal
      361 kavgk
//
LOCUS       WP_010695197             253 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Saccharopolyspora spinosa].
ACCESSION   WP_010695197
VERSION     WP_010695197.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..253
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27080
     Region          4..206
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mqkpilvtgg tgtlgkavlr rlldaghdvr vlsrrprpad vphgwatgdl rtgegiaaat
       61 sdvdaivhca ttlgrkdvaa tqclidaarr ngdphlvyis ivgvdqvplf yyrakfaaeq
      121 rvadsglpwt ilrttqfhdl varmtsvqrr spvigalagv dfqpidvrdv adrlaglavg
      181 epagripdmg gpeirshrdl aracldstgh rrvllpvrlp gaafagfrrg ghlapdqavg
      241 ritfdeflae rka
//
LOCUS       WP_010695236             206 aa            linear   BCT 01-JAN-2025
DEFINITION  regulatory protein RecX [Saccharopolyspora spinosa].
ACCESSION   WP_010695236
VERSION     WP_010695236.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Ragone,S., Maman,J.D., Furnham,N. and Pellegrini,L.
  TITLE     Structural basis for inhibition of homologous recombination by the
            RecX protein
  JOURNAL   EMBO J 27 (16), 2259-2269 (2008)
   PUBMED   18650935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..206
                     /product="regulatory protein RecX"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /calculated_mol_wt=22720
     Region          40..192
                     /region_name="RecX"
                     /note="SOS response regulatory protein OraA/RecX,
                     interacts with RecA [Posttranslational modification,
                     protein turnover, chaperones]; COG2137"
                     /db_xref="CDD:441740"
ORIGIN      
        1 mqmngdgarr gsgaqsrvpd dappggpsda aedskprrkp ddpeqlardt vyrlltarar
       61 scselrqall rkeidediad avlqkfvdag lvddasfaee wvhsrqrsqg lgrkalgfel
      121 rrkgveehvv eaalstvdgd aeveqarelv qrklrtmanl dhaakmrrmv gmltrkgyse
      181 alafrvvree iersgadapd pdlefp
//
LOCUS       WP_010695316             406 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Treponema denticola].
ACCESSION   WP_010695316
VERSION     WP_010695316.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..406
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46182
     Region          75..394
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mqnlldnvqk wlseysvrgd ifwlfavlav sfilhkvlkk ilsgtvkkil sritaktksk
       61 lddyifdkih vervsliiyi fafnflslkl sfgaglmqkl aslisiwivi rllhgfldgl
      121 tayteneprf agrpyrsyiq vfilivyiag fiiaagtisg kspwsllsgi gamtavlllv
      181 fretilsfva slqissydlv rrgdwisvpk ydadgdvtev alhtikiqnw dktisvlpts
      241 dlmqsgfknw rgmqetggrr ikrsifldvs svkfmdeelr rrvgkidllk syfaevessd
      301 isaqygsdte hplndrrltn igtfrmyvtr ylqsldtlrk dltflvrqle pgatgvplei
      361 yvftattnwg eyekiqadif dhlfasvhef dlrifqypvg gflsnk
//
LOCUS       WP_010695329             213 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Treponema denticola].
ACCESSION   WP_010695329
VERSION     WP_010695329.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..213
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=24673
     Region          18..192
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mikfsnllrk espeavqdrl lckavlagnt eafsliasky qkrvyslgms ffknhddsed
       61 fvqdimlktf salpkfrges sfstwlmria ynsainsvkr krefvsafdd feiktndltp
      121 eerqiqncvk nairravndl pekyricidl yffydmpyad iesvtgipvn tikshifrsk
      181 kilktelehq giygqeespe ypvlfklnla ydm
//
LOCUS       WP_010695354             303 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF4097 family beta strand repeat-containing protein [Treponema
            denticola].
ACCESSION   WP_010695354
VERSION     WP_010695354.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..303
                     /product="DUF4097 family beta strand repeat-containing
                     protein"
                     /calculated_mol_wt=34244
     Region          <142..302
                     /region_name="YvlB"
                     /note="Uncharacterized conserved protein YvlB, contains
                     DUF4097 and DUF4098 domains [Function unknown]; COG3595"
                     /db_xref="CDD:442814"
ORIGIN      
        1 mkkniilafa wfclafavia fftnelrrfk rsgykdfmrf giingkfnsh asvlkemqfd
       61 ineihsikas lisedikfip snddkiivki igieenkklp eikkekdali ikafetekkr
      121 fffgwnyshr ieisipsael yiaanagngr aentisafid stssdiriyd itlknlhfks
      181 vsgdvifrns kienqfefnt ksgdikgeaf iygftgssvs gdfklrflsa pkndstfnst
      241 sgdfsiylpk ditgfscdfn sssgdyknhf tgssaekkiy dayktdsprl fiktvsgdcr
      301 irs
//
LOCUS       WP_010695380             693 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Treponema denticola].
ACCESSION   WP_010695380
VERSION     WP_010695380.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..693
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=76494
     Region          107..693
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkirtsvnlf ltltlvivvf galtstiyyt rsfiesifyk nihyildssf selqrdiesg
       61 lvlsksfagq nnlirwfesy eedeqvgedi ktmmlslasd ekfstcfaas eltgsyyavd
      121 knknivrdql skdnsadswf ydilkkkeei fynidynktl gtvnfwfdyk vvnnrgealg
      181 lagvavnldk avekmkksip sdnswlgfig kddeviissn sdligkkiel itgslipvkg
      241 iselyycmdk dlgkviiakk qlknfpysiv lfapmvdfvp sillilrlpf iwsfailvim
      301 lilssfllrv ffgrfakmns vfnkiaegdf siradvsnde vgsitsvlnn aiekvsasla
      361 nigkhtdkmq gicenlsanm vesaaalnei taniegvrgq vltqnssven avskvdeisk
      421 giseldvhid tqtesfmsst kavveivsni egvrgkaqdn lkaikeleqa thqgketvks
      481 vvditaivte qseglldais viqntasqtn llamnaaiea ahageagkgf avvadeirkl
      541 aeesgeqgkn itkvleelks kienlngagp rvfeqfekis smmdfiyrhe dgmirtmneq
      601 lkdaeavlhe ihgmeevsqa vkegsdemll kiekisqelk tlsslsenit qsmtemsigv
      661 gqvnktvqdv tdiarvnket asgvaseiak fkv
//
LOCUS       WP_010695387             412 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Treponema denticola].
ACCESSION   WP_010695387
VERSION     WP_010695387.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..412
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45187
     Region          3..410
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mfedfinalh nfrtnkmrtl lsllgivigv tsviivtsla sslsnsmike feefsmdiin
       61 igtqmdnpef agegksikfd eafrkklmqk ipeikhvfys ntfqasiirn dlriefsdie
      121 gieaerlesh rvvmdygsff sssdystgae kaiigdriaf qlfpegravg kfitlpirsg
      181 senspphivr lqvigvvkpk ntwvlrtsda vfvprkfalr klpgkiaetv wsaevaisdp
      241 kdssnvevki qdfseelsgg nrfaiwvysa rqqfeqmtki tgmvslvlsa iagisllvgg
      301 igimnimlvt vterrreigi rkalgatgga irmqfliesa sltltgglig ivlglliskl
      361 ivnvffppei iflpnfsgsl iafsvsvctg iffglhpaik aarldpvlal ae
//
LOCUS       WP_010695396             996 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Saccharopolyspora spinosa].
ACCESSION   WP_010695396
VERSION     WP_010695396.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..996
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=107957
     Region          281..969
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mwavhglcav dgrlvlwaed selparvagr aprgpvshpf avpgealrda lageqlkads
       61 vrlqlpshps apaaspelvr dpltagpapr gklrlrewlv pavscspaav ialldegvpg
      121 crlgasahfl rsvagfaeqv vsqgrvlpsl vfeadrptar wrpslsgtds arfvalresm
      181 ppafrcergd ppaevlraal dtlvdgiara rvadvkmpgg rtaaaawlna laheprfdgd
      241 pkktrklagq ldawrasgag espvrtcfrl hepagddadw rlefmlqavd dpsvlvsane
      301 vwreesrvlq rwvaqpqell ladlgkagrv fpaldaallv phptelflda dgayefltha
      361 alldqagfgv llpswwgrtq qlglkltats sgtagtvakk sglgmdavvd yrwdlalgne
      421 rlteselael aaakvplvrl rgkwvqvdrk rlaaglayle rsgtgqmtag evllqagvhp
      481 edgdrplpvv evsghgwlgd llsgqaeqyl epvdppegft atlrpyqrrg lawlafldrl
      541 glgacladdm glgktvqlla lealarshgs raptllicpm svvgnwqrea arfaptlkvh
      601 vhhgggrlig edlmeevggh dlvittypla ardsavlrei rwdrvvldea qniknsasrq
      661 akavrglpar qrialtgtpv enrlaelwsi mdfanpgvlg slstfrarfa vpverdadtd
      721 aaarlrritg pfvlrrvktd paiisdlpdk iemkqlcnlt aeqaslyqav vddmlaridn
      781 segmerrglv latmsklkqv cnhpaqllgd gsplpgrsgk llrleeiles vladgdkalc
      841 ftqfagfggm lvphlsarfd tevqflhggt tkkardemvr rfqsedgpsi fllslkaggt
      901 gltltaanhv ihldrwwnpa vedqatdraf rigqrrdvqv rkltcigtle ekidrmiedk
      961 kalaqlvvgs genwltelst relrdlvsle aeaige
//
LOCUS       WP_010695418             435 aa            linear   BCT 01-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Treponema denticola].
ACCESSION   WP_010695418
VERSION     WP_010695418.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11720441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..435
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=47741
     Region          29..>87
                     /region_name="DUF1565"
                     /note="Protein of unknown function (DUF1565); cl23857"
                     /db_xref="CDD:305014"
     Region          189..320
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
ORIGIN      
        1 mkktiticll aalvlanlta aeyyvsketg kngnagtkda pfkniekaae kvqpgdkiyv
       61 aegnyygvrd kgfimiqkav eiyggyskdf skrdvlkyrt lvmppassng tgrankamef
      121 dikngegkkl vidgiifdkg lsngyhptkg kpqgvetgml vlppgqgvng neksitteka
      181 ifggsimkcd vliqncvfnn asnfaiqfgg tgnvkilnnv ftanamsace iwgkenkpna
      241 vtvefayntv lftwprthaf edmgygfrvm tkvevnihhn iiglsclsav drcridspas
      301 mengrkvlmd nnrffmnkqa dvtlpglgtf eyvwvkdfdd ldrfnsaegn eelkdiaslk
      361 nvlnkaylag flnatykekt dydpnspane frramgmnqt mtvqtdvsmf ankypqddav
      421 klfgavkgfg aqaik
//
LOCUS       WP_010695530             154 aa            linear   BCT 01-JAN-2025
DEFINITION  peroxiredoxin [Saccharopolyspora spinosa].
ACCESSION   WP_010695530
VERSION     WP_010695530.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..154
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16888
     Region          3..151
                     /region_name="PRX_AhpE_like"
                     /note="Peroxiredoxin (PRX) family, AhpE-like subfamily;
                     composed of proteins similar to Mycobacterium tuberculosis
                     AhpE. AhpE is described as a 1-cys PRX because of the
                     absence of a resolving cysteine. The structure and
                     sequence of AhpE, however, show greater...; cd03018"
                     /db_xref="CDD:239316"
     Site            order(25..26,28)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239316"
     Site            order(43,46,117)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239316"
ORIGIN      
        1 mtvevgaqap dftlpdfnke kvsladfcgk knvllvfypf afsgicqgel cqvrddlgef
       61 qndkvqvlgv svdspfalka waekegytfp llsdfwphge iakaygvfne aagmanrgtf
      121 lidtegtvrf aevnqpgear dqdvwkkala elve
//
LOCUS       WP_010695645             141 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010695645
VERSION     WP_010695645.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..141
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15336
     Region          13..136
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mttgegptvg vpglratkqr aavsnlldqv ddfrsaqelh eelrrqgegi glttvyrtlq
       61 tladagevdv lrtptgeavy rrcsshhhhh lvcrhcgrtv evadppvenw aerigqehgf
      121 sdvshtveii gscpdctarg f
//
LOCUS       WP_010695662             431 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Treponema denticola].
ACCESSION   WP_010695662
VERSION     WP_010695662.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..431
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48608
     Region          12..428
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(22..23,26..27,30,62,120..121,123..125,128,148,
                     151..152,155,232,235..236,239..241,244,284,288,355..356,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mqiqkrtekr nlfliyfgti tsligdeigs vaisiwvalq tdnpinfalv ysaakfsriv
       61 fslfsgsivd sfnkkkllyl sdsaqfvlni filflillnl dfklkvflfc lisvlqgfcl
      121 sifkpssrai lpeiihrenl kkansvlems kslismlavi faaglvmllg cevcilinal
      181 tffisalsei firydfkkkd aqkkaesklk kifdgyryvl sekgllrfal lasclnffct
      241 pifsniltyq fktvfmfnwq safsvinkfl kdeksfltll stivffglgi gnilgslasr
      301 kvsdknikff alvlpafsfl ilgfyfwflk ennflfniil lggiisssal lagfsmgvfn
      361 vyvtslyqkk vqpefsgrff afntvliqis spigmligss iaaigifypv flfaggilff
      421 syivycrfyf i
//
LOCUS       WP_010695700             570 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Treponema denticola].
ACCESSION   WP_010695700
VERSION     WP_010695700.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..570
                     /product="DEAD/DEAH box helicase"
                     /calculated_mol_wt=63651
     Region          4..404
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          460..521
                     /region_name="RRM_DbpA"
                     /note="RNA recognition motif (RRM) found in the DbpA
                     subfamily of prokaryotic DEAD-box rRNA helicases; cd12252"
                     /db_xref="CDD:409698"
     Site            order(467,472..475,477..479,481..482,488,491..494)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409698"
ORIGIN      
        1 mlitfkelgl ddivlqavea kgfeeptpiq vlaiprllsg eanviakart gtgktaafgl
       61 plvqelrsnt grvralilvp trelavqvag elesfrieey priatvygga aigpqlrslk
      121 tgveivvgtp grimdhlerg slkiedieyf ildeademln mgfiedieni fskanpearv
      181 lmfsatmpkq ilsiasdfmg dyeiveeepq eeraslteqf fwvvregdkt ealvrlidts
      241 pnfyglvfcq tkidaddvak elderhyeaa alhgdipqsq rekilerfrs kktrilvatd
      301 vaargidieg ishvvnyaip ydgptythri grtgragaag vavsfvrpne vkrieylrkh
      361 argelkegki psieqvieik rtrilketaa qiekriseek peqgfaafan klveygdaqt
      421 vlsfilqmqy gsflspahyk tikpvrsegr arksdedslr lyigvgrkdg itkrklaeml
      481 srllsiperl vddievmdkf slatmpknaa ndalrlckkk rglphmhidv kseapanygs
      541 igkgkrgqkq ktgtqrkren rsaaskykrk
//
LOCUS       WP_010695704             247 aa            linear   BCT 01-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Saccharopolyspora spinosa].
ACCESSION   WP_010695704
VERSION     WP_010695704.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..247
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=25800
     Region          1..231
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mtaplvavah gsrdprsaat ihalmdvvra mrpdldvrva fldlsaprvg dvlsavhgdg
       61 hdsavvvpll lgrafharvd vpaavadaer ryprfrvhva dvlgpdprld eaawrrlaea
      121 gasandpelg vllagagssh apanrlvadv aarwqsrtsw agavatfaaa aepdvpaaie
      181 alrargarri avaswflapg llpdriiela rkhatnplla apmaddegva dhryaeaqas
      241 pdlsval
//
LOCUS       WP_010695721             499 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Saccharopolyspora spinosa].
ACCESSION   WP_010695721
VERSION     WP_010695721.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..499
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53234
     Region          5..483
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(62,64,68,71,75,108,111..112,121..128,133,136,139,
                     232,236,239,242,244,419,421..422,424..425,428,431..432,
                     434,436..439,448,452,454,468,475..480,482..483)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(148..151,159,174,177,207,224..227,230,248..250,282,
                     384,386,412)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(151,248,279,282)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mtnelehfig gkrvagtsgs fgdvfdpntg qvqarvplas aeevaaavdn aaeaqpawaa
       61 mnpqkrarvl mrflqlvnde mdslarllas ehgktvadak gdiqrglevv efavgiphll
      121 kgeysesvgt gidvysmrqp lgvvagitpf nfpamiplwk aapaiacgna fvlkpserdp
      181 svplrlaelf ieaglppgif nvvngdktav dailteprie avgfvgssai aeyiystaaa
      241 hgkraqcfgg aknhlivmpd adldqatdal igagygsage rcmaisvavp vgeatanalv
      301 ekliervhql kigtsfdesa dfgplvtkqa wqrvrdligv gveegaellv dgrdfrlagh
      361 edgfflgasl fdhvtpdmri yqeeifgpvl svvraadydd avrlpseney gngvaiftrd
      421 gdaarefvsr vntgmigvnv pipvpiayht fggwkrsgfg dlnqhgpdsi rfytktktvt
      481 srwpsglkeg asftiptmh
//
LOCUS       WP_010695749             242 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Treponema denticola].
ACCESSION   WP_010695749
VERSION     WP_010695749.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19802864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..242
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=27223
     Region          3..180
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(125..126,128,155,158..159,162..163,165..166,191,
                     194..195,198..199,202)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          127..233
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          153..185
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          190..218
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mvleenkdla qkindflvqy rkivigilvc ilvavagviv wfvigenskk tsvtsvekii
       61 yeledfkred raknptaedd aednektvsa avkeaedkai eelktlgsky sssyagfran
      121 ttiaeiyfqr kmyedalkfy elaakavkns yiegvasfna aacadelgdk ekalayyera
      181 skvenfplip ralfntgrly ealskkedai lsynrllery pqnewsllak sriivltgnd
      241 kq
//
LOCUS       WP_010695752             286 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010695752
VERSION     WP_010695752.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..286
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=29347
     Region          1..278
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mpiavvtdst aylpagyaer yavrtvplhv svdgaaavde pvfgpgdlar afdrkhrvtt
       61 agatpqelak ayqdaldcga dgvvavhlsr qlsgtwdaar laarevdper vrvvdsrsaa
      121 mglgfsvlaa aeaaksgael aeversavst aertttlfsv qtleylrrgg rigtaaavlg
      181 talaikpllh vhdgridale kvrtttramt rlldislgaa gsgaaaiavh hlaaperaeq
      241 lagriraelg esadcvvsev gavigahigp gavgvvvlpn gwrsga
//
LOCUS       WP_010695753             206 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010695753
VERSION     WP_010695753.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..206
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22290
     Region          6..199
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 msldrlvlwr hgetgynaag rlqghldsal tetgqeqarr aapaiarftp dtavssdlsr
       61 arttaaafae fsgtsmrldk rlrethlgew qglsgaeveh gwpgamgtwr adptwappgg
      121 esrvevaera levveelesq hqgtallcah gglitaltak lvglpldlwp glggisnchw
      181 vvlkrrsnrd hrwrlmayna gipveg
//
LOCUS       WP_010695784             328 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Saccharopolyspora spinosa].
ACCESSION   WP_010695784
VERSION     WP_010695784.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..328
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36047
     Region          15..192
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,101)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(48,100..101)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            99..101
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mtdaapevev sllapakner enlprlfaei rdamqeqhrt wellvvddgs tddswqviae
       61 qarqdprfrg irlrrnfgka aalaagvaev rgkllvtlda dlqddpaeip rllaeldnga
      121 dlisghkaqr qdplgkrlps kvfnwvtgli tglkladhnc glkaartevy rrvplygelh
      181 ryipalahql gyrvrelavh hrprvhgksn ygleryvrga ldlltvvalt rygrrpahlf
      241 gglgllagti gtlillylsg vwlftdqsig trplltlgil leifavqmis vgllaelvlh
      301 rtgrgrdvdv lvadqttnas paqsgksp
//
LOCUS       WP_010695787             498 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010695787
VERSION     WP_010695787.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..498
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=52987
     Region          4..498
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mneiveldsg rvrgltyekh rlfqgipyaa ppvgelrwcs pqpvapwpqv rdatepgnpc
       61 pqlpqdfadi asldedclfl nvtaprtggs kpvmvwlhgg ggangegaif dahrlavaed
      121 vvvvtpnsrl gifgnfaypg laggggfgie dqqavlrwvq rnigafggdp gnvtlfgesy
      181 gglnvsahlv apgsaglfhr aivqsgfall rspagawapg spkmpaiwls ivefeglaeh
      241 lvgqlgwvqp gkgsaieqlr ripveqlinv ssvfsrpvfg gavlpespeq alpggrfhrv
      301 pvlaggtrde arlftalfwd aagqpitpdg ydklladgfd aaadkvaery pvdahatpsl
      361 awadvigdaa warsvwdlat alsaetttyv yefadrdapp vvpfppgfpp gahhsaevay
      421 qfdlgnpapl teaqrqlaat inrywanfar sgdpngpdlp gwqtfsaadp hvqslhpeqi
      481 tgtdfaaehr ldfwnala
//
LOCUS       WP_010695855             310 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Treponema denticola].
ACCESSION   WP_010695855
VERSION     WP_010695855.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..310
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34975
     Region          4..307
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mfsdshahff mifkrnegda sflhtmmerk frfamdigtq pgdlkerqkf vsdvfdgkiq
       61 gqetvhlper fpdfmhfaag lwphaesiae pekalaalkt didtlflqka eaektnsgkl
      121 fycglgecgl drywngpaae krgggvqadd ekgttdiege eflfkeqlki akeknlsviv
      181 hsrdayedtl kcidevghhk giihcysygl keaysflerg wyisfpgnit yakkqadkdr
      241 iaelvravpa dkllletdap ylapvpfrgk intpllieyt yaavseildk smealaeqiy
      301 qnccscflvk
//
LOCUS       WP_010695836             226 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010695836
VERSION     WP_010695836.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24617
     Region          3..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mskdivlisg ltktfssase klvifdklnf sieegkkisi tgesgsgkst flnilggles
       61 adsgeiiags ykvhsldeks lteyrgsflg lvfqfhyllk dftalenvml paliagrskk
      121 eikekalsll edvklaerkn hfpsqlsgge rqrvavarsl inspslilad eptgnldpan
      181 aetvqnllfs vvdkhkktlv lvthdqnias mtdisyklyk gnleev
//
LOCUS       WP_010695847             489 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Saccharopolyspora spinosa].
ACCESSION   WP_010695847
VERSION     WP_010695847.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..489
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52233
     Region          15..462
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(21..22,25..26,29,61,111..112,114..116,119,139,
                     142..143,146,270,273..274,277..279,282,310,314,366..367,
                     371,375,391,394..395,398..399,402)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 mrrleykwlv gitfvlalim qildvtilnv alatlgrefr vdaaalqwvl tgymislavf
       61 ipssgwiadr fgskrtfqta vviftfasvl cgvstemwql vgarvlqgvg ggmlvpvgqa
      121 mlfrafppde rakagavlai pitvapmlgp vlggllvqya nwrwiffinv pvgalalffa
      181 vvflreeprr dpgrfdfpgf vlagaglatl lygleqgaql gwgqpqvwss lvaavlligg
      241 lawreltvth pmldlrlltd rlfctgnvll lcqtgamfgv lfliplylqn lrgvspmhag
      301 lvlmpqaism llttqvisri ygrvgpkrli lagfavqvai glglqlqgtd tslwllvall
      361 avqgvamgll mtpvqtatfa risradmgqa ssmfnvsrqv atalgtaiva tvlvmltehg
      421 mstvdptaag qvaeaqlgay hgaflvsvvf aglglllglr vrdsdaaasl dtpatktqps
      481 erepsktvr
//
LOCUS       WP_010695923            1657 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Saccharopolyspora spinosa].
ACCESSION   WP_010695923
VERSION     WP_010695923.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 1657)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1657
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..1657
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=183119
     Region          32..1656
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mtsnpgqlkt gersradgdd aagersenpe lakrrlldra vefapelael lhayyrhvpa
       61 eelvddeptd lvgalrshyr lasarvagrp lvqisnpdrd ddgwqsqatv vqivtddmpy
      121 lvdsviaelg rdgaevqrii hpifvvrrdv agelqevlpg adpaeppada iaeswmfvev
      181 drvvdeerls vlqhgltdvl ndvrevaedt ermhatakal sdelertpll lpgeevhnga
      241 ellrwladgh ftflgyrhye lvngsgpalq avlasglgvl rsdsvaarsl tagpdvlasa
      301 lskdllvltq asapstvhrp vhpfyvgvkt fdesgqvnge hrflglfnta alhedvldip
      361 fierrvreii hragfpmesy sgqrmleeiq nyprtelfst dpdtlqetit gvlalaerrk
      421 lkpflrrdpy grfysclvyl prdryttssr lamqevllee lhgtgleyst rvgestlarv
      481 hfvvhtdpeh qvepdlariq rrldeaihtw ddqmieevda eqsgagrdgh hatrslseai
      541 sqigqscass fpesykedft aaegladlrr leslsgsrdl kmsfyaprda sagqrrfkly
      601 vggrvtlsrv lpvlqsmgve vvderpyevi vgdtdqqywi ydfglrldps lldsatsggl
      661 ldtlrerfed afraawlgda evdrfnalvl raglnwrqas vlrayakylr qvgvaysqdy
      721 iedailahrt ttttlvrlfe trfdpalgad drasreadlt ddvarlidev tsldadrilr
      781 sylsliratl rtnyfardeq rersylalkl epreipglpe prpqfeifvy spwvegvhlr
      841 fgsvargglr wsdrredfrt eilglvkaqa vknavivpvg akggfvvkrp ptptgdpavd
      901 rkatldegia cyrmfisgll dltdnlvgge vapprdvarh dgddtylvva adkgtakfsd
      961 iandvaksyg fwlgdafasg gsvgydhkam gitargawes vkrhfheldv dtqsedftvv
     1021 gigdmagdvf gngmllsehi klvaafnhmh vfidpapdta vsfaerrrlf elprstwddy
     1081 drtkisaggg vwsrslksip lnpqirqalg idesvrqlap aelikrilla ptdllwnggi
     1141 gtyvkaatet haevgdkand avrvngadlr vkvvgeggnl gltqlgridf araggkvntd
     1201 aldnsagvdc sdhevnikil ldhlvtdgkl tgeqrnella dmtdevgelv ladnhsqnav
     1261 lgisrahaap mvsvharqvt alekstgldr klealptpke frdrekaeeg lsspelatlm
     1321 ahvklslkrd vlasglpdae vfssrlpeyf pkplrehygn aiaahplrre iittllvnem
     1381 vdgagisyay rlseeisast tdavrafavv tnvfglrelw aqidalgrsm pssvadelvl
     1441 esrrlldraa rwmltnrpqp laigaeisrf qpvvaelsds vrgllrgraa egttemvdgw
     1501 vaagvpedla ervgvlldsf alldireiae laerdagvaa erspgesadl yyslaehldv
     1561 ermllavnel ergnrwhsla rlalrddfya slraitidvl rtsdpedspe ekiarwestn
     1621 esrlaranss meqiknsgrl dlatlsvaar qlrsmvw
//
LOCUS       WP_010695909             564 aa            linear   BCT 01-JAN-2025
DEFINITION  YifB family Mg chelatase-like AAA ATPase [Treponema denticola].
ACCESSION   WP_010695909
VERSION     WP_010695909.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Walker,C.J. and Willows,R.D.
  TITLE     Mechanism and regulation of Mg-chelatase
  JOURNAL   Biochem J 327 (Pt 2) (Pt 2), 321-333 (1997)
   PUBMED   9359397
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427378
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..564
                     /product="YifB family Mg chelatase-like AAA ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61819
     Region          3..555
                     /region_name="YifB"
                     /note="Predicted Mg-chelatase, contains ChlI-like and
                     ATPase domains, YifB family [Posttranslational
                     modification, protein turnover, chaperones]; COG0606"
                     /db_xref="CDD:440371"
ORIGIN      
        1 meilsfssfg yegelikvea dlrrglpvid ivglpgsavk eardrmraai rnsglefpvs
       61 rilinlspad qkkegsgfdl piaiavltak eaekksaevk akaqtiipqd edraeksvmi
      121 mgelelsgrv rpvrgligai saarsqgiky fivpkeneae aliedginvf gvsdlieale
      181 ffyqiesgkf ntkpqglkke sfpdtgtapl fvwsdteepe dfdfqkdski glglvkgfed
      241 irgqdglira leiaaagghn liaygppgcg ktlslsrfsl llpdmeekta mettriysia
      301 gllpqssprl lkrppfrmps qnasmegiig gagkcmpgev slahggvlfl deaaqfkasv
      361 lqslraplet gsvtlsragr sstfparfql llainpcpcg nfgspgkvct clpyeiekyw
      421 kkltaplldr idirvpvmpp kpenilaeak ystqtmreki knarliqwer lkftnkekkm
      481 qniiyenakl spqetaevck msgeaerffs vivdskklsg rgshallkis rtiadiessk
      541 nislahieea aalrqwikyl pdfl
//
LOCUS       WP_010695998             502 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp70 family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010695998
VERSION     WP_010695998.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Fernandez-Fernandez,M.R. and Valpuesta,J.M.
  TITLE     Hsp70 chaperone: a master player in protein homeostasis
  JOURNAL   F1000Res 7 (2018)
   PUBMED   30338057
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Mayer,M.P. and Bukau,B.
  TITLE     Hsp70 chaperones: cellular functions and molecular mechanism
  JOURNAL   Cell Mol Life Sci 62 (6), 670-684 (2005)
   PUBMED   15770419
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Bukau,B. and Horwich,A.L.
  TITLE     The Hsp70 and Hsp60 chaperone machines
  JOURNAL   Cell 92 (3), 351-366 (1998)
   PUBMED   9476895
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Rensing,S.A. and Maier,U.G.
  TITLE     Phylogenetic analysis of the stress-70 protein family
  JOURNAL   J Mol Evol 39 (1), 80-86 (1994)
   PUBMED   7545947
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..502
                     /product="Hsp70 family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
                     /calculated_mol_wt=53042
     Region          6..476
                     /region_name="DnaK"
                     /note="Molecular chaperone DnaK (HSP70) [Posttranslational
                     modification, protein turnover, chaperones]; COG0443"
                     /db_xref="CDD:440212"
ORIGIN      
        1 madelvlgid lgttysavas ivdgdvevvr nrlgelttps vvhfasagta vvgaaardsl
       61 dpentvelik rrmgtafelm fhgarhtpes vsalilrslv ddaiarfgph gtvravitvp
      121 ayfgirerea tlqaarlagi dvlevlsepa aaalhyatqa esgaalvydl gggtfdttvl
      181 rvaanevhvv atdgdsrlgg tnwneriaeh ladaftrefp gadpddedfq qqlqdateqv
      241 krqlstvtrr rvglrcgada asfdidrktl edlgadlvdr tlrivdrala aaaakgvsri
      301 devllvggat kmpairtalq ahlgrapkiv dpdlavvsga avrarrlass qagarttaav
      361 vprsfgvlie dshdeklrsf vehlvhrnep lpavatarfa tivdrqrsvr iqvfeqsgdv
      421 pspevghnrr vldgefaglp plpagsviev tlrvsadgll avtareplgg aaldleayvd
      481 gvvdgaeteq laetiaglsv rc
//
LOCUS       WP_010696015             244 aa            linear   BCT 01-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010696015
VERSION     WP_010696015.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..244
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26472
     Region          14..230
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 maddlkpmpq dwrralaiva hpddleygcs gavaawtasg revayllvtr geagidgvtp
       61 edaaplreae qiasaaevgv rsvefldhrd gviehglplr qdlarairqh rpelvitlnh
      121 hddwgpgswn sadhravgra vldavadagn rwifpelieq gyepwrgvrw igiaaspqpt
      181 haeditgtld ravaslaahr tylealsdep aeehargfle aavhehadrf ggracvtfel
      241 igea
//
LOCUS       WP_010696097             330 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Saccharopolyspora spinosa].
ACCESSION   WP_010696097
VERSION     WP_010696097.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..330
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33502
     Region          3..330
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mpevlvlier vevdgvrevt kpslelltia rrlgdpsavv igspdadvag tlkkygaaki
       61 ysvstgegae dagvsgylva peaevlaqli ektspaavlv vstgrgkeia grlavktesg
      121 litdavdvta adgtpttkqs vfagsfvvqa rvtkgtpiit vkpnsvtpee vdgagsdvae
      181 eafavtisda akgakvtgae prkasgrpel teaaivvsgg rgtggdfepi qafadslgaa
      241 vgasraavds gwyphsfqvg qtgktvspql yvangisgai qhragmqtsk tivavntdee
      301 apifelvdfg vvgdlhtvlp aatdainrgr
//
LOCUS       WP_010696098             271 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Saccharopolyspora spinosa].
ACCESSION   WP_010696098
VERSION     WP_010696098.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..271
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27799
     Region          1..271
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mnivvcvkyv pdaaadqkfe ddntvdrigv dgllseldey aveqalqike tgddpdstvv
       61 tvlsmgpeqa tvavrkalqm gadkgvhvvd dalagsdala tslvlaeaik klgagpgwdl
      121 vvcgmestdg gmgvipamls erlgvpgvtl gseitvsske ggavvrirrn gdastdtieg
      181 tlplvlsvtd qscevrypsf kgimaakkkp vetwslgdlg vgpgqvgsga awsvvesaip
      241 rpartageiv tdgdgsgaka lvdflaskkf i
//
LOCUS       WP_010696106             224 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010696106
VERSION     WP_010696106.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..224
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24244
     Region          5..223
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtglnplepr nenltdlvfd sireaivdqt lppgsrvseq riasqlnvsk tpvregllrl
       61 rhiglvksfe rglrvvtpsv hairnayefr agiertaayy aahradnaqr eelmklarts
      121 ldaatagnal gfrasdrafh rliataadnd vliravedtl tlttvlrerd vpstgdsvsc
      181 ahehiaiaqh ilagaadeaq keagdhvlhv mslvlaahta laqp
//
LOCUS       WP_010696170             340 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Saccharopolyspora spinosa].
ACCESSION   WP_010696170
VERSION     WP_010696170.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..340
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34542
     Region          30..300
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mslglhesvq raaqarrprl rlprgpfvpv wamtavlfai spliapgsls gaalssmlpf
       61 aailvlaalg qafvitqrgi dlsvpgamal aalfatkvpe ltglplavsa vlgllagaag
      121 glvigvlvvr fgiaafvatl amntiligvv leiskgfpas anpavsafat gslwtvpnll
      181 ivavilvait qwlrrrsvlg rrfvsvganp aaarllgmra egyqvsayav ggllyalagl
      241 llaaylrtpd illgntyqls siaavvlggs lltggmssav atgvaalflt qlnqvvlaag
      301 aatsiqllvq aavlalavvl rrvplsaipr rlsgnraksr
//
LOCUS       WP_010696188             383 aa            linear   BCT 01-JAN-2025
DEFINITION  LLM class flavin-dependent oxidoreductase [Saccharopolyspora
            spinosa].
ACCESSION   WP_010696188
VERSION     WP_010696188.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..383
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41384
     Region          46..348
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mtdlvgtiga gvedgrpfrl gfllhldddq pparayreai elfavaeelg ydsgwviqrh
       61 frqgnehvsa plillaaiae htsrialgtg vlvlpledpl kvaedaatld elsggrlelg
      121 vgsgpfpgaw eafgkdladr hrlfdesvar lhevlegtal nslgevlhpp aagvrrrlwq
      181 attsdpqrag agaaaaalag dglqfsratg wrgttvreaq hqqarwiedy raawrepdrq
      241 arvqvsravy phpdretavr lvtpgvrrwq swlstrrdva gldveeylaa drallgppda
      301 laaelaadpa lrqitdllvs fvpgvpdfde hvrlltagaq elapllgwrp aplssarpad
      361 rplvgtghht grsdrattsr gtr
//
LOCUS       WP_010696218             281 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Saccharopolyspora
            spinosa].
ACCESSION   WP_010696218
VERSION     WP_010696218.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..281
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30660
     Region          5..260
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnngadslpe rvrvrydqls ksqrkiarfc ishaaeagsl tamriaeklg vsestvvrfa
       61 ikigydgfpq mqdalreelr gaptpsgeht erdthdvale slrndldalq qsideidlaa
      121 ltrattalge atnvyvcgfr tsfslayqay fhlrkvrpsv rllgdiggtl vddlemiepg
      181 davlaftfpv yddraiqvan ravsvgascv vvtdsalapl pidpllhllm vrhdslsffn
      241 stvaatalln siivrlaear srqepsfert lsksfhtkgk l
//
LOCUS       WP_010696226             319 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Saccharopolyspora spinosa].
ACCESSION   WP_010696226
VERSION     WP_010696226.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..319
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32309
     Region          3..317
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 maevlvlvdh vdaevkkvtf elltaarrlg epsavvvgep gtagkltesl aaygaakvys
       61 aesaeaagfl vtpqvdvlsg lvgsvspaav lvpatvdgke iagrlalrlg sgllsevvdl
      121 dgdgvgahsl fggaydakar itkgtpvitv lpgaieaeaa egaaaeeave vpaqdaskaa
      181 ritgrrpvea gdrpelteas ivvsggrgvg saesfevvek ladsmgaavg asraavdsgy
      241 yphqfqvgqt gktvspqlyi algisgaiqh ragmqtskri vavnkdpeap ifeiadfgvv
      301 gdlftvapql teeitkrng
//
LOCUS       WP_010696262             134 aa            linear   BCT 01-JAN-2025
DEFINITION  RidA family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010696262
VERSION     WP_010696262.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..134
                     /product="RidA family protein"
                     /calculated_mol_wt=14148
     Region          6..131
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msrsfrqein apgvpaprgh fshavvvndl vyvsgllaln drgkikdpgd araqaatifd
       61 sleailaaae tspemliklt tyvtriedrs vlnalrnerw pgiraastlv evsnlagdga
      121 aveidavaar rgqg
//
LOCUS       WP_010696271             253 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010696271
VERSION     WP_010696271.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..253
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26604
     Region          4..253
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msngsrtsst vatalrllkl laenpegigi sdiarrlgig kssahllvst lvqqdfalrn
       61 deslyvlgit afevgsavpd aarfggella pmreladisg eavslaiprn rdavivqrfe
      121 tkhvlraeig igtrmplvsc asgkvllaam seaeidnlyp deelprvtrh tlrskaslka
      181 tvlpvvrehr yaltegeyae gitgvaagia dasgalvaal svagpssrfh paewvdpllt
      241 aadamtalla srr
//
LOCUS       WP_010696283             447 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Saccharopolyspora spinosa].
ACCESSION   WP_010696283
VERSION     WP_010696283.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..447
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47750
     Region          23..410
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,259,262..263,266..268,271,299,303,352..353,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtelatigrt nqqrcdlskr ifrrivpllc vvyvisfldr tnigfakdrl evdlgisaaa
       61 yglgaglffl syallevpsn llmrkvgakw wiarimitwg llssamalvq geisfyvirl
      121 llgaaeaglf pgvilyftyw ftreerakan gyfllgasia nivgspvagl llsldglggl
      181 hgwqwlfive gvpavvlafi vlrvlpdspq saswvtkeev rdlqarldae advaqertgr
      241 hpvaqvlrdv qilmviavyf chqvaiyava yflpsiigsa nsltpiqtgl ltmlpwlasg
      301 vgalllprla ttasrarlli atalivmafg fvlglvagpv lglvgmcisg fvfwcvnsti
      361 ftfpasrltg aalagglafv nscgilggfv gpylmglmen atgnpasglw avavllvvga
      421 vlamllrqgh egpsvdtpar ksslefd
//
LOCUS       WP_010696287             217 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010696287
VERSION     WP_010696287.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..217
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23600
     Region          9..216
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mrsladdipl tqriydelrd alvrgeleag klysvveisr qlgvsrtpvr eallkfaseg
       61 vvsferskgv rileasvtdv hdlfglrlll evpsaalaav senseqldrm rqafsameda
      121 cargnelafq qhdttfhdai lraagnaqva eavsrargqa htrrlsttht rslaeviaah
      181 reihdavlsg dearasaavk ahltetrdil iaqiskp
//
LOCUS       WP_010696291             438 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Saccharopolyspora spinosa].
ACCESSION   WP_010696291
VERSION     WP_010696291.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..438
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46539
     Region          17..415
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(24..25,28..29,32,64,114..115,117..119,122,142,
                     145..146,149,249,252..253,256..258,261,289,293,344..345,
                     349,353,369,372..373,376..377,380)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mddapltwfh rrltlysagg plldgyvlgi iglaltqvvp lwdlspvwqg llaasallgm
       61 flgglvfgyv tdlvgrqamy tidlaaivvg svaqffvdgp vwllilrfvv glaigadypi
      121 atsllaeftp rrhrgsmlgw lttmwaagnt iaylvgeall elgpdawrwm llspaipaav
      181 lmvarfgtpe sprwllskgr teeakaalrk algpdaeldd lpaepgetsl rgliskgylr
      241 rtvfvavfwa cslwpvyaiy afgpallsal nlddprqanl gsaaigvffl agcviatlva
      301 nrlnrrtlli wpfavatval lllgliptap tpviatlfvl yalaiggpti lqwiypnelf
      361 ptairatavg lgttvsriga gvgtfvtpil lghmgigatm llaglicvlg livsvlmape
      421 trhhdlhqas svptdtgk
//
LOCUS       WP_010696368             392 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Saccharopolyspora
            spinosa].
ACCESSION   WP_010696368
VERSION     WP_010696368.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..392
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42109
     Region          7..392
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mthafarpad rlaaikpspi raifdraakl eadghkiyhf eigrpdfdsp avakqatida
       61 lesgkvhyap nagtadlraa iseyladkrh tqyqpngeii vtvganeavf laimafcgpg
      121 devvvpipaw ahyqscirla gatpvevpld aangyqldle alsaaisdrt rmvvlctpnn
      181 ptgtvasksd vdaiaemlrp tdalllsdei yadltyevdh aspasyeqlh prtlsvggfa
      241 kafamdgwrl gwlagpaeli apalrvrqyt tvcsttfiqd ggaaalrsar deaesmrqsf
      301 earrnaalqa isgtdklrva spdgafylyl syepetaepa eelavrllee hhvavvpgta
      361 fdphggthaf rvsyacpled lteglrriia al
//
LOCUS       WP_010696381             313 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Saccharopolyspora spinosa].
ACCESSION   WP_010696381
VERSION     WP_010696381.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..313
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32414
     Region          7..224
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mdtppavrar gitkcfgdvv aldgidldva qgqihglvgp ngagkttllg lllglavadg
       61 gtleilgtpv grslaapdav agfvdgpgly psltakqnla alavlrgrda rtagiddvld
      121 qvgladvadd rvrgfslgmr qrlglaaall tkprllvlde psngldpagk qhvhgvltrl
      181 aadgtsvvls shrmddleal ssevtivttg rvvfsgplsk laaenqeldy rirtsdpdaa
      241 rrlaadttgv rvaddvgtrh dtevlvvral vpaldelvvr lvhagialre lapvvsplea
      301 vflalteqqe ssr
//
LOCUS       WP_010696415             244 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Saccharopolyspora spinosa].
ACCESSION   WP_010696415
VERSION     WP_010696415.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..244
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27289
     Region          1..188
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtvppgnapq rgsatenaye hikhliltse lapgeelrev altestgfgr spvrealrrl
       61 vqegfvevrp rqgyrvsvit lasvqdlfem rlvlepvave faaqrapkee lealhalahk
      121 tyvhgdtrsy eqflqdnref hvriakatgn erlaralqgl leemqrlffi slgnrdrase
      181 mvhehhglhd allardaara reivveqiea srarvlegli egtnrgvrpa tgivlaekts
      241 qrrk
//
LOCUS       WP_010696447             292 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Treponema denticola].
ACCESSION   WP_010696447
VERSION     WP_010696447.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..292
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31402
     Region          8..289
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mkvencdvgf iglgvmgksm aerlraagak mhvftrtkks aeeilskgav wyddpaslap
       61 nckiiftivg ypqdveetyf gekgllktak pgtifadmtt sspilakkiy deakkkecfs
      121 vdapvsggdi gakngtlsim aggdekafke lepffacmgk twalqggaga gqhtkmanqi
      181 avaanlfgtv eavcyaeaag ldpqkmllai gggaagswqi lnngpkmlqk dfapgfyikh
      241 flkdlnitln vakelklhip vlelaqnffn kmneegyaek gtqaiyeyyk ti
//
LOCUS       WP_010696593             421 aa            linear   BCT 01-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Treponema denticola].
ACCESSION   WP_010696593
VERSION     WP_010696593.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..421
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47328
     Region          40..354
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mlkkiktadl kigvrfsapv ffddgknmfl lrgmalsene ldtlkrwkvq yvvtagdpvp
       61 egetlddeia eldeideied ledpeeieev eedypingtk ikraeieeis adcilkltqd
      121 arsmqlytey laiikniekl fenfkarrpv dnmpvtyhae elmelvrknp plcvgfilgt
      181 eleedslars svntailtii lsealelpkn rineitiaal lhdvgmmkip qkilnktetl
      241 tdiekqaiaa htaygyktam selmytreia lsimqhherw dgkgypngls gkdidigari
      301 itaadafvam itpkpyrdlm lgyqamknll adnarifdpe iikvmirsig iypigsivlm
      361 ndaslarvvk sspeapmrpf vrvlidatge vltgdsepld lkknknlfiv raidprayrn
      421 k
//
LOCUS       WP_010696606             290 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Treponema denticola].
ACCESSION   WP_010696606
VERSION     WP_010696606.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..290
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=32386
     Region          20..269
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 mnisleqiqt fvkenftlps fvsilsflgi ilityiffki iikslkkfte nkvspaiqnl
       61 itkilqytcl avilmtifkk lgininafvg aagiagvaig faaqtsvsni isgffvlaek
      121 afkvgdriql gditgnvesi dfmairvktl dgnivripne vvikgnliny sslpirriet
      181 kisvaygsdm ekvesvlmei pnrvpqilks pepfvfwsay adsgievafy awgknedflv
      241 iknsifklia elfeeaeini pfpqmdvyin pertkkepvf yesaeneqvf
//
LOCUS       WP_010696608             233 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Treponema denticola].
ACCESSION   WP_010696608
VERSION     WP_010696608.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..233
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27010
     Region          5..231
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mkygisaiaf didgtlypsw rfnlriipfl lkhfnfmsaf nktrkdirlw qeknpdkvls
       61 nffdfqaeil akyagrnken vknfleteiy egwkrrfari kpfvfaresi eefkrcglki
      121 allsdflpeq kndvwgilpl cdaafgteti galkpsplpf krlaealdlp cdkilyvgnn
      181 lrydvagaka agmhtaciks rlfillkkvf vqkdnekpdi yfsnyrqllk fmi
//
LOCUS       WP_010696637             330 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010696637
VERSION     WP_010696637.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..330
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36932
     Region          5..324
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mknpllevkn lhtyfftnkg tvkavqgvdf tieagktlgi vgesgsgksi tafsilnlle
       61 ypgrivqgei nfggvnlvnl dkheirkirg ndismifqep mtslnpvhrv grqlseplil
      121 hqhmskkeaw aaaidllrev kipnpenvvy nypfqlsggm rqrvmiamal aceprlliad
      181 epttaldvti qaqifklmnd lkkkhntaim fithdlgaia eladdvavmy tgeiverapv
      241 dvifdrqtqf shpykeglle siplldeeve ylaqiqgsvp hplklpkgcr fstrceyate
      301 kcrnekpelv eveeghlirc fypksggrhe
//
LOCUS       WP_010696668             269 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Saccharopolyspora
            spinosa].
ACCESSION   WP_010696668
VERSION     WP_010696668.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..269
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26912
     Region          2..268
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlvsflvllg fgcltgvttv lfgfgggfii vpvvfavvsa atgadamhta vatstavmiv
       61 nassatiaqa rsgrlhgkql hpliefialg avigavaanw apgsvlhvlf iaylaitivd
      121 sivrsgfldn arhqtsggkp lgkvastlgg lgigavasfl gvggsvmtvp llrrrglpms
      181 aaaamanpls ipvavagtav yalatpaaay pgqlghvnfv vaaallcgsl ptialtkrvv
      241 gkipdhihai aylvllvivl iamiatalr
//
LOCUS       WP_010696682             284 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Treponema denticola].
ACCESSION   WP_010696682
VERSION     WP_010696682.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..284
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33158
     Region          38..111
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 mniksisltd kiisqkevkd flqkanlnqk gnliglfdkk kiigagsiyt nsfhpyrdyi
       61 nihidkdyrn kglrsrllka lkeksekkrf qvmcssgkee liqfllkegf vlarrsysfd
      121 lkkeaqnifl skevsdefkn iqmkplinln skekeefqki fyfnyadthk sinplnkdic
      181 ikkfsneila dcdkeksscl isnnkvsayv ivyiekfpei gylggktiee ietylnyfqv
      241 iinnllnaye qiyfeiddid yyafplmtal qinckesynt yild
//
LOCUS       WP_010696711             409 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dicarboxylate/amino acid:cation symporter
            [Treponema].
ACCESSION   WP_010696711
VERSION     WP_010696711.1
KEYWORDS    RefSeq.
SOURCE      Treponema
  ORGANISM  Treponema
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Treponema"
                     /db_xref="taxon:157"
     Protein         1..409
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44533
     Region          1..406
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkiwikylig svlgiiiaal sssdsaffna avdfaaniai qfgryslypv lffgftvsis
       61 klresrsllk lsiyiavfii lssllaallg lisisisspp ripifveets avenlgvmes
      121 flrllpssaf eafmdglyil plcifagfag aacavdknis kpaltlfdsl srisyaimaf
      181 fvdmfsigli avsvnwcikf qamlstkfft glvvlllvdf fiialiiypi ilkiicrdin
      241 pykvlyasia pvcaaffsgd tnltlpvllr hsneslgvrr rissvslpvf svfgragsam
      301 vvtisfivil nsysslgisf edrfwlvgis tlfsfflgrf pitgtyvslv tvcaiygrgf
      361 esgflilrpa affigsvaaa idaltamvgt yiighlskmt ntrtlrffi
//
LOCUS       WP_010696730             725 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Treponema denticola].
ACCESSION   WP_010696730
VERSION     WP_010696730.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19960403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..725
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=81193
     Region          <30..>257
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          <197..707
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          301..333
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          339..367
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(377..378,381..382,384,408,411..412,415..416,
                     418..419,442,445..446,449..450,453)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          377..401
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          406..436
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          425..673
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          441..469
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          477..503
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(479..480,483..484,486,510,513..514,517..518,
                     520..521,544,547..548,551..552,555)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          508..538
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          543..569
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          576..606
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          611..639
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          645..673
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          679..706
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtdfqkflig ilagifiavl vvvgilfftk nkssdsaaad tqilakieae keelarlqek
       61 iakkeaeleq akkeaekere lleaesikka eeinknlaaa sekekkaaee ekkrkaeeal
      121 kraeearkrq eelikqqqal keaeakkkas ideakkiaaa kaeadrkaka eqerkakeea
      181 erkakaeqer kaklaaeqka kdeaakktad aerekkrlee eakkkaalda qkaqeaerla
      241 kqnadaktra qmeeverlvs eginflkngn lnsalstfsk asskmpdsea sftakkyldm
      301 asalndyasa regtgdaeka lsdadsyikk svnadgqnar ahyvysqiad aqkqpqvafv
      361 elekaqsldp dnylynyelg kkyyarghyq kaktsfersv ksnpkfdsaf fnlgmscrkl
      421 gleneafsaf ssavkikpdy vkaflemari rkaqrkfdqa ienyknavsy epanlpalre
      481 maqvyadlgq nnlaerhfke aitlgeddai tyynlatvqv dlekygeals naekayklkp
      541 adarvlytyg ltlekngrks eaydyytqaa stnknyakpr inlgrmylde gkfgeaeenl
      601 laayrlepnn fevntnlgkl yglkgdytks vnhysnavkn qprnitakqn laaayisadl
      661 kenavsvyeq iikvdtknwd ayyelgklyi sldkkadakl ilegvlnknp nyskaaeirs
      721 ilssl
//
LOCUS       WP_010696744             293 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Saccharopolyspora spinosa].
ACCESSION   WP_010696744
VERSION     WP_010696744.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..293
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=31414
     Region          1..140
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          153..290
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
ORIGIN      
        1 mskpvvvgfd fsessrravr watreavsrr rplllvyvit wpfegvtvgp lpggddvleh
       61 lqkglqhqlg vlaegcreie palevrselp fgdpveelst laaqaellvl ggarvdshsv
      121 lgstsaella rrsgapvvvv redrerpvpa sapvvvgvdg satselavgf aydfasrhdc
      181 elaavhswsd lpldpfarvr gwklpwnevr gdadevlaga iagwgehypd vvvrrvvtpe
      241 rpaeallrea reasllvvgs hgrgrirral lgsvshavan rapcpvavlr agr
//
LOCUS       WP_010696753             143 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Saccharopolyspora spinosa].
ACCESSION   WP_010696753
VERSION     WP_010696753.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15181
     Region          9..139
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mseqrdysiv vgidgsspsr nalrwavhqa rsnnghvtav mswqlpelyd wpmptaeecd
       61 ratekalatv iretvddvda aairgevarg hpakallkaa esadllvvgy rgaggiahal
      121 lgsvsqycvn hapcpvvvvr dha
//
LOCUS       WP_010696763             350 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease
            [Saccharopolyspora spinosa].
ACCESSION   WP_010696763
VERSION     WP_010696763.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..350
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37389
     Region          32..320
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mrsvsdpara aklvgllala alvvafpgla pdpfilsvgv vimsyavlat swnfvggftg
       61 yislghaays glggyatall vvradlnpwl alvlggvvia vlavpigvas lrvrgasfvi
      121 vsialvlitl lvfqswgdft ggsnglrvpr pfgpevlrpe qherffylha allavallcw
      181 waidrsrfga glkaireded kaealgvptf tyklvafvvs afftalgggl yalwfgfldp
      241 ifqfsvltgs ylvlmsllgg vrslfgpvlg alivgyavey fkaqygdtql hlvalgvlla
      301 avvlfmpdgi ipalrdllhr frprrasire vsqaelaeqr ragtveearr
//
LOCUS       WP_010696776             305 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine recombinase XerC [Treponema denticola].
ACCESSION   WP_010696776
VERSION     WP_010696776.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11493900
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..305
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=35102
     Region          6..305
                     /region_name="recomb_XerC"
                     /note="tyrosine recombinase XerC; TIGR02224"
                     /db_xref="CDD:274042"
     Site            order(146,251,254..255,286)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 mnevfenylt ysagvrqftk atidsykndl vifeewlkel dlnvfelkas dirifiaela
       61 dkkiapasin rmmstlrgfy kyalrfnltk inpissvrnl klaqklpvfm fpkqaqefck
      121 lpsntdilwe trdaalfasl ystgcrvsel agldikdldk tlsyaivfgk gkkerkvffa
      181 efakeylrey lkeradlvek fkgqvqkdhk gkirdalfin qkaqaltsrg iryiinryve
      241 lspelkhlsp hafrhsfast litrgadirv vqellghesv sttqrythit aeqlqnlykt
      301 ahphs
//
LOCUS       WP_010696798             175 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Treponema denticola].
ACCESSION   WP_010696798
VERSION     WP_010696798.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..175
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=20243
     Region          23..>148
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mfnfdkktey ddflellkkt dslnslnlsg lefdgldfsk ksftgcifsn skfkncncsn
       61 lhlrmcffdf ceiescnfqn sdiqfssfgg akiirtdfkn sellqnnfng iraeevffnd
      121 sdlyssrfmf sflknvyfqn cnlkktlflh skedavsyks sntreavfte gdefv
//
LOCUS       WP_010696811             294 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Saccharopolyspora spinosa].
ACCESSION   WP_010696811
VERSION     WP_010696811.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..294
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=30777
     Region          6..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          156..292
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
ORIGIN      
        1 mqafdvvgid gsdiaadavr waaadaalhr aalrlvcvva ggaddaddgm ptspnvlgvi
       61 enerrrwlsq aaelaatvag dvaitqelrh gkpaavlvee sagarrvvvg trglgdatgv
      121 kralgstaet vamlaqcpvv vvpasrtdpg vartrpvvvg vdgsavsera levafeeasv
      181 rrvplvalhv wsdtaidewf aldaerdwda iearegmlla erlagwqeqy pdvqvqrvve
      241 rdrpvrflal hgadaqlivv gsrgrggltg mllgstsral vhsapcpvlv vrag
//
LOCUS       WP_010696850             392 aa            linear   BCT 01-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Treponema denticola].
ACCESSION   WP_010696850
VERSION     WP_010696850.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..392
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44696
     Region          19..330
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mntynaehtk dlsffnknvy ldkkflllip etpltaelka ilnewdfsll ysdgepssfm
       61 svrtdtsask dvldsskene iiseklkkqk eimeetenkf wdflrftdki ftdytmkkil
      121 dprlvfdkvk elcdfvkndk knilliemqk yssptnylvm hslrssifai iiglqlkmpp
      181 hrlielgaac llheigmfrl ppqyymydap lseegkkalf thpvlsynil knssfslpic
      241 lgalehhere nghgyprglt rekismygki iavacsyeav taprpykeaq dassgivemi
      301 kntngqydet ilkallysls fypvgmyvhl sngkiakvid vnpddprfpi vqiygqttpt
      361 gdpvivqtka tevtvkrqls keelksidrn tv
//
LOCUS       WP_010696886             231 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Saccharopolyspora
            spinosa].
ACCESSION   WP_010696886
VERSION     WP_010696886.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..231
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24583
     Region          16..145
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..220
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mtanrdkprs rrerpakpal trdcivtaav gimraeglrk vtmrrlaqel dtgpaslyvy
       61 vsntaelhaa ildevlgtie ppaaggdwre rleelltayt vvlfanpsla rsalaarpsg
      121 qhylnlieal lalldeggaa paqaawgvdl llqfatataa eqatrdqsad apdewddlvh
      181 alantsgrth phiaalapql tsgtpqerls wglralvngi lhtpgpegnk p
//
LOCUS       WP_010696961              88 aa            linear   BCT 01-JAN-2025
DEFINITION  HPr family phosphocarrier protein [Treponema denticola].
ACCESSION   WP_010696961
VERSION     WP_010696961.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..88
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=9516
     Region          1..88
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 miskiikvqn ragiharpaa liaqksnnfs seiflcreda kinaksvigi itmaaaygte
       61 itltcdgpde keaceaieti fnnkfeee
//
LOCUS       WP_010696965             397 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Saccharopolyspora
            spinosa].
ACCESSION   WP_010696965
VERSION     WP_010696965.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..397
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43747
     Region          13..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          213..365
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maevsnppar ntrprnrral itaaaadlfy rlgyarvgms diaeavgvgs salyrhfagk
       61 qqlltrvvld elhpfssiaa qvadrdldev vaqlaaaald hrqlgvlwqr earhlpedqr
      121 dvlreelrgv asglaevara frpeltgeda rfrawcmfsv ltspsyhqvd lprrefeqll
      181 ratvvvigtq ppqrfadhra aysdqrsalf agrasrrrll lsaamrlfsd agytevtted
      241 vgaaagiagp slynyfaskq ellgtvitrg nawleveler ilantpaadd alrellrsyi
      301 tfafdhgrfi dilvsevnhl pdaerhrarq tqhayvaewv gllcearpel dpvrsrilvq
      361 aaltaandma rtgsvrdvda lsrigsalml dtpasav
//
LOCUS       WP_010696966             177 aa            linear   BCT 01-JAN-2025
DEFINITION  cyclic nucleotide-binding domain-containing protein [Treponema
            denticola].
ACCESSION   WP_010696966
VERSION     WP_010696966.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Wang,Z., Jiang,Y., Lu,L., Huang,R., Hou,Q. and Shi,F.
  TITLE     Molecular mechanisms of cyclic nucleotide-gated ion channel gating
  JOURNAL   J Genet Genomics 34 (6), 477-485 (2007)
   PUBMED   17601606
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Kaupp,U.B. and Seifert,R.
  TITLE     Cyclic nucleotide-gated ion channels
  JOURNAL   Physiol Rev 82 (3), 769-824 (2002)
   PUBMED   12087135
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Canaves,J.M. and Taylor,S.S.
  TITLE     Classification and phylogenetic analysis of the cAMP-dependent
            protein kinase regulatory subunit family
  JOURNAL   J Mol Evol 54 (1), 17-29 (2002)
   PUBMED   11734894
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Aiba,H., Fujimoto,S. and Ozaki,N.
  TITLE     Molecular cloning and nucleotide sequencing of the gene for E. coli
            cAMP receptor protein
  JOURNAL   Nucleic Acids Res 10 (4), 1345-1361 (1982)
   PUBMED   6280140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10034975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..177
                     /product="cyclic nucleotide-binding domain-containing
                     protein"
                     /GO_function="GO:0030551 - cyclic nucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=19781
     Region          20..126
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(88..89,98..100)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
ORIGIN      
        1 mnkvemdrdi ffqevkqtai fsciedadlm qiidfseils yergesiite gtenngffvl
       61 lsgkleivkn gkwgdvkigi lqnnasfget slfkdqpata tvnaldpsti lliskeqfta
      121 yinahpkagn viltyivfsl lqklnttnee rvqekniefs pedlafmvdm ftppkea
//
LOCUS       WP_010695699             311 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfate adenylyltransferase subunit CysD [Saccharopolyspora
            spinosa].
ACCESSION   WP_010695699
VERSION     WP_010695699.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Mougous,J.D., Lee,D.H., Hubbard,S.C., Schelle,M.W., Vocadlo,D.J.,
            Berger,J.M. and Bertozzi,C.R.
  TITLE     Molecular basis for G protein control of the prokaryotic ATP
            sulfurylase
  JOURNAL   Mol Cell 21 (1), 109-122 (2006)
   PUBMED   16387658
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Snoeck,C., Verreth,C., Hernandez-Lucas,I., Martinez-Romero,E. and
            Vanderleyden,J.
  TITLE     Identification of a third sulfate activation system in
            Sinorhizobium sp. strain BR816: the CysDN sulfate activation
            complex
  JOURNAL   Appl Environ Microbiol 69 (4), 2006-2014 (2003)
   PUBMED   12676676
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Malo,M.S. and Loughlin,R.E.
  TITLE     Promoter elements and regulation of expression of the cysD gene of
            Escherichia coli K-12
  JOURNAL   Gene 87 (1), 127-131 (1990)
   PUBMED   2185135
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Leyh,T.S., Taylor,J.C. and Markham,G.D.
  TITLE     The sulfate activation locus of Escherichia coli K12: cloning,
            genetic, and enzymatic characterization
  JOURNAL   J Biol Chem 263 (5), 2409-2416 (1988)
   PUBMED   2828368
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     gene            1..311
                     /gene="cysD"
     Protein         1..311
                     /product="sulfate adenylyltransferase subunit CysD"
                     /EC_number="2.7.7.4"
                     /GO_component="GO:0009336 - sulfate adenylyltransferase
                     complex (ATP) [Evidence IEA]"
                     /GO_function="GO:0004781 - sulfate adenylyltransferase
                     (ATP) activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0070814 - hydrogen sulfide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=35440
     Region          14..311
                     /region_name="PRK05253"
                     /note="sulfate adenylyltransferase subunit CysD"
                     /db_xref="CDD:235375"
ORIGIN      
        1 mttvelptdr tdvppqvdnl daleseaihi frevagefdr pvilfsggkd stvlvhlalk
       61 afwpapvpfp llhvdtghnf pevlafrdel verhdlrlvv asvqdyiddg rlqeradgtr
      121 nplqttplld gisenrfdav fgggrrdeer arakerifsl rnafgqwdpr rqrpelwnly
      181 ngkhrpgehv rvfplsnwte ldiwryiqre kielpeiyya hrrevflrdg mwltsgpwgg
      241 prdgevaatr tvryrtvgdg sctgavesea ytvddviaev aasrlterga traddrisea
      301 amedrkregy f
//
LOCUS       WP_010697010             587 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Treponema denticola].
ACCESSION   WP_010697010
VERSION     WP_010697010.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..587
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66560
     Region          195..535
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 maagkqlike nsayidilpe waqelsrkyc sktanlyfvh gnirdflphq iteyghnflf
       61 vkirdyisev lfgnqdiivy ydksggisfc tsdmerayle tmhmtypdvp penflsrdpe
      121 eafsyleryf vlnfgknlri vlivdyaeti ipadeignld etdryclvtl nrwshepsft
      181 redisiimlt enltdlnprl taspstikvr iplpdaavrv nflehlrrte eillaergls
      241 permgaltsg lnllnlyqlv gesyqddkpi sldylatkkr eiieneaggl lefidtdydl
      301 slvsghdfvk krfkiaakal kaartdvlpm gylisgpigt gktfivsafa geigipmvrl
      361 rnfrsqwqga tesnlekvln ilramspvav mideadvvlg nrtandvsgt ssrvfaqian
      421 fmgntayrgk iiwflitcrp dlipvdlkrq graeehlalf ypetdaerld lfetlqrklr
      481 iklhdvnlns iikkikfdvs gadieailvr akmnatvegr amviqkdlee tiadfippsy
      541 pyeielqnlv aaiectskem vpkryqsmqr samsaeifei kqllgek
//
LOCUS       WP_010697150             262 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator
            [Saccharopolyspora spinosa].
ACCESSION   WP_010697150
VERSION     WP_010697150.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..262
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28572
     Region          14..253
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 masapkkqsa rllrqqkiid hvvsqgfasa aelseltgvs lmtvhrdldd lvtrgllrky
       61 hggvsaqpst vfesssdfrl hthtaekeal akdalqfinp gmsvmlddst talalarllp
      121 evgpltvvsn yrqvqealrd vpdirliglg geysrthdsy lglpcqemis afsvdivfls
      181 tsamnarlty hqeqeivlvk ramlasattk vlmmdaskva rsalhqfapv rafdhvllag
      241 eldaalveem reqtdvrlsp mg
//
LOCUS       WP_010697318             425 aa            linear   BCT 01-JAN-2025
DEFINITION  fibronectin type III domain-containing protein [Treponema
            denticola].
ACCESSION   WP_010697318
VERSION     WP_010697318.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Bloom,L. and Calabro,V.
  TITLE     FN3: a new protein scaffold reaches the clinic
  JOURNAL   Drug Discov Today 14 (19-20), 949-955 (2009)
   PUBMED   19576999
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Koide,A., Bailey,C.W., Huang,X. and Koide,S.
  TITLE     The fibronectin type III domain as a scaffold for novel binding
            proteins
  JOURNAL   J Mol Biol 284 (4), 1141-1151 (1998)
   PUBMED   9837732
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Potts,J.R. and Campbell,I.D.
  TITLE     Structure and function of fibronectin modules
  JOURNAL   Matrix Biol 15 (5), 313-20 (1996)
   PUBMED   8981327
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10637183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..425
                     /product="fibronectin type III domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49486
     Region          198..251
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
ORIGIN      
        1 mkkyffgltv fiiivstlft gcetlesgkg ekqpyfsekn eqkflkpdqk irftieglse
       61 kiqftkdgkr lmlpvsyqea eqifgfdeee ieilndtstg nplwyrmnkv lnankkqwpl
      121 qaaktndwgg nvlyilylad finvyedkap smvdmtnapd wfkdvlayrk tvpnygktek
      181 dfsintlnak ikagnkevvv swttnkylkg viiewyhdey mnrkkititd gstkyvfkdl
      241 qnlkpykfkv sfadnsgevi kkywldttpr sgdknkdyik gtsdfvnaky ellltedyhi
      301 scydwgsdvn kiafskdgkm ilvpnkflka enifdytkee mgyedifwtr mekvlktedk
      361 qksffasiag engnvlwlly cadflniyqk klpgvvdlsn apdwfktlme qrknspdsyv
      421 kdeyk
//
LOCUS       WP_010697340             324 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010697340
VERSION     WP_010697340.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..324
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35647
     Region          4..323
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 meellniedl siyyiteage tkavnnlnlk lgkgetlgfv getgagkttt algimrlvpn
       61 ppgkivsgki sfdgedilsk tekemqeirg nkismifqdp mtslnpvmtv geqigevlal
      121 hqnlkkeelk ektaqmletv gikrerindy phqfsggmkq rvviamalac npmliiadep
      181 ttaldvtiqa qvlelmielq nkyntsmimi thdlgivaei cdhvaimyag svieygtvek
      241 lytdpkhpyt kglfasiptl dadeeslhvi kgtppnpvdl ptgckfhprc efaterckce
      301 vpkmidldds hcvscflfdk ggek
//
LOCUS       WP_010697342             331 aa            linear   BCT 01-JAN-2025
DEFINITION  lipoate--protein ligase [Treponema denticola].
ACCESSION   WP_010697342
VERSION     WP_010697342.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000589
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..331
                     /product="lipoate--protein ligase"
                     /calculated_mol_wt=38242
     Region          2..243
                     /region_name="LplA"
                     /note="Lipoate-protein ligase A [Coenzyme transport and
                     metabolism]; COG0095"
                     /db_xref="CDD:439865"
     Region          245..329
                     /region_name="Lip_prot_lig_C"
                     /note="Bacterial lipoate protein ligase C-terminus;
                     pfam10437"
                     /db_xref="CDD:431286"
ORIGIN      
        1 mkyivnnshd peynmafeey cfrnlplene eyvflwsnsp tillgknqnt yqeinekyin
       61 engikvvrri tgggaiyqdl enlnfsfvtk tkgnekidfk kyyipivnal kkigvdaels
      121 grndvtiegq kcigasqsvw qgrvlsdgsi lfnvemeals kaltvrkekl eskgvksvrs
      181 rvtnikpylk rditvdqfkd ellkaifeve nqepveykls eeelkgvmki yeerfsrkew
      241 nygaspkaey shyerfpigs ievffnvenm kinslkihgd ffgtadkael eellngceys
      301 envlteklrn tdltpyfgnl ekkdfigmff k
//
LOCUS       WP_010697378             481 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010697378
VERSION     WP_010697378.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 481)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..481
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53739
     Region          3..450
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mgivearikn ftyendespt lyaidlsiee gelvvltgfs gcgkttltri lnglipyhyg
       61 gildgevril gknildykkg elakyignvf qnpsdqffat iaeeevafag enlgmdfqtl
      121 cektnaafqt mqieslkgak lselsggqkq kvaiastliy dtkllffdep ssnldyegiv
      181 qfqamirdlk amgktiiiae hrlfflnely dkliymkdgt iekiflkgel ttedcrrygl
      241 rairynslvc enpsvpkqav thiedlsvsi grreliknls fdvhageita vigkngigkt
      301 tlgkalggll sckgqigygk rrqqrlrnay ymmqdvdyqi ffdtveneli pssklkdtah
      361 lqqaaeylhi idlwekrldh pqelsggqkq rlalatafls grriiildep tsgldykrmd
      421 eiaklilhca qevpvliith dlellfkvcn tallfgenay kkisvngneg eiigfmgkls
      481 i
//
LOCUS       WP_010697383             211 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Treponema denticola].
ACCESSION   WP_010697383
VERSION     WP_010697383.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24117
     Region          7..>116
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mntgtyaqth etilkngkel flkegferan lreicrlsgv ttggfyrhfk dkadlfsalv
       61 epaiqglqaq ysaseklcft vlensgidei wkvsaealed fvsyifdnle afklilccas
      121 gtkyaeftdw mvereikdty ktyellekkg itvrrlppke lhmlthayfs cifetvlhnf
      181 kkkdalnsmk tlaeffsagw rkifglqdge k
//
LOCUS       WP_010697489             846 aa            linear   BCT 01-JAN-2025
DEFINITION  penicillin-binding protein 1A [Treponema denticola].
ACCESSION   WP_010697489
VERSION     WP_010697489.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..846
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=94391
     Region          20..777
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnklskiiyl yliliflila ggafalgkmm amtknikqse lfvdfnpalp srildirgdl
       61 itefsldekr elinygdisp nliaallare drlfyehkgf riksiiravi gqltrrslgg
      121 gstitqqiag ilycdrtdks vkrkikelww aiqmerrhsk deimmlylne ayfgggtngv
      181 saasrfyfgh saseltpaea ailiiqlsnp tkynpfnypn rakerqenvl egmiglgfis
      241 keeaaesfed ywanfdytri alsawltred karwfseyvr revadnmlyg tmnlykdgyt
      301 vhttcdlrhq eiadkefqky iaiandkvsa ststsfsqae qysnltalls lcfgieslsm
      361 gekqlkvktn syyrnklnnt idvlalmcgi dnlktltkqs takmqevlme rvvegtfisi
      421 enetgyitsl iggsqysesn qliratqskl qvgstikpli ysaaidekvi taatrmddsp
      481 qvfesadgvq yipnnyggkw ngtvlvykal plslnipaik tlelvgfdra idrisslmgi
      541 tdpveinktf ekvyplalgi savtpiqllr afaifgnqgr avdpiavrai enrdgvtimd
      601 peldlrieqr krgaamqvis psnafimtei lkktltlgtl ygatsggkkf dykdektgkv
      661 frmpmaaksg ttqnwsdswt siyspyysai vwygfdrgsh slgtdntgsm lsgyvaanfm
      721 revhknkpfk dfvrpekgvi mvdvckksgm ipsenctdet itlpflygte pteictehta
      781 giklrdigid rikdsgmaqg eeeikidttp ieidpsifmd ppaggegvte tkntneesae
      841 sgnpwi
//
LOCUS       WP_010697547             265 aa            linear   BCT 01-JAN-2025
DEFINITION  TM2 domain-containing protein [Treponema denticola].
ACCESSION   WP_010697547
VERSION     WP_010697547.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10524121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..265
                     /product="TM2 domain-containing protein"
                     /GO_function="GO:0001540 - amyloid-beta binding [Evidence
                     IEA]"
                     /GO_function="GO:0004930 - G protein-coupled receptor
                     activity [Evidence IEA]"
                     /GO_process="GO:0097190 - apoptotic signaling pathway
                     [Evidence IEA]"
                     /calculated_mol_wt=30524
     Region          165..205
                     /region_name="TM2"
                     /note="TM2 domain; pfam05154"
                     /db_xref="CDD:428337"
ORIGIN      
        1 mnkfskvtgl iafwtelsll iaiilliffq ksivgiylss ldeykdifiv pwqeiiknfi
       61 fffllgifcl ksnsnereyg iltlyfyili tiifdnpfsv salfiavsqk gvnyltffsa
      121 fnsaqnsily ifilirnisf ilsagsmivk sesryleikn nkrispksrt ylilysaflg
      181 flgidrfyig rtvigigkll lgliivteff lvfrywysll lidrsvfiil ligfvsisvl
      241 vnsidfilav fgrmkdsekn lvrnw
//
LOCUS       WP_010697558             106 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Treponema
            denticola].
ACCESSION   WP_010697558
VERSION     WP_010697558.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..106
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12223
     Region          3..103
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 miykieisah aesdlrdiye yiafklfspk aaaaqlvrlk agimsldqmp krfrayqkep
       61 wyskglrvmp vdkflvfyip sesdkkvyii rviyggrnie kelnsg
//
LOCUS       WP_010697622            1026 aa            linear   BCT 01-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Treponema denticola].
ACCESSION   WP_010697622
VERSION     WP_010697622.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Burnim,A.A., Dufault-Thompson,K. and Jiang,X.
  TITLE     The three-sided right-handed beta-helix is a versatile fold for
            glycan interactions
  JOURNAL   Glycobiology 34 (7) (2024)
   PUBMED   38767844
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12131601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..1026
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=109546
     Region          551..707
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
ORIGIN      
        1 mkkllkiltm vaavlttavl fttckqfldd pedflsywaa evvptgydid iakpylisnd
       61 gvicvpsnny llsdgsvtvt iylrnpkkfs lvmpsstssa ldvqkiihfp gfdadhqpky
      121 sadndytleq tpdkqalklk ykssflkkhe wgtadigpei tlkstdgrqf nkkfslnlkv
      181 ntapsfdykg vgktyaggkw yyvlifqakn meeqataghy vhediknlhi vkrdeaeahy
      241 tvsnidfpnk kikwktsdpf ldgatqltag dcegtlpvlp tgdwliyfkt dvevstssal
      301 ktyeawlsdk agllsnkvqg stcirkigdi evlstpphss gtgsfsdryk incdgdgvql
      361 evwcqtpded vnilywiwke npttqliksg eetaspnnhl ktirlsapad igdtirykvk
      421 fnakktpgfg dnerfvyyel krkvgsvidg nepnawaklk yaieyenese itikntikaq
      481 nssitiggqi iknyeqinvg revkikgfdt navinadskc rifnvannrk ltleklkltg
      541 gralgsddaa nsgggiyags gttitmtgct fdgnvasydt smgssglgga vyavqaanvi
      601 ikncifdknm iltngvhgvh dgetgkggav cmvstanvti egctftgnka kdgsgvcafr
      661 snsviitkci fknninalkg tagyggavca ldganviitd ctltgnkaey ggavaaiknd
      721 sstatsyiti kggiiggtgd edaniakgss ygggiyvgeg cdlklqknsa gqgvqiignm
      781 adhggglyae katvimtgct ftgnkeelpn npnyisqmeg gaicaygstv tindctfrgn
      841 kavfggaiya sklnpsqtls pnnpasviti kggiiggtns ndankadnlk dsglgggiyv
      901 ggdcsltlqd ftaiksvkil gntarmlgng iyvgrngkln mqggtqvnen ndvylglssk
      961 iylsgaltts gkaalitpdv yeasvqvldg siiagtpqny kkfkvtpkdg ipwyvastgf
     1021 lttvep
//
LOCUS       WP_010697670             318 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Treponema denticola].
ACCESSION   WP_010697670
VERSION     WP_010697670.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..318
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=35540
     Region          1..313
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mtylsvcsgi eaatvawepl gfkpigfaei epfpcellrq kypnvknygd itqyekwnig
       61 kfdvlvggtp cqsfsiagkr ggtddirgql mysyldivgk ykpqwviwen vpgvlssgkg
      121 ldfasflagl eecgygwayr vldaqyfgvp qrrrrvfvig hsdnrtdlaa kvlfeqekpr
      181 tsfeasegkk keitgtlttg fgardfdcdk ilnnqfsves ytlssfaqyk egvgtlkasg
      241 gdfgggseti ikegknirrl tplecerlqg fpdnytqiew ndktkdqcpd tprykaigns
      301 mavpvmrwig eriernkv
//
LOCUS       WP_010697734             448 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Treponema denticola].
ACCESSION   WP_010697734
VERSION     WP_010697734.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 448)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..448
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48808
     Region          30..250
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          153..446
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mknlvfikma frflgigsgk tvsnarkslf gavlgigisi iplivvlvvs dgmiqgitsr
       61 tielgtghlq vinmrsissy knaeteknvr slilefdegn fvenawierq gnglvigkng
      121 rsggairave pefftqnira lnlikvisgs lefennksai lgtaiaeklg lkvgdtcrii
      181 tisknekgkt iprvssfkis glvssgyqel dalwvfiple eglkimpmss sltsivvstn
      241 dpfdddkmqa iqlklssilp etfsiyswad lnrsaftsfk ttknillfim flivlvasan
      301 issaivmlvm errreiailk aagahpssis lafllagllt slggiilgmp lgilaaihin
      361 eifayaekil nhiqnffytf vygtggtgkp leihlldpay yleyipvkln lfdlytiavs
      421 mlilsvvvcl ipavragkek pieimrkl
//
LOCUS       WP_010697758             183 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Treponema denticola].
ACCESSION   WP_010697758
VERSION     WP_010697758.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..183
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20073
     Region          29..121
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(39,41..43,49,72,74..76,78..80,83..84,106,110..111,
                     113)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            75
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 msnnsviagf ddekddslki rlqrvdgldk cvvvflngyi dtynsaffqk riakiidsgf
       61 iqivfncaal nyvsstgigs ftaflktvkp rggdivlldv qpkvyeifql lgfsqffnik
      121 dalsdavsff qsssttantk vfpkifacpi cskklkatka grfrcseckt ilaidnnaqv
      181 flg
//
LOCUS       WP_010697735             426 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Treponema denticola].
ACCESSION   WP_010697735
VERSION     WP_010697735.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 426)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..426
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47341
     Region          29..>190
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          142..426
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mkknncrwif fvlnrfnsad tkgrssistl fsilgiafgv mvltvilsim nglqmgyidt
       61 ilqvssghir lygekedlke aenlklhkaf fvfqesqtlm qgnygkqhgv lirsveedim
      121 qkdkglasal kitsgsfnil ekdsvilgye larqlgvkvg dnvniiavsg ssetslfpen
      181 qdlivtgifk tgyyevdssf afmslengen vfgkesklya svklqnqnnd aayisslnas
      241 sinlkaeswr tynhaffgal rieknmmmll viliflvvsv niyngmrrsi yerreeisvl
      301 aslgayskhi qalfiangft igligasagl llglllsvqi nsifnlieni vnsvlsfisi
      361 lfqnssdadf svfspvyfym etvpvriffn eilliflfgv fsssaaamia arrilklkpa
      421 evlrye
//
LOCUS       WP_010697767             379 aa            linear   BCT 01-JAN-2025
DEFINITION  formylglycine-generating enzyme family protein [Treponema
            denticola].
ACCESSION   WP_010697767
VERSION     WP_010697767.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..379
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=41772
     Region          90..379
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mkkifvlfla ilfvsvsack npffknmldk dsgnegsgdw nsqssdvgsf edagdfvkii
       61 ppangivgva pdyalpgnea wwqgvfiagr tvklspykig kmevtyelwy svlkwntdng
      121 kgyvfankgl egwdgtgggg typnyanigk pptanknhpv tmvswrdciv wcnaytekek
      181 gigecvyrkk dnhtvvlkda tatadcdaay admskkgfrl ptdaeweyaa rwqndntnat
      241 dygeggsnvw ltklnsasga kdkwdtaetg evvwysvnsg ykthtvgkkr analglydms
      301 gnvwewcfdw wnnnpasnda ayeqggivtd pqgaasgsdr vlrggswfdl ayfcsvgvrg
      361 yygpdywrnf vgfrlacrp
//
LOCUS       WP_010697794             127 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Treponema denticola].
ACCESSION   WP_010697794
VERSION     WP_010697794.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..127
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=14091
     Region          6..32
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <7..126
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(7..8,11..13,15..16,20,23,32,34,36,40..41,44..46,
                     48..49,53,56,65,67,69,73..74,77..79,81..82,86,89)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          34..65
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          67..95
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mniaefikaa kkndielikt ylqkgfdint qdkdgftavm eaaefgykdl fwfliekgad
       61 vlikadynfs ivhavglggd kkmldyvisk garldekvtg geqdgmtikd yallakndel
      121 ykglkll
//
LOCUS       WP_010697770             329 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Treponema denticola].
ACCESSION   WP_010697770
VERSION     WP_010697770.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..329
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36434
     Region          17..252
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msfisraarf graarqkppv slcvpvygte gligrfldsi laqkdaplfe tiivndgspg
       61 tkelrsivkt yekrfkergl pfvflehskn lgtlearrta vtaasgeyla fadpddelpp
      121 aalrilydaa atsgadivhg kaavcgmege pdarvaafaq raqnvyngvl tgdeilrkci
      181 venvyssfvw sklfktglvq ktygkipfty ctmaedmlly ffialyagky igipdivyny
      241 rintgltsrr qitdlaawqk vcsvssvfti lfsylddhpa vgsdireavr dlghahyadn
      301 lkqleicvvp slqeearaml eewwgiynl
//
LOCUS       WP_010697798             304 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Treponema denticola].
ACCESSION   WP_010697798
VERSION     WP_010697798.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..304
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34147
     Region          24..288
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mqtiyqtmsd gsavavhqwl pkkkpkavih ivhgmaehal ryadfaedac trgftvfasd
       61 hrghgktcgk imlkgyladk dgfrrvvedq keindeiqki yqdipiiilg hsfgsfitqn
      121 yienygktvk aailvgsagp npmlkiagla aglnklfsgr kkpskfmdkl sfgaynktvd
      181 spktnfdwls rdekevkkyi ddefcgftct vgfyqdlikg lkqthmstem vkipnelpil
      241 itsgdrdpvs nlgksvkkly diykangisd lnlklyegar heilnetnke evkadifewi
      301 ekrl
//
LOCUS       WP_010697803             502 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010697803
VERSION     WP_010697803.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 502)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..502
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56402
     Region          1..481
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mntavelkdv sfiyesskdg ranlkktsln ikkgefllvt gisgcgkstl tkcinglipr
       61 fyegefsgsv finekdvsnf sideiskdig svfqspksqf ftddvisels fpcenygisr
      121 deiieriaev csilhienll tekleslsng qkqkiaiasi ltlrpkiivl depssnldfn
      181 sililadilk ilkqrgftii iaehrlhylk dlfdrviyin egsiqneytr eeflaltnte
      241 lnskglrslh lftneneetp igpipnkfny dteaekicsl sdisfsfkdg teilnsvnld
      301 lykndiaalt gkngagkttl akiisgiyrq sagsikfgek ilsekervsr tnfvlqdvey
      361 qlfgadvfse llignkqlen vnkkiekalk klnlydykde hpfslsmgqk qrliiaatyv
      421 rgcpltilde ptsgldyrnm vrvgelieei aetsavliit hdfefiskic nrlillkdkk
      481 ialdsrlgkn dkklesifst yl
//
LOCUS       WP_010697834             435 aa            linear   BCT 01-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Treponema denticola].
ACCESSION   WP_010697834
VERSION     WP_010697834.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11720441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..435
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=47708
     Region          29..>87
                     /region_name="DUF1565"
                     /note="Protein of unknown function (DUF1565); cl23857"
                     /db_xref="CDD:305014"
     Region          189..320
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
ORIGIN      
        1 mkkgiiicll avlvltnlta aeyyvsketg kngnagtkda pfkniekaae kvqpgdkiyv
       61 aegnyygvrd kgfimiqkav eiyggyskdf skrdvlkyrt lvmppassng tgrankamef
      121 dikngegkkl vidgiifdkg lsngyhptkg kpqgvetgml vlppgqgvng geksitteka
      181 ifggsimkcd vliqncvfnn asnfaiqfgg tgnvkilnnv ftanamaace iwgkenkpna
      241 itvefayntv lftwprthaf edmgygfrvm tkvevnihhn iiglsclsav drcridspas
      301 mengrkvlmd nnrffmnkqa dvtlpglgtf eyvwvkdfdd ldrfnsaegn eelkdiaslk
      361 nvlnkaylag flnatykekt dydpnspane frramgmnqt mtvqtdvsmf ankypqddav
      421 klfgavkgfg aqaik
//
LOCUS       WP_010697865             415 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidase U32 family protein [Treponema denticola].
ACCESSION   WP_010697865
VERSION     WP_010697865.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..415
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=47312
     Region          1..317
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
ORIGIN      
        1 mellspagnf ekldyaweyg adaayiglkn fslrakadnf sgeeyknisl lkeeykkrgl
       61 tkklycaini sfhnedlknl leevkyfkqy pfdafivqdl gaarilkesf peislhlstq
      121 ancinyeavr vykdlgfsrv vlgreasled vreikqrvpe melecfvhga mcisysgrcl
      181 isayltdrsa nsgacthscr wnykmysekg ghffveeser kgelfpveeg enytalfssk
      241 dlcmidyldk mkeagvdslk iegrmksiyy taltarayrk kidflngkis aaeaapfvee
      301 lyntahrefs tgfyfssaea nkttagesks pymlagkigk rlseneyefi smnkidsgip
      361 leyvgpdics iedrdytllk pdtkekmdwv chghpciikt ykpiaekflv rcken
//
LOCUS       WP_010697848             359 aa            linear   BCT 01-JAN-2025
DEFINITION  formylglycine-generating enzyme family protein [Treponema
            denticola].
ACCESSION   WP_010697848
VERSION     WP_010697848.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..359
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=39069
     Region          81..359
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mkkifvlfla ilfvsvsack npffknmldk dsgsegagdw nsqsydfvlv tppvngiigv
       61 apgcilpgsq dywksvfiag rtvklspyki gkmevtyelw ysvlkwntdn gkgyvfanqg
      121 regshgidga aptgnknhpv tmvswrdciv wcnaytekek gigeciyrks ktdttvlkna
      181 tvaadcdsay admekkgfrl pteaeweyaa rrqndntnat dygeggsnvw ltklnsasga
      241 kdkwdtaetg evawyngnsg gkahpvgrkr analglhdms gnvwewcfdw ynnnpasnda
      301 ayeqggivtd pqgaasgsgr verggswdgg agycavgvry gnspdhrfsn lgfrlacrp
//
LOCUS       WP_010697958             325 aa            linear   BCT 01-JAN-2025
DEFINITION  dipeptidase [Treponema denticola].
ACCESSION   WP_010697958
VERSION     WP_010697958.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..325
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36950
     Region          1..325
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mnyidlhcdt lmmtwkedtg etivsnksfs vdferlkksg ayaqffaifm ltesifnyik
       61 rpvisddeyi eslldqikrg iekvdyvkic ksydeflqnk sqniisaflt ledgrsvngd
      121 lkrldhfyek girlitltwn nencigfpns kdpdimnkgl kpfgielier mnqlgviidv
      181 shlsdggfyd vakyskkpft ashsnsrils phtrnmtddm ikvladkggi mglnlgpefl
      241 neditnknst valmvkhlnh qkniggievl algsdfdgvl gnmeingcdk yyllfdalkk
      301 dgwteqeiem layknaerfl kdvlk
//
LOCUS       WP_010697965             158 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Treponema
            denticola].
ACCESSION   WP_010697965
VERSION     WP_010697965.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Leiros,H.K., Tedesco,C. and McSweeney,S.M.
  TITLE     High-resolution structure of the antibiotic resistance protein NimA
            from Deinococcus radiodurans
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 64 (Pt 6), 442-447
            (2008)
   PUBMED   18540048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..158
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17686
     Region          1..157
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 mrrvdravtd nrqiqsiiek akvvhigmid ndrpyvvpmq ygfifnedkl tlyvhcakkg
       61 rkldiinknp hvfieletea viisggevpc aygseyasvm gdgtavfved vkekilglql
      121 lmktqtgrdf eiteqmtkqv tvlridvpcv taksrakv
//
LOCUS       WP_010697937             382 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Treponema denticola].
ACCESSION   WP_010697937
VERSION     WP_010697937.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..382
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43821
     Region          169..370
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mknkffifih yfliassliq isvngskitg iqfllylcfi ilfnlrlfyi nnktlffilc
       61 ltdwalclfl hitgltipfl lfliplidgf yynskpytyi lgiiglavci fslknfdmgi
      121 iinytaifil sggvleyfkl nqnkiissqn kieelniqke ellnsihdle iynesiedlm
      181 tlkernrisr eihdsvghgl stmiiqlnal yaaaknnnnd lpqkildlna fakknleevr
      241 falrelkpvd ynkyeiiilv hnligefkkm tninvqftfs kdiwslnekq shavykavqe
      301 flsnsakysn askitihfsy teaslivtmk dngdgctdik kgiglkaiee rvketdgtvy
      361 yeslpavkgf fmrlaffqnk al
//
LOCUS       WP_010698066             278 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Treponema denticola].
ACCESSION   WP_010698066
VERSION     WP_010698066.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 278)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..278
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29578
     Region          4..258
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mlqygfmqna fivsffigil cpaiglflvl rrysligdtl shsslagvtl alasginpil
       61 gafifttaag aliealrnaf keyqdlilsi vlslsvgiai tlissgtvra naetylfgsv
      121 ltvsssdlit vialsilslv tlglmyhkmv yialdediak imgvkvrlin ylfsgltaat
      181 iavslkivgm lvlssmialp vatalqlkms fkktlifsil isvadimlgl vlsyhlnvap
      241 ggftalvsvt vliitigins flkyvrfmas prttkikl
//
LOCUS       WP_010698125             371 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Treponema denticola].
ACCESSION   WP_010698125
VERSION     WP_010698125.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..371
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=41140
     Region          36..350
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mfkksifllf lafyillafs crpaikeysk twlsigtvcr vriltfepqk kaeevlekvy
       61 aelikldsif nantdkisae nnnlkgltta neselerlnk eaglsplevs pelyellqis
      121 lmmaeltdga fnpaigplvk lwnigfenes vpspedikev lplldyknii lsegnkaflq
      181 kegmrldlgg iakgytadki akillehgik dflidlggni lvsgknpsgk twktalrnpv
      241 igkqnpvism nlqdaslvts gnyerfikkd giiyhhifds ktgypvqnsl nassivsess
      301 tladalstss yvlgeektra llkklitmdf pligkpkmpa cilfykdnsi svfgndeisv
      361 eiidqnffik k
//
LOCUS       WP_010698133             202 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Treponema denticola].
ACCESSION   WP_010698133
VERSION     WP_010698133.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23119
     Region          3..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprdktanhi kiiaaakaef memgfdkssm rsiskrcgmt aagiyrhcvd kedlfdqiva
       61 pavgrinawl dahvaryvga vnhkehiqwr dseidmmrei iypnmdeyhl llaksqgsky
      121 enflhdlteq qqeqllkylp mlkaqgyavk didskelhll lsayttalfe pvihnyslee
      181 alhclkavea ffvpgwkqlf gf
//
LOCUS       WP_010698136             563 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010698136
VERSION     WP_010698136.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..563
                     /product="ABC transporter ATP-binding protein"
                     /calculated_mol_wt=62089
     Region          1..560
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
     Region          246..304
                     /region_name="oligo_HPY"
                     /note="Oligopeptide/dipeptide transporter, C-terminal
                     region; pfam08352"
                     /db_xref="CDD:400588"
ORIGIN      
        1 mmpeeilrve nltvtycsnt gdtdraeagi rnvgfslkrg elcgiigesg ggkstllsai
       61 mgllqeksgg gafnagtaev tgkivydgle iqnagktewk nirfkeiglv fqnqderlnp
      121 altvgeqite vlrkeitdtk lseqklaavl rsvglesgvk nryphelsgg mrqrvfiama
      181 iclhppllli depttaldpa skqqilqllr nihseydttm livshdlevi etltdnlmvl
      241 lhgyviekgk tqnileeakh pytsallqss tylnpwkdlw gikdaeerqs cpfyerctqk
      301 sseclsytpy lppecsegca cakngiqtil rvrnlskkfd tgkekteavk dcslrvrhge
      361 ivallgksgs gkttvlhiia gllnkdtgsi vfenteiekn dllarehalq iveqdafssm
      421 ntaltvreii aepsviryhk saaaftetvm kyaklcglpa deamlnkrar elsggqrqkt
      481 aiaralsmqp vllladeina mlddsskvni mrllkqlqye lgfsmllvth didlvkkvad
      541 yvycmeagci veegsirkvf gks
//
LOCUS       WP_010698150             217 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010698150
VERSION     WP_010698150.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..217
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24091
     Region          3..216
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mqilktenlt kiynnqvral ngvsisierg efvavmgssg sgkstllhil ggvdkptsgt
       61 vyidgedisa lkekdlalfr rrkiglvyqf fnlipnlsvk knillpilld kknpdqnyfd
      121 eivsvlglke klnsfpsels ggqqqrvaia rsliyrpsil ladeptgnld rknsdeiigl
      181 lklsnknykq tiimithder ialeadriik iedgeil
//
LOCUS       WP_010698156             150 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Treponema denticola].
ACCESSION   WP_010698156
VERSION     WP_010698156.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..150
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=16990
     Region          32..145
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mylfsisllt kivilyifni yritgggvrv niflnnssgv plyeqlseqi knqilsgslk
       61 keepmpsmra laaslrvsvi ttkrsyedla regflysvpa kgyfvadvnf kkieksikks
      121 ieeklkevcg qakkinlnae dlyeilrriy
//
LOCUS       WP_010698158             414 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Treponema denticola].
ACCESSION   WP_010698158
VERSION     WP_010698158.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..414
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45321
     Region          4..396
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(14..15,18..19,22,54,109..110,112..114,117,137,
                     140..141,144,223,226..227,230..232,235,257,261,314..315,
                     319,323,339,342..343,346..347,350)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mktfmviwfg qfismlgsal safglgiwif qktgnaasfa msaactvlpa llfapfagsi
       61 adrkkrkaii lltdsidafl kilivtllif nklelwmvyp lvfisgtlgt fqnpafgasi
      121 pmlvptdklt rangllqfss aiqnllapvi agflypliel kglfiidfvs fffalasiaf
      181 ikipqpliek tkdslvlaal kdlkyawkyl iqkeglmqli vffaflnfia nlsmillgpl
      241 mmsvynsqay gnvqagigla mllgglcssl ipdtknkmkr illilslcsi gpiisgttln
      301 riiitagffi fmfpvpyvnt llmsifqiki ernvlgrvga lmtailaait piaylcagpl
      361 adyvfeplmn ekgrgiglif iisgifliis cllmrlnktv tsiekrlpdy vdnk
//
LOCUS       WP_010698184             632 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Treponema denticola].
ACCESSION   WP_010698184
VERSION     WP_010698184.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..632
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71628
     Region          3..397
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mlnkqkkmtw rtylaygaad lygggcffiv ttfamyylvn viglhpvlag lipaigkfwd
       61 avsdpmmgyi adntpqnrfg krrvwflvsi ipialsfiii wvptgiesqa gkfifytiay
      121 iifftvstvs yipyaalsae itkdfsernk lngsrlmfsf iatllgglla qpiidafhgs
      181 mmgyfvmsiv falifalpwi plyfetwelp eeksqkksda kfiknflslf ksrscrihia
      241 myvcsygald ivmslvlfyi vdylnrgsvf viaqgalllt mmatlpihnr iinkkghkpv
      301 yvaaliifav sivlmsfhtp qtnpvfliln mvlmgvgisa nnliphqllp fladidklms
      361 genragtysa amtltrklfl glvimttigf vlsgigyknp vpsvltqkqf keaqnlavkn
      421 nenfeninky yslredgnfh lkymsrdtde iitsmykkak knqhanplfs ffegkdnfae
      481 ipqdvfenll ssfdkkdfne idkkflvess yiksgevykk iepqdfytkd dlydlkelld
      541 kidfkysgig qvqkpqqkes tlkgvkisfi implfmilfg iffglkfnvs penhkiilde
      601 lnrleaggkk edadektkki celligepyg rt
//
LOCUS       WP_010698206             108 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Treponema
            denticola].
ACCESSION   WP_010698206
VERSION     WP_010698206.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..108
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12443
     Region          2..100
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mfeikiapqa aadlleikny ienelqnpia ahntiskiie tyenltvfpn vgipvekyvs
       61 fptdykfvla nnysifyrie devirivril ysrrdfvril fgeiansv
//
LOCUS       WP_010698234             876 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Treponema denticola].
ACCESSION   WP_010698234
VERSION     WP_010698234.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 876)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 876)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 876)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 876)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 876)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   6  (residues 1 to 876)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   7  (residues 1 to 876)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..876
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..876
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=93108
     Region          3..71
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          108..779
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(413,415,735)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(457..459,522,540..542,571,624..626,646,649,652,671,
                     674)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(736,764,768)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Region          812..876
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mgkkikfnit gmtcsacssh vqravekleg aaevqvnllt nsmsvnydea ilgtdkiiea
       61 vekagygasl adslknsssn knsaggktsg trsfqndaak lerdkikkrl ilslvfmipl
      121 fyvsmghmas lpiphflhgi enalifsftq fllalpvlii nkkfftggfk aflnkapnmd
      181 slvavgsgaa liygifaiyk maygmghgdm etvrlfagdl yfesaamilt lvtlgkflea
      241 nakgktsqai tklmnlkpkt alvirngnee eipveeivkg dlilikpgfs ipvdgiiveg
      301 nssvdeaait geslpvekta gdkvvsasin lsgtftfkae rvgddttlsq iialveeasa
      361 skapvsklad kisnyfvpav iaiavitlfv wfiagegfef alsraisvlv iscpcalgla
      421 tptaimagtg kgarlgilir saealetahk tntvvldktg titqgrpdvi dikktenfse
      481 devlsfaysl evlsehplan avikrakekn lealkikdfk aehgfgisgi eeasglkila
      541 gneklfqknn ieishakaei dalaekgatp lligvsgrtg gsssetdtga kligiiavad
      601 kikegsiesi aefkamgikt imltgdnkkt anaikaqtgv ddfsaellpq nkkneieklq
      661 qaglktamig dgindapalm tadvgiaign gtdiaiesad iilmndnlqt avdsiqlsra
      721 vmrnikenlf walfynslci plaagvfypl fgivlspmia aaamslssvs vvsnalrlny
      781 fkpkrkykis rdagstesca adknkikeke lmntvlkvng mqcqhcvshv kealtkisgv
      841 saeidlgakt atithpesvs vadlkkaied agytve
//
LOCUS       WP_010698240             555 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 3 protein [Treponema denticola].
ACCESSION   WP_010698240
VERSION     WP_010698240.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..555
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61590
     Region          52..>446
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mkikgsnfkk nilfftsifl lvinlnseek nlpnfydnvp neelaadive nmtdeellaq
       61 tfmfgwagqd pgdlliswie dyglgsikvf gwntgdsrkl aksisilqkk slegrfgipl
      121 fvatdqeggw vrhvkgltse tpgnlaigas gipqdsyysg yyisreiral ginlnfaptv
      181 dlltdhdssi igprsfgdsp haagilgaaf vrgsrdagvl ttakhfpghg dtsidshgrl
      241 pkidiseetf rnrelipfky lidagvpaim tghlnfssil pngepatfsk yllidilrge
      301 lgfkgliitd dmmmhgamnf aggiakavkm aleagndiie ssttprhyqa fwkdnikamk
      361 eepqfkervk eaafrillek lkyfksdnhv pilpdmekld eripdkegqk fflslagrst
      421 tivrdadipf kpeededill vsaykdffky glkrfpkaki ievdsayyhv rrfdtiifcl
      481 sdkyslsvlq kimysypnkk yivisvlspa flakvpkaet aiaiysyspa sftaafgalc
      541 gdftpngklp isgie
//
LOCUS       WP_010698277             447 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Treponema denticola].
ACCESSION   WP_010698277
VERSION     WP_010698277.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..447
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47658
     Region          8..447
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mkikeneklg lgscvtilvg gcigsaifsl sgmtmyyagp aalitwfvaa lilglygiqv
       61 aelsirypks ggvfvfpaka mgkneregkv wgfisawgyv isniiavafs aiyvavylgv
      121 gfqalvgfri plaiisivic talnlikvts agkynnvlva llvitmltfv siamfagrwn
      181 pqnmvpfftq gakgvagfiq aipnamvgyg svvaiafmvg evenpnrtvp kslaislilv
      241 vllyqlmilg tmgnittefl iknpgmrfip mfaaaftsln mfpwlsklis isallalltt
      301 mlvvgflnar avcsmanakm lpaffgkvnk ngvpstaclt lsactivlsc fpsitellvn
      361 lgsisaaiti vivcfslias rkklphvegn yaapggnivs iltiililvc yipaifngsv
      421 ymwlftfily giggiimfim mkknkad
//
LOCUS       WP_010698310             337 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA-dihydrouridine synthase family protein [Treponema denticola].
ACCESSION   WP_010698310
VERSION     WP_010698310.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Finet,O., Yague-Sanz,C., Kruger,L.K., Tran,P., Migeot,V.,
            Louski,M., Nevers,A., Rougemaille,M., Sun,J., Ernst,F.G.M.,
            Wacheul,L., Wery,M., Morillon,A., Dedon,P., Lafontaine,D.L.J. and
            Hermand,D.
  TITLE     Transcription-wide mapping of dihydrouridine reveals that mRNA
            dihydrouridylation is required for meiotic chromosome segregation
  JOURNAL   Mol Cell 82 (2), 404-419 (2022)
   PUBMED   34798057
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Bou-Nader,C., Bregeon,D., Pecqueur,L., Fontecave,M. and Hamdane,D.
  TITLE     Electrostatic Potential in the tRNA Binding Evolution of
            Dihydrouridine Synthases
  JOURNAL   Biochemistry 57 (37), 5407-5414 (2018)
   PUBMED   30149704
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Xing,F., Martzen,M.R. and Phizicky,E.M.
  TITLE     A conserved family of Saccharomyces cerevisiae synthases effects
            dihydrouridine modification of tRNA
  JOURNAL   RNA 8 (3), 370-381 (2002)
   PUBMED   12003496
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..337
                     /product="tRNA-dihydrouridine synthase family protein"
                     /EC_number="1.3.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0017150 - tRNA dihydrouridine synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /calculated_mol_wt=38135
     Region          2..247
                     /region_name="DUS_like_FMN"
                     /note="Dihydrouridine synthase-like (DUS-like) FMN-binding
                     domain. Members of this family catalyze the reduction of
                     the 5,6-double bond of a uridine residue on tRNA.
                     Dihydrouridine modification of tRNA is widely observed in
                     prokaryotes and eukaryotes, and also...; cd02801"
                     /db_xref="CDD:239200"
     Site            order(6..8,33,62,89,145,175,206,208,230..231)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239200"
     Site            order(62,92..93,145,147,174..175,177..178,207..208,231)
                     /site_type="active"
                     /db_xref="CDD:239200"
     Site            order(92,147,175,177)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239200"
     Site            order(93,145,174,178,207..208)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239200"
ORIGIN      
        1 mklisapmaa ithsafrrlt acfkepdeyf semihapsai sgggfekwyf ranpspeklv
       61 wqitspdeks aaacvplllq yggfgidlnm gccapqivnt gagfawmkkp lsetaslvsk
      121 vkkavllyde qkagpqtepi rlsvklrlge eenydrllsf ckmlvsegvn litlhprtqk
      181 qkysrpckhe ytarlaydlp ipvygngdin sletlekias kypcsgwmig rsavqkpwif
      241 yelskgilkn gtaedkdeki eidllktael flsflreeqp qefyltraqr ffaffcdnfs
      301 fahhikskvl ncknlddmlh slsdyfeevp edrlinv
//
LOCUS       WP_010698327             365 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Treponema denticola].
ACCESSION   WP_010698327
VERSION     WP_010698327.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..365
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41747
     Region          147..353
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mllflenfli vlfsslfvfs ktgsfivipc fiiffsmglw sgmihsnikp fifivfvift
       61 aafnknlaff spvfiamnle aeenqkhlsl ifkflpllcv ffnfdliffl ftliiffysg
      121 ikenyllktl evtglkdkla eskinsekre rilenevlkn aevlilaern risgslhnsi
      181 ghtlsagilq vnalkyisnq eevkeslnil qnslengmte ireclhnmhn dsfnlqtgle
      241 elvestkkik iqltykvdsi pyelkydifs ivkeslsnti khsgaselnl svlehlgfys
      301 liikdngrgf sgkqirnlny giglkviadl vekhrgiikf ysengfkthi ifpkikdkyn
      361 ednns
//
LOCUS       WP_010698332             692 aa            linear   BCT 01-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Treponema
            denticola].
ACCESSION   WP_010698332
VERSION     WP_010698332.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..692
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=77907
     Region          245..616
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mtvekkrlfl gsipffclfi llyltnlfkl vyehkiidle vkngkvsipa ktlsepslfs
       61 lsgdfyytpn rfyslknspe esyakvpgdf asknlgnvfg ygsyglelyg ldpgtiyaih
      121 iphifsscsi iingidresq gqpgidrete npgtrssqia frplkdgtan ivinvsnffn
      181 nkgyipspii lgeasqigim frgdlifygt ifavtfsval fffmlsffyk nssfviwfal
      241 tsmvlairgi ffyphifmil fpdipwianf imryvtvplp iifftvfltk alklrykipy
      301 iiilsvsily aistivlppe vstflliyyq ifalfcvsyi iaiaiiglkk kkefavwift
      361 stvvlflfgv ydllvslgii pgefflqigt vfaviilsvm vlddyassin kiedlsvemq
      421 linrslirfv pdqivellnk ksitdvklgd sveltmpils tdirsfthts eklapnqvfe
      481 llneyfalva pivrkyngvi tkylgdgffa lfpdganaal lcgiaiqkai rdngiavpns
      541 spikvgigid mgdillgiig nstrmdsiii snsyhiaeil qestkkycsy miisdriyda
      601 indisehyir piqrvknssn ketflyevyd cdddlirdlk hstqgymena lkalsnegae
      661 saakyfdkvl sifpddpvsl yykkifekin sr
//
LOCUS       WP_010698345             696 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Treponema denticola].
ACCESSION   WP_010698345
VERSION     WP_010698345.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12036995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..696
                     /product="methyl-accepting chemotaxis protein"
                     /calculated_mol_wt=74334
     Region          36..271
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          <294..696
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkkrfsiryk liivfgvlia iassmegfla trtarnalae kvdthlldka adiaeiidgr
       61 vtalfqfleg iarmpelsgs sysysqivsf lqkesrfndr ikelditdtn gtfyyaggsv
      121 qvsdrewfka alagkkfvte pyieratgtl vttfavpild stdtivgvls advkglllse
      181 yisdivvgkt gicyilgltg ttiadrdeel vtghmnfsee akknaayasl aefermavka
      241 dessigfyey kgvskiasha kmkttgwtiv inapvnefmg svntlgtsmi gtgvitflia
      301 qlivffiagt ivkpiktavs alkniaqgeg dltvhlpirg ndeitdlsgy fnqtiskiss
      361 svkqvslntg nmedignela snmtetasai hqisanidgv kqqaltqaas vsetaatiee
      421 iirtikqlng sienqaanva esssaieqmv gniasitqtl gktddviktl asatadgkdt
      481 itgansvtqk iteesgglle assviqhias qtnllamnaa ieaahageag kgfavvadei
      541 rklaeesssq gkaitstlkl lsgeiealss ssktaeekfn aiftlseqvk tmsqnlmdam
      601 reqengskev lsairdinmv tsqvndgsae mlrggenvak emqkldaltr iitdsmnema
      661 agalqisnai qevndisqkn kasiqnlvee vgkfkv
//
LOCUS       WP_010698368             380 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Treponema denticola].
ACCESSION   WP_010698368
VERSION     WP_010698368.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18643657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..380
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=43593
     Region          <71..255
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          119..163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..196
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          203..>375
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          226..253
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          261..287
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(263..264,267..268,270,302,305..306,309..310,
                     312..313,336,339..340,343..344,347)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          292..330
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          335..363
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mqnpidslly vqisaeqagk ifealessip lpiqlsepgl kedfkaenik pemilagmlt
       61 vfaydrenpn iqyyrkifnl lrpdirkemt eaaiikiknn dfdmaeeill sleglnpndg
      121 itklnlallm eersqfcemr elfedalsfn kkaeelysel ilfepplpsv ffnaayffik
      181 qknyikaksl lktyleiend ssetaefrka kasellktis eqalddelfq kaykyidlge
      241 eekaaesikl flrknpkvwn awfllgwalr rmgrwedars sflkaielle nseisdkepl
      301 cdvynelaic lmelklfdea ekhlinalsl dsenikiisn lgtlalkqgk qeeaeaffrt
      361 vleinpddki alnvlgksra
//
LOCUS       WP_010698387             361 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010698387
VERSION     WP_010698387.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..361
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40792
     Region          3..360
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mkvslkdigk kyegrenfti rhinleiddk efcvilgpsg cgkstllrmi aglnsitege
       61 lifgekivnk vapkdrdiam vfqsyalyph mtvydnmafs lkmkkerkei ihervleaak
      121 ilqisdnlya kpsdisggqr qrvalgramv rrpgvflmde plsnldaklr ehmrvelvrl
      181 hkqlgttsiy vthdqteamt matkivllnk gkiqqvgkpe efynkpanif takfigsptm
      241 nifegkiehg rfitasgvie vfpkeadakv laayegkkvy lgirserfia geneknsfha
      301 kidvievlgk eqllytkldd gtdcimsepg yfkyavdeih nftfdldalh ffdgetteri
      361 n
//
LOCUS       WP_010698393             189 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Treponema denticola].
ACCESSION   WP_010698393
VERSION     WP_010698393.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..189
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21929
     Region          5..133
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mqvlkeevkd riltaaekvf yeqdyrsakl tdiaeqadip valiytyfkn keglfdevva
       61 gvldkiikmm edeekmeags pyerfnrgga sqlpkllknr ikliilidks sgtkhenakd
      121 mwvkrleqhi kdglkryskt khdpmlahil annyvenlme iarhyknekw aedmlfvlnk
      181 cyfngvesl
//
LOCUS       WP_010698422             489 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010698422
VERSION     WP_010698422.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 489)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..489
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54001
     Region          1..471
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mitlrnisfs ykgtkennly dislhipkgq cvllcggsgc gkttltrlin gliphffege
       61 fsgeaiingm nsaeadiaql sdsvgtvfqn prtqffntdt dseivfglen rglppeqlls
      121 rlekvtedlq iqnlrersif elsggekqki afasvyaaap difvldepss nmdyhsikel
      181 selikkiklq gktiiiaehr iwylmdiadr vifmengkia hdmdiktfvd lpevqiksmk
      241 lrcrnladak aetvnvspdv svsfgrhafa vkditvklgh tsvlkdisfs ttggeiiait
      301 gengagkttl artlcgltqe aagsisfdgn plsrkmrrer symvmqdvgh qlftdsvyae
      361 crlgikdlpd paidevltel slnrlkerhp lslsggqkqr lavavsvlcg kdilifdept
      421 sgldlksmqe agriikrlad dkktvivith diefiktics rvlilsggki vkelcgekkn
      481 elemqletf
//
LOCUS       WP_010698453             439 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Treponema denticola].
ACCESSION   WP_010698453
VERSION     WP_010698453.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..439
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49294
     Region          24..439
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mnepppqwfy illlivllfl smmfssgeta flsvnklkik ylrekknkka arvekilkdk
       61 qkflttslig nslvnilisv lltalmvelv gakglsiavt aatiailifg eilpksialv
      121 fsepialkfs gfilflikvl aplewlfsgf tkfflkflgv knlqsnealt dadlkdffdv
      181 sqehgdlrse ekavlekils ygditvknim tprpdiiglt advnpeeiie lshssrfsrf
      241 pvyeedidei igifyikdfl fseatakdfl qeskekfdik kylrkpvlvf entelsklqe
      301 ifrkekqnmv vvideyggtl giatledlne eifgniadey dtddaaaeep nldnindeat
      361 qnlsqtilgs mrlsdlnenl gtsfsseyyd tigglimekc gevpqigsti kienynftvm
      421 ktegnrisel qvniagdee
//
LOCUS       WP_010698419             221 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Treponema
            denticola].
ACCESSION   WP_010698419
VERSION     WP_010698419.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..221
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24753
     Region          120..214
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mhngisigkg ilwvlvwfgf milytildvs iwrkiapehs rvlniitvil cmtiflvllt
       61 rktnfrpnlf tnisfqglil avgcsilfyf lldkgldpif esffpssren yqqtiqsira
      121 apiiglldfc ilapileeil mrgfllegls inygkivall isaalfamlh fniaqivpsf
      181 icgvilglly fhtgsifsci lahmgynlia ysvivlpiyn k
//
LOCUS       WP_010698470             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Treponema denticola].
ACCESSION   WP_010698470
VERSION     WP_010698470.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Kaatz,G.W., DeMarco,C.E. and Seo,S.M.
  TITLE     MepR, a repressor of the Staphylococcus aureus MATE family
            multidrug efflux pump MepA, is a substrate-responsive regulatory
            protein
  JOURNAL   Antimicrob Agents Chemother 50 (4), 1276-1281 (2006)
   PUBMED   16569840
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..455
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49783
     Region          15..440
                     /region_name="MATE_MepA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Streptococcus
                     aureus MepA; cd13143"
                     /db_xref="CDD:240548"
ORIGIN      
        1 mdskelrrfn iltkpifpll vktsiptiig mlisviynlt dtffvgrlnn ramiaaigiv
       61 fsfvsiiqai gfwfgygsgn amskkigeqd yaeaetissv givfaiiigi liaigasifi
      121 lplskfiggs asqdvltftv qylriiiisi pfslyaltvy nqlrlcgnvr dgmigllsgm
      181 lsnmvldpvl mfifkqgfig agyatligqi igcivltlla krhesisfnl kkaqyskerm
      241 yhilaggmpn fsrqaitsaa lvllnvkaaq ygesmiaalt vssrvaalay mimigwgqgf
      301 qpicamnyga kqysrvkkaf ittvligtif ltaasitlfl faeqcigvms kddevifagi
      361 kilrmqcfsl pllsffavss mfmqnighyf ssllisisrq gffylpllyi lpalygktgi
      421 yllqpfsdvl sflfavavvy rwyssgafss alsae
//
LOCUS       WP_010698473             184 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Treponema denticola].
ACCESSION   WP_010698473
VERSION     WP_010698473.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..184
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=20587
     Region          3..182
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mpktliilah pnisqstvhk hwsdavrqhs drftvhelya vypqgkidva aeqkliethd
       61 slvwqypiyw fncppllkqw ldevlthgwa ygskgkalkg rkialavslg apaadycadg
      121 avgcsvaevl rpfeltakyc nadyrppftf htidsnagys eaarqevers ardylawlda
      181 lqqt
//
LOCUS       WP_010698475             282 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Treponema denticola].
ACCESSION   WP_010698475
VERSION     WP_010698475.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..282
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30933
     Region          25..268
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mkkimllsaa ilfigiiaaa qtktpafkve eqsfqrngmk iygklfipds espvplvils
       61 hgfggnhsgv kgyaaafaeh giaayifdfi gggnhiksdg kmtemsvlte aedltvifdn
      121 lkadsrfkpe qiflfgesqg gfvstyiaal rpadvaglvl lypafvlhdy irqrtpdper
      181 mpdtmkllgk tigriynkdv lsfdiytlmp rysgktliih gtadslvplp yseraiktfp
      241 naklikldga khvfhgdmmq kaaedavkfv qsiigekrsq gr
//
LOCUS       WP_010698560             216 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Treponema denticola].
ACCESSION   WP_010698560
VERSION     WP_010698560.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..216
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24332
     Region          5..216
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnpifknipa qeaekylknt kaktlnykkd afiffegdtp afffvlksgi vqiekntadg
       61 krlivnrfen pgtvfaevya lldsavydya crvisdaeil clpiegvfga gaysethfkv
      121 lknllnilah kayflnqkll ifssfslrqk ialyllqqae gsskvelnln reamaeylav
      181 prpslsrelm smqkdgllki ekdtiivnld kledfs
//
LOCUS       WP_010698490             316 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010698490
VERSION     WP_010698490.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..316
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35872
     Region          2..315
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 myleltnltk tykeknavkn isfnlekgkl lcllgpsgcg kstvlksigg flkpdsgkii
       61 ldgkeitndp penrnvstvf qsyglfphmn vlsniiyglk fkkmpkaerv eagmkmiktm
      121 glsgyekkhi selsggeqqr valarsliir pklllldepl snldaklrin mrkeikqiqk
      181 efnittifvt hdqseafeia dkiilmnnge iiqegtaesl ynqpasefal dfigannkie
      241 nsyirpekik vfkslpeent kdfkeaqinn iifkgeiiel flktkekelk aivlnndcny
      301 kkdervyiky nrenln
//
LOCUS       WP_010698623             323 aa            linear   BCT 01-JAN-2025
DEFINITION  formylglycine-generating enzyme family protein [Treponema
            denticola].
ACCESSION   WP_010698623
VERSION     WP_010698623.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..323
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=35667
     Region          32..323
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mnktlflvaa liamtggsag vnaenadisl agktytvngv sftmiaipav tdgtlgygey
       61 dvnpahtvsl payqigetev tqelwqavmg nnpsgfngnd eetkpaggee qkkrpiemin
      121 wyqaiafcnk lslklglepc ytvtvkgkpi dfaslpfdki psedeympqk driikawdav
      181 tvdiskngfr lpseaewewa akggvesrwa gsddeeevdr ymwhdgnsen rthevkklkp
      241 ngyglydmsg nvwewcwdrf kdflpdslve agvvdiddip dscrvfrggg ididiynaal
      301 pirlfytpdf hagslglrla crl
//
LOCUS       WP_010698627             354 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Treponema denticola].
ACCESSION   WP_010698627
VERSION     WP_010698627.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..354
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=40786
     Region          2..276
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          51..79
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(85,88..90,92..93,97,100,109,134,136,147..148,
                     151..153,155..156,160,163,172,174,181,185..186,189..191,
                     193..194,198,201)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          134..172
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          174..208
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mitignigkf vsipqilndv lnenisalee hllkgwklnk eirvgkytdl spldfalime
       61 kfqsikwlte kgaslnakeh psfllavryc neevirylvs hgakidvvnn vdseafleay
      121 ygkrfdnfsi iqelghsaak yggqllrhav sdrnykilef liehgadiny nksdmvyssq
      181 stplcvaary vdlkmckflv khgadltiae kdgmrpysia lekgdeemae yfksleppef
      241 hqmqnkldel kpyklpkkii eflnggtlhf dladsdfvyl effklidtip fkfgrqkllr
      301 lsrslgdynd iyivwnpktk kiasydmehe elidlaafdd fienmtkymn rile
//
LOCUS       WP_010698650             361 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Treponema
            denticola].
ACCESSION   WP_010698650
VERSION     WP_010698650.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..361
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40959
     Region          <171..359
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mrarrlflfl pltvlailll ltaafflfvt iaeyrpkave kadinvnakk tilqtdevlk
       61 vlnwnigycg ldaqndffyd ggknvtarsk eavldnlekv kallkkedcg fnllqeidvk
      121 srrsfyvdqk kvlsdffady dsvfaanyda vivpapvlnp lgrvksgvft lskygiqkae
      181 rlqlpgtfsw plktvnlkrc llvseiktdv pdknlyiinl hlsaydadgv lrkqemeflq
      241 nlalklyneg hwviaggdwn slfpgveknr fipyttsdef lewieylpad figkewkwgf
      301 dsstptvrll ekpyvkgeny ttiidgfics pnveiigvkt gdlnfevsdh hpviaeftlm
      361 k
//
LOCUS       WP_010698756             695 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Treponema denticola].
ACCESSION   WP_010698756
VERSION     WP_010698756.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..695
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77914
     Region          4..688
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mdktfvsdle fenqewacli rssdadakii dieipdlpeg fsffsakdiv gknsigflkt
       61 evpvfadeki eyagqavgil tgpdkkklle lsslfqiktq ylsrpkaqft feeeeknyfd
      121 ypivsresls sgnaeevfek ssqvvystfs fkqryhyhae tacvktnwvd drleihlatq
      181 wpyqvltsvc nvldvpkeki nvvshaeaes ldgriwfpal laaqvsvasf ltkknivief
      241 srqedflyti ktpivmiqhk tsvselgkit amdvsiivda gsfnpfitqm lkqmvvtaag
      301 iyhlpvymis avaiktekgl tglfsgwgds yvssalekhi seiveqldlc piqfrlqnnl
      361 kvgqktitgi kkeedfvfen ilkavcntsd fyrkfyayrl mnkgrknryd gnwrgigvsv
      421 gcqynglhil vksgmnysae itltkddkvl vkaeptsegl krilkkqiak elevednqiv
      481 flgastdemi ptgaatascg isilpdliek cctgiknqrf rkplpitvsk tyklprskdw
      541 dnetltgnpf isetpgacvi eleldpstyq iivrgiwfac dpgkiyskkm vhrnihktia
      601 navsnisved irennllpsn ykiiatgaip pirdfvldse lktrglgela eslvpaayis
      661 alnqiminhk ridflpvfte difnavtkse avded
//
LOCUS       WP_010698824             234 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Treponema denticola].
ACCESSION   WP_010698824
VERSION     WP_010698824.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..234
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=26776
     Region          42..118
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
     Region          137..222
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mkirfllfiv livnislisc gievevedvk gsrleylnsd snkdsilvid vrpydkykqg
       61 hlshainipl neiknrlrei tdwkdksvyv ysetndesfk aaeilvgnrf sqiynaegvn
      121 qynyktvtyn svrgivfeem lkdpdalild crtksfydig hiegaisfpi feiennldki
      181 pdknkkllly cnvgtassra ayelsnlgyt kiynsidgva eypfklvree edkn
//
LOCUS       WP_010698933             202 aa            linear   BCT 01-JAN-2025
DEFINITION  LemA family protein [Treponema denticola].
ACCESSION   WP_010698933
VERSION     WP_010698933.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..202
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22688
     Region          1..202
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mskglkigli ivavvlvlaf slynffvgty nsivkaeegv ksawsqvenv yqrrfdlipn
       61 lvntvkgyas heakvftdia earskaggvm qvsdevlnnp esfekfqqaq selgaalqrl
      121 lvitenypel kanqnfmdlq tqlegtenri averkrynea vqsynvyirq fprsiianmn
      181 gfrekayfka ddqastapkv nf
//
LOCUS       WP_010698872             474 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010698872
VERSION     WP_010698872.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 474)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..474
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53447
     Region          2..463
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mavelqnysf sydgrtqiln ninikvnqge fvvitglsgc gkttlirvln glcphfysgt
       61 vqgryelygk daknmsigel skywgsvfqd prsqflarkv kdelviamen acedrvlmkn
      121 kleeaarele iekildtdmm ylssgekqkv aigsvfctqp kgfvldepsa nldsaatsgl
      181 aeflkrvkek gcmvvisehr lhylkklidr liimkdgqii kdmskheihs lnnfdlrnlg
      241 lrqfnlpkin vdkkvngdns faackgivyi kncyriletv dlnlesgkvh vivgengagk
      301 sslckiitgl ykqteggmyi dtapvkkker lqrtffvgqd idyqlygysi rnefqignkr
      361 ltdekikacl delhlkisld tnpqvlsggq kqrlligiay lsgrdiivfd eptsgldgfh
      421 mkiiadlfry laekgktiiv ithdieftae vadtiiymsk gkiqyhkyit nenr
//
LOCUS       WP_010699025             303 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF4097 family beta strand repeat-containing protein [Treponema
            denticola].
ACCESSION   WP_010699025
VERSION     WP_010699025.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..303
                     /product="DUF4097 family beta strand repeat-containing
                     protein"
                     /calculated_mol_wt=34116
     Region          <156..302
                     /region_name="YvlB"
                     /note="Uncharacterized conserved protein YvlB, contains
                     DUF4097 and DUF4098 domains [Function unknown]; COG3595"
                     /db_xref="CDD:442814"
ORIGIN      
        1 mkkniilala wfclafavia fftnelrrfn rlgykdfmrf givngkfnph tsvlkemqfd
       61 ineihsikas lisedikfip snddkiivki igieenkelp eikkenevll itasknekkr
      121 fffgwdyshr ieisipsael yiaenagngs aentisafie stssdiriyd itlknlhfks
      181 gsgdvifrns kienqfefnt ksgdikgeaf icgfagtsvs gdfklrflsa pkndstfnst
      241 sgdfsiylpk ditgfscdfn sssgdyknhf tgssaekkiy dvyktdsprl fiktvsgdcr
      301 irs
//
LOCUS       WP_010699044             449 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Treponema denticola].
ACCESSION   WP_010699044
VERSION     WP_010699044.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..449
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49241
     Region          13..444
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mykkdldlte gviwktliif tlpilagnff qhlytaadav ivgkftgkeg laaidsvlsl
       61 lklpinlfsg lsagatiiis qlfgakkike lftaihtsig ltliagisls iigvlispll
      121 lfmmgvpqdi femtlsyvri yfagmgislf ynigsgilra mgnsktpfya livssilnvi
      181 ldlifigifk wgiggaalat vlsqlisavi ilfaltkktg ycplliskik idrlssikia
      241 rlglpigiqs affpianmii qatvngtgtd niaawalcgk ldfliwille amttsvatfv
      301 aqnygarkyd ritgvvrigl imsgiiigsi cvmlyfwnvp lgklfinskd yevliisekl
      361 mhilapfytv fiftevfsaa ihatgetfkp mlitllgvca sriiwiflfv pinpviemiv
      421 lafpiswtlt siiftvyyfi yrkklyqvr
//
LOCUS       WP_010699139             542 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Treponema denticola].
ACCESSION   WP_010699139
VERSION     WP_010699139.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..542
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=63213
     Region          1..199
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 maerktilvs qvlpnldrkm ggygnidtla asikeiglin pitvryesgd nefpytiiag
       61 rrrleavktl glkeieavvy aedelipdee ialaenvnrl dmhpvdegan fkkllkegkt
      121 idelsktfdr spphiyqrik lteltdnmke ffkkgsinis qaariaclpt evqeniynai
      181 skdtwfdgna dyairryakn rldfpctlck nctkrtrytd nnlfpelnnq edycldhecy
      241 ekeivkyykg kikkgvsnys nldflfvngi keeflmplqk ffdfkidlcs fmdytqldqr
      301 vdvctlfdev rkciipwydv indkikfvmk dedyskyfka kreitedekl iieslpdkyk
      361 eearitadkq nlfnysmerq aqtaaisall kkeflkpnpt fylsdnffdc ifrssnkdfi
      421 cdafkimtga nltnlkdtkr fnfkhidfln lffyafilri idsnlydgld tvikllgldv
      481 keakkifnee lknliiedlk kapeeksdde seyeleeted editddsfrs eknedgekvc
      541 yi
//
LOCUS       WP_010699156             304 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Treponema denticola].
ACCESSION   WP_010699156
VERSION     WP_010699156.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..304
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33909
     Region          56..301
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mknklfiilg flcmstllfa ggskegstkq ekgremygym vpasvpqrta vgqvvllqml
       61 dmldvdivar pstkreisar ykdkteigmp mrvdleklke vnpdfylatg drgapiaeql
      121 kalnipaefl qtttytdiln smkylgevyn kqkeaaayvk kvedvvakvk aanknkkplk
      181 vliiagfpns msihtegsfv gslikvlgae niwkdntvkn ttvpmnlelv kasnpdiill
      241 tshgdakdta kmyekefqsd fwqkidavkn kryysldtri ffiagspyip ealetlgnyf
      301 ygsk
//
LOCUS       WP_010699176             305 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine recombinase XerC [Treponema denticola].
ACCESSION   WP_010699176
VERSION     WP_010699176.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11493900
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..305
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=34904
     Region          6..305
                     /region_name="recomb_XerC"
                     /note="tyrosine recombinase XerC; TIGR02224"
                     /db_xref="CDD:274042"
     Site            order(146,251,254..255,286)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 mnevfesylt ysagvrqftk atidsykndl iifeewlkel elnvfelkas dirifiaela
       61 dkkiapasin rmmstlrgfy kyalrfnltk inpissvrnl klaqklpvfm fpkqaqefck
      121 lpsnagilwe trdaalfasl ystgcrvsel agldikdldk tlsyaivfgk gkkerkvffa
      181 efakeylrgy lkersdlvek fkgqvqkdgk gkirdalfin qkaqpltsrg iryiinryve
      241 lspelkhlsp hafrhsfast litrgadirv vqellghesv sttqrythit aeqlqnlykt
      301 ahphs
//
LOCUS       WP_010699184             422 aa            linear   BCT 01-JAN-2025
DEFINITION  YncE family protein [Treponema denticola].
ACCESSION   WP_010699184
VERSION     WP_010699184.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..422
                     /product="YncE family protein"
                     /calculated_mol_wt=47651
     Region          <76..230
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <168..377
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          371..>418
                     /region_name="PQQ_ABC_repeats"
                     /note="PQQ-dependent catabolism-associated beta-propeller
                     protein; TIGR03866"
                     /db_xref="CDD:274824"
ORIGIN      
        1 mkkflcifcf flsamlcfad fafdlnlqpy knteffadgl kvesklissd ktlghlsftl
       61 kdrttslvik kegfrthild ltsienkkaf vvlsptdsky dvvkvfptgr kpksvtfvnd
      121 ktvavalldg sgfdlidiet getkrisppk eyaekfgfve slvlkhknel wvsqmptasi
      181 hifdltsfey krtinstgtw skvmayntgl drvylsnwts qdisvidpss ykeekkiktk
      241 avprgmafsq dgkfiycaqf edsagnsqck likksladyk tvyeggvkga krhivtdyer
      301 kliyvsdmrn divevystdk delvasikvf fnpntiqlsp dksllyvscr gpnnpdkgyl
      361 ykgyvfgrld iidtktftri esieagnqpt gldvspdgkk ivlsdfldnr irvyelkssl
      421 le
//
LOCUS       WP_010699197             658 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Treponema denticola].
ACCESSION   WP_010699197
VERSION     WP_010699197.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18641232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..658
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=75695
     Region          25..50
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          26..284
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          58..84
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(60..61,64..65,67,91,94..95,98..99,101..102,125,
                     128..129,132..133,136)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          89..119
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          124..152
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          158..186
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          192..220
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          225..255
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          227..375
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
ORIGIN      
        1 mkkpffgfmf iallsaslfc npadlyqkga eyqanedwyg aiemyqsalk enpsynlvyq
       61 glaecfyald eydqalsfae sarkykkddp dlqnlhgfil vglgkidaak tlfngvlkky
      121 pnnpearfgl aeievsqgkl ylasemykqn lqrqgenrka llslalvsye agnvkqaedy
      181 inralkyhgd npqvhyfaay lhsldgklee aegriysalk lkedydeaya llasvlyaqk
      241 ryeevikisd mriskkrdra dawylktlsl rrlarygeai naakvglsld addeimrcll
      301 eelaienlnf edsfrmelsk yhaekalgff rrnmteqaly eyrrtlkiyp ydvesreaya
      361 gillrlgype ryleqmlfiq sivksntkvn davetyekhl lssiqskwri dplyldkahi
      421 siglfyames snvlhpeaer itqiltsdif synprikits ysdkpvtyre askksrtane
      481 dyfgiiklke nrrdiqiile lyvsrtgspa ktftvyrsgn drfsngirrl ssmlneampi
      541 vgklinryqn eavidigkhd sdfkdlkiav irkdrlviek eglgivfdps dllgyfepsk
      601 seenlsegil krngyydrmn agdsvilvse ntkekaaedy tnsyqknsll llllrkir
//
LOCUS       WP_010699214             154 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Treponema denticola].
ACCESSION   WP_010699214
VERSION     WP_010699214.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..154
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17295
     Region          8..140
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mstfrakvrr eekfrmkces gnhtmlldep lkaggtdmam npveallsal gackcinawi
       61 faeqfginlk divfemegdi galekvdncl plifksihtk itvfsdntee eikkfieyie
      121 lrcpvrntii nqvpctseii ighlqtievf ksvl
//
LOCUS       WP_010699241             191 aa            linear   BCT 01-JAN-2025
DEFINITION  HDOD domain-containing protein [Treponema denticola].
ACCESSION   WP_010699241
VERSION     WP_010699241.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..191
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=21879
     Region          <23..>89
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mlpskeeaer lleeaylknp gpwrehsiva akcaqkiasa ckdlnpdkay ilgllhdigr
       61 regvtalahv idgyeylmkl gydeaarvci thsfsikkie tyigkndvsp evykkikkli
      121 deyeyddydr liqlcdsial pqgsakieer msdvkkrhgy ypqdkwnkhi elkkyfeqks
      181 gldidelgik v
//
LOCUS       WP_010699263             587 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Treponema denticola].
ACCESSION   WP_010699263
VERSION     WP_010699263.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..587
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66534
     Region          195..535
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 maagkqlike nsayidilpe waqelsrkyc sktanlyfvh gnirdflphq iteyghnflf
       61 vkirdyisev lfgnqdiivy ydksggvsfc tsdmerayle tmhmtypdvp penflsrdpe
      121 eafsyleryf vlnfgknlri vlivdyaeti ipadeignld etdryclvtl nrwshepsft
      181 redisiimlt enltdlnprl taspstikvr iplpdaavrv nflehlrrte eillaergls
      241 permgaltsg lnllnlyqlv gesyqddkpi sldylatkkr eiieneaggl lefidtdydl
      301 slvsghdfvk krfkiaakal kaartdvlpm gylisgpigt gktfivsafa geigipmvrl
      361 rnfrsqwqga tesnlekvln ilramspvav mideadvvlg nrtandisgt ssrvfaqian
      421 fmgntayrgk iiwflitcrp dlipvdlkrq graeehlalf ypetdaerld lfetlqkklr
      481 iklhevnlns iikkikfdvs gadieailvr akmnatvegr amviqkdlee tiadfippsy
      541 pyeielqnlv aaiectskem vpkkyqsmqr samsseifei kqllgek
//
LOCUS       WP_010699277             434 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Treponema denticola].
ACCESSION   WP_010699277
VERSION     WP_010699277.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..434
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45761
     Region          1..432
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 merffklkeh nttvrtevia gittflamay ilavnpgils eagmdrgavf tatalsaaia
       61 tlamgllanl pvalasgmgl nafftysvvi glgyspstal tavflegvlf illslvnvre
      121 aivksiplnl kkavaagigi fitfiafqns giivdnpatl vglgkftwgs pavlamigli
      181 itcalfilrv pgailigili ttvigiplki tvpfggwegw spislpsapa vlnfdfsnil
      241 sfkffivffs flfvdifdtv gtlvgvatqa nlvdkdgnip kikqaflsda igtvvgaaig
      301 tstvtsyves tagvaaggrt gltsvvtagm fiiallfspi fllipsaata paliivgflm
      361 mtqageinyk dptegipafl tmimmpftys vaegivygvl ayvilkcikg kfkeipvvtw
      421 ilfvifmlrf fvkf
//
LOCUS       WP_010699280             127 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Treponema denticola].
ACCESSION   WP_010699280
VERSION     WP_010699280.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..127
                     /product="VOC family protein"
                     /calculated_mol_wt=14404
     Region          2..126
                     /region_name="VOC_BsYyaH"
                     /note="vicinal oxygen chelate (VOC) family protein similar
                     to Bacillus subtilis YyaH; cd07241"
                     /db_xref="CDD:319905"
ORIGIN      
        1 mriehiamyv ndienakkff ikyfkanssd gyhnkttnfr syfltfddga rlelmnhpdm
       61 qdpnkeirrt glshvafsvg skkmvdeltq ilqndgykvl sgprttgdgy yesciigpeg
      121 nqieitv
//
LOCUS       WP_010698986             234 aa            linear   BCT 01-JAN-2025
DEFINITION  orotate phosphoribosyltransferase [Treponema denticola].
ACCESSION   WP_010698986
VERSION     WP_010698986.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..234
                     /product="orotate phosphoribosyltransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004588 - orotate
                     phosphoribosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0046132 - pyrimidine ribonucleoside
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=25664
     Region          19..222
                     /region_name="PyrE"
                     /note="Orotate phosphoribosyltransferase [Nucleotide
                     transport and metabolism]; COG0461"
                     /db_xref="CDD:440229"
ORIGIN      
        1 mhkdekkiae vqkkygplla ktafelgalk lspnepftwa sgyrmpiynd nrrflalpem
       61 rhtiaeafae llkavdfdpe wlagtatagi phsvslgdll kksvsyvrsg gkdhglknqi
      121 eglganadyk gagvlvvedl istggssika veavrnangk vpfcfaifsy gfeeaekafs
      181 elnppcipvt ilnydimlde avkqnyisee nkkslaewrl dpfgwgekhg fpkv
//
LOCUS       WP_010699319             179 aa            linear   BCT 01-JAN-2025
DEFINITION  dTDP-4-dehydrorhamnose 3,5-epimerase family protein [Treponema
            denticola].
ACCESSION   WP_010699319
VERSION     WP_010699319.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14377735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..179
                     /product="dTDP-4-dehydrorhamnose 3,5-epimerase family
                     protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /calculated_mol_wt=20841
     Region          5..169
                     /region_name="cupin_RmlC"
                     /note="RmlC carbohydrate epimerase, involved in
                     dTDP-L-rhamnose production; cd00438"
                     /db_xref="CDD:380337"
     Site            order(24..32,34,47..54,57,59,77,133,137,163)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380337"
     Site            order(49,51,62,64,72,119,132,166)
                     /site_type="active"
                     /db_xref="CDD:380337"
ORIGIN      
        1 miekketpie glfiltnnif sdcrgsfkkl ftqeefktln ldfdfkeiyy sinkknvirg
       61 mhfqipphdh ikmvyviqge itdvcldire nsktygkwfs velsgkddcy lyipkgiahg
      121 fasmedmsiv hyvqtscysk ehdcgihyks fgfdwniaep iiserdasfp dihyykgvf
//
LOCUS       WP_010699382             425 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Treponema denticola].
ACCESSION   WP_010699382
VERSION     WP_010699382.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 425)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..425
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46146
     Region          164..424
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mfwrmiagal frqkgkmvmi aftialgasl stsmlntmlg vgdkvnqelk tyganinvah
       61 kessllddiy geesgntkkf lkedelykik tifwaynivd yapflnvqvd ydgadkpvrl
      121 sgtwfdfrid lhtgqevitg irrmrtwwev ngnwvsdddn sscmvgslfa grnnlkvgde
      181 ikltgaaask tlkvsaifns gsnedevift tlhtaqeflg ktnvcesiev salttpdndl
      241 arkaarnpls ltikemeiwy ctayvssicy qiqevitdav akpirqvaes egailnktsl
      301 lmllitvlsl iasalgisnl vtasvmdrra eiglkkaiga sntavtvsvl tevmvigiig
      361 gaagyfvglg ltqiigrsvf gsaippapmv ipivvliifl itllgslpsv ryllklnpte
      421 vlhgk
//
LOCUS       WP_010699463             443 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Treponema denticola].
ACCESSION   WP_010699463
VERSION     WP_010699463.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Kaatz,G.W., DeMarco,C.E. and Seo,S.M.
  TITLE     MepR, a repressor of the Staphylococcus aureus MATE family
            multidrug efflux pump MepA, is a substrate-responsive regulatory
            protein
  JOURNAL   Antimicrob Agents Chemother 50 (4), 1276-1281 (2006)
   PUBMED   16569840
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..443
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48694
     Region          17..435
                     /region_name="MATE_MepA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Streptococcus
                     aureus MepA; cd13143"
                     /db_xref="CDD:240548"
ORIGIN      
        1 mnqdmktqll tksprellfk laipgiigmv viglysfmdg ifagriigdy amsaisisms
       61 ltlingavsa llgvgsasil sraigkgdte tvdkifgnvc ywvllfsali taagvlsapy
      121 flemvgakga ikdlgvrylr ivflgsvfvn faqagnmtmr gegalkqsmf imgagallni
      181 mldpifmllm geyaiegaai atvlsqmvqa vltlryfakk spfvkihkik kykeiyremf
      241 gigssamlmq llfavqqtvl fkqaftfggd nwgilmsatm rlymfsfipl wgmsqglqpv
      301 iganygakqy grvretmklf mygatllaal swvpamlfse sllsifnvrp eiiaaglinf
      361 klfystfily gimimtltff qsigdakkag aivllrqlil fvpamlilph lfgnlavwwa
      421 epavdftmil igfimqqrvl rrl
//
LOCUS       WP_010699572             419 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphoglycerate kinase [Treponema denticola].
ACCESSION   WP_010699572
VERSION     WP_010699572.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..419
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=45300
     Region          4..417
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 miktvkdvnl kdkriimrvd fnvpmkdgvv qddtriraal ptikyileqg arslvlmshl
       61 gdpskdakka kekaekdgkp fdeeayingk hrmkpvaeyl sgllklpvdf apscmgqler
      121 vkalpqggil mlentrfhke etskekaeqq ilakelslyg diyvndafgt ahrshastae
      181 ianfintrva gflmekeiky lepmlnnpak pmtaiiggak vsskiavles llknasslii
      241 gggmaytflk vqgkkigksl feedfmdtak nlldkaekqg vkiilpvdhi csetfspnae
      301 avlvessdip dnlmgmdvgp ktlalykeii lssksivwng pvgvfefeaf skgteetarl
      361 vaaatekgal tivgggdsva avnkfnladk vshvstggga sleflegkvl pgiacldti
//
LOCUS       WP_010699596             239 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Treponema denticola].
ACCESSION   WP_010699596
VERSION     WP_010699596.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..239
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28330
     Region          8..238
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mkqytsylfd mgstllefhn pkwneseilk nghnrmiayi sniygkfiad kidkevilpw
       61 ydyvekerki krieyricea lflkfgelgi yisyneiiei lkkdyldfyn yahpnegvid
      121 clkflkekky kigvvsnimy pkeiyleifk regldlfidn ytfsyentym kphssiflra
      181 lmslnakise tlmvgdnekv dvigakavgl ktclydkdkk ykqhqadfyi nnfmelidn
//
LOCUS       WP_010699619             250 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Treponema denticola].
ACCESSION   WP_010699619
VERSION     WP_010699619.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..250
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27848
     Region          1..246
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnivqvknlk ktyplgkvsv eavkgidfai eqgefvsisg psgsgkstil nmiglidtps
       61 ggeliinnes iykesdfasl lkkqnkkvkv pnkldkkmtv lrheylgfif qsfnlvpvln
      121 vyeniefpll fgkakeskan qkewinylid kvglsewkhh ksnelsggqr qrvaiarala
      181 tkpqivlade ptanldsktg iqilelmkev nrelkttfif sthdakivdm tnhrikildg
      241 qiledvkvsa
//
LOCUS       WP_010699641             241 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Treponema denticola].
ACCESSION   WP_010699641
VERSION     WP_010699641.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..241
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27638
     Region          7..239
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mkspamiifd ygntliyeke ldleraykal yaqihknpdk idfitfykkg maifekvksq
       61 alqndveiht hnfynclfqi lnvefnlsyt eleilfweal apcrampnie klllflegkn
      121 irtavisnia fsekaviari nkylpqnkfe fiiasseygf rkpdcllfea alkkarlsad
      181 evwycgdnpr advigsaalg ikpvlytssf acpydnenhi spnfeftkis dwdelielie
      241 g
//
LOCUS       WP_010699654            1024 aa            linear   BCT 01-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Treponema denticola].
ACCESSION   WP_010699654
VERSION     WP_010699654.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Burnim,A.A., Dufault-Thompson,K. and Jiang,X.
  TITLE     The three-sided right-handed beta-helix is a versatile fold for
            glycan interactions
  JOURNAL   Glycobiology 34 (7) (2024)
   PUBMED   38767844
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12131601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..1024
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=108850
     Region          549..705
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
ORIGIN      
        1 mkkllkiltm vaavlttavl fttckqfmdd pedflsywaa evvptgydid iakpylisnd
       61 gvicvpsnny llsdgsvtvm iylrnpkkfs lvmpsstssa ldvqkiihfp gfdadhqpky
      121 sadndytleq tpdkqalklk ykssflkkhe wgtadigpei tlkstdgrqf nkkfslnlkv
      181 ntapsfdykg vgktyaggkw yyvlifqakn meeqataghy vhediknlhi vkrdeaeahy
      241 tvsnidfpnk kinwtdsykf lsgatqlaae dcegtppvlp tgdwliyfkt dvevspssal
      301 ktyeawlsde aglvsnkvqg stcirkigei qvtatpsals gtgtnsspye iscngdgvkl
      361 gvwcqtpids vkirywvtnl gtnniessgd gtaspttplq gikllapsai gstikyevrf
      421 kadkpgfvsn ektvyykltr ivgnvidgne pnawaklkya ieyeneseit ikntikaqns
      481 sitiggqiik nyeqinvgre vkikgfdtna vinadskcri fnvannkklt leklkltggr
      541 algsddaans gggiyagsgt titmtgctfd gnvasydtnt gssglggavy avqaanviik
      601 ncifdknmil tngvhgvhdg etgkggavcm vstanvtieg ctftgnkakd gsgvcafkps
      661 nvtitkcifk nninalkgta gyggavcald ganviitdct ltgnkaeygg avaaikndgs
      721 tnpsyitikg giiggtgded aniakgssyg ggiyvgegcn ltlkkksdgr pvqiignmad
      781 hggglyaeka tvimtgcifk gnkeelpnnp syvsqmegga icaygstvti ndctfrgnka
      841 vfggaiyask lkpsqalstn npasyitikg giiggtnpnd ankadnlkds glgggiyvgg
      901 dcsltlqdft aiktvkilgn tarmlgngiy vgrngklnmq ggtqvnennd vylglsskiy
      961 lsgalttsgk aalitpdvyd fsvqvldgsi itgtpqnymk fevtpkggit wyvdsngflt
     1021 tvqp
//
LOCUS       WP_010699691             102 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Treponema
            denticola].
ACCESSION   WP_010699691
VERSION     WP_010699691.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..102
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12136
     Region          4..96
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mkkyilrylp lakqdldgii nyiqnnlqnp iaaentlski esailerldn pedfaiwssk
       61 kqrpypyrri nvgnytvwyv vidnimevrr ilysrryeen li
//
LOCUS       WP_010699722             424 aa            linear   BCT 01-JAN-2025
DEFINITION  leucine-rich repeat domain-containing protein [Treponema
            denticola].
ACCESSION   WP_010699722
VERSION     WP_010699722.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..424
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=46152
     Region          62..419
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          85..105
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          106..125
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          127..147
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          148..168
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          169..189
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          190..210
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          211..234
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          253..273
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          274..294
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          295..315
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 mmaeskklfi tillaagllt avaatenagr avlgisphek eitvtavtad gspvqvegct
       61 vtefpsgeet vltatgtkvv lkgalielvc yknrltsldv rglttlqely cqdniltsld
      121 vreltglhtl ycgknrftal dirgltalqe lycndneias ldvrgltglh tldcdnnrlt
      181 sldvqgltal qwldchfnkl tsldvhglts lqvlecssnr ltsldvhvlt alknlycqdn
      241 kltsldvrgl tglrtlfcss nrltaldvrr ltalqkldcs snaiasidvr gltglhtlyc
      301 dnnrltsldv qgltalqllv csdnqltaln vqdlptlqal gfqhnrleed alirilnslp
      361 drktdeegla vlysegeklp kesgsavpas aefraafkaa kqknwklymq tedgdgteir
      421 lqee
//
LOCUS       WP_010699697             418 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Treponema denticola].
ACCESSION   WP_010699697
VERSION     WP_010699697.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..418
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44413
     Region          12..405
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 msagkipige ialqivlsvg iivivakylg llakklnipq vageivagll lrylpffrnf
       61 ggvepniiya etnqfigyms eigvilimfs aglgtnlksl vasgikstvi aacgvivplv
      121 lgtamalgfw gfdgfgtpvf yqalfigtil tatsvsitva alkelgkins evgqtiisaa
      181 iiddvlgiia ltvvlgassg kgdylaliik taaffaaslv vgyviyrifk wydkrhphth
      241 risiyglgva lifaycterf fgiaditgay vagvvlcnlh dasymekkid insymffspi
      301 fftsiglktd fsglnmsllw fsiafvlvgc iskiigcggs altlgfkrke slqiglgmmv
      361 rgevalivaq kglavgmvka eyfapvilli ivssmivpil lgkafsdrsv appmkeqv
//
LOCUS       WP_010699751             194 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pantoea agglomerans].
ACCESSION   WP_010699751
VERSION     WP_010699751.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21032
     Region          4..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mekqsskaht rrrildeaar vmretgtegi gvaalmkrvg lthggfyahf tsreelveev
       61 lkhmfaeadt fkpaesvtep aqqladfids ylseahrnap aqgcplaalv sevahlpqpt
      121 rqifaqgfna mhaglaqilr elrlpdaeal assmlaemvg alalaracpd aeqasqmlqr
      181 srdalkqrtl evaa
//
LOCUS       WP_010699781             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Pantoea].
ACCESSION   WP_010699781
VERSION     WP_010699781.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..224
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=25049
     Region          24..219
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mdilqsllha lwqqdyetls dptlvwaiyg vlfmilflen gllpaaflpg dsllilvgvl
       61 iakgtmsfpl tilvlttgas lgcwvsylqg rwlgntptvq kwlshlpaqy hlrahsmfhr
      121 hglsalligr fiafvrtllp tiaglsglsn arfqffnwvs aflwvviltv igfalgktpi
      181 frryedemmf flmmlplall vfglvgslvv iwrkrqanqn gkae
//
LOCUS       WP_010699868             188 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Acinetobacter].
ACCESSION   WP_010699868
VERSION     WP_010699868.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..188
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21818
     Region          1..163
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mglglfilff vvliiaviyi rnsivrhyna aqrawadvat yerqkvkvld glvplveqya
       61 gfekstlerv telrqqimql nlkstdisql qrveslshel mrnlnviven ypelkaneiy
      121 lrmineideq nenvsaaisi fnrnvelfnn hiqifpnnmi ntlttgkkai rpfrdqstlq
      181 nfdyrpnf
//
LOCUS       WP_010699962             594 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Acinetobacter radioresistens].
ACCESSION   WP_010699962
VERSION     WP_010699962.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..594
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66275
     Region          141..548
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 maaaldsikr ffsiqadfnl idlrhlalgg rkdgwmlllf iigclaanpf vidniyyrmi
       61 vliacgipca tllfygkiky ffdkeftfdp imeqdkarpf rlpssnpvgs lednigkgic
      121 vgyttdtgea vfipyshisq hiaingstgt gksvlatsmm aqqmrngggl cfidgklsnk
      181 ellavwqlac wsgreldlli inagdpstsn tinpilrgdp qevtsrimml lpevsggaeh
      241 yrnsalialq vivaafqrig lpysfqdita clqdfdafky vesklqlefp dsqetvawfs
      301 lmksfvknkf fdfdsfrnll sglaarlsqf segsfgqvmn synpeidfee cilqnkiiyv
      361 mlptmakneq sialakilia dmrtaishfq rlpahllpnp pfmilpdeag syidetwgri
      421 feqarssrif lapcyqtyan lkpngletls evvmgntlfk vffkqlstls aqqaadeigl
      481 ykqttwalgs gegvsssgde vdtspiqnrg dnrasnftqr eeevyhvkte efkyipigdc
      541 ilyyggthly hlrvplttlt dkaakefgnv qfnhyamdvv eglnlreivr esvs
//
LOCUS       WP_010700114             202 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Acinetobacter
            radioresistens].
ACCESSION   WP_010700114
VERSION     WP_010700114.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22534
     Region          2..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meermaqnrl ailqatrdlt arggfkdaqi naiaelagis sglvyryfns knqllvevlt
       61 daamqeiril esiyredlpp keklfkavta fvkraltgpq layslifepv dvaieiervr
      121 vkqliknaii dilkegqesg dfsfddvnta alcivgamtf avvepidpar rkkfdkqdfv
      181 ryvaefclqa vvrvpqpvqg en
//
LOCUS       WP_010700121             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Acinetobacter].
ACCESSION   WP_010700121
VERSION     WP_010700121.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..301
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33065
     Region          1..300
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mthiilalvp lvaliatgyl fkryhflste fwsgaeklny yilfpallfh tlatakiefd
       61 slkmllaamf itvltativl yllryikhiq parfgvhtqs ivrfntyigl alvaalfkqe
      121 gmailavlla vciplvniis vlsltsseqm slrpviisll knplimsclv gaivnvlkip
      181 vwegvfnlik lfsaaslplg llcvgaalqf memkkdiltl mldtfarllv mpalaigicw
      241 wmqlpvlqtq ilviffalpt asaayiltkv lkgdsqlmaa vislqtlcaa itlplviawv
      301 m
//
LOCUS       WP_010700167             813 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LPS-assembly protein LptD [Acinetobacter].
ACCESSION   WP_010700167
VERSION     WP_010700167.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..813
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92700
     Region          81..791
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mkhkfkfnpl atailtllcg ssissyaeqs epfstvsnnq lkesineayp gqqffeqyyv
       61 dksapeaqlr ntqalssafc qgtwitpvsp dnnapdpdkv tsvitadygy ynpqgdstle
      121 gnvvidqegr siradkvtld qtrtyanaqg rvqlaqggll aqsdqinynl ktqtgdlnns
      181 fyiaeqqhah ghaekierts ptvailsnas yttcppgeap awrlqadrie lnqetgrgvt
      241 tgtklyvknt pvlavpyfnf piddrrttgi lnpqfgfsnd gglelsvpvy lnlapnydat
      301 itpryladrg pmaegefryl tenfgegrvw ggylpsdkey ndedrkefhf lhdwvinpyw
      361 stnleynyvs dkdyfadlds spnsktdlnq rrawvinyrn qipglkaqlk vedfqtldkd
      421 ikdedrpyar lpqfllnyvg gnpqglqyef nndtgyfkks inddsdvles sgtriynqfa
      481 vrynyrnpws fvipevsfrs intfydrdsr edrgieadsl tksvavpqft ldtgllfeke
      541 gtflqsispr lfyayapykd qndypnfdtt tasisydqlf npyrfyghdr lednnflslg
      601 vtyslmdqig lerlrasvgq syffedrrvt lynedeldqe krtgpvlsls sqlnqnftis
      661 ansawmsnge nsqrdfqvyy tgnqgnlynl gyfyrkdipn rqdsydqvva sfiqpvynnw
      721 rimghvqydi dqdvareyll gvnyesccwg vsvygrsyyn dlddinepgv kpkravmaef
      781 tlkglgglnn klasllesrv lgfskinqsw tqr
//
LOCUS       WP_010700405             374 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu, partial [Acinetobacter radioresistens].
ACCESSION   WP_010700405
VERSION     WP_010700405.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     gene            1..>374
                     /gene="tuf"
     Protein         1..>374
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
     Region          1..374
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makakfernk phvnvgtigh vdhgkttlta aiaticakty ggeakdyaai dsapeekarg
       61 itintshvey dsptrhyahv dcpghadyvk nmitgaaqmd gailvcaatd gpmpqtrehi
      121 llsrqvgvpy iivflnkcdl vddeellelv emevrellst ydfpgddtpi irgsalqaln
      181 gndgqygesa vlalvealdt yipeperaid kaflmpiedv fsisgrgtvv tgrvesgivk
      241 vgeeveivgi kdtvkttvtg vemfrkllde gragencgvl lrgtkredvq rgqvlakpgt
      301 ikphtkfdae vyvlskeegg rhtpflngyr pqfyfrttdv tgaiqlkegv emvmpgdnve
      361 msvelihpia mdag
//
LOCUS       WP_010700429             391 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thiolase family protein [Acinetobacter].
ACCESSION   WP_010700429
VERSION     WP_010700429.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 391)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..391
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40559
     Region          1..389
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mtdivivnga rtamggfqgs lsgltapelg avtikeaiar aglqptdvee vimgcvlpag
       61 lkqgparqam rkaglpdstg avtinklcgs gmkavmqaad mikagsaeiv vaggmesmtn
      121 apyvlpkara gyrmghgeik dhmffdgled aetgrlmgsf aqdmantrgy treqmddfai
      181 rslkraqtai tegyfkdeiv pvtvstrkgd vivdqdeqpl nakidkipsl kpafakdgti
      241 taanassisd gasalvltss evaaqrglqp lakiiatasn sqhpseftia pvgaiekvlk
      301 kagwnaqdvd lgeineafam vtmcpiddfk ldpekvnihg gacalghpvg stgsriiltl
      361 ihalkrtggk kgvaalcigg geatavaiei l
//
LOCUS       WP_010700583             292 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Bartonella
            bovis].
ACCESSION   WP_010700583
VERSION     WP_010700583.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..292
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33200
     Region          47..278
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mikkphkpkf rwpttfiqqk lhkpllnvir nysghqpntf hcdkdydlvv asynvhkcvg
       61 vdkifnptri vrviaelqad ilalqeadkr fgervglidl kllkaetnli pvplntmspn
      121 ghgwhgnalf vrqgrvhdil qislpgiepr gaimaeleme tgfiriiaah fgllrhsrnq
      181 qvkmlltllq krsfmptlli gdfnewrvgk ksslnhffpy fditlgtvps fpsrfpflal
      241 drifafpphl vtkveshysp larvasdhlp ikahlnlanv matfndkise kn
//
LOCUS       WP_010700639             389 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA recombination protein RmuC [Bartonella bovis].
ACCESSION   WP_010700639
VERSION     WP_010700639.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..389
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44218
     Region          60..376
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mfdsffslil lnrhfyevia lfllasfvvm miirsnrkka ievaahahem qiqmaallkt
       61 qaemqgrmqt maeifgqrqa elnqsireql ngmttnlgqt lqvqtkstye nltrlqerla
      121 vidaaqnniq sltgqiiqlq ailnnkqtrg ifgqgrmeai iadalpanty vfqavlsngk
      181 qpdclihmpn kapalvvdak fpleawhamr kassseerkk aerqfrtdmd vhirdiaqky
      241 lipgethdta flfvpsesif atiyedfepl vqkanrahvi ivspsllmls vqvvqtimkd
      301 akireqahlv qsevaklmed fgrmdmrvrs lqkhfyktge dieailtsss kimrrasrie
      361 afelkendfm pksitahvqp qtlrlndeq
//
LOCUS       WP_010700650             303 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Bartonella bovis].
ACCESSION   WP_010700650
VERSION     WP_010700650.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..303
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33031
     Region          12..290
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 midqlllpfq lsfmikgmti tvilsipmam lscflilkgw allgdaisha vfpgvvigym
       61 ttpwvitflt slpfswfhhl hpanvtmili vfgafvagmi caiiigflgs nsrikqdtvm
      121 gvvfssmfgl glvlataiys nldlnhilfg nllgvnwldi tqtaiisiiv tlilgtkwrd
      181 fmlyifdsiq graiglqism lhytlltmis ltivaalkav giilvislli apgaiaylit
      241 krffsmllia vlvavfssfl giylslfigs dsastivlil tlifaavfvw ifvqqattqe
      301 kqv
//
LOCUS       WP_010700705             342 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Bartonella bovis].
ACCESSION   WP_010700705
VERSION     WP_010700705.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..342
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=38655
     Region          <50..316
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mvdkinthnn nqisshtega ssqrtnhiek nsflshlfsf lrgrnytslr ddltdalaah
       61 neddatlfsp eerimlhnil rlretriddv miprseieal eintplgeal eyfekigysr
      121 mpvyaetldd prgiihirdi lshitrfitn sastkngqks vplqlshtee lhipigkldl
      181 irtvlfvpss mlasklltrm qatrtqmalv ideyggtdgl vsmediveli vgdiedehdn
      241 innvivrepd nkwlvdarte ledvekalgp dfivgeygde vdtigglivs ildripskge
      301 iieaipgyrf rileadkrri krlriirise nehlneeats kg
//
LOCUS       WP_010700732             272 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Bartonella bovis].
ACCESSION   WP_010700732
VERSION     WP_010700732.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..272
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=29541
     Region          <153..271
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mircliiica ltvasisivr asgymviqep ipvffpstfs weglylggqi gggvgrlsvn
       61 priisgkstv skksqtvssd kynlagfigg fyigsnlrld nglilsvdtd ivlsnqknvq
      121 fgkrmtvsdq salvhnalvs rfghkksgsi kvgnevtynt trkekwagat ririgfatgh
      181 impyiaggia ytnlqiipwf lvnsanplnl maekktligy tlgagvnfai sdnvilrgey
      241 rysdfgkkkf mevpvnvsys thdlrvgvay kl
//
LOCUS       WP_010700733             290 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Bartonella bovis].
ACCESSION   WP_010700733
VERSION     WP_010700733.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..290
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30878
     Region          85..290
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mnmkcvvtas ifalvsasaa qaadmpiqer pttvlpqvvv apafswtgfy lggqiggfss
       61 ksnskgtyek apnellennk afpkfsgfvg glyagsnvdf dngfvlgvdt divwsgekak
      121 asktytlaqd gtddkkrlva radgedggtg geggtggegd kpntppvpsd vtrnvtfnsk
      181 wsgatrvrlg fafdrimpyv aggiaysqik asvaqreggs vvekpledws nsktfvgytl
      241 gagvdfamte svmlraeyry sdfgkksfvn dnievdfktn dfrvgvaykf
//
LOCUS       WP_010700736             161 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Bartonella bovis].
ACCESSION   WP_010700736
VERSION     WP_010700736.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..161
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17890
     Region          6..146
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mtltpmeial leaqlaakqd eipvgavimr gktiiaragn ciktacdptg haeirairma
       61 cemlqnerip dcdlyvtlep camcaaaisf arirrlyyat sdpkggaiey gprfyqqptc
      121 hhipevysgf kekeanhllk effaqkrnqk hilsspqtht l
//
LOCUS       WP_010700855             242 aa            linear   BCT 01-JAN-2025
DEFINITION  RlmE family RNA methyltransferase [Bartonella bovis].
ACCESSION   WP_010700855
VERSION     WP_010700855.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Hirata,A., Okada,K., Yoshii,K., Shiraishi,H., Saijo,S.,
            Yonezawa,K., Shimizu,N. and Hori,H.
  TITLE     Structure of tRNA methyltransferase complex of Trm7 and Trm734
            reveals a novel binding interface for tRNA recognition
  JOURNAL   Nucleic Acids Res 47 (20), 10942-10955 (2019)
   PUBMED   31586407
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Caldas,T., Binet,E., Bouloc,P., Costa,A., Desgres,J. and
            Richarme,G.
  TITLE     The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S
            ribosomal RNA methyltransferase
  JOURNAL   J Biol Chem 275 (22), 16414-16419 (2000)
   PUBMED   10748051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..242
                     /product="RlmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=26738
     Region          32..235
                     /region_name="RlmE"
                     /note="23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ
                     [Translation, ribosomal structure and biogenesis];
                     COG0293"
                     /db_xref="CDD:440062"
ORIGIN      
        1 mkktiktstg grggagshel yqrvkkkagt ikassrrwle rhlndpyvhq skmdgyrsra
       61 ayklieiner ykilkkgqki idlgaapggw cqvvarivgs ndqrpsvvgi dylhvdplpg
      121 vvmlemdffh edapqklina lgakpdvvls dmaapttghr qtdhlrtvyl cesaadfais
      181 vlkpgghfla ktfqggaent lltklkqnfk tihhvkppas rtesvelylv alklkektet
      241 qq
//
LOCUS       WP_010700898             316 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Bartonella bovis].
ACCESSION   WP_010700898
VERSION     WP_010700898.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..316
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=35516
     Region          152..285
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mkfklttlfv tttllvgtsl svmaqdhvks vpndlntlkk aseksvapsh vmaiingksi
       61 tageldelal einpnlarls deqrritvlk ayldmqalak aaieegidkt evynkrmvim
      121 rdnvlqqlyf kqmvvdkikd tdlqalydke vaalpkedev karhilvktk eeaeaiikrl
      181 kkgenfeeia kkystdgsas vggdlgyfsy gqmvkpfeda afglkvgeyt kkpvespfgw
      241 hiikvedrrl kqppafddvk evlrtqimkd ryhtlitdlr nkvdvkypds hiaklmqsln
      301 ennaalpget sneeee
//
LOCUS       WP_010700921             259 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Bartonella bovis].
ACCESSION   WP_010700921
VERSION     WP_010700921.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..259
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28196
     Region          7..251
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mtshsdetid efhrgkfylv qprlqghrsg mdamllaslv pnhfkgkvvd lgagagaagl
       61 avasrcfeth vtlversafm isyaqktlal kqnkklsdrv clleadvalk gnarlkaglm
      121 dnvfdfaimn ppfnnpvdrk tpdeqkseah vmpeamfdnw lrsaaaiikp ggylgliarp
      181 qslndilhal egrfgnicii pvhsraktaa trilfyakrg sraalsilpa livhegegha
      241 fsphvdainn gcislwelf
//
LOCUS       WP_010700976             252 aa            linear   BCT 01-JAN-2025
DEFINITION  hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Bartonella
            bovis].
ACCESSION   WP_010700976
VERSION     WP_010700976.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..252
                     /product="hydroxymethylpyrimidine/phosphomethylpyrimidine
                     kinase"
                     /EC_number="2.7.1.49"
                     /EC_number="2.7.4.7"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008902 - hydroxymethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008972 - phosphomethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=26850
     Region          7..241
                     /region_name="HMPP_kinase"
                     /note="4-amino-5-hydroxymethyl-2-methyl-pyrimidine
                     phosphate kinase (HMPP-kinase) catalyzes two consecutive
                     phosphorylation steps in the thiamine phosphate
                     biosynthesis pathway, leading to the synthesis of vitamin
                     B1. The first step is the phosphorylation of...; cd01169"
                     /db_xref="CDD:238574"
     Site            order(12,24,45,81,213)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238574"
     Site            order(13,15..16,18,22,25..26,29,32..37,39,42..46,51..52,
                     54,56..57,60,63,67..68)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238574"
     Site            order(106,143,177,210,212)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238574"
ORIGIN      
        1 malipsiliv agtdptggag ivcdietaah fqtktslait cvnvqdnnhv akitpmsgef
       61 vsaqmrvale anpisaikig mtgtkeiiaa icnvledhsh ipvvfdpvlt assggkltte
      121 ktieimlnkl lphielltpn meelallsqs plasnceeai qqakkllsfg prhilikggh
      181 angtlatdil idknqvinis aprlkgemrg tgcilssait ahlafnksit tavkkakeyl
      241 ytlflnyhqk dh
//
LOCUS       WP_010701079             245 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Bartonella bovis].
ACCESSION   WP_010701079
VERSION     WP_010701079.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..245
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28029
     Region          24..240
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mwdftsqhnn spllskqfke slfnvplivi vlivfcflgy iipqyffsdq lyikslilfs
       61 fipfffqaep lmfcytivsy sfmhgsfghv vmnmvwllvf gsplarhfgn lrflffwilt
      121 agisaltyfi fhqdnmiplv gasgaisgmm gaiarygffs vfdsnmrser flgpvwpirk
      181 alrsktvlvy igvwliincl tgifpylfgn sdiliaweah vgglisgfil isffdhpwkk
      241 lkini
//
LOCUS       WP_010701081             391 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu [Bartonella bovis].
ACCESSION   WP_010701081
VERSION     WP_010701081.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     gene            1..391
                     /gene="tuf"
     Protein         1..391
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=42723
     Region          1..391
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makskfertk phvnigtigh vdhgktslta aitkyfgefk aydqidaape erargitist
       61 ahveyeteqr hyahvdcpgh adyvknmitg aaqmdgailv vsaadgpmpq trehillarq
      121 vgvpaivvfl nkvdqvddae llelvelevr ellskydfpg ddipivkgsa laaledsdks
      181 igedavrrlm sevdnyiptp erpvdqpflm piedvfsisg rgtvvtgrve rgiikvgeei
      241 eiigirptsk ttvtgvemfr klldqgqagd nigallrgid regiergqvl akpgsvtpht
      301 kfkaeayilt kdeggrhtpf ftnyrpqfyf rttdvtgivt lpegtemvmp gdnvamdvsl
      361 ivpiameekl rfaireggrt vgagivskii e
//
LOCUS       WP_010701112             235 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Bartonella bovis].
ACCESSION   WP_010701112
VERSION     WP_010701112.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..235
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=26899
     Region          10..235
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mipewlhflf npellshygp rlisglivtl eltfiscfig fflgilitla hlssnkplqy
       61 lsrsytyffr gspllaqlfl fyyglgsmsd fwqkiglwwf fqnawyccif ifalnsaayq
      121 akifigsfqs latgqheask alglsgsttf frvfvpqami lalrplgnef ilmikssala
      181 slvtiydlmg iakliyartf dfqvyvwvai iylfivelih gltvliehrl trylr
//
LOCUS       WP_010701127             458 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Bartonella bovis].
ACCESSION   WP_010701127
VERSION     WP_010701127.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..458
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51070
     Region          4..445
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 msvnklkrgm nkrqviflaf gsaigtglfy gstqainlag psvliaycia glavfmvmra
       61 lgemiihnpl pgsfaryaan hisplagflt gwtyvfevvl vgladitvfa tymgfwypgv
      121 spwiwtlsit liitainlaa vkvygelefw lssikviaii vmivlgiaii vfnwnmgtqs
      181 tvhnlwqngg ifpngwfgfl acfsvvvfsf ggveivgiaa metqdpnkti skainsipir
      241 illfyvitlt vlmilypwnk igligspfvs ifenlgissa anilnvvvvt aaisainsem
      301 ygasrmihgl sqegyvfkkf qylskngipi fiillisvvf ffgvvlnyfy hdqlffliaa
      361 matfatvfvw lmillsqifm rlkmpkekqh nlkfpipfwp vgsifailfm ififvllcff
      421 ddtrpvlmig vawlswlvvc fyalkffnke krktickn
//
LOCUS       WP_010701179             358 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Bartonella
            bovis].
ACCESSION   WP_010701179
VERSION     WP_010701179.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..358
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39314
     Region          4..358
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mntemfiqhf lnalalgsly gliaigytmv ygvlrlinfa hgdifmlgay fvffstisfm
       61 pawvaillil lalliyysvf igfkkrpkiy wiailfilis cliyylkiap qnftpiwiva
      121 icfsvfitsa lgiavdqcay rplrnapris vlisaigisf fienlatvlf sgvpkgvkqp
      181 dflvtpiqwh fgqgldtiir ispmsfivpv vsfilviill wiihktkpgl amraishdie
      241 tarlmgvsvn kiiaftfaig salgavagim walrypqiqp ymgilpglka fiatviggig
      301 silgamlggl llgflevmiv affpalsgyr dafafillii illvmptglm gkksqeki
//
LOCUS       WP_010701181             191 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Bartonella bovis].
ACCESSION   WP_010701181
VERSION     WP_010701181.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..191
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21280
     Region          28..92
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
     Region          118..182
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mtskdtlkny slsednfdvc geiteisgvi kwfdsskgyg fivpdlyelp dillhvtvmr
       61 rdgfqtaleg akiicvvkkt erglkcvqvk sidlssavhp seipvrthiv vtpesglera
      121 ivkwfnrdkg fgflsrgqgt edifihietl rrfglaelrs gqvvivrfgk gekglmtaei
      181 ypdiafpftt h
//
LOCUS       WP_010701208             121 aa            linear   BCT 01-JAN-2025
DEFINITION  NADH-quinone oxidoreductase subunit A [Bartonella bovis].
ACCESSION   WP_010701208
VERSION     WP_010701208.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012780
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..121
                     /product="NADH-quinone oxidoreductase subunit A"
                     /EC_number="1.6.5.9"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=13708
     Region          1..121
                     /region_name="PRK06602"
                     /note="NADH:ubiquinone oxidoreductase subunit A;
                     Validated"
                     /db_xref="CDD:180638"
ORIGIN      
        1 mthllssylp vlifiiisav iagallitpy ivayrapdpe klsayecgfn sfddarmkfd
       61 irfylvsilf iifdlevafl fpwavsfgsi gmlgfwsmmi flailtigfi yewkkgalew
      121 d
//
LOCUS       WP_010701244             411 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Bartonella bovis].
ACCESSION   WP_010701244
VERSION     WP_010701244.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..411
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=45788
     Region          <293..411
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mntkclists iitlftasva qaadiivpqe srpvvsppak mskqvlppve mnpnsdappv
       61 isaptfswng fylggqiggf sgktgisvya kketgtrewt pvekdklpql sgfmgglyag
      121 anvdlgnslv lgvdtdivws nkqdtkivak gqfekpelpe kpgeteerel nerrertinl
      181 krvlspqriq hednhlpqqe lyssqtlmre shssrsssqq hlsttsglgs nlrqkrsarn
      241 sseelqrqqr sqpevsdfpi lrsdresspv rrrhvreves vdedelvgsi kktdsntlkq
      301 kwsgatrvri gfaadrilpy iaggiaytql qntysrsiei fgreirsssv sdtkmmvgyt
      361 lgggvdfamv dnvilraeyr ysnfgkqkfa kdkleidyqt ndfrvgvayk f
//
LOCUS       WP_010701306             443 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A [Bartonella bovis].
ACCESSION   WP_010701306
VERSION     WP_010701306.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..443
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=49675
     Region          7..437
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mnkdfftlsf dshvsknrpl aermrprsls evigqdhlig tegflsrmia agsfgsmifw
       61 gppgtgktti arllalqtnf ifeqvsaict gvtelkkife vaqarfmsgg rtllfvdeih
      121 rfnraqqdif lpfmedgtvv lvgattenps felnnallsr arvlkfrlhd gkslstllkr
      181 aeevegktlp lddqarnlli rmsdgdaraa ltlaeeiwca arpeeifnak alqeiiqrra
      241 piydkgqdsh ynlisalhks irgsdpdaal yylarmfdag edplyigrrl vriavedigl
      301 adpqaliicn aakdaydylg spegelalaq aclyiatapk snavylayka amhcarkngs
      361 lpppkhilna ptklmkedgy gegylydhse pdafsgqeyf peklgrqiyy qpqergfere
      421 ivkrlewwkk lrqkrgsqkq dcd
//
LOCUS       WP_010701251             404 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Bartonella bovis].
ACCESSION   WP_010701251
VERSION     WP_010701251.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..404
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=44788
     Region          48..398
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mnkisdshnn pttlqsmkek ikesslegry tsyipayaqv tlpnsmkkqv ffwlgtliff
       61 vifmfvfgsi llpfvagivl ayflnpivql lekvgicrvf gtilitlfiv iifvvaltil
      121 ipvigwqiqq fvssglpvyi sriqnfltes nfdwigryfg sdpnelqtni ktllgqssdf
      181 itsllnsllr sgksivniis lfviapvvaf ymlldwqrmv eavdswiprd hletvrsify
      241 emdraiagfv rgqgtvclil ggyyaiglti tglnfgllig mfvglisfip yigtmsgfil
      301 sggvawvqfy pdnwgriiiv mtvffigqfi egyilqpklv gssvglhpvw lmfalfafgs
      361 lfgftgmlva vpaaaaigvl vrfalhtyln sqmysqsgns gsve
//
LOCUS       WP_010701345             274 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Bartonella bovis].
ACCESSION   WP_010701345
VERSION     WP_010701345.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..274
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30396
     Region          87..274
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mntkclitas iltlvtssvv qaenstisqe stsvslsnva ptfswtgfyf ggqiggfssk
       61 tslnlnyfkg inskklssie kdllpklsgf igglyaganf dlnnslvlgv dtdiiwsdkk
      121 dtkvikrsay rmqdgpklqr ennkveavdi khllekftvt yshtlkqkwa gatrvrigfa
      181 adrimpyiag gvaytqlqdi flasieaked kvvdetkami gytfgggidf amtddfilra
      241 eyrfsnfgkk kfvkdkfeid yktndfrvgv sykf
//
LOCUS       WP_010701394             193 aa            linear   BCT 01-JAN-2025
DEFINITION  SCO family protein [Bartonella bovis].
ACCESSION   WP_010701394
VERSION     WP_010701394.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11133300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..193
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21285
     Region          33..163
                     /region_name="SCO1-SenC"
                     /note="SCO1/SenC; pfam02630"
                     /db_xref="CDD:460630"
ORIGIN      
        1 mknviyifgl tviflagvft ydawknkplg dnftliastg qtvteadirn kpsaiffgft
       61 mcpescpttl tdldrwltei gpnadklgiw fvtvdperdt pevlrdylsn ftnniigisg
      121 dpekvhkmvs sfnivaekvp gtdgnytydh taaifllkkg gklagiipyn taenenqlkd
      181 diaikqlkkl tsn
//
LOCUS       WP_010701408             379 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Bartonella bovis].
ACCESSION   WP_010701408
VERSION     WP_010701408.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..379
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=41961
     Region          13..371
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mmvtranqdp ianwwwtvdr fifaaclilm gigvmlsfaa spavakkigi adsfyfvrwh
       61 iifsilafft mvtisffspr nirrlcilll faalilmvat llfgselkga rrwislfgis
      121 lqasefmkpa fvvvsawlfs dqmkhygrfr yilsialyal cctllvlqpd igqtllisat
      181 wgglffvtgv pltiilffvi lavvggflay ffvhhvreri ngfltgegdt fqvdvgreai
      241 lnggwfgqgp gegtikriip dshtdfvfsv aaeeygiifc llimalfgfv virslyialn
      301 trdsftcfgi tgmaimiglq sginmavnlh lippkgmtlp fisyggssmv aiaismgill
      361 sltrrwpetr fsafpppii
//
LOCUS       WP_010701424             408 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Bartonella bovis].
ACCESSION   WP_010701424
VERSION     WP_010701424.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..408
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46401
     Region          118..387
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mteflaqhpl leaiswlvil tliallinil arkllihkak qlfsflpadt tddteyiirh
       61 mantasafif sigvnfiptl pnplstiirn vsnafiifvi vliisallni vntlyeqrpt
      121 srlkpikgyi qiakialftv atvlilakli drsplilfsg lgamaavlil vfqdtllslv
      181 asiqisstdm vrvgdwieip nlgadgdvie ialhtvkvqn fdktittvpi rklvtdpfkn
      241 wrgmeesggr rikrslfidq ssirfhkeee qeylmqfnll enyfakkipe inewnakldk
      301 nrdipaniry ltnigtfray vlsylqnhpn ikknmtcmtr qlsptpnglp levycftntt
      361 iwieyeqiqa difdhlysil psfglklfqn psgydfihaf kttqnhkf
//
LOCUS       WP_010701430              69 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Bartonella bovis].
ACCESSION   WP_010701430
VERSION     WP_010701430.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..69
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7348
     Region          1..57
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mstgtvkwfn ttkgfgfiqp ndgsadvfvh isaiersgls nlnegqkisy dvvqdrrsgk
       61 fsagnlail
//
LOCUS       WP_010701445             362 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Bartonella bovis].
ACCESSION   WP_010701445
VERSION     WP_010701445.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..362
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=40695
     Region          2..349
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 matlrekike iiavngpitv sqymtlaltd pqfgyyqtkt pfgstgdfit apeisqlfge
       61 miaiwvlasw kaqgnpnpfi laeigpgrgt lmndvlrtiq klcktafnaa eiflveisqr
      121 laieqkkrls syqkhihnie yfnqipsghl flianelfda lpihqyikin gewrercitl
      181 dqdghftfia gvhkfsaddl paycakmpng tiwehaplrn qlmqqisnrl iqtkgsalli
      241 dygasdcafg dtlqaiskhk frdvfanpge hdltshvdff slktialqqg cfaeileqgd
      301 flfkmgiler akqlsinkai siqnkirqdi erlvssdqmg klfkvlhvsd qpttisnfld
      361 sq
//
LOCUS       WP_010701494             230 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Bartonella bovis].
ACCESSION   WP_010701494
VERSION     WP_010701494.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..230
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26552
     Region          1..212
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltlfhhpls sasrfirlil eeysiethli eehewarkpe flalnpaghl pvflaeheip
       61 lsgaiviyey ldetrgslrp dkqffpanpl eraevrrlnd wflnklenev trhivreriy
      121 kremplaigg gapnsqilrs aranilphmn ylnwlctsrd wlagstlsya dlaaaasisi
      181 ldflgeidwe qfsavrewym riksrpsfrp llndrvrgit psshyadldf
//
LOCUS       WP_010701461             302 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Bartonella bovis].
ACCESSION   WP_010701461
VERSION     WP_010701461.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..302
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33352
     Region          7..290
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mstkikiqkl tlwsilvaci vftlkywayq itgsvalysd alesivniia alaawwavki
       61 slkpadqnhp fghhkaeyfs ailegiliiv aaimilrkal fsfstvelpq qpgiwiginl
      121 svciinylwg lllirqgkih hspalkadga hvmmdvftsf giliglvtaf vsgwavldpi
      181 laiivaihif vqgwkvihns vqglmdvgve lnetmqisdl ilanacgaie ihdlrtrvag
      241 rvifiefhlv vptmmqvgea hqicnkieea lkvefenari tihiepenea kflpgtmtip
      301 ft
//
LOCUS       WP_010701498             305 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Bartonella bovis].
ACCESSION   WP_010701498
VERSION     WP_010701498.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..305
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=33715
     Region          <185..305
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mntkclitts ifilaatslv qaadsvvfqe nlktdalpiv rpptfswsgf yiggqvggfs
       61 skisaishdd dipllpsrsg rpkkwipvde kflpklsgfi ggfyagsnvd lsnglilgid
      121 tdillsarkn tktivitdpn vdespeiden peengsepqn esrqkqrsrr avqlkentsd
      181 tekgeediit fkytlnqkwt gatririgfa adrimpyiag gvaygqfqni islsstdkel
      241 nntsdetktm igytvgagid famtdniilr aeyrysdfgk qkfakdsfel hyktndfrag
      301 isykf
//
LOCUS       WP_010701503             377 aa            linear   BCT 01-JAN-2025
DEFINITION  type III PLP-dependent enzyme [Bartonella bovis].
ACCESSION   WP_010701503
VERSION     WP_010701503.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Eliot,A.C. and Kirsch,J.F.
  TITLE     Pyridoxal phosphate enzymes: mechanistic, structural, and
            evolutionary considerations
  JOURNAL   Annu Rev Biochem 73, 383-415 (2004)
   PUBMED   15189147
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10089786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..377
                     /product="type III PLP-dependent enzyme"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41262
     Region          18..377
                     /region_name="PLPDE_III_ODC"
                     /note="Type III Pyridoxal 5-phosphate (PLP)-Dependent
                     Enzyme Ornithine Decarboxylase; cd00622"
                     /db_xref="CDD:143482"
     Site            order(46,48,67,133,176,179,215..216,253..256,300,325,357)
                     /site_type="active"
                     /db_xref="CDD:143482"
     Site            order(46,48,67,133,176,179,215..216,253..256,325,357)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143482"
     Site            order(48,69..70,72..73,95,100,113,116,120,147..149,270,
                     272..273,283,285,287,290..291,299,301,322,324,326,329,361,
                     363,366..368,370)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143482"
     Site            order(48,325)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143482"
     Site            order(299..300,325..326,357,366)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143482"
ORIGIN      
        1 mttqrirdfl sthrpkgpcl ivdldvvren ylnfekalpq srifyaikan papeilslla
       61 slgssfdaas iaeiemalea gataerisfg ntikkecdia yahtlgisly avdcveevek
      121 iaraapgari fcriltngeg aewplsrkfg cvpdmavdvl rrahqlglqa ygvsfhvgsq
      181 qthlnawdha lsdvalvfer lekegiqlkl vnmgggfptr ylkevptaqv ygiaifdslk
      241 kyfgnripet iiepgraivg nagvirtevv liskkadgdn irwvyldvgk fnglaetmge
      301 airypietih ddkamepcil agptcdsadv myektpyllp lsltigdell ihgtgaytat
      361 yasvafngfe plrsyii
//
LOCUS       WP_010701522             226 aa            linear   BCT 01-JAN-2025
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Bartonella bovis].
ACCESSION   WP_010701522
VERSION     WP_010701522.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..226
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25338
     Region          4..221
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mgiikfdkvt qifgdlcvlk nitvqlterr vaiigangsg kstfvrling lqlpssgfvs
       61 vdgldtkrda kavkskvgfv fqnpdnqivl plvhedlsfg lknlklskee irqrvneilq
      121 rydlqnlknh avhllsggqk qliaissviv mkpdyiifde pttlldlrnk rkvaqvieel
      181 pqtaivvshd leflkkfdrv lvfdkgeiii ddtplvaike ymmkml
//
LOCUS       WP_010701700             263 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Bartonella bovis].
ACCESSION   WP_010701700
VERSION     WP_010701700.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..263
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28716
     Region          6..248
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(36,40,46,69..70,86..91,213..214)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(39,41,92..93,95..100,152..154,156,158..159,167..168,
                     171,174..175,178,182..188,196,200..203)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 marsaimnvm vqaalkagrs lvrdygevqn lqvslkgpad yvsqadrkae kiifselika
       61 rpkfsflmee seeiigedsq hrfivdpldg ttnflhgipf favsialerq gqivagviyn
      121 pildelftae rgcgsflndr rcrvaarrkl gecviatgtp hfgghnhghy lvelrnvmge
      181 vsgvrrfgaa sldlayvaag rtdgfwednl qiwdmaagii ivreaggfvs dkdgesamfg
      241 tkniiagnef ihaqlsqtlk kgv
//
LOCUS       WP_010701715             398 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphoglycerate kinase [Bartonella bovis].
ACCESSION   WP_010701715
VERSION     WP_010701715.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..398
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43271
     Region          5..394
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mkfrtidevd vagkcvlvrv dfnvpmlqgk vcdetrlerh ketlselqkr gaklilishc
       61 grpkgqkvse lslrpvaqal skimgqeisf ldkcvglevr aavqalkegd illlenlrfh
      121 qdeednddaf aealacsadi yvndafsvsh rahastegit hflpsyagrs lqrelhaleq
      181 glgnpaypla avvggakvss klfvlnhlvq kvnilviggg mansflaaqg yaigkslyeh
      241 tlmetveeii ekaheyqcel vlpvdvvvgl hcekntpyrq cdledisdne mildvgprsi
      301 erinemldta atvvwngplg vfevppfdqg tiavarhvak rtqqgklvsi agggdtvfal
      361 nhagvandft ylstaggafl ewmegkslpg vlalcrle
//
LOCUS       WP_010701764             332 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine recombinase XerC [Bartonella bovis].
ACCESSION   WP_010701764
VERSION     WP_010701764.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..332
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=37084
     Region          22..322
                     /region_name="xerC"
                     /note="site-specific tyrosine recombinase XerC; Reviewed;
                     PRK00236"
                     /db_xref="CDD:234698"
     Site            order(161,175..176,247,249,268,303)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271175"
     Site            order(175,268,271,294,303)
                     /site_type="active"
                     /db_xref="CDD:271175"
ORIGIN      
        1 mspnnnnkkg qnaplipaeq gllvarkkwl ealvktrrma trtkeayerd trqfliflch
       61 hlghevtckd ltdlcvadlr aylayrrtlk isarslsrni aslrsffnyl sregivdtla
      121 aklirtpkhp kllpkplsvq aalhivkpen qqadepwiia rnvavlally gcgmriseal
      181 altpeqfsdp eitslsvigk ggkarlvpli ktvhemvety lkccpyplas tqpmfrgtrg
      241 gplqaaiiqr lvqnlrarlg lpetttphal rhsfathlls rggdlrtiqe llghaclstt
      301 qvythidtdr llevyqkthp raskvieskk is
//
LOCUS       WP_010701770             258 aa            linear   BCT 01-JAN-2025
DEFINITION  SURF1 family protein [Bartonella bovis].
ACCESSION   WP_010701770
VERSION     WP_010701770.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..258
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=29301
     Region          21..251
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mikmnqsptk sqsknisffs ilfgilcigf fllfsalgvw qvqrlnwktn liasvnqrih
       61 lppikappqn qwkritfdkd eyrpvtltgn lltdknifvt altqnttgyw vltplqtadn
      121 tltfinrgfi pmdarhhfeq ekaspyphss tnieqititg flrmsegdvi fprknnpdqn
      181 lwytrqlpam aqklglsnva pyfidvtqki atqgdlpivg ltvvhfnnnh lsyaltwfil
      241 aagvlgafff lfskynnn
//
LOCUS       WP_010701786             144 aa            linear   BCT 01-JAN-2025
DEFINITION  EVE domain-containing protein [Bartonella bovis].
ACCESSION   WP_010701786
VERSION     WP_010701786.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Bertonati,C., Punta,M., Fischer,M., Yachdav,G., Forouhar,F.,
            Zhou,W., Kuzin,A.P., Seetharaman,J., Abashidze,M., Ramelot,T.A.,
            Kennedy,M.A., Cort,J.R., Belachew,A., Hunt,J.F., Tong,L.,
            Montelione,G.T. and Rost,B.
  TITLE     Structural genomics reveals EVE as a new ASCH/PUA-related domain
  JOURNAL   Proteins 75 (3), 760-773 (2009)
   PUBMED   19191354
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..144
                     /product="EVE domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=16581
     Region          2..137
                     /region_name="EVE"
                     /note="Predicted RNA-binding protein, contains EVE domain
                     [General function prediction only]; COG2947"
                     /db_xref="CDD:442190"
ORIGIN      
        1 maywlfksep qkwswtmqkq kgthgeqwdg vrnyqarnnm ramkygdkgf fyhsnkglei
       61 vgivevcaqa hpdsttsdpr wecvdiralc dmptpvslkq ikanpklknm alvktirlsv
      121 qpvtedewke icsmgrlkpe mflt
//
LOCUS       WP_010701781            1570 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Bartonella bovis].
ACCESSION   WP_010701781
VERSION     WP_010701781.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 1570)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1570
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..1570
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=177801
     Region          14..1563
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mskqetldik nnqkqlvkil fahtdkedia cykkdeleka aaiaaqalsl hqagksticf
       61 eqkeltrsgk pitaitlvnd nkpflldsvl nvfnqqvshi yliahpvldc psgqrisliq
      121 ihiealskqk akilkdeltl vleqvnaavq dwkpmleelk khihayqtnl pqnyqkegek
      181 aieflnwltd nnfiflgmrt ynfiknkepq nslkagnvel giltdasiri igdthveerp
      241 qevlsfmenn dllivtkans rskihrpiwl dyigikifnk egrvcgelri vglftssayt
      301 rsvlqipflk ekaqtiiqrl gynqadysgk alinvletyp rdemfrsdvd tltenaelil
      361 qlderprlrv lahtdsfgrf isilvyvprd qyssnipeki gtyfvdiyeg dffesyplfl
      421 estlirihyi ihrkgnnsvp aierttleqh irsitrnwed nvqavalahk ateqqtllas
      481 qfpnsyrdlf saedaivdad hilslndekp lfvtfyhthh kekhnialrl fhrhealals
      541 irvpllenmg frviaeqtle lpdghgkyvy lhdmllesaf qtcidlnkng qkhaetfeai
      601 wakdadddaf naltqtaqld wreivilrhy grylqqagip ysqkrvaqtl naypditkdl
      661 yalfhlkfhp shkekerqnn eqiiqqriee klqmvpnldd dlilrryrnl iaaslrtnaf
      721 vplpngnprr ilatkldprq ieglpeprpy reifvygpev egvhlrfgpi arggirwsdr
      781 aldyrtevld lvkaqqvkna vivpvgakgg fyphhlpktd dravvaeaar qayidyital
      841 lsitdnlins kisaptnvir hdgddpyfvv aadkgtatfs dtanaisqad nfwlddafas
      901 ggsagydhka igitakgawe avkrhfrelf dhniqttpfs cvgvgdmsgd vfgngmllsk
      961 qtkliaafdh rdifidpepn iaesyaermr lfqlprsswq dydkaklskg ggifsraakt
     1021 itlspeaaqa igfekqtgtp feiitailka pvdllwfggi gtyirattet daqvgdrand
     1081 alritgeqvr akvigeganl gltqrgriey vlnggrcntd aidnsagvnc sdlevnikiv
     1141 lasamraqml trkardtllk qmtpqveqlv lrnnylqtla lslaenrgii dlpyqarfih
     1201 dleqkklldr rveilpddqi lrqrmdqgqs ltrpelavil ayakltlqee itsnsivdnr
     1261 yfdatllnyf ptqlqksfkn eiidhqlrrd iiatliandi vnrggptfvs rlqdktgqkv
     1321 eniirvfiai rdgfeipqls dqidnldnki pglvqnkfya aitsmlfett nwgllnidls
     1381 vpleelvtti qqarktiekq lthsnnkdih ekiaekialy seqgipntla kqlalletap
     1441 micdisliak qsqsdltkta kiyfsltqii rvnrineasq tipvldyydg mvlsqakeni
     1501 aenvrrivik ilknygdknd plaawlktee dkicdvtnri galiendlni srfifaanmi
     1561 aqlkniafqt
//
LOCUS       WP_010701793             229 aa            linear   BCT 01-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Bartonella bovis].
ACCESSION   WP_010701793
VERSION     WP_010701793.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..229
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26224
     Region          87..208
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(117,120)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mipqifinwk nkktqclfts fiialslytt inhdhktplf shfisvakaq etntnkikae
       61 kiiaikketk gffkhirfad tsynigqfsf kdiqgkdhkf seftgkplli nlwaiwcapc
      121 rvempelaql krdmkeenfd viainidkaa spekiqqflr evhadnltyy rdekmniftn
      181 irkqglalgl pitllvdqdg dliasfngia pwanddakaf iktiikktk
//
LOCUS       WP_010701794             284 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Bartonella bovis].
ACCESSION   WP_010701794
VERSION     WP_010701794.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..284
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32183
     Region          10..284
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 miknvlwysy rilinavshy vrddgsafas hivlsgllaf fpfcifgasl asffwdfayt
       61 pqkiealmyl lpdaiaepfs keiinvlttq rrglltlsfv gvayfasngv ealrtalnka
      121 yrvvdhrslf fcrfqslffv ivgaigitvi sfllvlapll ikitqnhfpf iaeyigvirl
      181 wrytiavvil fisllivhkw lpakrrklid ilpgivvtlf lwfaasitfa hyltmfnyvs
      241 tyaglasimi aiiflymlsa ifilggeina aimfyrtrlq rldp
//
LOCUS       WP_010701825             302 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Bartonella bovis].
ACCESSION   WP_010701825
VERSION     WP_010701825.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..302
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33911
     Region          49..301
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mnddqskkrl grglaaligd asldsngahl lnsvrftmks nvdsivserl vsielisrnp
       61 nnprrhftdl elenlaqsir qhgvvqpilv rpsphhpgrf eliagerrwr aaqranlnql
      121 pviirdvddk talelaiien iqradlnpie eaigyemlln eygytqadla qvigksrsyv
      181 tntlrllklp sevqklling qlsagharcl itvnnpqdla ekiireglsv rqvevltheq
      241 tnpkikkrtl vkkdtetksl eklltdmigm kvvirhgkeg gdlkihyssl eelddicrrl
      301 qs
//
LOCUS       WP_010701956             342 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Bartonella bovis].
ACCESSION   WP_010701956
VERSION     WP_010701956.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..342
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=38627
     Region          <50..316
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mvdkinthnn nqisshiega ssqrinhiek nsflshlfsf lrgrnytslr ddltdalaah
       61 neddatlfsp eerimlhnil rlretriddv miprseieal eintplgeal gyfekigysr
      121 mpvyaetldd prgiihirdi lshiirfits sastkngqks vplqlnhteg lhipigkldl
      181 irtvlfvpsf mhasklltrm qatrtqmalv ideyggtdgl vsmediveli vgdiedehdn
      241 innvivrepd nkwlvdarae ledvekalgp dfivgeygde vdtigglivs ildripskge
      301 iieaipgyrf rileadkrri krlriirise nehlneeatl kg
//
LOCUS       WP_010701970             536 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bartonella bovis].
ACCESSION   WP_010701970
VERSION     WP_010701970.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..536
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60009
     Region          1..532
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtkmlsvrnf svafcqaeek kyvvdqisfd igkgeivalv gesgsgksvt alsilqllpf
       61 vktlyqsgei lfnnqdlmkq keedlrkvrg kdiamifqep mislnplhtv ehqigevlki
      121 hsnisgkllr triidlltqm gisepekrlg sfphqlsggq rqrvmiamal annpqllvad
      181 epttaldvtv qtqiltlliq lkkscnmsml lithdlaivr rvaervyvmk egkivesgst
      241 neifnnpqhs ytkkllaaef qgyplqandn apvlmqgqki hvwfpikkgl lrrtvgyvka
      301 vqdvditvha gqtlgvvges gsgkttlgla ltrmisskgq iyfdnidisn ftfnqmrslr
      361 rhiqivfqdp fgslsprmsv seiiteglsi hepylsdser ndrvlealhe vdldpavrhc
      421 yphefsggqr qrisfaraii lkprfimlde ptsaldmstq aqivdllrrl qqkyhlgylf
      481 ishdlkvvka lahevlvmhk gkvveydsad rifscpqnsy tqtlmaaafa lesgrl
//
LOCUS       WP_010702008             247 aa            linear   BCT 01-JAN-2025
DEFINITION  creatininase family protein [Bartonella bovis].
ACCESSION   WP_010702008
VERSION     WP_010702008.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..247
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=27578
     Region          7..241
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 misdtlslal lplgaheyhg nhlpfetdwi iaeafakaly sqikgqfhik llpvekigys
       61 iehmdvsgtq tltfsdaier winigekcyh ngikrfllln ahggnsplms ivitelrkrf
      121 smlavatswh rfglpeglie psehhldihg gfietslmly lapekvqmeq aenfynkqad
      181 mianyqylra ygphafgwtm rdlnpqgaag nakkatpkag kaifshvlcg llnlledvsq
      241 fntsilq
//
LOCUS       WP_010702051             156 aa            linear   BCT 01-JAN-2025
DEFINITION  crossover junction endodeoxyribonuclease RuvC [Bartonella bovis].
ACCESSION   WP_010702051
VERSION     WP_010702051.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002778
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..156
                     /product="crossover junction endodeoxyribonuclease RuvC"
                     /EC_number="3.1.21.10"
                     /GO_component="GO:0048476 - Holliday junction resolvase
                     complex [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008821 - crossover junction DNA
                     endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=17079
     Region          8..147
                     /region_name="RuvC"
                     /note="Holliday junction resolvasome RuvABC endonuclease
                     subunit RuvC [Replication, recombination and repair];
                     COG0817"
                     /db_xref="CDD:440579"
ORIGIN      
        1 msfhsqtilc ldlgtktgwa issedgtias gtvnfstrrf egggmrylrf kqwltetkai
       61 lghidavyfe evrchigtda ahvyggllai ltswceryqi pyqgipiati kkamtgrgna
      121 pktemikavr tkghepeddn eadalailyl ikqggv
//
LOCUS       WP_010702104             108 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF167 domain-containing protein [Bartonella bovis].
ACCESSION   WP_010702104
VERSION     WP_010702104.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..108
                     /product="DUF167 domain-containing protein"
                     /calculated_mol_wt=12294
     Region          1..84
                     /region_name="YggU"
                     /note="Uncharacterized conserved protein YggU,
                     UPF0235/DUF167 family [Function unknown]; COG1872"
                     /db_xref="CDD:441476"
ORIGIN      
        1 mlyridasgl ilfvrlipra svdsivgves wdggtqhlvi rlrtipangk ankalikfla
       61 rqwkipssyi slksgtisry kqlrfsgyid eleqklqfms nihlrkye
//
LOCUS       WP_010702116             428 aa            linear   BCT 01-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Bartonella bovis].
ACCESSION   WP_010702116
VERSION     WP_010702116.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..428
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=48586
     Region          6..427
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mrlggrlqaa idilkeieir hrpasealkd wglshrfagv ndraaigtiv ydvlrrrysl
       61 qwrmdsddvr niafgalldt gamtieqids tlerdrfapq llapeqrysw qkrqlvdapd
      121 yirgdipqwc qvhlqplfad nwaieaaala trppldlrvn slkatpekvl kelakikvqs
      181 fswfrqalri apiekfgrhp nvqvepafqk ghfevqdlgs qivahltetk agvqlldyca
      241 gaggktlala anmnnrgqiy aydsnkvrla pifnrlrrag ihnvqsrvhv eelksligqm
      301 divlldapcs gtgtwrrrpd akwrltleqv kqrqaeqfai lnealvylks ngrlvyitcs
      361 lfideneeqi srflkqhsnf cpidlralwq rhfnsstvqp ifsnygltls pastqtdgff
      421 lailqrah
//
LOCUS       WP_010702132             138 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Bartonella bovis].
ACCESSION   WP_010702132
VERSION     WP_010702132.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..138
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15929
     Region          1..133
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mdkkqnyeqv lraaglritr qrrvildilt dtdnhpnafe ifqyankids sislstvyrt
       61 mktleengti hrhafsggps rfeqangqhh dhlidvetgr iiefqsdiie klqeeiarsl
      121 gydiihhrle lygkkrns
//
LOCUS       WP_010702155             574 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Bartonella bovis].
ACCESSION   WP_010702155
VERSION     WP_010702155.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13537404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..574
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=65435
     Region          <33..538
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          311..337
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          347..371
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          374..>555
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          379..409
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(416,419..420,423..424,426,450,453..454,457..458,
                     460..461,485,488..489,492..493,496)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          416..443
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          448..479
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          484..512
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          518..546
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mhyaikscff tlaiagivli psltyskids atnassftga ylagrvanhe nktnlainyf
       61 kqaltynpnn idaqkevfea mlsvgafkea vkqakklqeq nihhpfislt lsidslikkn
      121 ykdikllpqp ktspainnpa fdvisawatf gsgnhsqaia dlkkllgpiw ynlfihyhla
      181 lmsdlakrpk dakkyfmqal nnqqgamvsp dtyeriiiay asfqlrqkmr sqaiqtiqng
      241 ekilsgreil knirqkvekg anldnpvktp qqgageilyd fgttlnrrks ehvarifeql
      301 sltlypqnda tlfqlanvsa klndphqaik lyralsphsp yyregqlqla ltlannnqht
      361 eaiksltsle kkypndrtiy ialsavymrk nnfieavkvm draitqtidf qkddwklfyq
      421 rgiaferlkh wtkaetdlrk alelfpdqpq vlnylgytli drnqkleesl ymlqkasalq
      481 pkngyildsl gwahyklkqy nqavkileta vklqpqdptl ndhlgdvywk vgrkreaifq
      541 wnhaidgqpe nldkikeklk fglqdttmld hakq
//
LOCUS       WP_010702212             252 aa            linear   BCT 01-JAN-2025
DEFINITION  hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Bartonella
            bovis].
ACCESSION   WP_010702212
VERSION     WP_010702212.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..252
                     /product="hydroxymethylpyrimidine/phosphomethylpyrimidine
                     kinase"
                     /EC_number="2.7.1.49"
                     /EC_number="2.7.4.7"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008902 - hydroxymethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008972 - phosphomethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=26772
     Region          7..246
                     /region_name="HMPP_kinase"
                     /note="4-amino-5-hydroxymethyl-2-methyl-pyrimidine
                     phosphate kinase (HMPP-kinase) catalyzes two consecutive
                     phosphorylation steps in the thiamine phosphate
                     biosynthesis pathway, leading to the synthesis of vitamin
                     B1. The first step is the phosphorylation of...; cd01169"
                     /db_xref="CDD:238574"
     Site            order(12,24,45,81,213)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238574"
     Site            order(13,15..16,18,22,25..26,29,32..37,39,42..46,51..52,
                     54,56..57,60,63,67..68)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238574"
     Site            order(106,143,177,210,212)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238574"
ORIGIN      
        1 malipsiliv agtdptggag ivcdietaah fqiktslait cvnvqdnnhv akitpmsgef
       61 vsaqmrvale anpisaikig mtgtkeiiaa icnvledhsh ipvvfdpvlt assggkltte
      121 ktieimlnkl lphielvtpn meelallsqs plasnceeai qqakkllsfg prhilikggh
      181 adgalatdil idknqvtnis aprlkgkmrg tgcilssait ahlafnksit tavkkakeyl
      241 ytlllnyhqk dh
//
LOCUS       WP_010702342             235 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Bartonella bovis].
ACCESSION   WP_010702342
VERSION     WP_010702342.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..235
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=26947
     Region          10..235
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mipewlhflf npellsrygp rfinglivtl eltfiscfig fflgilitla hlssnkslqy
       61 lsraytyffr gspllaqlfl fyyglgsmsd fwqkiglwwf fqsawycclf ifalnsaayq
      121 akifigsfqs vatgqheask alglsgsttf frvfvpqaii lalrplgnef ilmikssala
      181 slvtiydlmg iakliyartf dfqvyvwvai iylfivelih gftvlierrl trylr
//
LOCUS       WP_010702355             467 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Bartonella bovis].
ACCESSION   WP_010702355
VERSION     WP_010702355.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..467
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52049
     Region          7..424
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mkpplnsfdd lglsekvika vrsagyatpt piqsetiphv lqhkdvlgia qtgtgktasf
       61 vlpmltllek grararmprt lileptrela aqvqenfdky gvnhrlnvvl liggvsfedq
      121 nrkleqgadv liatpgrlld hfergkllli gteilvidea drmldmgfip dierickltp
      181 ftrqtlffsa tmapeitklt eqflhspiyv evtkasstak titqrlvksg skawdkravl
      241 reliynegdk lknaiifcnr kkdiselfrs ltkynfsvga lhgdmdqhsr mntladfkdn
      301 kltllvasdv aargldipdv shvfnydvpt haedyihrig rtgrakrsgk aftivtpndq
      361 kyisaiekis kekiewlngd lstlsvkdqa ndsiiktksa kllkkstpkk htahikklsk
      421 edkafyneta knkvnspdls nlekdkgsip lgfgsdipaf mlikirs
//
LOCUS       WP_010702391             285 aa            linear   BCT 01-JAN-2025
DEFINITION  DsbA family protein [Bartonella bovis].
ACCESSION   WP_010702391
VERSION     WP_010702391.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16062126
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..285
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32283
     Region          75..100
                     /region_name="ScsC_N"
                     /note="Copper resistance protein ScsC N-terminal domain;
                     pfam18312"
                     /db_xref="CDD:465704"
     Region          129..282
                     /region_name="DsbA_Com1_like"
                     /note="DsbA family, Com1-like subfamily; composed of
                     proteins similar to Com1, a 27-kDa outer
                     membrane-associated immunoreactive protein originally
                     found in both acute and chronic disease strains of the
                     pathogenic bacteria Coxiella burnetti. It contains a
                     CXXC...; cd03023"
                     /db_xref="CDD:239321"
     Site            order(145,148)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239321"
ORIGIN      
        1 mthqlhhltt tfiakvsmia alsiliclpl ssleakekvs nnsiienlki qlledstfls
       61 klsekitpsi nddyireivk dyllknpeim iemqlvlqek lggieeqqaf iikslekeif
      121 hsfhdavfgn pngkitlvef fdyncnfckr sypsmvnlik eypdlriiik dlpilgpdsi
      181 eahtiayafr qqlpekyfqf ykellsgqnr ankakaikia vslganekdl hnaiqnpnlq
      241 ksfkrniqia svlningtps yiigdrifmg avsedilkkv iesiq
//
LOCUS       WP_010702408             352 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Bartonella
            bovis].
ACCESSION   WP_010702408
VERSION     WP_010702408.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..352
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38526
     Region          29..335
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 maksttlfls fisivaligf lfyadnhfnd yilriinlia inailaisln liygftgmfs
       61 lghagfmaig ayvcaillls peqkemmwil epiaeplqsl qlpffiavii sglcaavvgl
      121 liafpilrlg gdylgiatlg faeiiriiit natsltngsl gikgipqnat lwwnygwlaf
      181 tiifitlllq snignvlrai rddeiasktm ginnffyrsf sftvgaffag iggaltaali
      241 stidpkmfnf lltfnilmiv vagglgsitg siigsiiitv lleslriies plnlsfiyip
      301 gipglrmvvf sllllviilf rrkgllgqre fswnwiycll trripfssee ks
//
LOCUS       WP_010702409             358 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Bartonella
            bovis].
ACCESSION   WP_010702409
VERSION     WP_010702409.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..358
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39357
     Region          4..358
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mntemfiqhf fnalalgsly gliaigytmv ygvlrlinfa hgdifmlgay fvffstinfm
       61 pawvaillil lalliyysvf igfkkqpkiy wiailfilis gliyylkiap qnftpiwiva
      121 icfsifitsa lgiavdqcay kplrnapris llisaigisf fienlatilf sgvpkgvkqp
      181 dflvtpiqwh fgqgldaiir ispmsfivpv isfilvilll wiihntkpgl amraishdie
      241 tarlmgisvn kiiaftfaig salsavagim walrypqiqp ymgilpglka fiatviggig
      301 silgamlggl llgfleimiv affpvlsgyr dafafilliv illvmptglm gkksqeki
//
LOCUS       WP_010702461             821 aa            linear   BCT 01-JAN-2025
DEFINITION  penicillin-binding protein 1A [Bartonella bovis].
ACCESSION   WP_010702461
VERSION     WP_010702461.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..821
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91090
     Region          4..789
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 miiffryllt sfvalgifgv ivwaamtnsq anelpdyevl slyepsvmtr vhaadgslma
       61 efatkhrlyl piesipnllk eafisaedkn fyhhfgldpe glaralinni inigsgrrpe
      121 gastitqqva knfllnseat lerklkegil airiektysk dhilelylne iylgrgtygv
      181 aaasltyfnk svheltleec aylaalpkgp gnydpfkntq raierrnwvi drmvankyit
      241 peqgkqtkkr plgvkvrgsd syvfaadyft eevrrhlmhh ygattlyegg lsvrttldph
      301 lqliarrslq dglikfdhsq gwrgaykhid vtddwgitla nitglsdvpe wnlavvlsss
      361 ankieiglqp qrensgllsk ewiitalsie qskwalnvig ennhrtiahn lsdvlhvgdv
      421 ifvekipntn niyrlqqvpk iegaivamdp htgrvlamvg gfsftesefn ratqahrqsg
      481 safkpfvyaa aldngytpas vvldgpveif qgngriwqpk nyggtfagps tlrygiehsr
      541 nlmtvrlahh mgmplvaeya erfgvtdklp pylsmalgad ettvlrmvta ysviangghs
      601 ikpsfidriq drygrtiyhh ddrlcencnv qswnnqtept lidereqvld pmtayqitsm
      661 megvvqrgta arlrylnrhi agktgttnes kdawfigftp dlvvgvfigy dqpaslgrtg
      721 tgsslgapif gefmqaalkd kpnvpfkmpk gmilmkinrk tgmlakaddn dvifeafkpg
      781 tgpadvyqvi getnsfqegv ptvttspqvn kalqngsggl y
//
LOCUS       WP_010702473             412 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Bartonella bovis].
ACCESSION   WP_010702473
VERSION     WP_010702473.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..412
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=45879
     Region          <295..412
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mntkclints iitlftasva qaadiivpqe srpvvsppak mskqilppae mnpnfdappv
       61 isaptfswsg fylggqiggf sgktgislya kketgtrewt pvekdkllrl sgfmgglyag
      121 anvdlgnsli lgvdtdivws nkqdtkiiak kqfrkpelpe legeeeeels eerkkkhlkd
      181 itallrensh qseenntlys rntilreqpl sqsspssprs srekrsfdtt qrngerikql
      241 slrdedlese sqqrvqrqta ealvssshsg alssvrphvi eepvdemvei vdkvysntlk
      301 qkwsgatrvr igfaadrivp yiaggvaytq lqntysrsie ilgkeiyssn lsdtkmivgy
      361 tlgggvdfam tdnvilraey rysdfgkqkf akdkleleyq tndfrvgvay kf
//
LOCUS       WP_010702478             102 aa            linear   BCT 01-JAN-2025
DEFINITION  ETC complex I subunit [Bartonella bovis].
ACCESSION   WP_010702478
VERSION     WP_010702478.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10521567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..102
                     /product="ETC complex I subunit"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_process="GO:0001932 - regulation of protein
                     phosphorylation [Evidence IEA]"
                     /GO_process="GO:0006120 - mitochondrial electron
                     transport, NADH to ubiquinone [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /GO_process="GO:0032981 - mitochondrial respiratory chain
                     complex I assembly [Evidence IEA]"
                     /GO_process="GO:0042776 - proton motive force-driven
                     mitochondrial ATP synthesis [Evidence IEA]"
                     /GO_process="GO:0072593 - reactive oxygen species
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=11751
     Region          2..95
                     /region_name="NDUS4"
                     /note="NADH dehydrogenase ubiquinone Fe-S protein 4;
                     pfam04800"
                     /db_xref="CDD:461433"
ORIGIN      
        1 mvariyspak tsmqsgkani gvwilqyepe qakmleplmg ytatsdmnsq ikiwfkmkee
       61 aiafalknsi pyrvenscks ffrraisysd nfrsdrqqsw th
//
LOCUS       WP_010702610             110 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Bartonella
            bovis].
ACCESSION   WP_010702610
VERSION     WP_010702610.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..110
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=11654
     Region          1..109
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mnrgeiwlvs ldpssgyeqk gtrpvlivsp eafnsvtktp vvlpitsggs fartagfvvs
       61 lmgvglhttg vircdqpral digarkgkkl ekvpvmimne vlaklstflt
//
LOCUS       WP_010702648             193 aa            linear   BCT 01-JAN-2025
DEFINITION  SCO family protein [Bartonella bovis].
ACCESSION   WP_010702648
VERSION     WP_010702648.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11133300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..193
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21282
     Region          30..163
                     /region_name="SCO1-SenC"
                     /note="SCO1/SenC; pfam02630"
                     /db_xref="CDD:460630"
ORIGIN      
        1 mknviyifgl taiflagvft ydawknkplg ddftliastg qtvteadirs kpsaiffgft
       61 mcpescpttl tdldrwltei gpnadklgiw fvtvdperdt pevlrdylsn ftnniigisg
      121 dpekvhkmvs sfnivaekvp gtngnyiydh taaifllkkg gklagiipyn taenenqlkd
      181 diaikrlkkl isn
//
LOCUS       WP_010702657             298 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Bartonella bovis].
ACCESSION   WP_010702657
VERSION     WP_010702657.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..298
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=33629
     Region          79..278
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 myalnvdrin vlmvqsvpff prlyrrfrrf ifqfivsiyv prhfgsfavl fffslsalyg
       61 issngqmdsi ikaaplnfgf vvtdvdmngn kriarqdilk vlgldaypsi isfdvnkarf
      121 ileqqawiqs anvqkiypnq vsisvierep yaiwqhdgim diidhtgyvi apfqvglvqn
      181 lplvvgqgaq naaklfiqel waypqlsnri sayvrvgdrr wdivldngvr imlpekraie
      241 slssliktgv aedlfardvl sidlrlsdri tvslsdealv hhravvaeke rvlkaggv
//
LOCUS       WP_010702662             379 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Bartonella bovis].
ACCESSION   WP_010702662
VERSION     WP_010702662.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..379
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=41900
     Region          11..371
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mmvtranqdp itnwwwtvdr fifaaclilm gigvmlsfaa spavakkigi adsfyfvrwh
       61 iifsilafft mvtisffslr nirrlcilll fsalilmvat llfgselkga rrwislfgvs
      121 lqasefmkpa fvvvsawlfs dqmkhygkfr yvlsialyal cctllvlqpd igqtllisat
      181 wgglffvtgg pltiilffvv lavvggflay ffvhhvreri ngfltgegdt fqvdvgreai
      241 lnggwfgqgp gegtikriip dshtdfvfsv aaeeygiifc llimalfgfv virslyialn
      301 thdsftcfgi tgmaimiglq sginmavnlh lippkgmtlp fisyggssmv aiaisvgill
      361 sltrrwpetr fsafpphii
//
LOCUS       WP_010702684              69 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Bartonella bovis].
ACCESSION   WP_010702684
VERSION     WP_010702684.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..69
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7300
     Region          1..69
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mstgtvkwfn ttkgfgfiqp ndgssdvfvh isaiersgls nlnegqkisy dvvqdrrsgk
       61 laagnlavl
//
LOCUS       WP_010702706             158 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA (cytidine(34)-2'-O)-methyltransferase [Bartonella bovis].
ACCESSION   WP_010702706
VERSION     WP_010702706.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..158
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=17891
     Region          3..152
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 mtlhialfqp diagntgtil rlsacfgihv hiiepagfnl sdrnlkragm dyleyaller
       61 hidwqhfiet mrhfnrrlll lstkaktcyt dihyqkndvl lfgresagvp nyvyetvdha
      121 ltipmqphar slnlamsvai ttgealrqig yneieniv
//
LOCUS       WP_010702733             248 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Bartonella bovis].
ACCESSION   WP_010702733
VERSION     WP_010702733.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..248
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27056
     Region          1..244
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkiivavkhv vdynikirvk sdgtgvdlsh vkmsmnpfde iaveeairqk eadktsevvl
       61 vsigpeeaqe tlrsglamga drailvktee vleplaiakt lktiireekp nmvflgkqai
      121 ddesnqtgqm laallgwgqa tfashlnied hqaiitreid ggtqticlpl pvvmttdlrl
      181 neprytslpn iikakkkpie qkaladlcvd trarltvlti eepqsrqagi kvanvaelvs
      241 alkktsci
//
LOCUS       WP_010702714             302 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Bartonella bovis].
ACCESSION   WP_010702714
VERSION     WP_010702714.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..302
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33344
     Region          7..290
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mstkikiqkl tlwsilvaci vfalkywvyq itgsvalysd alesivniia tlaawwavki
       61 slkpadqnhp fghhkaeyfs aiiegiliiv aaimilrkal fsfstielpq qpgiwiginl
      121 svciinylwg llliqqgkih hspalkadga hvmmdvltsf gilvglvtaf vsgwavldpi
      181 laiivaihif vqgwkvihns vqglmdigve lnetmqindl ilanacgaie ihdlrtrvag
      241 rvifiefhlv vptmmqvgea hqicnkieka lkvefenari tihiepenea kflpgtmtvp
      301 ft
//
LOCUS       WP_010702747             302 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Bartonella bovis].
ACCESSION   WP_010702747
VERSION     WP_010702747.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..302
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=33478
     Region          <184..302
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mntkclitas ifilaatslv qaadsivsqe nlkmdvlpiv rpptfswsgf yiggqvggfs
       61 skisamshde dipllpsksg rpkkwipvde kflpklsgfi ggfyagsnvd isnglilsid
      121 tdillsarkn tktivitppn vdespeengl eirgenrqer rfrrslqlde dtsdieegge
      181 niitfkytln qkwtgatrir igfaadrimp yiaggaaygq fqniislsst kindkelnnt
      241 sdetktmigy tfgagidfam tdniilraey rysdfgkqkf aqdsfelhyk tndfragisy
      301 kf
//
LOCUS       WP_010702744             230 aa            linear   BCT 01-JAN-2025
DEFINITION  glutathione S-transferase family protein [Bartonella bovis].
ACCESSION   WP_010702744
VERSION     WP_010702744.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..230
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26600
     Region          1..212
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltlfhhpls sasrfirlil eeydvathli eehewarkpe flalnpaghl pvflaehemp
       61 lsgaiviyey ldetrgslrp dkqffptnpl eraevrrlnd wflnklenev trhivreriy
      121 kremplaigg gapnsqilrs aranipphmn ylnwlctsrd wlagstlsya dlaaaasisi
      181 ldflgeidwe qffavrewym riksrpsfrp llndrvrgit psshyadldf
//
LOCUS       WP_010702958             263 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Bartonella bovis].
ACCESSION   WP_010702958
VERSION     WP_010702958.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..263
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28678
     Region          6..248
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(36,40,46,69..70,86..91,213..214)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(39,41,92..93,95..100,152..154,156,158..159,167..168,
                     171,174..175,178,182..188,196,200..203)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 marsaimnim vqaalkagrs lvrdygevqn lqvslkgpad yvsqadrkae kiifselika
       61 rpkfsflmee seeiigedsq hrfivdplng ttnflhgipf favsialerq gqivagviyn
      121 pildelftae rgcgaflndr rcrvaarrkl gecviatgtp hfggrnhghy lvelcnvmge
      181 vsgvrrfgaa sldlayvaag rtdgfwednl qiwdmaagii ivreaggfvs dkdgksamfg
      241 tkniiagnef ihaqlsqtlk kgv
//
LOCUS       WP_010703041             144 aa            linear   BCT 01-JAN-2025
DEFINITION  EVE domain-containing protein [Bartonella bovis].
ACCESSION   WP_010703041
VERSION     WP_010703041.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Bertonati,C., Punta,M., Fischer,M., Yachdav,G., Forouhar,F.,
            Zhou,W., Kuzin,A.P., Seetharaman,J., Abashidze,M., Ramelot,T.A.,
            Kennedy,M.A., Cort,J.R., Belachew,A., Hunt,J.F., Tong,L.,
            Montelione,G.T. and Rost,B.
  TITLE     Structural genomics reveals EVE as a new ASCH/PUA-related domain
  JOURNAL   Proteins 75 (3), 760-773 (2009)
   PUBMED   19191354
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..144
                     /product="EVE domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=16407
     Region          2..137
                     /region_name="EVE"
                     /note="Predicted RNA-binding protein, contains EVE domain
                     [General function prediction only]; COG2947"
                     /db_xref="CDD:442190"
ORIGIN      
        1 maywlfksep qkwswtmqkq kgahgeqwdg vrnyqarnnm ramkygdkgf fyhsnkglei
       61 vgivevcaqa hpdsttsdpr wecvdiralc dmpnpvslkq ikanpklknm alvktirlsv
      121 qpvtedewke vcsmgglkse mllt
//
LOCUS       WP_010703048             229 aa            linear   BCT 01-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Bartonella bovis].
ACCESSION   WP_010703048
VERSION     WP_010703048.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..229
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26170
     Region          87..208
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(117,120)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mipqifinwk nkktqclfts fiialslyat inhdhktplf phfislakaq etntnkikae
       61 kiiaikketk gffknirfad tsynigqfsf kdiqgkdhkl seftgkplli nlwaiwcapc
      121 rvempelaql krdmkeenfd viainidkva spekiqqflh evhadnltyy rdekmniftn
      181 irkqglalgl pitllvdqdg dliasfngia pwanddakaf iktiikktk
//
LOCUS       WP_010703163             110 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system PemK/MazF family toxin
            [Bartonella].
ACCESSION   WP_010703163
VERSION     WP_010703163.1
KEYWORDS    RefSeq.
SOURCE      Bartonella
  ORGANISM  Bartonella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Bartonella"
                     /db_xref="taxon:773"
     Protein         1..110
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=11700
     Region          1..109
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mnrgeiwlvs ldpssgyeqk gtrpvlivsp eafnrvtktp vvlpitsggs fartagfavs
       61 lmgmglhttg vircdqpral digarkgkkl etvpvmimne vlaklstflt
//
LOCUS       WP_010703211             242 aa            linear   BCT 01-JAN-2025
DEFINITION  M48 family metallopeptidase [Bartonella schoenbuchensis].
ACCESSION   WP_010703211
VERSION     WP_010703211.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..242
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27845
     Region          1..238
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 maiyeqdfil sdrvvplrvr ehkharrftl ridadgqgic ltippamnln avqsflekhr
       61 cwiethlthv lisressglk egatipllgv ahiikhkegr gvdeiiaggm eqkpqiiiys
      121 rleylprria dvlkkqakii itplveqyah kverkvksir ykdiksrwgs csvdgrlsfs
      181 wrlvmaprei veyvvaheva hliemnhrsq fwdlceklcp gsktyhawlk knghtlhain
      241 fh
//
LOCUS       WP_010703231             388 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA recombination protein RmuC [Bartonella schoenbuchensis].
ACCESSION   WP_010703231
VERSION     WP_010703231.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..388
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44104
     Region          60..388
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mfdsffslil lnerfyafiv lfllagfvim miirsnrkkt ieatthahem qmqmaallkt
       61 qaemqgrmqt maeifgqrqa elnqsireql ngmttnlgqt lqvqtkstye nltrlqerla
      121 vidaaqnniq sltgqiiqlq ailnnkqtrg ifgqgrmeai isdalpanty vfqavlsngk
      181 qpdclihmpn kapalvvdak fpleawnamr kassseerkr aerqfrtdmd vhirdiaqky
      241 lipgethdta flfvpsesif atiyedfesl vqkanrahvi ivspsllmls vqvvqtimkd
      301 akireqahlv qsevaklmed fgrmdmrvra lqkhfyktge dieailtsss kimrrasrie
      361 afelkendfv skpitahiqs qtlrlsde
//
LOCUS       WP_010703344             163 aa            linear   BCT 01-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Bartonella schoenbuchensis].
ACCESSION   WP_010703344
VERSION     WP_010703344.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Burnim,A.A., Dufault-Thompson,K. and Jiang,X.
  TITLE     The three-sided right-handed beta-helix is a versatile fold for
            glycan interactions
  JOURNAL   Glycobiology 34 (7) (2024)
   PUBMED   38767844
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12131601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..163
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=16891
     Region          2..148
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
ORIGIN      
        1 mgiyaaggev mldevnisgv emgvkvekgt lkilegtqih fmgeygvklg sgvksadlrg
       61 ttirgdgsgg tgiyvmgggt lemtldgvtv sgvqmgitmm sgaldvkert tidfekngwg
      121 iymrdgvtsa sltgtsnygk gkwvwdtcgg gdrddddvgw gnd
//
LOCUS       WP_010703400             241 aa            linear   BCT 01-JAN-2025
DEFINITION  RlmE family RNA methyltransferase [Bartonella schoenbuchensis].
ACCESSION   WP_010703400
VERSION     WP_010703400.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Hirata,A., Okada,K., Yoshii,K., Shiraishi,H., Saijo,S.,
            Yonezawa,K., Shimizu,N. and Hori,H.
  TITLE     Structure of tRNA methyltransferase complex of Trm7 and Trm734
            reveals a novel binding interface for tRNA recognition
  JOURNAL   Nucleic Acids Res 47 (20), 10942-10955 (2019)
   PUBMED   31586407
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Caldas,T., Binet,E., Bouloc,P., Costa,A., Desgres,J. and
            Richarme,G.
  TITLE     The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S
            ribosomal RNA methyltransferase
  JOURNAL   J Biol Chem 275 (22), 16414-16419 (2000)
   PUBMED   10748051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..241
                     /product="RlmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=26461
     Region          32..235
                     /region_name="RlmE"
                     /note="23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ
                     [Translation, ribosomal structure and biogenesis];
                     COG0293"
                     /db_xref="CDD:440062"
ORIGIN      
        1 mkktiktstg grggagshel yqrvkkkagt ikassrrwle rhlndpyvhq skvdgyrsra
       61 ayklieiner ykilkkgqki idlgaapggw cqvaarivgs ndqrpsvvgi dylhvdplpg
      121 vvmlemdffh enapqqlisa lgakpdvvls dmaapttghr qtdhlrtvyl cesaadfais
      181 vlkpgghfla ktfqggaena lltklkqnfk tihhvkppas raesvelylv alklkektkt
      241 q
//
LOCUS       WP_010703408             436 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S41 family peptidase [Bartonella].
ACCESSION   WP_010703408
VERSION     WP_010703408.1
KEYWORDS    RefSeq.
SOURCE      Bartonella
  ORGANISM  Bartonella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Bartonella"
                     /db_xref="taxon:773"
     Protein         1..436
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46946
     Region          39..370
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mirkvvflvv gvllsassmi vvqsvsanne nntykqlaif gdifervraq yvtvpddkkl
       61 venaingmls sldphssymd aekakdmrds tkgefgglgi evtmeknlik vvspiddtpa
      121 skagilagdv iskidgketn gqtlseavnk mrgavgtpit ltiirsgvde pleikivrdi
      181 ikvkavkyri endigylrli qfseqtfvnl kaaikdiqsk ipqdnlkgyv ldlrlnpggl
      241 ldqavnvsda flnkgeivst rgrkksdvmr fdakqgdiin gkplivling gsasaseiva
      301 galqdhrrat ilgtqsfgkg svqtiiplge ngalrlttal yytpsgtsiq gtgitpdiiv
      361 eqplpekykg ynvtlgesel kghikgkres dkgsgsaafv pkdpkddvql nqaykllrge
      421 ivnaafppdp nkgilk
//
LOCUS       WP_010703412             108 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF167 domain-containing protein [Bartonella schoenbuchensis].
ACCESSION   WP_010703412
VERSION     WP_010703412.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..108
                     /product="DUF167 domain-containing protein"
                     /calculated_mol_wt=12299
     Region          1..84
                     /region_name="YggU"
                     /note="Uncharacterized conserved protein YggU,
                     UPF0235/DUF167 family [Function unknown]; COG1872"
                     /db_xref="CDD:441476"
ORIGIN      
        1 mlyridssgl vlfvrlipka smdsivgves rdgetqhlvi rlrtvpedgk ankalikflg
       61 rqwkippsyi slksgmtsry kqlrfsgyve eleqklqlms nvhsqkye
//
LOCUS       WP_010703427             240 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerophosphodiester phosphodiesterase [Bartonella
            schoenbuchensis].
ACCESSION   WP_010703427
VERSION     WP_010703427.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..240
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26560
     Region          3..239
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mfkpkivahr gganlysent lsafrhaial gvdeiecdvh llksgevvvf hdfcleqlvg
       61 qkgyihdidn etrkqlcvkg stesppllee lldllvptnv alhleiktcg aiereyilsq
      121 kalglinsrn lakrvsaisf dstclrpfie agipsgpcid nfegdmsyqf skwkklgysd
      181 lsldgsivsr kfiesaldag ftvgvwting karlshwldm pvhyittdqp dlalqlrsqk
//
LOCUS       WP_010703433             290 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Bartonella schoenbuchensis].
ACCESSION   WP_010703433
VERSION     WP_010703433.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..290
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31036
     Region          3..260
                     /region_name="AztB"
                     /note="zinc ABC transporter permease AztB; NF040871"
                     /db_xref="CDD:468808"
ORIGIN      
        1 myefflapfi dfkfmqnali gstllaisac pigvfltlrg msligdamsh ailpgvaisf
       61 lfygfalipm aiggiiagii valatalisr ngfqkedasm avfylialag gviiislkgs
      121 tvdllhflfg svlsidteal wlittlmlit msslcifwra limesldplf fkslsplgky
      181 ihilllgltv fnlvggfhsl galmsvgimm ipaitarfwl srlgpicvls tilgiissaf
      241 glllsfhmsl psgptiilva gfiyilscfi sprgliaarf prlfytssss
//
LOCUS       WP_010703462             262 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Bartonella
            schoenbuchensis].
ACCESSION   WP_010703462
VERSION     WP_010703462.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..262
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28480
     Region          10..254
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mdsatnhsde tidefhrgkf ylvqprlqgh rsgmdamlla glvpdnfkgk vvdlgagaga
       61 aglavasrcl ethvtlvers afmisyaqkt lalkqnkela srvclleadi alkgnarlka
      121 glmdnvfdfa imnppfnnpm drktpdeqks eahvmpeamf dnwlrsaaai vkpggylgli
      181 arpqslndil halegrfgni cvipvhsrak taatrmlfya krgsraalsi lpalivhede
      241 ghafsprvda inngcislwe lf
//
LOCUS       WP_010703506             278 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Bartonella schoenbuchensis].
ACCESSION   WP_010703506
VERSION     WP_010703506.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..278
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=31204
     Region          139..273
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Site            order(163..164,166,190,193..194,197..198,202..203,227,
                     230..231,234..235,238)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          188..221
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          226..253
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlslilaaff lilltsaiff llhfdygskk grqvlimdeg ksqihriesg feydfidker
       61 iqevhlelps taisvethka fvqkpykhrk glsvlkafvv lfvpfvtcgi ysltgspgtk
      121 syffnelmdk dpqtlnrhek lvrlqtlffr tpndgkiada laisyfeegl fqdavniyld
      181 alrlngetap rlmgyglalv gyeggiitqe aqnafqkaad lapddfyprl fladalcqag
      241 kpeqavqllq nflgtmskdv sgrsrieemi vqlrntcn
//
LOCUS       WP_010703518             252 aa            linear   BCT 01-JAN-2025
DEFINITION  hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Bartonella
            schoenbuchensis].
ACCESSION   WP_010703518
VERSION     WP_010703518.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..252
                     /product="hydroxymethylpyrimidine/phosphomethylpyrimidine
                     kinase"
                     /EC_number="2.7.1.49"
                     /EC_number="2.7.4.7"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008902 - hydroxymethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008972 - phosphomethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=26993
     Region          7..246
                     /region_name="HMPP_kinase"
                     /note="4-amino-5-hydroxymethyl-2-methyl-pyrimidine
                     phosphate kinase (HMPP-kinase) catalyzes two consecutive
                     phosphorylation steps in the thiamine phosphate
                     biosynthesis pathway, leading to the synthesis of vitamin
                     B1. The first step is the phosphorylation of...; cd01169"
                     /db_xref="CDD:238574"
     Site            order(12,24,45,81,213)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238574"
     Site            order(13,15..16,18,22,25..26,29,32..37,39,42..46,51..52,
                     54,56..57,60,63,67..68)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238574"
     Site            order(106,143,177,210,212)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238574"
ORIGIN      
        1 malipsiliv agtdptggag ivrdietaay fqtkaslait cvnvqddnhv akivpmsgef
       61 vgaqmrvale anpiraikig migtqeiive icnvledysh ipvvfdpvli assggkltte
      121 ktteimlnkl lphielltpn meelallsqs plasnceeai qqakkllsfg pryilikggh
      181 ahgafatdil idktqainis aprlkkgmrg tgcilssait ahlafnksit tavkkskeyl
      241 ytlllnhsqk eh
//
LOCUS       WP_010703577             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bartonella schoenbuchensis].
ACCESSION   WP_010703577
VERSION     WP_010703577.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..429
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47295
     Region          18..418
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(30..31,34..35,38,77,135..136,138..140,143,163,
                     166..167,170,253,256..257,260..262,265,293,297,348..349,
                     353,357,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msisverqrv nqtnspiril laslvgttie yfdfyifata aalvfpylff ppqnnqlail
       61 qsflvfgvaf farplgsvif ghfgdkigrk atlvaalltm gistvvigil ptyetvgwwa
      121 pflltmcrlg qgiglggewg gavllatena ppekrgwyam fpqlgspagl llsiavyfgl
      181 wntldsdqlf twgwripfia saflvilglw vrtsigetle fkkaldheer vkvpvinvff
      241 khprivllgt fasmtafvlf ylvtayllsy sknhlqlpfn qtlqiemiga ivfglsialt
      301 gkfadrikrr tlmiwvtist giysfaipyf lhsgivgvla msiiglmllg itysplgtil
      361 aspfptairy tgvsltfnla givggsfapy iaeslvqhfd vtyvgyyllf safislicfi
      421 cftdkeisy
//
LOCUS       WP_010703620             245 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Bartonella
            schoenbuchensis].
ACCESSION   WP_010703620
VERSION     WP_010703620.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..245
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27791
     Region          24..242
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mwdfvpqhnn spllskqlke plfnvpfiii vliafcffgy iipqyflsdq lymrslilfs
       61 fipvffqaep lmfcytivsy sfmhgsfghi amnmvwllvf gsplakhfgn lrfllfwmlt
      121 agisaltyfi fhqdsmiplv gasgaisgmm gaiarygffi vfnsnihner flgpvlpikk
      181 alrsktvlvy igmwliincl tgifpylfgd sdiliaweah vgglisgfml isffdsprkk
      241 skinv
//
LOCUS       WP_010703665             467 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Bartonella schoenbuchensis].
ACCESSION   WP_010703665
VERSION     WP_010703665.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..467
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51809
     Region          7..433
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtpplnsfdd lglsekvika vrsagytapt piqsetiphv lqrkdvlgia qtgtgktasf
       61 vlpmltllek grararmprt lileptrela aqvqenfdky glnhrlnvvl liggvsfedq
      121 nrkleqgadv liatpgrlld hfergkllli gteilvidea drmldmgfip dierickltp
      181 ftrqtlffsa tmapeitklt eqflhspicv evtkasstat titqrlvksg skawdkravl
      241 relidnegde lknaiifcnr kkdiselfrs ltkynfsvga lhgdmdqhsr mntladfkdn
      301 kltllvasdv aargldipdv shvfnydvpt haedyihrig rtgrakrsgk aftivthddq
      361 kyisaiekis kekiewlngd lstlsisdqt ndsivktksa klskkstpkk htahtkkask
      421 edktshsktt knkvnspgls hsekdqnhtp lgfgadvpaf mliktrs
//
LOCUS       WP_010703733             358 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Bartonella
            schoenbuchensis].
ACCESSION   WP_010703733
VERSION     WP_010703733.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..358
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39271
     Region          4..358
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mntemfiqhf fnalalgsly gliaigytmv ygilrlinfa hgdifmlgay fvffstisfm
       61 pawvavllil lalliyysvf igfkkrpeiy wiailfilil gliyyskiap qnftpiwila
      121 icfsifitsa lgiavdqcay kplrnapris vlisaigisf fienlatvlf sgvpkgvkqp
      181 dflvtpiqwh lgqgsdaiir ispmsfivpv vsfilvvlll wiihrtklgl amraishdie
      241 tarlmgvsvn kiiaftfaig salgaiagim walrypqiqp ymgilpglka fiatviggig
      301 silgamlggl llgfleimii affpalsgyr dafafilliv illvmptglm gkksqeki
//
LOCUS       WP_010703735             191 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Bartonella schoenbuchensis].
ACCESSION   WP_010703735
VERSION     WP_010703735.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..191
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21086
     Region          28..92
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
     Region          118..182
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mtskdtlkny slsednfdvc geiteisgvi kwfdgskgyg fivpdlcglp dillhvtvmr
       61 rdgfqtaleg akiicvvkkt erglkcvqvk sidlssavhp seipvrthii vtpesglera
      121 ivkwfdrdkg fgflsrgqgt edifihmetl rrfglaelrs gqvvivrfgk gekglmtaei
      181 ypdialpfat h
//
LOCUS       WP_010703760             439 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Bartonella schoenbuchensis].
ACCESSION   WP_010703760
VERSION     WP_010703760.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..439
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=47788
     Region          <322..439
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mntkclists iitlftasva qaadimvpre srpvvsppqa skqisppvem sptpvisapt
       61 fswngfylgg qiggfsgktg islyakkgps trewtpvekd tlpqlsgfmg glyaganvdl
      121 gnslilgvdt divwsnkqdt kivakrkfee leleeieeve eieegpntes errklyehas
      181 mpqgesvnhs psqsphassv ssavehghss pervkrskrt vrssdsssss qsssqvesqt
      241 qqtqahtqaq tsqsssatqp tvqlhspqva hshtlqqvas qrgsegrplv sgyphssrpa
      301 lparhirete evdetaevtk vysstlkqkw sgatrvrigf avdrivpyia ggvayaqlqn
      361 ifsrsiemeg heisssslsd kkimvgytlg ggvdfamadn vilraeyrys dfgkqkfakd
      421 kleldyqtnd frvgvaykf
//
LOCUS       WP_010703786             821 aa            linear   BCT 01-JAN-2025
DEFINITION  penicillin-binding protein 1A [Bartonella schoenbuchensis].
ACCESSION   WP_010703786
VERSION     WP_010703786.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..821
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91061
     Region          2..789
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mmtffrylls sltalgfcgv ivwtamtssq adelpdyevl slyeppvmtr ihaadgrlma
       61 efatkhrlyl piesipnllk eafisaedkn fynhfgldpe glsralinni inigsgrrpe
      121 gastitqqva knfllnseat ferklkeail airiektysk dhilelylne iylgrgtygv
      181 aaasltyfnk svheltleec aylaalpkgp gnydpfkntq raierrnwvi drmvanryvt
      241 peqgkqakek plgvkirgsd syvfaaeyft eevrrhlmhh ygattlyegg lsvrttldph
      301 lqliarralq dglikfdhsr gwrgaykhid itddwgiala ditglsdvpe wnlavvlsss
      361 tdkieiglqp krensgllsk eraiaalsie qskwalnvig ennrrttaqn lsdvlhvgdv
      421 ifvekisntd nvyrlqqipk iegaivamep htgrilamvg gfsfsesefn ratqayrqsg
      481 safkpfvyaa aldngytpas vvldgpveil qgngqiwqpk nyggtfagps tlrygiehsr
      541 nlmtvrlahh mgmplvaeya erfgvadklp pylsmalgsg ettvlrmvta ysviangghs
      601 ikpsfidriq drygrtiyyh ddrlcencnv qswnnqsept lidereqvld pmtayqitsm
      661 megviqrgta arlrylnrhi agktgttnds kdvwfigftp dlvvgvfigy dqptslgrte
      721 tgsslgapif gefmqaalkd kpnvpfkipk gmilmkinrk tgmlataddn dvileafkpg
      781 tgpadvyqvi getnsfqegi ptvttspqvn kalqngsggl y
//
LOCUS       WP_010703805             403 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Bartonella schoenbuchensis].
ACCESSION   WP_010703805
VERSION     WP_010703805.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..403
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=44676
     Region          47..397
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mnkisdshnn pnlqsmkeki kesslqgryt syvpayaqvp lpnsmkkqvf fwlgtliffv
       61 ifmfvfgsvl lpfvagivla yflnpivqll ekigirrvfg tilitlfivv vfvaaltili
      121 pivswqiqqf vssglpiyvs riqnfltesn fdwvgryfgs dpnelqtdik vllgqssdfi
      181 tsllnsllrs gksivniisl lvvapvvafy mlldwqrmve avdswiprdh letvrsifye
      241 mdraiagfvr gqgtvclilg gyyaigltit glnfglligm fvglisfipy igtmsgfils
      301 ggvawvqfyp ddwsrivivm vvffigqfie gyilqpklvg ssvglhpvwl mfalfafgsl
      361 fgftgmlvav pasaaigvlv rfalhtylns qmysqsgnsg sve
//
LOCUS       WP_010703858             260 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP12 family chaperone protein [Bartonella schoenbuchensis].
ACCESSION   WP_010703858
VERSION     WP_010703858.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009246
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..260
                     /product="ATP12 family chaperone protein"
                     /GO_process="GO:0043461 - proton-transporting ATP synthase
                     complex assembly [Evidence IEA]"
                     /calculated_mol_wt=29290
     Region          27..250
                     /region_name="Atp12"
                     /note="Mitochondrial FoF1-type ATP synthase assembly
                     chaperone ATP12 [Posttranslational modification, protein
                     turnover, chaperones]; COG5387"
                     /db_xref="CDD:444150"
ORIGIN      
        1 mrkilddfnm pldddnpvyk vqklscqplp krfykevsia heeggfsill dgtpvktpar
       61 hcllmpteal aalvaqeftv qeesidpgkm pitrlvntvv dgiadnmqii fedllrfvac
      121 dmifyraqtp kelveqqceq wdflldwaee klgarfniaa gvmhieqpwe aiqavsnylr
      181 kiespyilaa lhamttltgs aliafavaek kinldnawdi ahldenwtkk qwgvdkeamm
      241 rraykksefn aaaaiitaca
//
LOCUS       WP_010703967             169 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase [Bartonella schoenbuchensis].
ACCESSION   WP_010703967
VERSION     WP_010703967.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..169
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18675
     Region          5..168
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(8,25,30,60,104,110,123)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(10,17,47..49,67,105..108)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mklpiyliaa vaqngvigce gtmpwrlstd lqrfkaltlg kpiimgrktw dslgrplpgr
       61 tnivitrnht ftaegaviah slsqacdiae eaatqngada vfiigggeif qqglmiahki
      121 flteifasie gdsffpifdk ekwtiietqy ipqgdkdnyp trfviyerq
//
LOCUS       WP_010703975             193 aa            linear   BCT 01-JAN-2025
DEFINITION  SCO family protein [Bartonella schoenbuchensis].
ACCESSION   WP_010703975
VERSION     WP_010703975.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11133300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..193
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21438
     Region          30..163
                     /region_name="SCO1-SenC"
                     /note="SCO1/SenC; pfam02630"
                     /db_xref="CDD:460630"
ORIGIN      
        1 mknviyifgl tiiflagvft ydawknkplg ddftlidsng qivteadirs kpsaiffgft
       61 mcpescpttl tdldrwltei gpnadklgiw fvtvdperdt pevlrdylsn ftnniigisg
      121 dpekvhkmvs sfnivaekvp gtngnytydh taaifllkkg gklagiipyn veenenqlkd
      181 diaikrlkkl isn
//
LOCUS       WP_010704038             408 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Bartonella
            schoenbuchensis].
ACCESSION   WP_010704038
VERSION     WP_010704038.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..408
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46376
     Region          118..387
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mteflaqypl leaiswliil tliailinil arkllihkak qlfsflpadt tndteytirh
       61 mantasafif sigvnfiptl pnplstiirn vsnafiifvi vliisallni vntlyeqrpt
      121 srlkpikgyi qiakialftv atvlilakli drsplilfsg lgamaavlil vfqdtllslv
      181 asiqisstdm vrvgdwieip nlgadgdvie ialhtvkvqn fdktitnvpi rklvtdpfkn
      241 wrgmqesggr rikrslfidq ssirfhreee qeylmqfnll enyfakklpe lnewnakldk
      301 nrdisantrr ltnigtfray vlsylqnhpn iannmtlmir qlsptpnglp leiycftntt
      361 iwieyeqiqa difdhlysil psfglklfqn psgydfvhaf etkqnrks
//
LOCUS       WP_010704085             294 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bartonella schoenbuchensis].
ACCESSION   WP_010704085
VERSION     WP_010704085.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..294
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32766
     Region          5..267
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mdkklleikd lrisfpttrg ilevvrgvsf svgkekigiv gesgsgkstt grailklnpr
       61 saiikaqkmc fndidllaas ehqmrsirgk rismilqdpk yslnplmrig kqimeayrih
      121 yrvskieawe rtisvlesvh irdperimrl fpheisggmg qrvmiammli pkpdliiade
      181 ptsaldvtvr cqvlaildel vtksgaglif ishdlnliad fcdrvlvmya grileelpar
      241 dlsrachpyt kallqslpql dkpvgvlsvp ernpdwlhgp tivngvegty hdql
//
LOCUS       WP_010704108             302 aa            linear   BCT 01-JAN-2025
DEFINITION  outer membrane protein [Bartonella schoenbuchensis].
ACCESSION   WP_010704108
VERSION     WP_010704108.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..302
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=33465
     Region          <178..302
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mntkcliats iftlaaislv qaadsivfke nykmgvspiv rpptfswngf yiggqvggfs
       61 skisamshdd dipllpnksg rpkkwvpvde kflpklsgfi ggfyagsnvd lsnglilsid
      121 tdiilsarkn tntivvtgps iddmpgennl ipnhensqyr lsrrdvqlre niidteeaek
      181 tiitfkytln qkwtgatrir igfaadrimp yiaggvaygq fqnilslsst athdkelnni
      241 sdetktmigy tfgagidfam tddiilraey rysdfgkkkf akdsfelhyk tndfragvsy
      301 kf
//
LOCUS       WP_010704142             318 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Bartonella schoenbuchensis].
ACCESSION   WP_010704142
VERSION     WP_010704142.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..318
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34695
     Region          1..318
                     /region_name="CeuB"
                     /note="ABC-type enterochelin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4606"
                     /db_xref="CDD:443656"
ORIGIN      
        1 mksywiaiiv ivllsvvsif vgysdvtpss lfsgdpnawl lfwqtriprt vavllagmal
       61 alsgmimqll trnrfvepst agtvesaslg ilfvmifvpn mpvlgkmvva ttfamagtll
      121 fmfllrqipl kstlivpltg imlgyvigsl tnaiadyeml lpslqaylfg sfsmvldgky
      181 ellwlslplc ilayftadrf tvaglgedlt nnlglnyrav mlwglfiial itavvictvg
      241 ripfvglivp nlvssykgdn mhrsapwvai sgagmvlicd llgriihpsf eipisvmmgv
      301 igsfifilll lhwrkrfg
//
LOCUS       WP_010704328             263 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Bartonella
            schoenbuchensis].
ACCESSION   WP_010704328
VERSION     WP_010704328.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..263
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28655
     Region          6..248
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(36,40,46,69..70,86..91,213..214)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(39,41,92..93,95..100,152..154,156,158..159,167..168,
                     171,174..175,177,182..188,196,200..203)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 marsaimnim vqaalkagrs lvrdygevqn lqvslkgpad yvsqadrkae kiifselika
       61 rpkfsflmee seeiigedsq hrfivdpldg ttnflhgipf favsialerq gqivagviyn
      121 pildelftae rgcgaflndr rcrvaarskl gecviatgmp hfggrnhgqy lvelrnvmse
      181 vsgvrrfgaa sldlayvaag rtdgfwednl qiwdmaagii ivreaggfvs dkdggsamfg
      241 ikniiagnef ihaqlsqtlk kgv
//
LOCUS       WP_010704398             257 aa            linear   BCT 01-JAN-2025
DEFINITION  SURF1 family protein [Bartonella schoenbuchensis].
ACCESSION   WP_010704398
VERSION     WP_010704398.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..257
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=28982
     Region          21..252
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mtkmkqspte shnknigffs illgilcisf fllfsalgiw qmqrlnwktn liasanqrih
       61 lppikappqd qwehvtfdkd eyrpvtltgk lltdknilit altqdatgyw vltplqtadn
      121 tltfvnrgfi pmdarhhfeq entpphphss tnteqttitg flrmsegegi fprknnpdqn
      181 lwytrqlpam aqklglsnva pyfidvtqki atqgnlpivg ltvvhfnnnh lsyaltwfil
      241 aagvlgasff llskynn
//
LOCUS       WP_010704422             284 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Bartonella
            schoenbuchensis].
ACCESSION   WP_010704422
VERSION     WP_010704422.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..284
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32021
     Region          11..276
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 miknvlyygc rilinavshy vrdngsafas hivlsgllaf fpfcifgasl asffwdfayt
       61 pqkiealmhl lpdaiaepfs keivnvlvtq rrglltlsfv gaayfasngv ealraalnka
      121 yrvvdqrslf fcrfqslffv iigtigisvi sfllvlapll ikitqnhfpf iveyigvirl
      181 wrytiavvvl fisllivhkw lpakrrklrd ilpgiivtlf lwfsasitfa hyltmfnyvs
      241 tyaglasimi aiiflymlsa ifilggeina aimfyrtrlq hsds
//
LOCUS       WP_010704454             265 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Bartonella schoenbuchensis].
ACCESSION   WP_010704454
VERSION     WP_010704454.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..265
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28545
     Region          4..259
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgetriiaia nqkggvgktt tainlatala aigenilimd idpqgnastg lgidrnsrpl
       61 ssydvlisgi svvdaalktv vpnlhivpst ldllgvemei assqdriqrl rkalcedqmv
      121 sqkfsyilid cppslnlltl namgaadsvl vpmqceflal eglsqlletv kqvryalnps
      181 leiqgivltm ydgrnnlsnq vvedvrsfmg ekvyrtvipr nvrvseapsf gkpallydlk
      241 cagsqaylrl ateviqrekq aktaa
//
LOCUS       WP_010704502             132 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bartonella vinsonii].
ACCESSION   WP_010704502
VERSION     WP_010704502.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10596854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..132
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14691
     Region          3..>40
                     /region_name="Mor"
                     /note="Mor transcription activator family; cl02360"
                     /db_xref="CDD:470549"
     Region          83..>127
                     /region_name="Csa3"
                     /note="CRISPR-associated protein Csa3, CARF domain
                     [Defense mechanisms]; COG3415"
                     /db_xref="CDD:442641"
ORIGIN      
        1 mqeevysdfp allreiadva gseaawnmmr afggrevyip grlenadwli eivgfaeaqq
       61 likhfcfnga gvrlliplgk daerrqkmie alqkgwsade aaavsgmhvr tayrlkkkis
      121 srepqgllfp el
//
LOCUS       WP_010704546             251 aa            linear   BCT 01-JAN-2025
DEFINITION  M48 family metallopeptidase [Bartonella vinsonii].
ACCESSION   WP_010704546
VERSION     WP_010704546.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..251
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28629
     Region          1..238
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 miiyeqlfif sgrvvplkvr thkyarrltl rfdangqgic vitppaislc svqafieknr
       61 swietrltrv cvsqkspylk egttipllgv ahtirhkegr gvteiiarna grepqiivyg
      121 qleylprrva dvlkkqaalv itplvayyae kverkvksvc ykdtksrwgs csidrrlsfs
      181 wrlimapkei veyvvaheva hliemnhgpk fwalceklcp gskthcawlk enghtlqain
      241 fhsyeldkle i
//
LOCUS       WP_010704579             288 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Bartonella vinsonii].
ACCESSION   WP_010704579
VERSION     WP_010704579.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..288
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31029
     Region          11..269
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 miswllepls yqymvnamwv sglvgcvcaf lsaflmlkgw sligdalshs ivpgvagayl
       61 lglpfslgaf fsgglaaaam lffnhrtklk edtiiglifs sffafglflk slkpmavnid
      121 tivlgnilav sssdivqlaf igffslfill lkwkdllvsl fdetharaig lnvkllkilf
      181 ftllaactva amqtvgaflv iclvvtpgat ayllsdrfvn vliiavligt ftsilgvyvs
      241 yflnaqtggv vvlfqaflfm mafifapkhg yiaarlrika akkgvmls
//
LOCUS       WP_010704643             436 aa            linear   BCT 01-JAN-2025
DEFINITION  S41 family peptidase [Bartonella vinsonii].
ACCESSION   WP_010704643
VERSION     WP_010704643.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..436
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46923
     Region          39..373
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mirkvillva gvflgacsmi mvqsvaanne gdvykdlaif gdifervrmq yvtvpddkkl
       61 ienaingmlt sldphssymn aqeakemrds tkgefgglgi evtmeknlik vvspmddtpa
      121 skagilagdl iskidgvqtn gltlneavsk mrgapgtpit ltiirsgvdk pleikvvrdi
      181 ikvkavkyrv eddigylrii qfseqtfgnl qaaikdvqsk ipqdklkgyv ldlrlnpggl
      241 ldqavsvssa flnkgeivst rgrkksdvtr fdakpgdiin gkplivling gsasaseiva
      301 galqdhrrat ilgtqsfgkg svqtiiplge ngalrlttal yytpsgtsiq gtgitpdiiv
      361 eqplpekykg ydvkigestl kghikgkren nkgsgsaafv pqdpkddvql hesykllrge
      421 mahaafppdp hkdilk
//
LOCUS       WP_010704822             261 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Bartonella vinsonii].
ACCESSION   WP_010704822
VERSION     WP_010704822.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..261
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=29326
     Region          15..253
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mlcfqeialn sgnilskfie rfltilyppi cpgckqrvsa ygticsvcwk dlqfitkpyc
       61 pvmgipfvcd mgdgflsgea lqkslpfsrv rsaivhkgva qtlvtrlkyg dhielapfma
      121 nwmvfagrei indcdviisv plhfrrflqr rynqsaelar yiavaqkknf kpgwlvrcrh
      181 trpqvrlsar erklnvlnaf evprkvkkyl kgcsillidd vfttgatvta aaatlkraga
      241 rqvdvltfsr vlkeasmfps s
//
LOCUS       WP_010704807             840 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK [Bartonella vinsonii].
ACCESSION   WP_010704807
VERSION     WP_010704807.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..840
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=93271
     Region          <337..838
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mhnskkksvs tssfsdenpq sasegnastk iveifpypev wkkafslgqn vrftrtpeve
       61 ilrrrietdp vfakqfkift kqeqknltni irthkktknl sltkrvinsq sienktsich
      121 savlkqlsrq avsrplekdt eenklqvesv eekikpvfhl sddaffeces fmleqvdaqi
      181 sgedlsiect nnestsdtps afdesitaly rvleyrfpqf ydsitaetpa gkirerkqis
      241 dlmyaknhpv kenqecyskl vfkdssdgls dgevsietkn tsniacstsk nitkkskdss
      301 vmrakgeslr ststllsnyn ssfrsdvqsf ddatyefppi nllqepvfhe gtvipqetle
      361 rgagllesvl edfgikgeii hvhpgpvvtm yefepaagvk ssrvinlsdd iarsmsaist
      421 rvavipgrnv igielpnavr etvylreliq tssfrenqfk lalalgkgin gepviaelak
      481 mphllvagtt gsgksvaint milsilyrmt pkqcrlimvd pkmlelsvyd giphlltpvv
      541 tdpqkavtal kwavremeer yrkmaklgvr nidgfnarva laaqkgetim ctvqsgfdke
      601 sgeilyneea mdltqlpyiv vivdemadlm mvagkeiena iqrlaqmara agihlimatq
      661 rpsvdvitgt ikanfptris fqvtskidsr tilgeqgaet llgqgdmlhm agggrivrvh
      721 gpfvsdeeve svvahlkmqg kpdylatvtd sedkntedel aasvsgvske erlnedgeel
      781 ymqavkivmr dkkcstsyiq rrlaigynka aslvelmeer gvvgaanhvg kreillneyt
//
LOCUS       WP_010704883             200 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Bartonella vinsonii].
ACCESSION   WP_010704883
VERSION     WP_010704883.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..200
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22963
     Region          4..191
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mtfelaalpy dydalspyms retleyhhdk hhlayltntn nfvkelglen esledivkks
       61 fgkniglfnn aaqyynhnhf whwmkkgggg qklpeklaka veadlggydr frtnfiaaat
      121 aqfgsgwawv avkdgkleim ktpngenplv hdaqpilgid vwehsyyidy rnarpkyiea
      181 fidhlinwdy vlklyedcgl
//
LOCUS       WP_010704954             467 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Bartonella vinsonii].
ACCESSION   WP_010704954
VERSION     WP_010704954.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..467
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52379
     Region          7..376
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mipslksfdd lglstkvika vksagytvpt piqsgtiphv lkrkdvlgia qtgtgktasf
       61 vlpmltllek grararmprt lileptrela aqveenfdky ginhrlnval liggvsfeqq
      121 drklergadv liatpgrlld hfergkllmm gveilvidea drmldmgfip dierickltp
      181 ftrqtlffsa tmapeisklt qqflhspvsv evtkasstat titqrlvksg nnswdkravl
      241 relihnegde lknaiifcnr kkdiselfrs lirhdfsvga lhgdmdqhar mntladfknn
      301 klkflvasdv aargldipav shvfnydvpt haedyihrig rtgranrsgk aftivtksdq
      361 kyisaieems nekiewfngd lstlttddqe ddiilkkksp kslkktsqke rvvqtkkflk
      421 ddevdylqta nhkakpseqy hprknkdssp lgfgddipaf mliktrh
//
LOCUS       WP_010705038             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bartonella vinsonii].
ACCESSION   WP_010705038
VERSION     WP_010705038.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..429
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47361
     Region          17..418
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(30..31,34..35,38,77,135..136,138..140,143,163,
                     166..167,170,253,256..257,260..262,265,293,297,348..349,
                     353,357,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msinseiqsi skknsprril fasligptie ffdfyvfata aalifphvff ptqndqlail
       61 qsflifgaaf farplgsivf ghfgdkigrk atliaalltm glstviigfl ptyetagwwa
      121 pffltlcrig qgmglggewg gavllatena ppekrgwyam fpqlgvpigl fssiivylgl
      181 lhfldhdell awgwripfig svvlmiiglw vrlsinetva fkktlerker vkvpilevfl
      241 kcprilflgt fsgmatfvlf ylvtayllsy stnylqltfy qaleveiiga ifcgiftvit
      301 gkladrirrr tlmiwitiit glysfaipyf lnsgiigvla msviglsimg miysplgavl
      361 aspyptairy tgssitfnls givgaslapy iaehlvqhfd tsyigyylll ssfislicfv
      421 gftddeisn
//
LOCUS       WP_010705067             162 aa            linear   BCT 01-JAN-2025
DEFINITION  CinA family protein [Bartonella vinsonii].
ACCESSION   WP_010705067
VERSION     WP_010705067.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..162
                     /product="CinA family protein"
                     /calculated_mol_wt=17084
     Region          10..160
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mtyfcekqtr evltacrhkg lllttvesct ggliaanlts iagssdvfdc gfvvysnesk
       61 trlvgvcakl iknygavske valamaeggl kyshagiavs vtgiagpgga ypdksvglvh
      121 favahknhkt lhtekhfgnl drnairyatv enalnmilka lq
//
LOCUS       WP_010705084             391 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu [Bartonella vinsonii].
ACCESSION   WP_010705084
VERSION     WP_010705084.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     gene            1..391
                     /gene="tuf"
     Protein         1..391
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=42707
     Region          1..391
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makskfertk phvnigtigh vdhgktslta aitkyfgefk aydqidaape erargitist
       61 ahveyeteqr hyahvdcpgh adyvknmitg aaqmdgailv vsaadgpmpq trehillarq
      121 vgvpaivvfl nkvdqvddae llelvelevr ellskydfpg ddipvvkgsa laaledkdks
      181 igedavrllm sevdnyiptp erpvdqpflm piedvfsisg rgtvvtgrve rgvikvgeei
      241 eiigirptsk ttvtgvemfr klldqgqagd nigallrgvd regiergqvl akpgsvtpht
      301 rfkaeayilt kdeggrhtpf ftnyrpqfyf rttdvtgivt lpegtemvmp gdnvamdvsl
      361 ivpiameekl rfaireggrt vgagivskii e
//
LOCUS       WP_010704414             144 aa            linear   BCT 01-JAN-2025
DEFINITION  EVE domain-containing protein [Bartonella schoenbuchensis].
ACCESSION   WP_010704414
VERSION     WP_010704414.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Bertonati,C., Punta,M., Fischer,M., Yachdav,G., Forouhar,F.,
            Zhou,W., Kuzin,A.P., Seetharaman,J., Abashidze,M., Ramelot,T.A.,
            Kennedy,M.A., Cort,J.R., Belachew,A., Hunt,J.F., Tong,L.,
            Montelione,G.T. and Rost,B.
  TITLE     Structural genomics reveals EVE as a new ASCH/PUA-related domain
  JOURNAL   Proteins 75 (3), 760-773 (2009)
   PUBMED   19191354
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..144
                     /product="EVE domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=16405
     Region          2..137
                     /region_name="EVE"
                     /note="Predicted RNA-binding protein, contains EVE domain
                     [General function prediction only]; COG2947"
                     /db_xref="CDD:442190"
ORIGIN      
        1 maywlfksep qkwswamqkq kgahgeqwdg vrnyqarnnm ramkygdkgf fyhsnkglei
       61 vgivevcaqa hpdsttsdpr wecvdiralc dmpnpvslkq ikanpklknm alvktmrlsv
      121 qpvtedewke vcsmgglkpe mllt
//
LOCUS       WP_010705142             197 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Bartonella vinsonii].
ACCESSION   WP_010705142
VERSION     WP_010705142.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..197
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=21257
     Region          27..196
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mylrffavlt clfcffslna iadvshtagd sdilvlslkn gdvvirlrpd laprhvvqik
       61 kltkggaynn vvfhrvipgf maqtgdvqfg kkgsadfdvk rvgtgasnyp nipaefskqp
      121 fkrgtvgmar aqdpnsansq fficfddasf lngqytvvge vikgmdvvdk ikkgtssnng
      181 svkdpdvint atlqadk
//
LOCUS       WP_010705145             475 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bartonella vinsonii].
ACCESSION   WP_010705145
VERSION     WP_010705145.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50524
     Region          18..413
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mnkqnwsall lgkngirflt ftggvvlhat niyvvitilp slmsdiggel cyswaatvfi
       61 tasllgtsla tkilekigpr kaylisgcif tvgtfmcaia stmplfligr fiqgfgsgsl
      121 lslsysmvri vlsppvwsya lstisgmwgi stllgpaigg isvhygiwra sfwvigvlai
      181 ifllialkvl pkenentvps splpllqlfi lifliiiisa ggainttitq igglviglsl
      241 lfvlakiess tlhrmlphks fsfsseffsi yalilvmttv vysielyfpl flqelhgqap
      301 liagyiaslm sfgwtcgsls sagvnakkih siivyspils llgisgllwl vpitdstsgh
      361 iviiclalfa igmsagiawp hlltrilqca nnedalrase sitsvqlfsa alsatlagti
      421 tnfsgllnpg givgmilaak tllavlisll fclgiplalr vsynifknpt gqsnn
//
LOCUS       WP_010705250             226 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bartonella vinsonii].
ACCESSION   WP_010705250
VERSION     WP_010705250.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24826
     Region          1..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtailelvei eqhffesqkp liildkanfi lnrgelvalv apsgagkstl lhiagllekp
       61 tagdvrlrgi scakrsdser tairrhdigf vyqfhhllpe ftalenvmip qmiagfkksv
      121 aedralkllt ylrishranh rpselsggeq qrvaiarava ngpsvllade ptgnldpvts
      181 ayvfqalsvl vrqsglsali athnyalakq mhrritlkdk kiiell
//
LOCUS       WP_010705366             348 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Bartonella vinsonii].
ACCESSION   WP_010705366
VERSION     WP_010705366.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..348
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=39891
     Region          9..345
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mqtdtlqitq ellaliteid efkgawralg tlaperlnal rhiatvesig sstriegskl
       61 tdreieqllv nleikhfksr deqevigyak vmetifqsws disitenhik qlhrdllcns
      121 ekdqrhrgey ktlrndvaaf nsqgkmvgiv fetatpfdtp hrmqelitwf nktnelkdlh
      181 plltigifnv tflaihpfqd gngrlsrilt tllllqkgyv yvpysslesi iennkesyyl
      241 alnqtqktiy tktpswepwi lfflralqkq krqleikies eknalfslse lalnildyvr
      301 nhgrvttrdm vrevgaspnt lkvtftslve kgllirhggg rstwysap
//
LOCUS       WP_010705407             169 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase [Bartonella vinsonii].
ACCESSION   WP_010705407
VERSION     WP_010705407.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..169
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18504
     Region          5..168
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(8,25,30,60,104,110,123)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(10,17,47..49,67,105..108)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mtvpicliaa vaengvigre gampwhlstd lqrfktltfg kpiimgrktw dslgkplpgr
       61 vnivitrnyd fiaegaitth slsqacavak reasqsgana vfiigggeif qqgfsiadki
      121 fltevlasik gdsffpvfdk ekwtivqtqy ipegdkdshp trfvvyerk
//
LOCUS       WP_010705415             778 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Bartonella vinsonii].
ACCESSION   WP_010705415
VERSION     WP_010705415.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..778
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=89044
     Region          42..695
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mnnfldhipf feedsslpsn ekssgtpiha rrvkektqcd adyleqlnpe qrqavmnteg
       61 pllvlagagt gktrvlttri shilhsglas pkqilavtft nkaaremkmr igafigeive
      121 gmpwlgtfhs tgakilrrha elvdlksnft ildsddvlrl lkqliqaegl ddkrwparsf
      181 ammidswknq glsperises dahsfgngmg rklyrsyqer lktlnacdfg dlllhsislf
      241 qhnpdilrey hskfryilvd eyqdtntaqy lwlrllaqqs kgqhvnlccv gdddqsiygw
      301 rgaqvdnilr fekdfppaki irlernyrst shilktashl isynqerlgk tlfshqinte
      361 eekvkihaaw dsgeearaig eeieraqqng hslnhmailv rasfqmrefe drfvtlglny
      421 rviggprfye rmeirdamay lrvvfqpadd laferiintp krglgdatlr tlyesarara
      481 iplfsaaaai ietdelkpka rsalrsiied frrwqnmlpy tphrelaeti ledsgytamw
      541 qedrspeapt rlenlkemir smeqfeslhs flehvalvid aennettdav nimtlhsakg
      601 lefetvflpg weeglfphqr sldeggrlgl eeerrlayvg ltrakkhlhi wfvsnrkvhg
      661 lwqpalpsrf ldelpaehie vvemgtsygg ygkspfkdhn sfyndyaplk qkriqknieg
      721 kvivqpvaet ssnfsindri fhikfgygri taiddhklti mfekagekrv ldnfvska
//
LOCUS       WP_010705434             473 aa            linear   BCT 01-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Bartonella vinsonii].
ACCESSION   WP_010705434
VERSION     WP_010705434.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..473
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=51515
     Region          4..469
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mialwdkqal vsaidgfvvg smpesfsgvs idsrtltegd iffcikghhl dghdfaaqay
       61 argagvlvva eshltdmeki sapllvvsdv lqaleqlaqa arkrsrakii aitgsvgktt
      121 tkealkqvfa tvgkvhanla slnnhwgvpl tlarmpmesd ygifeigmnh kdeirplvkl
      181 vyphvalith isaghmgyfk nleeiadaka eifegldeeg iailnadhdf fsylvqkakq
      241 wgvkkilsfg etgncdyqar dirlltdyss mrvhisgqdr likigapgrh ilqnslgvla
      301 vcdaigvdle rvlrslscfs lqkgrgiryr lslpsggefh lidesynanp asmraaldll
      361 asgpvgvggk riailgdmle lgtyseklhr dlvkpvslsg adlvflfgea mkflaidlsa
      421 yvkvhyaeni eqilplifae isngdllmik sshslyssdi vtalldrypr vsl
//
LOCUS       WP_010705450             245 aa            linear   BCT 01-JAN-2025
DEFINITION  SIMPL domain-containing protein [Bartonella vinsonii].
ACCESSION   WP_010705450
VERSION     WP_010705450.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..245
                     /product="SIMPL domain-containing protein"
                     /note="The SIMPL domain is named for its presence in mouse
                     protein SIMPL (signalling molecule that associates with
                     mouse pelle-like kinase). Bacterial member BP26, from
                     Brucella, was shown to assemble into a channel-like
                     structure, while YggE from E. coli has been associated
                     with resistance to oxidative stress.; The SIMPL domain is
                     named for its presence in mouse protein SIMPL (signalling
                     molecule that associates with mouse pelle-like kinase).
                     Bacterial member BP26, from Brucella, was shown to
                     assemble into a channel-like structure, while YggE from E.
                     coli has been associated with resistance to oxidative
                     stress."
                     /calculated_mol_wt=26366
     Region          16..245
                     /region_name="YggE"
                     /note="Uncharacterized conserved protein YggE, contains
                     kinase-interacting SIMPL domain [Function unknown];
                     COG2968"
                     /db_xref="CDD:442208"
ORIGIN      
        1 mtktifqpln hysikiamva laliasslsi haeaskikna titvtaiges qaapdmaiin
       61 lavvtedqta qkalaannks mndivtafkn ngiqandlqt sglsiyqssp ekphdkknhe
      121 klyhvsnslt vrirdlanag kifdqamalg vnsvngitft nadtkpfyqe arkkaiteai
      181 ekaetiaqaa nlklgkiiei nenndnyypk prlmsiaaha nyadtnfsgg elgynvsvtv
      241 vfaid
//
LOCUS       WP_010705462             400 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Bartonella
            vinsonii].
ACCESSION   WP_010705462
VERSION     WP_010705462.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..400
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=44048
     Region          1..400
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,207,236,238..239,247)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,200,245..247,276,279)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            239
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mafiadrlsy ikpsatiavs qkarnlkalg rdvialsage pdfdtpdnik naaieairrg
       61 etkytpisgi pelrqaiaak fkrennltyq peqiivgtgg kqilfnalma tlnkgdevii
      121 pspywvsype mvtlnggrpv faetktefsy klqpkeleaa itpktkwfif nspsnpsgaa
      181 ythdelkklt dvliehphiy iltddiyehl tyegftfvtp aevepklydr tltmngvska
      241 yamtgwrigy aggpqelika mdtiqgqqts gtssisqwaa vealtgpqdf itqnknifqa
      301 rrdlvvsmln qapgihcptp egafyvypsc aeligkktpe gkvishdedf vialleaesi
      361 avvhgsafgf gpafrisyat seklleeacl riqrfcnnll
//
LOCUS       WP_010705526             254 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Bartonella vinsonii].
ACCESSION   WP_010705526
VERSION     WP_010705526.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..254
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27804
     Region          1..244
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkiivavkrv vdynikihvk pdstgvdlsh vkmsmnpfde iaveeairqk esgkisevvl
       61 vsigpeaaqk tlrtglamga drgilvttek tleslaiaki lkaivheekp dmvflgkqai
      121 dddnnqtgqm laallgwgqa tfashfnien ghatvtrevd ngtqtirlpl pivmtadlrl
      181 neprytslpn imkakkkpie qkalsdlgie tqsrlttlsv eepkprqpgv kiahvaelvs
      241 vlkqtnciey tkik
//
LOCUS       WP_010705527             307 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Bartonella vinsonii].
ACCESSION   WP_010705527
VERSION     WP_010705527.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..307
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32352
     Region          3..307
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mailllaeqn teqtakalta ahainneidi lvcgknvqai aeshakltgv rqvliaeady
       61 lahqlaepta dtivklakdy dvimaastsi gknvmprvaa lldlmqisdi iavlapdtfk
      121 rpiyagnale tvrtndpqkv itvrtaaftp tashndnsap iqtitpapnp nlssfvkaet
      181 nksnrpdlts arviisggrg lgsqeqfmal llplanklea algasraavd agyapndwqi
      241 gqtgkivape lyiavgisga iqhlagimda qiivainkda eapimqiady alvgdlhhii
      301 pelekal
//
LOCUS       WP_010705545             130 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Bartonella vinsonii].
ACCESSION   WP_010705545
VERSION     WP_010705545.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..130
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14671
     Region          4..128
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 msskltrnqt lvlntlknaq gplsayaild hlreegfrap lqvyralekl vqlkcihrle
       61 svnafmaclh pencqheltt fiicencskv neiqnqtivs nlkqmvqavd fqarrstlei
      121 rgickkcate
//
LOCUS       WP_010705562             344 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Bartonella
            vinsonii].
ACCESSION   WP_010705562
VERSION     WP_010705562.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..344
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37814
     Region          7..342
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mekpslislk nvsrcyskaa gipaidnlsl nihageilgi igrsgagkst lirclnglek
       61 idsgsiffed invsnlsete wapyrqrigm ifqhfnllss qtildnialp lklaginkkq
      121 rhqralelie lvglcgkehc ypaelsggqk qrvgiarsla ahpkillsde atsaldpett
      181 qsilelladi nkrlnltivl ithemevvrt iahrvvvlnk grimeegrvk diftspqeet
      241 tiamlklvtp qlpekfaknl kamgqeavie iniageiaqq pflhlledai glrarilhgg
      301 idtvqgetig rlflaipnqn keasekavkw ltekarycev lgyv
//
LOCUS       WP_010705691             191 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Bartonella vinsonii].
ACCESSION   WP_010705691
VERSION     WP_010705691.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..191
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20878
     Region          28..92
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
     Region          118..182
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mtikdalkdc slsedsigac geiieisgvi kwfdgskgyg fivpdlphfs dillhvtvmr
       61 rdgfqtaleg akvicavekt erglkcvqvk sidcssaihp seiparthvv vtpesglera
      121 ivkwfnrdkg fgflsrgqgt edifihmetl rrfglaelrs gqvvlvrfgk gekglmtaei
      181 ypdigipfat h
//
LOCUS       WP_010705805             619 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Bartonella vinsonii].
ACCESSION   WP_010705805
VERSION     WP_010705805.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..619
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69863
     Region          8..492
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          540..600
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mvvpllrldr ifltfgttpl lnqaclsveq garialvgrn gcgkstllki aagirepngg
       61 eifrhprvtv cyvsqnpdcs gfenvhafle aglgntpdvq wvntlrtnlg fsgteklatl
      121 sggekrrvsl lralaakpei llldeptnhl dlptiewlea algalrsavv vishdrrfle
      181 nvtrstlwld rgvtkrlemr fsqfenwrdk mleeealeqh klerqivree qwlrygitar
      241 rkrnmrrlge lkelrqthqt ykgqpgsalf tavkshhsgq lvleakcisk sygdrtlvkd
      301 fslriqrgdr iglvgpngig kttllstlig keavdggtvk hgynlsmall dqqrilneee
      361 tlaqyltggr gdtllingqe rhvvsymkdf lflpeqartp lkefsggera rlmlarlfsr
      421 panflildep tndldietld llqefiadfa gtvllvshdr dfldrtvthm lapqgdghwv
      481 lyaggysdmi aqnkqavlvq rkdkelqrkv lsnlrargqe kqvsstnqgf ggrekatprk
      541 lsykqvyale klpeqiavlq deikkieqel sdpalycndk erferlsaal eekknacaqk
      601 eeewlelell rediecvks
//
LOCUS       WP_010705873             206 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Bartonella vinsonii].
ACCESSION   WP_010705873
VERSION     WP_010705873.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..206
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=23242
     Region          150..>201
                     /region_name="DnaJ"
                     /note="DnaJ-class molecular chaperone with C-terminal Zn
                     finger domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0484"
                     /db_xref="CDD:440252"
ORIGIN      
        1 mvttsklfds irissqkkgk aesqaqqcqw egcekagtyk apagrnhegq ylyfciehvr
       61 aynknfnyfs glsdkdiakf qkdaltghrp twptdfsngt skktaahyaq irsgtaayqn
      121 rmrdpfmlft qrhatrnssr klkpleakaf dtlglpanas senikakyke lvkkhhpdsn
      181 ggnrsseerf rdvlhaynll krsglc
//
LOCUS       WP_010705895             153 aa            linear   BCT 01-JAN-2025
DEFINITION  EVE domain-containing protein [Bartonella vinsonii].
ACCESSION   WP_010705895
VERSION     WP_010705895.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Bertonati,C., Punta,M., Fischer,M., Yachdav,G., Forouhar,F.,
            Zhou,W., Kuzin,A.P., Seetharaman,J., Abashidze,M., Ramelot,T.A.,
            Kennedy,M.A., Cort,J.R., Belachew,A., Hunt,J.F., Tong,L.,
            Montelione,G.T. and Rost,B.
  TITLE     Structural genomics reveals EVE as a new ASCH/PUA-related domain
  JOURNAL   Proteins 75 (3), 760-773 (2009)
   PUBMED   19191354
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..153
                     /product="EVE domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=17430
     Region          2..137
                     /region_name="EVE"
                     /note="Predicted RNA-binding protein, contains EVE domain
                     [General function prediction only]; COG2947"
                     /db_xref="CDD:442190"
ORIGIN      
        1 maywlfksep hkwswdmqkq kgavgeqwdg vrnyqarnnm ramkygdkgf fyhsnkglei
       61 vgiveicaea hpdstssdpr wecidiralc dmptpvslkq ikanpklknm vlvnasrlsv
      121 qpvsedewke iclmgnlket flvtpnsisq qhs
//
LOCUS       WP_010705901             221 aa            linear   BCT 01-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Bartonella vinsonii].
ACCESSION   WP_010705901
VERSION     WP_010705901.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..221
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25185
     Region          79..200
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(109,112)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mfpqifirkk rqrfllfsii fpsfiialsi yatithshkk vqaintdkar aeqmmaikka
       61 akgffthmrf adtlsdmkel sfkdiqgkdy klndftgkpm lvnlwaiwca pcrtempela
      121 qlkrelggen fdviainidk taspekiqkf lqdihadnll yyrdetmdif nnvrkqglal
      181 glpvtflidk ngyliasfng aapwadddak alirafikea l
//
LOCUS       WP_010705903             284 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Bartonella vinsonii].
ACCESSION   WP_010705903
VERSION     WP_010705903.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..284
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32165
     Region          10..278
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mlknifwysy rilvdavshy wrdngsvfas hialsgllaf fpffifgtsl asfigaftyt
       61 pqkikallql lpdvivepls teivnvltiq rrgvltisvi gaayfasngi ealrtalnka
      121 yrvverrsll fcrfqslffv ilgavglvvi sfllilapll lkimqnhsff mteyigvirl
      181 wryiiaavvl fvsllivhkw lpaerrkfie ilpgivvtml vwfmasiafa qyltmfdyis
      241 tyaglasvmv aiiflyilsa ififgaeina aimfyrkhlq hsed
//
LOCUS       WP_010705921             311 aa            linear   BCT 01-JAN-2025
DEFINITION  site-specific tyrosine recombinase XerD [Bartonella vinsonii].
ACCESSION   WP_010705921
VERSION     WP_010705921.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Spiers,A.J. and Sherratt,D.J.
  TITLE     C-terminal interactions between the XerC and XerD site-specific
            recombinases
  JOURNAL   Mol Microbiol 32 (5), 1031-1042 (1999)
   PUBMED   10361305
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Cornet,F., Hallet,B. and Sherratt,D.J.
  TITLE     Xer recombination in Escherichia coli. Site-specific DNA
            topoisomerase activity of the XerC and XerD recombinases
  JOURNAL   J Biol Chem 272 (35), 21927-21931 (1997)
   PUBMED   9268326
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..311
                     /product="site-specific tyrosine recombinase XerD"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007049 - cell cycle [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=34723
     Region          1..305
                     /region_name="xerD"
                     /note="tyrosine recombinase; PRK00283"
                     /db_xref="CDD:234713"
     Site            order(143,157..158,230,232,251,286)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271175"
     Site            order(157,251,254,277,286)
                     /site_type="active"
                     /db_xref="CDD:271175"
ORIGIN      
        1 mkngavidhf lemmsaerga sphtlaayqh dlqwaqdels shsaslfsaq kedligllsl
       61 mhtlgftass qarrlstlrq fyqflyaegl raddpsydid aprqgrplpk ivsedavtkl
      121 ldlaqleveq adygsknyfr alrlqllmem lyatglrise lvslpvqtvr gegysilvrg
      181 kgkkermvll skkayqvlsq wlnfrdqgkd aeslylfpah setgyiarqv varelkslar
      241 ragiksgfsp hvlrhafash llqngadlra vqhllghsdi attqiythvl eaglyrlvne
      301 hhpladkqka g
//
LOCUS       WP_010705934             412 aa            linear   BCT 01-JAN-2025
DEFINITION  saccharopine dehydrogenase family protein [Bartonella vinsonii].
ACCESSION   WP_010705934
VERSION     WP_010705934.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..412
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45909
     Region          <3..>49
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
     Region          29..403
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mkkniliiga ggvarvvahk caqnnnifgd ihiasrtlek ceaiiasike knamkeqgvl
       61 kghalnamnv eetikliqkt kceivinvgs aflnmsvlsa cietkcayid taihedplki
      121 cetppwygny ewprrqecek agitailgag fdpgvvnaya alarecyfdk itdidiidin
      181 agnhgrwfat nfdpeinfre ftgevwswqn kkwvsnkmfe vshewdlpvv gkqkaymtgh
      241 deihslsknl dvenirfwmg fsehyitvft vlknlgllse qpikiaegqe viplkvvkav
      301 lpdpaslapt ytgktcigdl ikgekdgkpr evfiyniadh kqafhetgaq gisytagvpa
      361 avaafliatg ewdvktmvnv eelpsrpflk sldhmglstw ireqqeekkl lf
//
LOCUS       WP_010706094             692 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thioredoxin domain-containing protein [Leptospira].
ACCESSION   WP_010706094
VERSION     WP_010706094.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442502
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..692
                     /product="thioredoxin domain-containing protein"
                     /calculated_mol_wt=79182
     Region          8..692
                     /region_name="YyaL"
                     /note="Uncharacterized conserved protein YyaL, SSP411
                     family, contains thoiredoxin and six-hairpin
                     glycosidase-like domains [General function prediction
                     only]; COG1331"
                     /db_xref="CDD:440942"
ORIGIN      
        1 mqfssrspnr lskekspylq qhaynpvdwf pwgeealtka reqdklifls igyatchwch
       61 vmekesfenq mvadylnshf vsikvdreer pdidriymda lhamdqqggw plnifltpdg
      121 kpitggtyfp pepgygrksf levlnilrkv wsekrqeliv asselsrylk dsgegraiek
      181 qeegslpskd cfnfgfslye syydaefggf ktnhvnkfpp smglsfllry hhssgnpkal
      241 emventllam krggiydqvg gglcrystdh rwmvphfekm lydnslflet lvecsqvskk
      301 isaesfaldv isylhrdmri vgggicsaed adsegeeglf yiwdfeefre vcgedsrile
      361 kfwnvtnkgn fegknilhes yggeatklse eewkridsvl erarakller rskrvrplrd
      421 dkiltswngl yikalakagi afrredflkl aeetysfier nlidpdgril rrfrdgesgi
      481 lgysndyaem isssivlfea gcgirylkna vlwmeeairl frspagvffd tgndgevllr
      541 rsvdgydgve psansslays lvklsllgid svryrkfael ifsyftkels thslsyphll
      601 saywtyryhs keivlirkda nsgkdllaai qtrflpdsvf avvnenelee arklsalfds
      661 rdsggnalvy vcenfscklp vsnladlqkw ie
//
LOCUS       WP_010706107             269 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus faecium].
ACCESSION   WP_010706107
VERSION     WP_010706107.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..269
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29781
     Region          4..265
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,196,218..220,222..223)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 miklvaidld gtllneqkli sdenkqalaq akqqgvkivl ctgrplaama hylqelglvd
       61 egdysitfng glvqkndtge iiekkvmevs diqrlyklaq qldlpldvls dnvvlqlpsa
      121 prkqslynvl nkllqfqpad isditdefvl nkaviaydqe eldpkikeip aefhemyeii
      181 ktrsmllefm pkgvtkaygi sllakdlglk qeeimaigde endlpmiqya glgvamenav
      241 pfvkeaadfv tasneengva kviqkfvle
//
LOCUS       WP_010706325             430 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus faecium].
ACCESSION   WP_010706325
VERSION     WP_010706325.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..430
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=45654
     Region          8..423
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mkdniaaklt sfmgkfseit svkamtqgmm atmpltlgtf viailsslpi dswqgwlsss
       61 gvladmqava ggtteilaif lvlsisykya slrgknslsa avmslgfyfv lvpqkievat
      121 dnilnafqkd ylgssgvfva iivalviskl ycgltekgli lklpdsvphy vsesfstvfv
      181 aiiiftsafv vrmlfgftsy gnifdfiqal itapimgigs stvaiiglsc ianlvwffgi
      241 hpatvqtvam piyavsiagn ieafqagnpl pyitfavltf gfltiggqgg tlglainlal
      301 fskseryktl gklaivptif ninepiifgl piilnviyfi pmvlssvvag iigvigiklg
      361 afasmnplim lpnvipvpis ifvstglvaa ltvvvaiaal tllyypffri gdkralaeek
      421 vaeseakine
//
LOCUS       WP_010706342             117 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Enterococcus faecium].
ACCESSION   WP_010706342
VERSION     WP_010706342.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..117
                     /product="VOC family protein"
                     /calculated_mol_wt=13001
     Region          3..117
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(3..6,22,60..61,64,82..87,89,93)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mdiylnfkne sreaiafyek vfqteasgit tygempgieq mnlpeeaknl itnarlniyd
       61 tlvmfadtpe gigpelvvgn nvslviqtrn eeetkrlfes laeggkiemp ldavpwa
//
LOCUS       WP_010706408             429 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 125 protein [Enterococcus faecium].
ACCESSION   WP_010706408
VERSION     WP_010706408.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..429
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49168
     Region          6..426
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 maykdipksv qkfmeditqk cgdihadwak nftaafantl lttvkkqndg ttflltgdip
       61 amwlrdstaq vrpylviake deeladmisg lvkkqffyin idpyanafne eangaghqtd
      121 htkmndwiwe rkyeidslcy piqlayllyk ntgktdqfnq sfiegikkil dvfkteqdhe
      181 hspytfvrdt trkedtlind grgaktaftg mtwsgfrpsd dacrygylvp snmfavvvlg
      241 yveeifqtil ddkeivqqtq klkkeiqegi qnhgrtvnqk gqtiyayevd gmgnatvmdd
      301 snvpnliaap ylgycseqee dylqtrrtll skenpyfyeg kyakgigssh tpekyvwpia
      361 lamegmttsd ksekerilnl lvatdagthl mhegfdvnnp enytrewfsw anmmfcelvm
      421 dyfdtrvek
//
LOCUS       WP_010706572             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Enterococcus].
ACCESSION   WP_010706572
VERSION     WP_010706572.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15659
     Region          4..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msvyqhilva ldgsdqseka fheavriake eqatlylati indaefttsp fsfeelydle
       61 khkseemltg kakqaseigv ktvkkivelg spkrylanti senyaidliv lgatgrgaiq
      121 rtligsttdy vvnhalcnvl vvr
//
LOCUS       WP_010706541             280 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Enterococcus].
ACCESSION   WP_010706541
VERSION     WP_010706541.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..280
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31303
     Region          6..>216
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mskngkvisi inmkggvgkt alsvgissfl sekkdekvll idsdpqfnat qafidpedyl
       61 ksektifklf kpqtelhqsf vmpkreelvt kinknldilm gdlnlvlvnk ssdsglikrl
      121 krfitknnlr nyydyiiidc pptltlytds alvssdyyli pnridrysni gisslnraig
      181 dlidqedlel kclgliytmv qnhlsdkqke vkaelesnka meniyvfkss tslvndmqvg
      241 kqgpiatrya ksnkdisdvv delqallskn sskegvtvdg
//
LOCUS       WP_010706601             154 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ImmA/IrrE family metallo-endopeptidase
            [Enterococcus].
ACCESSION   WP_010706601
VERSION     WP_010706601.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..154
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=17684
     Region          35..122
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mvtseelmar fsdltykfep nmpekqkgly innvvylnpq qhpreltstv aeeighhlts
       61 vgdiinqdtn ekrkqeqkar digatmvvtp qdlidcyher ftyvwecadf lgitkqaler
      121 alsayskqfp eglvygdykl ffkpngtlgi vkwf
//
LOCUS       WP_010706720             356 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Enterococcus faecalis].
ACCESSION   WP_010706720
VERSION     WP_010706720.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..356
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39219
     Region          1..324
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mnnlfifvcf cfmwlmifgv ilyyvglvnh ryihhtlilg lvtiisgtlc wlfvgyslsf
       61 fgniqysify splasseivs iliqllfcly svimiigsvl ergnwkyivl fvplwivfvy
      121 apicfslwgh gnwlgkmgvl dysgglvvht tagigslvla itspirlkns lifksqemia
      181 fvgmlfitlg wfgfnmapsg kigeeaiqvw lntlisilgg siswtftqwi likkvsiysv
      241 mngiigglvg stcsvgyvsp afsllisviv ctlcpivihi mhlsianfdd aadsfgmnav
      301 ggiagsiltg vmaekgdffl qlfgtflisi wslslsllih yllkkivndc ysqcik
//
LOCUS       WP_010706780             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010706780
VERSION     WP_010706780.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..243
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27488
     Region          7..239
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mdklesnkka plyqqlydai lnkvrsgeyq vgekipseeq lmtiygvsrv tvrnaikqlv
       61 denilikrhg kgtfvsmpsy vesmtaggsf tesglkmnrk pttkiisicl kkatghvaev
      121 lgvekatevi vierlrsldn mpaifeidyf rkedqfmldl eltdtslldi lrqyrgvias
      181 yfdniieial adeklaeala iseeealvki nqtvvdndnq ilyfneqyil sesykvairs
      241 ynk
//
LOCUS       WP_010706951             520 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010706951
VERSION     WP_010706951.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..520
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59645
     Region          7..139
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          244..516
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msvrvndllk lpslreatvl sgknqldtsv aslsflevsd mslfseklhk tneyhageil
       61 igsfcairhd vvkqcetirh lhelgevgli lyyvgiivpk vaeeviqlad slgfiliqmp
      121 kndptlryne viyevmkllv nknkmasfat dllekvsllp eqnrsvemtl kilsdflkvn
      181 ialttytnei istinwprst klpltkllyq sqekvalget tyfitsqklp qkdgqtlkly
      241 fireeeqlts femnqavevv qmalnlwgkn ydevseyalv qaiindesdk myqlakklmi
      301 dissvetmwl lpiwqqgqei haiqqdlkdf lryyyqttiv qqtenylivl lgnylhkqpe
      361 asiskeylqa tdyqdylgei ilcpkvrntt evrvsyqtan qvapflkrvy pqrkvlsiae
      421 irtvqqmmtc lqageeaiqq rlaviqpllk eseqlmtlgt flldassdfk ecgerlfvhk
      481 ntvkyriski nealgydmtn aaeayevyla milyrlvtne
//
LOCUS       WP_010707073             402 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010707073
VERSION     WP_010707073.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..402
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43835
     Region          6..402
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkrsiiwkta frsilknkrr slltmlgivi giasvitiva igngfkedmv dklsaekqke
       61 nvkkisfsay ntsdmfsdqa mftdndlgvv rmvpgvekid fdqrevdgaq kgtlnfqagp
      121 knlsvtyela dkttkellag rqlndgdngk ldktvvvdel vakelyqdpt aavnrtfpyk
      181 eqlftivgvt tntsgaigpg nddsllyfpk ktyehyfgkl kdtstlkltv apgyqpdqvl
      241 ketiktlsqq gtmknsgtyq eynvkdtike mgsllnnltl fisaiaaisl viagvgvmnm
      301 myisvserik eigirralgg tasdikkqfl tegialtlig gitgyllgmi iaylasmalp
      361 fsvrpdlmtv slaigisvfi gvvfsyfpas aaskkdlidi mk
//
LOCUS       WP_010707199             374 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Enterococcus faecalis].
ACCESSION   WP_010707199
VERSION     WP_010707199.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..374
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=41991
     Region          58..301
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 msrkrkisli slviilffvt vgsayfavag sylkktidkg yvpikndyte aqnkdsqsfl
       61 vmgldntier klgttrtdam mvitvnnktk kitylslprd sfvqidakny qgmqrieaay
      121 tydgptasvn tvekllnipi nhyvvfnfls fiklidavgg idvnvkqafd gvtkdgpgsi
      181 hfdagkqhld gtkalsyare rhsdndimrg frqqeiiqav edklksgqsi mkimdiidsl
      241 ngniqtdvds nelthlvkeg ltwtnydkqq lsfgwrtfsn egrsmvelyp dsienvrhql
      301 rvslnlekpd erdqdgyvfh tngeflyqsd ytvqdeaaee nemtsingnt yigvpgntqt
      361 gplpsvkten gfik
//
LOCUS       WP_010707103              67 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Enterococcus faecalis].
ACCESSION   WP_010707103
VERSION     WP_010707103.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..67
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7356
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mktgtvksfn hkrgygfiia edgseifvhq tgicmpgfrk liegqtveye taehegrtka
       61 vnvtvie
//
LOCUS       WP_010707244             335 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: XdhC family protein [Enterococcus].
ACCESSION   WP_010707244
VERSION     WP_010707244.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..335
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37194
     Region          2..335
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 mrevfqrlkq ailekqdtml ltigtssgst prsqgarmlv saegriagtv gggavefqae
       61 qvakklliek enaqrqfila pnniadlgmv cggnvtiffh ylswetpflk elcesiethf
      121 qnnqqgwlmt eldqnnlgkv sfysetgeli gstswegels llpkgihcvq keettfltea
      181 ilqvgkvyif gsghvaralv pilnylsfyc vvvddrpefl taqafpqaee lrviplenla
      241 afieitaddy givitrghnf dfivakqlle tpakyigvmg skhkiasqvr rlkevgytmn
      301 eierifmpig ldiaaetpee laisiageli qqryq
//
LOCUS       WP_010707351             472 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cytochrome ubiquinol oxidase subunit I
            [Enterococcus].
ACCESSION   WP_010707351
VERSION     WP_010707351.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..472
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53161
     Region          2..457
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mfdivtlari qfamttvfhf ffvpfsigla lvvaimetmy vvkkeeryrk makfwgnifl
       61 lsfavgvvtg iiqefqfgmn wsdysrfvgd ifgaplavea llafflestf lglwiftwdk
      121 mnpkvhvtfi wlvvfgsmms afwilvansf mqhpvgyvin ngraemvdfv avisnpkvwy
      181 efshvimgaf tlggmavagm aafqllkkrd isfhkasmri glwvtlfgsi gvllagdlqm
      241 kaliegqpmk faamegayed sddpaawtli awaderehkq vfgidipyml silsynklsg
      301 svdgmdtvnk rlvekygddk nyyppvntlf wsfrimagfg almllvaalg lfftrkkkps
      361 lyekkwmlwv valctfapfl anttgwlvte lgrypwtvyg lftieqsvsp nvsvaslits
      421 nviyfllfag lgsvmvylvi lelrkgpdye akklakenep aldpfdkgvf ge
//
LOCUS       WP_010707355             442 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus faecalis].
ACCESSION   WP_010707355
VERSION     WP_010707355.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..442
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47215
     Region          1..437
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mekkqlkrei tmfgalstvm gtvigagvff kaasvvghaq saslaifawv lggalticag
       61 ltsaelatai petggavkyi eytygklagf llgwaqsiiy ypanisalsi ifstqlinlf
      121 hlsanllipi ailagtsiti inllgtkias lvqsttlvvk lipialislv glftpgqvav
      181 slfpiettan tgflvafsga lvatmfaydg wlgvgnvage mkrperdlpk aiifglllit
      241 liyalinfvf lktlpieqia gnlnaasdas vaifgpiggk ivtigilisv ygalngytmt
      301 giripyalal dnlmpfsrqf qklskrfvvp yvagifqlav aiimmffgtf dlltdmlvfv
      361 mwlfnllifl avfilrkrep elkrpykvpg ypiipiiasl ggifilvtts itqpilalig
      421 igitllgipv ylvnkqktkp kt
//
LOCUS       WP_010707380             108 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Enterococcus faecalis].
ACCESSION   WP_010707380
VERSION     WP_010707380.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..108
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=12338
     Region          13..>61
                     /region_name="T4P_ComGE"
                     /note="competence type IV pilus minor pilin ComGE;
                     NF041013"
                     /db_xref="CDD:468942"
ORIGIN      
        1 manirrklti ysgfillesl vsfsivcvva gifsltitql iqqnyqreqe ltrtrlgyea
       61 ilfleqtgdl rfkeriyqgg tyrfslmeke grrvlkvtds rgailigq
//
LOCUS       WP_010707386             425 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A [Enterococcus
            faecalis].
ACCESSION   WP_010707386
VERSION     WP_010707386.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..425
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=46990
     Region          1..425
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mqqplayrmr prhldevvgq qhlvgpgkii rrmveakmls smilygppgt gktsiasaia
       61 gstnyafrml naatdtkkdl qivaeeskms gtvillldei hrldktkqdf llphlengri
      121 imigattenp yitinpairs rtqifevkpl tetdiqqaiq ealtdstrgl gdypvhleek
      181 alqhltratn gdlrsalngl elavkstpkn eqgeikitlp iieecvqrka lthdkdgdah
      241 ydvisafqks irgsdvdaal hylgrlveag dlpiicrrlm viayediglg npaaaartvt
      301 avqaaeklgf peariplasv vidlclspks nsavtaidaa ladirqgsvg dvpdhlrdah
      361 yagakelnrg igyqyphnfe ngwvdqqylp dklkearyye pidigkyeqa lhqqlkriqe
      421 wkqkk
//
LOCUS       WP_010707404             319 aa            linear   BCT 01-JAN-2025
DEFINITION  aromatic acid exporter family protein [Enterococcus faecalis].
ACCESSION   WP_010707404
VERSION     WP_010707404.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10532842
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..319
                     /product="aromatic acid exporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36164
     Region          1..141
                     /region_name="ArAE_1"
                     /note="Aromatic acid exporter family member 1; pfam06081"
                     /db_xref="CDD:428756"
     Region          147..307
                     /region_name="ArAE_1_C"
                     /note="Putative aromatic acid exporter C-terminal domain;
                     pfam11728"
                     /db_xref="CDD:432028"
ORIGIN      
        1 mkiglrtvkt aisaalamii aeklgllyap sagiisvlsv tstkktsvmt giyrllslal
       61 atilayicft flgftaiafg iflllfipaa vyfqlsdgiv vssvlvthyl veknlswaii
      121 gnefllmsig vglallansy mpdtekrlre dqevietmfr kilremalhl nnatgernlv
      181 mhcadlktfi rtgetwaknh aenqllstnt yyleyfamrk mqsnilknml elleditvda
      241 qqvryiqqll eytaetfaen ndgqeimnri ktvyetyrtk plpqtrsefe nrarlfqflq
      301 lfqsfiqvka dfaklqldk
//
LOCUS       WP_010707450             120 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Enterococcus
            faecalis].
ACCESSION   WP_010707450
VERSION     WP_010707450.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..120
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=13583
     Region          4..111
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mvkvphqgni lllnktprse heqtgkrpyi vlshdiiany snvvivapis stkrnyplyv
       61 sinpsygmkt sgkvlldqlt tidyearqcv fletahekli delllkvrtv fqkvnktdkf
//
LOCUS       WP_010707710            1196 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Enterococcus faecalis].
ACCESSION   WP_010707710
VERSION     WP_010707710.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..1196
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=138906
     Region          4..1173
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 msvqfirgta vadleapliq atkqwleeda qhevfylvpn hikfeqeiqv lqklrqlqtt
       61 tsdsitstrl qvfsfyrlaw yylqhtpfys advlsdagaa mifrkilvea eeelqifrge
      121 inkpgfiqql fqlyqemreg nieiaelypf lekqtenpkg qdlqlkfqdl tliftrfqlq
      181 msqygyesae iiqhlseylq tvdlsnvqfv isgyqqftar elklievlma qagsvkvall
      241 ldkqyphdlp dprslfyeag qtyhqlyqla rqkqipilsd yvekkevlit npalqelndy
      301 wiqsqehlpp lsttdwsgdg lflwraenvk eelthvatei rrlvveegyr ykeiqvltrd
      361 ldcyenllep ifaeheipvy vdrdmamdrh plvewieslf aihsynyryr dvlrflrtel
      421 fmpmnqlats eesltdwlnq rnawrrkvdi tenvvlaygy egyywsqekd wefirydfea
      481 eeqedvttme eesnairqsl qrllpsyfqa misaktglea atvfyhfllq sgvatqlkmw
      541 rlqaieagql etarnheqtw dalmslldey vtvygessfd fttfqeifvs gleglhyskv
      601 ptaidqvqvr amdltrpgaa kvtfaigmte eifpqkienk tllsdeerqt indtltenqy
      661 lrgttgrkia qepyvaylvf ssarerlylt ypsvkdtaqe vkpspyfkni qkdlnlpvfe
      721 knettifdde ttslahisty rtligeltrl krqrketqeg llpfwlnmek almnqsiapl
      781 akqvfeslth qnipekidev laeplygkdi ytsvsrmesf yrcqyqyfsr yglrlkerdv
      841 fglspaatge ffhealdqff kllimnqrnl seltdqevnl laeevlnsil gdarfsvltt
      901 ssrmnyiryq lsqtikkvsw alkrqsqrsg mttvqtevlf gqiaakkgis glelplknqg
      961 kihvrgkidr idqlvtpest ylgvidykss hrkfnmteay yglamqmlty ldvalmdavq
     1021 lvgqeakpag slylhvhnpt lsyegkddie qqmlkkyqfd gllmkdpdll dhldtslqak
     1081 qssllfpiee sakeqikpgr rqedkfvtep elgallshnr nkfieagnqi iggevqlnpa
     1141 yqgkeriacr ycpfrsvcdf dvmlkennyh rienlskeei marllnkdee gatede
//
LOCUS       WP_010707786             492 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010707786
VERSION     WP_010707786.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..492
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=58592
     Region          79..156
                     /region_name="Mga"
                     /note="Mga helix-turn-helix domain; pfam05043"
                     /db_xref="CDD:428276"
ORIGIN      
        1 mlkrdflekp ydymndillf lynnkgqatr nelvdffnis lptlneylsf leqflkeeql
       61 qenltltvlg dtlylnkapt fsmkamimlf ldksikfhmv qqlfhknein ggyfqqnyai
      121 ssatyyrkiv elndllnefn lrikrgklvg eekqirffff nffwfifeek tdlekelanq
      181 ylglieilqe ipritfdhte ilqiklwmki sfrrmvlepl ptisphdvql drplfekinl
      241 sihtymkrid rpytineaym fydffcsmhn ysanaafafr lakqqriekt ylnemnrvil
      301 tylkargyls hyvlpirlly ienllfqlha qlyyfsgfil pfdywtiqsl lkvlrhpfse
      361 sevyelveia ttnfatkata skyqnqftei nytlilnhia elnekkitig vyhslssays
      421 elvaqkiqqs iagkyplkie pynaenhydl llmntnneql vaqydhyyif sdisnrydlq
      481 siekiiqlll gk
//
LOCUS       WP_010707824             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010707824
VERSION     WP_010707824.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..245
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27292
     Region          3..243
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msltiehltg gyghipvlkd infdvksgem vgliglngag ksttikniig lltpqkgkim
       61 idgetlqqap eeyrkkigyi petpslyeel tlkehievta laydipleea fkraepllkt
      121 frldnklewf panfskgmkq kvmvlcafli epslyiidep flgldplaih allelmdtmr
      181 kqgaailmst hilataekyc drfvvlhegk lwangtmael raefnlpess lddiylaltk
      241 eekvg
//
LOCUS       WP_010707837            1014 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Enterococcus faecalis].
ACCESSION   WP_010707837
VERSION     WP_010707837.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1014)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1014)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1014)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1014)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..1014
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=117947
     Region          1..1014
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mvenkeirfe qdietsltty gkwkketfne snfdpiigld cqkllgfvqk tqpkqwvrhq
       61 rnynndgevk flqrfnqeve thgmlhvlrn gikdrgvrfk vayfkpasel ndermekyea
      121 nsftctrqfa yspnnhktid mvlslngipl valelknqyt gqtvenaklq fqkdhdpkel
      181 vfrfnrrflv yfavdhtdvy mttkldgkkt yflpfnqgsn gpgrvggagn psnkdgypta
      241 ylwekvltrd nlmdiiqrfm nleikkekqg drevtkktli fpryhqldvv rklvadvksh
      301 gsgenyliqh sagsgksnsi awlayhlasi hdqlnypifs siiivtdrtv ldrqlqntim
      361 nfdhqtglve tiddrkssqd lkeaindgrk iiittlqkfp viyqevdqve grnfavivde
      421 ahssqtgnsa qklkaalsdk sksleeyyel egevddvlpd aedelvqqla aqgkhqnlsf
      481 faftatpkek tlemfgtkqp dwhfepfhvy smrqaieegf ildvlknymt ystsykiare
      541 iednpelpks eatraivrfq slhpwavaqk tavmveqfra vtrtaiggqa kamvvtasrl
      601 havrymkefk kyiankgynd lnvlvafsgl vvdgeteyte tkmnvtksge nvrenqlkea
      661 fhtdnfnili vaekyqtgfd epllhtmfvd kklkgvkavq tlsrlnrtmp gkkdtfildf
      721 vndvedieaa fqpfyeqtnl reeinvnliy dtqsklrkfn vynqgdierv mklvkqaqkq
      781 qnerllgris smfkpimdry eemnkdnqyq frvtlrnfsk wydyisqldr lfdmelleer
      841 iftgyllkfl pketrenidi sdkvkleyyk lrqdfsgeih lvnkegelvn pktidagikp
      901 pderdsleei ihkinerfpn dfdegdrvlv eilyrsfadn pdlkvvsmak nndaqmfeks
      961 lfpdvfkdkv meqyeknnaa fekmfghddr yfdlvytlva rdlykllrtn nlyk
//
LOCUS       WP_010708062             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Enterococcus].
ACCESSION   WP_010708062
VERSION     WP_010708062.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..389
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43179
     Region          50..372
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mdkkqttdkr lswfwrwfln nqvvtalliv llvlliiltf tkvsylfkpv wqffgvvglp
       61 vimagilyyl lnpivdylek kqisrvwsii glfilivall iwggivivpk ireqsvsfvn
      121 hfpqyidtid qksqeilsdp lfaqfreqle aagdkvvssl gtiiknvstf tvqgignffg
      181 avatifvaii tmpfilfyll kdgknlapyl mkflpvkmrk ptlkvlaevn hqvssyirgq
      241 ltvafavaim fmigfsvigl dyavtlgiaa gflnlipylg sflamipavf lgivsgpall
      301 ikvlivfaie qtvegrfisp lvlgsqlsih pvtilvvllt sgklfgivgv ilgipvyaaa
      361 kviithifew yqivsglyde dkpdqqest
//
LOCUS       WP_010708146             345 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010708146
VERSION     WP_010708146.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..345
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38355
     Region          25..341
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mlkefkmiea vapdmldvlq erfqilrniy wmqpigrrsl setmgiterv lrtetdvlkq
       61 lnliepsksg mtlterglev yqglelvmnq llgmhqieke mtqyfgiqrc ivvagdsdiq
      121 kkvlsdfgdv ltntlnlllp ngentivvmg gttmamvaen mgsletekrh nlfvparggi
      181 geavsvqans isavmanktg gnyralyvpe qlsretynsl lqepsiqevl tlishancvv
      241 hsigralhma arrkmsddem vmlkqknava esfgyffdee gkvvykipri glqlknlqei
      301 pyvvaiaggk tkakairaym knapkqtwli tdeaaaneil kgvtl
//
LOCUS       WP_010708157             420 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus faecalis].
ACCESSION   WP_010708157
VERSION     WP_010708157.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..420
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=46377
     Region          3..394
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 msekimntiq nkvlpiatki gnqrflvalr dsfmgtmpvi mtgsvailln aflvdfpmqf
       61 gyekitdyfq wlvdinnlis kgsisivsll fiyclgvnia kiyktdtlss glvalssfii
      121 sisnsmtsty ylsnnnnidl ttlftdvegi tvtgnslnvt isgllpgtqi nsngyftaii
      181 igflssiifc klmnknwtik lpdtvppaia kpflsiipal vslyiiailt fllnritgki
      241 ltdviyeilq rpmlglsqsf fvvilvaflv qffwffgihg gnvmapimeg vfgvallvnl
      301 eayqnnetip yvwtsvsygs fvwyatlgll iaifwvskns hykevaklgi mpvlfnigep
      361 vmyglptvln pilfipfllc pavmssvayl vtdfklgfss ntkcnlgntt gliwilfdri
//
LOCUS       WP_010708206              73 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010708206
VERSION     WP_010708206.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 73)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..73
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7993
     Region          1..63
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 msnsvrefri skgitqtkla emanisrpyl aeiekgdsnp saqiaisiak sldttvetif
       61 lpkmsymnnr ege
//
LOCUS       WP_010708208             154 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Enterococcus faecalis].
ACCESSION   WP_010708208
VERSION     WP_010708208.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..154
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=17654
     Region          35..119
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mvtseelmar fsdltykfep nmpekqkgly innvvylnpq qhptelistv aeeighhlts
       61 vgdiidqdtn ekrkqeqkar diaatmvvtp qdlidcyher fkyvwecadf lgitkhalec
      121 altayskkfp eglvygdykl ffkpngtlgi vewf
//
LOCUS       WP_010708336             595 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: terminase large subunit [Enterococcus].
ACCESSION   WP_010708336
VERSION     WP_010708336.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..595
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68112
     Region          7..592
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mdlskitskh fetalnyara ivdckilanl drrlacerfl kdltrtdidf rqeqfdfvin
       61 liegtihhvq gedrngisyk gqpllltdwq kfvcvnlfgf fekdsdirrf kealiflprk
      121 qgktafsaal teaksildrr sgskayivan svkqtlecfn flvdnvnelk edveklrird
      181 nnqehsisin fgdgtsdiya ianqedklds lncnclvlde lhswkragak kytlmknamk
      241 ayrnklligi stagdipdgf lanrlktlqk vlngsitdsa ydsyfifick adqdeegnil
      301 nskgeittid dpevlemctp sinvtvtlee llddasqamn epqlktefln ktlnvftnam
      361 dayfdinefr ssdmqydwtl ddlarlpivw yggadlsklh dltagalygs ykgidicith
      421 affpklaavk kaeedgiplf gwkedgwltm sntptvlhdd ivnwfismkq kgfkiklvgf
      481 dkkfgrefff kmkkagfkik dqpqyfykks egfrhievkv knkqfyylhs dayeycvqnv
      541 raiektddmi qydkldgdgg vqridlfdas vfsccqmled maygnvgtew lnrky
//
LOCUS       WP_010708362             468 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Enterococcus faecalis].
ACCESSION   WP_010708362
VERSION     WP_010708362.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..468
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49131
     Region          1..467
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mntffklken kttvsteima gvttffamsy ilfvnpsils etgmpfqavf latiiasiig
       61 tlimglfanv pyaqapgmgl nafftftvvf gmgytwqqal amvficglin ilitvtkirk
      121 miikaipesl qhaigggigi fvayvglkna gllsftvqae pqngvvngss ivpalgnfdn
      181 paiilavigl vlttilvvtn vrgailigiv vttlvaipmg vvdtasvdwh anslgnsfke
      241 lgttfgaafg aeglqslfsd sskipqvlit iiafslsdtf dtigtfigtg rrtgifsked
      301 elaledskgf stkmdkalfa daiatsigai fgtsntttyv esaagigagg rtgltsvvva
      361 ilfalsslfs pliaivpaqa tapalilvgi mmlasfkdin wtdledaipa ffasifmglc
      421 ysisygiaag fifyavvkvv kgkakevspi iwvidalfil nfvilail
//
LOCUS       WP_010708524             539 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein,
            partial [Enterococcus faecalis].
ACCESSION   WP_010708524
VERSION     WP_010708524.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         <1..539
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          22..510
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 lllgtsefgl pyiinfsefn qhvlvpattg sgkttllqll vqhavkfnfp vilidgkgar
       61 dtlesmreia kfydkevhaf tddgdmrynp vehgndisir dklvslaete svfysgaaka
      121 llqvtiqlld efkgakvtls gdtrttetve rslpfvqrfl lprnvlhlfa dailpnnpkl
      181 feievekkiq kpkkksvkeg seilpdsdld keekeedsqi knskfrnisq lgiaqketet
      241 ivlnpetldl dsyylllkrn lrylptdket genikqklfe rlfiryehkd spfylyatse
      301 alqtninmll dselgklfdt knaknvldvq eivnqrklvy vsfngliyke yirtlaqmlv
      361 gdvnyfasem yrknvkrevl vifdepasyl netfidmvnk grgagvygif tpqtmadiak
      421 lgdklmeqlv gnvntlfigk tnekgeaeyw setmgtyqdi dvtsvteqed gysdvgksdw
      481 sgdrgtkrnv drfkispnki kelrtgefii yrtaenvnlp pqkvyvrnal nwlknnski
//
LOCUS       WP_010708388             455 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecalis].
ACCESSION   WP_010708388
VERSION     WP_010708388.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..455
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=53412
     Region          5..386
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 maneikqval yirvstdqqa khgdsldeqq htlneyvrqq gnmrvfktyi ddgisgqkly
       61 rdefqklldd vkkgkidtil ftkldrwfrn lrhylniqei ldknnvtwla vtqpffntet
      121 amgrsfvnqs mgfaeleaqm tseriravfd nkirkgevvs gkvplgydik dkhlvpneka
      181 eivkeifqyy letgsmratv rhlenhfsmt rdyqsvrqml tnrkyigelr dnknfcepii
      241 drdvfervql qlsknirmnk krdymftgll vcsecgcnys atavisryvr kdgttnpner
      301 hlyrctknrn nvkkcsnkkg iyettlenfl leniekqaee lsvkmqqese vkktkntndk
      361 ikkkidrlkk aylnevitle eykkdreele allipeqdnk iskidlnslh nystaefrdg
      421 ykqltvseks slwrqvikni vvypdgnlki nflgy
//
LOCUS       WP_010708752             239 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010708752
VERSION     WP_010708752.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..239
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26852
     Region          1..233
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mlkvcdasvf ynnflaleki sfeikkgtit givgpngagk stllkavlni iphqgeimid
       61 nedskkkikk vayveqkati dstfpikvke cvslgtyaem kifqkvknke wkkvtealqk
      121 vnlsdysnrq igelsggqfq rvlvarclvq nadyifldep fvgidsiser iimntlkelk
      181 kqgktilivh hdlskvkdyf dnvlilnknl iahgrvadvf nelnlkkayg dtifiekev
//
LOCUS       WP_010708840             713 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GH92 family glycosyl hydrolase [Enterococcus].
ACCESSION   WP_010708840
VERSION     WP_010708840.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..713
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=81487
     Region          3..712
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mniqaidtqh gtanqhsfsn gnclpytgvp fgmnfyapqt tdqkgswwfh pedrtfqgyr
       61 vthqpspwmg dfshllmtpv sgslselslf haqssyrpee slfspveinl tqlryqitsq
      121 lipsmyggil tidyqqkdnh llltlpgryq vkqlddhqva vkvinysgce dpdfsfyfvl
      181 hfeqpltkwf apssgedgki llsfgniaqq vvhfsssfis ekqaqlnlar eislrsteml
      241 qqgiadwhny fdrlkvthen pehtktfyht lyrtflfpqt fyeldenqqp ihydtfsqtv
      301 rpgvlytnng fwdtyktvyp lfsliaqeky eemlegflns ynetgflpkw lspderglmp
      361 gtlidaviad aavkkirpdl mpqfleamkk gatqqseren ygrqgtldyl kygyvpstyh
      421 esvnhtldya ysdfcisqva ktlndsetat fyrqqalnyq qlfnpetgfm qakdteghfr
      481 pdfldirwgk dyaegsawqs sfavyqdfag liklygsela fekkliqlcn qapnfnvegy
      541 gfeihemsem aaidfgqlai snqpsfhypf lfsyigkpem aqpllkqlmq tfdasptgyp
      601 gdedngsmsa wyifnslgfy pvtpgtgeyv igmplvqtae vklsngkqlt iqtspnkvqq
      661 qfiheiqlnq ekhtapyfth qellnggtld yqlgivpnpq ttaerpfsls tek
//
LOCUS       WP_010708886             361 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010708886
VERSION     WP_010708886.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..361
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40918
     Region          1..344
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mrnhvisfen vvkqfdeepv lknvsfeiee gkfytllgps gcgkttilri iagfndvtsg
       61 dvyfdgkrin dvpankrqvn tvfqdyalfp hmnvfdnvaf glkikklska eiekkvkeal
      121 rlvrlpgyet reisemsggq rqrvaiarai vnepkvllld eplsaldlkl rtamqyelrd
      181 lqqrlgitfi fvthdqeeal amsdeifvmn kghivqsgtp vdiydepinh fvadfvgesn
      241 ivdgvmledn lvsfvgkkfe cvdggmrkne pvevvlrped ltittlekgk ltvtvdtqlf
      301 rgvhyeiicf deqgnewmvh strkakegaq vglsfepedi hvmrfnesee dfdarlesyd
      361 e
//
LOCUS       WP_010708975             389 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus faecalis].
ACCESSION   WP_010708975
VERSION     WP_010708975.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..389
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45658
     Region          73..382
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mklraniiek rgtlqvivsy kdsngkirqk wkdtklkkkg nkkraekird efllelesql
       61 amececanpd llfydyllny levskkqvaf ntyvgykhyv hnriykffyp kkiklnrlkp
      121 yhlqdfyqym lnddctantv ihyhafirka lqeaviteli stnvadkvrk pkkkqfvsqv
      181 ynqheilkll dilseeklyl vvlltafygl rrsevlglkw saidflnkki minhviienp
      241 enmsqlikkd qtknsssyrt lplvetiera lvnqakwqqd nrillgedyi lkdseyvftm
      301 edgrlmkpqy vthrlsklik knglkkirfh dlrhsnasim ldsgqnmksi qewlghasys
      361 ttanlythlt agvkervaea lenafgfke
//
LOCUS       WP_010709007             281 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Enterococcus faecalis].
ACCESSION   WP_010709007
VERSION     WP_010709007.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11573834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..281
                     /product="VOC family protein"
                     /calculated_mol_wt=30993
     Region          9..132
                     /region_name="VOC_BsCatE_like_N"
                     /note="N-terminal of Bacillus subtilis CatE like protein;
                     cd07255"
                     /db_xref="CDD:319918"
     Region          170..279
                     /region_name="VOC_BsCatE_like_C"
                     /note="C-terminal of Bacillus subtilis CatE like protein,
                     a vicinal oxygen chelate subfamily; cd16359"
                     /db_xref="CDD:319966"
ORIGIN      
        1 mvqalpsnig iqqvtlkvad ldkmvnfhtk tiglkllkqg egrawlapqg tndailvlke
       61 ltageesqgt tglyhiafll ptrkdlgnml lwllqenvqi gaadhgysea lylsdpenng
      121 ieiywdkpee vwdirpngei igvteeldgd slaaeadghw lgisegskig hihlkvadld
      181 ttetfyknlg fglksnfgqq akffaagqyh hhigtntwsg kqlptiqenq fglenytfrl
      241 ptaadleivq anaeeaklhf iakdhllale dpsgmiiqft y
//
LOCUS       WP_010709008             444 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MATE family efflux transporter [Enterococcus].
ACCESSION   WP_010709008
VERSION     WP_010709008.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Kaatz,G.W., DeMarco,C.E. and Seo,S.M.
  TITLE     MepR, a repressor of the Staphylococcus aureus MATE family
            multidrug efflux pump MepA, is a substrate-responsive regulatory
            protein
  JOURNAL   Antimicrob Agents Chemother 50 (4), 1276-1281 (2006)
   PUBMED   16569840
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..444
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49312
     Region          12..430
                     /region_name="MATE_MepA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Streptococcus
                     aureus MepA; cd13143"
                     /db_xref="CDD:240548"
ORIGIN      
        1 meqtqqnhft alfyknvllg ilsmaaqsif iladtffian gigtealagl nivlplvnii
       61 nglgwmfgvg gatlfsttva qkeikkanqy fsltiglvfv igslftlvsl ifsdqiirgl
      121 qgtgvlfgla keyymiylsc sllfifnncl itflrndhnp rlatiafvsg givniildyv
      181 fiyqfgwgma gaaiatvmsp ltslilitlh kwspqrvlrf ekfkvkfqdv reimsigfss
      241 flnefssafv mflfnivlln lvghvaisay aivanlniiv iaiftgigqg aqsllsryyg
      301 lgetkvlrkf vklsfitylv agflfflisq vftgqiievf nsegndqlaq iartairlya
      361 isflftglnf mgiyyfsavr kpkmalmiss lrgfflivpv lfilvkllgl tgvwlampvv
      421 efvtfglmlv gylayrnylk kekq
//
LOCUS       WP_010709012             459 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Enterococcus faecalis].
ACCESSION   WP_010709012
VERSION     WP_010709012.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..459
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51140
     Region          10..430
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mnnadpesqs liaqllllvv ltfinaflaa aeiavvsvnk nrveqkaedg dakaqkllkv
       61 lqdpnnflst iqvgitlvni lsgaslaetl ssrlapvlgg gaaakslasi iilalltyvs
      121 ivfgelypkr iamnkseeva qltsgavrfl gviarpfvwl lsastnllsk itpmtfddad
      181 skmtrdemry mletegvlen eelemlqgvf sldtkvarev mvprtdafmv diqddvqeni
      241 nlilgenysr ipvysedkdk ivgilhtktl lkaarnlgfe nielgaiiqe plfvpetifi
      301 ddllyelkrt qnqmaillde yggvvglatl edlleeivge iddetdeven lytqvadney
      361 lvqgrmlide fnevfetdlh msdvdtmagy litalgtipd egekpsfevg nikltaeeme
      421 gtrllvlrvh fydeetvdee peenrrffrk emeddeprr
//
LOCUS       WP_010709051             432 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S1C family serine protease [Enterococcus].
ACCESSION   WP_010709051
VERSION     WP_010709051.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..432
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44700
     Region          130..417
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mqrkdvtpns dkksllqkfg iglaggllgg alilggaysg iiptpnggnn aatttstnhg
       61 dtkvsnvsyn vssdvtkavk kvqnsvvsvi nmqsasnnss addpfgglfg gnegtqdssg
      121 nngndleaas egsgviykkd gktayvvtnn hvvdkaqgle vvlsdgtkvk gelvgtdayt
      181 dlavikissd kvdqvaefgn sskitvgepa iaigsplgsd yansvtqgii ssvnrnitnk
      241 nesgetinin aiqtdaainp gnsggplini qgqviginsv kivqstsqvs vegmgfaips
      301 ndvvniinql ekdgkvtrpa lgitmsdltg issqqqeqil kipasvktgv vvrgveaatp
      361 aekaglekyd vitkvdgqdv ssttdlqsal ykkkvgdkme vtyyrgskem katidltidk
      421 saltqqnnrs nq
//
LOCUS       WP_010709063             402 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010709063
VERSION     WP_010709063.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..402
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43852
     Region          6..402
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkrsiiwkta frsilknkrr slltmlgivi giasvitiva igngfkedmv dklsaekqke
       61 nvkkisfsay ntsdmfsdqa mftdndlgvv rmvpgvekid fdqrevdgaq kgtlnfqagp
      121 knlsvtyela nkttkellag rqlndgdnak mdktvvvdel vakelyqdpt aavnrtfpyk
      181 eqlftivgvt tntsgaigpg nddsllyfpk ktyehyfgkl kdtstlkltv apgyqpdqvl
      241 ketiktlsqq gtmknsgtyq eynvkdtike mgsllnnltl fisaiaaisl viagvgvmnm
      301 myisvservk eigirralgg tasdikkqfl tegialtlig gitgyllgmi iaylasmalp
      361 fsvrpdlmtv slaigisvfi gvvfsyfpas aaskkdlidi mk
//
LOCUS       WP_010709163             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010709163
VERSION     WP_010709163.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..222
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24262
     Region          133..217
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mnyvkrifsi filfiisqig itafgvikql sldageknln isstlvtvil vvinilfliy
       61 lakrmniikt nhpfltkkni liilvatlid rgiaiggtll lnmqghttta ndstliklfs
      121 gvspvlvvll lgiaapimee ivfrggiigy lvennallai lissflfgii hgptnfisfg
      181 myffmgiils vsyyktkdlr vsisihflnn lfpaiaiayg li
//
LOCUS       WP_010709189             828 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase
            [Enterococcus].
ACCESSION   WP_010709189
VERSION     WP_010709189.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 828)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457611
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..828
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87421
     Region          1..67
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          75..139
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          163..814
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(461,463,769)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(505..507,571,587..589,618,658..660,680,683,686,705,
                     708)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(770,798,802)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mesktfdieg mscascaqti ekataklpgm akasvnlate klsvtydqte vteeeikeav
       61 sdagykaisp aqqrtfaieg mscascaqti ekavnqlsgv qqaivnlate klvvsyddhq
      121 vtsaeiikav tdagyqatee vaagatadqd rekkqkhiae mwqrfwisav ftvpllyiam
      181 ghmvglplpd flnpmthatt famvqliltl pvlyvgreff tvgfkalfkg hpnmfslval
      241 gtsaafvysl ygtvmiflgd tsftmalyye sagviltlit lgkyfeavsk gktsdaikkl
      301 mglapktahi lrdgaeievp vdavqlddiv ivrpgdkipv dgvivsgsss vdeamltges
      361 lpvekkvgda vigasinkng sfqfkatkvg ketalaqiiq lvedaqgska piaqladkis
      421 gvfvpivigl avlsglawff lgqeswifal titisvlvia cpcalglatp taimvgtgkg
      481 aengvliksg daletthkiq tivfdktgti tegkpvvtdi lvadsalsea elltlaasae
      541 qgsehplgea ivgaakerql plaegsdfsa ipghgirvtv nervlllgni klmkeeaiel
      601 stfvqqadrl aeegktpmfv akdgsfagii avadtvkdss qtaiarlhkm gieavmitgd
      661 nkrtaeaiak qvgidrvlse vlpedkalev kklqaegkkv amvgdginda palaqadvgi
      721 aigsgtdvam esadivlmrs dlmdvptave lskatiknik enlfwafayn tlgipvamgv
      781 lhlfggplls pmiaaaamsf ssvsvllnal rlkgfkpstv krtsgsqk
//
LOCUS       WP_010709232             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010709232
VERSION     WP_010709232.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..272
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30091
     Region          1..271
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnyiylineh yplltkserk vadfilnsge siiystmndi ktkanvgdat iirfcqklgf
       61 sgfsdlkiei akedfskkke qpssgkyhde vakslievlq stsclineek ltkaiqlinq
      121 asslyifgvg ssgntsldle smflrvgiqa kavldphyqa qvaslltdsd lviifslsgk
      181 tkdtydslki aknngakila itnyihspig ksadlvlqta ieeflnggsl agkisqlyic
      241 dllvheyeqn nkinsldlre kvlrsiidkr ie
//
LOCUS       WP_010709657             356 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methionine ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010709657
VERSION     WP_010709657.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..356
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40020
     Region          1..342
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mielknisvt fqqkkqeiqa vqdvsltidk gdiygivgys gagkstlvrv inllqrptag
       61 tviinkenil tfskkelrqq rkkigmifqh fnlmkertif snidfslkys glskserrqk
      121 ishllelvgl sekrdaypsq lsggqkqrva iaralandpe illcdeatsa ldpkttgqil
      181 allkklnqel nltivlithe mqvvkeicnk vavmengyvv esndivsifs qpqqpltkdf
      241 irtathidqa lttilehpkl adldknqeli efsyvgdqtn epliaqlysq yqvytnilyg
      301 nveivqnvpi ghlivvlsgd eaqrqqalty lakqgvrtnv lktyqqtkqk qnlqvi
//
LOCUS       WP_010709783             281 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010709783
VERSION     WP_010709783.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..281
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31606
     Region          6..217
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mktkaleicn ltktfkdfkl dnvsftlpvg fimglvgeng agktttikli fdllekengv
       61 vkvfgndtkn ghnykqdiav vfddlffved wkisdiekav spfyskwdtk sfhtylnkfn
      121 ismnkkikel skgmkmklnl avalshqarl lildeptsgl dpvardelld illeyienen
      181 nsilfsthit sdldkiadyl tvmndgkify tgvkdelfdk ycivkggied ltpnietkli
      241 giqkgktgft allnvvnmky isdsiiveka tldeilihin k
//
LOCUS       WP_010710011             424 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010710011
VERSION     WP_010710011.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..424
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=45427
     Region          1..422
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mnkintyleq kmlpiagkls snkflvaird gitltmplii igslfmvias fpvpgwetwl
       61 gdvgvsgylw kgvdssfgli glvasfgiah sltkqygvdg vssgiislst fitvtpflss
      121 dagagmptgy maakglfvai ilglingyvy qwfinkniqi klpdtvpsav aksfsaiipg
      181 avlitfwlii fglldtfslp nihdiaqvvl gkplgllgsn ifgtiivval nslfwfigih
      241 ggnvinsvmq piwianldan reayqagqsl phiftvafmd nfvyigggga tiglvlvmgy
      301 larkkktskq tkvlapitvv pglfninept mfglpvvlnv mllvpfilap ivnvvvaysa
      361 mitglvpltr tvatwtmppi isgflttgsl mgsvlqivli vldillylpf flaiekqfkq
      421 eelv
//
LOCUS       WP_010710020             435 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Bacilli].
ACCESSION   WP_010710020
VERSION     WP_010710020.1
KEYWORDS    RefSeq.
SOURCE      Bacilli
  ORGANISM  Bacilli
            Bacteria; Bacillati; Bacillota.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Bacilli"
                     /db_xref="taxon:91061"
     Protein         1..435
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=47149
     Region          1..431
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdkltnwveq avvpkvsrit slryfqalrn gffaimplti igsifmlitd fpvagygdfm
       61 agifgadwad mispayratf nmmgiifagt msyklaesye mdrltslilg ivayvvvlpk
      121 tvttesgevv tkvlsfdwlg tqgvitaiim silsveltrf cikkklvikm pesvpsmvsq
      181 afsalipgif vvavalling iglsfadsfp qliyaviqap lqgligtpfa iiivaglngl
      241 fwwfgihptv insmlypily anadknqsla elgqltaqsg nfgtvqmldq fatiggagct
      301 iglaiamaiv ghssrmkams kisfvpaffn ineplifglp vifnplllip iavapivsvl
      361 iaflsmkigf mpmftniqap watpflfsgf lvgkwqgavt qvlavaasvv iyypfvkald
      421 rqyqkeeahe vpetl
//
LOCUS       WP_010710064             395 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu [Enterococcus faecalis].
ACCESSION   WP_010710064
VERSION     WP_010710064.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     gene            1..395
                     /gene="tuf"
     Protein         1..395
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43303
     Region          1..395
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makekfdrsk shvnigtigh vdhgkttlta aiatvlskhg ggeaqsydsi dnapeekerg
       61 itintshiey etetrhyahv dcpghadyvk nmitgaaqmd gailvvsaad gpmpqtrehi
      121 llsrnvgvpy ivvflnkmdm vddeellelv emevrdllse ydfpgddvpv iagsalkale
      181 gdesyeekil elmaavdeyi ptperdtdkp fmmpvedvfs itgrgtvatg rvergevrvc
      241 deveivgikd etskttvtgv emfrklldya eagdnigall rgvaredier gqvlakpati
      301 tphtkfkaev yvlskeeggr htpfftnyrp qfyfrttdvt gvvelpegte mvmpgdnvam
      361 dvelihpiai edgtrfsire ggrtvgsgvv teivk
//
LOCUS       WP_010710139             356 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ammonium transporter [Bacillota].
ACCESSION   WP_010710139
VERSION     WP_010710139.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..356
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39233
     Region          1..324
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mnnlfifvcf cfmwlmifgv ilyyvglvnh ryihhtlilg lvtiisgtlc wlfvgyslsf
       61 fgniqysify splasseivs iliqllfcly svimiigsvl ergnwkyivl fvplwivfvy
      121 apicfslwgh gnwlgkmgvl dysgglvvht tagigslvla itspirlkns lifksqemia
      181 fvgmlfitlg wfgfnmapsg kigeeaiqvw lntlisilgg siswtftqwi likkvsiysi
      241 mngiigglvg stcsvgyvsp afsllisviv ctlcpivihi mhlsianfdd aadsfgmnav
      301 ggiagsiltg vmaekgdffl qlfgtflisi wslslsllih yllkkivndc ysqcik
//
LOCUS       WP_010710252             133 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Enterococcus faecalis].
ACCESSION   WP_010710252
VERSION     WP_010710252.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..133
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=15641
     Region          <14..127
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mqqhyneksi qhqfdayckk vlrneaksir krntdikdne epltdsnegk ysqthfdeqd
       61 vyflfgmeil isdqklsaai dqlseirrki illyyfagfn daeigkilnm stsgiwyqrm
      121 kaveqlkmgy dlw
//
LOCUS       WP_010710377             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010710377
VERSION     WP_010710377.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28348
     Region          1..250
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 miqkkrleli leelktrgtl slkeiinltg ssrdtarrdi iklaqnnaid rtyggislpn
       61 tfsrldeyle rtedlsaekd ilaktasnlv kdnshifldi sttvsciprh irpyenviat
      121 tnslditdql lrntkcktki lggsvdpikr nvvgtkpmle ldsfifdvaf msaagittsg
      181 iyyaydedid fkkkirkqsk lvvllidntk iglshnykgl dfedidflvi esclpddler
      241 tisdsnvsii nsk
//
LOCUS       WP_010710397             238 aa            linear   BCT 01-JAN-2025
DEFINITION  pseudouridine synthase [Enterococcus faecalis].
ACCESSION   WP_010710397
VERSION     WP_010710397.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26653
     Region          1..226
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 merlqkaiah agvtsrrkae elivkgrvkv ngqvvielgt qvskqdtvev dgvpiyqeey
       61 gyylfykprg visavsddkg rkvvtdyftd vteriypvgr ldydtsglll ltndgsfsqk
      121 lthpkhevdk vyvakikgvp tkrdllplak giridgkrta panfqilsad iktgssvvel
      181 tihegrnhqv kkmfqavgfp vqklkreryg eltlqglrpg qyrdltkkei sqllnqak
//
LOCUS       WP_010710436             107 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010710436
VERSION     WP_010710436.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..107
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12401
     Region          3..101
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mkqtellkgi leglvlaiiq rketygyeit kilndqgfte ivegtvytil lrleknqwvi
       61 aekkpsekgp mrkfyrltss geaeladfwq rwtlfskqvn kmkkmeg
//
LOCUS       WP_010710533             143 aa            linear   BCT 01-JAN-2025
DEFINITION  NusG domain II-containing protein [Enterococcus faecalis].
ACCESSION   WP_010710533
VERSION     WP_010710533.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009210
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..143
                     /product="NusG domain II-containing protein"
                     /calculated_mol_wt=16100
     Region          36..140
                     /region_name="COG5341"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444125"
ORIGIN      
        1 mkkipitilt dyfgsgkigm kigdviilgi liissfiplf ifslekgnee ttkyavvrin
       61 gkevdrfnld esnhkfvkyy pakgqyniie ikdgkirdke dnspdqiavr tgwiskpgqt
      121 siclphklvi siekkgspdy yiy
//
LOCUS       WP_010710577             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010710577
VERSION     WP_010710577.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..249
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27261
     Region          1..236
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mrksfnlavq altvqyqgrt alnnihvtip sgkitgiigp ngagkstfik gllgliktke
       61 rdvllnnqai dqqktiiayv eqrsaldlsf pisvfetvll gtypnlgllk rpgkkekqaa
      121 maalkmvqle dyaqrqigel sggqlqrvfi arvlaqgaev ifldepfvgi dmssekvimd
      181 ilkslknqgk miiivhhdlh kvshyfdeli vlknrliaag pveqtftaet lqeaygdllg
      241 dlliqgvak
//
LOCUS       WP_010710702             374 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Enterococcus faecalis].
ACCESSION   WP_010710702
VERSION     WP_010710702.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..374
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=42143
     Region          86..316
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mwkisnendi fkkrkplppk kseesqpelt pwqkqnqeyl kkqaeeaalk geneqaevti
       61 tlqeqsqeep qqhlpqetve eeehfadrlp nvkktrnkrl yrrlafiltc lgtailvaly
      121 fvsplsrlse vtvsgnksve sqaiiqqskl etgsglweqy snrnyfsani qkkfpiikka
      181 niklnginsf kidiqeyqiv alaatkggyh pilengktla ettkaaesgk pifenfkedk
      241 lipelmasyn klpqeikqgi seikyapskt nkdlinvymn dgnrvivnis dlsekmayys
      301 qvaeqmdkpg ivdmevgifs ypyekeseet gsevsedstv enqevvdpna gvatdeanng
      361 tptngenqev qqae
//
LOCUS       WP_010710768             492 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Enterococcus].
ACCESSION   WP_010710768
VERSION     WP_010710768.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..492
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=58536
     Region          79..156
                     /region_name="Mga"
                     /note="Mga helix-turn-helix domain; pfam05043"
                     /db_xref="CDD:428276"
ORIGIN      
        1 mlkrdflekp ydymndillf lynnkgqatr nelvdffnis lptlneylsf leqflkeeql
       61 qenltltvlg dtlylnkapt fsmkamimlf ldksikfhmv qqllhknein ggyfqqnyai
      121 ssatyyrkiv elndllnefn lrikrgklvg eekqirffff nffwfifeek tdlekelanq
      181 ylglieilqe ipritfdhte ilqiklwmki sfrrmvlepl ptispqdvql drplfeeinl
      241 sihtymkrid rpytineaym fydffcsmhn ysanaafafr lakqqriekt ylnemnrvil
      301 tylkargyls hyvlpirlly ienllfqlha qlyyfsgfil pfdywtiqsl lkvvrhpfse
      361 sevyelveia ttnfatkata skyqnqftei nytlilnhia elnekkitig vyhslssays
      421 elvaqkiqqs iagkyplkie pynaenhydl llmntnneql vaqydhyyif sdisnrydlq
      481 siekiiqlll gk
//
LOCUS       WP_010710821             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010710821
VERSION     WP_010710821.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..155
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18082
     Region          16..103
                     /region_name="HTH_GlnR-like"
                     /note="Helix-Turn-Helix DNA binding domain of GlnR-like
                     transcription regulators; cd01105"
                     /db_xref="CDD:133380"
     Site            order(18..20,34,51..53)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133380"
     Site            order(65,68,72..73,82,85,89,95,99,102..103)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133380"
ORIGIN      
        1 mwskmiqrll neenlligis elseiaevsp rqlryweekg yissiakdan gprkyrlhtv
       61 vkvhwikrfl degytlqsav ekaeeqhrnv emtkkifsqm fhgisevcpn yvaidlgdfd
      121 eeqklyvvfn ettevseyll ipkdadvsde lkkrk
//
LOCUS       WP_010710773             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Enterococcus].
ACCESSION   WP_010710773
VERSION     WP_010710773.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..321
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35747
     Region          1..248
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mdkirygims taqivprfva giresaqaev rgiasrrlen aqkmakelai pvaygsyeel
       61 ckdetidiiy iptynqghys aaklalsqgk pvllekpftl ntaeaeelfa iaqeqgvflm
      121 eaqksvflpi tqkvkatiqe grlgeilwvq svtaypnvdh ipwfysreag ggalhgsgsy
      181 plqylqyvlg keiqevtgta tyqqgatdsq cnlalkfaeg tlgnifinvg lkipsemtic
      241 gtkgqivipn fwktdcayyt daqgntvkws eqftseftye inhvnqclqd kkltspvmtk
      301 eltiatvkiv esfyqewfdn e
//
LOCUS       WP_010710831             270 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Enterococcus].
ACCESSION   WP_010710831
VERSION     WP_010710831.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..270
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30682
     Region          26..>134
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mknnqtlang arvtiypttt eptnyvvylh gggmiygtks dlpeelkelf tsngytvlal
       61 dyllapntki dhilgtltet fqllneeiiq nqpfglcgrs aggylmlqlt kqlqtlnltp
      121 qflvnfygyt dlefikeprk llkqaisake iaaidqtkpv wddpflsryl lyhysiqqal
      181 lphfyglpen gdwsayalsd etlktfppcf stasssdeev pfryskkigr tipestfkav
      241 yylehdflkq tndpsvitlf eqldswlker
//
LOCUS       WP_010710856             113 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system PemK/MazF family toxin
            [Enterococcus].
ACCESSION   WP_010710856
VERSION     WP_010710856.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..113
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=13046
     Region          8..113
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mnvekkyipk kgdivwidfd paagkeiqkr rpglvvsrye fnrktmfavi cpiistikni
       61 ptrytlpddi ethgqvvisq lksldfterk lsqiehlplk dmakidqiie yif
//
LOCUS       WP_010710864             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cysteine hydrolase family protein [Enterococcus].
ACCESSION   WP_010710864
VERSION     WP_010710864.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..181
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20122
     Region          3..181
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mkalisidyt ndfvatdgkl ttgaagqaie talvqqtkhy fdngdfvvfa idghdpldry
       61 hpenklfpph nvlgtdgrnl fgsladfyqa hkneatvywl dkrhysafsg tdldirlrer
      121 gitelcltgv ctdicvlhta vdaynlgyql mipenavasf deqghewalr hfkqtlgati
      181 l
//
LOCUS       WP_010710868             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavodoxin family protein [Enterococcus].
ACCESSION   WP_010710868
VERSION     WP_010710868.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..233
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=26641
     Region          3..173
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mkkilaiigs rdknsetlsi vnriketvqd lnasfefeii tpydynlnfs dsprlafikg
       61 adtneqderd dskkikakie naslvilasp tyfanvsadi klfidrfchl ahlfyfakkp
      121 citvvtsdgn ghiqtsnylk sfcdglgmvr vqeiisirsn piseneieas vreglkyisn
      181 pqkispnlsm emsfqhwkks iskqnetlse yrywensglf scnsleeyfd ryr
//
LOCUS       WP_010710935             336 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Enterococcus].
ACCESSION   WP_010710935
VERSION     WP_010710935.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..336
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36980
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdekdiydl tiigggpvgl faafyagirk aktkiidslp qlggqltmly pekyiydipg
       61 fpaikageli anlekqmqpf qhdvcleeev thlaqeadgl lrldttkgth ysktvifaig
      121 ngafqprrla ienieafege sihyyvtdmk kfagkkvaia gggdsaidwa lmlenvaeev
      181 siihrrpqfr ghehsveqle kssvsirtpy iisdilkenk tftgiqltet kgdqtldlpl
      241 ddliinygft sslthlkewg ldvsrnainv hsdmstnipg vyavgdicsy egkvkliatg
      301 fgeaptavnn alhylrpdar rqpvhstslf engvpk
//
LOCUS       WP_010710940            1049 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type I restriction endonuclease subunit R
            [Enterococcus].
ACCESSION   WP_010710940
VERSION     WP_010710940.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1049)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1049)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1049)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1049)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..1049
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=121058
     Region          8..941
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mkishreeae veeqlirvlg eghnqwtyrp dlkseedlwv nlrqkiisnn qaelndfplt
       61 dkefetikte lllrtktpfd aakwlkgeng maritiered pqlgsvslil ysnqdigggi
      121 styevvhqia krgsnieard rrfdvtllin glpivqielk qvtakdgfyq afnqikkyae
      181 egmfrnnifs tlqlfvvsne qttryfanal pkdlhpkflf swrtkdnkkv enlyefckqv
      241 lnipdahrli adytivsedq dnktlmvlhp yqvhaiqalf iaankhqsgy vwhatgsgkt
      301 ltsfvstkll arksgidrti mlvdrkdldn qttaeftkfa sefntgissg nakanslivg
      361 tgsakelset lladananvv iittrqklda alkyakkqee kkgtnrfqkl mgqhivfvvd
      421 echralsaen meeikkmfpk stwfgftgtp ifpenrkqak gqlartthdq ygevlhtyti
      481 knaledgsvl gfqvehentv eptslenkiy rklkevetya eysseqinhm idqmepvkke
      541 syldpavfea dehiqkvihk mfrpdnaytk fdfrngrptk sailttssid makkyyraik
      601 emtkepdwlt kefpdqpire grtmedldfp riaityslee ntqdssaqqk emqkiieeyn
      661 qyydtawsla dieryngdin nrlarkraef kqfgkqidlv ivvdrlltgf daptiqtlfv
      721 drnleyagli qafsrtnrty pekikglivt frkpatmekn vedatklyse akeesgliyp
      781 syqeskkrfk qaygklkevs smesidehtp leirieyvka fqelnrayes lvtyddyndd
      841 mvksptlnnq iqlleeqigv yetvkgslie eepekegedf stiefysent tklydidsty
      901 idqllgtyaa nssdareeie kalaklnkte gvkevyrqil nafdvgtlds nedifvikrr
      961 yftqasddli hafsnewfvs ekelhasnlq ympgedpipn mkaiinskdy egyktkhpea
     1021 kpfkypqemk rawrkmldde liplenelr
//
LOCUS       WP_010711005             250 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Enterococcus faecalis].
ACCESSION   WP_010711005
VERSION     WP_010711005.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13397480
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..250
                     /product="Fic family protein"
                     /calculated_mol_wt=28862
     Region          6..243
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
     Region          64..155
                     /region_name="Fic"
                     /note="Fic/DOC family; pfam02661"
                     /db_xref="CDD:426907"
ORIGIN      
        1 mntkklaeli ysvaqydgyn tsilqtqknl stnkeewqft neadryifed lvkaihyvsn
       61 qleltvevfk ginaqmdshk egqpdspgql rnrveihvgd yipprtitek mvqreisaik
      121 gtsvadgwel yarlaklqaf dngnkrtali sanlligslk getqtfltip tdfrrtqfda
      181 nlmyyymadd lddhmpdvqy slnefvrfak eyteaqqknk feerleeaki qqtkqkkfka
      241 nhlrnngktl
//
LOCUS       WP_010710988             141 aa            linear   BCT 01-JAN-2025
DEFINITION  CsbD family protein [Enterococcus faecalis].
ACCESSION   WP_010710988
VERSION     WP_010710988.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10527613
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..141
                     /product="CsbD family protein"
                     /calculated_mol_wt=14713
     Region          26..77
                     /region_name="CsbD"
                     /note="CsbD-like; pfam05532"
                     /db_xref="CDD:428512"
     Region          82..139
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mmkktgfiig lfatafgiav vnkmqkinan kdsvkgkake lagdvvgnek lqaegtvdqv
       61 vgaskevled lkesvssvfs sgatdkvagk akevtgevtg dkkqevegli dqatgdtkkv
      121 adkakdkaen vvedakekld k
//
LOCUS       WP_010711117             464 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecalis].
ACCESSION   WP_010711117
VERSION     WP_010711117.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..464
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=53410
     Region          1..380
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mkraalyirv stmeqakegy sipaqtdklk afakakdmav akvytdpgfs gakmerpalq
       61 emisdiqnkk idvvlvykld rlsrsqkntl yliedvflkn nvdfismqes fdtstpfgra
      121 tigmlsvfaq lerdtiterm hmgrterakq gyyhgsgivp lgydyvdgel iindyeaqii
      181 qeiydlyvnq gkgqqyitkr mvakypdkvk tltivkyalt nplyigkisw dgkvydghht
      241 piidksmydk aqeiiarkaq kggeqhgnql glllgitycg kcgakvfryv sggkkyryny
      301 ymcrsvkkml pslvkdwnck qpslrqevve kkvidslksl dfkkierelk qvenktkski
      361 ttinnqiskk hnekqkildl yqygtfdvtm lnermkkidn einaltania nlegiksesl
      421 inkletlktf nwetettenk iliikefver ielfddevii kykf
//
LOCUS       WP_010711192             442 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus faecalis].
ACCESSION   WP_010711192
VERSION     WP_010711192.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..442
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=49449
     Region          16..369
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(19..20,23..24,59,62,118..119,174)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(116,119,203..209,238,265..270,297,316,319..322,324)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mnltfdytke psrdvlcidv ksfyasvecv ergldplktm lvvmsnaena gglvlsaspm
       61 akkvlgvsnv trknqvpahp dlyvvpprmn lymkknqein nlykkfvade dhsvfsvdes
      121 fldvtaslsy fhcetaykma riiqrvvynh vgiyvtvgig dnpllaklal dngakhspdf
      181 iaewrydrvp dtvwqlpslt dfcgigrrma krlnrlgias vyelaqanph llqetfgvmg
      241 lqlyahswgi drtflgkkap hkaeksfgns qilprdyarr dqielvlkel teqvaarlrk
      301 ahcqtecitv yvgyskgqid regrtgwrkq qtipatnntk vliiyvlalf rehylagtdv
      361 rqlglsygkl vwneslqldl fsepeeqise melnylidki rqkfgfqali hassllegat
      421 aisraslvgg haggtvglgt tk
//
LOCUS       WP_010711191             198 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecalis].
ACCESSION   WP_010711191
VERSION     WP_010711191.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..198
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22738
     Region          3..132
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,66..67,70)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(65,113..114,116..117,121)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(71,76..77,109,112..113,116..117,120,123)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94..96,109..110,113..114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94,114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(122,128..129)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 maiygysrvs tsnqdyktqi rklegagaek ifsekytgtk kegrkeleel lsivkagdkv
       61 lvtkidrlar sivdlnsiis alnhkgvtis flddhltfep dkkdsmqtlm mnmlgsfaqf
      121 erdlivtrtq egkqwhrann knyregrpkr vlndkykhal elmetnsmre verktgisls
      181 tlkrikkqak eeqllnek
//
LOCUS       WP_010711219             295 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010711219
VERSION     WP_010711219.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..295
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31185
     Region          1..292
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mivsaigqgm lwallglgif mtyrilnfpd mttegsfplg gavcvtaitt gvspfvatll
       61 gvgagmlagl vtgllftkgk ipiilagilv msglnsvilf vmkspnksll nqpkiqdvfq
      121 kmalpdyydt iflgisvlav vmilllfffn aslgqayiat gdneemarsi giqtdrmkil
      181 glvlsnglig lsgaliaqnd gyadvskgtg viviglasli igevlfgelt fgerlmaivv
      241 gsiiyqllil lviklgfdtt ylkifsavil aiclmipqlk kalrlhgfsd kgetk
//
LOCUS       WP_010711254             575 aa            linear   BCT 01-JAN-2025
DEFINITION  terminase large subunit [Enterococcus faecalis].
ACCESSION   WP_010711254
VERSION     WP_010711254.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..575
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66133
     Region          1..573
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 miepgvnyad lfakevrkhs kkypktvrla idrwyrwkkr kdiwfdvdra nemmdwvesf
       61 ivhtkgdmvg kpfilepwek fiyswiygwv kenekgqvvr vtreayvqip kkngktliav
      121 galgyamyge galsvdcyac asdfaqaqya akpfaatiln npvlldgtki fkgpkgtvss
      181 itydylhgdm aytnkfivqt knidniegsn pyfvlndelh kqekmeqydn fksaqislpq
      241 plmfnistag kgsssvgirv ykeakevlkr ddndsnfvli yepnkgydwt dkkvwemcnp
      301 nwgisvdlsa lesafktaqr sahskaeflt khldvfvnga dnffeqdqve pclvptnelg
      361 nlsgepcwig ldlsksrdlt cvslnfptwd aegkailkvk qlyfipseni dfrekednvp
      421 yselaeqgfv efcdgklidq eqifhfiedc mdfydvqqvn ydpamsdrlv eklenlglec
      481 vqvdqyarvl nspledaerl fyeqrimfdn plflycalnv vvkmdfqgrk vpsknqskkk
      541 idgfvaflca hketmdqmid vneddmdeyl dsiyr
//
LOCUS       WP_010711341             301 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Enterococcus faecalis].
ACCESSION   WP_010711341
VERSION     WP_010711341.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..301
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34282
     Region          97..299
                     /region_name="CE4_SmPgdA_like"
                     /note="Catalytic NodB homology domain of Streptococcus
                     mutans polysaccharide deacetylase PgdA, Bacillus subtilis
                     YheN, and similar proteins; cd10944"
                     /db_xref="CDD:200569"
     Site            order(102..105,156..161,201,203..204,229,235..236,269,271)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:200569"
     Site            order(104..105,156,160,203..205,229,269,271)
                     /site_type="active"
                     /db_xref="CDD:200569"
ORIGIN      
        1 mrhkkrkfki ngyvlfsali livlvfiqtf lltqpkitsk nddttqtstk nstakkdspt
       61 klekesthmt isskkyaysa dkirkyitge epykgeklvf ltfddgvnnq itpqvldtlk
      121 kynvhatffl vgntltsenq kivkrevaeg hsigfhssth dyatlypngi vnteeiqaei
      181 admenslkki lgetfqttlw rypgghmswg gteksdelfk qlgihwidwn amvgdaepld
      241 rqpstvaeml afhqhslevy pdynirvvlm hdsvdkeltk qalpqliefy qangyqfgvl
      301 y
//
LOCUS       WP_010711372             279 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Enterococcus faecalis].
ACCESSION   WP_010711372
VERSION     WP_010711372.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..279
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31232
     Region          80..259
                     /region_name="CE4_CtAXE_like"
                     /note="Catalytic NodB homology domain of Clostridium
                     thermocellum acetylxylan esterase and its bacterial
                     homologs; cd10954"
                     /db_xref="CDD:200578"
     Site            order(85..88,138..143,176,178..179,197,203..204,227,229)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:200578"
     Site            order(87..88,138,142,176..180,197,229)
                     /site_type="active"
                     /db_xref="CDD:200578"
ORIGIN      
        1 mkekkflilg iivllgmfff lgksiislan nqqektrdsv siekqssske sssssteeqs
       61 kelkkdveqa kqveqtgpek svalsfddgp npsttpqlle ilkekqvhat ffvlgenanq
      121 speivkqakk egheigshty dhqdlaqlst deiqmeiskt dealekiige kaaflrppyg
      181 svtevaarli nrpiidwsvd sedwktrdse qifqkiigtv ydgsillfhd iypetvsvip
      241 qiidylheqg yqletvgell nhpkegkvyy gkgdsrfat
//
LOCUS       WP_010711810             321 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010711810
VERSION     WP_010711810.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15747380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..321
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37569
     Region          <65..>96
                     /region_name="Cupin_2"
                     /note="Cupin domain; pfam07883"
                     /db_xref="CDD:462300"
     Region          108..314
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 myhfskeqva hffsyletld cyikseegmi delesfknnq nrkiaalvcq ntqeiltyka
       61 pyirilyvlq gsititldgk kmtyeagcli lankwtiidy qpvkkntmvi gfyfkpqyfs
      121 dsllnqiire pmlyrffves lsdeleqksh ycvyqfnpld dihfyvllll kqvvkmryfn
      181 nkvtkaafvl lvveisqmse nclqlnasdl sntvltkeil afiennvrta sltnvakkfh
      241 fhpnylsali kkqtgisysd wltnyrmnya knyleqtnls tqqiieevgy sdktfffkrf
      301 kehvgmtpge yrksivvske k
//
LOCUS       WP_010711926             828 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase
            [Enterococcus].
ACCESSION   WP_010711926
VERSION     WP_010711926.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 828)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457611
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..828
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87363
     Region          1..67
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          75..139
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          163..814
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(461,463,769)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(505..507,571,587..589,618,658..660,680,683,686,705,
                     708)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(770,798,802)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mesktfdieg mscascaqti ekataklpgm akasvnlate klsvtydqta vteeeikeav
       61 sdagykaisp aqqrtfaieg mscascaqti ekavnqlsgv qqaivnlate klvvsyddhq
      121 vtsaeiikav tdagyqatee vaagatadqd rekkqkhiae mwqrfwisav ftvpllyiam
      181 ghmvglplpd flnpmthatt famvqliltl pvlyvgreff tvgfkalfkg hpnmfslval
      241 gtsaafvysl ygtvmiflgd tsftmalyye sagviltlit lgkyfeavsk gktsdaikkl
      301 mglapktahi lrdgaeievp vdavqlddiv ivrpgdkipv dgvivsgsss vdeamltges
      361 lpvekkvgda vigasinkng sfqfkatkvg ketalaqiiq lvedaqgska piaqladkis
      421 gvfvpivigl avlsglawff lgqeswifal titisvlvia cpcalglatp taimvgtgkg
      481 aengvliksg daletthkiq tivfdktgti tegkpvvtdi lvadsalsea elltlaasae
      541 qgsehplgea ivgaakerql plaegsdfsa ipghgirvtv nervlllgni klmkeeaiel
      601 stfvqkadrl aeegktpmfv akdgsfagii avadtvkdss qtaiarlhkm gieavmitgd
      661 nkrtaeaiak qvgidrvlse vlpedkalev kklqaegkkv amvgdginda palaqadvgi
      721 aigsgtdvam esadivlmrs dlmdvptave lskatiknik enlfwafayn tlgipvamgv
      781 lhlfggplls pmiaaaamsf ssvsvllnal rlkgfkpstv krtsgsqk
//
LOCUS       WP_010711964             278 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus faecalis].
ACCESSION   WP_010711964
VERSION     WP_010711964.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..278
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30691
     Region          6..275
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,206,228..230,232..233)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mavkaivmdi dgtlltsekk ispktrqalv aaqkqglsli lasgrptngm rpladelema
       61 hynghllsyn gacvthhgsq qqlfnqtisk slsqqilehl kqfdvipmin detfmyvndv
      121 fhntlhletg dfniieyesr ggnfqlcewh dlaarlnfpl nkiliagepa ylqkyheaiy
      181 apfketvtaa fsapfyfeft aknidkarsl ekltlqlgit aeeviafgdg hndytmlewa
      241 gtgiamenav delkniatev tlsndndgia valakivg
//
LOCUS       WP_010711991             446 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Enterococcus faecalis].
ACCESSION   WP_010711991
VERSION     WP_010711991.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Kaatz,G.W., DeMarco,C.E. and Seo,S.M.
  TITLE     MepR, a repressor of the Staphylococcus aureus MATE family
            multidrug efflux pump MepA, is a substrate-responsive regulatory
            protein
  JOURNAL   Antimicrob Agents Chemother 50 (4), 1276-1281 (2006)
   PUBMED   16569840
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..446
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49415
     Region          12..430
                     /region_name="MATE_MepA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Streptococcus
                     aureus MepA; cd13143"
                     /db_xref="CDD:240548"
ORIGIN      
        1 meqtqqnhft alfyknvllg ilsmaaqsif iladtffian gigtealagl nivlplvnii
       61 nglgwmfgvg gatlfsttva qkeikkanqy fsltiglvfv igslftlasl ifsdqiirgl
      121 qgtgvlfgla keyymiylsc sllfilnncl itflrndhnp rlatiafvsg givniildyv
      181 fiyqfgwgma gaaiatvmsp ltslilitlh kwspqrvlrf ekfkvkfqdv reimsigfss
      241 flnefssafv mflfnivlln lvghvaisay aivanlniiv iaiftgigqg aqpllsryyg
      301 lgetkvlrkf vklsfitylv agflfflisq vftgqiievf nsegndqlaq iartairlya
      361 isflftglnf mgiyyfaavr kpkmalmiss lrgfflivpv lfilvkllgl tgvwlampvv
      421 efvtfglmlv gylayrnylk kreavt
//
LOCUS       WP_010712005             141 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HIT family protein [Enterococcus].
ACCESSION   WP_010712005
VERSION     WP_010712005.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..141
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16091
     Region          2..138
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mndcifckii ngeipsykvy edekvyafld itqvtkghtl mipkqhvadi feyndvlasd
       61 vfaripkvar alekafpeme glnilnnnke vayqsvfhsh vhlipryske ddfsihfgnh
      121 qkdysaeamq eiaetiakqv n
//
LOCUS       WP_010712034             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010712034
VERSION     WP_010712034.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..231
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26622
     Region          11..231
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mreirsensg iyaedisffy kknyfvledi nwkiengqcw gilghngagk ttlsylvlgl
       61 lkpskgvvhn yikkveylpe mggfyerltv renilfklel sgekqkskkl kqvlkefgli
      121 dyqfkrvdkl sqglkkrval amlflresea yyfdeptnal dpemkkklrq liihlkeagk
      181 iilinshdla fveeictnfl ilnngkvcfn epnigvnlee iylekvgghh e
//
LOCUS       WP_010712042             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010712042
VERSION     WP_010712042.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..222
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24654
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msnvlemkni ykkygekhte vialkelsfa vqpgefvavi gpsgsgkstf ltiaaglqap
       61 tsgevivggq slnkltkkqr laqrfqkigf ilqssnlvpf ltvedqfhli ekvdksrkns
      121 elkeqlletl glkelrnsyp rdlsggerqr vaiacalyhe pdviladept asldtekafd
      181 vvqllakeak ekdkgiimvt hderllkycd rvvrirdgel te
//
LOCUS       WP_010712045             406 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Fic family protein [Enterococcus].
ACCESSION   WP_010712045
VERSION     WP_010712045.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..406
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=47960
     Region          66..395
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mtykllkvdf yknrdsfekk yqerlnfdst lqtklfihpf dkeerktket yelfyvpllq
       61 hsvlqekimk nsqeimryih klpkivqkni ffyqlieeiq stneiegvks srkdiskvlh
      121 klnansterf qgivnmykgi vtdkmlkiet lgqfreiyde lfkadiqeed ypdgllfrks
      181 vvyisdkdkv vhqgssnees iiadleklil fmnqsalpsl lkccishyyf eyihpfydgn
      241 grmgrflmsn ylsrkldplt gltvsnavih nkikyekafs evtnprnrge vtlfvqtmye
      301 fillgqteil eelrtwtnql kratqwlkhs elpedecsvl flliqahmfr ngtesvsike
      361 iqenqnwsyg kvkritetle kqayiqvqgk kpktyritqq feetig
//
LOCUS       WP_010712061             321 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus faecalis].
ACCESSION   WP_010712061
VERSION     WP_010712061.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..321
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35500
     Region          1..248
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mdkirygims taqivprfva glresaqaev rgiasrrlen aqkmakelai pvaygsyeel
       61 ckdetidiiy iptynqghys aaklalsqgk pvllekpftl naaeaeelfa iaqeqgvflm
      121 eaqksvflpi tqkvkatiqe gglgeilwvq svtaypnvdh ipwfysreag ggalhgsgsy
      181 plqylqyvlg keiqavtgta tyqqgatdsq cnlalkfaeg tlgnifinvg lkipsemtic
      241 gtkgqivipn fwktdcayya daqgntvkws eqftseftye inhvnqclqd kkltspvmtk
      301 eltiatvkiv egfyqewfdn e
//
LOCUS       WP_010712086             211 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Enterococcus faecalis].
ACCESSION   WP_010712086
VERSION     WP_010712086.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..211
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=24038
     Region          25..191
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mkityplppn lpeqlplltn cqledeaile nhlyqqinls nqgvrnlvfr davfdhlsla
       61 ngqfasfdcs nvrfeacdfs nvewlsgsfh rvtflrcnlt gtnfadsylk dclfedckad
      121 yasfrfanfn lvhfnqtrlv eseffevtwk kllleacdlt esnwlntslk gldfsqntfe
      181 rltfspnyls glkvtpeqai ylasalglvi t
//
LOCUS       WP_010712094             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Enterococcus].
ACCESSION   WP_010712094
VERSION     WP_010712094.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..256
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29299
     Region          2..254
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mifdththln aeqfnddipe tiahaqelgv temavvgfde ptieksllls qeyaniysii
       61 gwhpteagsy tpeverrlqe qltlpkival geigldyywm edpkevqekv frrqiaiare
      121 mnlpfsvhtr ealedtyril kdekvsdigg imhsfsgdae wmkkfldlgl hisfsgvvtf
      181 kkaldvqeaa mavplermlv etdapylapv pyrgkrnepg ytryvvekia elrqltfeev
      241 aeqtrvnahr lfridk
//
LOCUS       WP_010712290            1196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PD-(D/E)XK nuclease family protein [Enterococcus].
ACCESSION   WP_010712290
VERSION     WP_010712290.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..1196
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=138917
     Region          4..1173
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 msvqfirgta vadleapliq atkqwleeda qhevfylvpn hikfeqeiqv lqklrqlqtt
       61 tsdsitstrl qvfsfyrlaw yylqhtpfys advlsdagaa mifrkilvea eeelqifrge
      121 inkpgfiqql fqlyqemreg nieiaelypf lekqtenpkg qdlqlkfqdl tliftrfqlq
      181 msqygyesae iiqhlseylq tvdlsnvqfv isgyqqftar elklievlma qagsvkvall
      241 ldkqyphdlp dprslfyeag qtyhqlyqla rqkqipilsd yvekkevlit npdlqglndy
      301 wiqsqehlpp lsttdwrgdg lflwraenvk eelthvatei rrlvveegyr ykeiqvltrd
      361 ldcyenllep ifaeheipvy vdrdmamdrh plvewieslf aihsynyryr dvlrflrtel
      421 fmpmnqlats eesltdwlnq rnawrrkvdi tenvvlaygy egyywsqekd wefirydfea
      481 eeqedvatme eesnairqsl qrllpsyfqa misaktglea atvfyhfllq sgvatqlkmw
      541 rlqaieagql etarnheqtw dalmslldey vtvygessfd fttfqeifvs gleglhyskv
      601 ptaidqvqvr amdltrpgaa kvtfaigmte eifpqkienk tllsdeerqt indtltenqy
      661 lrgttgrkia qepyvaylvf ssarerlylt ypsvkdtaqe vkpspyfkni qkdlnlpvfe
      721 knettifdde ttslahisty rtligeltrl krqrketqeg llpfwlnmek almnqsiapl
      781 akqvfeslth qnipekidev laeplygkdi ytsvsrmesf yrcqyqyfsr yglrlkerdv
      841 fglspaatge ffhealdqff kllimnqrnl seltdqevnl laeevlnsil gdarfsvltt
      901 ssrmnyiryq lsqtikkvsw alkrqsqrsg mttvqtevlf gqiaakkgis glelplknqg
      961 kihvrgkidr idqlvtpest ylgvidykss hrkfnmteay yglamqmlty ldvalmdavq
     1021 lvgqeakpag slylhvhnpt lsyegkddie qqmlkkyqfd gllmkdpdll dhldtslqak
     1081 qssllfpiee sakeqikpgr rqedkfvtep elgallshnr nkfieagnqi iggevqlnpa
     1141 yqgkeriacr ycpfrsvcdf dvmlkennyh rienlskeei marllnkdee gatede
//
LOCUS       WP_010712318             441 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: 2-hydroxycarboxylate transporter family protein
            [Enterococcus].
ACCESSION   WP_010712318
VERSION     WP_010712318.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..441
                     /product="2-hydroxycarboxylate transporter family protein"
                     /calculated_mol_wt=47114
     Region          7..441
                     /region_name="CitS"
                     /note="Na+/citrate or Na+/malate symporter [Energy
                     production and conversion]; COG3493"
                     /db_xref="CDD:442716"
ORIGIN      
        1 mekklhataa netdwrnklt ktrigsvtlp vylvtasiil vtalleqlpv nmlggfavil
       61 tmgwllgtig gnipilkhfg gpailsllvp simvffnlln qnvldstdil mkqanflyfy
      121 iaclvcgsil gmnrkilvqg lmrmivpmal gmilamgvgt lvgtllglgw khslfyivtp
      181 vlaggigegi lplslgygai tglpseqlvg qlipatiign ffaimcsgll srlgekrpel
      241 sgqgqlikit nsddlsdale edkapidvkl mgagvliact lfitggllqh ltgfpgpvlm
      301 ivvaaflkyl nvvpketqrg skqlykfisg nftfplmvgl gmlyiplkdv vgmlswqyfv
      361 vvisvvftvi atgffvsrfm nmnpveaaiv sacqsgmggt gdvailstan rmnlmpfaqv
      421 atrlggaitv itmtaifrml f
//
LOCUS       WP_010712325             277 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010712325
VERSION     WP_010712325.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..277
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31036
     Region          2..199
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mqleniskti dkkeiltnis itvepgeivg ligpngagkt ttmkimsgli vnfqgkvvgq
       61 erigvlidgp kyfpnrtare nlnyfralsk esysvdyves lfdmknygkk kvkdfslgmk
      121 qrlgmalali nknellilde pmngldpdgi qatiqtlkhl akelhigivi sshilgdldk
      181 lcdrayfikn gaiiqtvtlg kevsvyqftf deenedkvse isalfdgveq rhplwlisee
      241 dyplflkelv lndiiplemk khalnledvy fslvege
//
LOCUS       WP_010712344             702 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LTA synthase family protein [Enterococcus].
ACCESSION   WP_010712344
VERSION     WP_010712344.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..702
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=79901
     Region          16..638
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkklfktnil ntrlglfsli aillwlknlf ayavdfhlrl enineyfill inpiattvfl
       61 laialyvrrk kasyitmmii yflmslllfs nvvyyreftd fitvntmlga gkvasglges
      121 alrlfrpydv iyfldfiiig vllltkkikt darpvrarva vsvtllsvvf flfnlfmaet
      181 erpqllgrqf srdyivkflg lnaftvydgi ttyqtnqvra easandmkqv edyvkqqyaa
      241 pddskfgiak gknviyihle sfqqflvnyk lkdengvehe vtpfinslyn skstfsfdnf
      301 fhqvgqgkts daetllensl fgldqgslft qvggkntfea apdilkqtqg ytsaafhgna
      361 gnfwnrnety krlgydyffd asyydvnsdn sfqyglhdkp ffnqsvqyle hlqqpfyskf
      421 iavsnhypys qftndeagfp iaktsdetin gyfatanyld kaveeffnyl kssglyensv
      481 ivlygdhygv snsrnqnlae lvgktkadwn dfdnanmqrv pymihvpgqe nggvnhtygg
      541 qvdalptllh llgvdtknyi qlgqdlfskq hnqivafrng nvvtpkytil gssiydtktg
      601 tlitepteev kkeiadlkak atkqletsdq itngdllrfy tnsglkpvnp edydyknqlq
      661 qleaiekekg ekstsvyskn nnkstvdeyh tdsyqgyqkt gk
//
LOCUS       WP_010712426             593 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: V-type ATP synthase subunit A [Enterococcus].
ACCESSION   WP_010712426
VERSION     WP_010712426.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF003220.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK04192
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..593
                     /product="V-type ATP synthase subunit A"
                     /EC_number="7.1.2.2"
                     /calculated_mol_wt=64965
     Region          1..584
                     /region_name="NtpA"
                     /note="Archaeal/vacuolar-type H+-ATPase catalytic subunit
                     A/Vma1 [Energy production and conversion]; COG1155"
                     /db_xref="CDD:440769"
ORIGIN      
        1 mqigkivkvs gplilaenms dasiqdichv gdlgvigeii emrgdvasiq vyeettgigp
       61 gepvistgep lsvelapgli aemfdgiqrp ldtfqevths nflgrgvkid aldrekkwtf
      121 eptvavgeev sagdivgvvq etpiiqhkim vpfgvsgtiv eikagdfain etvysvetak
      181 gtesfsmmqk wpvrrgrpil eklspkvpmv tgqrvidtff pitkggaaav pgpfgagktv
      241 vqhqiakwad vdlvvyvgcg ergnemtdvl nefpelidpt tgeslmnrti liantsnmpv
      301 aareasiytg itiaeyfrdm gysvaimads tsrwaealre msgrleempg degypaylgs
      361 rlaeyyerag qvialgkdhr egsitaisav spsggdisep vtqntlrvvk vfwgldsqla
      421 qkrhfpsinw lqsyslyste vgqyldlelq gnwaamvaeg mrilqeesql eeivrlvgid
      481 slsdkdrltl etakslredy lqqnafddvd tftsrtkqak mlqliltfge egqkalslgt
      541 yfselmagtv eirdriarsk ylpeeelekl drlqaeiktt ikeiiaeggm tnd
//
LOCUS       WP_010712485             217 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            faecalis].
ACCESSION   WP_010712485
VERSION     WP_010712485.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..217
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24263
     Region          127..212
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 metvvrkrwl fgmqllgfli ldqiplmmvs vvqfstenfw frfvsglvav glgayfvylf
       61 vaflkkkkli twtflgiket lpvvllglvi ifcvgifgdf llrleglemt snqqsveeiv
      121 qsipkglili fagvigpife egifrvgiqa ffkpaskigi lvssilfalv htptdigsfv
      181 iywgmglals wvylrtgrfe aavlthfiwn vigilml
//
LOCUS       WP_010712577             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide deacetylase family protein
            [Enterococcus].
ACCESSION   WP_010712577
VERSION     WP_010712577.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..301
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34280
     Region          97..299
                     /region_name="CE4_SmPgdA_like"
                     /note="Catalytic NodB homology domain of Streptococcus
                     mutans polysaccharide deacetylase PgdA, Bacillus subtilis
                     YheN, and similar proteins; cd10944"
                     /db_xref="CDD:200569"
     Site            order(102..105,156..161,201,203..204,229,235..236,269,271)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:200569"
     Site            order(104..105,156,160,203..205,229,269,271)
                     /site_type="active"
                     /db_xref="CDD:200569"
ORIGIN      
        1 mrhkkrkfki ngyvlfsali livlvfiqtf lltqpkitsk nddtvqtltk nstakkdspt
       61 klekesthmt isskkyaysa dkirkyitge epykgeklvf ltfddgvnnq itpqvldtlk
      121 khnvhatffl vgntltsenq kivkrevaeg hsigfhssth dyatlypngi vnteeiqaei
      181 atmenslkki lgetfqttlw rypgghmswg gteksdelfk qlgihwidwn amvgdaepld
      241 rqpttvaeml afhqhslevy pdynirvvlm hdsvdkeltk qalpqliefy qangyqfgvl
      301 y
//
LOCUS       WP_010712725             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Enterococcus].
ACCESSION   WP_010712725
VERSION     WP_010712725.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..389
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43157
     Region          50..372
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mdkkqttdkr lswfwrwfln nqvvtalliv llvlliiltf tkvsylfkpv wqffgvvglp
       61 vimagilyyl lnpivdylek kqisrvwsii glfilivall iwggivivpk ireqsvsfvn
      121 hfpqyidtid qksqeilsdp lfaqfreqie aagdkvvssl gtiiknvstf tvqgignffg
      181 avatifvaii tmpfilfyll kdgknlapyl mkflpvkmrk ptlkvlaevn dqvssyirgq
      241 ltvafavaim fmigfsvigl dyavtlgiaa gflnlipylg sflamipavf lgivsgpall
      301 ikvlivfaie qtvegrfisp lvlgsqlsih pvtilvvllt sgklfgivgv ilgipvyaaa
      361 kviithifew yqivsglyde dkpdqqest
//
LOCUS       WP_010712654             439 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleobase:cation symporter-2 family protein
            [Enterococcus].
ACCESSION   WP_010712654
VERSION     WP_010712654.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..439
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46515
     Region          23..429
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 metkqlntpq qtetsngkaa vlglqhllam yagavavpll igtglnfdsq qmtylisidi
       61 fmcgvatllq ltvnkffgig lpvvlgcaiq avaplimigt nkgvgaiygs iiasgifvvl
      121 iagffskikr lfpplvtgtv itvigltlip vavekmgggl atdksfgdpk nlllafvtia
      181 liivvqvwgr gfiksiavli glvggtilaa flglvdlspv sqatwfhfpq pfyfgkptfd
      241 lssivlmiii sivsmvestg vyfalgditg kkigeddlrr gyhaeglavi lggifntfpy
      301 tgfsqnvglv qlsgiktrrp iyfsafflii lgllpkigam aqiipepvlg ggmlvmfgmv
      361 avqgmrmlsk vdysndknll iiaisigfgl gfnimptlfn kvpetvsmft gngivmssit
      421 aiilnllfng lketsesne
//
LOCUS       WP_010712762             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010712762
VERSION     WP_010712762.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..240
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27074
     Region          3..218
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnldylkety hltktesqil yyldqqstna adlsirevak hcfsspssii rlakklnlsg
       61 yneliyklke ahfsqpipfe tapsfettne fcqllakhks hlfvilghdf srhlaayise
      121 vfnfhgipsi ttahthsins qnnqnflfii lshsgeekyl ketallakek khpiisfvga
      181 knstlgrlad lvfstdsysp fstsvaqpqm ffgqtlitfe alicaylnhe dsipishknk
//
LOCUS       WP_010712730             648 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Enterococcus].
ACCESSION   WP_010712730
VERSION     WP_010712730.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..648
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73720
     Region          6..534
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          571..643
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 millqanqva rhfgsetlfe nihleiatks rialvgrnga gkstflkiia gidapdsgti
       61 aknktatlgy laqntglesd ktvwdemtka fadilemeqr mreletkise mepttsvyeg
      121 ilkeydqlqh tfsekngygy eneirsvlhg fgfdesfytk diqtlsggqk trlalarmll
      181 qkpdililde ptnhldietl swlesylpsy agallivshd ryfldkvvne vyelsrkkmt
      241 hykgnyskyl elkaeqlase wkayekqqee inkledfvak nlvrasttkr aqsrrkvlek
      301 mdrldrpqgd eksahflfds ekvsgnvvlq vedaaigydp ehilsepihl dirrkeaial
      361 vgpngigkst llksiidrip fikgsktfgt nvsvgyydqe qanlhgnktv laelwdehpt
      421 tpekeirsil ggflfsgddv ektipllsgg ekarvalakl amdrdnflil deptnhldid
      481 nkevlenali dyegtilfvs hdryfinria tkvvelsekg sklylgdydy ylekkqeeee
      541 iaallaneea akkpepvtak ntfyqnkeqq kllrtlqrki tqveenlaql dttiaqleaq
      601 msqpdilenh vellalnqql ddarqqqdel leqwenfsle leemennn
//
LOCUS       WP_010712782             191 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF805 domain-containing protein [Enterococcus].
ACCESSION   WP_010712782
VERSION     WP_010712782.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..191
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21695
     Region          14..>114
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mvkieekgkv tfgqafkdyf rgyvdfkgrt tragywwmtl vlsilalify iaivgkavsa
       61 ilaaeyfety dfgnllplml falvlwlall lptwamcvrr yrdagmtgwg vlvlyllsia
      121 csytqvfsvm stlkydvqtd tvitggspvf lfftlvislf fflltvlptd kltttsqnsv
      181 lrfffrykeg k
//
LOCUS       WP_010712830             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [Enterococcus].
ACCESSION   WP_010712830
VERSION     WP_010712830.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..245
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26676
     Region          3..242
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mkslsekviv imgassgige atarllakkg aklviaarrq erliaikkel peatilvqqa
       61 dvtkeeevqr vikltmekyg ridvlfnnag vmptapliea pkgewrqmld inimgvlngi
      121 aavlpimveq ksgqiiatds vaghvvypds avycgtkfav raimeglrqe qrenniksti
      181 ispgavqtel yqtisnrvva etlhleqlsw glkaediaqa vvfaidtpdr msisemvvrp
      241 ttqti
//
LOCUS       WP_010712834             669 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Enterococcus].
ACCESSION   WP_010712834
VERSION     WP_010712834.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..669
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=76534
     Region          24..649
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnykisylld eyagqkials laqqitdlsq relvtqlsai ggevqqntvs ipslsanewg
       61 kqlfqqrqvi yseaerqali flltyseiee lsvyhyqnfl dvskgtilad ikkvrhqlat
      121 enialsyerk rgfylegdef rirrfgknwl arllqqksgt falfcwlsqh qmsqyakmrd
      181 giqlavqeaq lqlvpsrlde isyflafsqk rlgkygtvvw penqliqslr aypvsrrils
      241 dlvgpvanve teslffticl mtalqgelrd tkleflldis geiirkmell avvqfeqpre
      301 llmnvyyhlv payfrinygf ylpnvlikdi rqsyrslyhl ceqalaplek ltkrsippee
      361 igfftilfgg eifgqkneqr qeklkalivc psgissslil qselrrlfpm iefketnavr
      421 eienvseksy diifstvpie takkvyltkp imssleknql mhqvqsdwll pgismpdvkd
      481 ildalkpyis lkkgvteaql yrvlhrkmnk ilekeedlrp mlsellttet vqvlpevadw
      541 ragiteaakp llkngsitek yidamiqkve sfgpfihicp dvalpharpe dgvnqlgmsl
      601 lkiqksvdll edpkheihlf iclaasdnet hlralssltk ilskkeslhr lvaaetvpei
      661 lsiiqegek
//
LOCUS       WP_010712900             903 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 65 protein [Enterococcus].
ACCESSION   WP_010712900
VERSION     WP_010712900.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 903)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 903)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 903)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 903)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..903
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=102236
     Region          118..902
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mtileltfat nqltttffnh kleplhqktf pfealtieet vpelcqlila eatpilggiv
       61 aefpadffsp eetlalfpqa viqafaeqln tplltaaeqa aapnlleafe ekrqylawhl
      121 dyygyvpgkn eyaveslltv gngflglrgt tpemtisddh ypatyiagly ntaasevagq
      181 vvenedfvna pdnqhialki gdatdwltis pdtlqqlhrq lnlktglfva emilkdadnq
      241 qiklttkkia nmaqpndyhl qytfeplnfs apitlktvtd gsvynynvar yrnltakhfq
      301 vtalsaqenk tvievctnqs nlsvretali tgdffekeai miqeeaekia qvvtvmahqg
      361 trytlekqvf vqashaeqsw qvpftpkdsf aaaaqesara wqtlwqqani tvtgdlmsqk
      421 llrihsyhll asaspfsnqa qaldvsitar glhgeayrgh ifwdeifilp fyiqhypdta
      481 kqlllyryhr lekakenaaa sqyrgamypw qsgrdgrett qklhlnplng hwgedhsilq
      541 rhvslaiayn awlywhstqd hefmkqygge mlleiaqfwn saatlddatg rffidkvmgp
      601 defhegypdq aesglknnay tnlmvvwlfe eltnilalfs eeeqaqlfak tqttsddlar
      661 mqqiqnslei evnsdgiiaq yegyfglkei dwtamkekyg niyrmdrilk aegespddyk
      721 vakqadtlml fynldktrvd qiledlgyql padyleknll yylkrtshgs tlsrivhaql
      781 aemaqfhels wqlyqealys dyrdiqggtt aegihtgvma atihvtlaty agvdtrqkel
      841 sicpnlpehw qalafqfihq gvtyqfsltq tsvtitadkd tqllvqgali pltaerpkev
      901 hyq
//
LOCUS       WP_010712948             457 aa            linear   BCT 01-JAN-2025
DEFINITION  vWA domain-containing protein, partial [Enterococcus faecalis].
ACCESSION   WP_010712948
VERSION     WP_010712948.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10076759
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..>457
                     /product="vWA domain-containing protein"
     Region          76..>203
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cd00198"
                     /db_xref="CDD:238119"
     Site            order(83,167,199)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238119"
ORIGIN      
        1 mfkkatklls tmvivagtvv gnfsptlala egvvkagdte gmtntvkvkd dsladckril
       61 egqaafpvqa getepvdlvv vedasgsfsd nfphvrqaid evvqglsdqd rvmltsyrgg
      121 kqfmfpdgkv kinsadydmn vrvdtqlthd ksqfvsgfgd vrtyggtpta sglklaldty
      181 nqthgdltnr ktyfllvtdg vantrldgyl hktntndsin eypdprhpfq vsveysndyq
      241 gaaaevlaln qeitnqgyem inaywesves lssvnsyfdk yktevgpfvk qelqqgsstp
      301 edfitsqsid dfttqlkqiv kdrlaqstpa tasltianqf diqsatatdd agndvpvqin
      361 gqtisatste gyvgnitihy evkentaida etlvssgtmn qgtiakefpe atipkndnah
      421 acdvtpedpt itkdienqeh ldltnredsf dwhvkta
//
LOCUS       WP_010712985              59 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010712985
VERSION     WP_010712985.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 59)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 59)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..59
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=6764
     Region          <2..52
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mgytqesfak eigiakttys syeqgyrnpt vqtakkmaki lqvpwtiffd eevletydf
//
LOCUS       WP_010713017             752 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Enterococcus faecalis].
ACCESSION   WP_010713017
VERSION     WP_010713017.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..752
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86034
     Region          235..723
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mqgnnlfnng llqpkkppig qeqqkmtryh qlrlvfglvg vllypfailg siplliglav
       61 dkrdkaanvf dmdyesflkr nsivflsfsa vlfvinvfaf ilwiprgyls ayllfplnll
      121 htalrfnwet ivalligssg mgaiflafss fvakrkvisk ederkkvtes keyknrqknk
      181 feesqrftde qekeyqeave svdidkykel snqlllgmse fglsyimnfs efnqhvlvpa
      241 ttgsgkttll qllvqhavkf nfpvilidgk gardtlesmr eiakfydkev haftddgdmr
      301 ynpvehgndi sirdklvsla etesvfysga akallqvtiq lldefkgakv tlsgdtrtte
      361 tverslpfvq rfllprnvlh lfadailpnn pklfeievek kiqkpkkksv kegseilpds
      421 dldkeekeed sqiknskfrn isqlgiaqke tetivlnpet ldldsyylll krnlrylptd
      481 ketgenikqk lferlfirye hkdspfylya tsealqtnin mlldselgkl fdtknaknvl
      541 dvqeivnqrk lvyvsfngli ykeyirtlaq mlvgdvnyfa semyrknvkr evlvifdepa
      601 sylnetfidm vnkgrgagvy giftpqtmad iaklgdklme qlvgnvntlf igktnekgea
      661 eywsetmgty qdidvtsvte qedgysdvgk sdwlgdrgtk rnvdrfkisp nkikelrtge
      721 fiiyrtaenv nlppqkvyvr nalewlqksn sk
//
LOCUS       WP_010713157             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010713157
VERSION     WP_010713157.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..239
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28257
     Region          1..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mnignslkmr rnelgltqse vaeklyvtrq tisnwennks ypnidcliel snlyemtldr
       61 llkedntmve klskdiregq kykklflill iivlciggyf tilqlrlnnl ysgvkewnqn
      121 gqtynliedn iqyhvvkidn ynlftipeel elmssyisen ekfnmyysgd dsnikiywtt
      181 galnglelsf dkefifdnvn qrnkfsyeiq elinknldkd kkeltilykq tknkweein
//
LOCUS       WP_010713211             443 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            faecalis].
ACCESSION   WP_010713211
VERSION     WP_010713211.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..443
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46398
     Region          28..438
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 msekkqnnlh ltvgpedsvs fgqatmlgiq hvlamdvyvv pviiasiigi staqtssliq
       61 atfiaaglat iiqshfcmrl pvaqgpsfip igaiagiyfa nnqqgngwga vlgaslvgai
      121 vviilgftgi fnrlitkfvp pivggtiifv vglslmpval sdniyhakge lgqnillafi
      181 aagtliffal lgsalkkgri frvssvilal lfgsiaaqll gvldlsavse aawfslpqlp
      241 lvnfsfqfdw saiatmlviy lvlmaettgt wfavshvvae plteekinrg vigeglgclv
      301 ssfiggtpvt systnagiis itgvasrkvf vaagawfvlf glsgklstli saipapvigg
      361 vfvvvcgiis vsgmkvmsdv tirekemyvi avpiimtlal tllpkeflet lpqflqylfs
      421 spvatasiva illqailpnv qeg
//
LOCUS       WP_010713363             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010713363
VERSION     WP_010713363.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..251
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29655
     Region          4..106
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(5..7,21,38..40)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(52,55,59..60,69,81,85,91,95,98..99)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          136..250
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mmeytikkma slsgvsartl ryydeigllq parinssgyr iygqaevnrl qqilfyreld
       61 lkldeikeil eqpdfnveqa lyehqqklle krneidrlla svqqtlhhyk geinmsdqqk
      121 feafkqqrvq eneekygkei rekygnetie qankkylnlt ekdmqvmqnv ekdlfsklam
      181 yqkspkltsq laqeifqlhk dwlmyswssy speahkwlgl myvgderfts yyeqhgagfa
      241 ealnaiiqny a
//
LOCUS       WP_010713364             184 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Enterococcus faecalis].
ACCESSION   WP_010713364
VERSION     WP_010713364.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..184
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20083
     Region          3..162
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mikkigifvg slrkdsfnkl vaktmadlfp adfepvfini gdlelynqdl ddegtpteaw
       61 ttfreevkqv dgvmfvtpey nrsvpavlkn aldvgsrpyg esvwdkkpgl vvsvspgais
      121 gfganhhlrq slvflnvptl qqpeayiggi tnligedgki idgtvgflqs ivdayvdffn
      181 rlta
//
LOCUS       WP_010713367             122 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010713367
VERSION     WP_010713367.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..122
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13611
     Region          1..115
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mefnfsgekp lfqqvadqia egifngayle geqipsttei sksyqinpat vlkgmnllve
       61 rqliekkrgi gmfvlpgaqe rvriarkeef lnkevlevva eakklgitae qlkqliergy
      121 ea
//
LOCUS       WP_010713368             427 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010713368
VERSION     WP_010713368.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..427
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46106
     Region          21..262
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          156..427
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mkfrdilksa stnlmrnkgr tvltiiaifi gaftialttg vnigvndyid kqvgsvggan
       61 qlfiqpkmem nvgngtepsk ynpekktsti qqqsmlaekd iekikkisdi tsvepmksva
      121 idyikgadkh kyvfsatsal demtidlaag rkvsqtsqdf einlspeyvk algytsskaa
      181 vgetvqlgis sslkgqeqvi eakivgvrnt sviqnglslm nkalidkvvs inqadlpehl
      241 knqyamiiae vkkdstpeqi kdikkdldka gylattvede igmirniina itgvltmfga
      301 iallaasfgi intlymsvqe rtreiglmka vglsngkvft ifsveaalig ffgsmlgilg
      361 avgvgnlvnr latdsflkal tgfkliqfsl psslmiilvi mfiaflagtl parraakldp
      421 ieslrye
//
LOCUS       WP_010712280             438 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Y-family DNA polymerase [Enterococcus].
ACCESSION   WP_010712280
VERSION     WP_010712280.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..438
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=49074
     Region          14..367
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(17..18,21..22,57,60,116..117,172)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(114,117,201..207,236,263..268,295,314,317..320,322)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mkfdyekeps rdilcidcks fyasvecaer gldplktmlv vmsnaenagg lvlsaspmak
       61 kvlgvsnvtr knqvpahpdl yvvpprmnly mkknqeinnl ykkfvadedh svfsvdesfl
      121 dvtaslsyfh cetaykmari iqrvvynhvg iyvtvgigdn pllaklaldn gakhspdfia
      181 ewrydrvpdt vwqlpsltdf cgigrrmakr lnrlgidsvy elaqanphll qetfgvmgiq
      241 lyahswgidr tflgkkaphk aeksfgnsqi lprdyarrdq ielvlkelte qvaarlrkah
      301 cqtecitvyv gyskgqidre grtgwrkqqt ipatnntkvl ityvlalfre hylagtdvrq
      361 lglsygklvw neslqldlfs epeeqiseme lnylidkirq kfgfqaliha ssllegatai
      421 hrsglvggha ggnvglgg
//
LOCUS       WP_010713549             140 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Enterococcus faecalis].
ACCESSION   WP_010713549
VERSION     WP_010713549.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..140
                     /product="VOC family protein"
                     /calculated_mol_wt=15978
     Region          5..135
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(5..7,23,61..62,65,83..88,90,94,123,133)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mlelyinfkg eakeaiafye dvfdtkcqnl mtfgeapedp ehpisdeikd lvmnasiiie
       61 gtyvmisdvp dmfgfevteg nnlslvvstd ddekidrlfk rlseggtvtm plsetfwskk
      121 ygslkdqfgi hwmfnyyeed
//
LOCUS       WP_010713578             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010713578
VERSION     WP_010713578.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..155
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18036
     Region          16..103
                     /region_name="HTH_GlnR-like"
                     /note="Helix-Turn-Helix DNA binding domain of GlnR-like
                     transcription regulators; cd01105"
                     /db_xref="CDD:133380"
     Site            order(18..20,34,51..53)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133380"
     Site            order(65,68,72..73,82,85,89,95,99,102..103)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133380"
ORIGIN      
        1 mwskmiqrll neenlligis elseiaevsp rqlryweekg yissiakdan gprkyrlhtv
       61 vkvhwikrfl degytlqsav ekaeeqyrnv gmtkkifsqm fhgisevcpn yvaidlgdfd
      121 eeqklyvvfn ettevseyll ipkdadvsde lkkrk
//
LOCUS       WP_010713609             311 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Enterococcus
            faecalis].
ACCESSION   WP_010713609
VERSION     WP_010713609.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..311
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33765
     Region          8..305
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mktkkssgmf aviaaliani lvaiskfvgf alsgstammn esihsvvdcs nqvlllfgnk
       61 rasrgqsalh qfgegrakyf fstivatmlf fgggalgvme aiqkllhpsh evenvaivig
      121 ilifgllveg sslrvamkei kelnteklsl lkflresrhs eiliiftedf caviglclal
      181 vgtlltmvtg iaafdaisgl liglllmcaa iflakefysl iigesvtatd lakiktafdr
      241 adveklidvk tvhlgpteil vaakidvvep meedapdvvn aierdirskm pdkkiyiyie
      301 vddydvnyvr k
//
LOCUS       WP_010713636             185 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010713636
VERSION     WP_010713636.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..185
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21043
     Region          18..>175
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mniklidvkv ltqknfflyq idfvefsske vsfiigksgv gkstllnila gehpyftgef
       61 vldekkvcld trkklisyrr sigyvhqdfq liewlsayen iayplkikki psqiikkqve
      121 klavelkite llhtrislls ggekqrvaia raiiknpeli ladeptgnld pdtskknney
      181 fipck
//
LOCUS       WP_010713668             831 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Enterococcus
            faecalis].
ACCESSION   WP_010713668
VERSION     WP_010713668.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..831
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92535
     Region          1..812
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mdelftesak avlaiaqeea kyfrhqsvgs ehlllalvle pngiagktlr qlntdtedir
       61 eeiehlsgyg tmqspmgnnn lylpysprak qifayagdea krlgaqkigt ehlllgllrd
      121 eeilasrilv nlglslskmr qlllkkmgvs epngaqrrrn gqnkntpqgt ptldslardl
      181 tklareqsld pvvgrgtevr rliqilsrrt knnpvlvgep gvgktaiaeg laqkivnrev
      241 pedmqgkrlm mldmgalvag tkyrgefedr lkkvvdeiyq dgqvilfide lhtligagga
      301 egaidasnil kpalargelq tigattldey qkyiekdaal errfariqva eptpeeaeei
      361 lkglrsryek hhgveitdea lhaavqlsir ylndrqlpdk aidlmdesaa kvrldkadqp
      421 seinelrtei sqlitekeea iqnqsfesaa rirqkekqvm ekleeliavk ekslsgystq
      481 vteedvagvv sqwtgvplqq lekkeserlm eletilhqrv vgqneaveav srairrarsg
      541 lkdparpigs fmflgptgvg ktelakalae amfgseeali rvdmsefmek ystsrligsp
      601 pgyvgyeegg qltekirqrp ysvilldeve kahpdvfnil lqvlddghlt dakgrkvdfc
      661 ntilimtsnl gataireekh vgfnvkdisk nhelmqkrim eelkkafrpe flnridetvv
      721 fhslkqeeih eivkimsqsv vkrmaeqevk vkitpaaiev igkvgfdpey garpirralq
      781 kevedrlsea llsgqiqlgd kvtlgaskgk itlnvrapka pkteakelqt v
//
LOCUS       WP_010713696             337 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus faecalis].
ACCESSION   WP_010713696
VERSION     WP_010713696.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..337
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37746
     Region          79..336
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkrkivrfil wllgiivvic lgvflafqls pkpgawvinq lfageveikd sasydkalpn
       61 vqlqenqtyp ssrkkntfdl yypqtskqav pvvlwvhggg yvggdksgmk efatrlvads
      121 svafismnye lapdapypsq lqqvdelvqf llekkqaypm ldlsklfigg dsagaqialq
      181 yatvqtntny akelgmtaal panhlkgtls ycgpvdlkqm anqqsdnrfm kffvktvaws
      241 llgtkdwqts aelqevslvd kvtkefppty ltdgnsfsfq eqglalvqrl ktlnvpvsal
      301 ffkdkkatit heyqfdyqtk eakqcyqetv qfvntyk
//
LOCUS       WP_010713768             221 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Enterococcus].
ACCESSION   WP_010713768
VERSION     WP_010713768.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..221
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25757
     Region          134..208
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mkimvitkni lsetafqnrl qhldhqvfct tcligeikes hlfyrkfdai ilsetiprke
       61 qylylkelar vktplflrse diptseelsi syqygilnwl rldatldtlr enlllaelnk
      121 piqredekld vegikltate rallavlyst pkehlpmerl ckliydteet annrkkmtkq
      181 ltklnkkiqv ggfkkqgiqn trykgyklhp qllpyigelf t
//
LOCUS       WP_010713901             505 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease/substrate-binding protein
            [Enterococcus].
ACCESSION   WP_010713901
VERSION     WP_010713901.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..505
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55928
     Region          2..208
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          236..499
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(242,244,292..293,296,339,341,419,443)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mqalietffa rkeeylqali ehmqlsfisl lfaaliaipl aiyltshrkl aesllqvtgi
       61 fqtipslall gllipligig rppaivalvi yalfpilqnt ytglteidps leeaaeafgm
      121 skkeklfkfe iqmalpfiis girtatvlii gtatlaalig agglgtfill gidrnnlsli
      181 figalssaal avlfnygihw lekangrrli iggtilglll ggsffwnqqt sskekqltia
      241 gklgaepdii inmykaliee nsdiqvtlkp nfgkttflyn alksdeidly peftgtviet
      301 flknppqldn qpqvvyeaar aglkkqenlt llkpmryent yavavkrsfa kahqlktisd
      361 lqkisnqlka gftlefidrq dgykglqeky hlnlnvqsme palryqainn gevnvidays
      421 tdselrqydl vtleddqalf ppyqgaplik tatlekypel aeilnklagk iseeemsemn
      481 yqvnvegqdp sivakdylke knllk
//
LOCUS       WP_010713959             532 aa            linear   BCT 01-JAN-2025
DEFINITION  terminase large subunit [Enterococcus faecalis].
ACCESSION   WP_010713959
VERSION     WP_010713959.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..532
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60231
     Region          17..531
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mplkkykptk fkeksskydk dladyavnfi eclshtkgtw agkpfelldw qeqiirdlfg
       61 tvkpngyrqf ntayieipkk mgkselaaav allltcgdge eraevygcaa drqqasivfe
      121 vaadmvrmcp alnkrvkila sqkrivfkpt nsfyqvlsae ayskhgfnih gvvfdelhtq
      181 pnrklfdvmt kgsgdartqp lyflittagt dtnsicyeth qkaldiidgr khdttfypvi
      241 ygadesddwt dpkvwkkanp slgvtvgidk vkaacesakq npaeensfrq lrlnqwvkqa
      301 irwmpmdkwd acgfkvaeks legrvcyggl dlssttdits fvlvfppede ddkfvilpyf
      361 wipeetldlr vkrdhvpydl wekqgwlktt egnvvhygfi etfieelgqk ynireiafdr
      421 wgavqmvqnl egmgftvvpf gqgfkdmspp tkelmkltle qkiahgahpv lrwnmdnifi
      481 rtdpagnika dkekstekid gaiatimald raircgnnia asvyddrgll fl
//
LOCUS       WP_010713965             121 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Enterococcus faecalis].
ACCESSION   WP_010713965
VERSION     WP_010713965.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..121
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14054
     Region          45..108
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mpmkpakpck ypgcphltha dyceehrlla rkryekyerd petnkrygra wkkiraryva
       61 ahplcemcqa egrltsteiv hhikelsegg thdfsnlmsv ckschsrihm trmntkdkti
      121 l
//
LOCUS       WP_010714000             377 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010714000
VERSION     WP_010714000.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..377
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39544
     Region          1..356
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mnnrsekirn ilvpvlsvim gfllgaiimv ifgydpvagy qamfetafqg kksigeifvt
       61 aapliftalg fsvansagff niglsgqalc gwvasiwval smpdaprmiv lpvaiivgav
      121 agalaaaipg flrayfgtse vivtimlnyi llytgnhian nvmkpsiman kgitkmigan
      181 aslrspflts isdgsrlnig iflafiflil vwflmkkttl gfeirsvgln pfaseyagms
      241 skrtiilsmm isgtlaglgg avqglgtfqn ffiqntslsi gfdgmavsll gagssigill
      301 sallfgmlkl ggqgmpliag vptelvdvvi aaiiffvgis ylirfllaka sgskkevaiv
      361 etieaapdkn nqeggdi
//
LOCUS       WP_010714234             205 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecalis].
ACCESSION   WP_010714234
VERSION     WP_010714234.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..205
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23773
     Region          3..132
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,63..64,67)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(62,113..114,116..117,121)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(68,73..74,109,112..113,116..117,120,123)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,96..97,109..110,113..114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(122,128..129)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 makigyarvs skeqnldrql qalqgvskvf sdklsgqsve rpqlqamlny iregdivvvt
       61 eldrlgrnnk eltelmnqiq fkgatlevln lpsmngiede nlrrlinslv ielykyqaes
      121 erkrikerqa qgieiakskg kfkgrqhkfk endprlkhaf dlflngcsdk eveeqtginr
      181 rtfrryrtry nvtvdqrknk ekrgs
//
LOCUS       WP_010714498             106 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein, partial [Enterococcus faecalis].
ACCESSION   WP_010714498
VERSION     WP_010714498.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..>106
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          12..>104
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(14,16,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            16
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mhfrfyvpct pysrvstsnq dyktqirkle eagaekifse kytgtkkegr keleellsiv
       61 kagdkvlvtk idrlarsivd lnsiisalnh kgvtisfldd hltfep
//
LOCUS       WP_010714650             752 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Enterococcus faecalis].
ACCESSION   WP_010714650
VERSION     WP_010714650.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..752
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85930
     Region          235..723
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mqgnnlfnng llqpkkppig qeqqkmtryh qlrlvfglvg vllypfailg siplliglav
       61 dkrdkaanvf dmdyesflkr nsivflsfsa vlfvinvfaf ilwiprgyls ayllfplnll
      121 htalrfnwet ivalligssg mgaiflafss fvakrkvisk ederkkvtes keykdreknk
      181 feesqrftde qeeayeeave tvdidkykel snqlllgtse fglpyiinfs efnqhvlvpa
      241 ttgsgkttll qllvqhavkf nfpvilidgk gardtlesmr eiakfydkev haftddgdmr
      301 ynpvehgndi sirdklvsla etesvfysga akallqvtiq lldefkgakv tlsgdtrtte
      361 tverslpfvq rfllprnvlh lfadailpnn pklfeievek kiqkpkkksv kegseilpds
      421 dldkeekeed sqiknskfrn isqlgiaqke tetivlnpet ldldsyylll krnlrylptd
      481 ketgenikqk lferlfirye hkdspfylya tsealqtnin mlldselgkl fdtknaknvl
      541 dvqeivnqrk lvyvsfngli ykeyirtlaq mlvgdvnyfa semyrknvkr evlvifdepa
      601 sylnetfidm vnkgrgagvy giftpqtmad iaklgdklme qlvgnvntlf igktnekgea
      661 eywsetmgty qdidvtsvte qedgysdvgk sdwsgdrgtk rnvdrfkisp nkikelrtge
      721 fiiyrtaenv nlppqkvyvr nalewlqksn sk
//
LOCUS       WP_010714054             512 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus faecalis].
ACCESSION   WP_010714054
VERSION     WP_010714054.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..512
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57819
     Region          6..509
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msiltiehlt hrfgekvlye easlqvnkgd hlgltgqngv gkstlikilt gevlpdegti
       61 qwqknckigy ldqhvsveqs ltmvdflkqa fqelfdkeak ltklyeeysq taseklleqa
      121 gklqtdldes nfyqidtiiq dlanglglqa igldkklgel sggqrskvil akllleapdv
      181 llldeptnyl ddthiqwlvr ylnnfegsfl lvshdyqfln evtnciadie fgkltkytgn
      241 veksfaqkeq nkqtylkqyq aqqekiekme ayirkykagn ratmaksrqk qldrlerltp
      301 pgsltkpaie fpyqglvatq alttqklvvg yrepllepld lmvhvgekva lkgfngigks
      361 tliktltkvi psldgefhyp lntkiayftq dlawpneqlt pldylsdrfp dttikerrsh
      421 laraglpdkl amqslallsg geqtkvklae lmmqtsnllf ldeptnhide aakkslqeai
      481 rvypgtvflv sheadfyeei vdrvidieel vk
//
LOCUS       WP_010715111             311 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FAD:protein FMN transferase [Enterococcus].
ACCESSION   WP_010715111
VERSION     WP_010715111.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..311
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=34548
     Region          10..302
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mqqsqtiylm gtvidvfvdh eepekileev hqrlityeqr fsandstsel mavnqqagkk
       61 pvsvhpelyq lialgkkhsc dpashlnvti gplvqtwrig fkdarvpsek eikaclkkin
      121 pekihlnplk qtvfleeegm kldlgalakg yiadllityl kevhvtsali nlggnivtlg
      181 psthqnkkwr igirnpqesr etisllveva nqsvvtsgiy erslteagrv yhhlldpttg
      241 ypletemasi tiisdasvdg eiwttrlfgy pipealeiln qldgiegvii tqdqqilyss
      301 gladtlhiih s
//
LOCUS       WP_010715165             700 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase
            [Enterococcus].
ACCESSION   WP_010715165
VERSION     WP_010715165.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 700)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 700)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 700)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..700
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75111
     Region          1..>49
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          89..692
                     /region_name="P-type_ATPase-Cd_Zn_Co_like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     Bacillus subtilis CadA which appears to transport cadmium,
                     zinc and cobalt but not copper out of the cell; cd07548"
                     /db_xref="CDD:319847"
     Site            order(354,356,654..655,676,680)
                     /site_type="other"
                     /note="putative HM ion binding site [ion binding]"
                     /db_xref="CDD:319847"
     Site            order(398..400,459,475..477,498,539..541,561,564,567,589,
                     592)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319847"
ORIGIN      
        1 mqksyklegl dcascadkie ksvqkihgve karvdfmaek mtlevesghd levenearav
       61 igklepdvkv islkdvkeee grnpnnnrli riiiafvlfl aliiikpsnn wvalasylvv
      121 yvliggdivk ravtnifrge vfdenflmsv atigaffige ypeavavmlf yqvgewfqsa
      181 avdqsrksia klmdirpdsa nllvngqika vapdtieigq qilvkpgekv pldgqiidgs
      241 smvdtsaltg esvprtvkvg deilggfink ngaltinvtk kfgdstvski ldlvenassk
      301 kapaenfisk faryytpvvv vlavllavip pfifpdtsin ewvyraltfl viscpcalvi
      361 svplsffggi ggasklgvli kgsnyleila ntetivfdkt gtltkgnfvv qnitsvvlpe
      421 eellrltata eqlsthpiai sikesygket vpataieeva ghgikatieg ktvlvgnakl
      481 mkqfgieape vkeagtlifv aidnqfagyl viadqlkpda isaikelkae gvkqtvmltg
      541 dnqqvaeaia kevgvdkvya ellpdgkvdr leellkassp knkvafvgdg mndapvlara
      601 dvgiamgglg sdaaieaadv vimndepsri asaiklsrkt lrivkqniif aiavkiivlv
      661 lgalglasmq aavfadvgvt iiavlnamrc lrvekmkdnn
//
LOCUS       WP_010715169             420 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010715169
VERSION     WP_010715169.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 420)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..420
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45839
     Region          1..409
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
ORIGIN      
        1 mskfwiiatd vykknvksls flimilapfl lvgivylags lasgfsgdtt iglvsenqal
       61 vkeltknkte dfsfkavsse kkaqeqlkde kidayllldt tdnqisgqly serslgnate
      121 mlipqmlnql qtmananrln ltaeqvamln qqatfkkaki sfdengkikt gedntgiqma
      181 lamgitillf vfissyssii aqeiasekgt rimevilsst kaqthfygkl tgvilvaltq
      241 ifiygvafvl gysqlknldf mksllsgisp qnifsstfif tlgffiigil vfavlaalcg
      301 slvskpedta kavqpimyig ligymigitf gtndpqnivv kvtsfiplis syimpvrlat
      361 etastmeaiv slvilavfgi iltifsarly ksnvlvyseg gmiqslkqsi silkneqkhk
//
LOCUS       WP_010715189             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptidylprolyl isomerase [Enterococcus].
ACCESSION   WP_010715189
VERSION     WP_010715189.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..249
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=27121
     Region          64..246
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mkhkkmlava svaaftllla gcnttnnkst tatsdsiaks sesktkdsvd lnsldlpqld
       61 dkvaedqdlv qmvtsmgnie iklfpkqapk tvenfmkhak dgyydgltfh rvinnfmiqg
      121 gdpsgdgtgg nsiwnkpfed efsnqlynir galsmanagp ntngsqffiv qntddqsdgl
      181 lyddypkaii daykkggyps ldkkhtvfgq vtkgmdivdk iakvevgand kpktdvkiek
      241 inilqeakk
//
LOCUS       WP_010715201             168 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: shikimate kinase [Enterococcus].
ACCESSION   WP_010715201
VERSION     WP_010715201.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..168
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=18869
     Region          4..168
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 mesivligfm gagkttigqs lanklkmphl dldtalieki grsipdyfek ygeaafreqe
       61 tqllkelskn tavlstgggi vvgpenrsll ksfqqviylh atpeellkri tedtenqrpl
      121 aiersskeii tlfesrksfy eecakmtidt tnrspeeiih eilqqlke
//
LOCUS       WP_010715228             217 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010715228
VERSION     WP_010715228.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..217
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24197
     Region          127..212
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 metvvrkrwl fgmqllgfli ldqiplmmvs vvqfstenfw frfvsglvav glgayfvylf
       61 vaflkkkkli twtflgiket lpvvllglvi ifcvgifgdl llrleglett snqqsveeiv
      121 qaipkglili fagvigpife egifrvgiqa ffkpaskigi lvssilfalv htptdigsfi
      181 iywgmglals wvylrtgrfe aavlthfiwn vlgilml
//
LOCUS       WP_010715236             427 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010715236
VERSION     WP_010715236.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..427
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46076
     Region          21..262
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          156..427
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mkfrdilksa stnlmrnkgr tvltiiaifi gaftialttg vnigvndyid kqvgsvggan
       61 qlfiqpkmem nvgngtepsk ynpekktsti qqqsmlaekd iekikkisdv tsvepmksva
      121 idyikgadkh kyvfsatsal demtidlaag rkvsqtsqdf einlspeyvk algytsskaa
      181 vgetvqlgis sslkgqeqvi eakivgvrnt sviqnglslm nkalidkvvs inqadlpehl
      241 knqyamiiae vkkdstpeqi kdikkdldka gylattvede igmirniina itgvltmfga
      301 iallaasfgi intlymsvqe rtreiglmka mglsngkvft ifsveaalig ffgsilgilg
      361 avgvgnlvnr latdsflkal tgfkliqfsl pssltiilvi mfiaflagtl parraakldp
      421 ieslrye
//
LOCUS       WP_010715263             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ComF family protein [Enterococcus].
ACCESSION   WP_010715263
VERSION     WP_010715263.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..228
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=26953
     Region          41..228
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mdckncaspi rleitlkmll rfkkwarpsl cqhcqakfqk lpmtgtcfgc grvsqeyycl
       61 dcrrwqllyp eysfhnaalf hydegmqewm erykfqgdyr lrmcfneein fyfqqqsady
      121 iipvplsekr mqergfnqvi glleaadvpy spflirkeen vpqskktrke rmqlqqpfai
      181 qkenqeklkn csiilvddiy ttgrtlfhaa avindcypks lntftlar
//
LOCUS       WP_010715289             640 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Enterococcus].
ACCESSION   WP_010715289
VERSION     WP_010715289.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..640
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71416
     Region          326..515
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mklsikkffe vflessways rpiltfdtrq nwfalvlsii ianavgavlt ivfpfafvlv
       61 nvgsflgtvi cvlprhgppq rsaingilmi figaslgill qsssifiill fvlglyfsgi
      121 vrnfsiglyi rclfgtisll agaqlkgnls igqsfeglga iilgmsilcl iyclyskpqn
      181 nearklvadl yeqlyllaqg kparyvhfri kvresvetmp wvnhqktpwi yplvsqadai
      241 agsldstnaa enlpalkail lflkgeqltf plqefalant eiksailliq nkqsfkkisf
      301 ksflptkegl aeakeilhsy kgssarfair laltglvchf cslilnymyp lplanhefwv
      361 visgclmvmp gyhgtlgkit srtigsilgg clgiflsqli anltnlnplw pmllscllvi
      421 lyetvrklsq aflmlsvttw ltftlggssa gytrvfdvii galiafvmff ifptwhsqvl
      481 rkninswskt issillalin eettlpsdaw vlayrvqrrv nysiqeivle spiysndasa
      541 eslmqqkqln dqllemqtam eelllelmkt qhylkklapv kpdtlntell nysqqilslt
      601 npqnnrlinq skqsiyfpqi eqslvilkns tanfflanik
//
LOCUS       WP_010715329             512 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Enterococcus].
ACCESSION   WP_010715329
VERSION     WP_010715329.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..512
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57784
     Region          6..509
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msiltiehlt hrfgekvlye easlqvnkgd hlgltgqngv gkstlikilt gevlpdegti
       61 qwqknckigy ldqhvsveqs ltmvdflkqa fqelfdkeak laklyeeysq taseklleqa
      121 gklqtdldes nfyqidtiiq dlanglglqa igldkklgel sggqrskvil akllleapdv
      181 llldeptnyl ddthiqwlir ylnnfegsfl lvshdyqfln evtnciadie fgkltkytgn
      241 veksfaqkeq nkqtylkqyq aqqekiekme ayirkykagn ratmaksrqk qldrlerltp
      301 pgsltkpaie fpyqglvatq alttqklvvg yrepllepld lmvhvgekva lkgfngigks
      361 tliktltkvi psldgefhyp lntkiayftq dlawpneqlt pldylsdrfp dttikerrsh
      421 laraglpdkl amqslallsg geqtkvklae lmmqtsnllf ldeptnhide aakkslqeai
      481 hvypgtvflv sheadfyeei vdrvidieel vk
//
LOCUS       WP_010715361             399 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent aminotransferase
            [Enterococcus].
ACCESSION   WP_010715361
VERSION     WP_010715361.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..399
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43899
     Region          1..394
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,206,235,237..238,246)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,199,244..246,275,278)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            238
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mnvsnraqql tpsvtlaaaa kakalkakgv dvlsltvgep dfvtpkniqk aaiasiedgr
       61 asyytpsggi pelkqaivsy vereyqlryq pkqvivtdga kyalyllfqa ilnvgdevii
      121 pvpywvsyge qvklaegkpv fvsstqeqsf kvsvaqletv rtdktkaiil nspsnptgvi
      181 yteeelrqig ewavahdili iaddiygrlv ynghrftpia tiseairqqt iiingvskty
      241 amtgwrigfa vgdekiiqam tqlasqstsn pvavsqyaai ealtgeqstv edmrqafekr
      301 lnhiypkvaa lpgvslikpe gafylfpnvk ktleicgydn vtnwvedllq eahvalvtge
      361 gfgapehvrm syatdlmtle kaiermndfi ekkriqhna
//
LOCUS       WP_010715420             296 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [Enterococcus].
ACCESSION   WP_010715420
VERSION     WP_010715420.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..296
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31718
     Region          1..285
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mskigfigtg vmgksiirnm mknnlsvnvy nrtksktddl vaegavwydt pkaiaeasdi
       61 iftmvgfpsd vegvyfnetg ifqadltgki vvdlttstpt laekiakkaa evgahaldap
      121 vsggdlgakn gtltimvggd qesyetvlpi fktfgktfml hgsagkgqht kmanqlmiag
      181 tmtgltemlv yanatgltle kvletvgggs aanwslsnyg prilkedytp gffvkhfikd
      241 lkialdeakk ldltlpatqk atelyeslad kgfendgtqa liklwwtdgk qptnkn
//
LOCUS       WP_010715452             419 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Enterococcus].
ACCESSION   WP_010715452
VERSION     WP_010715452.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45451
     Region          5..412
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtdktkssla ywkkivillc mgwviiwiyr salspvypqi raslngnasd talgsissfy
       61 flgyvvmqip agflvdkigk krvlipgfil ftlaalliaq aqtigtiylg sllaglgcgs
      121 fygsayslts qnipqakksf ataivnsgsa vgsglgmils sylvaqkglp wqvmmyisaf
      181 miicmlvafq viirnhkedm aliqptvvde kdneavkekv pfkklfaphm lfayilyfgt
      241 cyayymivtw lpnflsterg fqgaaiglss slvafasipg alffsrladk ymhkkvqfiv
      301 vleflataml lltvqvsnat lllialimyg flgklavepi iiswlgenap kigigttlgv
      361 fnffgmmssv iapaltgkis dttgskvmgf yiavvillig tilfmlvnlk krgadssnk
//
LOCUS       WP_010715617             319 aa            linear   BCT 01-JAN-2025
DEFINITION  aromatic acid exporter family protein [Enterococcus faecalis].
ACCESSION   WP_010715617
VERSION     WP_010715617.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10532842
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..319
                     /product="aromatic acid exporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36149
     Region          1..141
                     /region_name="ArAE_1"
                     /note="Aromatic acid exporter family member 1; pfam06081"
                     /db_xref="CDD:428756"
     Region          147..307
                     /region_name="ArAE_1_C"
                     /note="Putative aromatic acid exporter C-terminal domain;
                     pfam11728"
                     /db_xref="CDD:432028"
ORIGIN      
        1 mkiglrtvkt aisaalamii aeklgllyap sagiisvlsv tstkktsvmt giyrllslal
       61 atilayicft flgftaiafg iflllfipaa vyfqlsdgiv vssvlvthyl veknlswaii
      121 gnefllmsig vglallansy mpdtekrlre dqevietmfr kilremalhl nnaagernlv
      181 mhcadlktfi rtgetwaknh aenqllstnt yyleyfamrk mqsnilkkml elleditvda
      241 qqvryiqqll eytaetfaen ndgqeimnri ktvyetyrtk plpqtrsefe nrarlfqflq
      301 lfqsfiqvka dfaklqldk
//
LOCUS       WP_010715691             128 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Enterococcus
            faecalis].
ACCESSION   WP_010715691
VERSION     WP_010715691.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..128
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=14891
     Region          8..113
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 msdekkyipk kgdivwidfd psaekeiqkr rpglvvsrye fnrktlfavi cpitstiknm
       61 ptrytlpdem ethgqvvisq lksldfaerk lsqiehlplk dmakidqiie yifwfcckvl
      121 nllsnkve
//
LOCUS       WP_010715764             129 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase, partial [Enterococcus faecalis].
ACCESSION   WP_010715764
VERSION     WP_010715764.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..>129
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
     Region          2..127
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(6,23,28,58,93,99,112)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(8,15,45..47,65,94..97)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mtlsiivahd kqrvigyqnq lpwhlpndlk hikqlttgnt lvmarktfns igkplpnrrn
       61 vvltnqasfh hegvdvinsl deikelsghv fifggqtlye amidqvddmy itvidgkfqg
      121 dtffppytf
//
LOCUS       WP_010715869             295 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein, partial
            [Enterococcus faecalis].
ACCESSION   WP_010715869
VERSION     WP_010715869.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         <1..295
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
     Region          192..243
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(213,215..217,219,230..231,235..236,239,243)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 flgitlkmvk knhrfvcysh valkarkrik rqlkdqikri qrkkskitti reiqkynsmv
       61 igihnyynva thvskdfesi gsqlhrsfyn rfrnkgltkk gnykghdkgi lpymeskriq
      121 ylvnypilpi gfvrtktikg rnktlnkytp egrilvhknq qsvaewkvqw lrehpiiner
      181 atieyndnri slfiaqkgkc aitgnelfld dmhchhkklw seskddsykn lillskemhk
      241 lvhctdevki reyiywnkls dsqvnkvnkl rklvnktiil plceqmpkye qltlf
//
LOCUS       WP_010715917             178 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein, partial [Enterococcus faecalis].
ACCESSION   WP_010715917
VERSION     WP_010715917.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..>178
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          12..138
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(14,16,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            16
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,119..120,122..123,127)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,115,118..119,122..123,126,129)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(100..102,115..116,119..120,123,127,130,134)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(100,120,123,127,130,134)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(128,134..135)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mhfrfyvpct pysrvstsnq dyktqirkle eagaekifse kytgtkkegr keleellsiv
       61 kagdkvlvtk idrlarsivd lnsiisalnh kgvtisfldd hltfepdkkd smqtlmmnml
      121 gsfaqferdl ivtrtqegkq whrannknyr egrpkrvlnd kykhalelme tnsmreve
//
LOCUS       WP_010716137             303 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterococcus faecalis].
ACCESSION   WP_010716137
VERSION     WP_010716137.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..303
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34626
     Region          21..295
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 meknelslki inefrnvlrr pltitvansk ggvgkttiir ylsyvlsrlg fkvlvvdadp
       61 qanttktmll tknyysedei fivektmmag ivekdlsklv ipiienlyci pshidfknfp
      121 kyltrlygds ieglddnyke ieskrisvlr dlikpikady dfvlidtppt msdftrnaay
      181 asdymimafq tqpdsldgvt dyineeltpl mkdfdletei vgilpnhlsk gsidttvvnd
      241 aielfgeenf fnniipftkr vqttprtgln tdtywdekay nevfeplaln flerilmfek
      301 gen
//
LOCUS       WP_010716181             143 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus faecalis].
ACCESSION   WP_010716181
VERSION     WP_010716181.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15743
     Region          4..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msvyqhilva ldgsdqseka fheavriake eqatlylati indaefttsp fsfeelydle
       61 khkleemltg kakqaseigv ktvkkivelg spkrylanti senyaidliv lgatgrdaiq
      121 rtligsttdy vvnhalcnvl vvr
//
LOCUS       WP_010716315             261 aa            linear   BCT 01-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Enterococcus
            faecalis].
ACCESSION   WP_010716315
VERSION     WP_010716315.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10053807
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..261
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31537
     Region          16..83
                     /region_name="HTH_ARSR"
                     /note="Arsenical Resistance Operon Repressor and similar
                     prokaryotic, metal regulated homodimeric repressors. ARSR
                     subfamily of helix-turn-helix bacterial transcription
                     regulatory proteins (winged helix topology). Includes
                     several proteins that appear to...; cd00090"
                     /db_xref="CDD:238042"
     Site            order(17..19,33..35,48..51,53..54,57..58,60..61,67..69,
                     74..76)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(33,36,83)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mkpllynyyi dytkkdktrl iilcllhelr visvqqlidf fqiehiakks svyknlkllk
       61 edglidrski gmpkfyyltk eghnyiggyy tlpkvpeynl qhhlqindyl ikmlelcnkh
      121 phlkavvser rkvyevkdek knqkgvkyfv pdfifmflds igrevewqfe ieltlktkrr
      181 ysqgvfpkyi khlknyedar liyvtpssii keeldmfkey fidkegdeyk evfdrlhvfs
      241 aeefeselkr llekdkfinw e
//
LOCUS       WP_010716472             775 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Enterococcus faecalis].
ACCESSION   WP_010716472
VERSION     WP_010716472.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 775)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 775)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 775)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..775
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..775
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=88530
     Region          258..746
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mqgnnlfnng llqpkkppig qeqqkmtryh qlrlvfglvg vllypfailg siplliglav
       61 dkkdkaanvf dmdyesflkr nsivflsfsa vlfvinvfaf ilwidvcssd fsavlfvinv
      121 fafilwiprg ylsayllfpl nllhtalrfn wetivallig ssgmgaifla fssfvakrkv
      181 iskederkkv teskeyknrq knkfeesqrf tdeqekeyqe avesvdidky kelsnqlllg
      241 tsefglpyii nfsefnqhvl vpattgsgkt tllqllvqha vkfnfpvili dgkgardtle
      301 smreiakfyd kevhaftddg dmrynpvehg ndisirdklv slaetesvfy sgaakallqv
      361 tiqlldefkg akvtlsgdtr ttetverslp fvqrfllprn vlhlfadail pnnpklfeie
      421 vekkiqkpkk ksvkegseil pdsdldkeek eedsqiknsk frnisqlgia qketetivln
      481 petldldsyy lllkrnlryl ptdketgeni kqklferlfi ryehkdspfy lyatsealqt
      541 ninmlldsel gklfdtknak nvldvqeivn qrklvyvsfn gliykeyirt laqmlvgdvn
      601 yfasemyrkn vkrevlvifd epasylnetf idmvnkgrga gvygiftpqt madiaklgdk
      661 lmeqlvgnvn tlfigktnek geaeywsetm gtyqdidvts vteqedgysd vgksdwsgdr
      721 gtkrnvdrfk ispnkikelr tgefiiyrta envnlppqkv yvrnalewlq ksnsk
//
LOCUS       WP_010716601             109 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein, partial [Enterococcus faecalis].
ACCESSION   WP_010716601
VERSION     WP_010716601.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..>109
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          12..>104
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(14,16,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            16
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mhfrfyvpct pysrvstsnq dyktqiqkle kagaekifse kytgikkegr keleellsiv
       61 kagdkvlvtk idrlarsivd lnsiisalnh kgvtisfldd hltfepdkk
//
LOCUS       WP_010716638             752 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Enterococcus faecalis].
ACCESSION   WP_010716638
VERSION     WP_010716638.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..752
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86007
     Region          235..723
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mqgnnlfnng llqpkkppig qeqqkmtryh qlrlvfglvg vllypfailg siplliglav
       61 dkrdkaanvf dmdyesflkr nsivflsfsa vlfvinvfaf ilwiprgyls ayllfplnll
      121 htalrfnwet ivalligssg mgaiflafss fvakrkvisk ederkkvtes keyknrqknk
      181 feesqrftde qekeyqkave svdidkykel snqlllgmse fglsyimnfs efnqhvlvpa
      241 ttgsgkttll qllvqhavkf nfpvilidgk gardtlesmr eiakfydkev haftddgdmr
      301 ynpvehgndi sirdklvsla etesvfysga akallqvtiq lldefkgakv tlsgdtrtte
      361 tverslpfvq rfllprnvlh lfadailpnn pklfeievek kiqkpkkksv kegseilpds
      421 dldkeekeed sqiknskfrn isqlgiaqke tetivlnpet ldldsyylll krnlrylptd
      481 ketgenikqk lferlfirye hkdspfylya tsealqtnin mlldselgkl fdtknaknvl
      541 dvqeivnqrk lvyvsfngli ykeyirtlaq mlvgdvnyfa semyrknvkr evlvifdepa
      601 sylnetfidm vnkgrgagvy giftpqtmad iaklgdklme qlvgnvntlf igktnekgea
      661 eywsetmgty qdidvtsvte qedgysdvgk sdwsgdrgtk rnvdrfkisp nkikelrtge
      721 fiiyrtaenv nlppqkvyvr nalewlqksn sk
//
LOCUS       WP_010716659             268 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010716659
VERSION     WP_010716659.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..268
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30348
     Region          2..258
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mktmrriysi pyvmwlllfv iapvlmiiyq sffdmngqft lanyqtyfts gtylsmtins
       61 vwyaflitif tllvsyptay fltklkhkql wlmlvilptw vnlllkayaf fgifsihgsi
      121 nqfmsfmglg thqilftdfs flfvatyiei pfmimpifna leemnpslis asrdlgassa
      181 etfrrvifpl slngvksgvq avfipslslf mltrliggnr vitlgtaiee hflvtqnwgm
      241 gstigviliv amfivmlltg ekkkgrgk
//
LOCUS       WP_010716685             272 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Enterococcus faecalis].
ACCESSION   WP_010716685
VERSION     WP_010716685.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..272
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=30953
     Region          1..272
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mdlgmlqagi nvvesfeidk kccatlrknf nhkvnecdis kitvldqqda dvyigtfpct
       61 kyssiadisg trigddlflh ffrhvalaqp eiyvvenvpg mkkfqvvmec ltklpdyyir
      121 vecpvnanfw lpqerkrliv igskrpfpkl dypgqitnlr lkdileknpn vsvpdyvssr
      181 lngkyrdkpi itnldgiapt avahyakdks trlvddglri rpysllewqr lqgfpdwfsf
      241 egtdndgmrm vgnavavpma ewigkhivey fn
//
LOCUS       WP_010716781             432 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S1C family serine protease [Enterococcus].
ACCESSION   WP_010716781
VERSION     WP_010716781.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..432
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44728
     Region          130..417
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mqrkdvtpns dkksllqkfg iglaggllgg alilggaysg iiptpnggnn aatttstnhg
       61 dtkvsnvsyn vssdvtkavk kvqnsvvsvi nmqsasnnss addpfgglfg gnegtqdssg
      121 nngndleaas egsgviykkd gktayvvtnn hvvdkaqgle vvlsdgtkvk gelvgtdayt
      181 dlavikissd kvdqvaefgn sskitvgepa iaigsplgsd yansvtqgii ssvnrnitnk
      241 nesgetinin aiqtdaainp gnsggplini egqviginsv kivqstsqvs vegmgfaips
      301 ndvvniinql ekdgkvtrpa lgitmsdltg issqqqeqil kipasvktgv vvrgveaatp
      361 aekaglekyd vitkvdgqdv ssttdlqsal ykkkvgdkme vtyyrgskem katidltidk
      421 saltqqnnrn nq
//
LOCUS       WP_010716804             459 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Enterococcus faecalis].
ACCESSION   WP_010716804
VERSION     WP_010716804.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..459
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51169
     Region          10..430
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mnnadpesqs liaqllllvv ltfinaflaa aeiavvsvnk nrveqkaedg dvkaqkllkv
       61 lqdpnnflst iqvgitlvni lsgaslaetl ssrlapvlgg gaaakslasi iilalltyvs
      121 ivfgelypkr iamnkseeva qltsgavrfl gviarpfvwl lsastdllsk itpmtfddad
      181 skmtrdemry mletegvlen eelemlqgvf sldtkvarev mvprtdafmv diqddvqeni
      241 nlilgenysr ipvysedkdk ivgilhtktl lkaarnlgfe nielgaiiqe plfvpetifi
      301 ddllyelkrt qnqmaillde yggvvglatl edlleeivge iddetdeven lytqvadney
      361 lvqgrmlide fnevfetdlh msdvdtmagy litalgtipd egekpsfevg nikltaeeme
      421 gtrllvlrvh fydeetvdee peenrrffrk emeddeprr
//
LOCUS       WP_010716792             371 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: lipoate--protein ligase [Enterococcus].
ACCESSION   WP_010716792
VERSION     WP_010716792.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000589
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..371
                     /product="lipoate--protein ligase"
                     /calculated_mol_wt=42302
     Region          2..249
                     /region_name="LplA"
                     /note="Lipoate-protein ligase A [Coenzyme transport and
                     metabolism]; COG0095"
                     /db_xref="CDD:439865"
     Region          251..335
                     /region_name="Lip_prot_lig_C"
                     /note="Bacterial lipoate protein ligase C-terminus;
                     pfam10437"
                     /db_xref="CDD:431286"
ORIGIN      
        1 mryvimqsrd irenlatedy llntlsfeep lvlfyiqepc vilgrnqnay eeidlayare
       61 kgivitrrls gggavyddlg nvsfsfvvqe ghqafgdfka ftkpiiealh kmgatgaeis
      121 grndllidgk kfsgnamytk kgkmythgtl mydvdlaevq rvltvskkki eskgtksvrg
      181 rvtnlrpyld ekyqqltiee frnrllmelf dveslteiae keyvltkadq qeirklvaev
      241 ygneawifge apkftikkee kfkggivdar ltvekgkiie ltiygdyfak ketteivaal
      301 lgvdyqyssi wqalaafnfe dyfvnitkee fvhlfndgwl llekfpmnvp iasifgffqc
      361 lhsteanrmi g
//
LOCUS       WP_010716880             212 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ImmA/IrrE family metallo-endopeptidase [Bacillota].
ACCESSION   WP_010716880
VERSION     WP_010716880.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..212
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=25008
     Region          76..176
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mnldydtyfe yhdqayiiie kvanyygiel kelrwkhyrd ymidvenvdi ipykfgevsr
       61 kifsgniirl hdqcgisyns tmvkgrqnfs ilhesahyff dmnkdcksqs fsdllsgkgy
      121 sdedapkelr anifaslali nnealkecfr krmsfyqicd efemsaaaly vrlydfltkf
      181 illnqslart ainqfrynyd psklinyvkm sl
//
LOCUS       WP_010716984             169 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Enterococcus].
ACCESSION   WP_010716984
VERSION     WP_010716984.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..169
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19868
     Region          7..169
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdkistkklv qkakkgdgqa fvhlcqkyet vlynaaykml lnevdvadcl qetelcawek
       61 ittlkneyaf nswifkimln qvqnifrekq kttywmdtys pvpafddlyd ldkglhklpd
      121 nyrvplvmyy yvglsikeia qqldvstnti kirlsrgrkk lrtylketw
//
LOCUS       WP_010717293             128 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NusG domain II-containing protein [Bacillota].
ACCESSION   WP_010717293
VERSION     WP_010717293.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009210
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..128
                     /product="NusG domain II-containing protein"
                     /calculated_mol_wt=14822
     Region          1..125
                     /region_name="COG5341"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444125"
ORIGIN      
        1 mkkgdiivii fliaisfspy fiffhnnpfl pksfddvkya vvkidgkeie rinldnpkef
       61 iktfypskgq yntievkngh vrvkkdnspd qiavktgwis epgqtsicip hrfileivqq
      121 yskdyyiy
//
LOCUS       WP_010717269              77 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Enterococcus
            faecalis].
ACCESSION   WP_010717269
VERSION     WP_010717269.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..77
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=8196
     Region          1..73
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mekailqlet lscpscmqki egavksvkgv dkdslkvlfn sskvkvnfds avtsieeiqk
       61 aienvgypvl kakvkaa
//
LOCUS       WP_010717324             778 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus faecalis].
ACCESSION   WP_010717324
VERSION     WP_010717324.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..778
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=85761
     Region          10..659
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(300..302,365,384..386,411,463..465,509,512,515,534,
                     537)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(594,598..599,601..602,627,630..631)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
ORIGIN      
        1 mlnkvdlkkg lsteevakqk elglqnnyee nvakstkdii fdnvmtlfnf lnfaiavcll
       61 fvgaysnlaf laiiivnmsi gifqeiharn lvqklsivak envhvvrngv qqeidtkelv
      121 mediviisag eqvpsdmevi dgkveaneal ltgesdliek eigdtllsgs fivsgqayar
      181 vihvgaenya vkitqeakvh kpiqselvns irkvskftsw viiplgiilf veafwlrdag
      241 iktsvvassa allgmlpkgl vllisialtt gviklakkri lvqdmysiet lahvdtlcld
      301 ktgtitegkm kvqkaiilhd kyeelfpqii gsylsestdn nitmqairdh yevsnrfgak
      361 evlafsserk wgaiefpeig tvylgaperl vddsrlpeav ftaqengyrv lmlaiaeqqp
      421 lnetkmpyle plaileiddp irqnaketlg ylkeegidlk visgdnpvtv sniarraglp
      481 gyesyidlst ktteaevrea vqqytvfgrv spqqkrtivr elkdtehvva mtgdgvndvl
      541 alreadcsia maegdgatrq isnlvlldsd fttlpdvlfe grrvvnnvtr vssvffikti
      601 ysfilsiica ltaiafpfip iqvtlidlai egypafflsf egdkrkvvgk flptalknas
      661 vnallvvani iavyligqnq gfssldtttl myyllvgisc mavvraclpl nplriflvfs
      721 tiigiyvaam lfhnileigf ltsqtmglff immainivvr vtigfvqmkr agktikdl
//
LOCUS       WP_010717355             147 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system PemK/MazF family toxin
            [Bacteria].
ACCESSION   WP_010717355
VERSION     WP_010717355.1
KEYWORDS    RefSeq.
SOURCE      Bacteria (bacteria)
  ORGANISM  Bacteria
            Unclassified.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Bacteria"
                     /db_xref="taxon:2"
     Protein         1..147
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=17234
     Region          39..147
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mneldiqkkk qaldnwgvsk eilardwlem etvkrnrlfr qgeivmcelg enigyeickr
       61 rpvliisddr yskyghvvvi pltkntrplh thyilkkeky dfltwdscvk teqirsvasi
      121 rleniigkid sfdmrgiknr lkslini
//
LOCUS       WP_010717463             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: superoxide dismutase [Enterococcus].
ACCESSION   WP_010717463
VERSION     WP_010717463.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..202
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22595
     Region          4..197
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mtytlpelpy aydalepyid vetmhlhhdk hhntyvtnln aaiekhpelg eksvedlisd
       61 mnvipedirt avrnngggha nhtffweima pnaggqptga ikeaidetfg sfdemkaafk
      121 taatgrfgsg wawlvvnngk leitstpnqd splmdgqtpv lgldvwehay ylkyknvrpd
      181 yieafwnvvn wdkvnelfaa ak
//
LOCUS       WP_010717481             583 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF262 domain-containing protein [Enterococcus].
ACCESSION   WP_010717481
VERSION     WP_010717481.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..583
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=69387
     Region          10..573
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 mvergfqpli tikeaienid kniyllpaiq rkfvwspeqi eslfdsimrk ypinslmlwq
       61 itsdeiknny rfysflrkyk qrfgemneyy nsmgrtdnff avidgqqrln slyiglkgsy
      121 avklnhkrwv dnednfppmk lylnikntyk qetkidkeye fkflrrdkve kenklgekyw
      181 fevgsilgls deknrcsyle kvglenneys kdilnllyet ineekvlnyy ledeqnldkv
      241 ldifirtndg gtkltfsdll msfltvhwsd arenfeelir evnqfgdfsi tidfilknml
      301 vlyaddiksr vknfnedvin kiktnwerir ksilnafemf yrlgfenrtf paknaaipiv
      361 yyiyenkled eviknrflds ntqnansqlm kkwlllvflk rifggqsdsi lreirkiidd
      421 sssgvfplke iinsaksnpt knysfddaii eglfevqcgs ddaffvlslf ypdldyfnqn
      481 fdidhihpks kfqnktfmen hfskeeidri gnnwnkignl qllnkeknil kkdkslsewm
      541 einhlnnsfl fidedikldi enfelfyenr vakmkqdlke lvk
//
LOCUS       WP_010717506             492 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Enterococcus].
ACCESSION   WP_010717506
VERSION     WP_010717506.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..492
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=58626
     Region          79..156
                     /region_name="Mga"
                     /note="Mga helix-turn-helix domain; pfam05043"
                     /db_xref="CDD:428276"
ORIGIN      
        1 mlkrdflekp ydymndillf lynnkgqatr nelvdffnis lptlneylsf leqflkeeql
       61 qenltltvlg dtlylnkapt fsmkamimlf ldksikfhmv qqlfrknein ggyfqqnyai
      121 ssatyyrkiv elndllnefn lrikrgklvg eekqirffff nffwfifeek tdlekelanq
      181 ylglieilqe ipritfdhte ilqiklwmki sfrrmvlepl ptisphdvql drplfeeinl
      241 sihtymkrid rpytineaym fydffcsmhn ysanaafafr lakqqriekt ylnemnrvil
      301 tylkargyls hyvlpirlly ienllfqlha qlyyfsgfil pfdywtiqsl lkvvrhpfse
      361 sevyelveia ttnfatkvta skyqnqftei nytlilnhia elnekkitig vyhslssays
      421 elvaqkiqqs iagkyplkie pynaenhydl llmntnneql vaqydhyyif sdisnrydlq
      481 siekiiqlll gk
//
LOCUS       WP_010717468             446 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MATE family efflux transporter [Enterococcus].
ACCESSION   WP_010717468
VERSION     WP_010717468.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Kaatz,G.W., DeMarco,C.E. and Seo,S.M.
  TITLE     MepR, a repressor of the Staphylococcus aureus MATE family
            multidrug efflux pump MepA, is a substrate-responsive regulatory
            protein
  JOURNAL   Antimicrob Agents Chemother 50 (4), 1276-1281 (2006)
   PUBMED   16569840
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..446
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49453
     Region          12..430
                     /region_name="MATE_MepA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Streptococcus
                     aureus MepA; cd13143"
                     /db_xref="CDD:240548"
ORIGIN      
        1 meqtqqnhft alfyknvllg ilsmaaqsif iladtffian gigtealagl nivlplvnii
       61 nglgwmfgvg gatlfsttva qkeikkanqy fsltiglvfv igslftlasl tfsdqiirgl
      121 qgtgvlfgla keyymiylsc sllfilnncl itflrndhnp rlatiafvsg givniildyv
      181 fiyqfgwgma gaaiatvmsp ltslilitlh kwspqrvlrf ekfkvkfqdv reimsigfss
      241 flnefssafv mflfnivlln lvghvaisay aivanlniiv iaiftgigqg aqpllsryyg
      301 lgetkvlrkf vklsfitylv agflfflisq vftgqiievf nsegndqlaq iartairlya
      361 isflftglnf mgiyyfsavr kpkmalmiss lrgfflivpv lfilvkllgl tgvwlampvv
      421 efvtfglmlv gyfayrnylk kreavt
//
LOCUS       WP_010717575             311 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FAD:protein FMN transferase [Enterococcus].
ACCESSION   WP_010717575
VERSION     WP_010717575.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..311
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=34460
     Region          10..302
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mqqsqtiylm gtvidvfvdh eepekileev hqrlityeqr fsandstsel mavnqqagqk
       61 pvsvhpelyq lialgkkhsc dpashlnvti gplvqtwrig fkdarvpsek eikaclkkin
      121 pekihlnplk qtvfleeegm kldlgalakg yiadlliayl kevhvtsali nlggnivtlg
      181 psthqnkkwr igirnpqesr etisllveva nqsvvtsgiy erslteagrv yhhlldpttg
      241 ypletemasi tiisdasvdg eiwttrlfgy pipaaleiln qldgiegvii tqdqqilyss
      301 gladtlhiih s
//
LOCUS       WP_010717609             320 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ring-cleaving dioxygenase [Enterococcus].
ACCESSION   WP_010717609
VERSION     WP_010717609.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10327061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..320
                     /product="ring-cleaving dioxygenase"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36191
     Region          9..133
                     /region_name="VOC"
                     /note="vicinal oxygen chelate (VOC) family; cl14632"
                     /db_xref="CDD:472697"
     Region          160..315
                     /region_name="PcpA_C_like"
                     /note="C-terminal domain of Sphingobium chlorophenolicum
                     2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and
                     similar proteins; cd08347"
                     /db_xref="CDD:319935"
ORIGIN      
        1 mkkedqllgi hhvtamtsda eknyhfftdv lgmrlvkktv nqddiytyht yfaddlgtpg
       61 ttmtffdfpn npkglkgtnt isrtgfrvps daaltyyenr fnefavkhtg iseefgkkil
      121 rfwdfddqay qlisdelnqg vaagtpwkkg pvptefaiyg lgpveiaisy fhefkevfee
      181 ilgfhvvaqe gnryllevgq ggngaqvvlv dddtssqaqq gygevhhvaf rladrkslgt
      241 wqalfdhlgl qnsgyvdryy feslyvrigh ilvelatdep gfmgdepyet lgeklslapf
      301 lenrreyies vikpfntkra
//
LOCUS       WP_010717648             345 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar-binding transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010717648
VERSION     WP_010717648.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..345
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38317
     Region          25..341
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mlkefkmiea vapdmldvlq erfqilrniy wmqpigrrsl setmgiterv lrtetdvlkq
       61 lnliepsksg mtlterglev yqglelvmnq llgmhqieke mtqyfgiqrc ivvagdsdiq
      121 kkvlsdfgdv ltntlnlllp ngentiavmg gttmamvaen mgsletekrh nlfvparggi
      181 geavsvqans isavmanktg gnyralyvse qlsretynsl lqepsiqevl tlishancvv
      241 hsigralhma arrkmsddem vmlkqknava esfgyffdee gkvvykipri glqlknlqei
      301 pyvvaiaggk tkakairaym knapkqtwli tdeaaaneil kgvtl
//
LOCUS       WP_010717652             609 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010717652
VERSION     WP_010717652.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 609)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 609)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 609)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..609
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68442
     Region          <53..167
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnfnqfvirn tirnkhlyla yflstmfsvm ifftftgfvf hpalanglnp kaqmgmtaaa
       61 iiiygfsflf vlysmdvfiq srkkefgtlm iqgmspkqlk kmifienlvi gffatifgsi
      121 lgvgfsqfil wisnllmhlg lgfylpvmpf iitvisfavl flvisffiqf rlpkatlqel
      181 lkagemgkge iksskvksfl avlllivgyg ialvakgqlv lmvmfpvifl vilgtkflfd
      241 qlsvsvierl krkpkifwkk tnmvvlsdla frmkdnarsf flvsvistva faaigtlygv
      301 nemifkgiss vpyeltlsds tnpenqemkq fatktfqekn iqfdqidytm yktsagiqli
      361 ktseynklak fideptltge kvvnlsqkda psaasvdvks vqlandqvln idkteetnvl
      421 ptfggvvvip dststdgika etetiwqpka gtnreelika eniigdkypm lvgtaamsaa
      481 itqfytpvlf vglfigivff vsagsflyfr lysdmntdve kfkmiyklgl tkkelkkmiy
      541 qqvgilfftp ivvsfihgav alkamyavld qpmqlagwqv lgvflliqvv yyliartfyf
      601 kkvyhlvkd
//
LOCUS       WP_010717676             399 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent aminotransferase
            [Enterococcus].
ACCESSION   WP_010717676
VERSION     WP_010717676.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..399
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43868
     Region          1..394
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,206,235,237..238,246)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,199,244..246,275,278)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            238
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mnvsnraqql tpsvtlaaaa kakalkakgv dvlsltvgep dfvtpkniqk aaiasiedgr
       61 asyytpsggl pelkqaivsy vereyqlryq pkqvivtdga kyalyllfqa ilnvgdevii
      121 pvpywvsyge qvklaegkpv fvsstqeqsf kvsvaqleav rtdktkaiil nspsnptgvi
      181 yteeelrqig ewavahnili iaddiygrlv ynghrftpia tiseairqqt iiingvskty
      241 amtgwrigfa vgdekiiqam tqlasqstsn pvavsqyaai ealtgeqstv edmrqafekr
      301 lnhiypkvaa lpgvslikpe gafylfpnvk ktleicgydn vtnwvedllq eahvalvtge
      361 gfgapehvrm syatdlmtle kaiermndfi ekkriqhna
//
LOCUS       WP_010717715             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: gamma carbonic anhydrase family protein
            [Enterococcus].
ACCESSION   WP_010717715
VERSION     WP_010717715.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..163
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17356
     Region          6..157
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mkkeyfiaas advygnvqla kdsniwfqsv lrgdsntiti gegsniqdgt iihvdedapt
       61 ivgkyvtvgh qcilhgckig dgaligmgst ilnnaiigen sligagslvt egkiippnvl
      121 afgrpakvir pltaaeiasn htnalhyiqr aeefrqqkyp klt
//
LOCUS       WP_010717747             337 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Enterococcus].
ACCESSION   WP_010717747
VERSION     WP_010717747.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..337
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37714
     Region          79..336
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkrkivrfil wllgiivvic lgvflafqls pkpgawvinq lfageveikd sasydkalln
       61 vqlqenqtyp ssrkkntfdl yypqtskqav pvvlwvhggg yvggdksgmk efatrlvads
      121 svafismnye lapdapypsq lqqvdelvqf llekkqaypm ldlsklfigg dsagaqialq
      181 yatvqtnany akelgmtaal pashlkgtls ycgpvdlkqm anqqsdnrfm kffvktvaws
      241 llgtkdwqts aelqevslvd kvtkefppty ltdgnsfsfq eqglalvqrl ktlnvpvsal
      301 ffkdkkatit heyqfdyqtk eakhcyqetv qfvntyk
//
LOCUS       WP_010717932             320 aa            linear   BCT 01-JAN-2025
DEFINITION  ring-cleaving dioxygenase [Enterococcus faecalis].
ACCESSION   WP_010717932
VERSION     WP_010717932.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10327061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..320
                     /product="ring-cleaving dioxygenase"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36179
     Region          9..133
                     /region_name="VOC"
                     /note="vicinal oxygen chelate (VOC) family; cl14632"
                     /db_xref="CDD:472697"
     Region          160..315
                     /region_name="PcpA_C_like"
                     /note="C-terminal domain of Sphingobium chlorophenolicum
                     2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and
                     similar proteins; cd08347"
                     /db_xref="CDD:319935"
ORIGIN      
        1 mkkedqllgt hhvtamtsda eknyhfftdv lgmrlvkktv nqddiytyht yfaddlgtpg
       61 ttmtffdfpn npkglkgtnt isrtgfrvps daaltyyenr fnefavkhtg iseefgkkil
      121 rfwdfddqay qlisdelnqg vaagtpwkkg pvptefaiyg lgpveiaisy fhefkevfee
      181 ilgfhvvaqe gnryllevgq ggngaqvvlv dddtssqaqq gygevhhvaf rladrkslgt
      241 wqalfdhlgl qnsgyvdryy feslyvrigh ilvelatdep gfmgdepyet lgeklslapf
      301 lenrreyies vikpfntkra
//
LOCUS       WP_010717970             273 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterococcus faecalis].
ACCESSION   WP_010717970
VERSION     WP_010717970.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..273
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30362
     Region          3..226
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgkvyvignf kggvgktktv tmlayesalh lgrktlvidl dpqgnatrvl aktgdldeit
       61 ytvteafqeg slepaitnis knldlipant afrnltkilm tkfpsnefdq inylntllkp
      121 lkekydaiyi dvpptisdfs dnamlaadyc iivlqtqels ldgaqtyiay mqyladtydn
      181 dlqvlgiipc mlrpggrvdn kvleqakely ggnvlntvvk yqerlkvydv egikishnyt
      241 gkadgwdvka hkvfidvlne ldqhqlvlee leg
//
LOCUS       WP_010718063             727 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus faecium].
ACCESSION   WP_010718063
VERSION     WP_010718063.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 727)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 727)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..727
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=82752
     Region          2..718
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mkveekqfdl eyinkyasqm tigngffgir gsqeedyrnq vrgmfaagvy nrplgaesae
       61 lvnlpdvirw eikidgehfs letmkvlaye rvldlemgel kryalietaq gkkvevitcr
      121 vadqnnlhqa alkvvikplt edcqvdvktg idgqqtnfgt qqlvekelrv fgddlisasy
      181 qtteskidig iaakfnkaga fqaknrrita sfsekirknt sftlekiivl stslqqtdpf
      241 kksiaqaqks vsyteileqs msywtdfwhq hritiqgdss fdqlamdfaa yhlqimtprn
      301 dpsvsvgakg ltgegykghv fwdteifilp fflyqfpeva knlllyrydr legarqkard
      361 yhyqgalfpw esahtgqeet pkfaalnikt gtrqevasaa aehhisadla yavqeyvqat
      421 edqsfletkg ktlihetaaf wlsravkvdd hleihrvigp deyteyidnn aytnylahyn
      481 valavkyqag dplflkecqn fldklylpvp nkeqlipqdd tylskpvidl ttykerpgsq
      541 silldyarse vnelqvskqa dlvmllyllp eyfsqpivsk nlhyyenkti hdsslskaih
      601 aieacriqem ewayhlfqea clidlgpdph ssddgihaas lgalwlavif gfsgitvtng
      661 tlsisprlps awekisfpfi wknhrllfvl tkkqivikke tketlpifvn gdqyqlekel
      721 ilerrgk
//
LOCUS       WP_010718172             706 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus faecium].
ACCESSION   WP_010718172
VERSION     WP_010718172.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..706
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80294
     Region          16..638
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkyiktpafl nkrlgffsll vvllwlktif aylvdfhlgi esgiqyfilf inpiattlll
       61 lgialyirrp rvayitmmvi yflltllvfs nvtyyreftd fitintilga gkvasglges
      121 airlfrpydv iywidfiilt vlliakkikl dprpirarma faistlavmi fsgnlfmaea
      181 drpelltrtf srdylvkylg lnafmvydgv qtyqtnqvra easpndmkev enyvkehyaa
      241 pnddlfglak gknviyihle sfqqflidyk ltdekgvqhe vtpfinslyh snstfsfdnf
      301 fhqvkagkts daetlmensl fglnqgslft qlggkntfqa apdilsqteg ytsavfhgna
      361 gtfwnrnety knlgydyffd ssyydvnddn sfqyglhdkp ffqqsvqyle rlqqpfyskf
      421 iavsnhypys kftndeagfp lantndetin gyfatanyld tavqeffnyl kesglydnsv
      481 ivlygdhygv snsrnknlae lvgktsstwt nydnaqmqrv pymihipgqt qgginhtygg
      541 qvdalptllh llgvdtknyi qlgqdlfskd heqlvsfrdg dfvtpkytyy ggtiysnetg
      601 eaitepteev qneidslkek vdkqlavsdq inngdllrfy tnsgldpidt sdydykngle
      661 klkeaekslg dkstsvfsqh ngqstvdlyk tqtyqelhgt ttssse
//
LOCUS       WP_010718191             327 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Enterococcus].
ACCESSION   WP_010718191
VERSION     WP_010718191.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..327
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37945
     Region          1..239
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrigivglgs mgkrrlrliq svspnvsicg idtnktrcde vsndfnietf snleqaknlf
       61 eidtvficts pitheviisq vldldcnift einllnnyyp evqkkakekn kilylsstfl
      121 krkeikyiqd klnndnnfsy ryhvgqylpd whpweryqdf fvarketngc reifaielpw
      181 iiktfgkikk meviskkisa ldidypdsyn lllehengvv gsltvdivsr takrelsiis
      241 escqiewhgn pdslyvwnae kesmekiely sevthndays htiiedayle eikeffnvis
      301 vnapseydfd qdsytidlin kieglnr
//
LOCUS       WP_010718264             356 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010718264
VERSION     WP_010718264.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..356
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38625
     Region          126..355
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflalneimh sklryalvag vmfliaylvf fltglaygla qdnrtavdkw eadsivlskd
       61 ansnlgmsmi tkkiaeeveg gkvaylaqtp gvvtskdste egkinvsffg idknqfimpn
      121 lvegkafdnd deavgdislk eeyglavgdt vklsgsdktf kltgftdhak fnvspvlytt
      181 inayqeirfe kedtsenari naivvrgkis nlpedleqik iskfinelpg ynaqvltfgf
      241 migfliiiaa ivigifiyvl tmqkinifgv mkaqgitggf iarsvvaqtf ilsfvgillg
      301 llgtvgtslv lpdavpfqsn wlffgvisll mlvvavlgal fsvrtivkid plkaig
//
LOCUS       WP_010718250             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010718250
VERSION     WP_010718250.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..300
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33798
     Region          1..271
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mllrekikei sfspsenevi qfllsdspal gemtiqaiae rcyvhpstli rvakkmgfdg
       61 wvsfrnafla etaylegnfq didanlpfst tdgimtiank masleqmtiq dtlslihhdq
      121 lqkakylllq akkivifasn sntlisqdfm lkmkrikmdv tivttfgesf yeaynctsdm
      181 cgilisytge nkvilrtaei lkqnhvpila ltsigdstls amstaalrlt trerlyskig
      241 nftintsiyy lldvlyscvf aenyqqnlvh lisvgqkfdk rpissaimke pfnfenkkve
//
LOCUS       WP_010718265             454 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Enterococcus].
ACCESSION   WP_010718265
VERSION     WP_010718265.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..454
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51048
     Region          1..422
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mkiviigash agitaalnlr klqpkaevll idedhkdglg yvsnginlyl kgkirslaev
       61 ahnmrtlqes gaklitewrv teldpdkhql ilaskegkne titydkliva tgsspvtlyk
      121 qieaenvyty knlvqskqvl aalkeakevv ifgagyigle ladtlrnkgy iihlvdympn
      181 vlsryfdkdm insfqnqlqt kqinfypnef lidwkkseek vvsvqllsqt ikadmvifsa
      241 qthpnttllk ekvalyedet vivneylqts dpdiyaigdi vpvsfdknkr hlflplvtra
      301 vhmaravalt lsgqptaydl rqkitaavii dyflgtvglt edeapfleqn tgscsgefdl
      361 fpqydeenkt vnakliyhpd tleiiggqli sqefllsdln lladivkhkt tipqlavedf
      421 gflseytprf nylneltfkv lakransnrv dkrl
//
LOCUS       WP_010718277             327 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-quinone oxidoreductase [Enterococcus].
ACCESSION   WP_010718277
VERSION     WP_010718277.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..327
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35668
     Region          1..323
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,120,124,127,145,148..150,170..171,175,190,
                     214..215,236..237,239,262..264,312,317)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mraisikypg svdvleqiev pvpkpkqgel likvhtaavn rtdimkresv slkppypilg
       61 vevagevven ksdisiftpg tkvyglvnlg gyaeyavmpa draillpdtl dyvsaagise
      121 vfltayqtly wlgklqeget vlihagasgv gtaaiqlarq lshakiivta gseeklafck
      181 elgadeliny kkqdfqkevr kitegrgvdv ildfigasyw eknlasiavd grwvligmlg
      241 gtivpeidlg vligkrvqll gtlltprsdq ykaelaqtfm qkagpfleng kirpiidrtf
      301 qfsavkqahe ymeanknigk iilkite
//
LOCUS       WP_010718280             289 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Cof-type HAD-IIB family hydrolase [Enterococcus].
ACCESSION   WP_010718280
VERSION     WP_010718280.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..289
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31002
     Region          4..281
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,214,236..238,240..241)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mikliasdmd gtlldahmsv spenaeairf andtgvefmv atgrnyqear aaldevgidc
       61 amitlngaqv fdkegnslft vsipnnqais vldildangi yyevatndgl ysenqakrie
      121 sfasmvathl phltykmaia masaklellh ityvdsirai leeknlevlk iicfhtegpa
      181 vlgpvgkqis llgdlavtss gqnnievnhk naqkgiavah vahergisle evmtigdnfn
      241 dvsmlqvagv sfamgnaeie vkdyakyttd tnlesgvgka ilraiaedl
//
LOCUS       WP_010718317             191 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SOS response-associated peptidase [Enterococcus].
ACCESSION   WP_010718317
VERSION     WP_010718317.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..191
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=22316
     Region          1..>168
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgryffdle sellqnyyre aqkkqpeqaa elaagevfps nlvvtlrkee eniltpeimk
       61 wgftgfkkgq lminaraetv eekktfhqpf lqnrcvfpms gfygwneekd kfmfsnkeki
      121 vyiggfyrsh qdekmaesii mttepnrtva pihdrmplvl teeqiepwvt disfarkiit
      181 qqmpelvmek v
//
LOCUS       WP_010718171             392 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent rRNA methyltransferase
            [Enterococcus].
ACCESSION   WP_010718171
VERSION     WP_010718171.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..392
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=44746
     Region          2..389
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mkvqvkkras srlkkgypli qkedlahpqk ettqwvelvd pqnqfiakgy lgkqnkgigw
       61 vlsqqdipfd qsffeelfvk skekrtfffs ddsttafrif ngegdgiggl iidyyagyav
      121 fswynetlyt hrelliqafr eiypetiggy ekirfesvnl pesqfiygke apeplvvken
      181 gvkfavylne glmtgifldq kevrgslaeg fasgktvlnm fsytgafsva aamggaiett
      241 svdlakrslk ktqeqfevng ldvdqqkiiv mdvfeyfkya krkqflydmi vldppsfarn
      301 kkkvfrvakd ygelikdsld ilaedgilia stnaanvsie qfqtmieeef haknvsfeql
      361 alyrlpkdfq ttdtflegny lkvfvyqikn nh
//
LOCUS       WP_010718328             147 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_010718328
VERSION     WP_010718328.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..147
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16682
     Region          16..143
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mkvvqtkdtm sniyldavri rhqvfvveqg vplsreidkd eahcihfvly sdkkepqgtv
       61 rllplengkm klqrmailse yrhqglgkil ieeaenfakn qgyntillga qstaetfyek
      121 lgytaygdpf edagmphiym kktspfv
//
LOCUS       WP_010718331             189 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010718331
VERSION     WP_010718331.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..189
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21821
     Region          2..>104
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 markkaitre qilaaayeva atdgftrfta rniankmncs tqpiylefkn mddlrqalfe
       61 qiydhlqyev ftvehtgnti idlafnyihf arrekklyrs lyleeygggk emqnfsytyf
      121 vntvkrdpay vnlseeqies lyngtwiiat giaalmsssi ihptdeqiek miqdsidail
      181 kfkepieid
//
LOCUS       WP_010718332             406 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cell division protein FtsQ/DivIB [Enterococcus].
ACCESSION   WP_010718332
VERSION     WP_010718332.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..406
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=45929
     Region          99..325
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mskkkepkkl shpssdennl tpwqkanrky laeqemknqe pkkeditldt plsdseeekt
       61 vqeeqqeesq sekkieffee ikqkknggpy ngsflnrlpn lksqrhkvlf rrlaliitvl
      121 giplifliyy vspysklqav avsgnktvns qeiisdtkls lgenvwgqyf hrstyidrlk
      181 kaqprietan ihfkgmnefd ldvteykeia liaknnqyyp vlengtvlde kvanptknlp
      241 ileefkdsak ikeltkqynq lsselqkais eikytprasn knliqlnmnd gnqvivninn
      301 lanqmkyysq vakdmdekgv idmevgifsh pygstqetee sgqseettes eenadqtnes
      361 seeaetqeaq tpgssstngs sdsndssets qiednpsttp sslnen
//
LOCUS       WP_010718336             680 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010718336
VERSION     WP_010718336.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 680)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 680)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 680)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..680
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77944
     Region          <30..181
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mlyklavksf frqsrgylvy ffsltlsvmi yysfsamtyd qslvrrasqd tsidgglsfg
       61 gfiitvvllf fvfsanrffl nrrqkeigiy qlfgmnklqi sgiyvleimi iglfacisgi
      121 llgiifsklf smilvrmmdm dltspffisi psvvdtlfaf fiillavsvy siwkiwrypm
      181 irsfgekeqa dsstmrfrtr hrllavigll lltsgyfgas hfreitswmi syhyldtlvf
      241 ffpfliffvc vvgtylffcy tfrlfliils kwkiyyygin flimgntqvh llkswrtnsl
      301 itvilgislm tiggtasist ilsyqekvss pmdyqfdvet ekkikpilae egqkitkeit
      361 lhykvigsiy sqnleepmfq tanlitetqy qafrkvnpdl pnislkspgh tvlldqmqtl
      421 frnislygss iglpdnqelk iqqmlpsvlg detmvylspv livddtvfek akgvdyqvvn
      481 vdvsggnnek iderlsndls ikwlnavyys ydivngslqg eistkklpdd qmkeaqfsqe
      541 ssrlnfsssy sklravnrri ginifvtlfv gmiviiatgs iltvrqlaea eeekenyhll
      601 tklgipqrsi rrmifeqnal tffppmilgi thavfainvf tqyiktadyw laylvsglli
      661 liylllyvit sqlycriiee
//
LOCUS       WP_010718343             520 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecium].
ACCESSION   WP_010718343
VERSION     WP_010718343.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..520
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=59973
     Region          26..433
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mteknimvip arkrvgstaa kekikklrva aycrvstete eqnssyevqv shytefikkn
       61 newefagifa ddgisgtntk krdefnrmia ecmdgnidmv itksisrfar ntldclqyir
      121 qlkdknisvy fekeninttd akgevlltim aslaqqesqs lsqnvklglq yryqqgkvqv
      181 nhkrfmgytk dedgnltivp eeaeiikriy reylegqslv gigralekdg iltaagkprw
      241 rpesvkkilq nekyigdall qktvtvdflt kkrvkneghv pqyyvenshe aiipkelflq
      301 aqeeihrrsn iytgegknkr iysskyalsa itfcgdcgdi yrrvywnihg rkefvwrcvt
      361 rieqgpevck nrtvkedely gavmtainkl laggnnmikt leenihavig etteyqisei
      421 nnsleekqke liklankgqd ydhladeide lrdkrqillv edaslsgene rineliefir
      481 knkfrtleyd dklvrkiiqs vtvyedhfvi cfksgiemei
//
LOCUS       WP_010718356             205 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecium].
ACCESSION   WP_010718356
VERSION     WP_010718356.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..205
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23753
     Region          3..132
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,63..64,67)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(62,113..114,116..117,121)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(68,73..74,109,112..113,116..117,120,123)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,96..97,109..110,113..114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(122,128..129)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 makigyarvs sldqnldrql ellsecdkif sdkesgkdtn qegfqemmkf iregdivvvt
       61 elkrlgrnnk eltetmnliq lkkatlevln lpaltgitdd nlrrllnnli ielykyqaee
      121 erryiretqq qgialakakg kykggtlkyr endprlqlaf nlfltgstdk eveeltginr
      181 rtfrryrmkh gitnevreqk nksfs
//
LOCUS       WP_010718475             193 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Enterococcus hirae].
ACCESSION   WP_010718475
VERSION     WP_010718475.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..193
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=22084
     Region          1..188
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mkrrcpwgdq tasmkhyhdt vwgvpeyddq llfrklmldi nqaglswqti lnksasfdea
       61 ydffsigkva eyteakinel menkgiirnr rkieaavana qgvqkiqhef gsfadylwsf
      121 sdhqvinhsy keqnevptts plsdqiakdl kqrgfkfigs ttiyafleav givndhldhc
      181 frkqevsqmg kge
//
LOCUS       WP_010718439             119 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010718439
VERSION     WP_010718439.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..119
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13898
     Region          1..113
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(49,52,56..57,66,84,88,94,98,101..102)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mnikqvseak gispdtlryy ekiglippvh rtkggirdyt eedlnwvdft icmrnaglsi
       61 eslieynklc kqgdqtiaar kqllmterqh liqkidemqe cltrlhkkie nydrylleq
//
LOCUS       WP_010718481             821 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus hirae].
ACCESSION   WP_010718481
VERSION     WP_010718481.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..821
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=90840
     Region          30..685
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(321..323,390,408..410,437,489..491,534,537,540,558,
                     561)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(618,622..623,625..626,651,654..655)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
ORIGIN      
        1 mrifshqtev ekdqtsvkni tryapdyreg ltveqvaerv haqatnetid psfktnkqiv
       61 lqniftyfnl ifivlavllc lvssyknltf lpvilantgi aiyqeirskk ildnlsvlna
      121 akvtvvrngv ankidmeelv lddvilletg qqipadgyvl dgklqvneal ltgeadeivk
      181 evddylmsgs fvvsgkayvr ldkvgydsyi sqltakakkm gggeqsemia slnklikwig
      241 iiiipigitl fsqsyffngn tikesvvame aaligmipeg lyllttiala msaarlakqr
      301 vllhdmksie tlarvnvlcv dktgtitenq msvqklviak neqaeqqatr iqelisdyak
      361 amandnatmq aiktyfnkpt dqeplsilpf ssvqkfssvt fadgvyvlga pemvlrerfe
      421 tvknefsqya dqgyrvlvfg syqgilseal leaeviplay llianpirke apdtfayfke
      481 qgvaikvisg dnpqtvstva lqagianadq yidvsqlaee dylsavekyt vfgrvkpeqk
      541 mqfvqllkqk ntvamtgdgv ndilamkead csiamasgye atiqaaqval ldsdfsrmpe
      601 ivaegrrvvn niersaslfl vknifsflls vfsvlfalty plepsqitli slftiglpsf
      661 llaleenknr iegkfivnvl ekaipggltd mtvvgtlvvg gvilhlnktd vstastmllt
      721 avgflvlyki chplnqfrgr iilfcaagil fsvvflhklf sisaispvsi llllilffaa
      781 dsifrqysrm ienysqlkdg kkkrsvwfwl kvlfsvdnkh d
//
LOCUS       WP_010718493             486 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Enterococcus].
ACCESSION   WP_010718493
VERSION     WP_010718493.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..486
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53574
     Region          4..481
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mndkqlrwft valiafnmvw gmgnvvnnya qqgisvvtsw llilaiyfip yalivgqlgs
       61 afkdskggvs swventtsnk rlayyaawty wvvhipylaq kpqailiaag wavqgngniv
      121 ntmtvqmvav islviflafl ylstkglstl kvigglagta mfvmsllfil mavtapfitt
      181 dmefattgmn qvktyiptfd fsyfttvsml vfavggaeki spyvnstrnp akefpkgmif
      241 laamvgvcav lgsvamgmlf asdnipkdlm angaysafqi lgnyygigns lmiiyaltnm
      301 vgqisalafs idaplkilla dadpefvpsw lrkrsnkgtl vngylltgil vsiiillpif
      361 gikdmnelvk wltnlnsvvm pmrylwvfla ymmlnkaykk ftseykfvkn pkvgfifgaw
      421 cfaftafaci lgmvpkveya adpkawwfql isnvvtpiil imlgmilpai arrdknknvk
      481 etliet
//
LOCUS       WP_010718528             323 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PhoH family protein [Enterococcus].
ACCESSION   WP_010718528
VERSION     WP_010718528.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..323
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=35738
     Region          5..319
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 mteassslei rltaaddism llgshdkhvk lieemtetti htrgemiqii geepglslaq
       61 svirtlqeli krgihvstpd vvtalkmgqk gtldyfiemy eeeivkdrng kpirvknsgq
      121 kqyveavakh divfgvgpag tgktflavvl aiaalkkgev qkiiltrpav eagenlgflp
      181 gdlkekvdpy lrpvydalyq ifgldhtnrl mergiieiap laymrgrtld dafvildeaq
      241 nttvaqmkmf ltrlgyqskm ivngdtsqid lpkgtmsgli haertlkqik kiafvnfeas
      301 dvvrhpvvae iikayekadl hqe
//
LOCUS       WP_010718657             356 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus hirae].
ACCESSION   WP_010718657
VERSION     WP_010718657.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..356
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38584
     Region          126..355
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflalneiih sklryalvag vmfliaylvf fltglaygla qdnrtavdkw eadyivlskd
       61 antnlgmsmi tkktaqevkg dkvaylaqtp gvvtskdnde agkinvsflg idpdqfimpn
      121 ivegkafvgn deavgdislk eeyglgigdt vklsgsdktf rltgftenak fnvspvlytt
      181 ldayqeirfe ktdtsenari navvvrgqid dlpndlekis iskfinelpg ysaqvltfgf
      241 migfliviaa ivigifiyvl tmqkinifgv lkaqgmtggf iarsvvaqtf llsffgiglg
      301 llgtvgtsfl lpdtvpfqsn wlffgfisvl mlvvailgal fsvraivkid plkaig
//
LOCUS       WP_010718754              65 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Enterococcus].
ACCESSION   WP_010718754
VERSION     WP_010718754.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..65
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6925
     Region          1..65
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mnngtvkwfn sdkgfgfitg edgndvfahf saiqgdgfkt ldegqavsyd ieegqrgpqa
       61 vnivk
//
LOCUS       WP_010718759             110 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [Enterococcus].
ACCESSION   WP_010718759
VERSION     WP_010718759.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..110
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12639
     Region          3..93
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 maitvniyys gtngnakkfa kemvstgvve diraekgnik yeyffsmnde dtillidswt
       61 dqdaldkhhe spmmahitkl rekydlhmkv eryvtdikni sakdsafirk
//
LOCUS       WP_010718807             575 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: terminase large subunit [Enterococcus].
ACCESSION   WP_010718807
VERSION     WP_010718807.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..575
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66375
     Region          1..572
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 miepgvnyad lfakevrkqp kkypktvrla idrwyrwkkr kdiwfdvdra nemmdwvetf
       61 ivhtkgemvg kpflleswek fiyswiygwv kenekgqtvr vtreayvqip kkngktliav
      121 gslgyamyge galsvdcyac asdfaqaqya akpfaatiln npillegtki fkgpkgtvss
      181 itydyihedm aysnkfivqt knidniegsn pyfvlndelh kqekmeqydn fksaqislpq
      241 plmfnistag kgsssvgmrv yreakevlkr ddndsnfvli yepnknydwt drkvwemcnp
      301 nwgisvdlsa lesafktaqr sahskaeflt khldvfvnga dnffeqdqve pclvttqelg
      361 dlsnepcyig ldlsrtrdlt cvslnfptwd edgkailkvk qlyfipnenl efrekednvp
      421 ysdladkgfv efcdgkmidq dqilqyiedc mnlydiqqvn ydpamsdkfv eklenlglec
      481 vevpqfprvl nspfddverl fyekriqfdn plflyctlnv vaitningqk apskrqskkk
      541 idgfvaflcg hketmnqmtd idsneldeyl dsiyr
//
LOCUS       WP_010718830             410 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Fic family protein [Enterococcus].
ACCESSION   WP_010718830
VERSION     WP_010718830.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..410
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=47889
     Region          60..394
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 meyqklrils yergididee fkkrissytt istdleiipf lneqkvvekk fqlfylplqr
       61 isnkaekiky nsddlrklse rlpgvaetki flstminevq stnetegves tkyeigkaii
      121 nrndktskke krrfegivnm ylnlnekkfe fineskdfrn iydalfeges digdwpdgki
      181 frhdqvelkd ndkiihrglt tesdiltace kliafmnnkk ipylekcfis hyyfeyihpf
      241 ydgngrmgrf lissylarkl dpytglsvsn avnnnkpkyy kafeevshpr nmgemthfid
      301 dmmdliisgq ekslsdlkea dikmkfvshy lkemtdande qkkvlfvliq dylfsmfgsm
      361 ddeevsiavn lsryklniil hqlvelglie kikkspskhk isakiiedis
//
LOCUS       WP_010718943             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010718943
VERSION     WP_010718943.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..245
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27207
     Region          5..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 maekilvehl vkkygentvl ndinvsineg dvvciigpsg sgkstflrcl nrleepsdge
       61 iiidgahlmd kntdinlvrq higmvfqhfn lfphlsvlen itlapmdlkk eskeaaekka
      121 ikllqtvgle dkkdmypeml sggqkqrvai aralamnpdi mlfdeptsal dpemvgdvln
      181 vmkklakqgm tmvivthemg fakevanrvm fidggnfled gtpqqifenp qnertkdfld
      241 kvldi
//
LOCUS       WP_010718996             263 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010718996
VERSION     WP_010718996.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..263
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30758
     Region          5..114
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(6..8,22,39..41)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(53,56,60..61,70,96,100,106,110,113..114)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mpklytigev sellnvpkst irfwdeqgli hslrheengy rmfniddifq iydinfyrkl
       61 dvpikqmknl ygktieehya tiaeteqrik qekislqkkh eeilarkeql klmidnrgit
      121 ketipfaaiv ivdsddilds kaylenyasf ggyfdfslsd emiygfctdq tsatiplski
      181 vwynqpgkty hrfllqvevn hteknnieev rltlaqrgyq tgnvigqyll tkqteegvyh
      241 eyylgwiesq kveadltned kqk
//
LOCUS       WP_010719028             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [Enterococcus].
ACCESSION   WP_010719028
VERSION     WP_010719028.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10065661
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..243
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=28113
     Region          6..219
                     /region_name="MPP_PPP_family"
                     /note="phosphoprotein phosphatases of the
                     metallophosphatase superfamily, metallophosphatase domain;
                     cd00144"
                     /db_xref="CDD:277316"
     Site            order(10,12,37,41,67..68,143,163,183)
                     /site_type="active"
                     /db_xref="CDD:277316"
     Site            order(10,12,37,67,143,183)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277316"
ORIGIN      
        1 mkkwvyaigd vhgkydlfkk lvnefdplnh qlvlmgdlnd rgpntkecfl lgmqlvkenn
       61 aiylrgnhee yflqflqspe dwyepylrng gketfdsllh pgsteeyspt eialmirsry
      121 gelidflcer plyyewhnyl fvhagvdltk kdwhdtnphd fiwirepfhe gknntgktiv
      181 fghtitpmlh gdmettdlwi hdkkigidgg avfggsmhgv vfdetgivqd ieyqntegpw
      241 qgn
//
LOCUS       WP_010719150             185 aa            linear   BCT 01-JAN-2025
DEFINITION  guanylate kinase [Enterococcus hirae].
ACCESSION   WP_010719150
VERSION     WP_010719150.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..185
                     /product="guanylate kinase"
                     /EC_number="2.7.4.8"
                     /GO_function="GO:0004385 - guanylate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006163 - purine nucleotide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21167
     Region          3..177
                     /region_name="Gmk"
                     /note="Guanylate kinase [Nucleotide transport and
                     metabolism]; COG0194"
                     /db_xref="CDD:439964"
ORIGIN      
        1 mnkcyvfigp sgsgktsian alfepkekiv tsttrpprkg etdqkdyyfl sedkfeqlit
       61 eqafvewdey aghkygstkr eiaqklkngd cytiltaagf walfhafgeq iqpvfvtiak
      121 nklkqrleqr gdapdqikkr lalfeqdtke ldelkkrpnl ivlannegle atknqfkrqi
      181 kmlke
//
LOCUS       WP_010719144             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus hirae].
ACCESSION   WP_010719144
VERSION     WP_010719144.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..282
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31176
     Region          1..272
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkivtivcl fvlvligggc hskdqslhaq kkheivmgvt ggpyndlfdd aiapileseg
       61 ytikriefsq fiqsntalge gkidvnvaqh saymnvfnke ngtdlvplva tpsvpcnlys
      121 skytskeevk kgmmigipqd psnaarayav lakagfiqvd kqvkstdlta kaitnnpyql
      181 nikemdtntl phvlddldfe vipgstveda gireqlhlie lekmvpelqi vaavtkenek
      241 tdwakaikka yqsekfrtyi nshnkdnywi vpdisetens sq
//
LOCUS       WP_010719166             266 aa            linear   BCT 01-JAN-2025
DEFINITION  hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
            [Enterococcus hirae].
ACCESSION   WP_010719166
VERSION     WP_010719166.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..266
                     /product="hydroxymethylpyrimidine/phosphomethylpyrimidine
                     kinase"
                     /EC_number="2.7.1.49"
                     /EC_number="2.7.4.7"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008902 - hydroxymethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008972 - phosphomethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=28685
     Region          3..246
                     /region_name="HMPP_kinase"
                     /note="4-amino-5-hydroxymethyl-2-methyl-pyrimidine
                     phosphate kinase (HMPP-kinase) catalyzes two consecutive
                     phosphorylation steps in the thiamine phosphate
                     biosynthesis pathway, leading to the synthesis of vitamin
                     B1. The first step is the phosphorylation of...; cd01169"
                     /db_xref="CDD:238574"
     Site            order(3,10,12..13,15,19,22..23,26,29..34,36,39..43,48..49,
                     51,53..54,57,60,64..65)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238574"
     Site            order(9,21,42,78,212)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238574"
     Site            order(103,140,174,209,211)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238574"
ORIGIN      
        1 mrkiltiggs dpfagggiqs dlktfenfql fgmsaltcvg mldennafll enlpakwleq
       61 qlasiqkmtd lagikigllh sleaimivrd flkkhpqipi vldpvlafke ttslanqqyi
      121 eclvkelfpl vdlvtpnlke aallsgkkki ssineviett kfihtlgska vvvkggsgih
      181 gdeaidvlys hdglttftme kltrstvnga gctfssaita nlvhgytlpk aiqrsktyvy
      241 qcilngvemn dqtgsvwsgg nikggi
//
LOCUS       WP_010719225              68 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Enterococcus].
ACCESSION   WP_010719225
VERSION     WP_010719225.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..68
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7703
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mttgtvkwfd nkkgygfisy deteeifvhf taieeegfkt leenqsvefe iiegnrgaqa
       61 ahvkkmil
//
LOCUS       WP_010719278             304 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Enterococcus hirae].
ACCESSION   WP_010719278
VERSION     WP_010719278.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..304
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33657
     Region          41..297
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mflqlattat tstgetltdq avhqvnafqr fwntidwdai fatfiqkgly lvflillfai
       61 lnrvgkylid ksfkqyskks vlnesrlktl hsllntifqy tmgfffiyai lsvigvpigs
      121 llagagiagv aiglgaqgfm sdviagffii meqqmdvgdy vklanlsieg tvasvgirtl
      181 qlkavdgtvh fipnrnitti snlsranmqv lldirivpee gydsiyeiid rvnqrlaeky
      241 qddlqtepti fglvdlgnsn fairticyal ngkqfvlkee flssyvkelt tagftipnsp
      301 islk
//
LOCUS       WP_010719306            1176 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Enterococcus hirae].
ACCESSION   WP_010719306
VERSION     WP_010719306.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1176)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1176)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1176)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1176
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..1176
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=137568
     Region          4..1159
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mslqfilgta rkdhrtalid esvewlakds thqvfflvpn ynkfeqeqei ltelrqrsgk
       61 tsfsttnvqv fsfyrlawyl lqqttllsgn elsesgsami lrqileknee nltifrgein
      121 kkgfirqlqe lhnelrigni spedlvfsel adtvkaenqq lkmkdlqlif tafeeelvqr
      181 alqsedalti lanylqtqdm skvkfivsgf trvnaqeyql lqvmmekgql vidllldrpy
      241 itnmpevltl fhetgklyfq linsakerrv pvlvekfape herplalmhl qkmweetssn
      301 kksqplkigq qealriweae nateevrqla veirrlvsee nyryrdiqvl tkdmafygnl
      361 lqpvfkemai pfyideeqlm enhpliewin slfaldryay rlndimrffk telficeadd
      421 tldlaswreq rnqfrakldv tenvalayny qgsywtrekd wqfvsydfea eqledvqele
      481 krsndirhff kekvptffdk ikkckngqeg atifyrflvn sgvqqqlvfw rnqeiergnl
      541 aaarnheqtw galidlldey sliygesefd whlfqeiits glenlsygki ptaidqvrin
      601 rlelvrsnqa kvtfviglnd qvfpdrhetk gllsseeret lnarlaeekf lfdpakenls
      661 feplqaylvf asatqrlyls yaqsydtntl kispylkrim eylmipaerk ehlvldsdps
      721 cyigtyrsgi ntinhiyrla keekkkipvy wrqlreqilq sqwrnfalri fesqehlnvp
      781 vslpkkmaee lygkdiytsi srlenfynce ykyfvqfglk lkermvyglt paatgdfyhe
      841 sldrffkllf snqislvemt dtqrkeftek vlqdvfgelr feildssarm nyiryqlgqt
      901 iqkvawalqk qsentgmkpl qteilfgqia gaqgipglel plnnggklhv rgkidrvdva
      961 veqadtwlsv vdykssgrsf dvteayygma mqlltyldva lmdavkltgk alvrpagsyy
     1021 lhvhnpilse aneieketlk kfsydgifvd epellevldh sleakensli ypikknakdv
     1081 yqkgsfskek fyteqelqlf mahnranmrl agdkitsgei klnpaykdke rlacqmcpfr
     1141 svctfdvmlq ennyhrlekl nkeealrrie krseee
//
LOCUS       WP_010719392             436 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleobase:cation symporter-2 family protein
            [Enterococcus].
ACCESSION   WP_010719392
VERSION     WP_010719392.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..436
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45913
     Region          14..420
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 meketkngqa avlglqhlla myagavavpl ligtglgfnq eqmtylisid ifmcglatll
       61 qltvnrffgi glpvvlgcai qavaplilig sdqgvgaiyg siiasgifvv lvsgffskik
      121 rlfppivtgt vitvigltli pvaiekmggg dssatnfgnq tnlllafvti alivgvqmla
      181 kgfvrsiavl iglvggsila avlgmvdlsa igqapvfhvp qpfyfgkptf dvwsillmii
      241 isivsmvest gvyfalgdit gqkvgeeelk kgyraeglav ilggifntfp ytgfsqnvgl
      301 vqlsgiktrk piyfsaifli ilglfpkiga laqiipepvl gggmlvmfgm vavqgirmlm
      361 evdftndknl litavsigfg lgfnimptlf sqlpptvqmf tgngivmssv taivlnlifn
      421 glkkdeeiie ealakk
//
LOCUS       WP_010719450             255 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            hirae].
ACCESSION   WP_010719450
VERSION     WP_010719450.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..255
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29043
     Region          2..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 metrrtsdll sylvkkkqat skelcthlhc sistlrrell elekrklirr twggailnet
       61 tnmeytylqr easnipekki iselardfia pgmcifldss stvlhlipll vkipnliiit
      121 nglrtalkls ecqneslkiy ltggevklna stvisntldp itsssrfnaa flscrgldhe
      181 giyeanfnqa qikkemmnka qeivlladet kfdsthffki gdyydydaiv tnkkppkiyh
      241 riiekndihl vypte
//
LOCUS       WP_010719560             419 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Enterococcus].
ACCESSION   WP_010719560
VERSION     WP_010719560.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18643657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..419
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=48106
     Region          33..62
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          38..301
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          67..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          177..200
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          208..233
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(209..210,213..214,216,240,243..244,247..248,
                     250..251,274,277..278,281..282,285)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          210..>411
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          238..268
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          273..301
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          307..332
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          339..366
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          373..401
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mntnsekmlq alseedlaqa qlyltqalke dpadvlaelg eellaigfle eakqifeqlv
       61 kqypendelf iplaeiaied neidqafeyl eniskesdyy pqallaiadl yqvigipevs
      121 eaklkeaaal lpdepliqfa laelyfsvdr faeaatiyql llssnideis gismqerlgq
      181 slsmqgefea aiepleqalq eertddrlfq laftnlqlke nekainylqe lrevnpqyqs
      241 lylylgqalq eeelieeaqk vledgikenp yqvelyhlas enayrlhdke kaeklllnal
      301 elgekqdetl ltlsnlylde eryedviksi eqmeetanpy aewnlahayn eledftlaav
      361 hyeqayhele hepdflkeya lflreegqlt ktkdllthyl elepgdleal svlddlaer
//
LOCUS       WP_010719600             258 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Enterococcus hirae].
ACCESSION   WP_010719600
VERSION     WP_010719600.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..258
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=29310
     Region          26..203
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(106,113,129..131,173,179,183)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 msdyqqkalk lsivplclli glilcvkinp pwfetldlav ytkidlpnfp qltaivrlfa
       61 klatigptlc faflfafyiw kknyhllaiw nicnifavsf fgyilkklia rirpavsqle
      121 irtsysfpsg hsllffalfl tiilslsiiw srqdtrrvaw ylisypllma atrlylrvhy
      181 psdilagfsl savvvllsyv icfsfistds ilktrqlekk ktlfskkqkv vlgllvllla
      241 vilsgvayel nvfyhahg
//
LOCUS       WP_010719605             242 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Enterococcus hirae].
ACCESSION   WP_010719605
VERSION     WP_010719605.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18604970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..242
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28491
     Region          15..>110
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
     Region          42..196
                     /region_name="Methyltransf_31"
                     /note="Methyltransferase domain; pfam13847"
                     /db_xref="CDD:463998"
ORIGIN      
        1 mneeewdafa ndyymnqkes dktivrdvie ylkkeaalpt ekivdvagga grylamskea
       61 ttyelidfsn emlkfateea arlgrenihl tkqtfsefle ngktydfifs asnpalddsv
      121 klsrmltkmk kycvilrvvs skedlltsle kklgifeeda vtspvimdql esylkdeews
      181 ykrkeftytf keeitedfmr ayyqeyleet ffkeyiqkyf dlkekivstt mltyrlllik
      241 ke
//
LOCUS       WP_010719617             202 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus hirae].
ACCESSION   WP_010719617
VERSION     WP_010719617.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..202
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22723
     Region          15..196
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 meyffqagkq tsrnllllhg tggdeyslle taqflepdtt ilsfrgsike dgmnrffrrn
       61 glnqfdyqsl aeetallyhe isavsqkeni slhdwvivgy snganiaahl llsrntelrk
      121 gilfhpmsln anypakimtd tqiwlsyskt dpivssiait nlikdfemqk ahltfqetft
      181 ghqltkaeli aakswlssls vn
//
LOCUS       WP_010719646             269 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus hirae].
ACCESSION   WP_010719646
VERSION     WP_010719646.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..269
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30158
     Region          5..264
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,195,217..219,221..222)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mnrkliaidl dgttlnpdsi itskteetlk kainaghhvs iatgrpfrms yhyyqqlgls
       61 tpmvnfngal vhipnqywah eketsidkri vfeilaqkrq lnldfiaaen retyfidsfd
      121 ffdekifaas npspqnllsp knlttdptsl lvrtekcyae qvsaeltrqf ghfvdvrtwg
      181 gpmailelvs kgiekakgvh rianyldidq kdviafgdeh ndlelleyag wgvamkngtd
      241 qlkgvandvt ehtnqedgla tyledllal
//
LOCUS       WP_010719663             244 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Enterococcus
            hirae].
ACCESSION   WP_010719663
VERSION     WP_010719663.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..244
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26983
     Region          5..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 makslikith lnkkfgeqev lkdvsaeiyp gevvvllgps gsgkstllrc inlleiptsg
       61 eikfegmtit dkqndifktr ekmgmvfqqf nlfpnmtvle nitlspikvk kqskeeatki
      121 ardllkkvgl lekadtypqs lsggqqqrva iaralamqpd vmlfdeptsa ldpemvgevl
      181 eimlqlaree mtmiivthei gfakevsdrv lfmdggtile egtptaifeq tshprtvafl
      241 skil
//
LOCUS       WP_010719729             324 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Enterococcus].
ACCESSION   WP_010719729
VERSION     WP_010719729.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..324
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37498
     Region          4..211
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mceisiivpv ykvekylkkc vdsilaqtfs dfelilvddg spdnsgricd dyakkdarvr
       61 vvhkqnggls sarnagieva kgkylgfvds ddyiaedmye llykaiikee adlsicgiyd
      121 vyegkdpiik ptikktvtae ealllilqgn iisvhavnkl ykrelfstir ypegkyheds
      181 fiivdllnqc hkvaidseqk yyyyhrlgsi ntesfsekqf efieawenne iklkdrsqei
      241 kkaahqrvcf anflvldkii vanvtdrpet keivsylrhn frfimeneif tksrkfstll
      301 lmislhlykf pvefrrkhit ktkd
//
LOCUS       WP_010719734             346 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus hirae].
ACCESSION   WP_010719734
VERSION     WP_010719734.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..346
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39644
     Region          3..>179
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msnpkfsivi piynaestia rtiaslkefd ftdyevllin dgstdqteai itrliendpk
       61 frlittanqg pglarnegim qaqgtyilff daddtpkkev lsdydkllak hpdtdlivss
      121 fifrtmdgeq iisekenlvt ehhyqshdsf ikdmyrlmnd qlmyvvwnkc yrrdilkqnq
      181 llfkgynsce drifnlhyyk ycqnvlmnpk isyiyefegg kgitnqyrpn kfstfkefyq
      241 lanevtnevd kpgmaalhlk gttsvifsiy gtstrtakek kaeakriltd ptiveakkia
      301 ctdstvkkvt kqlynlpssl fltavrigsf veikmpglma tlkrvy
//
LOCUS       WP_010719739             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010719739
VERSION     WP_010719739.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..268
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31428
     Region          9..268
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mfkdlflfmk diyqnrklll qfsvndfksr yagsflgilw afinpvftvl iywlvfgfgl
       61 kaamtdgkyp fivylitgmi pwfffsdaft sttlvfreyt ylvkkvvfni rilpttkils
      121 nlyahlffif vglvvvighg iyptwmtlql iyylfcmcaf ltgltwltas iqpflpdimq
      181 litivlqlvm wtlpilwsps qfnpvivqil klnplyyvvq gyresflgqa wfwehgmytl
      241 yfwvftlaif vigsavfrrl kphfsdvl
//
LOCUS       WP_010719777             415 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cell division protein FtsQ/DivIB [Enterococcus].
ACCESSION   WP_010719777
VERSION     WP_010719777.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..415
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=46511
     Region          110..336
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mskkkkpdkl pnesegeqnl tpwqkanrky laehekkeeq keeqkeekne ntnepaasts
       61 atkeadsaeg ekqeatasdp mkkgdsepfe kieqpkigsp yngsflnrlp nlknqrnkvl
      121 yrrltfiisi ltiplifliy yvspysrlqg itvsgnqmit sqtaiadshl aidgnvwsqy
      181 fhknqyldtl kkeqprvesa qlhfksintf elaikeykei alvmkdgeyf pviengkvlk
      241 ekvanptknl pilenftdna kisqlvkeyn qltselqkai seikytpkes nknliqlnmn
      301 dgnqvivniq nlasqmkyyp qvakemkekg vidmevgifs ypyseskken ggatdpsvqt
      361 sstenltgqs gassdqsdqs sesvesnqag qsentsessq iddnssssss dlten
//
LOCUS       WP_010719812             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: O-methyltransferase [Enterococcus].
ACCESSION   WP_010719812
VERSION     WP_010719812.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..228
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25598
     Region          47..222
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mrnemmhrpv vkeelvdfmr tkqkklsgel glieeeahla evpiiphetv vfmqfllgql
       61 kpknvleiga aigfssslma qlisekghvt tidrfdvmik kakatyerlg ltekvtlleg
      121 qaadilpelt gpydfifmds akskyieflp eclrllkkdg vlmvddifqg gtillpdeei
      181 prgkraihrk lneflqvvmt hpdltstlvp lgdgvilitk ekeqihlp
//
LOCUS       WP_010719843             361 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010719843
VERSION     WP_010719843.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..361
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41034
     Region          1..344
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mgkpiisfdq vvkryddeti lkkvsfeieq gkfytllgps gcgkttilri iagftdateg
       61 emyfegkrln dvpankrqvn tvfqdyalfp hmnvfdnvaf glkikkmnkv diekkvkdal
      121 rmvqlpgyen reisemsggq rqrvaiarai vnepkvllld eplsaldlkl rtdmqyelre
      181 lqqrlgitfi fvthdqeeal amsdeifvmn kgkivqsgtp vdiydepinh fvadfvgesn
      241 ivdgvmiddn lvefvgkrfe cvdggmrpne pvevvlrped ltittpdkgk lvvtvdtqlf
      301 rgvhyeivcy deqqnewtvh stkkakegsk vglafdpedi hvmrfnesee efdarldsye
      361 e
//
LOCUS       WP_010719889             185 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Enterococcus hirae].
ACCESSION   WP_010719889
VERSION     WP_010719889.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..185
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21048
     Region          2..172
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mlyvtrhget twnaaervcg radapltekg qkqaeklaek vselqipvtk iihsplqrak
       61 dtaqavadkl hlpmevderl iemdfgeydg mpshetifqe arqefavrfp ngesvldvya
      121 rvvplieecl adeenvyllv chnalirimn ayfhpmpnet ffvffvente lvtfpskhel
      181 ntiks
//
LOCUS       WP_010719903             411 aa            linear   BCT 01-JAN-2025
DEFINITION  M20 family metallopeptidase [Enterococcus hirae].
ACCESSION   WP_010719903
VERSION     WP_010719903.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133889
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..411
                     /product="M20 family metallopeptidase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43974
     Region          23..365
                     /region_name="M20_Acy1L2"
                     /note="M20 Peptidase Aminoacylase 1-like protein 2,
                     amidohydrolase family; cd03887"
                     /db_xref="CDD:349883"
ORIGIN      
        1 mttstistnr ssllketiqe rlpeyqalal dihqhpevsn yefyssaali rqlekegftv
       61 ekevaghrtg faasyrsdkp gptiaflaef dalpgighac ghnlfgtysv laasiikkqi
      121 deiggeirvy gtpgeeggen gsakgsfvre glfddvaaal cahpayrygk tteslandpv
      181 dikfygvash aaaapekgvn alealiqvfn vinalrlqlp kdvnihgiit nggvaanvip
      241 eyaagrfylr agnrqtldiv fkkveqivkg aalstgtsye fglfqnavdh miptpsfdel
      301 ffthakaagv peteidvtek tslgssdvgn vsqviptiqp tisisdeyia ghseefkaaa
      361 ksekglasia iaaellaata ldlfeqpall tkiqeehqql leksqltgst f
//
LOCUS       WP_010719933             444 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus hirae].
ACCESSION   WP_010719933
VERSION     WP_010719933.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..444
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=48446
     Region          1..423
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdkfvglieq kimpvanrig tqrhmtairk giiatmplti vgsfftilln ipiesvaavi
       61 epyrqildip frytigilal yatfgiassl aksykvdflt agilalmsfl ivaapptqvl
      121 edlegitagr yinianlgsg slfgaivtai isveiyrffi ekkitikmpd gvppevtnsf
      181 valipgavil iffwvirhml gfdlngflse llmplkgila gnslfggllt vflicffwvl
      241 gihgpaimgp virpfwdisi aenidafnag anahnmpnif teqflqwyvw iggagttlal
      301 vvlfmfsksk ylkslgrlsi lpglfninep mifgapivmn pvlgipfila plvtttlsyv
      361 ltvsglipmm tarlpfaips piaawmstnw svaagvlvia nflitlaiyy pffkvfekqq
      421 lareaeeqaq eeapmvtgvt eeqa
//
LOCUS       WP_010719965             368 aa            linear   BCT 01-JAN-2025
DEFINITION  AAA family ATPase [Enterococcus hirae].
ACCESSION   WP_010719965
VERSION     WP_010719965.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 368)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19843850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..368
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42930
     Region          3..>291
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          4..>101
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
ORIGIN      
        1 mslklkgiki dsfraferqk yfdyvnpvfn eisnlivlya pngtgktsff daiewsltge
       61 isrlnenknv rdidsqerky ilknkyssae vgsvelafdd gsfyalttkk lngkqttdyv
      121 egnetkktvd ltakelkilr qknllthnqi daflrsqsae grydalsnfw dkenvsedyk
      181 nlvlfvnemn kalgqqetkm nqltkeiekl esnakiwqti nqlkenyakl ngknskkdpl
      241 lknqlglqel yiesnklksn nqiklnqfde erqqlenlit mtqeyrqipq qiewsekqva
      301 dvneklahlt eietieekkk alfdekidls nhlkrcnfli nheadfqaqe maeknsnrei
      361 newinqrk
//
LOCUS       WP_010719994             315 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus hirae].
ACCESSION   WP_010719994
VERSION     WP_010719994.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..315
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35152
     Region          81..288
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mterisleks aiefsdanap hpriyelppe egrallekvq espvdklpvd iedltvdtgq
       61 wgsinvrfvr pegntdklpv ifyihgagwv fgsaqthdkl irelavrtns vvvfpeysrs
      121 peakyptaie qsyavlqkls elaeskgldl selavagdsv ggnmatvmti ltkerqglpi
      181 qkqllfypvt danfttdsyq efaenyfltk egmkwfwdqy ttdesersei tasplratse
      241 eladlppali ltgeadvlrd egeayarklr dagvavtqvr fqgmihdfvm vnsldqtnat
      301 raamllatqw lqqdr
//
LOCUS       WP_010720006             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010720006
VERSION     WP_010720006.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..220
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24565
     Region          110..214
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mtkritepnn qvlrimiafg vlgagfyglt qvdfyyiqfs flvisglvsy llvfgfvgvr
       61 qlfstpkrfi ktfllilvgs qiygmlasmi mgilaqlldi qtkansaqdn pwwffvfilp
      121 iallgeelfs itifdtlrkk mgintkvasl ltaiifglih fetylgssal ftivqvilvq
      181 ggirlwfnqa ylktkslnts wavhyafdli afvlgsllss
//
LOCUS       WP_010720077             252 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010720077
VERSION     WP_010720077.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..252
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28560
     Region          22..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mtesrkeqil tllkkykkld nselqkqlfc spstlrrelv alekdgiirr yrggvvleve
       61 rnhvistnyr envmvqekek iaeiastfig pgmslfidss stvkqllpyl vklsnlvvit
      121 nglkiayels qactedskvf mlagevikda esvvgdygns fldlfqidlc ifsstgidls
      181 giyeanfaqa lvkkkvmsrg dkslllvdyt kfdkkhaykf sdwtsfeyiv tdqqpaddyl
      241 qlalkhdtef ly
//
LOCUS       WP_010720175             176 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: shikimate kinase [Enterococcus].
ACCESSION   WP_010720175
VERSION     WP_010720175.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..176
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19910
     Region          4..167
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 mtslvligfm gagkttiskk laarldqpvi dmddylvqql gcsieqyfat fgeaafrdhe
       61 tallktilqk kaviatgggv vlqkenqell kqqqviylkg eadilierir qdqtnirpla
      121 lknsdtklre imwerekiyk slakitidts kkspdeiite iikwvennde nwvsrs
//
LOCUS       WP_010720188             323 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Enterococcus].
ACCESSION   WP_010720188
VERSION     WP_010720188.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38147
     Region          41..125
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <161..323
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mftfeqlktf lmenneiecr qqidgqnind qqlpyetvav pkmpknqffk egnifinkhh
       61 ryaempahth efvefnymls gscvqyvndk kihlkegell lldkeivqri dpleeedlli
      121 nillkgesit tdivinmvks rglvneflln asqekgkhde fihfhcgdnl evqgllhkmi
      181 leyynkqdyy mralnlrlsl llieltrdle eyvtqrenqe lleilryidl hfrkltlknl
      241 akhfgynany lsnklkketg ssfqelinsl ryktmielmr etnktfeeis yelgfetlas
      301 lyklvgkyte ltpkelkdsl lkk
//
LOCUS       WP_010720250             490 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Enterococcus hirae].
ACCESSION   WP_010720250
VERSION     WP_010720250.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..490
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52487
     Region          23..477
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,279,282..283,286..288,291,319,323,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 mnknqpvdiy gkpynrtllv vvlligtfct vlnqtlltta fptlmkdfdi sassvqwltt
       61 gfllvngimi pitawlinkf ssrslylsam svfligtitc fvapsfstll igrliqacgv
      121 gvsmpllqni mlsifppekr gsamgmsgiv iglapalgpt lsgyiidnyh wrdlfgmvlp
      181 ivvlvlvlaf flmrsvipls npsidilsai lstigfgsll ygfssvgdag wgsakvigfl
      241 ivgvifialf awrqlrlenp flelrvfkss tftiaavlag vtnmamvgae mvvplyiqni
      301 rgesafhsgl mllpgalimg ammpitgaif dkhgakrlai vgmfvltaat apfafltktt
      361 pvlyivvlya irmfgismvm mpvttsgmna lpnklishgt avnntfrqia ssigtailis
      421 vltnvtkdnl paksvlestp ltykdqaina tlsgyhaaff vaivfgvigf viafllkrke
      481 pvlakagdka
//
LOCUS       WP_010720252             183 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010720252
VERSION     WP_010720252.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..183
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21897
     Region          3..90
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          98..178
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 markntlryi llgllskkkm tgyelnqsfk neigefwqak hsqiypelar meergiikhe
       61 veitgmklek kvyqltdegk allnewirtp tnelpvnrde fvlklyfvkd vndpmlreii
      121 eqqrdlheek rahllarqer ifptrkeqee nyghylilsh ainreteyan wltsvleeqk
      181 rqk
//
LOCUS       WP_010720258             764 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus hirae].
ACCESSION   WP_010720258
VERSION     WP_010720258.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..764
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88308
     Region          4..757
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mkqikrlfqi dpwkistntl drenlrlqes ltsigngymg mrgnfeeays gdhhqgtyla
       61 gvwypdktrv gwwkngypey fgkvinainf iamdiyideq lldlatiepe dfywelnmkn
      121 gvlsrsytvt tatnklkitf erflsivkse aayirltvtm legngtvkvi skldsnvqne
      181 dsnydehfwn eigrgtsdet aylmtktipn nfaieqftvt aamrhfvnee laqpiyhedt
      241 lavlgefsfe lttnqsvild kevlvltsrd ipeaqqvqqi lqefsdlqsh ylqakaeqtt
      301 awskrwalad vviegdeeaq qgirfnlfql fstyygeder lnigpkgftg ekyggatywd
      361 teayavplyl alakpevtkn llkyrhnqlp qaihnaqqqg lkgalypmvt ftgvechnew
      421 eitfeeihrn gaiayaiyny tnytgdtayl kkeglevlve iarfwadrvh fskrhnkymi
      481 hgvtgpneye nninnnwytn tiacwvltyt renylkfqte tavtvtdeel tnwqtiaenm
      541 yfpkdeelgi fvqhdtfldk ellpvselsp selplnqhws wdkilrscfi kqadvlqgiy
      601 ffndsfskee kqrnfdfyep mtvhesslsp sihailaael gmedkavemy qrtarldldn
      661 ynndtedglh itsmtgswla ivqgfaqmkt dheqlrfapf lpntwtaysf hvnyrgrllf
      721 vsvsseqvql tlvsgescpl kvyektylle dqlkvplrke eldv
//
LOCUS       WP_010720412             269 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus hirae].
ACCESSION   WP_010720412
VERSION     WP_010720412.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..269
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29532
     Region          4..265
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,196,218..220,222..223)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mikliaidld gtllneekqi sdenkqalak akekgvkivl ctgrplaama hylqelglvd
       61 egdysitfng glvqkndtge iiekkvmeva dihrlydlaq klalpldils dhvvlqlpta
      121 pgkkslyntl nkllqfqpan ladltdefvl nkaviaypqa eldpkikeip aefheryeii
      181 ktrsmllefm pkgvtkaygi sllakdlgle paeimaigde endlpmieya gmgvamanav
      241 pfvkeaadyv tssnlehgva kviekfvld
//
LOCUS       WP_010720469             377 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010720469
VERSION     WP_010720469.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..377
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39833
     Region          1..357
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mndrnekirn llvpifsvil glvlgailma afgynpgqgy ssmlnaslgs qrsigetlrq
       61 atpliftalg fsvansagff niglsgqalc gwivsvwval afpdlpkvil lptcvilgal
      121 agalaaaipg vlraffgtse vivtimmnyi llylstfalh dimpdtyrss ldssnligqn
      181 aslrlpwltq mfggsrvnag lflalialvv vwllmkkttl gfeirsvgln pfaseyagms
      241 skrtivfsmm isgalaglgg vveglgtyqn ffvqttslai gfdgmavsll gsgsaigill
      301 sallfsilki gglgmqtgag ipfeivnvsi aliiffvgin flirfimakf fqgkkqeaiv
      361 etveskptnq sqeggel
//
LOCUS       WP_010720478             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Enterococcus].
ACCESSION   WP_010720478
VERSION     WP_010720478.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..201
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22342
     Region          18..200
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mtnhyysqep ttehdfeqws felkgknfqf vtdsgvfsre tvdfgsrvli dtfnweelpv
       61 dgkildvgcg ygpiglaiaf asqrfvemvd insravelaq gnanrngikq vdihqsniye
      121 avheetyaai vsnppiragk kvvheiltea yprlksggtl tiviqkkqga psakskmaet
      181 fgnaeivhke kgyyiiksik e
//
LOCUS       WP_010720667             196 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus hirae].
ACCESSION   WP_010720667
VERSION     WP_010720667.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..196
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22204
     Region          1..176
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mismivyssl issvmtvaht lledhtrkfd lfvalrpgsk sqyylsmliv flslnilsvl
       61 alimtgilvn qltinwfhli gllflvplls fpliligmii sllgsdnvvn llsnlivfpm
      121 ailsglwwpl simppwvqkv ghwlptyqta vilrrfinyq rfnfvsfgvl lvwtiilfvl
      181 fkvvvffqsk sevsti
//
LOCUS       WP_010720677             355 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Enterococcus hirae].
ACCESSION   WP_010720677
VERSION     WP_010720677.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..355
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41132
     Region          19..347
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mavkefnyre lkklslsydl lnmltkihey kgkqelyiat kpeilnkltd laliqsteas
       61 nkiegiattd grlkqiveek vmprnrdeee iagyrdvlkl ihdsyeyirv vpndiltlhk
      121 nlyrysgkny kgkfksgdnv itekdvdgne rvrfvpapay ltpdlieelc yqynqaiqka
      181 didplllipc fvldflsihp fsdgngrmsr lltllllyks gylvgkyisi emliegskqt
      241 yyealqessi dwleneqdyt pfvrylvgii lrayenfser fdmiinrelt paerlveelq
      301 ksfeplsrad lenllpdisr rtieralsel qtenkiqkig qgrstkyrls ntlka
//
LOCUS       WP_010720687             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010720687
VERSION     WP_010720687.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..304
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31526
     Region          4..298
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mtnlisifls sasqgvlwal laigvfltfr ildiadltae gsfplgagia avsitnglsp
       61 ivacllgflg gaaaglvsgl lhtklkipal lagiitmtgl ysvtsrimga pnlsllgqkt
      121 vftwaeslgv skenavliag llvalivvtl lvlflrtetg lairatgdnl amseangint
      181 dtmkiigymi sngcialsgs llaqnngfad lnsgigtivi glasiiiaev lfrnqplllr
      241 lltiilgavi yrfilalvfe lnvqpsdskl asalvlvicl sfpqiqqklk lpkrtkakgg
      301 sind
//
LOCUS       WP_010720721             194 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptidylprolyl isomerase [Enterococcus].
ACCESSION   WP_010720721
VERSION     WP_010720721.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..194
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=21189
     Region          11..194
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mvfpqlslen ekgpkavikt nrgditvqlf pelapktvkn fielakkgyy dgvifhrvip
       61 dfmiqggdpt gtgmggesiy gesfedefsr elfnlrgals mansgpntng sqffivnnen
      121 vpanmldqle gagfpaeiie aykgggtpwl dfrhtvfghv idgmttvdei anvqrgpqdr
      181 pvhdvviekv evse
//
LOCUS       WP_010720796             211 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010720796
VERSION     WP_010720796.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..211
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22981
     Region          1..205
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mielkkvska fgekkvinal dlvipdgqtm aivgpsgggk ttllrilagl ekadsgefyl
       61 dgvafdpfel ktkeqvvgvv fqdfqlfphl sifdnitlap kmvlkqsket ytkkaqelad
      121 slgisdllnn ypyqlsggqk qrvaiarala mnprvlayde ptsaldpelr qqvenlivsl
      181 kaegvtqiiv thdlvfaenv gdqlvkvipn k
//
LOCUS       WP_010720857             301 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus hirae].
ACCESSION   WP_010720857
VERSION     WP_010720857.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34124
     Region          19..96
                     /region_name="cupin_MmsR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MmsR, N-terminal cupin domain; cd06986"
                     /db_xref="CDD:380391"
     Region          <113..273
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 meqaiflkke rqelakgcyf dfcgfsktlp yhsfgpairq dyvlhvvmeg kgtyhvkeqq
       61 yqlqkgdlfl irpgdstfyl adgeepwvyc wlsfggplak eiierslfke dqytmvsagi
      121 sayidiildc lhysqdglad eleltaltyr flsvllkdgg kiglgnqkvs splaietvky
      181 ieehypenlt veeiarqlsv nrshlsrvfk nqlgtsikey ligvrinraa fllsltddsv
      241 esiayqvgfn slvvfsrmfk katgetatny rkrmkneask nlslgalkke leeqeivsws
      301 t
//
LOCUS       WP_010720866             235 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HAD family hydrolase [Enterococcus].
ACCESSION   WP_010720866
VERSION     WP_010720866.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..235
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27354
     Region          2..228
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 miksvvfdvd dtmydqqqpf rnavkkvvpl vsdidmgply lrfrhhsden fpkvmagkwt
       61 leymrahris qslkdldyph iteeeglyfq qvyeeeldni clheevkktl dfltemnipl
      121 giitngptdh qtkklnqlql anwipsqhmi vsqatgfqkp ekeifqlaee rfnltaeetl
      181 yvgdnydndv lgakragwqa lwfnhrerkv dgplncdiei tsfdqlletm kvifs
//
LOCUS       WP_010720888             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Enterococcus].
ACCESSION   WP_010720888
VERSION     WP_010720888.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..155
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16897
     Region          5..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlqqykkimv avdgsdeael afkkavnvai rnngelllah vidtrsfqtv ssfdgmlaeq
       61 atemakqtla dyeanakkag lnnvttviey gspkqiiake ipednhvdli mlgatglnav
      121 erlfigsvse yvirnatcdv lvvrtdlenk lpeke
//
LOCUS       WP_010720905             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HIT family protein [Enterococcus].
ACCESSION   WP_010720905
VERSION     WP_010720905.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..144
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16681
     Region          2..136
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mencifckii kqeipsykiy edekvyafld isqatkghtl vipkqhvsdi feydevlaad
       61 vfsripkiar sieeafpemq glnilnnnre layqsvfhsh vhlvpryske ddfsihfgnh
      121 qseysaeelq qiqhtivkqv knid
//
LOCUS       WP_010720918             433 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 125 protein [Enterococcus hirae].
ACCESSION   WP_010720918
VERSION     WP_010720918.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..433
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49183
     Region          6..430
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 maykdipksv qqfmdeitak cgeehadwat nfsaafantl lttvkrhedg ttflltgdip
       61 amwlrdstaq vrpylviake dedlasmisg lvkkqfeyin idpyanafne esngaghqsd
      121 htemndwiwe rkyeidslcy piqlayllyk ntgrtdqlnd sfvegikkal hvfkteqdhn
      181 qspytferdt trkedtlvnd grgsavaptg mtwsgfrpsd dacqygylvp snmfavvvlg
      241 yieeiftnil meetsskail eeakrlkedi qkgiedyalt knqqgetiya yevdglgnas
      301 imddsnvpnl iaapylgycs ttdeqylatr ktllskenpy fyegkyakgi gsshtpenyi
      361 wpialamegm ttedkeekkr ildllvatda gthlmhegfd vddpnnytre wfswanmmfc
      421 elvmdyfdir vak
//
LOCUS       WP_010720936             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: toll/interleukin-1 receptor domain-containing protein
            [Enterococcus].
ACCESSION   WP_010720936
VERSION     WP_010720936.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Nimma,S., Gu,W., Maruta,N., Li,Y., Pan,M., Saikot,F.K., Lim,B.Y.J.,
            McGuinness,H.Y., Zaoti,Z.F., Li,S., Desa,S., Manik,M.K.,
            Nanson,J.D. and Kobe,B.
  TITLE     Structural Evolution of TIR-Domain Signalosomes
  JOURNAL   Front Immunol 12, 784484 (2021)
   PUBMED   34868065
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Essuman,K., Summers,D.W., Sasaki,Y., Mao,X., Yim,A.K.Y.,
            DiAntonio,A. and Milbrandt,J.
  TITLE     TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes
  JOURNAL   Curr Biol 28 (3), 421-430 (2018)
   PUBMED   29395922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..272
                     /product="toll/interleukin-1 receptor domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=31488
     Region          17..>98
                     /region_name="TIR_2"
                     /note="TIR domain; pfam13676"
                     /db_xref="CDD:463954"
ORIGIN      
        1 mfeifkgkti slsnptvlls hssknknygd lirdllvscg vpndmllyss hkmneipvgn
       61 nifdylekti kvkkhavfll sddyfestac lnemgaiwln qnqytqlflp dfdlkhhsyl
      121 sccinskdkg ifltgddrcq kgltdfvrni lrdsflsfne telaynaeic cknlrdlipr
      181 dkvwksrise itenkgyvfa kienliptge vfkegenhwl qlntnyfpea esmkvgdria
      241 fkvkdfteck sfqelknyrn iyayretlei id
//
LOCUS       WP_010720985             439 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Enterococcus hirae].
ACCESSION   WP_010720985
VERSION     WP_010720985.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..439
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48751
     Region          2..434
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 merttmkktl tnrniqmial ggaigtglfl gsakaiklag pavlltyfvc glaiyglmya
       61 mgelflsnne fqsigdfiqy ylgerwaflv nwtywlcwmg aglteltaig lyirfwlpal
      121 splisgilal ialviinvva vrwfgelesl fstikifgil lfillgigvc flyfksprig
      181 vrenfdqlqt ifpfgltglv aafpmvlfsf agvemigltv getadpqknl kkaiqclpar
      241 ilffyigtiv aillvvpwqs ldlkesplvt mlqfihcskg agvinliilv aslsstnsai
      301 ystsrilynt akeknlskwf ltlssrgvpl hgilftggmf llglclhffv sdsrilfqll
      361 agmttisflf vwsailfahl kltksqlkkw kdrlilcffg lvgislffep ttrvipvvsv
      421 vwfgalnliy qrirqtspk
//
LOCUS       WP_010721042             491 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Enterococcus hirae].
ACCESSION   WP_010721042
VERSION     WP_010721042.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..491
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53412
     Region          14..407
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(21..22,25..26,29,60,110..111,113..115,118,138,
                     141..142,145,269,272..273,276..278,281,309,313,365..366,
                     370,374,390,393..394,397..398,401)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mkretnvklv tisvfiatfm taiegtivtt amptivgslh gmeimnwvfs iylltnamlt
       61 piygklvdkv grkpififgt llfiigslfc glsqtmmgli aaravqgmga gammpvalti
      121 igdlytiekr akvlglnssa wgiasvfgpl aggfivetis whwiffinvp iglllmvliw
      181 lylnepqreh eskpmdlfgs fslmamlval llgfqllgdq gftpvvigll igsllllflf
      241 iaaekrakdp vimlhlfanp lfvvvnlaaa lasgflmgid vyipmwmqgv lglnaavggl
      301 vlaplslvwm vgsflaskwm tqmatnwvlr iglliaslgg awlwlmpfes nflwffaist
      361 vigvglgitm ttstvsaqns vsrdqlgvat sfntlvrtig qtvmvavfgl lingvtqrel
      421 natnltndad imnklvnpqt akniaselit plrkilyegl hqvyfvglll vvvafaltfv
      481 vreksdrire y
//
LOCUS       WP_010721047             203 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus hirae].
ACCESSION   WP_010721047
VERSION     WP_010721047.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..203
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23617
     Region          3..132
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,63..64,67)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(62,113..114,116..117,121)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(68,73..74,109,112..113,116..117,120,123)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,96..97,109..110,113..114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(122,128..129)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 makigyarvs sidqnldrql ellskcdkif tdkasgkdtn regfqemmkf iregdivvvt
       61 elkrlgrnnk eltetmnliq lkkatlevln lpaltgitdd nlrrllnnli ielykyqaee
      121 erryiretqq qgialakakg kykggkpkys endprlqlaf klflegytdk eveqqtginr
      181 rtfrryrmky gvtsekrekk nel
//
LOCUS       WP_010721059             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010721059
VERSION     WP_010721059.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..256
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29086
     Region          1..247
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mnqqkrlmii merlekeksl tlqdimqltg vsrdtarrdt ikltdsnlvi rtyggislan
       61 sfnkidgylg rtdqelqvkk qiakeaskll lekqtvyldv sttisllpqy lanrninlav
      121 tnsidiadqf lkttsiptti lggtlnresr svtggypiwe ltkyrfdssf lscaginnqg
      181 iyyaheedia mkqavreksn kvvllcdhtk inlshnylvy sfeeidylit dkkipeelvv
      241 rigkskiiyt kensyd
//
LOCUS       WP_010721250             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar transferase [Enterococcus].
ACCESSION   WP_010721250
VERSION     WP_010721250.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..224
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25495
     Region          <21..223
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mdiqiedvvg aekikqnqkk yrmakrgidi vggviglvpf ciaygilyip ykvgsnkgpi
       61 ifkqsrigen gelfniykfr smrvnadeil kadeklhqky itngykleqs edpritrlgr
      121 firktsidel pqfinvikge mslvgprpiv teeleeyrne dkvaeflsmk pgitgvwqta
      181 grsnvgypdr vfleisyakk dsilfdlkil aktvfkvfmk egay
//
LOCUS       WP_010721261             191 aa            linear   BCT 01-JAN-2025
DEFINITION  VanZ family protein [Enterococcus faecium].
ACCESSION   WP_010721261
VERSION     WP_010721261.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..191
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21904
     Region          105..179
                     /region_name="VanZ"
                     /note="Glycopeptide antibiotics resistance protein
                     [Defense mechanisms]; COG4767"
                     /db_xref="CDD:443799"
ORIGIN      
        1 mrviksvvvl liavgisgll ihfialpvla gypriaqtme rfvytelvli sflalviwlf
       61 ylqwslgkls vvylylffsv ylfllfavlf tkapryqali lnpidfligg rlswlealln
      121 vcyfiplgll ygmkaryref vivalltivg iemiqfvfyl gtfaisdifl nfigcllgyh
      181 lyqplhehfq e
//
LOCUS       WP_010721265             140 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Enterococcus faecium].
ACCESSION   WP_010721265
VERSION     WP_010721265.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..140
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=16245
     Region          <6..136
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkdlldfrvv qifdsfcktv irnevrnikk qyarlrerqi sltelpesal asfqindtsm
       61 ensevflalg mellvanldv aeaihqlcep krkiillyyf agfndreige iigmsvggvw
      121 yqrrkaeeel rkyleenshe
//
LOCUS       WP_010721404            1049 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Enterococcus faecium].
ACCESSION   WP_010721404
VERSION     WP_010721404.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1049)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1049)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1049)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1049)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..1049
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=120968
     Region          8..943
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mkishreeae veeqlirvlg eghnqwtyrp dlkseedlwv nlrqkiisnn qaelndsplt
       61 dkefetikte lllrtktpfd aakwlkgeng maritiered pqlgsvslil ysnqdigggi
      121 styevvhqia krgsnieard rrfdvtllin glpivqielk qvtakdgvyq afnqikkyae
      181 egifrnnifs tlqlfvvsne qttryfanal pkdlhpkflf swrtkdnekv enlyefckqv
      241 lnipdahrli adytivsedq dnktlmvlhp yqvhaiqalf iaankhqsgy vwhatgsgkt
      301 ltsfvstkll arksgidrti mlvdrkdldn qttaeftkfa sefntgissg nakanslivg
      361 tgsakelset lladananvv iittrqklda alkyakkqee kkgtnrfqkl mgqhivfvvd
      421 echralsaen meeikkmfpk stwfgftgtp ifpenrkqak gqlartthdq ygevlhtyti
      481 knaledgsvl gfqvehentv eptslenkiy rklkevetya eysseqinrm idqmepvkke
      541 syldpavfea dehiqkvihk mfrpdnaytk fdfrngrptk sailttssid makkyyraik
      601 emtkepdwlt kefpnqpire grtmedpdfp riaityslee nsrdssaqqe emqkiieeyn
      661 qyydtawsla dieryngdin nrlarkraef kqfgkqidlv ivvdrlltgf daptiqtlfv
      721 drnleyagli qafsrtnrty pektkglivt frkpatmekn vedatklyse akeesgliyp
      781 syqeskkrfk qaygklkevs smesidehtp leirieyvka fqelnrayes lvtyddyndd
      841 mvksptlnnq iqlleeqigv yetvkgslie eepekegedf stiefysent tklydidsty
      901 idqllgtyaa nssdareeie kalaklnkte gvkevyrqil nafdmgtlds nedifvikrr
      961 yftqasddli hvfsnewfvs ekelhasnlq ympgedpipn mkaiinskdy egykakhpea
     1021 kpfkypqemk rawrkmldde liplenelr
//
LOCUS       WP_010721646             741 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-galactosidase [Enterococcus faecium].
ACCESSION   WP_010721646
VERSION     WP_010721646.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 741)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16044983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..741
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85442
     Region          39..298
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          302..648
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Site            order(349,380,424,489,493,539,558,561)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          661..738
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mdithrktek nfilfdeksr vfhlrntfls ylikieesnv lahiyfgkpv kqykenknyp
       61 rrdrgfsgni plnpdrslsk dtlpqeyssh gsmdfrtpas iiqrkngsdl ldlrydshyi
      121 tdgkpdiedl pqtyvldkse aqtlvislkd retaiyfdlf ytifsdravi trsvkirnet
      181 retiklekaa sfqldfahtr rfdevialpg aqvnerqisr qsllsgtkvf esrrgtsshh
      241 mnnfialvhh httentgeai glqfvysgnh sfelekdqin qlrvvggins hrfswelnan
      301 qsfqtpemil syssqglnkm sqihhellre riargrhqfa erpilvnnwe atyfdfnsek
      361 ikaiideake lgiemfvldd gwfgkrdadn sslgdwfeye gkltnglrei adyahskglk
      421 fglwfepemi sidselyrth pdflmqepgr mpsasrsqhv ldftrldvrq tiekqmrnil
      481 dtipldyikw dmnrslsdvy sitldpqrqg evahrymlgl yellehltad ypeilwegcs
      541 ggggrfdagf iyympqswts dntdavermk iqygtslayp issitahvsa vpnhqtgrst
      601 slktrgetam savfgyeldl tklspeekkq vkdqiisyqt irpviqyghy yrlaspfeen
      661 iaawmfvspk qdeaivflgr ilasaqpafh evylmgldde alyqeqtskr ifsgaelmav
      721 glyfpdfqgd fqtellhfkk l
//
LOCUS       WP_010721603            1049 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Enterococcus faecium].
ACCESSION   WP_010721603
VERSION     WP_010721603.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1049)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1049)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1049)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1049)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..1049
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=121005
     Region          8..943
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mkishreeae veeqlirvlg eghnqwtyrp dlkseedlwv nlrqkiisnn qaelndsplt
       61 dkefetikte lllrtktpfd aakwlkgeng maritiered sqlgsvslil ysnqdigggi
      121 styevvhqia krgsnieard rrfdvtllin glpivqielk qvtakdgfhq afnqikkyae
      181 egmfrnnifs tlqlfvvsne qttryfanal pkdlhpkflf swrtkdnkkv enlyefckqv
      241 lnipdahrli adytivsedq dnktlmvlhp yqvhaiqalf iaankhqsgy vwhatgsgkt
      301 ltsfvstkll arksgidrti mlvdrkdldn qttteftkfa sefntgissg nakanslivg
      361 tgsakelset lladananvv iittrqklda alkyakkqee kkgtnrfqkl mgqhivfvvd
      421 echralsaen meeikkmfpk stwfgftgtp ifpenrkqak gqlartthdq ygevlhtyti
      481 knaledgsvl gfqvehentv eptslenkiy rklkevetya eysseqinrm idqmepvkke
      541 syldpavfea dehiqkvihk mfrpdnaytk fdfrngrptk sailttssid makkyyraik
      601 emtkepdwlt kefpnqpire grtmedpdfp riaityslee nsrdssaqqe emqkiieeyn
      661 qyydtawsla dieryngdin nrlarkraef kqfgkqidlv ivvdrlltgf daptiqtlfv
      721 drnleyagli qafsrtnrty pdktkglivt frkpatmekn vedatelyse akeesgliyp
      781 sykeskkrfk qaygklkevs smesidehtp leirieyvka fqelnrayes lvtyddyndd
      841 mvqsstlnnq iqlleeqigv yetvkgslie eepekegedf stiefysent tklydidsty
      901 idqllgtyaa nssdareeie kalaklnkte gvkevyrqil nafdmgtlds nedifvikrr
      961 yftqasddli hafsnewfvs ekelhasnlq ympgedpipn rkaiinskdy egykakhpea
     1021 kpfkytqemk rawrkmldde liplenelr
//
LOCUS       WP_010721738              77 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Enterococcus faecium].
ACCESSION   WP_010721738
VERSION     WP_010721738.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..77
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=8700
     Region          1..65
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mttgivkwfd nkkgygfisy ddteeifvhf taieeegfkn leenqvvefe iiegnrgtqa
       61 ahvkkgnvqt tdtsmhe
//
LOCUS       WP_010721853             486 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010721853
VERSION     WP_010721853.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..486
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=51436
     Region          1..478
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mnglsswmek yilpvaakig aqkhlvalrd afigtlpatm agsvavmina iirdlpqqfn
       61 styadslaad kgifavlnvi igingfvwng tlaiaglifa fswgynlara ygvndlaggi
      121 vglatliqgi sfgpalsaal dvnvpsnvad ainsseigat ivdgtlsvgl wgwlkldhln
      181 gnayftvmim gaisviifck lmlanitikm pdsvppavsk afaailpati alyviaiiny
      241 ivgrvadgql iidlvqkyia epflglsqgl gavlivtvfv qvfwffgihg pnvlapvleg
      301 iwgqaqlini difqkgyngk tgtpavldai edgkaymwvr gsfdafawfg gsggtivlli
      361 ailifskrad yltvaklsig pgifninepv mfglpivlna imfipfliap vvataigwta
      421 tylglvapvs qqvtwvvppf llsflatgad wrapivtlvc mvvtfliwap fvisankmdp
      481 aageqq
//
LOCUS       WP_010721899             337 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus faecium].
ACCESSION   WP_010721899
VERSION     WP_010721899.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..337
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38186
     Region          79..336
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkkkilkfig wffgiilgia faiflafqls prpgaflinh mfsntvqitd kktfdqaekn
       61 vakktdltye skykentydi yypknskgpv pvlfwvhggg fvggdksgvk efatklvsda
      121 ntavvamnye lapdseypnq vlqvnelikd llaeekddkl ldmeqlffgg dsagsqialq
      181 yaaiqtnday akqmkikqll pkdslkgtis ycgpvdlklt aqqhsddrfm kffvktvaws
      241 ligtkdwkts eqlkeasvad hvskefppty itdgnaysfq eqgqalenrl telkvpvqsl
      301 fytdtkkeit heyqfdytlk esqncyqqtl dfvnkyk
//
LOCUS       WP_010722100             474 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Enterococcus faecium].
ACCESSION   WP_010722100
VERSION     WP_010722100.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..474
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54716
     Region          5..397
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mntkaksvik nlyytvaanf atlgisilln lfvpkllgvt eysywqlyvf yssyvgflhf
       61 gwidgiylki ggeeynkldk rslgsqfwyl tifeffvsia ivvwayffmp nssqslilil
      121 tavvsvitiv ktfilyifqs tnrikeyaql srndrylyvl fiaiyfalgg rdfywliimd
      181 iasklivtlw gmsrikdmlq vnmislkelv peifdninig sklmlssias mlilgtirff
      241 vqqrwsietf gklsftlsis nmfltfinav givmfpllrr tnqqrlpelf rilrdlfvpl
      301 tygllifyvp akivltmwlp eyteslnfmg ilfpiviyeg rmsllintyl kslrkektil
      361 mvnvmtlsfs lvaslviifv ignlnlavgl illslafrcn laeyflcrgm klpvgyrqlv
      421 etiltiafif sniwfggnfi slgiysliyv iyllyvhrsf lasfgefrsl lkdr
//
LOCUS       WP_010722328             159 aa            linear   BCT 01-JAN-2025
DEFINITION  TRAP transporter small permease [Enterococcus faecium].
ACCESSION   WP_010722328
VERSION     WP_010722328.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..159
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=17166
     Region          4..155
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mkvilnkvle ilgavllvgm vavvlwqvfs rtvlgnpntv teelvrfglv wfamlssayv
       61 vgqkahlavt vlseklsgkk skilevvvqs lflvfaamim vyggwnavtl tmgqispsls
      121 ilmgyvylsv pvsgiliiiy slinlidtls nkpaiqeki
//
LOCUS       WP_010722497             373 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Enterococcus faecium].
ACCESSION   WP_010722497
VERSION     WP_010722497.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..373
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40054
     Region          1..372
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mefigilcli listtigshi srrlgipavi gqllvgvllg qaglnwvkpd ilvhdfseig
       61 villmflagl esdlsllkky frpgmfvall giifpvvfgw ltgeafqvsg neaiffgiil
      121 aatsvsisve vlkelnvvnt kegstilgas vvddilvvlv lsfslsfltg eassnaslpl
      181 vlieqliyfv fifllvkwia sfllsfaekl yanssiiivs lviclgmsyv adlvglssvi
      241 gaffagiavs qtkvkeevyh nvealgyavf ipvffvsvgl evdfsdfseq llfisiltlv
      301 ailtkllggy fgaqitgfsq hsslmvgagm isrgemalii lqigqqsqli epqyysplvi
      361 villstlisp lvr
//
LOCUS       WP_010722596             188 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010722596
VERSION     WP_010722596.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21747
     Region          1..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrrkvytkdq ilkaaydvva kegfkgftar niakkmgist qpiylefknm edlkntllds
       61 ifeqlkedvf piertgdkii dlglnyiyfa kkhhslymal yidehgdgkk mhdfsynyfr
      121 eivkederyn qlsdeyvdal htgtwvavtg laslmssnim hpteeqiial ikrtidsilv
      181 ldnpeiir
//
LOCUS       WP_010722684             117 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Enterococcus faecium].
ACCESSION   WP_010722684
VERSION     WP_010722684.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..117
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=13355
     Region          8..99
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(29,32)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkqttnlsev qdilqqssva ivylsmsncs vchavrprle ellthydipa lhldafetpe
       61 vasrfevlta pvvlifhhgk eisrqarfid fkkirhllde ltaeddslsy eeifrte
//
LOCUS       WP_010722687             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus faecium].
ACCESSION   WP_010722687
VERSION     WP_010722687.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..279
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30444
     Region          1..273
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkiirfvvi tfvaiiwlag csqgkadttd kkettvklgi igedtdvwdn vkdrlkkeni
       61 nleyvkftdy nqpnaaladg sidlnsfqhq ffldnynkkh gtdlvsignt vnaplgiysn
      121 tlkdvadikd gakvaipndv tnggrallll qtaglikvdk akgqaptvsd itenrknldi
      181 seldasqtar alsdvdisvi nsgvavdagf npasdaifle pvddharpyv niivarkede
      241 knktyqkivd ayqtedtvkv iektskgssv pawetfgrk
//
LOCUS       WP_010722761             301 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010722761
VERSION     WP_010722761.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34484
     Region          16..97
                     /region_name="cupin_MmsR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MmsR, N-terminal cupin domain; cd06986"
                     /db_xref="CDD:380391"
     Region          <167..273
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 meqsiflkke hqqvekelyf dfcgfsktmp fhsfgpairn dyilhvvmeg kgsyhvknqq
       61 fqlkkgdlfl irpgdstfyl sdgedpwiyc wlsfggsaae eiirqslfre dqytmvssdi
      121 qkyidiilec mkdteetlen elqltaltyr flsvllkdgg kvsggvqkvh sslavetvky
      181 ieahyaekls veeiaqhlav nrshlsrvfk nhmgtsikey ligvrinrga fllsltdesv
      241 esiayqvgfn slvvfsrmfk kstgetatny rkrmknenfk nialdtlkkq lekqtavswt
      301 t
//
LOCUS       WP_010722800             512 aa            linear   BCT 01-JAN-2025
DEFINITION  gluconokinase [Enterococcus faecium].
ACCESSION   WP_010722800
VERSION     WP_010722800.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..512
                     /product="gluconokinase"
                     /EC_number="2.7.1.12"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046316 - gluconokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /GO_process="GO:0046177 - D-gluconate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56792
     Region          5..486
                     /region_name="ASKHA_NBD_FGGY_GntK"
                     /note="nucleotide-binding domain (NBD) of gluconate kinase
                     (GntK) and similar proteins; cd07770"
                     /db_xref="CDD:466790"
ORIGIN      
        1 mnvsigldig ttqtkavaft deaqeaasay frypliqetq gmaeqdqeli fqgvctvike
       61 vikqlpsdti iqfvsfssam hglilldeek tplsrmitwa dnraadeaek lkytvlgkef
      121 yrqtgtpihp mtplnkikwl qnsqpelfkk tayfvgikdy ifyrlfgeli sdygtasgtg
      181 yfdihefqwa eevldylnir ieqlpqvfps tyqvtglpsk taaelglpnd isfvlggadg
      241 plsnlglgaf gdtiaaltvg tsgalrfitt qpqfhpemet fcyvldqkhw vvggatsnga
      301 gifdwaghtf lqevvqsake kgenpydall saiafvpaga nglifhpyll geraplwdad
      361 afgsfiglqr qhtekemmka ilegiclnly rilkgvcqen qlteiratgg faqspifrqm
      421 madvlgyplv fptvteasal gavilgwrsi gkiqsiseaq elielkeqvg lqetdhkkyq
      481 kiyplfvstq khlaqtyqqf aqlreelads ek
//
LOCUS       WP_010722900             184 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Enterococcus faecium].
ACCESSION   WP_010722900
VERSION     WP_010722900.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..184
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20318
     Region          3..161
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtkkigffig slrkdsynkk vaeafakllp egyesvfvki ddlpfynedl etpeqapakw
       61 trfreevrgl dgvvfvtpey nrsvpavlkn aldvgsrpyg hsvwdhkpgl vvtaspggig
      121 gfganhhlrq slvflnvptl qqpeayignv anlidengni vegtlsffqt ildayldfsn
      181 klte
//
LOCUS       WP_010722938             258 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010722938
VERSION     WP_010722938.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..258
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29023
     Region          1..250
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlmedrlrki knrlkeqqsv sveelaeelg vskdtvrrdl iklekqkfvr rthggaille
       61 ekapifnyeq rasnanqvkv algekansli eedhsvifds sttvehviqh lsdkkinavt
      121 nslvhamlla klngttisll pgelhktqlf lygtetiekl kqykvdytll giyalssegv
      181 fihteeeglv krqmvkqatt viavadhskl dktgffkvcd laeidvlvtd rplsktldea
      241 lrqnhvscvc lekrstkr
//
LOCUS       WP_010722994             195 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar transferase [Enterococcus].
ACCESSION   WP_010722994
VERSION     WP_010722994.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..195
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22454
     Region          <28..192
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 myqkilkrif divialplli llipffivis lmikiedhgp vfynalrlgk ngvifkmfkf
       61 rtmkvnapdi rnedgstfns eldprltrig kllrksslde ipqlinvlig nmslvgprpd
      121 lpehydlytp lekkkllvlp gitgynqalf rnsipwkqrl qkdiyyveni sfnfdikiii
      181 ktfsnvimkk nvfgg
//
LOCUS       WP_010723021             602 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase, partial [Enterococcus faecium].
ACCESSION   WP_010723021
VERSION     WP_010723021.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         <1..602
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          <484..602
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 ppgasppvgq ppttsgqvgp ksgklrqdsk nprpserlwr dgepppgges agaaphagpa
       61 dkkaakdgkh meksklrmek sgkklntare klaaqkppkk pgpiktvgra akyqtwryvh
      121 gkihqveren vgteavhkte lagehlirgg trfiqkrirt rpvrqvrkwe rktisakady
      181 ayrqlvqenp slqsnplsrl wqkrqlkkqy rkqakeaakt gakaakkmav takniagaaw
      241 rfvrsnpkii llaaclflli vvlqscmgal ttigngliga vggtsyvssd sdieaveady
      301 taletalrek larierdyps ydeyrysvde ighdpfelas yltakyddyt pakvraelqy
      361 lleqqytlti tetvevryrt etrtdtwtet dpetgettth sdtyevevpy nyyilnvslr
      421 nkslgavala nldpeqiery hvyqktkgnr pnlfegniyv hpgeytdydi ppaaladpaf
      481 aaliveaeky lgypyvwggs kpstsfdcsg fvcyvldksg vypmsrttaq gifnqcakip
      541 pgeakpgdii fftgtydssg pvshvgiyvg dnmmlhcasg gvqyartdtk ywtehfyamg
      601 rl
//
LOCUS       WP_010723150             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Enterococcus].
ACCESSION   WP_010723150
VERSION     WP_010723150.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..135
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14915
     Region          26..127
                     /region_name="cupin_HNL-like"
                     /note="Granulicella tundricola hydroxynitrile lyase
                     (GtHNL) and related proteins, cupin domain; cd02233"
                     /db_xref="CDD:380361"
     Site            order(35..36,67,69,90,92,94..95,114,116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380361"
ORIGIN      
        1 mtlnnevkdg iifplgdenk dyaqyfigks ylaglvnepq ltvgvanvtf epgcrnnwhk
       61 higgyqlllv tggegwyqea gkdpkklmpg dvvvtyegvk hwhgatkdsw fshiaitsgt
      121 aewleavkdd qydtl
//
LOCUS       WP_010723126             170 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecium].
ACCESSION   WP_010723126
VERSION     WP_010723126.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..170
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=19489
     Region          3..131
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,63..64,67)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(62,113..114,116..117,120)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(68,73..74,109,112..113,116..117,122)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,96..97,109..110,113..114,117,120,123,127)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,114,117,120,123,127)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(121,127..128)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 makigyarvs sidqnldrql ellsncdkif tdkasgkdtn regfqkmmef iregdivvvt
       61 elkrlgrnnk eltetmnliq lkkatlevln lpaltgitdd nlrrllnnli ielykyqaee
      121 rryiretqqq gialakakgk ykggkpkyre ddkrlqlafk lflagstdwc
//
LOCUS       WP_010723193             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010723193
VERSION     WP_010723193.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..249
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28516
     Region          3..249
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdhklseteq ylwnfiehhi leipnysivk lseqanvsta tivrtmkkkg yegftsfkhh
       61 lkegenkdin fsfldkvdkg irrailkneq evvrtinmle igniedaiqr ikfadrvfvf
      121 drgfsemigq emlvklqltg kncqmhtdpe iiksisrklt kkdsvifvsl ngetkelvta
      181 akncydaeis silvtanhss tlkdyceinl vsfksegsyf pdyevrsrlp lqiiarilld
      241 ayalrmgen
//
LOCUS       WP_010723285             108 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Enterococcus faecium].
ACCESSION   WP_010723285
VERSION     WP_010723285.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..108
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12048
     Region          21..89
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mtmnkrrlkq aklngnfqgw ltkkkimkik gntccwcgce ctndfiiigg qkqplphtat
       61 vehlipiakg gqhninnvai acfecnqkks dtdlnewitf knskkvta
//
LOCUS       WP_010723419             167 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dTDP-4-dehydrorhamnose 3,5-epimerase family protein
            [Enterococcus].
ACCESSION   WP_010723419
VERSION     WP_010723419.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..167
                     /product="dTDP-4-dehydrorhamnose 3,5-epimerase family
                     protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /calculated_mol_wt=18886
     Region          2..161
                     /region_name="RfbC"
                     /note="dTDP-4-dehydrorhamnose 3,5-epimerase or related
                     enzyme [Cell wall/membrane/envelope biogenesis]; COG1898"
                     /db_xref="CDD:441502"
ORIGIN      
        1 mvkvfdiikf sdfrgytava ldnetlfsig iefhikqinq gfshnkytmr glhyqsgeha
       61 qgkivmclhg eimnialdir qgsstygcvy vntlsesngk cayiprgyah gyltmedntl
      121 vqwcvdndfn snaakcisye svdiewpvsr qcfvisekdk nverlsf
//
LOCUS       WP_010723447             540 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus faecium].
ACCESSION   WP_010723447
VERSION     WP_010723447.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..540
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60772
     Region          4..527
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mitvndvslh fsdrklfddv nikftpgncy gligangagk stflkvlsgd lqpstgsvtm
       61 gpdermavlk qnhydyedyt vletvimghk rlyevmkekd eiymkedftd edgiraaele
      121 gefaelngwe aepeaavllq glnipeelhh qqmseltggq kvkvllaqtl fgkpdvllld
      181 eptngldiqs inwleeflin fentvivvsh drhflnkvct hmadldfgki klyvgnydfw
      241 lessqlaakl qananakkee qikelqefia rfsanasksk qatsrkkmle kitlddiqps
      301 srrypfvgfk pereigndll qvenvsvtid gkkilddisf nlnkedkvaf vaenditttt
      361 lfkvimgeit pdtgtvrwgv ttsnsylpkd ttkefdtdlt ildwlrqyas keeddntflr
      421 sflgrmlfsg eevlkpvnvl sggekvrcml skmmlskanv lvlddptnhl dlesitalnd
      481 glmaftgsil fashdhqfiq tlanriiavs dkgvidradt tydeflenad iqkqlndlwa
//
LOCUS       WP_010723450             362 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecium].
ACCESSION   WP_010723450
VERSION     WP_010723450.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..362
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40407
     Region          6..327
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 menqtilsve nisvsfhvrh relkairnvs lelkeketla ivgesgsgks vltktftgml
       61 eqngnitsgt irykdkilse lkkdeewedi rgkeiatifq dpmtslnpik tigsqisevi
      121 ikhqkksake akrlavelme ktgihnaakr ydeypfqysg gmrqriviai alacrpkili
      181 cdepttaldv tiqaqileli kelqeeyqft tifithdlgv vaaiadkvav myagqiiesg
      241 tveeifydpk hpytwsllss lpqlaqkgdv lysvpgtpps lykdiqgdaf aprsayamkv
      301 dftseppmfq vsethfaktw lldprapkvl kpkqienlhe kmialaaeld seeqdggkqv
      361 vs
//
LOCUS       WP_010723468             192 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010723468
VERSION     WP_010723468.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22958
     Region          1..142
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          74..175
                     /region_name="TetR_C_8"
                     /note="Transcriptional regulator C-terminal region;
                     pfam14278"
                     /db_xref="CDD:464123"
ORIGIN      
        1 msdttrtkql iknvlidlcq tqsfrkisvq kianeakinr qtfyyyftdk ydllrwvyce
       61 dalhyldpqc lsldnweeqa lkmlkaiaek kefyantvls dpeilqkefs qliqksfiki
      121 feqmdeerql sardklfyar ffsygcsgvl vnwitneyee tpmeiamqlf rlakdtelys
      181 yrlyakeele eq
//
LOCUS       WP_010723501             417 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus faecium].
ACCESSION   WP_010723501
VERSION     WP_010723501.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..417
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=44029
     Region          1..417
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdkfvafmek hfipvaskig aqrhlvaird sfmvsmplmi lgalavminn lpipgfqelm
       61 nsifggeswk gfgaaawngt failsvliaf llayhlangy rkdgvsagvi slgsffalgg
      121 algmssnglf iaiivgiist eifvrlsgne kliikmpdgv ppavakafas llpamitisa
      181 falvaaifaa fgvddivgsf ytvvqepfmg lansypsall lafitpflwf fglhganmvd
      241 plmqtinapa ieanvnaiaa ghsapfivnk pffdsfvnlg gtgatlglll aiylvgrknk
      301 pymvvtnlsi apgvfninep tmfglpivln pimfipfilt pmvlvsvayf atstglvpaa
      361 tvmppwvtpp iiggvlatks iagdvlaavn lvlsiliylp fvkvatiqer rkealda
//
LOCUS       WP_010723523             764 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 65 protein [Enterococcus].
ACCESSION   WP_010723523
VERSION     WP_010723523.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..764
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88112
     Region          4..757
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mkqikrlfai dpwkisttql dkknlrlqes ltsigngymg mrgnfeetys gdhhqgtyla
       61 gvwypdktrv gwwkngypey fgkvinalnf iaidisindq lidlaslepe dfyweldmkn
      121 gvlsrtftit tstnkvrisf erflsivkke sayiyltiem legsgtvklv skldgnvqne
      181 dsnydehfwn eiergtieei gylttktipn nfgieqftvt aamrhfvngk svipdyhedt
      241 lalhgclsae lsqgetwsve keiivltsrd ipeaqqaeka vseltnqtnn yiqakeeqta
      301 awaerwklad vviegdeeaq qgirfnlfql fstyygeder lnigpkgftg ekyggatywd
      361 teayavplyl alakpevtkn llkyrhnqlp qaihnaqqqg lkgalypmvt ftgvechnew
      421 eitfeeihrn gaiayaiyny tnytgdteyl kneglevlae iarfwadrvh fskrankymi
      481 hgvtgpneye nninnnwytn tiaawvlryt renyltyqke aaitiseeel akwkdiaenm
      541 yfpvdeelgi fvqhdtfldk dlmpvsdipt sdlplnqhws wdkilrscfi kqadvlqgiy
      601 ffndtftkee kqknfdfyep mtvhesslsp sihsilaael gmeskavemy qrtarldldn
      661 ynndtedglh itsmtgswls ivqgfaqmkt ahdqlrfapf lpktwkaysf hinyrgrllf
      721 isvtdeqvtf ellegsplei yvyeqsysla drleitlrke eanv
//
LOCUS       WP_010723539             227 aa            linear   BCT 01-JAN-2025
DEFINITION  YoaK family protein [Enterococcus faecium].
ACCESSION   WP_010723539
VERSION     WP_010723539.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10536473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..227
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25982
     Region          12..210
                     /region_name="DUF1275"
                     /note="Protein of unknown function (DUF1275); pfam06912"
                     /db_xref="CDD:462038"
ORIGIN      
        1 mqtsfhegrt igllltfigg amdsytyiqy gafasaqtgn iilsiiqafd gewlsvgkkv
       61 lstlffflgi lltkylidyf rkkekhfwrl fvlyyeaaif ffvsltpvhe hpalvtilia
      121 ftasiqwvaf dkingraytn lfttgnlkgv atnlydycis kekadfdrff hylsvvlafi
      181 agaivlvfch hlfdahsili vsilflimal tqtfhlwqfy htnrfti
//
LOCUS       WP_010723569             443 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus faecium].
ACCESSION   WP_010723569
VERSION     WP_010723569.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..443
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=48021
     Region          8..432
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mgkssrkdiv fekfgivatk lgnqihlrtl rdafatfmpf mmlagfvtli nsvileptgf
       61 mgeivdtstl ttlqqigtsi angtlsittl lvvaavsyhm casrnytnhi aavlvaistf
      121 vvltpmqmmf tpenadkave vtgvipvsyt gasgmfvgif vglaatelfi klsnnkklqi
      181 qlsgnippav lksfnvlipi iititsfall sfiiiqlfnm dinklittiv teplskittg
      241 lpgfllitsi anlffgfgih qavisgslld pfliqnmqen maayankeqi phiinmafkd
      301 tfavmggsgn tialliaifi fsrrkdykdf aklsvtpaif nisepiifgl pivfnislii
      361 pfvlapifsl tvayfatavg linhvvvqip wttppvisgf latagdwraa vlqiliiaas
      421 vfiylpflri dehvttklse net
//
LOCUS       WP_010723576             400 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus faecium].
ACCESSION   WP_010723576
VERSION     WP_010723576.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..400
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42540
     Region          26..382
                     /region_name="MFS_YfmO_like"
                     /note="Bacillus subtilis multidrug efflux protein YfmO and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17474"
                     /db_xref="CDD:341027"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,151,
                     154..155,158,226,229..230,233..235,238,263,267,318..319,
                     323,327,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341027"
ORIGIN      
        1 meilenqidi qeqtnegtkg kssalvvaat cmiafmglgl vdpilktiaa qlnatpaett
       61 llftsymlvt gvvmlftgfl ssriglkktl mtglfiivvf aglgglsgni gmliglragw
      121 gvgnalfvst alativsilv gntekaimmy eaalgcgmav gplvggvlgs gswrypflgv
      181 aflmfcgfia lavllpetek pkrkvglweg vkalsnhklr svgliallyn fgfftllaya
      241 pflligysel evgfvffgwg vllaiasifv apalerkftt yrtilaafvl fiicllllga
      301 gtsmpvlvpi sivlagffqg iintllttia meipglqrnv asssysfirf fggalapfia
      361 gvigehiges yafyfagaiv lisvcciiyh rnyfatneee
//
LOCUS       WP_010723603             717 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Enterococcus faecium].
ACCESSION   WP_010723603
VERSION     WP_010723603.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..717
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=82525
     Region          6..715
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mnigqidtrh atanqpnfsn gncqpytgvp fgmnyfapqt tdqngswwfh pddrvfqgyr
       61 lthqpspwmg dfshmlftpi ngklqentlf haqssyrpee sifcpthlsi cqlrygicst
      121 lipsmyggil sidyskndsg lllsfpgrhq lfvidpytve gkithfagse dpdfsfyfil
      181 rfeypltide lavsnknsds iplyfeqtkk qtirfgtsfi sseqaaynle leqnqskety
      241 lahsqeqwqs yfdriqlthh dqqqlrtfyh nlyrvflfpq tfyeidpsgq kihydttsrs
      301 ikpgvlytnn gfwdtyktvy plysliavek yeemlegfln syresgylpk wlspderglm
      361 pgtlidavia daavkdirrd lmpefltame kgatvqskhp nygrqgtedy ltygyvpnhy
      421 hesvnhtldy aysdfcisqv akvleeeema kkyqqqslny qnifdyesgf mrskdkdgkf
      481 repfsanrwg qdyaegsawq ssfavyhdfs gligkyggse rykeklielc nqpptfdpgg
      541 ygfeihemse maaiefgqla isnqpsfhyp ylfsyigqpe maqpllkqlm tqtfddspmg
      601 ypgdedngsm sawyifnslg fypvtpgtge yvigmplidk avlllsngke ltieatpnrp
      661 qqqfihkikr mdkeytklyf thqdllkggt isyqlgivph pkkyqakdlp fslsnyn
//
LOCUS       WP_010723643             310 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecium].
ACCESSION   WP_010723643
VERSION     WP_010723643.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..310
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34361
     Region          3..224
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 miieidklvk rygdfvalnh fdlqvqegev lgllgpngsg kstaincmls llnydkgtik
       61 lfgttmtpen yavkamigvv pqdvavfdel svqenidyfc glyvsekekr kalieeviel
      121 vglekyvsfr pgelsgglkr rlniacgiah kprlifldep tvavdpqsrn kilesikeln
      181 rqgativytt hymeeveilc dqivimdqgq viakgtkesl kdmvrtadrl tidipllpen
      241 vlsaiqrtia sdgiaykkgq lqvtttelnt vllpiltilq eekisygkia tkeaslndvf
      301 leitgkelrd
//
LOCUS       WP_010723766             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Enterococcus].
ACCESSION   WP_010723766
VERSION     WP_010723766.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 202)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..202
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23133
     Region          2..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(7,9,65..66,69)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            9
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(64,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(70,75..76,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93..95,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          <165..197
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
ORIGIN      
        1 mlvgyarvss ddqnlerqle efrkigvekv faekksgrnt verpefnkml afvregdtlv
       61 feslerlgrn sdeildtvsf idkngmglmv lnlpildtkf gdpnleklvr slvisifswt
      121 aqnereeikr kqkqgiaiak kkgiykgkpy eysstaknpq krfiyseivr mlgegvpvkq
      181 iaektgtnrt lvyriknril ke
//
LOCUS       WP_010723816             680 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_010723816
VERSION     WP_010723816.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 680)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 680)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 680)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..680
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78073
     Region          <30..181
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mlyklavksf frqsrgylvy ffsltlsvmi yysfsamtyd qslvrrasqd tsidgglsfg
       61 gfiitvvllf fvfsanrffl nrrqkeigiy qlfgmnklqi sgiyvleimi iglfacisgi
      121 llgiifsklf smilvrmmdm dltspffisi psvvdtlfaf fiillavsvy siwkiwrypm
      181 irsfgekeqa dsstmrfrtr hrllavigll llmsgyfgas hfreitswmi syhyldtlvf
      241 ffsfliffvc vvgtylffcy tfrlfliils kwkiyyygin flimgntqvh llkswrtnsl
      301 itvilgisli tiggtasist ilsyqekvss pmdyqfdvet ekkikpilae egqkitkeit
      361 lhykvigsiy sqnleepmfq tanlitetqy qafrkvnpdl pnislkspgh tvlldqmqtl
      421 frnislygss iglpdnqelk iqqmlpsvlg detmvylspv livddtvfek akgvdyqvvn
      481 vdvsggnnek iderlsndls ikwlnavyys ydivngslqg eistkklpdd qmkeeqfsqe
      541 ssrlnfsssy sklravnrri ginifvtlfv gmiviiatgs iltvrqlaea eeekenyhll
      601 tklgipqrri rrmifeqnal tffppmilgi thavfainvf tqyiktadyw laylvsglli
      661 liylllyvit sqlycriiee
//
LOCUS       WP_010723854             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010723854
VERSION     WP_010723854.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..282
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31194
     Region          1..277
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 msvisriesm medyssaekk lanyiignie kvptmtanel aeasglsapt vvrfskkigf
       61 qsltdfkiti stelqtgide gfsdieanes fysiknklgn naqvaiketv dileeetiqk
      121 vveclesaet vflygvgass lvvedilqkw srvgkpiife kdihvllpql vsnekkkvlw
      181 lvsnsgrsad vaalaelaks mnieiialtq fgnnplskia dvlvqtsrpk eitnrsaatn
      241 sllaqfatid iifyfymakn eklsekvkkt reaiqeyfmd sk
//
LOCUS       WP_010723861             256 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            faecium].
ACCESSION   WP_010723861
VERSION     WP_010723861.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..256
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28881
     Region          7..254
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mknslvniek rqkeilellq qteqlstfel aesldvsist irrdlnllee kneiirnygy
       61 csynyknqtd fdqsgperik qaiareasky indydtlfin sssttlktld flqsnhltvi
      121 tnnvkinysp hkdncsyilt ggemrfpkea lvgdialnti ssvnadicii gcsgvdvvhg
      181 vttkilnest inemmvnkti kckilvadhr kigltskfki adisvfdyli tdkfcsekvl
      241 eeirntgikt iqvdsf
//
LOCUS       WP_010723887             640 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus faecium].
ACCESSION   WP_010723887
VERSION     WP_010723887.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..640
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74950
     Region          8..637
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnqrqqsliy qlsennnyit tkklaehfhv sertihsdln tietwlgdkh lplmferkkg
       61 tgillnglph ereqlkraln eetqtemdkk qlrqllifhl lvakdgfsle elseklyvgk
      121 rtirkeltel qsffeyhhlq lvsktklgtf lkgdeqekrq llvktlrnmq kedpqspslk
      181 effakdtlkv iqhtlqdvfy enhleqpngl asveihiyfm lermkqyqkv klskdenevv
      241 ehtqaqklss qilaklatiy piefspdein ylalrianlf tnsqaatrfq kessaladhl
      301 ieqveqflgy slkedqllkq nlrshlssty frlhyglqis npltknvfst ytqlflvlql
      361 iledyfeken fyvpqeetay ltihfqaaie rhkhqksrry qtvlvseysk amatflearl
      421 nrelpeltim dlveykpelk rqdfpsvdfi latlpfkhis ipvieispmi tetdlayltk
      481 ymlehvpikk kktfdlasft hpflifpqle rtdpadilnf mgnvlvehhy vepefidsvl
      541 erdshsstrv apfvtiphgn plyvkhsmis iatmkepvlw hgeqirivll laikkndlkh
      601 aefkkifsvi hylekqpeqm aqlmqsnhpl eiltllssye
//
LOCUS       WP_010723892             201 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus faecium].
ACCESSION   WP_010723892
VERSION     WP_010723892.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..201
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22641
     Region          14..194
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtyifekgts gkhlillhgt ggdehslldi ahilapnstl lsfrgtvqed gmnrffkrng
       61 lnqfdldsle ketdklheki keisekelip lsdwllvgys nganiaahll leretelnkg
      121 lffhpmslgv hqsrstledk tvwlsygdnd pivspasfke ladqfetrqa nvtiqltvtg
      181 hqltmdeieq arewtdhllt k
//
LOCUS       WP_010723926             318 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus faecium].
ACCESSION   WP_010723926
VERSION     WP_010723926.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..318
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35601
     Region          1..246
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkkyqwgivg lgtiahefae sfnqetselt avasrtseka enfarrynip kaygsyqeml
       61 ddaeidivyi avpnrqhidh ilaaleagkh vlcekaitmn kkeladamrl aeeknlilae
      121 amtifnmply qqlrsimdtg klgalkmiqa pfgsykepdp knrffnpela ggalldigty
      181 avsfarffls sqpevvastm vpfetgideq svtilrnken elaavsltfq akmpkvgiva
      241 fengyvtiad ypradraeil ftdgtkefie sgntseamny eiknmvhmie gdlpnrslfl
      301 tkdvieildq mqvlwknm
//
LOCUS       WP_010724028            1175 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Enterococcus faecium].
ACCESSION   WP_010724028
VERSION     WP_010724028.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1175)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1175)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1175)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..1175
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=136771
     Region          4..1158
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mslqfilgng kkdhrqvlid easawldqda snqvfflvpn yskfeqeqei laemrrrsgk
       61 kafsttnvqv fsfyrlawyl lqqttlltgn elsesgsami lrqileknee eltifrgein
      121 krgfirqlqe lyselrtgni qpgdlmllfg dspnaedqql kmkdlklifs aydseltqra
      181 ltnedalsil anymqtqdfn nvkfivsgfs ringqeyqll qammekgqlv vdllldrpyt
      241 adlpevltlf hetgklyfrl fqsarerkvp ilvdrfapeq trptelqllq tmweetssqk
      301 kaavhklggq ehlhlweaen pteevrqlav eirrlvseen yryrdiqvlt knmslygnil
      361 qpifqemaip fyideeqmme nhpliewins lfaldrysyr lsdimrffkt elflsteaet
      421 eldewkqerd efrkkldite nvalaynyqg tywtrekdwq fvaydfeaeq iedvqyleeq
      481 sntirrlfqk avpvflkkik ksktgqeaan gfyqfliqsg vqqqllfwrn qevdrgnlea
      541 arnheqtwga lidlldeyvv iygesafdws lfqeiitsgl enlsygkipt aidqvrinrl
      601 elvrpnqaav tfalglndqv fpdrketkgl lsseerevln qalpdgqflf dpskesisfe
      661 pfqaylvfls gtdrlylsya qsydtdgslk mspylrrite ylsvpverke hltiesnpnc
      721 yvgtyrsgin tvnriyrlal dekkpvpkhw qklkelvlns swrnfalqif esqehlnvpv
      781 smpekmaeel ygkeiytsis rmenfyncey kyfmqfglkl kertvygltp aatgdfyhes
      841 ldrffkllfs nqlslvnmsd tqrrdftekv lqevfgelrf eildssarmn yiryqlgqti
      901 qkvawalqkq skntgmhplq teilfgqiag akgitglelp lsnggklhvr gkidridvas
      961 eqedtwlsvv dykssgrsfd vteayygmam qlltyldval mdavrltgka tvkpagsyyl
     1021 hvhnpvltet ddvekntlkk fsydgvfvdd pallevldhs leakeqsliy pvkknakdey
     1081 qkgsfskdkf fteeelqlfm ahnrenmrla gdaitsgeik lnpaykdkqr iacefcpfrs
     1141 ictfdvmlke nnyhrlekid keealrrilk rseee
//
LOCUS       WP_010724043             449 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus faecium].
ACCESSION   WP_010724043
VERSION     WP_010724043.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..449
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48123
     Region          15..449
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 meeyqatpvk evkienelkr tmgfftalst vmgtvigagv ffkaasvaev tgsaslhmfs
       61 wflggmisvc agltgaelaa aipetggmik yieriygnta afllgwaqvv iyfpanvaal
      121 siifgtqfvn lfglsqsmiv pvavtaavsi llinflgska ggafqsitlv ckliplfviv
      181 ifglfrqegv dfqlfpiqag enlsffsalg agllatmfay dgwihvgnis gelkkpakdl
      241 pkaislgiig imivyllvna vflrtasidg vagnsnaasd vakmifggfg grlvtvgili
      301 pvygtingyt ltgmrlpyvm akennlpfsk lfaklhdktk vpvaagilel viaigmimig
      361 gfdtltdmli fviwifytmv fvgvillrkk epdlfrpykv pmypfiplva iiggtfivss
      421 mlitqtflas mgivltlagi piylylkrr
//
LOCUS       WP_010724074             311 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Enterococcus
            faecium].
ACCESSION   WP_010724074
VERSION     WP_010724074.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..311
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33916
     Region          8..305
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 menfkksgmf sviaalgani lvaiskfvgy aisgsaamln esihsivdcs nqilllfgdk
       61 qankgqselh qfgegrakyf fstivammlf fgggalgvme afeklthpsh evgnpiivia
      121 illfglvieg sslrvamkei kelnteilst mrflresrhs eiliiftedl caviglvlal
      181 agtiltyatg iaafdaisgl ligfllmgaa iflakefysl iigesvtasd lskiklafer
      241 peisrlidik tvhlspteil vaakadivgn keneaysvin dieknmrqsl pdkkmyiyie
      301 tdkydpnysr k
//
LOCUS       WP_010724079             182 aa            linear   BCT 01-JAN-2025
DEFINITION  guanylate kinase [Enterococcus faecium].
ACCESSION   WP_010724079
VERSION     WP_010724079.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..182
                     /product="guanylate kinase"
                     /EC_number="2.7.4.8"
                     /GO_function="GO:0004385 - guanylate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006163 - purine nucleotide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20526
     Region          5..178
                     /region_name="Gmk"
                     /note="Guanylate kinase [Nucleotide transport and
                     metabolism]; COG0194"
                     /db_xref="CDD:439964"
ORIGIN      
        1 mnycyvfigp sgsgktslae aifqpeqkii tytnrsprpg ekdqedyyfv sdntfnqmik
       61 gnefaewdqy aqhkygsska eikkkltvgn cyavltangf whlyeyfgtv vrpifitisk
      121 etlqsrlkkr gdsseqisar lavyvedlaq lkrlktipsl lvvsndgafq eaadkikkgl
      181 li
//
LOCUS       WP_010724103             196 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010724103
VERSION     WP_010724103.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23072
     Region          30..>108
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mptkpvlseq ekyqlkqdle hlcerywinn gykktsiral cqeakisigt fytlyptkem
       61 lffnvlnkiq krlsecflef ieenkskagf aralqamlve yldkpflydt tsedfrlfks
      121 kltpkmihql efdnfhlfrr givlaglrlk keenfafsvy ntlfssikak etisssynyl
      181 pvlnfmitem tnilfd
//
LOCUS       WP_010724265             596 aa            linear   BCT 01-JAN-2025
DEFINITION  terminase large subunit [Enterococcus faecium].
ACCESSION   WP_010724265
VERSION     WP_010724265.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..596
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69499
     Region          38..567
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mdlmklsyse lekwwfdyke eqaswggill epypellttw yaerlidgsi paskenilaa
       61 krhlldlkrq gteefpwifd eevghrpirf iedncrpteg dfdrfilqpw qhfiigsmfg
      121 wihkdtgirr frealtfvgr kngktslisg lsaymlgydh eqganvyvla nakdqasilf
      181 dktkemvkqs prldkkykpq rslikdeatf skmearasds kkldglnthf aifdeihefi
      241 nfklinvikk srgtrrqpli vyittagyvl dgplmqyydn aldclehled gldervfyfv
      301 aklddvsead dprnwikanp niglmsfvdl vtdwkterns pqeradwitk qfnlfsdide
      361 lsfldmqtin knnkiidwet megeecvggy dlsetqdfts anlefpiyet geiavlehsw
      421 isqerynndn nkqrldawik sgdltvtpgs yvdyqfvfdw fveqskkyki lkirydrrns
      481 lilnrqmidy gfvmeeaiqg fttlggpmkd lkerfldgkv iynrqkifrw ylsnvklvqd
      541 rnnnwmptkq sknrkidgfa avlnshvsvv emfatkskqs gtigfisvre mmrggk
//
LOCUS       WP_010724341             311 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus faecium].
ACCESSION   WP_010724341
VERSION     WP_010724341.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..311
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=36403
     Region          1..306
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdyerlvkey llelklenys krtiesyeqh hrkfidyyrk eisspiliee vskihyklfi
       61 sflldcqlks syinailkth kafwnylvae kvvrvsplet irllketkpl lttfndkevk
      121 dmlnvwkfdt ylgarnkcii alladtgirv sellnlkdtd laenyirilg kgskwrvvpi
      181 sselnyfitr yrrirdshfy tlrnyhgktr kldeqlflgk tgrkiktvtn ielilketgk
      241 ragvratvrc sphtlrhywt vknlqmgqdi ftiskmlghs kldttkiyis sitdeqlvdk
      301 avktsplgsi l
//
LOCUS       WP_010724367             356 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010724367
VERSION     WP_010724367.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..356
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38623
     Region          126..355
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflalneimh sklryalvag vmfliaylvf fltglaygla qdnrtavdkw eadsivlskd
       61 ansnlgmsmi tkkiaeeveg gkvaylaqtp gvvtskdste egkinvsffg idknqfimpn
      121 lvegkafdnd deavgdislk eeyglavgdt vklsgsdktf kltgftdhak fnvspvlytt
      181 inayqeirfe kedisenari naivvrgkis nlpedleqik iskfinelpg ynaqvltfgf
      241 migfliviaa ivigifiyvl tmqkinifgv mkaqgitggf iarsvvaqtf ilsfvgillg
      301 llgtvgtslv lpdavpfqsn wlffgvisll mlvvavlgal fsvrtivkid plkaig
//
LOCUS       WP_010724366             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010724366
VERSION     WP_010724366.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..222
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24713
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mkaiefkeve ksfldgdqvv kalkettmsi dkgkfvaiig psgsgkstfl tlagglqtps
       61 sgsvfingqe fsnqkeserv klrfkeigfi lqasnlvpfl tvkkqlllvd kikhehrqke
      121 anelfeqlgv dklinkypee lsggerqrva iaralyndps iiladeptas ldsekarevv
      181 dilakeskdk nkatimvthd trlidkcdri fmmedgvlke ke
//
LOCUS       WP_010724427             635 aa            linear   BCT 01-JAN-2025
DEFINITION  M13 family metallopeptidase [Enterococcus faecium].
ACCESSION   WP_010724427
VERSION     WP_010724427.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..635
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71995
     Region          8..635
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mnkerlkqdf yeavneewqk takipadkpa tggfqdlvdg idqllmgetd dllahpekvs
       61 sekmkhflay yqlandydrr nelhaqplqp iiekveslqs fdelnkqfpe wlldtlplpf
      121 nldvdadmkn aqtnaffayp pslflpdkty yasdhpngaq ligvffdmav qllelagkek
      181 sqaeaiteqa vqfdkliaph vksaeenady skmynpqsfd tfiqytdkld lkklvtglig
      241 ttpdkvivtd pvyfdhlndi lteahfplfk swmiiktvrs lsgylseefr qvsgiysrvl
      301 sgtdeampqk kaayylasgq fdqvvgdyyg kkyfgetakk dveqmvkkmi avykkrleen
      361 dwlgdatkek aviklnnlgi qvgypdkipa lfdqfktvpa dqggtllsnt lvfskltlkd
      421 rfskwnkpvd rsewemsadt vnayyhpfrn vivfpgailq apfysleqss sanyggigav
      481 iaheishafd nngalfdeyg nlnnwwteed ltqfqnkaqa mieefdglpf adgkvngklt
      541 vseniadagg lscaleaakt esdlsieeff vnwatiwrtk akkeyqqlll qidvhapakl
      601 ranvqpknld efyetfgite qdamylapek rvriw
//
LOCUS       WP_010724447             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Enterococcus
            faecium].
ACCESSION   WP_010724447
VERSION     WP_010724447.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10478446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..298
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=32311
     Region          255..297
                     /region_name="LysM"
                     /note="LysM domain; pfam01476"
                     /db_xref="CDD:396179"
ORIGIN      
        1 mydenewgen vrmtrrrqqk qaarkrmimi gaavavflii aggvaslyfh gknsseakst
       61 titetttkkt etkqtsesst ktketqtsee ktanglpeql qaivndyskk ieektpalie
      121 eyqteiqgnq egiaglsava nqkarelqai sdegirklra ayqaaenkdg vdldtlinql
      181 sanytnhvak isdiylqtsa slqaeststq dttssdseta esveasemqa rttqdttdss
      241 etntnsatsq aattvvlege gpnqiaertg vpvetilsln gmsmenyflt pgetlkln
//
LOCUS       WP_010724553             285 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Enterococcus faecium].
ACCESSION   WP_010724553
VERSION     WP_010724553.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..285
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=33440
     Region          69..163
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mvktsirvak hiekwvksvn hqksltdyna akylvsfled rglymevpfr nklilghsli
       61 delgastmin kniptlerki ftqahelghh ildpdllrnn seidiltedp vvlnkeaemr
      121 anafaahlll pddvldasmv ehktrreika tqqisyetlg yrlstymnsi fkipkdltef
      181 ivnefmesdi nseinknfyd fwknaytrkp iysteslsti nqeiaikycd ypthmyrklk
      241 kiqiqenenf yktreerlly salaenyeii ddfvysyenn kdlpf
//
LOCUS       WP_010724654            1112 aa            linear   BCT 01-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Enterococcus faecium].
ACCESSION   WP_010724654
VERSION     WP_010724654.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Burnim,A.A., Dufault-Thompson,K. and Jiang,X.
  TITLE     The three-sided right-handed beta-helix is a versatile fold for
            glycan interactions
  JOURNAL   Glycobiology 34 (7) (2024)
   PUBMED   38767844
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12131601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..1112
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=122420
     Region          491..>662
                     /region_name="NosD"
                     /note="Nitrous oxide reductase accessory protein NosD,
                     contains tandem CASH domains [Inorganic ion transport and
                     metabolism]; COG3420"
                     /db_xref="CDD:442646"
     Region          600..766
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
     Region          <1018..1111
                     /region_name="pullulan_Gpos"
                     /note="pullulanase, extracellular, Gram-positive;
                     TIGR02102"
                     /db_xref="CDD:273973"
ORIGIN      
        1 mlkkrikysa lmmnllmlst pvlisvveva aneqqsvnee nahvniegms tmeevprtse
       61 dmdteegndp mmkesenekt kkqseeanee wkgvvfgest sasryaiepl edgvrlsstn
      121 nggkfqssgs dgmtyyyqai pkdinfrmra tieieswtyt naqegfalmv rdavpkdhlf
      181 gqafysnsfa ilgsrieyvw dsdrqevvnt sgskytmrlg lgtraitgis sedpqaapap
      241 gsvsvettpl etsagfleke tgsynifgng hgnlfpatns itkldvemkk tntgleayyy
      301 dpetgeemas dimydwekly asdesviyag faaarnmtik vegievaysd patdppgqer
      361 ptrlidpiyt vtssnhsgnq dhtmsfrana dglltiknqa tgevlenakd lvitanrefd
      421 yqtklmegtn eftfsftpdk nyppeeyvem asyetkeilh tvdyrkpnys tvyvtpegsd
      481 tgngsrqnql sltqalryay agqtivlapg tysferglti pkgvngtren piqliaeknp
      541 enkrpvldfk gtgngmtlfs hywvlrgfdv tnsaamqkgl qisgnhnlie eihayrngnt
      601 giqisgssnd pfeawpahnl vknctsfena dpgfedadgf aakltigegn vfdgciayhn
      661 addgwdlfak netgsigkvv iknsvayrng wvpgvegegn gngfkmggss lsgphelins
      721 lsfenlakgi dsnsgtdiiv nsstsfnngs ynvalytssa gntdfhasgi lsfrtenlem
      781 reqirplnqn edqiyhslny ywnerekqse ntlghtvskd wieslnthsq egqqpvtrya
      841 ngsihvhglm qikpenrqte kgrvdglpls vgatfdrets psseypeyai vqepnqtkpn
      901 eqnnpiiiqe angvaenaeg niielkpftv fvstftpnqg tpvfedmryf pekiqivetq
      961 ssaqfsnhta ifsapskgey tlevtyrsei fdgekwsaht esvtqqkait vretadvppg
     1021 ndkperenpg nespngkpng kpngkpngkp ngkpngkpng kpshpdrtak esekngtqgl
     1081 pktgefnnpl lalaggilli gvvvyvmkqr kk
//
LOCUS       WP_010724668             301 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_010724668
VERSION     WP_010724668.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..301
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31551
     Region          14..298
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mtnllslfls sasqgvlwal laigvyvtfr ileiadltae gsfplgagia avsitngyhp
       61 ltacllgflg gaaaglvsgl lhtklkipal lagiitmtgl ysvtsrvmga pnisllgqpt
      121 ifhwvesfgi tkdnavlivg llfalivvcl lvlflrtetg lairatgdnl amseangint
      181 dnmkiigymi sngcialsgs llaqnngfad lnsgigtivi glasiiiaev llrnqplflr
      241 lltvvlgavi yrfilalvfe lnvepsdskl asafvlvicl sfpqiqqkfh lpqkkkggsv
      301 k
//
LOCUS       WP_010724677             441 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus faecium].
ACCESSION   WP_010724677
VERSION     WP_010724677.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..441
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=50169
     Region          13..369
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(16..17,20..21,57,60,118..119,179)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(116,119,208..214,243,270..275,302,327..331,333)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mmdyskepvn dyflidmksf yasveciern ldplttelvv msradntgsg lilasspaak
       61 kkygisnvsr prdlpqpfpk tlhvvsprmn lyikrnmqvn nifrkyvade dlliysides
      121 ilkvtrslnl fttegtrsqr rkklaqmiqe nikeelglia tvgvgdnpll aklaldneak
      181 hnegfvaewt yenvpekvwn ipemtdfwgi gsrmkkrlnq mgimsirdla nwnpytiknr
      241 lgviglqlyf hangidrtdi aippettkek sygnsqvlpr dytrrneiel vvkemaeqva
      301 irirqhnckt gcvhlnigts iletrpgfsh qmkipitdnt kelqnyclfl fdkyyegqev
      361 rhvgityskl fytdslqldl fsdpqkqide enldkiidki rqkygftsiv hassmlegar
      421 sitrstlvgg haggnggikn d
//
LOCUS       WP_010724730             454 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Enterococcus faecium].
ACCESSION   WP_010724730
VERSION     WP_010724730.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..454
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51048
     Region          1..422
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mkiviigash agitaalnlr klqpkaevll idedhkdglg yvsnginlyl kgkirslaev
       61 ahnmrtlqes gvklitewrv teldpdkhql ilaskegkne titydkliva tgsspvtlyk
      121 qieaenvyty knlvqskqvl aalkeakevv ifgagyigle ladalrnkgy iihlvdympn
      181 vlsryfdkdm insfqnqlqt kqinfypnef lidwkkseek vvsvqllsqt ikadmvifsa
      241 qtrpnttllk ekvalyedet vivneylqts dpdiyaigdi vpvsfdknkr hlflplvtra
      301 vhmaravalt lsgqptaydl rqkitaavii dyflgtvglt edeapfleqn tgscsgefdl
      361 fpqydeenkt vnakliyhpd tleiiggqli sqefllsdln lladivkhkt tipqlavedf
      421 gflseytsrf hylnelafkv lakransnrv dkrl
//
LOCUS       WP_010724775            1175 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Enterococcus faecium].
ACCESSION   WP_010724775
VERSION     WP_010724775.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1175)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1175)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1175)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..1175
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=136871
     Region          4..1158
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mslqfilgng kkdhrqvlid easawldqda snqvfflvpn yskfeqeqei laemrrrsgk
       61 kafsttnvqv fsfyrlawyl lqqttlltgn elsesgsami lrqileknee eltifrgein
      121 krgftrqlqe lyselrtgni qpedlmllfg dspnaedqql kmkdlklifs aydseltqra
      181 ltnedalsil anymqtqdfn nvkfivsgfs ringqeyqll qammekgqlv vdllldrpyt
      241 adlpevltlf hetgklyfrl fqsarerkvp ilvdrfapeq trptelqllq tmweetssqk
      301 kaavhklggq ehlhlweaen pteevrqlav eirrlvseen yryrdiqvlt knmslygnil
      361 rpifqemaip fyideeqmme nhpliewins lfaldrysyw lsdimrffkt elflsteaet
      421 eldewkqerd efrkkldite nvalaynyqg tywtrekdwq fvaydfeaeq iedvqyleeq
      481 sntirrlfqk avpvflkkik ksktgqeaan vfyqfliqsg vqqqllfwrn qevdrgnlea
      541 arnheqtwga lidlldeyvv iygesafdws lfqeiitsgl enlsygkipt aidqvrinrl
      601 elvrpnqaav tfalglndqv fpdrketkgl lsseerevln qalpdgqflf dpskesisfe
      661 pfqaylvfls gtdrlylsya qsydtdgslk mspylrrite ylsvpverke hltiesdpnc
      721 yvgtyrsgin tvnriyrlal dekkpvpkhw qklkelvlns swrnfalqif esqehlnvpv
      781 smpekmaeel ygkeiytsis rmenfyncey kyfmqfglkl kertvygltp aatgdfyhes
      841 ldrffkllfs nqlslvnmsd aqrrdftekv lqevfgelrf eildssarmn yiryqlgqti
      901 qkvawalqkq skntgmhplq teilfgqiag akgitglelp lsnggklhvr gkidridvas
      961 eqedtwlsvv dykssgrsfd vteayygmam qlltyldval mdavrltgka avkpagsyyl
     1021 hvhnpvltkt ddvekntlkk fsydgvfvdd pallevldhs leakeqsliy pvkknakdey
     1081 qkgsfskdkf fteeelqlfm ahnrenmrla gdaitsgeik lnpaykdkqr iacefcpfrs
     1141 ictfdvmlke nnyhrlekid keealrrilk rseee
//
LOCUS       WP_010724855             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar transferase [Enterococcus].
ACCESSION   WP_010724855
VERSION     WP_010724855.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..204
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22952
     Region          <1..190
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mykdglkrgi dfllslvgii vlspillilc iaikidskgp vifkqkrvgk nkshfyiykf
       61 rtmkvdtpqe tpthllsnpd ffitrvgkfl rktsldelpq lfnilkgdma vigprpalwn
      121 qydlieerdk yhandirpgl tglaqisgrd eleidykarl dgqytanitp wmdlkcffgt
      181 iisvfksdgv veggtgsvkk edak
//
LOCUS       WP_010725017             824 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus faecium].
ACCESSION   WP_010725017
VERSION     WP_010725017.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..824
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=91268
     Region          32..688
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(323..325,392,410..412,439,491..493,536,539,542,561,
                     564)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(621,625..626,628..629,654,657..658)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
ORIGIN      
        1 mknkwinrsk kkkvtqrssd kvirlfpsyk egltadqvke riekgaanns vdptfktnqq
       61 ivleniftyf nliflilail lclvesyknl tflpviiant giaifqeirs kkildelnvl
      121 ntakvnvird gieqtidied lviddivile tghqipadae vvegklqvne alltgeadei
      181 tkeigdplms gsfivsgkay arldkvgads yisqltvkak tmgegeqsem iaslnqlikw
      241 igiiiipigi llfsqsyffn gntikesvva meaaligmip eglyllttia lalsatklak
      301 qrvllhnmes ietlarvnvl cvdktgtite nkmsvqkviv skkqeiisqs dqleaciady
      361 akamagdnat meavkayftk ttdqsyhhvi pfssvqkfss valadkvyvl gapemvlrdq
      421 lpeyaeefvs faekgyrvlv fgvydgilee pvlteavtpl gyilianpir kearatfdyf
      481 kkqqvaikvi sgdnpltvsn vavqagisha dqyvdaskls eeeyeaavek ytvfgrvkpe
      541 qkkifvqllk rrnntvamtg dgvndilamk eadcsiamas gneaamqasq vvlldsdfsr
      601 mpevvaegrr vvnniersas lflvknifsf llslfsvifa ltyplepsqi tlislftigl
      661 psfllaleen kkrirgkfim nvmekavpgg ltdmivvgal vicgvtlnln ktdvstastm
      721 lliavgflvl ykicsplnkf rsqiilfcas gnffsviflh klfsitgisa vsllllsilf
      781 fsadsifrhl ttlveylfer knekeqkpfs rvvkkflsif kren
//
LOCUS       WP_010725067             867 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Chlamydia
            trachomatis].
ACCESSION   WP_010725067
VERSION     WP_010725067.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia trachomatis
  ORGANISM  Chlamydia trachomatis
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 867)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 867)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 867)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..867
                     /organism="Chlamydia trachomatis"
                     /db_xref="taxon:813"
     Protein         1..867
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=96500
     Region          1..858
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mekfsdavse alekafelak nskhsyvten hllksllqnp gslfclvikd vhgnlgllts
       61 avddalrrep tvvegtavas pspslqqlll nahqearsmg deylsgdhll lafwrstkep
      121 faswrktvkt tsealkelit klrqgsrmds psaeenlkgl ekycknltvl aregkldpvi
      181 grdeeirrti qvlsrrtknn pmligepgvg ktaiaeglal rivqgdvpes lkekhlyvld
      241 mgaliagaky rgefeerlks vlkgveaseg ecilfidevh tlvgagatdg amdaanllkp
      301 alargtlhci gattlneyqk yiekdaaler rfqpifvtep sledavfilr glrekyeifh
      361 gvritegaln aavvlsyryi tdrflpdkai dlideaasli rmqigslplp idekerelsa
      421 livkqeaikr eqapayqeea edmqkaidrv keelaalrlr wdeekglitg lkekknalen
      481 lkfaeeeaer tadynrvael ryslipslee eihlaeealn qrdgrllqee vderliaqvv
      541 anwtgipvqk mlegesekll vleesleerv vgqpfaiaav sdsiraarvg lsdpqrplgv
      601 flflgptgvg ktelakalae llfnkeeami rfdmteymek hsvskligsp pgyvgyeegg
      661 slsealrrrp ysvvlfdeie kadkevfnil lqifddgilt dskkrkvnck nalfimtsni
      721 gsqeladyct kkgtivdkea vlsvvapalk nyfspefinr iddilpfvpl ttedivkivg
      781 iqmnrvalrl lerkisltwd dslvlflseq gydsafgarp lkrliqqkvv tmlskallkg
      841 dikpgmavel tmakdvvvfk iktnpav
//
LOCUS       WP_010725095             503 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Chlamydia trachomatis].
ACCESSION   WP_010725095
VERSION     WP_010725095.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia trachomatis
  ORGANISM  Chlamydia trachomatis
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 503)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Chlamydia trachomatis"
                     /db_xref="taxon:813"
     Protein         1..503
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56227
     Region          242..503
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mklelllafk ylipkrkrls ssivsafsmg ivalvvwlsv vfmsvihglq qrwvgdlasl
       61 hssiriepsd kyyesyyyqi dshaeasqyi yktigekllc eqtdpydpdv dfllpeafpd
      121 pefsdngemi dpvrtanerm lslfssrkgs fvefeegmgh vhmdrafrgh kgepralsqy
      181 iayssdilyq qrmlpfeetd ystevlnrfn assegwladf lvlqekfrgm svilpvvyrd
      241 qgyrvgdtas lsvfsvkkeg evrfplrvig fynpgvspfg gktifidkel aasirseseg
      301 lgmhngwqvf lpsvqdipvm kqsiqkifke sevssyweis slydyeffkp ildqlqsdqv
      361 lfsivsfivl ivacsnivtm sillvnnkkk eigilkamgv sssrlqlvfg lcgacsglvg
      421 allgsilaal tlknlgilth wlsklqgrea fnpsffgeql pqdfhlptvi clslgalvla
      481 aisgaipaqh varmqvsdil kse
//
LOCUS       WP_010725131             415 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Chlamydia trachomatis].
ACCESSION   WP_010725131
VERSION     WP_010725131.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia trachomatis
  ORGANISM  Chlamydia trachomatis
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Chlamydia trachomatis"
                     /db_xref="taxon:813"
     Protein         1..415
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44956
     Region          59..399
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mrsplkllfs peksnmmlgl sillglllgw phlsfvslsa evisavflkl lrllslplvf
       61 faigstitsi nnlksmvsvv rsslyytllt tlisaamalv lfifikpsvp lsgfnaatet
      121 natgylsvls ktipgnilep flesnviaaa flsallatfs lslpenerlf vrnafntlfs
      181 lllsiskgil kmlllatfaf sllfvremrt gnlelssfge ylfcivtanc lqgflvlpll
      241 lkmkgisplr tfklmsrpla taffskssaa tlpltmevae enlhirptis rfvfplcsvi
      301 nmnacaafil ttvlfvgvsn givfsplsli swvfiatlaa vgnagvpmgc yfltssllas
      361 mnvplcllgl ilpayalldm letlinvwsd ccvvsvinkk fsetedlppc sytne
//
LOCUS       WP_010725248             343 aa            linear   BCT 01-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Chlamydia
            trachomatis].
ACCESSION   WP_010725248
VERSION     WP_010725248.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia trachomatis
  ORGANISM  Chlamydia trachomatis
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Chlamydia trachomatis"
                     /db_xref="taxon:813"
     Protein         1..343
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38101
     Region          9..330
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrtffllyrf ficlapffls fplyadphtv ltkgiaaavv hadsgailke knldhkifpa
       61 smtkiatall ilrqypdvlt rfittrrepl tsitpqakqq sgyrspphwl etdgmtiqlk
      121 vkeevsgwdl fhallissan daanvladac cqsvsafmrq lneflrelgc qnthfnsphg
      181 lhhpdhytta rdlslimkea lkeplfrqvi htasytmeat nlspervlss tnkllsssst
      241 yfyppclggk tgttksagkn iifaaeknnr siivvaagyf gpaaqlyqda ialcedlfne
      301 qllrcflipp ashypvptrf gtvtapvaqg iyydfypsee ips
//
LOCUS       WP_010725251            1199 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Chlamydia trachomatis].
ACCESSION   WP_010725251
VERSION     WP_010725251.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia trachomatis
  ORGANISM  Chlamydia trachomatis
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 1199)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1199)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1199
                     /organism="Chlamydia trachomatis"
                     /db_xref="taxon:813"
     Protein         1..1199
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=136012
     Region          <703..1159
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 milnslsmfr hqatrflqdn rdsiavsfsk ntykitipde dspdgewist lsfndeerls
       61 faacscpdgd ccehlltatl aaydptegal lhvkfkssfw wglfyqlfls kaplhapgdk
      121 vytiqsqqls vslqclsaea ltywlpivha spepqtiske tfsqsalyri arelfmfsqk
      181 gaslviqenp qgfpslfslq wegialsiev ldvdtlkalf pllefsqtsl ysgepyllhn
      241 vhvvpeqari yftkeypplp ksikeyqetv lgpikyfaea kkctsipktl slpihiipal
      301 drsfrehlls qlcyeteerp ihyaihflrd aslsfsayle tpgdlseghi iypgfcyipn
      361 kgllavsgll spessftirs dhienfldey gpfikepgfe tfsnqspvgs lsynvteqgv
      421 llfhydtgna adielrfgkw tyysrqgffl nsrldlalqd gltieapqva dfiltheval
      481 ksipnffaaq pplksirfev hkekkgsgiy lqpifegleh escrlfgqfl yrenvgfsll
      541 paalqmlcqi pteipadqva efllqfskdd rmvfsdpqla lpervelnil aihrphpssp
      601 lhlkieiktn igsiplgtvl qalkgkkdfl fskagflnld nclfvflkqf lssqrydiqe
      661 ntlitmvtdi fkldalapmi tdpniqasee dlayfsqlks aclppipvnl fstdhklrpy
      721 qnsgllwlwf lynhrlsgll cdemglgkth qatalldiva qtaknpkflv vcptsvlphw
      781 ehvlashlpq aslfsfhgph kpktlpdcdi litsygtlrq nyalfykvsf tvavfdeiht
      841 aknkssqihk ilcrldaqmk lgltgtpven nliefkglld iilpnylpsd alfkrlfthk
      901 nasetdedii sskdlllklt rpfilrrtkk lvlpelpekv eslipcrlsp eqsqlysstl
      961 kkekcqiqql ekeedpasvn ylhvfallnq lkqicdhpav yfkdpesykn hssgkwaafv
     1021 kllndslasg ykvvvfsqyi qmiriialyl eehaieyalv qgksqnrkee idrfsndpnc
     1081 rvfigsllaa gtginltagn vvimydrwwn pakenqaldr vhrigqkntv fiyklvtedt
     1141 leehihylie kkmrllnqvt ttqdsnilhv lnredlitil sykdehmlse evqedsgds
//
LOCUS       WP_010725255             391 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Chlamydia trachomatis].
ACCESSION   WP_010725255
VERSION     WP_010725255.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia trachomatis
  ORGANISM  Chlamydia trachomatis
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Chlamydia trachomatis"
                     /db_xref="taxon:813"
     Protein         1..391
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=43426
     Region          2..391
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 marflctyld qsekkrrsfv eafhqreare llaaqgahil dirkvrerny rvtttelvif
       61 tkqlvlllrs gislydalts lrdqyqgral agvltslmea lrsggvfsea larfphifds
      121 fyqnsvrsge signlegalm niikvleeke klskslaaal sypvillvfs cavvvfflig
      181 viptlketfe dmemtrltka vfscstwfcr ykflvllggi ggaislrivw kkrigkrtle
      241 aiikkipilr slvikigfcr fcsvtsavlq gggnliealt lgceavsqdf lreelqeviq
      301 avvrggslsr elshrtwtpk lvigmvalge esgdlavvfa hvaqiynedi qrvltwvtaw
      361 cqpivlvllg gfiglimlsi llpltsgiqt f
//
LOCUS       WP_010725272             634 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Chlamydia trachomatis].
ACCESSION   WP_010725272
VERSION     WP_010725272.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia trachomatis
  ORGANISM  Chlamydia trachomatis
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Chlamydia trachomatis"
                     /db_xref="taxon:813"
     Protein         1..634
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72596
     Region          2..634
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mltselnaaq vtavtaplqp vlvlagagag ktrvvthril ylieesrldp kqilaitftn
       61 kaanelkerv qsqcrelgys dvpmvstfhs lsvyilrrsi hlldrqsnfv iydqsdsekl
      121 ikqclrklnl dkklcnamqf tisqaknrlq spedldskey pdptrtvyae yqeqlraana
      181 ldfddllflt ekllrtpevq qeyanhwkal lideyqdtnh aqyliakrla aahnnifvvg
      241 dpdqsiyswr ganisnilnf eqdysqalvv rleenyrscg tileaanali qnnsarlekt
      301 lrsvkgpgdk ifcftgkndr deaeqvleei snlhsykdip lsdicilyrt nfqsqsfeaa
      361 llkrgypyei iggisfykrr eiqdilaflr lfsnnydmaa fertislkkc gigattlaal
      421 mnyakttdlp ilqacwdvle kksirltkkq qqglfsylth fhqmeqlygn cdlhefinet
      481 iritdylsil kedpetyedr knnleqllae tqtwgkssen lpgfledlal kssadetass
      541 hdrlklmtih nskglefpvv flvgleenll phanskgmhe nieeerrlcy vgitraqeyl
      601 ylsraktrfl wgtertmvps rfiselpral lkfv
//
LOCUS       WP_010725367             163 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Chlamydia trachomatis].
ACCESSION   WP_010725367
VERSION     WP_010725367.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia trachomatis
  ORGANISM  Chlamydia trachomatis
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Chlamydia trachomatis"
                     /db_xref="taxon:813"
     Protein         1..163
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=18372
     Region          4..150
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mciekdlffm kkaldearka yeqdevpvgc iivhgdkiia rghnsveqlk dptvhaemic
       61 isaaaeylen wrlkdtilyc tlepclmcag aiqlaripri vwgapdlrlg aggswlnvfl
      121 ekhpfhqvec csgvcyqese qlmknfflek rkakdegrns rat
//
LOCUS       WP_010725419             131 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein, partial [Enterococcus faecium].
ACCESSION   WP_010725419
VERSION     WP_010725419.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         <1..131
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          <1..111
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 miplqaeees tnniqnyisy lidlqeqfnp gldmigfvpy lvdtdsatik snleelykeh
       61 eednlvfqni ikrsnkvstw skngitehkg ydkkvlsmye nvffellrai knrynmyiyi
      121 akgtlslllt q
//
LOCUS       WP_010725430             105 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system RelE/ParE family toxin
            [Bacteria].
ACCESSION   WP_010725430
VERSION     WP_010725430.1
KEYWORDS    RefSeq.
SOURCE      Bacteria (bacteria)
  ORGANISM  Bacteria
            Unclassified.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Bacteria"
                     /db_xref="taxon:2"
     Protein         1..105
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12298
     Region          4..100
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 meeytlvysk sfqtsletii dewenelels pesikrfvga iqkaleltkt fpkmyeevse
       61 iygmdiptyr ivigksyalf yridhakkei lvgrifqskq mkldf
//
LOCUS       WP_010725469            1049 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Enterococcus faecium].
ACCESSION   WP_010725469
VERSION     WP_010725469.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1049)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1049)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1049)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1049)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..1049
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=120988
     Region          8..952
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mkishreeae veeqlirvlg eghnqwtyrp dlkseedlwv nlrqkiisnn qaelndsplt
       61 dkefetikte lllrtktpfd aakwlkgeng maritiered pqlgsvslil ysnqdigggi
      121 styevvhqia krgsnieard rrfdvtllin glpivqielk qvsakdgvyq afnqikkyae
      181 egmfrnnifs tlqlfvvsne qttryfanal pkdlhakflf swrtkdnkkv enlyefckqv
      241 lnipdahrli adytivsedq dnktlmvlhp yqvhaiqalf iaankhqsgy vwhatgsgkt
      301 ltsfvstkll arksgidrti mlvdrkdldn qttaeftkfa sefntgissg nakanslivg
      361 tgsakelset lladananvv iittrqklda alkyakkqee kkgtnrfqkl mgqhivfvvd
      421 echralsaen meeikkmfpk stwfgftgtp ifpenrkqak gqlartthdq ygevlhtyti
      481 knaledgsvl gfqvehentv eptslenkiy rklkevetya eyspeqinrm idqmepvkke
      541 syldptvfea dehiqkvihk mfrpdnaytk fdfrngrptk sailttssid makkyyraik
      601 emtkepdwlt kefpnqpire grtmedpdfp riaityslee nsrdssvqqe emqkiieeyn
      661 qyydtswsla dieryngdin nrlarkraef kqfgkqidlv ivvdrlltgf daptiqtlfv
      721 drnleyagli qafsrtnrty pektkglivt frkpatmekn vedatklyse akeesgliyp
      781 syqeskkrfk qaygklkevs smesidehtp leirieyvka fqelnrayes lvtyddyndd
      841 mvqsstlnnq iqlleeqigv yetvkgslie eepekegedf stiefysent tklydidsty
      901 idqllgtyaa nssdardeie kalaklnkte gvkevyrqil nafdvgtlds nedifvikrr
      961 yftqasdeli hafsnewfvs ekelhasnlq ympgedpipn rkaiinskdy egykakhpea
     1021 kpfkytqemk rawrkmldde liplenelr
//
LOCUS       WP_010725457            1049 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Enterococcus faecium].
ACCESSION   WP_010725457
VERSION     WP_010725457.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1049)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1049)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1049)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1049)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..1049
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=121000
     Region          8..943
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mkishreeae veeqlirvlg eghnqwtyrp dlkseedlwv nlrqkiisnn qaelndsplt
       61 dkefetikte lllrtktpfd aakwlkgeng maritiered sqlgsvslil ysnqdigggi
      121 styevvhqia krgsnieard rrfdvtllin glpivqielk qvtakdgvyq afnqikkyae
      181 egmfrnnifs tlqlfvvsne qttryfanal pkdlhpkflf swrtkdnekv enlyefckqv
      241 lnipdahrli adytivsedq dnktlmvlhp yqvhaiqalf iaankhqsgy vwhatgsgkt
      301 ltsfvstkll arksgidrti mlvdrkdldn qttteftkfa sefntgissg nakanslivg
      361 tgsakelset lladananvv iittrqklda alkyakkqee kkgtnrfqkl mgqhivfvvd
      421 echralsaen meeikkmfpk stwfgftgtp ifpenrkqak gqlartthdq ygevlhtyti
      481 knaledgsvl gfqvehentv eptslenkiy rklkevetya eyspeqinrm idqmesikke
      541 syldpavfea dehiqkvihk mfrpdnaytk fdfrngrptk sailtmssid makkyyraik
      601 emtkepdwlt kefpnhpire grtmedpdfp riaityslee nsrdssaqqe emqkiieeyn
      661 qyydtawsla dieryngdin nrlarkraef kqfgkqidlv ivvdrlltgf daptiqtlfv
      721 drnleyagli qafsrtnrty pdktkglivt frkpatmekn vedatelyse akeesgliyp
      781 sykeskkrfk qaygklkevs smesidehtp leirieyvka fqelnrayes lvtyddyndd
      841 mvqsstlnnq iqlleeqigv yetvkgslie eepekegedf stiefysent tklydidsty
      901 idqllgtyaa nssdareeie kalaklnkte gvkevyrqil nafdvgtlds nedifvikrr
      961 yftqasddli hafsnewfvs ekelhasnlq ympgedpipn rkaiinskdy egykakhpka
     1021 kpfkypqemk rawrkmldde liplenelr
//
LOCUS       WP_010725182             694 aa            linear   BCT 01-JAN-2025
DEFINITION  ribonuclease R family protein [Chlamydia trachomatis].
ACCESSION   WP_010725182
VERSION     WP_010725182.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia trachomatis
  ORGANISM  Chlamydia trachomatis
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Domingues,S., Moreira,R.N., Andrade,J.M., Dos Santos,R.F.,
            Barria,C., Viegas,S.C. and Arraiano,C.M.
  TITLE     The role of RNase R in trans-translation and ribosomal quality
            control
  JOURNAL   Biochimie 114, 113-118 (2015)
   PUBMED   25542646
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Chlamydia trachomatis"
                     /db_xref="taxon:813"
     Protein         1..694
                     /product="ribonuclease R family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77935
     Region          18..649
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
ORIGIN      
        1 mgkaknkkkf lknrkqvlvp gtlfvhsrkg fgfvspdqpe lypfdifisa sdlkgaldgd
       61 hvlvalpfsl rggekrkgvi hkvlsrgktv lvgtivslin ptlamvyvnt igpehplkae
      121 llpkrtyklg drlllktpvw kenypsrepp plamlefign isnaktdfpv ikaefsitee
      181 fpdavvqeas qflqkhvtqa lhsrkdlrdl lcftidsssa kdfddavslt ydhegnyilg
      241 vhiadvshyv tpnsaldrea akrcnsiyfp gkvipmlpsa lsdnlcslkp nvdrlavsvf
      301 mtfskegfls dyrilrsvir skyrmtydev deiiekkqth pisktilkma elsrifsdir
      361 eqrgctrlvl psftmsldnl qepvalienk qtaahkliee fmlkanevia yhishqgitm
      421 pfrtheppne esllvfqeta kamgftitqt paqepdyqyl lqettaghpl epilhsqfvr
      481 smktasyste nkghyglcld yythftspir ryvdlivhrl lfhplsveee hleqivracs
      541 sqeriaakae gafvnikkar flkkfieeqp atlykafiit aspegisfvl pefchegfip
      601 aaklpqayvl qtkigleelp ehlrpgavis vqlasvtllt qsiewtlvea ttkakakrts
      661 kkkktesvtt kekkkspakk kkgatktkkg sgkn
//
LOCUS       WP_010725978             333 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus faecium].
ACCESSION   WP_010725978
VERSION     WP_010725978.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..333
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38271
     Region          80..>219
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkwfkrivia vpviivvilv tvflinqitp kpisllvrkq fdtsekeqvy arpddfqqki
       61 eqidikkeis ypskyknnnm diytpkvekk kspilfwmhg gayvggdknd crdyleylcs
      121 dtqqiivnid yerspeakhp tpviqlneai qaakkeikdq adwsnisigg dsadaqisge
      181 yllalqneei kkadhldptl enkqitkfis lsglldpsaf tqvsdkissf lyekcgwayf
      241 dnkdfeqsek vkslalvrha drwtqntflt dgntntftkq meevtsvfek agvkvtkvdy
      301 aeknavlnhe yqfdfsnkqa qetykklvmf fke
//
LOCUS       WP_010726094             500 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_010726094
VERSION     WP_010726094.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 500)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..500
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53276
     Region          194..498
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnfmkrawks tkvkwgrsll lfavftaili fvlagltirs aaeeaanqaq kevgatvtls
       61 anreasfkkq eqtsssgstt eerpdpgsfs ltpvsltdak kiaeldnvks ysfessasam
      121 akdgitaits sdssedsset tdvggepvgg mggnpqmtqa dfqisgvsat aqnsnfsdgt
      181 akitdgegid dsdkgtnnvv idstlaetnd lavgdtftit stededttye mtikgiyess
      241 etsssmgmkf nfmnpsntly tsytfaneln gtsddntids aiytlsdpdk mdeflkeaek
      301 lidtdtfslq sndsmyqsml eplnnvasfs knvvllvava giiiltliim itirerrhel
      361 gvllslgesr skiilqlfte vaicmilalg vasisgnvva navgqqlldq qtetttqnqq
      421 apgggqmpgn rqeqggqrgg qqgntnnpfa vsdqvselei nvkpaqlgll vgvafgislf
      481 svflasigil rlnprkilln
//
LOCUS       WP_010726117             377 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_010726117
VERSION     WP_010726117.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..377
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39839
     Region          23..357
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mndrsekyrn llvpvlsvvl glilgaivma afgfqpiqgy ssmldatlgs qrgigetlrq
       61 atpliftalg fsvansagff niglsgqalc gwvvsvwval afpdlpkvvl lplcvilgal
      121 agamaaavpg llraffgtse vivtimmnyi llyvstfalh evmpesyrss ldssnmisqn
      181 aslrlpwltq afggsrvnsg lflaiialif vwllmkkttl gfeirsvgln pfaseyagms
      241 skrtivlsmv isgalaglgg vveglgtyqn ffvqttslsi gfdgmavsll gsgsvigill
      301 sailfsilki gglgmqtgag vpfeivnvsi aliiffvgin flirfvmakv fqgkkqeeiv
      361 atieskptnq nheggel
//
LOCUS       WP_010726444             345 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus faecium].
ACCESSION   WP_010726444
VERSION     WP_010726444.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..345
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37392
     Region          165..345
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mnrsikralv slglllvlas acsrnpggtd sftteskrsi vteekgseqa tmqkftlnst
       61 vgevladpaf enfghllfpv drsvtenmsl advstsrifv wynnlqpekt veiihhlksr
      121 amdgqrifyp iyeedeiaid sskadtglfy fggeagkpfa imnagggfsy vgamhdsfph
      181 alavtdhgyn gfaliyrpnd ayadlakaie ylydhaeeln lsgenyslwg gsagarmaas
      241 lgnaaslfql tgrkdipqaa avvmqytgys vyspadapty anvgtndgia swqtmesrlr
      301 rleslgiatd fhvydglshg fglgtgtvae gwfadaiafw esqmk
//
LOCUS       WP_010726448             383 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Enterococcus faecium].
ACCESSION   WP_010726448
VERSION     WP_010726448.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..383
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41232
     Region          1..380
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mefigilcli listtigshi srrlgipavi gqllvgvllg qaglnwvkpd ilvhdfseig
       61 villmflagl esdlsllkky frpgmfvall giifpvvfgw ltgkafqvsg neaiffgiil
      121 aatsvsisve vlkelnvvnt kegstilgas vvddilvvlv lsfslsfltg eassnaslpl
      181 vlieqliyfv fifllvkwia pfllsfaekv yanssiiivs lviclgmsyv adlvglssvi
      241 gaffagiavs qtkvkeevyh nvealgyavf ipvffvsvgl evdfsdfgeq llfisiltlv
      301 ailtkllggy fgaqiagfsq hsslmvgagm isrgemalii lqigqqsqli epqyysplvi
      361 villstlisp lvlkyftkkv yev
//
LOCUS       WP_010725935             171 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YjbQ family protein [Enterococcus].
ACCESSION   WP_010725935
VERSION     WP_010725935.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Morett,E., Saab-Rincon,G., Olvera,L., Olvera,M., Flores,H. and
            Grande,R.
  TITLE     Sensitive genome-wide screen for low secondary enzymatic
            activities: the YjbQ family shows thiamin phosphate synthase
            activity
  JOURNAL   J Mol Biol 376 (3), 839-853 (2008)
   PUBMED   18178222
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..171
                     /product="YjbQ family protein"
                     /calculated_mol_wt=19345
     Region          5..169
                     /region_name="YjbQ"
                     /note="Thiamin phosphate synthase YjbQ, UPF0047 family
                     [Coenzyme transport and metabolism]; COG0432"
                     /db_xref="CDD:440201"
ORIGIN      
        1 mityteqlvl tsngqrvtyh niteqvkeiv aksgikngic lvqsphttcs vifeefmhdl
       61 dfngdeflqv dlnrildrii preltentdy rypgpkhldf llslddpdya gdagtilngd
      121 ahirasffga senfivkeei lmtgtvgsiy fidfdqnrvr nrkchilvmg e
//
LOCUS       WP_010726630             771 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus faecium].
ACCESSION   WP_010726630
VERSION     WP_010726630.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 771)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 771)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 771)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..771
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=84772
     Region          3..654
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(293..295,358,377..379,404,456..458,502,505,508,527,
                     530)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(587,591..592,594..595,620,623..624)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
ORIGIN      
        1 mngltqqevv qkmasgqqnd yqedaskstk qifsdniltl fnflnfgigi cllfvgaysn
       61 maylaiiivn ivigiyqeih arnlvrklsi vsqsevlvir dgkeqsistk elvlgdlvki
      121 gageqipadl qvisgraean ealltgesdl ivkeagaell sgsfltsgsv maevirvgae
      181 nyavrltsea kthkaihsel vdsirkvskf tsfviiplgi ilflealfir dasikisvia
      241 saaallgmlp kglvllisia lttgvtklak krilvqdmys ietlahvdtl cldktgtite
      301 gkmsiqrvea lhplyekaip eimgtylaes sdnnitmram reyfelsnry dvtnkvafss
      361 drkwgamefp elgvvyvgap erlveedrlp dslktaqang yrvlmlgiap nqqlneetpa
      421 fvepvalfei ddpirknape tlaylheegv dlkvisgdnp ftvsniarra glpnydayid
      481 lsqiteesdv reaahqytvf grvspqqkkl lvnelkdsgr tvamtgdgvn dvlalreadc
      541 siamaegdga trqianlvll dsdfttlpev lfegrrvvnn vtkvsgiffi ktiysfilsi
      601 icavtaigfp fipiqitlid laiegypsff lsfeqdkrki tyrylptali nalpnallvv
      661 vniiavyllg ktfawgsset ttlmyyllig iscmavvkac ypfnplrifl avttivgiyv
      721 aamlfhgile vnlglgetig yfvmfmivni vlrllywkad iqnqllkrva n
//
LOCUS       WP_010727029             171 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010727029
VERSION     WP_010727029.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 171)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..171
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20207
     Region          1..80
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          88..167
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mntlayillc vllskprsgy elkqlitifw eahhsqiytt lakldqqgyv tvldkdehsq
       61 kkiyhltdeg ralveewike etpaptqkde flakiyafst ldkttatgll ftreqqlnki
      121 mqknqkkmnd lsldkkqefg ryvviqrrim lcqqelqwcq qvreqmqqff e
//
LOCUS       WP_010727081             693 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase
            [Enterococcus].
ACCESSION   WP_010727081
VERSION     WP_010727081.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 693)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 693)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 693)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..693
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75339
     Region          1..63
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          89..687
                     /region_name="P-type_ATPase-Cd_Zn_Co_like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     Bacillus subtilis CadA which appears to transport cadmium,
                     zinc and cobalt but not copper out of the cell; cd07548"
                     /db_xref="CDD:319847"
     Site            order(352,354,650..651,672,676)
                     /site_type="other"
                     /note="putative HM ion binding site [ion binding]"
                     /db_xref="CDD:319847"
     Site            order(396..398,457,473..475,496,537..539,559,562,565,585,
                     588)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319847"
ORIGIN      
        1 mksyrlegld cancamkiek gvqqidgvke atvnftsgkl tidvaedrla tveqetkkvv
       61 relepdvkvt eidkekvseh gnekerntli rilfslagiv vlllfdfnep irligylliy
      121 lligydvvkk avmnivkgqi fdenflmsva tigamligey peavavmlfy qigeyfqgla
      181 vnhsrksire lmairpetah iqteeglmtv npedvqigqy vlvkpgervp ldgtiieges
      241 lvdtsaltge svpksvyvge tvlsgfinkn kpflvqveks yenstiskll elvenasskk
      301 apaenfitkf aryytpvvvg lavllavlpp ivsgaafsew iyraltflvi scpcalvisv
      361 plsffggigg askigvlikg snylellaqt etvvfdktgt ltkgdfsiqt idptgidpkk
      421 fmqyiasaeq fsthpiaqsv legyegpllp atniqefvge gilaevdskq ilvgnhklme
      481 rfeisfpssq eigtllyiai nqsysgylvi adtlkedavd alvqlkqagv khtvmltgds
      541 kkiadhigkq vgvdkiysel lpedkvqrle eilqrsnkkt afvgdginda pvlaradvgi
      601 amgglgsdaa ieaadvvimn dqpskiadai rlakktlkiv kqniifaigi kmlvlalgaf
      661 gyatmgdavf advgvtvlav lnamrslhvk nky
//
LOCUS       WP_010727129             188 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010727129
VERSION     WP_010727129.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21689
     Region          1..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrrkvytkdq ilkaaydvva kegfkgftar niakkmgist qpiylefknm edlkntllds
       61 ifeqlkedvf piertgdkii dlglnyiyfa kkhhslymal yidehgdgkk ihdfsynyfr
      121 eivkederyn qlsddyidal htgtwvavtg laslmssnim hpteeqiial ikrtidsila
      181 ldnpetir
//
LOCUS       WP_010727192             204 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Enterococcus faecium].
ACCESSION   WP_010727192
VERSION     WP_010727192.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..204
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22995
     Region          <1..190
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mykdglkrgi dfllslvgii vlspillilc iaikidskgp vifkqkrvgk nkshfyiykf
       61 rtmkvdtpqe tpthllsnpd ffitrvgkfl rktsldelpq lfnilkgdma vigprpalwn
      121 qydlieerdk yhandirprl tglaqisgrd eleidykarl dgqytanitp mmdlkcffgt
      181 iisvfksdgv veggtgsvkk enak
//
LOCUS       WP_010727279             104 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Enterococcus faecium].
ACCESSION   WP_010727279
VERSION     WP_010727279.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..104
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11621
     Region          7..96
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mnllfqsiks itvpelkekl lenpalldvr tpaeyrgghi kgaknvplqs inrydrdkek
       61 tvyvicqsgm rskqaakelk ksgydvvnvr ggmnqwfdrt vggk
//
LOCUS       WP_010727284             536 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_010727284
VERSION     WP_010727284.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..536
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58971
     Region          1..533
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 mtdkfsrwst lfsqnlsrdw kkiliwlvgv tafsggfvpa feeltsgqgl aglyetlqnp
       61 amiamvgptp asnaaeytlg amyanemllf cslfaavisv lhvvsqtrkk eelglielir
      121 sfrvgrqans laviaesili nlllaisisc tmiffqadsi taegawlfgl svgsmgilgs
      181 avalfaaqlm pssassngls laflgglyll raitdvadss lsmwnplgws yltypfttnn
      241 wipllylflf sliliissfv leehrdlntg yiperegkpy akrsllslrg llfylnkgmt
      301 iswlitfglm gaaygsiygn mqqflesndl mkqmfiqsga sieknftsti mvvliclaai
      361 lpiasinrlf teethgrmnq lfatkisrnq lywtnmllai lfailailis sgalglsala
      421 smkdakdmdl lmflkagfnf lpavlvfigi sgflfgwlpr mgklayiyla ysfalnyfgg
      481 ildlpewfsk tavpswvprm pndsfdlsvf ltlscislal fvlgsigyrr rdlleg
//
LOCUS       WP_010727302             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphatase PAP2 family protein [Enterococcus].
ACCESSION   WP_010727302
VERSION     WP_010727302.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..218
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=25179
     Region          25..203
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(105,112,128..130,173,179,183)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mkyktsfqva gsfflvlffi lgwivkfhls wlsgfdqwft givrasypdl nsyqlfmtkf
       61 gnpltviilf acaalwmwyk kkraetfwfv sgfiviagii npviklffmr erpslvhlvv
      121 etsysfpsgh aagsmilygs llfllpafvq krtlrtllql lmvfiivsvg isriylgvhf
      181 ptdiiggyll slswlcltyp vyrekrkqid nsyrkkdf
//
LOCUS       WP_010727315             574 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus faecium].
ACCESSION   WP_010727315
VERSION     WP_010727315.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 574)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..574
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=66214
     Region          181..571
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mnkfrilfsk gtllnrllrk yavimigvtm tatvifsiht weqnqkqaen mtsdavqsts
       61 rmlndkttls riiknqlvgn sekienvtty ltnpidqylm yvyeqqnstd elvsfpnqik
      121 dlyanyeels aiyivlnqlp eyyessrenk ggkikkgtpk lldafyiklp itqggaesgs
      181 ifigfqkkel dmilenltsf nglslymisg ttnrlytfhd nkiaketfer qemiiteslq
      241 knsqlpiddl eknnfvqyqe lsddyrilav ldkksvkiet gknlapliig iiildnilli
      301 flyktfkrys qqvsivmqam dqtaagnlet riditnteye lkelsigine mldsinqfve
      361 diykleikqq dahmralqaq inphflyntl eyirmyaise gseeladvvy afsallrnnt
      421 nqektitlke eldfcekyvy lyqmrypnrv ayhfmidpdl ekievpkfvi qplvenyfkh
      481 gidftrfdna lsvkvlqegk rvriiikdng kgmtekrlkq veeklshpkv elhgsiglqn
      541 vnerlrasfg ssyymslenn etggltvsit fkeg
//
LOCUS       WP_010727316             717 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Enterococcus faecium].
ACCESSION   WP_010727316
VERSION     WP_010727316.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..717
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=82513
     Region          6..715
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mnigqidtrh atanqpnfsn gncqpytgvp sgmnyfapqt tdqngswwfh pddrvfqgyr
       61 lthqpspwmg dfshmlftpi ngklqentlf haqssyrpee sifcpthlsi cqlrygicst
      121 lipsmyggil sidyskndsg lllsfpgrhq lfvidpytve gkithfagse dpdfsfyfil
      181 rfeypltide favsnknsds iplyfeqtkk qtirfgtsfi sseqaaynle leqnqskety
      241 lahsqeqwqs yfdriqlthh dqqqlrtfyh nlyrvflfpq tfyeidpsgq kihydttsrs
      301 ikpgvlytnn gfwdtyktvy plysliavek yeemlegfln syresgylpk wlspderglm
      361 pgtlidavia daavkdirrd lmpefltame kgatvqskhp nygrqgtedy ltygyvpnhy
      421 hesvnhtldy aysdfcisqv akvleeeemt kkyqqqslny qnifdyesgf mrskdkdgkf
      481 repfsanrwg qdyaegsawq ssfavyhdfs gligkyggse rykeklielc nqpptfdpgg
      541 ygfeihemse maaiefgqla isnqpsfhyp ylfsyigqpe maqpllkqlm tqtfddspmg
      601 ypgdedngsm aawyifnslg fypvtpgtge yvigmplidk avlllsngke ltieatpnrp
      661 qqqfihkikr mdkeytklyf thqdllkggt isyqlgivph pkkyqakdlp fslsnyn
//
LOCUS       WP_010727317             429 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 125 protein [Enterococcus faecium].
ACCESSION   WP_010727317
VERSION     WP_010727317.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..429
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49222
     Region          6..426
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 mvykdipksv qkfmeditqk cgdihadwak nftaafantl lttvkkqndg ttflltgdip
       61 amwlrdstaq vrpylviake eeeladmisg lvkkqffyin idpyanafne eangaghqtd
      121 htkmndwiwe rkyeidslcy piqlayllyk ntgktdqfnq sfiegikkil dvfkteqdhe
      181 hspytfvrdt trkedtlind grgaktaftg mtwsgfrpsd dacrygylvp snmfavvvlg
      241 yveeifqtil ddkeivqqtq klkkeiqegi qnhgrtvnqk gqtiyayevd gmgnatvmdd
      301 snvpnliaap ylgycseqee dylqtrrtll skenpyfyeg kyakgigssh tpekyvwpia
      361 lamegmttsd ksekerilnl lvatdagthl mhegfdvnnp enytrewfsw anmmfcelvm
      421 dyfdirvek
//
LOCUS       WP_010727383             376 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerate kinase [Enterococcus faecium].
ACCESSION   WP_010727383
VERSION     WP_010727383.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..376
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39518
     Region          2..367
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mriliapdsf kesltaleaa qaiqsgfqev fvqaeydllp igdggegtvs sladslrlkr
       61 qtavvtnsfg knkeiqyasd gqtaifemae ivglkdvpln qrqplrlstr gvgelirqll
      121 qqgvrhiiig vggsstndgg igmaeglgya fydqdnqkve algenlgkia ivdktnvpie
      181 likakitvit dvtnllcgke gasfvfgpqk glkenelava dqamhdfymr fapqvieasg
      241 sgagggmgag llafasgkiv sgidyvldll efdkrvqqad lvivgegrld gqslkgkapv
      301 giarrvpegv pviaicgsvg kgsekaadvg isavfpilpa avplqealqq atdnlhrtak
      361 niasllqvvh fqggnr
//
LOCUS       WP_010727438             564 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I mannose-6-phosphate isomerase [Enterococcus].
ACCESSION   WP_010727438
VERSION     WP_010727438.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Jensen,S.O. and Reeves,P.R.
  TITLE     Domain organisation in phosphomannose isomerases (types I and II)
  JOURNAL   Biochim Biophys Acta 1382 (1), 5-7 (1998)
   PUBMED   9507048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..564
                     /product="class I mannose-6-phosphate isomerase"
                     /EC_number="5.3.1.8"
                     /GO_function="GO:0004476 - mannose-6-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009298 - GDP-mannose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64919
     Region          217..564
                     /region_name="ManA"
                     /note="Mannose-6-phosphate isomerase, class I
                     [Carbohydrate transport and metabolism]; COG1482"
                     /db_xref="CDD:441091"
ORIGIN      
        1 myekrpriil keqistftgy tkiinellkd kktkkialec ypgidsekva heiralkmed
       61 lfitttnqfy qssneikekl tevltddrvf grltdatfld flakeknesl nqadrvllig
      121 vgaaelidad mvvyanltkr niqlklkaga enwqadnaqe eflkkvkray yfewpaader
      181 kklvlpssqy lidlneentp kmiktkdyyn alrhfsnqpf rlvpyfepgi wggkwmqkkf
      241 dvgkeevnla wcfdgvpeen svifeigtvt fevpgndlvl fypvsilgek vfgrfgsdfp
      301 irfdyldtma ggnlslqvhp tldyayrkfg lkytqdesyy imdceedayi ylglkeevgt
      361 pdfiqalees ritgrldvek yinkikvkkh dhflipagti hcsgencvvl eisatpnrft
      421 fklwdwervd ldgiprpihi ehgkqvines mktnrvfsel vnqvvdltit enihiertgl
      481 hplepiethr ltfcvpieqt tegsvnmlnl vegegivies taetfeplki nygetfiipe
      541 niknyvirpi vdketcivmk afik
//
LOCUS       WP_010727482             644 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus faecium].
ACCESSION   WP_010727482
VERSION     WP_010727482.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..644
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73742
     Region          6..533
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          569..631
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 millqanqia rhfgaevlfe nihleistga rvalvgrnga gkstllkiia gieapdegki
       61 aknktatlgy laqdtgldsn etvwnemlka feqvrqmeer mreleifise gtpdtpayts
      121 ylkeydrlqh dfsdrngygy eneirsvlhg fkfdssfydq kidtlsggqr trlalarmll
      181 qhpdililde ptnhldietl swlenylqsy tgallivshd ryfldkvvne vyelsrrkmr
      241 hykgnyskyl dlkaeqlase wkayekqqte ihkledfvar nlvrasttkr aqsrrktlek
      301 mdrldrpqgd ekqanflfsi ekpsgnvvlq iedaaigydn vtlsepinld irrqeaialv
      361 gpngigkstl lksiihqipf irgketlgtn vtigyydqgq adlhtnktil aelwdehptt
      421 pekeirsalg aflfsgedve kpipllsgge karvalakla mnkenflild eptnhldidn
      481 kevlenalid ydgtllfvsh dryfinriat kvvelsengs kvylgdydyy lekkqeeeei
      541 aellaqdepe sapaptnksd yyqskeqqkl irslqrkitq veeemalide widqleqemv
      601 apenledhvk lnelnqdlea arqdqetklt eweelslele eyen
//
LOCUS       WP_010727484             267 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Enterococcus faecium].
ACCESSION   WP_010727484
VERSION     WP_010727484.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..267
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28938
     Region          1..239
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 migliyfvvi vlantvgais gmgggvlikp ildligahsi agisfystva vftmsivstv
       61 rqvssgksln wqivgwvsgg avvggiagni vfevflrlfe nekhvqliqi fltvltlvfa
      121 ffytkhhqpk fhltswiwyl icggilgfla sflgigggpi nvsllmlmfa lpikeatlys
      181 lstiffsqla klvtialtsg fmrfdlsmlf yiipaavigg lwgakfsril spkkvtfifq
      241 vivlvvllvn cynafvilqt lgesrlt
//
LOCUS       WP_010727492             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HD domain-containing protein [Enterococcus].
ACCESSION   WP_010727492
VERSION     WP_010727492.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..455
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52661
     Region          13..425
                     /region_name="YdhJ"
                     /note="HD superfamily phosphohydrolase [General function
                     prediction only]; COG1078"
                     /db_xref="CDD:440696"
ORIGIN      
        1 mttpykyqml pmekvfrdpv hnyihvqhqv ildlinskev qrlrrikqlg tssftfhgae
       61 hsrfthslgv yeisrricdi fsrnfskeki gnggwddqer lvtlcaallh dvghgpysht
      121 fehifhtnhe aitveiitsp etevyqilnr veegfpekva sviqktypnp qvvqmissqi
      181 dadrmdyllr dayftgteyg tfdltrilrv irpyeggiaf smsgmhaved yivsryqmyv
      241 qvyfhpvsrg mevilehllh rahelyqeda ssfelhsqll lpfldgsftl eeylklddgv
      301 lgtyftqwse sadpilndla krflnrkplk satfsgnrds nliqkltllv ekvgynpvyy
      361 tavnssydlp ydfyrpeqgr hrtqieilrn dgtlielsqv sqlvaalagq eqgderfffp
      421 kemvdpslrd hydlfdetyq efashirnga liein
//
LOCUS       WP_010727526             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010727526
VERSION     WP_010727526.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..249
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28430
     Region          4..249
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdrklseteq ylwnfiehhi leipnysivk lseqanvsta tivrtmkkkg yegftsfkhh
       61 lkegenknin fsfldkvdkg irrailkneq evvrtinmle igniedaiqr ikfadrvfvf
      121 argfsemigq emlvklqltg kncqmhtdpe iiksisqklt kkdsvifvsl ngetkelvta
      181 akncydaeig silvtanhss tlkdyceinl vgfksegsyf pdyevrsrlp lqiiarilld
      241 ayvlrmgen
//
LOCUS       WP_010727798             791 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Enterococcus faecium].
ACCESSION   WP_010727798
VERSION     WP_010727798.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..791
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=92596
     Region          178..779
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mikqskisvr hlvefilrrg sidnrkksnh talegarihr klqkdageny ekevflkttv
       61 qldeyhlive gradgifkrd giyyideikt seprfedlep eqvelffhqa rvyayiysqe
      121 hdlqeinlql tyfqtaeevi trkvehqtre qletffkklt edykewlvfq enwrtvrnas
      181 lmalkfphde yrkgqrelav aayktirtkq klfveaptgt gktistlfpa lkavgeeege
      241 kifyltakti trqvaedamt alkdtgaevk svtltakdki cfldettcnp dqcpyangyy
      301 nrineglwdl lnhenqitre vietyarkht lcpfelsldv siwcdviigd ynylfdptvy
      361 lrrffedekn edylflidea hnlvnrsrem ysaelsyekt krskeaipke fkklhrrfnk
      421 llkefdsire iakedhwdyh hqkapaeslv kagyqlseki kewlaefpeh psqeqllpyy
      481 fdllhflkvs efyddhyett vektyrdliv kefcidpslf leqsldkgks silfsasfsp
      541 lsyyqetlgg qkslayklps pfpegnqqvf ianylettyr krehslaklv etihafadgk
      601 vgnyfvffps yqyldlavea frqqypdsnv liqetdmnee ererflekfq tnpaetligf
      661 cvlggifseg idlrgdrlig smivgvglpq mnheqeliks yydekehlgf ayayqlpgmn
      721 kvlqaggrvi rgmadqgivv ladqrfssfs yrrlfpqhwq tarevrsvge leegiqrfwl
      781 skeavnqkne e
//
LOCUS       WP_010727811             435 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            faecium].
ACCESSION   WP_010727811
VERSION     WP_010727811.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..435
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45961
     Region          14..420
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 meketqngka avlgmqhlla myagavavpl ligtglgfnq eqmtylisid ifmcglatll
       61 qltvnrffgi glpvvlgcai qavaplilig tnegvgaiyg siiasgifvv lvsgvfskik
      121 klfppivtgt vitvigltli pvaiekmggg nataadfgdk tnlllafvti llivgvqmla
      181 kgfirsiavl iglvggsila afmgmidlsa igdaplfhvp qpfyfgkptf dvwsillmii
      241 ismvsmvest gvyfalgdit gknvgeeelk kgyraeglav ilggifntfp ytgfsqnvgl
      301 vqlsgiktrk piyfsaffli vlglfpkiga laqiipepvl gggmlvmfgm vavqgirmll
      361 evdfsndknl livavsvgfg lgfnvtptlf sqmpqtlqmf tgngivmssi taiilnlifn
      421 glkkdeeile eafkk
//
LOCUS       WP_010727816             240 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Enterococcus faecium].
ACCESSION   WP_010727816
VERSION     WP_010727816.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10470251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..240
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27402
     Region          4..237
                     /region_name="TatD_DNase"
                     /note="TatD related DNase; pfam01026"
                     /db_xref="CDD:425997"
     Site            order(6,8,115,138,184)
                     /site_type="active"
                     /db_xref="CDD:238617"
ORIGIN      
        1 mlsdahchld gsqslallqq ehtiltiinc dspeewkenr qlaasktqal sygihpwkad
       61 sytfeqvepf lkkariigei gldniwtnvp mttqkkvfer qlafaainek pvvlhtkgce
      121 keilsyiqan pnhylihwys sldyqqdyid lgcyfsigld lkknpavwql aktvpidhll
      181 ietdglhaae walgdsfsek dyvslleeql ktiaeikels veevkknayq nlerfirlgk
//
LOCUS       WP_010727887             425 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus faecium].
ACCESSION   WP_010727887
VERSION     WP_010727887.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..425
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47890
     Region          8..425
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnefvqvfpe nwqkkyedkg fispsliqra vfqplsnkqs ivavsptgsg ktlaylwpll
       61 lnvepgeasa lvifassqel aiqvadvare wgkdkelkvq slvgganvkr qieglkkkpe
      121 iligtpgril elmkakkika hqvktmvfde adqlfdagns qiidqilhqa pteyqlaffs
      181 atadrslesi ekitgktfet idvtaeddsr kglrhyflrv pirkkddylr rlthiedfhg
      241 liffnqltel gvmeekllyr gvpvgslasd qnkllrkaal eqfkkkmvra llttdvaarg
      301 ldvtglpyvv naevplseea ylhrsgrtgr mgnegivitl vqdnnlrdlk rllrpsnitl
      361 eeiflyggkl qteqptkeda apavnkkyak tfsgkeqnpe ynkekirkkv knkskkernk
      421 garrk
//
LOCUS       WP_010727968             540 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus faecium].
ACCESSION   WP_010727968
VERSION     WP_010727968.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..540
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60731
     Region          4..527
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mitvndvslh fsdrklfddv nikftpgncy gligangagk stflkvlsgd lqpstgsvtm
       61 gpdermavlk qnhydyedyt vletvimghk rlyevmkekd aiymkedftd edgiraaele
      121 gefaelngwe aepeaavllq glnipeelhh qqmseltggq kvkvllaqtl fgkpdvllld
      181 eptngldiqs inwleeflin fentvivvsh drhflnkvct hmadldfgki klyvgnydfw
      241 lessqlaakl qananakkee qikelqefia rfsanasksk qatsrkkmle kitlddiqps
      301 srrypfvgfk pereigndll qvenvsvtid gkkilddisf nlskedkvaf vaenditttt
      361 lfkvimgeit pdtgtvrwgv ttsnsylpkd ttkefdtdlt ildwlrqyas keeddntflr
      421 sflgrmlfsg eevlkpvnvl sggekvrcml skmmlskanv lvlddptnhl dlesitalnd
      481 glmaftgsil fashdhqfiq tlanriiavs dkgvidradt tydeflentd iqkqlnelwa
//
LOCUS       WP_010728005             242 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010728005
VERSION     WP_010728005.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..242
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28711
     Region          5..242
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mkktannipl yaqiadelrt kifmeewitg mkipteenlc esyhvsritv rtaidslvne
       61 glverkrakg tfvtdwktek dehftlvrsf tdemrelgke iktihasisi ekanrkiakl
      121 lnvspdekvm vmrrtratta dekpfvyfit yfkyradfpt edsayydsfy ellnryhiqv
      181 nqskeyieai lpdkeiqevl nitehepilk rvritkqlet dfreysecyy ignkyryyid
      241 fs
//
LOCUS       WP_010728017             335 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Enterococcus faecium].
ACCESSION   WP_010728017
VERSION     WP_010728017.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..335
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36795
     Region          <1..335
                     /region_name="trifunc_aldol"
                     /note="KHG/KDPG aldolase/sugar kinase fusion protein;
                     NF041633"
                     /db_xref="CDD:469516"
ORIGIN      
        1 mgkvvtlgei mlrlsteqgt ridsserfaa hygggeanva islanyghea ifatkvpdna
       61 lgkavkkhlq cygvdtkqvl sggprlgtyy metgsgeraa sviydragss faemdhlews
      121 leelfqgidi fhvsgitpal skkwqkmtkq vieaakktgc lisfdinyrg klwtqqease
      181 vihqllplvd icsagkmdal yllgiekape aeeqpliyyy qkmqekfpni qvfystkrtv
      241 hsasenelkg tlwmnheyve sqvhritpiv drvgggdafa ggvlhgilsn mspqeiidfa
      301 taasalkhti hgdcnqfsqe evaqflacgs gkiir
//
LOCUS       WP_010728055             536 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_010728055
VERSION     WP_010728055.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..536
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59105
     Region          1..533
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 mtdkfsrwst lfsqnlsrdw kkiliwlvgv tafsggfvpa feeltsgqgl aglyetlqnp
       61 amiamvgptp asnaaeytlg amyanemllf cslfaavisv lhvvsqtrkk eelglielir
      121 sfrvgrqans laviaesili nlllaisisc tmiffqadsi taegawlfgl svgsmgilgs
      181 avalfaaqlm pssassngls laflgglyll raitdvadss lsmwnplgws yltypfttnn
      241 wipllylflf sliliissfv leehrdlntg yiperegkpy akrsllslrg llfylnkgmt
      301 iswlitfglm geaygsiygn mqqflesndl mkqmfiqsgv sieknftsti mvvliclaai
      361 lpiasinrlf teethgrmnq lfatkisrnq lywtnmllai lfailailis sgalglsala
      421 smkdakdmdl llflkagfnf lpsvlvfigv sgflfgwlpr mgkfayiyla ysfalnyfgg
      481 ildlpewfsk tavpswvprm pndsfdlsvf lmlscislal fvlgsigyrr rdlleg
//
LOCUS       WP_010728079             510 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus faecium].
ACCESSION   WP_010728079
VERSION     WP_010728079.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..510
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57650
     Region          6..509
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msiltlnnit qqfgdkilye gvdlqlnage hlgligqnga gkstlikiit geilpddgqi
       61 hwqknihkgy ldqyvevdet ltieeflkta yakeyekeek iaflyqtyse tfddslleka
      121 gklqteldqg vfyqidtlva emssglgidv lgldsllknl sggqrskvil aklllenpdv
      181 lildeptnhl ddqhiqwlmq flqdfdgayi vishdqefld qitthiadie fgkitkytgh
      241 lkqalkqkeq nresylrqyh aqqkqiekte ayirkykags rstmaksrqk qldkierltp
      301 pasaskavfd fpfspivttl avettdlvig ydrpllapin ltirfgenia irgfngigks
      361 tllktligei ekisgdfhfp dntkinyfsq dlywenplet plqylssqfp katikelrrq
      421 lakaglvnql aseplttlsg geqtkvklaq ltmnqgnlli ldeptnhidq etkeslqdgi
      481 qkfpgtviiv sheqefyqdl vqrvieiepk
//
LOCUS       WP_010728085             173 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RDD family protein [Enterococcus].
ACCESSION   WP_010728085
VERSION     WP_010728085.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..173
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=19610
     Region          1..147
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mnkksgietl pnyvfagfwl rffaflidli cisiithati glfykimgle sdksiitfyg
       61 iaslaiylty fvlltklnsg qtigkmifgi rvvsfeekel swqtifirec icrfilknfv
      121 fqigylvaaf tpkkqhigdy fsntsvviir sleainygqk isnsktpnle gik
//
LOCUS       WP_010728103             211 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Enterococcus
            faecium].
ACCESSION   WP_010728103
VERSION     WP_010728103.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..211
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23257
     Region          1..205
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mielkkvnka fgekkiikdl nliipdgktl aivgpsgggk ttllrilagl essdsgefyl
       61 dgvpfnpfel kmkeqvvgvv fqdfqlfphl nifenitlap kmvlkqtkee ytkkaeelaa
      121 slgisdllnn ylyqlsggqk qrvaiarala mnprvlayde ptsaldpelr qqverlilsl
      181 kedgvtqiiv thdlvfaenv gdqllkvspi h
//
LOCUS       WP_010728135             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus faecium].
ACCESSION   WP_010728135
VERSION     WP_010728135.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..282
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30870
     Region          3..277
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkkifgfaa allltvglaa cgnnsdskds ankaddttlk vgasptphae ilehvkpllk
       61 degidleivk fddyvlpnqs leegdidany fqhipylnke ikekgydfvn agavhiepmg
      121 lyskkvkdvs elkdgatiit snsesdwgri itilqdaglv kvkdgvdlet stfddieenp
      181 knlkfnhtid psllastyqn degdlvaina nfaygaglnp ledavllekd nspyvniiat
      241 rkgdedsdki kklievlhrk evqewitdkw ggsvkpvkad ak
//
LOCUS       WP_010728161             306 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus faecium].
ACCESSION   WP_010728161
VERSION     WP_010728161.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..306
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35669
     Region          1..227
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkigvigvgn iaekaylpty akkqgtldfy fatrnketke riqkeygfqh lyetidelle
       61 ekieacmiha atkvhyelak kclengihvy idkplsihln evrelqelad knqkilmigf
      121 nrrfapmvee lkripdkrli hlqknriaak ettefvlydl flhlidtavy lldepilrtk
      181 yqiretkefl eyailqletq nqtailtmdl asganiekyq vtskngtyev ndltqlviqd
      241 adgkkvkefg dwtntlvkrg fepmveaffs qirlgksete mlkqkevvrs helceevlkd
      301 hyryql
//
LOCUS       WP_010728263             448 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010728263
VERSION     WP_010728263.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..448
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=49155
     Region          1..419
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mekleqflss rllpmseklq knkvlaalme gfirtspitl giafitiign fpfpgwidfl
       61 knvgifphve aitngatgvf slyvvyslaf syakqlgtne rnasiislas fimlmpqsvm
      121 ttvtqdgkav eqavgalrld ylggqglfig mlvallitrf yaflakknim iklpesvppm
      181 vtqslspvfv vtiifvvvfa lrvlfgltqs gtifqffidv inaplnslva splsiiiime
      241 llavlwffgi hnavlqgplg aismtmvvgn iaafqegkal pylvpsviym gmyaagfmgf
      301 vtffmiksks akmrqlgkls fvpslfnvte plmfgmpiil npiffipqif tqliagfvtw
      361 gltttilpis lnptmsllpw ttptfvkmpl sgglnytilm vicmvigvvm wypfikiadk
      421 keleleaale keeaetkaek iinaevea
//
LOCUS       WP_010728264             304 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Enterococcus faecium].
ACCESSION   WP_010728264
VERSION     WP_010728264.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..304
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33234
     Region          9..293
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mkgksmwtls idiggtyiks alimdtqire krqietpktd kdnfilvlve liysyqqiep
       61 iefvgfsvpg avkeastvff ggavaclnev nlkqeiekhl pvrvfvenda raavlgeasf
      121 ghlkgienga giilgtgvgv gllldgqvrk gphcqagevs fliqdrging aesfaginls
      181 avrlvkelak lfqcepegpl vfdylyqked dqaqtlyrty cnqvailcfn iqclldldki
      241 iigggiskqk rlirdiqkny eaifsvspmi eqtitkmtie aaafeseanl igaakgvrln
      301 eisn
//
LOCUS       WP_010728266             321 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus faecium].
ACCESSION   WP_010728266
VERSION     WP_010728266.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..321
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36195
     Region          31..237
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mqintmtidn eantaltvyl heekpefhri dkrpfilvip gggygfcser eaepialkfa
       61 aegyhagvlr yhvgehrdfh kaladaeksm dliallaeka kidqskvavi gfsagghlaa
      121 alstlsdrkp sacilaypai lrsfaeamki kapsldmcvt pqtpptflfs tfednvvpie
      181 nsilylrale endvpfethi fqkgkhglsl gnkwsgnsee mvdprfakwf elciewleii
      241 wsqaavettq kiedvwqvpi knlyaieanr sillehlpfl adksrykiir slslnqlcef
      301 spekftktki sqwvneltwn l
//
LOCUS       WP_010726502             441 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Y-family DNA polymerase [Enterococcus].
ACCESSION   WP_010726502
VERSION     WP_010726502.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..441
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=50319
     Region          13..369
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(16..17,20..21,57,60,118..119,179)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(116,119,208..214,243,270..275,302,327..331,333)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mmdyskepvn dyflidmksf yasveciern ldplttelvv msrsdntgsg lilasspeak
       61 krygitnvsr prdlpqpfpk tlhvvpprmn lyikrnmqvn nifrryvtde dlliysides
      121 ilkvtpslnl fttegtrsqr rkklaqmiqe rikeelglia tvgvgdnpll aklaldneak
      181 hnegfiaewt yenvpekvwn ipemtdfwgi gsrmkkrlnq mgimsirdla nwnpytiksr
      241 lgviglqlyf hangidrtdi aippeptkek sygnsqvlpr dytrrneiel vvkemaeqva
      301 irirqhnckt gcvhlnigts iletrpgfsh qmkipitdnt kelqnyclfl fdkyyegqev
      361 rhvgityskl fytdslqldl fsdpqkqide enldkiidki rqkygftsiv hassmlegar
      421 sitrstlvgg haggnggikn d
//
LOCUS       WP_010728344             294 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Enterococcus faecium].
ACCESSION   WP_010728344
VERSION     WP_010728344.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..294
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=32627
     Region          50..294
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mkvsqkiils illlltlvvg yfsiefihgf ssakqsstvk kvepksvptt lnvaligsda
       61 rskdengrsd sllvaqynqk tqqaklisim rdsyvdipgy gmnkinaays yggvdllnqt
      121 lkenfkfeap yyasitfqdf idcvnelfpg gvkidaeksl dldgvyinkg eqvmdgntll
      181 qyarfredke gdfgrirrqq qvikaisqql kdvtsifklp kavgkllgsi qtnlpesvll
      241 dcgmdflkdn nkkidtlsvp vdgtwdfndn tpsgsvleld ltknqeaikk flnn
//
LOCUS       WP_010728354             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecium].
ACCESSION   WP_010728354
VERSION     WP_010728354.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..228
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25425
     Region          1..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mkkiltmkkv tktfgsghtk vsalkaidfy vkegefvsii gpsgsgkstf ltisgglqtp
       61 tsgeivingh sltelpekkr adlrfkeigf ilqssnlitf ltvkeqfelv dqvtskkeds
      121 tkidsllqsl diqslknsyp kdlsggerqr vaiaralyne psliladept asldtdhaye
      181 vvkllvkeah ekqkatimvt hdvrmiqwsd rvyrmedgyl teeekkke
//
LOCUS       WP_010728371             382 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Enterococcus
            faecium].
ACCESSION   WP_010728371
VERSION     WP_010728371.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..382
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43238
     Region          20..301
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 makkqeekkk qipqqrtkkg vlagilglvt nlilfvsklm iglfsgsvsi madavnslsd
       61 tassiltlig fkiaakpadq ehpygherfe yisglfvsii ityvgfqfle ssaekiihpe
      121 nvsltpivff vliisiflkf aqgkmyqvia qsidsetlra tatdsyndvf ttlavllsaa
      181 iewvtgwrid gyigfalaly ilysgltmlr nfvyellgsr ptpaeieeme eqlnacddil
      241 gyhdllvhny gpnkrfasvh ievdesmnln vahkiidlie kdfkksldve lvchldpmpv
      301 dnekyynilr qlkqilletg tglnihdfrv ihqgktlqfd vvvpekfqfd dtelerilrs
      361 qieekigdyq leitfdhnyl ly
//
LOCUS       WP_010728445             295 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Enterococcus faecium].
ACCESSION   WP_010728445
VERSION     WP_010728445.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..295
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31660
     Region          1..284
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mklgfigtgv mgsavarhll eaghevavyn rtkakadplv tegaiwadtp kavaeqsnil
       61 ftmvgypkdv eeiyygqsgi fsadisghil vdlttstptl aekiaktake kgadaldapv
      121 sggdlgakng tltimvggee avydqvlplf kefgttftlh gsagkgqhtk manqimiagt
      181 mtgmtemlvy aqkngldlkk vietlsggsa anwslsnysp rilkedytpg ffvkhfikdl
      241 kialeeaekm dlvlpattqa lklyeeladk gfendgtqal iklwwpegki pekks
//
LOCUS       WP_010728408             888 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus faecium].
ACCESSION   WP_010728408
VERSION     WP_010728408.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 888)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..888
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=96388
     Region          5..885
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 menkeqaqqa vyketidslm qqtqsstdgl sttqakekle rdglnqlkek pkkptwklfl
       61 etfkdamviv llivaliqmv mgdyieflvi favlmlnsii svvqtkkaeg slealknlsa
      121 pdarvirdgk ektipanelv vgdivlldag dyvpadgrll dagslkvdeg mltgestsae
      181 kevtdiistv pigdrtnmvf sgtivtygrg kflvtstgnn teigqvagll estteqvtpl
      241 qrgldkfskk lslailalsl lilgiqlfri ylgegtgdmt adivsavmfa vavavaaipe
      301 alqsivtivl slgtnkmakr haiirklpav etlgstsiic tdktgtltqn kmtvvdyflg
      361 ngdtgdftnd pskwtaderr lieisvland asisedgtkl gdptevafid fseklnqpyq
      421 eirnnyprqa elpfdsdrkl mstghtidnk nylfvkggpd ivfqrskkvl lngevvpmtd
      481 elmkkfqeqn eafstralrv lafayrpldn fdlsfededd lilvgllami dppraevtqa
      541 vtearsagik timitgdhkt tavaiakqig ifeegnlalt gteldelted qlnevlekvt
      601 vyarvspenk irivrawqnk ghisamtgdg vndapalkqa digiamgtgt dvakdaaamv
      661 ltddnfasiv savevgrnvf dnvkkaisyl fagnlgaiia iifalvadws npftalqllf
      721 inlvndslpa ialgtekaep atmnrpprdp nsgiftdktl isvtyrgvli giavifaqwl
      781 gmqhspefgv amsfstliwc rtlqtfpars ntqtaiqagf fsnrsvllav vvcsalyclt
      841 mipglkevfs ipsafgltev ftcmgialvt ivlmeitkli ivrvqgnk
//
LOCUS       WP_010728494             425 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus faecium].
ACCESSION   WP_010728494
VERSION     WP_010728494.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..425
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48032
     Region          8..425
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnefvqvfpe nwqkkyedkg fispsliqra vfqplsnkqs ivavsptgsg ktlaylwpll
       61 lnvepgeasa lvifassqel aiqvadvare wrkdkelkvq slvgganvkr qieglkkkpe
      121 iligtpgril elmkakkika hqvktmvfde adqlfdagns qiidqilhqa pteyqlaffs
      181 atadrslesi ekitgktfet idvtaeddsr kglrhyflrv pirkkddylr rlthiedfhg
      241 liffnqltel gvmeekllyr gvpvgslasd qnkilrkaal eqfkkkmvra llttdvaarg
      301 lditglpyvv naevplseea ylhrsgrtgr mgnegivitl vqdnnlrdlk rllrpsnitl
      361 eeiflyggkl qteqptkeda apavnkkyvk tfsgkeqnpe ynkekirkkv knkskkernk
      421 garrk
//
LOCUS       WP_010728540             301 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_010728540
VERSION     WP_010728540.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..301
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31551
     Region          14..298
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mtnllslfls sasqgvlwal laigvyvtfr ildiadltae gsfplgagia avsitngyhp
       61 ltacllgflg gaaaglvsgl lhtklkipal lagiitmtgl ysvtsrvmga pnisllgqpt
      121 ifhwvesfgi tkdnavlivg llfalivvcl lvlflrtetg lairatgdnl amseangint
      181 dnmkiigymi sngcialsgs llaqnngfad lnsgigtivi glasiiiaev llrnqplflr
      241 lltvvlgavi yrfilalvfe lniepsdskl asafvlvicl sfpqiqqkfh lpqkkkggsv
      301 k
//
LOCUS       WP_010728602             272 aa            linear   BCT 01-JAN-2025
DEFINITION  ZIP family metal transporter [Enterococcus faecium].
ACCESSION   WP_010728602
VERSION     WP_010728602.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..272
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28829
     Region          8..270
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mvewllrlep wqqalagtaf tyfmtalgag lvfffkeikk evlnlmlgfa sgvmiaasfw
       61 slldpaitka eengdiawlv vsigfglggv flymadktlp hmhfgpqhea eglpthlkrt
      121 illvfsitlh nipeglavgv afgaaatadn ptaailaavs valgisiqnf pegaavsipl
      181 rqeglsrkka fvygqasgiv epiagvigal lvtkvelllp yalafaagam iyvvveelip
      241 eaqqtlsskr hfavfgvmsg fiimmildva lg
//
LOCUS       WP_010728652             255 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecium].
ACCESSION   WP_010728652
VERSION     WP_010728652.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28487
     Region          1..227
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mekmievkhl sksygsklsp vkaldnisft veegefvgim gpsgagkttl mnilstinlp
       61 tmgsvsiqgk eitkmknsel sdfrrkklgf ifqefnlidt lnakdnillp lavermtkee
      121 mekrvrhvaq llnieellkr ypdelsvgqr qriavaralv vqpqvifade ptgsldsksa
      181 tellnylktm nqkekatill vthdpytasy cdrilfikdg vifsevvrrg trreffekvi
      241 dmqatigggg kmnav
//
LOCUS       WP_010728615            1049 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Enterococcus faecium].
ACCESSION   WP_010728615
VERSION     WP_010728615.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1049)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1049)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1049)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1049)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..1049
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=121145
     Region          8..943
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mkishreeae veeqlirvlg eghnqwtyrp dlkseedlwv nlrqkiisnn qaelndsplt
       61 dkefetikte lllrtktpfd aakwlkgeng maritiered sqlgsvslil ysnqdigggi
      121 styevvhqia krgrnieard rrfdvtllin glpvvqielk qvtakdgfyq afnqikkyae
      181 egmfrnnifs tlqlfvvsne qttryfanal pkdlhpkflf swrtkdnekv enlyefckqv
      241 lnipdahrli adytivsedq dnktlmvlhp yqvhaiqalf iaankhqsgy vwhatgsgkt
      301 ltsfvstkll arksgidrti mlvdrkdldn qttaeftkfa sefntgissg nakanslivg
      361 tgsakelset lladananvv iittrqklda alkyakkqee kkgtnrfqkl mgqhivfvvd
      421 echralsaen meeikkmfpk stwfgftgtp ifpenrkqak gqlartthdq ygevlhtyti
      481 knaledgsvl gfqvehentv eptslenkiy rklkevetya eyspeqinrm idqmepvkke
      541 syldptvfea dehiqkvihk mfrpdnaytk fdfrngrptk sailttssid makkyyraik
      601 emtkepdwlt kefpnqpire grtmedpdfp riaityslee nsrdssvqqe emqkiieeyn
      661 qyydtswsla dieryngdin nrlarkraef kqfgkqidlv ivvdrlltgf daptiqtlfv
      721 drnleyagli qafsrtnrty pekkkglivt frkpatmekn vedatklyse akeesgliyp
      781 syqeskkrfk qaygklkevs smesidehtp leirieyvka fqelnrayes lvtyddyndd
      841 mvksptlnnq iqlleeqigv yetvkgslie eepekegedf stiefysent tklydidsty
      901 idqllgtyaa nssdareeie kalaklnkte gvkevyrqil nafdvgtlds nedifvikrr
      961 yftqasddli hafsnewfvs ekelhasnlq ympgedpipn rkaiinskdy egykakhpea
     1021 kpfkytqemk rawrkmldde lvplenelr
//
LOCUS       WP_010728654             574 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Enterococcus faecium].
ACCESSION   WP_010728654
VERSION     WP_010728654.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..574
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=66013
     Region          <85..197
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkkklltlfl vmsfsivlsv yyntiifseq inyreeqyni ekekalkvgy seeqfkqime
       61 iptnlsnens etrivnytmt snqtkvinka meqigkpyew gasgptsfdc gglvkyvykq
      121 avnielpmgt tnqeqygtev slnslkpgdl lfygnrgaty hvgiykgngv mihapqpget
      181 vkevniqyfy psfakrilpd epdypyidyn kmvtvtkaws iwndlqfshe ikkaiigdny
      241 kigkvytnpe nnnkygeilv snkvygyinf davkeltsvq inryltskds gqpiwgnlec
      301 tiskgqttkd kiyfvkgayn lgdgkylysi ykdqdssewl gylkahvsla ytsieeinkn
      361 vtvtknwsiw nnlqrekeie kpqigsvfsa rlkltnvsnn avyyklyksg kfygyinaea
      421 vkdltttkln kyvtfsvnne dfwssldvny skgktergrv fyisisynta dnqpiysvyt
      481 detctewrgy ykgnnfedtq itmlenksvk vtksgytvwg dlnfwtksgi sntgdiyttd
      541 rkfynftnna yyyelkkdgk vygyinseaa vemn
//
LOCUS       WP_010728769             640 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus faecium].
ACCESSION   WP_010728769
VERSION     WP_010728769.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..640
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=75010
     Region          8..637
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnqrqqsliy qlsennnyit tkklaehfhv sertihsdln tietwlrdkh lplmferkkg
       61 tgillnglph ereqlkraln eetqtemdkk qlrqllifhl lvakdgfsle elseklyvgk
      121 ctirkeltel qsffeyhhlq lvsktklgtf lkgdeqekrq llvktlrnmq kedpqspslk
      181 effakdtlkv iqhtlqdvfy enhleqpngl asveihiyfm lermkqyqkv klskdenevv
      241 ehtqaqklss qilarlatiy piefspdein ylalrianlf tnsqaatrfq kessaladhl
      301 veqveqflgy slkedqllkq nlrshlssty frlhyglqis npltknvfst ytqlflvlql
      361 iledyfeken fyvpqeetay ltihfqaaie rhkhqksrry qtvlvseysk amatflearl
      421 nrelpeltim dlveykpelk rqdfpsvdfi latlpfkhis ipvieispmi tetdlayltk
      481 ymlehvpikk kktfdlasft hpflifpqle rtdpadilnf mgnvlvehhy vepefidsvl
      541 erdshsstrv apfvtiphgn plyvkhsmis iatmkepvlw hgeqirivll laikkndlkh
      601 aefkkifsvi hylekqpeqm aqlmqsnhpl eiltllssye
//
LOCUS       WP_010728781             335 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Enterococcus faecium].
ACCESSION   WP_010728781
VERSION     WP_010728781.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..335
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36836
     Region          <1..335
                     /region_name="trifunc_aldol"
                     /note="KHG/KDPG aldolase/sugar kinase fusion protein;
                     NF041633"
                     /db_xref="CDD:469516"
ORIGIN      
        1 mgkvvtlgei mlrlsteqgt ridsskrfaa hygggeanva islanyghea ifatkvpdna
       61 lgkavkkhlq cygvdtkqvl sggprlgtyy metgsgeraa sviydragss faemdhlews
      121 leelfqgidi fhvsgitpal skkwqkmtkq vieaakrdgc lisfdinyrg klwtqqease
      181 vihqllplvd icsagkmdal yllgiekape aeeqpliyyy qkmqekfpni qvfystkrtv
      241 hsasenelkg tlwmnheyve sqvhritpiv drvgggdafa ggvlhgilsn mspqeiidfa
      301 taasalkhti hgdcnqfsqe evaqflacgs gkiir
//
LOCUS       WP_010728790             536 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_010728790
VERSION     WP_010728790.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..536
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58949
     Region          1..533
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 mtdkfsrwst lfsqnlsrdw kkiliwlvgv tafsggfvpa feeltsgqgl aglyetlqnp
       61 amiamvgptp asnaaeytlg amyanemllf cslfaavisv lhvvsqtrkk eelglielir
      121 sfrvgrqans laviaesili nlllaisisc tmiffqadsi taegawlfgl svgsmgilgs
      181 avalfaaqlm pssassngls laflgglyll raitdvadss lsmwnplgws yltypfttnn
      241 wipllylllf sliliissfv leehrdlntg yiperegkpy akrsllslrg llfylnkgmt
      301 iswlitfglm gaaygaiygn mqqflesndl mkqmfiqsgv sieknftsti mvvliclaai
      361 lpiasinrlf teethgrmnq lfatkisrnq lywtnmllai lfailailis sgalglsala
      421 smkdakdmdl lmflkagfnf lpavlvfigi sgflfgwlpr mgklayiyla ysfalnyfgg
      481 ildlpewfsk tavpswvprm pndsfdlsvf ltlscislal fvlgsigyrr rdlleg
//
LOCUS       WP_010728839             644 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Enterococcus].
ACCESSION   WP_010728839
VERSION     WP_010728839.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..644
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73699
     Region          6..533
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          569..631
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 millqanqia rhfgaevlfe nihleistga rvalvgrnga gkstllkiia gieapgegki
       61 aknktatlgy laqdtgldsn etvwnemlka feqvrqmeer mreleifise gtpdtpayts
      121 ylkeydrlqh dfsdrngygy eneirsvlhg fkfdssfydq kidtlsggqr trlalarmll
      181 qhpdililde ptnhldietl swlenylqsy tgallivshd ryfldkvvne vyelsrrkmr
      241 hykgnyskyl dlkaeqlase wkayekqqte ihkledfvar nlvrasttkr aqsrrktlek
      301 mdrldrpqgn ekqanflfsi ekpsgnvvlq iedaaigyds vtlsepinld irrqeaialv
      361 gpngigkstl lksiihqipf irgketlgtn vtigyydqgq adlhtnktil aelwdehptt
      421 pekeirsalg aflfsgedve kpipllsgge karvalakla mnkenflild eptnhldidn
      481 kevlenalid ydgtllfvsh dryfinriat kvvelsengs kvylgdydyy lekkqeeeei
      541 aellaqdepe sapaptnksd yyqskeqqkl irslqrkitq veeemaride widqleqemv
      601 apenledhvk lnelnqdlea arqdqetklt eweelslele eyen
//
LOCUS       WP_010728873             564 aa            linear   BCT 01-JAN-2025
DEFINITION  class I mannose-6-phosphate isomerase [Enterococcus faecium].
ACCESSION   WP_010728873
VERSION     WP_010728873.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Jensen,S.O. and Reeves,P.R.
  TITLE     Domain organisation in phosphomannose isomerases (types I and II)
  JOURNAL   Biochim Biophys Acta 1382 (1), 5-7 (1998)
   PUBMED   9507048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..564
                     /product="class I mannose-6-phosphate isomerase"
                     /EC_number="5.3.1.8"
                     /GO_function="GO:0004476 - mannose-6-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009298 - GDP-mannose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64933
     Region          217..564
                     /region_name="ManA"
                     /note="Mannose-6-phosphate isomerase, class I
                     [Carbohydrate transport and metabolism]; COG1482"
                     /db_xref="CDD:441091"
ORIGIN      
        1 myekrpriil keqistftgy tkiinellkd ektkkialec ypgidsekva heiralkmed
       61 lfitttnqfy qssneikekl tevltddrvf grltdatfld flakeknesl nqadrvllig
      121 vgaaelidad ivvyanltkr niqlklkaga enwqadnaqe eflkkvkray yfewpaader
      181 kklvlpssqy lidlneentp kmiktkdyyn alrhfsnqpf rlvpyfepgi wggkwmqkkf
      241 dvgkeevnla wcfdgvpeen svifeigtvt fevpgndlvl fypvsilgek vfgrfgsdfp
      301 irfdyldtma ggnlslqvhp tldyayrkfg lkytqdesyy imdceedayi ylglkeevgt
      361 pdfiqalees ritgrldvek yinkikvkkh dhflipagti hcsgencvvl eisatpnrft
      421 fklwdwervd ldgiprpihi ehgkqvines mktnrvfsel vnqvvdltit enihiertgl
      481 hqlepiethr ltfcvpieqt tegsvnmlnl vegegivies taetfeplki nygetfiipe
      541 niknyvirpi vdketcivmk afik
//
LOCUS       WP_010728874             228 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010728874
VERSION     WP_010728874.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..228
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26694
     Region          2..227
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtngipyylq iaddmrsniq iekwkegeki ptelqlcdiy hvsritvrka idelvkdnll
       61 drkrakgtfv kkldaklsdh ftlvksftee mkevgidivt qtvnvlitha dkrlaqyldv
      121 dlgeklivlk rlrgdkkksi gyfityfkye dffslntrdy ygsfyaylkq hdiivtnkke
      181 iiesihptqe iayflkvsqn tpilkrtrft sdltnsfkey tecfyigk
//
LOCUS       WP_010728895             301 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010728895
VERSION     WP_010728895.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34476
     Region          16..97
                     /region_name="cupin_MmsR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MmsR, N-terminal cupin domain; cd06986"
                     /db_xref="CDD:380391"
     Region          <167..273
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 meqsiflkke hqqvekelyf dfcgfsktmp fhsfgpairn dyilhvvmeg kgsyhvknqq
       61 fqlkkgdlfl irpgdstfyl sdgedpwmyc wlsfggsaae eiirqslfre dqytmvssdi
      121 qkyidiilec mkdteetlen elqltaltyc flsvllkdgg kvsggvqkvh sslavetvky
      181 ieahyaekls veeiaqhlav nrnhlsrvfk nhmgtsikey ligvrinrga fllsltdesv
      241 esiayqvgfn slvvfsrmfk kstgetatny rkrmknenfk nialdtlkkq lekqtavswt
      301 t
//
LOCUS       WP_010728968             167 aa            linear   BCT 01-JAN-2025
DEFINITION  VanZ family protein [Enterococcus faecium].
ACCESSION   WP_010728968
VERSION     WP_010728968.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..167
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=19222
     Region          40..125
                     /region_name="VanZ"
                     /note="Glycopeptide antibiotics resistance protein
                     [Defense mechanisms]; COG4767"
                     /db_xref="CDD:443799"
ORIGIN      
        1 mryvskfllg iylffllwli lfklsfnlpq fltysysnvn lvpfstfsfe nttvlretty
       61 nlivffpfgv llnvnfkrls fskkigiifl vsflaeliqf lfgigvadit dlitnttggl
      121 iglwayqlln khlstnkldr laiilgyilf lflivaflfl trtvrlq
//
LOCUS       WP_010728969             258 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Enterococcus faecium].
ACCESSION   WP_010728969
VERSION     WP_010728969.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..258
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28992
     Region          1..243
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mnihhirnat aildyggkkf lidpmlaekg tlppfiskgp fpsprkdqmn plvdlpmpve
       61 diingidavi vthlhldhwd diakevlpke iklfvqdend aneirlygfk nvevlredtv
      121 fesiqlvktk gkhgrgeiln yvgnvcgivf khstektlyf tgdtvwyeav kqtidqykpe
      181 iivanagdnh flvgeslimg kddlcelhka ipdstiiavh meavnhwgls reelksfnke
      241 kgisekvlvp edgdnifi
//
LOCUS       WP_010728970             135 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010728970
VERSION     WP_010728970.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..135
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15417
     Region          1..134
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mldqtdinii eelsknsrit mkelgekvhl tgpavsarvt kleesgvien ytvklnmekl
       61 gfsihaflii itqnlnhkpy lsfiknhekf lirnykisgg scyllecrft skksmnsfle
      121 qlneyanykl sivid
//
LOCUS       WP_010729022             193 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010729022
VERSION     WP_010729022.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22238
     Region          1..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mktkekilea tkdliykkgy hetsirdila asdtgkgqfy yyfsskkevc lavihahmdv
       61 wqtelfedil nagkqpeeal eemldwifad hetqityhgc pvgnliiels tvdeeyrlll
      121 lelvnqwvky tkqnilalse eklsdeeayr qakaliaeiq gsilllkvtq dlsllrqnfq
      181 likerlltsq kvl
//
LOCUS       WP_010728992             457 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecium].
ACCESSION   WP_010728992
VERSION     WP_010728992.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..457
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=53552
     Region          1..376
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mrvacydrts vyeeakisnd aqydavkeyv lekyeqvpqr fsdkgesggk adrpafrqlr
       61 awvcaseeeg viyvwrydrl arqakialef ielcqqhqvq vysiseplpa sfshastnkl
      121 fvqllftfae qqrnviienv raglaykkqq rqylssavpy gyrlvngkiq qeaheakvvc
      181 hifqlyltkk ygykklcqql tqqkfffrer pfqpyhiysi lknplyygei kggslgkylg
      241 tfepilskat flqvqeirqs rctakkdtyp yllrqkikcp fcgrhlssky qwntkktktl
      301 hyyhctdqsc qgiflraerv esevlekiqa ffqhegvyqa liaqltqqla ekrkdekrkv
      361 iqqkkqeaqw ikafeegncs leelkqqlqa lqkpmstssf fslqqceakv kewlqlkdls
      421 srqllcdhvc rievtkektv cgiyfrqmtq nilegne
//
LOCUS       WP_010729078             255 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecium].
ACCESSION   WP_010729078
VERSION     WP_010729078.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28429
     Region          1..227
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mekmievkhl sksygsklsp vkaldnisft veegefvgim gpsgagkttl mnilstinlp
       61 tmgsvsiqgk eitkmknsel sdfrrkklgf ifqefnlidt lnakdnillp lavermakee
      121 mekrvrhvaq llnieellkr ypdelsvgqr qriaaaralv vqpqvifade ptgsldsksa
      181 tellnylktm nqkekatill vthdpytasy cdrilfikdg vifsevvrrg trreffekvi
      241 dmqatigggg kmnav
//
LOCUS       WP_010729143             311 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus faecium].
ACCESSION   WP_010729143
VERSION     WP_010729143.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..311
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34923
     Region          62..309
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mklwmkillg valalivalv fagnyfynya vvpsekdfld edtpgttqts ketdahkwfs
       61 skenrsdwti tskdglklsa iylpaetkse ktalvahgym gnaetmtnya kmfhdmgynv
      121 lvpdarghgk segdyigfgw perkdyvqwi nkvlenngks qeivlygvsm gaatvmmtsg
      181 eklpdnvkai iedcgyssvh delayqlddm fslpafplmq vtslvtkvra gyffgeanav
      241 eqlkknqcpm lfihgdedtf vpfemldkvy ratkgpkeky vvkgaehaea yktdpekyqq
      301 vvqqflsqyv h
//
LOCUS       WP_010729547             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010729547
VERSION     WP_010729547.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22176
     Region          1..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mktkekilea tkdliykkgy hetsirdila asdtgkgqfy yyfsskkevc lavihahmdv
       61 wqtelfedil nagkqpeeal eemldwifad hetqityhgc pvgnliiels tvdeeyrlll
      121 lelvnqwvky tkqnilalse eklsdeeadr qakaliaeiq gsilllkvtq dlsllrqnfq
      181 lvkerlltsq kvl
//
LOCUS       WP_010729578             433 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Enterococcus faecium].
ACCESSION   WP_010729578
VERSION     WP_010729578.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..433
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48729
     Region          1..433
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mvinfiilfl miaitsffva sefalvkirr srleqleken vknaklalhv thhldnylsa
       61 sqlgitltgl iigwvgegsv aallepvigk lpfssaisst isvalgfilv tyidvvigel
      121 lpksysivnt ekvvlfvvkp lhyfykvmfp fiwvlnhsaa glgkllgvrl vsegeetlsr
      181 eeltlvalns yekgeltkee yyylenvfef ddtlakdiqv drtsmqvfea setvkeaika
      241 sieqghtryp vileskdnvl gyvtlpdlik qsykddqltv eqlieepivt tetipikkll
      301 timrkkgkhi ailkdeyggt sglvtiedil eeivgeirde tdldealiae qsdgsyiisg
      361 kltlddfqry fhveipefee tnfttlagfa ssrykeikag tiieiasfrf tvleyqhahi
      421 dyfkvester kte
//
LOCUS       WP_010729700             458 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Enterococcus].
ACCESSION   WP_010729700
VERSION     WP_010729700.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..458
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50631
     Region          1..457
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 merkfgirdk igymfgdfgn dftfifassf lmifytkvlg isgaavgtlf lvarfidavt
       61 dvtmgrivdr skatkqgkfk pwilrmsgpv alasflmyqt smisasmsvk vvymyvtyil
      121 wgsifytsin ipygsmasai tsiteertml stfrnvgatl aslvigvltp lfiytrddsg
      181 aqivrggstf tivagifsic alicylicyk lttervridq sqykvsllks lkglvknral
      241 lsiigaaifl llaqllimsm nnyvfpdyyn daqgivlmnf inpilvlivv spltlflskk
      301 ygkkelasvg mffsaivyli lflikasnmy vflilssvgy mglgvfntvi wanitdvidd
      361 qevksdqred gtvyavysfa rkigqalagg vggwtlsiig ydslanvqtg dvleklynas
      421 tlipsicfli vglilfflyp lskdkvlenc ellkqkhk
//
LOCUS       WP_010729731             441 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus faecium].
ACCESSION   WP_010729731
VERSION     WP_010729731.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..441
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=50302
     Region          13..369
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(16..17,20..21,57,60,118..119,179)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(116,119,208..214,243,270..275,302,327..331,333)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mmdyskepvn dyflidmksf yasveciern ldplttelvv msrsdntgsg lilasspeak
       61 krygitnvsr prdlpqpfpk tlhvvpprmn lyikrnmqvn nifrryvade dlliysides
      121 ilkvtkslnl fttegtrsqr rkklaqmiqe rikeelglia tvgvgdnpll aklaldneak
      181 hnegfiaewt yenvpekvwn ipemtdfwgi gsrmkkrlnq mgimsirdla nwnpytiksr
      241 lgviglqlyf hangidrtdi aippeptkek sygnsqvlpr dytrrneiel vvkemaeqva
      301 irirqhnckt gcvhldigts iletrpgfsh qmkipitdnt kelqnyclfl fdkyyegqev
      361 rhvgityskl vytdslqldl fsdpqkqine enldkiidki rqkygftsiv hassmlesar
      421 sitrstlvgg haggnggikn d
//
LOCUS       WP_010730291             591 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecium].
ACCESSION   WP_010730291
VERSION     WP_010730291.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..591
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=68327
     Region          27..431
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mktnnveiik adslvrrrgv nverhlkrva aycrvssdse dqknsyesqv rhykdyisqr
       61 sdweladiya degisgtqvg krqdfqrlin dcvngeidyi vtkaiarfar ntldtlkyvr
      121 mlkdmqigvy feeenidtlt mdgellltil ssvaqqeven tsahvkkglk mkmqrgelig
      181 fqgclgydyd vetkqlsink keakivryif erylegiggk viareldelg yksprgldhw
      241 ndttvlgiik nekykgdilm gktftvdpis krrlsnfgee dkyyikdnhe piiskedfek
      301 aqeirlrrag nkktvanvng kreryskmya fssmlecgfc gsllsrrswh crsdyrkvvw
      361 hcvtsikkgk kyckhskgle elaiegafme ayrqlyhsne nlmtdlleti eselndnsln
      421 kelkritnkl rtllkkeenl vnlklegkis dtiynekyne issekvflae ekvniettlk
      481 seidvkkrlt efkhllssqk mltefdravf esivekiivg gvnsdgeidp amltiifktg
      541 etqnkdgnqf kskrknakle tdklcpqnsd edkkmysqgp dntyrisrfi r
//
LOCUS       WP_010730467             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010730467
VERSION     WP_010730467.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..249
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28414
     Region          3..249
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnhklseteq ylwnfiehli leipnysivk lseqanvsta tivrtmkkkg yegftsfkhh
       61 lkegenknin fsfldkvdkg irrailkneq evvrtinmle igniedaiqr ikfadrvfvf
      121 argfsemigq emlvklqltg kncqmhtdpe iiksisrklt kkdsvifvsl ngetkelvta
      181 akncydaeig silvtanhss tlkdyceinl vgfksegsyf pdyevrsrlp lqiiarilld
      241 ayvlrmgen
//
LOCUS       WP_010730473             239 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Enterococcus faecium].
ACCESSION   WP_010730473
VERSION     WP_010730473.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..239
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=27976
     Region          32..239
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mrccccskdi vqnltfseii gvskyrlpqt csvcraqfhl letrgcsgcq kpihfnlest
       61 kkkvksipvy csdcqewkkk yptydfqhra ffvydenmka wlnqykfmgd irlagtfayk
      121 wtqikkeypt yiycpiplse krrtergfnq vsemlkaari pfqmllkrek hllaqakntr
      181 krrlempqpf elavtfskiq nkkiliiddv yttgqtlfha adclqvaqpk iirtislar
//
LOCUS       WP_010730514             574 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Enterococcus].
ACCESSION   WP_010730514
VERSION     WP_010730514.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 574)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..574
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=66216
     Region          181..571
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mnkfrilfsk gtllnrllrk yavimigvtm tatvifsiht weqnqkqaen mtsdavqsts
       61 rmlndkttls riiknqlvgn sekienvtty ltkpidqylm yvyeqqnstd elvsfpnqik
      121 dlyanyeels aiyivlnqlp eyyessrenk ggkikkgtpk lldafyiklp itqggaesgs
      181 ifigfqkkel dmilenltsf nglslymisg ttnrlytfhd nkiaketfer qemiiteslk
      241 knsqlpiddl eknnfvqhqe lsddyrilav ldkksvkiet gknlapliig iiildnilli
      301 flyktfkrys qqvsivmqam dqtaagnlet riditnteye lkelsigine mldsinqfve
      361 diykleikqq dahmralqaq inphflyntl eyirmyaise gseeladvvy afsallrnnt
      421 nqektitlke eldfcekyvy lyqmrypnrv ayhfmidpdl ekievpkfvi qplvenyfkh
      481 gidftrfdna lsvkvlqegk rvriiikdng kgmtekrlkq ieeklshpkv elhgsiglqn
      541 vnerlrasfg ssyymslenn etggltvsit fkeg
//
LOCUS       WP_010730591             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ZIP family metal transporter [Enterococcus].
ACCESSION   WP_010730591
VERSION     WP_010730591.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..272
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28780
     Region          8..270
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mvewllrlep wqqalagtaf tyfmtalgag lvfffkeikk evlnlmlgfa sgvmiaasfw
       61 slldpaitka eengdiawlv vsigfglggv flymadktlp hmhfgpqhea eglpthlkrt
      121 illvfsitlh nipeglavgv afgaaatadn ptaailaavs valgigiqnf pegaavsipl
      181 rqeglsrkka fvygqasgiv epiagvigal lvtkvelllp yalafaagam iyvvveelip
      241 eaqqtlsskh hfavfgvmsg fiimmildva lg
//
LOCUS       WP_010730624             271 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Enterococcus faecium].
ACCESSION   WP_010730624
VERSION     WP_010730624.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..271
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29508
     Region          1..239
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 migliyfvvi vlantvgais gmgggvlikp ildligahsi agisfystva vftmsivstv
       61 rqvssgksln wqivgwvsgg avvggiagni vfevflrlfe nekhvqliqi fltvltlvfa
      121 ffytkhhqpk fhltswiwyl icggilgfla sflgigggpi nvsllmlmfa lpikeatlys
      181 lstiffsqla klvtialtsg fmrfdlsmlf yiipaavigg lwgakfsril spkkvtfifq
      241 vivlvvllvn cynafvilqt lgesrltrer q
//
LOCUS       WP_010730715             374 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Enterococcus faecalis].
ACCESSION   WP_010730715
VERSION     WP_010730715.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..374
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=42059
     Region          86..316
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mwkisnendi fkkrkplppk kseesqpelt pwqkqnqeyl kkqaeeaask geneqaevti
       61 tlqeqsqeep qqhlpqetve eeehfadrlp nvkktrnkrl yrrlafiltc lgtailvaly
      121 fvsplsrlse vtvsgnksve sqaiiqqskl etgsglweqy snrnyfsani qkkfpiikka
      181 niklnginsf kidiqeyqiv alaatkggyh pilengktla ettkaaesgk pifenfkedk
      241 lipelmasyn klpqeikqgi seikyapskt nkdlinvymn dgnrvivnis dlsekmayys
      301 qvaeqmdkpg ivdmevgifs ypyekeseet gsevsedsav enkevvdpna gaatdeanng
      361 tptngenqev qqae
//
LOCUS       WP_010730760             244 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase family protein [Enterococcus faecalis].
ACCESSION   WP_010730760
VERSION     WP_010730760.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10065661
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..244
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=27932
     Region          6..219
                     /region_name="MPP_PPP_family"
                     /note="phosphoprotein phosphatases of the
                     metallophosphatase superfamily, metallophosphatase domain;
                     cd00144"
                     /db_xref="CDD:277316"
     Site            order(10,12,37,41,67..68,143,163,183)
                     /site_type="active"
                     /db_xref="CDD:277316"
     Site            order(10,12,37,67,143,183)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277316"
ORIGIN      
        1 mkpyvyvisd ihgqadlfda lltdydpveh qlvligdlnd rgphskacfl kgkelveqhd
       61 avylrgnhee yflqflqnpe dwfagyvrng gketiesllh pgataeyspt emalmirsry
      121 pelvdfltkr plyfewqhyl fvhagvdltm edwrqtapkd flwiretfhq gknntgktiv
      181 fghtitpmlh gdmqttdlwq sdgkigidgg aifggsvhgv ifnekgivqd ieyqkrtpaw
      241 qpef
//
LOCUS       WP_010730826             807 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK [Enterococcus faecalis].
ACCESSION   WP_010730826
VERSION     WP_010730826.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..807
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=88939
     Region          305..799
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 maqkrstnkk ksttkkktkk qqqqqerlny mflglifilf gvfglfrlgf lgtllanclr
       61 lvvgntfpfa aillilygll vmiygkdfpl krgrpifgav liyisvllff hafmfrnvsg
      121 sqpdilgntw eflqsdlkan qvtqnvgggm igallyqgty flvaqfgsyl iatllllagi
      181 flmsmwdfqq ivdhfqsiqd rlshvsaksq arqeekeakr aakkeakave rqakieaaaq
      241 qklqererme qaaaerltkt pvethqpmve epaaptpvqi dsfqqqnqam pvppiaatkp
      301 qreqeeeatd eagvlefeis eeaedrdyql pptdlldtiq atdqsgeyek ieknigvleq
      361 tfksfgvdak vvkaslgpsv tkfevqpavg vkvskivnlt ddialalaak dvrmeapipg
      421 ksligievpn saistvsfrd iveaqpshpd kllevplgrd isgmvqtadl skmphlliag
      481 stgsgksvai ngiitgilmq akphevklmm idpkmvelnv yngiphlltp vvtnprkaaq
      541 alqkvvqeme fryekfaatg vrnitgynql iqqknaedge nrpilpfivv ivdeladlmm
      601 vasnevedai irlaqmaraa gihmilatqr psvdvitgii kanvpsrmaf avssgtdsrt
      661 iidtngaekl lgrgdmlflp mgenkpiriq gafisdqeve rvvafvtdqq eaeyqesmmp
      721 tdepttsggg eapqdelfee vknlvvemqt asisllqrrf rigynraarl vdeleahgvi
      781 gpsegskprk vflqaeseea atetpeq
//
LOCUS       WP_010730839             439 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            faecalis].
ACCESSION   WP_010730839
VERSION     WP_010730839.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..439
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46611
     Region          23..429
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 metkqlntpq qtetpngkaa vlglqhllam yagavavpll igtglnfdsq qmtylisidi
       61 fmcgvatllq ltvnkffgig lpvvlgcaiq avaplimigt nkgvgaiygs iiasgifvvl
      121 iagffskikr lfpplvtgtv itvidltlip vavekmgggl atdksfgdpk nlllafvtia
      181 liivvqvwgr gfiksiavli glvggtilae flglvdlspv gqatwfhfpq pfyfgkptfd
      241 lssivlmiii sivsmvestg vyfalgditg kkigeddlrr gyhaeglavi lggifntfpy
      301 tgfsqnvglv qlsgiktrrp iyfsafflii lgllpkigam aqiipepvlg ggmlvmfgmv
      361 avqgmrmlsk vdysndknll iiaisigfgl gfnimptlfn kvpetvsmft gngivmssit
      421 aiilnllfng lketsesne
//
LOCUS       WP_010730940             104 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Enterococcus faecium].
ACCESSION   WP_010730940
VERSION     WP_010730940.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..104
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11492
     Region          7..96
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mnllfqsiks itvpelkekl lenpalldvr apaeyrgghi kgaknvplqs inrydgdkek
       61 tvyvicqsgm rskqaakelk ksgydvvnvr ggmnqwfdrt vggk
//
LOCUS       WP_010730970             425 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus faecium].
ACCESSION   WP_010730970
VERSION     WP_010730970.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..425
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=48151
     Region          1..352
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(1,4..5,41,44,102..103,163)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(100,103,192..198,227,254..259,286,311..315,317)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mksfyasvec iernldpmtt plivmsrsdn tgsgltlass ptakkkyhit nvsratdlpy
       61 plpkelhivp prmnlyikkn mevnqifrky vadedlliys idesilkvtk slnlftssgt
      121 rserrrelak iikdeiqket gliatvgigd npllaklald neaksskefi aewtyetvpe
      181 kiwkinemtd fwgigsrmkk rlnhmgimsi edlanwnpyt iksqlgvigl qlyfhtngid
      241 rtdiaippep tkeksygnsq vlpkdytrre evelvvkema eqvairirqh ncktgcvrla
      301 igtsileeks gfshqmkipi tdntkelqny clflfnkfye gqevrhigvt ysrlvytdsl
      361 qldlfsdprk kiaeenldri idkirqkygf taiihassml egarsitrst ligghagglg
      421 glhnd
//
LOCUS       WP_010731072             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Enterococcus faecium].
ACCESSION   WP_010731072
VERSION     WP_010731072.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..238
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24560
     Region          3..238
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mnsdmtqimg efigtlilvl lgdgvcaavn lnkskaqasg wiviafgwgl avtmavyisg
       61 fmgpahlnpa vslamamtga iswnlvvpfi iaqvlgafag silvwlsylp hwnatkdesa
      121 ilgtfatgpa irnypanvit eligtfvlvl gllafgqnef apgtnvfavg glilaiglsl
      181 ggptgyainp ardfgprlah avlpiankgt sdwayswvpi agpmigaiia vgvyslmv
//
LOCUS       WP_010731082             764 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus faecium].
ACCESSION   WP_010731082
VERSION     WP_010731082.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..764
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88126
     Region          4..757
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mkqikrlfai dpwkisttql dkknlrlqes ltsigngymg mrgnfeetys gdhhqgtyla
       61 gvwypdktrv gwwkngypey fgkvinalnf iaidisindq lidlaslepe dfyweldmkn
      121 gvlsrtftit tstnkvrisf erflsivkke sayiyltiem legsgtvklv skldgnvqne
      181 dsnydehfwn eidrgtieei gylttktipn nfgieqftvt vamrhfvngk svipdyhedt
      241 lalhgclsae lsqgetwsve keiivltsrd ipeaqqaeka vseltnqtnn yiqakeeqta
      301 awaerwklad vviegdeeaq qgirfnlfql fstyygeder lnigpkgftg ekyggatywd
      361 teayavplyl alakpevtkn llkyrhnqlp qaihnaqqqg lkgalypmvt ftgvechnew
      421 eitfeeihrn gaiayaiyny tnytgdteyl kneglevlae iarfwadrvh fskrankymi
      481 hgvtgpneye nninnnwytn tiaawvlryt renyltyqke aaitiseeel akwkdiaenm
      541 yfpvdeelgi fvqhdtfldk dlmpvsdipt sdlplnqhws wdkilrscfi kqadvlqgiy
      601 ffndtftkee kqknfdfyep mtvhesslsp sihsilaael gmeskavemy qrtarldldn
      661 ynndtedglh itsmtgswls ivqgfaqmkt ahdqlrfapf lpktwkaysf hinyrgrllf
      721 isvtdeqvtf ellegsplei yvyeqsysla drleitlrke eanv
//
LOCUS       WP_010731098             706 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus faecium].
ACCESSION   WP_010731098
VERSION     WP_010731098.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..706
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80248
     Region          16..638
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkciktpafl nkrlgffsll vvllwlktif aylvdfhlgi esgiqyfilf inpiattlll
       61 lgialyirrp rvayitmmvi yflltllvfs nvtyyreftd fitintilga gkvasglges
      121 airlfrpydv iywidfiilt vlliakkikl dprpirarma faistlavmi fsgnlfmaea
      181 drpelltrtf srdylvkylg lnafmvydgv qtyqtnqvra easpndmkev enyvkehyaa
      241 pnddlfglar gknviyihle sfqqflidyk ltdenglqhe vtpfinslyh snstfsfdnf
      301 fhqvkagkts daetlmensl fglnqgslft qlggkntfqa apdilsqtqg ytsavfhgna
      361 gtfwnrnety knlgydyffd ssyydvnddn sfqyglhdkp ffqqsvqyle rlqqpfyskf
      421 iavsnhypys kftndeagfp lantndetin gyfatanyld tavqeffnyl kesglydnsv
      481 ivlygdhygv snsrnknlge lvgktsstwt nydnaqmqrv pymihipgqt qgginhtygg
      541 qvdalptllh llgvdtknyi qlgqdlfskd heqlvsfrdg dfvtpkytyy ggtiysnetg
      601 eaitepteev qneidslkek vdkqlavsdq inngdllrfy tnsgldpidt sdydykngle
      661 klkeaekslg dkstsvfseh ngqstvdlyk tqtyqelhgt ttssse
//
LOCUS       WP_010731147             379 aa            linear   BCT 01-JAN-2025
DEFINITION  MraY family glycosyltransferase [Enterococcus faecium].
ACCESSION   WP_010731147
VERSION     WP_010731147.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..379
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=42324
     Region          41..290
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            94..95
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            216..219
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133463"
     Site            order(266,280..283)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 mlvsfsmvir ffltillsli ltpvfkiisv qtgmvdkpne rrinkvpmps agglpifisf
       61 vistlflfrk iipqsyivpi liaslviivt gvlddkyelt pkqksigili asliiyfvad
      121 iridsftlpf igyiqlgwls fpvtifwifg itnavnlidg ldglaagisl iglitigiig
      181 yfflhastvy ipvvifclva siigffpynf ypakiylgdt galflgfmma vlslqglknv
      241 tfvssislli vmgvpvtdtf faiirrkanr vsfstadkkh lhhrlislgf thkgavltiy
      301 amalmfsfta mvmnytgrig tiiliiailf aaillfelig linekhqfil ktlrflgnke
      361 yrtqvkqkyl kkwnrhide
//
LOCUS       WP_010731181             175 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Enterococcus faecium].
ACCESSION   WP_010731181
VERSION     WP_010731181.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..175
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19744
     Region          2..175
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mlyvtrhget twnaqglvcg radvpltekg qmqaqklaek vvdlpvpitk iihsplqrar
       61 dtaqavayrl slpltvderl vemdfgdydg lpskdenfqk arlafavrfp ngesvldvya
      121 rivpllkeci edeenvyllv chnalirvin ayfhpmpneg fftfmvdnte lvsye
//
LOCUS       WP_010731199             395 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Enterococcus faecium].
ACCESSION   WP_010731199
VERSION     WP_010731199.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..395
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=43631
     Region          52..391
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mekklkasnd nridygvilp vfllcligll slyvalshdp nnpavlkgvg mqvvwylvga
       61 aaivvimhln skwiwkltpy lyglglvvmg lllkfydqnl tastgsknwf rfgaftfqpa
      121 elmkiayilm malivtkhnt qvkertmksd fwligklliv tipvlalima qddfgtmlvf
      181 laifggiflm sgiswriiap vvilavvvga gtiflvtteg grdllykvgf ksyqfarids
      241 wldpfhdtsg msyqpaqgll aigtgglfgk gfnvsniyvp vresdmiftv igenfgfigg
      301 afviflyfil iyrmirvcfd tnnefyayia sglimmllfh vfeniganig llpltgiplp
      361 fisqggssil gnmigiglil smryqneapa rssrr
//
LOCUS       WP_010731201             191 aa            linear   BCT 01-JAN-2025
DEFINITION  SOS response-associated peptidase [Enterococcus faecium].
ACCESSION   WP_010731201
VERSION     WP_010731201.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..191
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=22342
     Region          1..>168
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgryffdle sellqnyyre aqtkqpkqaa elaagevfps nlvvtlrkee eniltpeimk
       61 wgftgfkkgq lminaraetv eekktfhqpf lqnrcvfpms gfyewneekd kfifsnkeki
      121 vyiggfyrsh qdekmaesii mttepnrtva pihdrmplvl teeqiepwvt disfarkiit
      181 qqmpelvmek v
//
LOCUS       WP_010731373             465 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus faecium].
ACCESSION   WP_010731373
VERSION     WP_010731373.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..465
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=53028
     Region          20..378
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(23..24,27..28,68,71,129..130,185)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(127,130,214..220,249,275..280,307,328..332,334)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mlgnqnpifd yhkepsrdil cidcksfyas vecvergldp lkaklvvmsy pserqkergs
       61 glilasspaa kkaygisnis rardlpfpyp pdlviapprm ayymqknmei nniyrkyade
      121 nnhhvysvde sfidvtdglk lfnvktafel akiiqtdvyr qtgiyttvgi gdnpllakla
      181 ldnaakhapn mkaewryeni retvwkipni tdfwgigrrt akrlqrlgif svydiahsdy
      241 yklkedmgil gtqlyahswg idrtfigqky kpksrsigns qvlnrdyykr eeieivikem
      301 adqvatrlrr agaktsvisl wigysigyid yegktsfhqq mkidptnssk eiadhllkif
      361 hrkyrnqtvr nigvncsklv yghflqlnlf eepeqqisea kidyvvdtir kkygfksivh
      421 ahsllkggra iarsglvggh aggmsgiegk qedkkknsnd yfhkn
//
LOCUS       WP_010731421             627 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation-translocating P-type ATPase [Bacilli].
ACCESSION   WP_010731421
VERSION     WP_010731421.1
KEYWORDS    RefSeq.
SOURCE      Bacilli
  ORGANISM  Bacilli
            Bacteria; Bacillati; Bacillota.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 627)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   5  (residues 1 to 627)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 627)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11492716
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Bacilli"
                     /db_xref="taxon:91061"
     Protein         1..627
                     /product="cation-translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0043169 - cation binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /calculated_mol_wt=67998
     Region          66..606
                     /region_name="ATPase-IB2_Cd"
                     /note="heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type
                     ATPase; TIGR01512"
                     /db_xref="CDD:273665"
ORIGIN      
        1 misyliksrq gqflaigilf aaagfifgtm nseysrwlfy aaifflgfya sknaivetvr
       61 dkspnvdllm ilaalgavii dfesegaall lifaaaevle dyannkstsa iselmaqvpe
      121 taqvlkenge vvtvptedln vgervvvskg ekipidgiid rksivnesal tgesvpvvke
      181 aedevfagti negdvfyidv tkssdetvfs niirmveeaq srpsriskfi drieskyvis
      241 vlvivpifiv vmyalmdlpf eeafyrgmvf ltvaspcalv asatpatlsa isngakngil
      301 fkggaameal stmdilytdk tgtltygefk vdeysapddv lkeviymeqq sshpiaraiv
      361 tafketdlss vdhnepvsei agsgikkgtv rvgkpsafst fknydrfkqy fqkgntiila
      421 akeeevvgyf slsdqirrqs adavanfqke gikvtlltgd neevtetvae vvgvddykas
      481 mlpedkiayv resqdkeevv gmigdginda palanadigi amgsgssvav essdvvvvkn
      541 dlsklfysyk lskklnkiil qnvifsisvi vtlivlnlfg vlelplavlf hegstilvil
      601 nglrllgskg pkqeervsdp slksvkv
//
LOCUS       WP_010731429             591 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF262 domain-containing protein [Bacilli].
ACCESSION   WP_010731429
VERSION     WP_010731429.1
KEYWORDS    RefSeq.
SOURCE      Bacilli
  ORGANISM  Bacilli
            Bacteria; Bacillati; Bacillota.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Bacilli"
                     /db_xref="taxon:91061"
     Protein         1..591
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=68756
     Region          6..551
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 mirndiqpdl qtieqyfnrk efyipsyqrp yawqvaqceq liediethqe nfdqesqdny
       61 ffgailiaqe sgedhevtli dgqqrtstfm lllkalllki nkesaklsde tlenakliek
      121 lnrlkssiis mlynlnedns fyyrkgdykl qptdikylne siselyaadm ekiligesfe
      181 diagsvtqiy rrqkdnrftn fyknfryfwk ycdeltnfqv aefaehfiky cqvititsfn
      241 tdqainifns lngtgvpltp ievivskata naaerktfes nwqaivnktd hsslnlnllm
      301 thyifvqlsq qhgaitrnpg iraffaknke llkhdveftn slntildnlg dfertelgki
      361 lnqfnsnlkp fvssylyfrp mnqeyltyll rlgaileltd fayanrnfkg flerinlkys
      421 qvdivsdeel ieeikkhist afnkedilqt lmesgvpnsi iflneyvyck qhdqefniyg
      481 nvdiehvmpq sglnrenima dagftepeef heyaeklgnk illeseinrg igdawfrtkk
      541 entitshhgf igsqykiaqa lvgyhkdtwv kddikiatek aahrisdflf e
//
LOCUS       WP_010731433            1049 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type I restriction endonuclease subunit R
            [Enterococcus].
ACCESSION   WP_010731433
VERSION     WP_010731433.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1049)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1049)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1049)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1049)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..1049
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=121062
     Region          8..952
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mkishreeae veeqlirvlg dghnqwtyrp dlkseedlwv nlrqkimsnn qaelndsplt
       61 dkefetikte lllrtktpfd aakwlkgeng maritiered pqlgsvslil ysnqdigggi
      121 styevvhqia krgsnieard rrfdvtllin glpivqielk qvtakdgfyq afnqikkyae
      181 egmfrnnifs tlqlfvvsne qttryfanal pkdlhpkflf swrtkdnekv enlyefckqv
      241 lnipdahrli adytivsedq dnktlmvlhp yqvhaiqalf iaankhqsgy vwhatgsgkt
      301 ltsfvstkll arksgidrti mlvdrkdldn qttteftkfa sefntgissg nakanslivg
      361 tgsakelset lladananvv iittrqklda alkyakkqee kkgtnrfqkl mgqhivfvvd
      421 echralsaen meeikkmfpk stwfgftgtp ifpenrkqak gqlartthdq ygevlhtyti
      481 knaledgsvl gfqvehentv eptslenkiy rklkevetya eyspeqinrm idqmepvkke
      541 syldptvfea dehiqkvihk mfrpdnaytk fdfrngrptk sailttssid makkyyraik
      601 emtkepdwlt kefpnqpire grtmedpdfp riaityslee nsrdssvqqe eiqkiieeyn
      661 qyydtawsla dieryngdin nrlarkraef kqfgkqidlv ivvdrlltgf daptiqtlfv
      721 drnleyagli qafsrtnrty pdktkglivt frkpatmekn vedatklyse akeesgliyp
      781 syqeskkrfk qaygklkevs smesidehtp leirieyvka fqelnrayes lvtyddyndd
      841 mvqsstlnnq iqlleeqigv yetvkgslie eepekegedf stiefysent tklydidsty
      901 idqllgtyaa nssdareeie kalvklnkte gvkevyrqil nafdvgtlds nedifvikrr
      961 yftqasddli hafsnewfvs ekelhasnlq ympgedpipn mkaiinskdy egykakhpea
     1021 kpfkypqemk rawrkmldde liplenelr
//
LOCUS       WP_010731480             257 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010731480
VERSION     WP_010731480.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..257
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29079
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlkterqrsi lamcdrygti tvkfiqevln vsdmtirrdl eelaqkkkll rvhggaqkid
       61 ylemstsiea nelshtekkk lhtkekeyia knaaahinqe ddtiflgsgt tielmtryik
      121 psslrivtns lpvfnllsei krfelyligg lyrektgafv gsianeavqk igikkafvgv
      181 nglkgsevsn fsieegtlqk ivldnaaekc lvsdankfdh sdfynfydlr kidklftdst
      241 lsaelksyyq qftkiiq
//
LOCUS       WP_010731541             361 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA cytosine methyltransferase [Enterococcus].
ACCESSION   WP_010731541
VERSION     WP_010731541.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..361
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=40522
     Region          1..361
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mrtkvvslfs ggggldlgfq kagydiiwai dneknavety kknlgdhiil gdinefdine
       61 ipkadivigg ppcqsfslag krntedergq lvwryisiik hlkpkafvfe nvtgllsakn
      121 ssgekivdll kdafsqldyn lelqvinaad ygipqrrkrv livglrddev fkfpkpthse
      181 sddnllpyvs vkealddlpe steginevve ylvspqndfq rkmrsgdtvt ehftptmsel
      241 dkyiishvkp ggnymdipsd vpserirrlq rngghttcyg rllpskpsyt intyfnrpnv
      301 gcnihykadr litvrealrl qtfpdsyeiv stskqgrnki vgnavppmls eiiavelkky
      361 i
//
LOCUS       WP_010731682             164 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein, partial [Enterococcus faecalis].
ACCESSION   WP_010731682
VERSION     WP_010731682.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..>164
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          3..130
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,65..66,69)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(64,111..112,114..115,119)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(70,75..76,107,110..111,114..115,118,121)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93,97..98,107..108,111..112,115,119,122,126)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93,112,115,119,122,126)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(120,126..127)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mrkigyirvs stnqnpsrqf qqlneigmdi iyeekvsgat kdreqlqkvl ddlqeddiiy
       61 vtdltritrs tqdlfelidn irdkkaslks lkdtwldlse dnpysqflit vmagvnqler
      121 dlirmrqreg ielakkegkf kgrlkkyhkn hagmnyavkl ykeg
//
LOCUS       WP_010731763             433 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Enterococcus faecium].
ACCESSION   WP_010731763
VERSION     WP_010731763.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..433
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48672
     Region          1..433
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mvinfiilfl miaitsffva sefalvkirr skleqleken vknaklalhv thhldnylsa
       61 sqlgitltgl iigwvgegsv aallepvigk lpfssaisst isvalgfilv tyidvvigel
      121 lpksysivnt ekvvlfvvkp lhyfykvmfp fiwvlnhsaa glgkllgvrl vsegeetlsq
      181 eeltlvalns yekgeltkee yhylenvfef ddtlakdiqv drtsmqvfea setvkeaika
      241 sieqghtryp vileskdnvl gyvtlpdlik qsykddqltv ehlieepivt tetipikkll
      301 timrkkgkhi ailkdeyggt sglvtiedil eeivgeirde tdldealiae qsdgsyivsg
      361 kltlddfqry fhveipefee tnfttlagfa ssrykeinag tiieiasfrf tvleyqhahi
      421 dyfkvetmer kte
//
LOCUS       WP_010731783             578 aa            linear   BCT 01-JAN-2025
DEFINITION  class I mannose-6-phosphate isomerase [Enterococcus faecium].
ACCESSION   WP_010731783
VERSION     WP_010731783.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Jensen,S.O. and Reeves,P.R.
  TITLE     Domain organisation in phosphomannose isomerases (types I and II)
  JOURNAL   Biochim Biophys Acta 1382 (1), 5-7 (1998)
   PUBMED   9507048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..578
                     /product="class I mannose-6-phosphate isomerase"
                     /EC_number="5.3.1.8"
                     /GO_function="GO:0004476 - mannose-6-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009298 - GDP-mannose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66779
     Region          226..577
                     /region_name="ManA"
                     /note="Mannose-6-phosphate isomerase, class I
                     [Carbohydrate transport and metabolism]; COG1482"
                     /db_xref="CDD:441091"
ORIGIN      
        1 mkynlkptvd vrnkgkaivg yraiieeiks ylgnredavi vlecypgvrk eeiendflse
       61 fpeikekifi deygltveev qkkirdhite drvfgvyshy niqdfypseq leaarkrlvg
      121 kglkviygfg aslltkadvl isigvsrwei qlryrneqmt nwktnnpdee gigkfkrgff
      181 fewpmadrlq hgiypiidyy idtvktnqpk mitgsqyrqa taqiakqpfr tvpyfdesvw
      241 ggqwmkknfh lpedkenygw afdgvpeens lllqfendiv eipsqvvvee ettnllgekv
      301 rarfgrkfpi rfdyldtmdg gnlslqvhpl teyafdkfgm pftqdesyyi ldckegakvy
      361 lgtktgitkd tlfndlkkan qtgenfeaek yvneitvkkh dhfsipagti hcsgkntvvl
      421 eisatpyift fklwdwgrvg lnglprpihl ehgieniqmd rneeyinehl ftrlgkcekl
      481 enqqigvtse rtglaeiefi dsirhwftde iqlqtnesvn mlclvegsei lvcstdntfq
      541 pmevhygetf ivpesvkeyt lkakekgkfa viqafvki
//
LOCUS       WP_010731952             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010731952
VERSION     WP_010731952.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..248
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27304
     Region          1..241
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mertaieiqd lsaayqgktv lktinltikp qkitgiigpn gagkstfmka llelipastg
       61 kvafsgqpvk svrkkiayve qrseldlsfp idvlgvvllg typslrigqr pgkkekerar
      121 qalkkvgmed yakrqisels ggqlqrvfia ralaqgaewi fldepfvgid alserkifdi
      181 lqelknsgkt ilivhhdlhk veeyfdevvl lnkqliasgp vqevftsknl qlaygeiigh
      241 lvkggekk
//
LOCUS       WP_010731974             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Enterococcus].
ACCESSION   WP_010731974
VERSION     WP_010731974.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 187)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..187
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21038
     Region          45..181
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mlnneqfeek tisrkeiysg kiidvavdev rlpdggtskr elvfhpggvg iiafdeldrl
       61 llvkqfrkpl ekvileipag kidpgegknp emtaarelee etgyraksls hltsmylspg
      121 fanevlhiyh aqgvekvenp laqdedevle lyhltleeaq qamkdqlicd aktiyaiqyw
      181 elltkgk
//
LOCUS       WP_010732023             149 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010732023
VERSION     WP_010732023.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..149
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17681
     Region          1..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mrdlfpkklk qlrkehghtq eelakklait rqtvsnweng rsfpdhenvy rlaklygqtl
       61 yiflpdlpea pmeseeisse riqlirffic llvvlsflip fvsvialflf nmwkkyihsh
      121 flrlcypfmy flalcnclgi lllfyfqll
//
LOCUS       WP_010732078             644 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus faecium].
ACCESSION   WP_010732078
VERSION     WP_010732078.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..644
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73831
     Region          6..533
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          569..631
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 millqanqia rhfgaevlfe nihleistga rvalvgrnga gkstllkiia gieapddgki
       61 aknktatlgy laqdtgldsn etvwnemlka feqvrqmeqr mreleifise gtpdtpayts
      121 ylkeydrlqh dfsdrngygy eneirsvlhg fkfdssfydq kidtlsggqr trlalarmll
      181 qhpdililde ptnhldietl swlenylqsy tgallivshd ryfldkvvne vyelsrrkmr
      241 hykgnyskyl dlkaeqltse wkayekqqte ihkledfvar nlvrasttkr aqsrrktlek
      301 merldrpqgd ekqanflfsi ekpsgnvvlq iedaaigydd vtlsepinld irrqeaialv
      361 gpngigkstl lksiihqipf irgketlgtn vtigyydqgq adlhtnktil aelwdehptt
      421 pekdirsalg aflfsgedve kpipllsgge karvalakla mnkenflild eptnhldidn
      481 kevlenalid ydgtllfvsh dryfinriat kvvelsengs kvylgdydyy lekkqeeeei
      541 aellaqdepe sapaptnksd yyqskeqqkl irslqrkitq veeemtride widrleqemv
      601 apenledhvk lnelnqales arqdqetklt eweelslele eyen
//
LOCUS       WP_010732096             454 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Enterococcus faecium].
ACCESSION   WP_010732096
VERSION     WP_010732096.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..454
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50850
     Region          1..413
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mkiviigash agitaalnlr klqpeaevll idedhkdglg yvsnginlyl kgkihslaea
       61 annertlqas gaklitewrv teldpdkhql iltseegkke tltydkliva tgsspatlyk
      121 qieaenvyty knlvqskqvl aalkeakevv ifgagyigle ladalrnkgh mihlvdympn
      181 vlsryfdkdm igsfqnqlkt kqinfhpnef lidwkksgee vvsvqllsqt lkadivifsa
      241 qtrpntsllk dkvalyeddt vmvneylqts dsdiyaigdi vpvsfdkner hlflplvtra
      301 vhmaravalt lceqptaydl kqkitatvit dyflgtvglt edeapfleqs acscsgefdl
      361 fpqyyeenkt vnakliyhpd tleiiggqli skefllsdln lladivkqkt tipqlavenf
      421 gflaeytprf hylnelafkv lakranrnrv ekrs
//
LOCUS       WP_010732225             184 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Enterococcus faecium].
ACCESSION   WP_010732225
VERSION     WP_010732225.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..184
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20238
     Region          3..161
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtkkigffig slrkdsynkk vaeafarllp egyesvfvkf ddlpfynedl etpekapaew
       61 trfreevsgl dgvvfvtpey nrsvpavlkn aldvgsrpyg hsvwdhkpgl vvtaspggig
      121 gfganhhlrq slvflnvptl qqpeayignv anlidengni vegtlsffqt ildayldfsn
      181 klvg
//
LOCUS       WP_010732234             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010732234
VERSION     WP_010732234.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..218
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24941
     Region          124..218
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mtfirtnkre lslfilyflf igfqlgilpl allsmvtnsd lihsefvvfa vnlcipsivg
       61 iilfrkeiie sfsyfkektw lriasiffwv gliflvdvfm qyilgptnqs anqeyllqlg
      121 kqtplfltli vfaffgpile elifrhllin wlsqsiglil sslisiflft fihvthpidf
      181 fmyapgtill tiayltanrs lafimaihil nnvlgfvl
//
LOCUS       WP_010732256             304 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Enterococcus faecium].
ACCESSION   WP_010732256
VERSION     WP_010732256.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..304
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33228
     Region          9..293
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mkgksmwtls idiggtyiks alimdtqire krqiktpktd kdnfilvlve lirsyqqles
       61 iefvgfsvpg avkeastvff ggavaclnev nlkqeiekql pvrvfvenda kaavlgeasf
      121 ghlkgienga giilgtgvgv gllldgqvrk gphcqtgevs fliqdrging aesfaginls
      181 avrlveelak lfqcepegpl vfdylyqked eqaqtlyrty cnqvailcfn iqclldldkm
      241 iigggiskqk rlindirkny eaifsvspmi eqtitkmtie aaafeseanl igaakgvrln
      301 eisn
//
LOCUS       WP_010732363             110 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease signature motif containing protein
            [Enterococcus].
ACCESSION   WP_010732363
VERSION     WP_010732363.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..110
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12265
     Region          16..80
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(49,51..53,55,67..68,72..73,76,80)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 malradkqga hrvafdknrk rllktenvcg icgkpinkkl kapdpmspvv dhiipinkgg
       61 hpsaienlql ahwtcnrqks dklfnnkkee tkvignrnlp ksldwtlysg
//
LOCUS       WP_010732393             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010732393
VERSION     WP_010732393.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..268
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29647
     Region          3..255
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrlraadia agyenkkiie nmsvtipegk itsligpngs gkstllksft rilpvksgki
       61 ivndsdisty sskelakkia llaqtsehpi gmtveevvsy grypyqklfs gmdaqdheai
      121 ewaldatgls gyrtrdiatl sggqtqrvwi amalaqetdi lildepttfl dpshqleilq
      181 lltqinqikq ttilmsihdi nlasrfsdyl lgmkngelit egtpeevitk ecmkkifeid
      241 ativtlpktn kpvfltydll pkeqedql
//
LOCUS       WP_010732426             349 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Enterococcus faecium].
ACCESSION   WP_010732426
VERSION     WP_010732426.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 349)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15329249
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..349
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39893
     Region          100..285
                     /region_name="COG1223"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440836"
ORIGIN      
        1 mkkknilnli kyhaekndlq freeaieiar yfdtigdhql seyimsmlss antfvpqses
       61 feslffkeik lnteslplpe qiandikgii navnhnigin kflfegspgt gktetvkqva
      121 rlldrklymv efselidskm gqtaknvvav fneinrvpfp skvvilfdei daialdrins
      181 ndlremgrvt stilkeldkl neevvliatt nlyenfdkal trrfdtvidf nryekedlle
      241 iaeiilnall kkfksagrdi kifrkiisnm eeipnpgelk nlikislafs dpnnefdylr
      301 rllistqklp niignkelkr lqslgftvre ieiltgisks qvsrelkge
//
LOCUS       WP_010732536             597 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Enterococcus faecium].
ACCESSION   WP_010732536
VERSION     WP_010732536.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..597
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=69866
     Region          21..>592
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mnkteyprpq fvrkkwqnln gewlfafddq cvgmkekwgs hpkyydqkil vpfvyqcles
       61 gindqtphdi vwyyrefdin kqdgqrailh fgavdyyadi fvnghhvgrh sgghtsfsfd
      121 itdyltnekh qqlsvraedp hkdesiprgk qfwqekpegi wytnstgiwq tvwlevvedv
      181 yfshlrftpl fdegkvvael elnefreglt vdcciafkgg ivaklahsfv ekrviltvdl
      241 lqnyifrtnf hhegwswtpe tpnlfdvefv lkqkenikdv vssyfglrki hqengmiyln
      301 nkpyyqklil dqgywptglm taptddalak diqvakemgf ngcrkhqkte dprflywadk
      361 lgylvwgeca apavfthdss krlmqewtei vdrdynhpci vtwvpinesw gvpkisfdrq
      421 qqhfsqslyh ylhsldttrl visndgwamt etdicaihhy ghgeekeedk yqdfvttlst
      481 redllnrpst pwpifangfi yqgqpillte fggigfdfsg qkgwgytsvk sevdfikdyr
      541 riinavyrsk glwgfcytql tdveqeingl ltydrqpkcd lkeikkinds frtpyle
//
LOCUS       WP_010732726             430 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus faecium].
ACCESSION   WP_010732726
VERSION     WP_010732726.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..430
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48869
     Region          8..322
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkkkyvqvgl ggrarffyea iastyhqtce lvgfcdvsqt rmdyanrvlv nkygqkkvkt
       61 cmpsqfeqll ddvrpdevii tsvdrthhdy iiramrkgyd vicekpltid eekaqeiitv
      121 qkqtgrnlrv tfnyryapyh tkikellekd iigdvfsihf ewllntqhga dyfrrwhrnk
      181 hnsggllvhk sthhfdlvnf wlsshpkkvf afgglnfygm hnaekrgvet fysrcygsel
      241 akndpfaidl saneelremy leaeedsgyi rdrsvfsddi siedtlgvtv kyetgtilty
      301 slnaympweg fnvsfngskg riemkvieks yinaggdkkd egaavlqsiq vypmfgepye
      361 viveqeaggh gggdprlldd lfgevkeedl wnraathvdg ilsiltgiaa nhsiasgkav
      421 aidelvsfke
//
LOCUS       WP_010732878             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: histidine phosphatase family protein [Enterococcus].
ACCESSION   WP_010732878
VERSION     WP_010732878.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..219
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24665
     Region          3..191
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 melyftrhgk tqwnqerrfq gsngdspllp qsyeeikafg kkvkyvpfka iysstakrar
       61 dtaeginkel arpveifytd klrelglgtl egqsidemyq kypdnlpnlr nhldlydpsp
      121 fhgetiesai trietvvada vaqhkngpll fvghgaslta aiqwmtgkel selremgglf
      181 nssltilete epckllpyel kvwnqtdflg tetapepll
//
LOCUS       WP_010732914             209 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [Enterococcus].
ACCESSION   WP_010732914
VERSION     WP_010732914.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..209
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=23054
     Region          2..208
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mkiaiigatg hagsfildea lsrdldvtai vrhpeklpsd vpfiqkdlfe ltttdltsfd
       61 vvvdafnapk gkeemhqtsl shlieilegt dtrlivvgga sslfldtekt trmidqvpkn
      121 apfyptafnm yegllklkqs knlqwtyisp aslfdphgkr tgtyllsddy lqrnaagdst
      181 ismadyaias vdeildkqhe kqhisvvsr
//
LOCUS       WP_010732916             220 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            faecium].
ACCESSION   WP_010732916
VERSION     WP_010732916.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..220
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24107
     Region          118..211
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mslkkysfls ifcyglifis plilasiglv kstselitat avmyilgavv laifyfkqre
       61 plaiesavkk asvpkiviyg lvgifvalil qsiavmlesv lfgeatpsen tqniiqmime
      121 apafilattv agpimeefvf rrsilgiisr ysnfwvgavi ssllfafahn dghlliyffl
      181 gfffsleyka tgriwtsmit hvgmntlvvl vqlavqqglv
//
LOCUS       WP_010732934             553 aa            linear   BCT 01-JAN-2025
DEFINITION  xylulokinase [Enterococcus faecium].
ACCESSION   WP_010732934
VERSION     WP_010732934.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..553
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60728
     Region          17..477
                     /region_name="ASKHA_NBD_FGGY_BaXK-like"
                     /note="nucleotide-binding domain (NBD) of Bifidobacterium
                     adolescentis xylulose kinase (XK) and similar proteins;
                     cd07809"
                     /db_xref="CDD:466809"
ORIGIN      
        1 mkevnaqsml dvidgrtslg iefgstrika vlidssftpi aagsyewenk lengiwtysl
       61 ediwkglrvs yrkmaaevfe iygenlttig sigfsammhg ylafdskeql lvpfrtwrnt
      121 iteeaerilt ekfqynipqr wsiahlyqai lnkeehvrei dflitlagyv hwqltgekvl
      181 gvgdasgmfp idpstktyhq emknifgqlv ekehvaidld hilpkvlvag eeagklsesg
      241 aylidptgnl kpgipicppe gdagtgmvat nsvakrtgni sagtsafami vlekelenvh
      301 peidmvttps gelvgmvhtn ncssdinawv sifeeftnsl gmeisrdklf tvlfnkaleg
      361 dtdcggllsy gyfsgenitg vnegrplfvr tpgshfdlan fmrihlasaf gamrigmdil
      421 ksedvqidrl vghggifktp evgqrilasa meapvtvmdt ageggawgia llaaymidqh
      481 gkslenflae dvfgqdqgvt itpsaeeiag yqifmrryre gidiektaih qlqekgvien
      541 agtterrsvs sks
//
LOCUS       WP_010732998             178 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_010732998
VERSION     WP_010732998.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..178
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20659
     Region          21..>73
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mmgrvtnysk eyllfksmvy veeygmksit trdladfcgc stypiythfk sisglkekil
       61 eeitvcfery laecnsndvl stvyllkdff sihesirgii akseldmnsl fkrpffsyik
      121 shtkikeekl lellwlnalg slssdnfsqd ffetmnavwd knevtdeyle silkdqls
//
LOCUS       WP_010733171             403 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Enterococcus faecium].
ACCESSION   WP_010733171
VERSION     WP_010733171.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..403
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=45586
     Region          5..373
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mdkkrinfvg lgyvglpaal mlqnsgyeiv gtdinqelis elqdkkksfd epglqeeyik
       61 ainkgiqftt eyqkatvyiv avptpfdtit kkidpsylik avteiskncl egaliivest
      121 ispgtidqyv rpifkykkvn lchaperilp gnilkelrfn srtigadnek talavkeiyk
      181 sfcegeivlt diktaelskv ventfrdini afanelklic dregldvhsv ieisnkhprv
      241 nilnpgtgvg ghcipvdpwf lvgdypdqar lirmarevnd avpkrilekv relmkkrffg
      301 krlgiyglty kdnvddvres pslqiyqlmt dkeheevmfy dplikkaivn nqamdfenfl
      361 qnndlilvmn khqhlfenea llkqseitll dpigdleiag ivl
//
LOCUS       WP_010733132             274 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_010733132
VERSION     WP_010733132.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 274)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..274
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29521
     Region          6..265
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mallsyefmr raflaaifia giapmlgvfl virrqslmad tlshvslagv algfflnlnp
       61 tlttmlvvvl aavileylrt iyrtyseisi ailmagglal alvlmnlsgg nsatsiqsyl
      121 fgsivtitwe qviflgilfi aigilfflfk rpmyvltfde dtahvdglpv hlmsmmfnvi
      181 tgvaiavmip iagallisai mvlpaaigmr lgksfnvvia isvcvgflgm lsgltssfyl
      241 dtppgatitl vfialflivn iikrilvafr rknn
//
LOCUS       WP_010733177             199 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Enterococcus faecium].
ACCESSION   WP_010733177
VERSION     WP_010733177.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..199
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22551
     Region          <29..198
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mrviesiinr ilagtallfl spllilfsil lkienpelsp fytqtrigkd qksftiyklr
       61 smreiseqel ialtqlneag eqmfkikedp rittigriir ktsidelpql invlkgdmal
      121 vgprpplpne vakytdydlq rltvlpgctg lwqvsgrsdv sfeemvdldl kyienknlwl
      181 dlkilcltvp avlkmkgay
//
LOCUS       WP_010733424             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_010733424
VERSION     WP_010733424.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..144
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16362
     Region          19..144
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mkvvqtkdtm sniyldsvri rhqvfvveqg vplareidkd eahcihfvly sekkepqgtv
       61 rllplengkm klqrmailse yrhqglgkll ieeaetfakn qgyntillga qstaeafyek
      121 lgyiaygepf edagmphiym kktl
//
LOCUS       WP_010733528             310 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecium].
ACCESSION   WP_010733528
VERSION     WP_010733528.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..310
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34336
     Region          3..224
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 miieidklvk rygdfvalnh fdlqvqegev lgllgpngsg kstaincmls llnydkgtik
       61 lfgttmtpen yavkamigvv pqdvavfdel svqenidyfc glyvsekekr kalieeviql
      121 vglekyvsfr pgelsgglkr rlniacgiah kprlifldep tvavdpqsrn kilesikeln
      181 rqgativytt hymeeveilc dqivimdqgq viakgtkesl kdmvrtadrl tidipllpen
      241 vlsaiqrtia sdgiaykkgq lqvtttelnt vllsiltilq eekisygkia tkeaslndvf
      301 leitgkdlrd
//
LOCUS       WP_010733649             100 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus faecium].
ACCESSION   WP_010733649
VERSION     WP_010733649.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 100)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..100
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11462
     Region          7..96
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mesfvslnlt nnkeknrlal fndeqqeige mtwsdagpdi miidhtfvdp ayrgqklaek
       61 lvytgvelar rdgkkiiplc pyakkefekk peyqdvlrqs
//
LOCUS       WP_010733764             154 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Enterococcus faecalis].
ACCESSION   WP_010733764
VERSION     WP_010733764.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..154
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=17621
     Region          35..119
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mvtseelmar fsdltykfes nmpekqkgly innvvylnpq qhpreltstv aeeighhlts
       61 vgdiidqdtn ekrkqeqkar digatmvvtp qdlincyher ftyvwecadf lgitkqalec
      121 alsayskqfp eglvygdykl ffkpngtlgi vkwf
//
LOCUS       WP_010733917             136 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NusG domain II-containing protein [Enterococcus].
ACCESSION   WP_010733917
VERSION     WP_010733917.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009210
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..136
                     /product="NusG domain II-containing protein"
                     /calculated_mol_wt=15402
     Region          9..136
                     /region_name="COG5341"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444125"
ORIGIN      
        1 mkefiqksll kpwdiiiill lvmlsflpvv ifsyqqvdat pnkeavlrvd gteiktfplv
       61 tetkaytyly eddhgdknvi eidgeririk eadcddqicv rrgwatnnge tivclphklv
      121 ievrstdgsg edsliy
//
LOCUS       WP_010734086             226 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010734086
VERSION     WP_010734086.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..226
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25789
     Region          1..214
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mryieiadlt fyydeepvle gvsyhvdage fviltgenga akstlikasl gllkpskgti
       61 kiagknqdgd klsigyipqq vssfnagfps tvlelvrsgr yprgrwfkrl sekdhehvkr
      121 alesvgmwdm rhrrigelsg gqkqrislar ifatdpdlfv ldepttgmde esrnefyrll
      181 rhsahdhgka vlmithdhed ikqyadrqir lvrkedsqwr cfhmns
//
LOCUS       WP_010734087             273 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Enterococcus mundtii].
ACCESSION   WP_010734087
VERSION     WP_010734087.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 273)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..273
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29611
     Region          6..265
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mallsyefmr raflaaifia giapmlgvfl virrqslmad tlshvslagv algfflnlnp
       61 tmttmvvvvi aaiileylrs myrtyseisi ailmagglal alvlmnlsgg nsatsiqsyl
      121 fgsivtitwp qvlflgilfa vigllfflfk rpmyvltfde dtahvdglpv rwmsmmfnii
      181 tgvaiavmip iagallisai mvlpaaigmr lgksfnivil isiivgfigm lsglissfyl
      241 dtppgatitl vfiflfllvn lskrillgir rkk
//
LOCUS       WP_010734190             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HIT family protein [Enterococcus].
ACCESSION   WP_010734190
VERSION     WP_010734190.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..144
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16703
     Region          2..138
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mdncifckii nqeipsykiy edekiyafld isqstkghtl iipkehvtdi fdyneelasd
       61 vfaripkiar siekafpeme glniinnnre layqtvfhsh ihlipryskq ddfsihfgnh
      121 qadytteemt aiqekikeqv tihg
//
LOCUS       WP_010734263             167 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tRNA (cytidine(34)-2'-O)-methyltransferase
            [Enterococcus].
ACCESSION   WP_010734263
VERSION     WP_010734263.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..167
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=19042
     Region          1..156
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 mnhivlfepl ipantgniar tcaatntplh lieplgfstd dkqlkragld ywhdvdityh
       61 adlpafmayl gdrklhlisk fankvysden fadgeehffl fgkettglpe pfmreheekc
      121 lripmndthv rslnlsntaa mivyealrqq gfpnlelthh yendkld
//
LOCUS       WP_010734215             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Enterococcus].
ACCESSION   WP_010734215
VERSION     WP_010734215.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..157
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17284
     Region          5..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlqqyrkimv avdgseeael afkkavnval rnnselllah vidtrsfqtv ssfdgmlaeq
       61 atemakqtla dyemkakkag lhqvttvvey gspkhiiake ipedhevdli llgatglnav
      121 erlfigsvse yvirnaacdv lvvrtnlenq lpkkedk
//
LOCUS       WP_010734312             342 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Enterococcus mundtii].
ACCESSION   WP_010734312
VERSION     WP_010734312.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..342
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37740
     Region          13..340
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mslsetlsnv inmeiisait stlfiillgy flrkrevfss dvgktlskvv ltvaipalaf
       61 nsfmqelnde vlnqginili lgilvhvfli flskffffry apnkedtlrv lsifgsttff
      121 gipvvgavfg aegilyasif nigyriflys yaylkmsglk markniremi lnpivlatfi
      181 glfiwlfqds lpqiaqssse svaflridqt lpwlfkpltf lsslasplaw laigitlgdl
      241 pfgktlssht swyysfikvi vfplvillsi lllnamnilp vnsvglstmi immatpaatv
      301 avayainfek eavlasnasl lstlfsivli piwiivlnli gn
//
LOCUS       WP_010734324             644 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus mundtii].
ACCESSION   WP_010734324
VERSION     WP_010734324.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..644
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74065
     Region          12..644
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 msklayqrld dllevltrqt vplpmkeltk nfsisertvr tdianlndll tnvgasikli
       61 rgqgyllsig skeqfhdwwt esmstteffl ttseerqtyl lfllfknenp lslddfldrl
      121 fiskntfysy lktardnlat yhlkivnrpn igfevlgnef akrqaisdll iekdlqeyli
      181 gftemelelf dtinlvhlqe lalnhlasld lldsdyyhkn ilshfalais rfiagheine
      241 fplhvpalkk daqkvvghfl eeidhafdiq ltagekqyfi yylamnaprl vetgdsndss
      301 tetakaivee lltaikqtsn yaletdkmli edltshiegf inmnlmdarr snpllatikk
      361 sfpqaydlcl thletvsmkh gfyfssdeig yialhiagam erssirnhhk hrvilvcgtg
      421 ramsriieak iikhyqetve vvdrfsyvel qqcdlsaidf vittvplelf svpsiyinma
      481 qldkeiskie sfietlseak ngiyslfqea fflhenhadk etllekmaqq lyqkdfvpkd
      541 fydsvkkrea inqtninewl aiphpmtlma krsvvsvaii pdgvdwgngd lvrfvflfai
      601 qkneyeetee iyslllelmd redvqqailq ksdyphflsc mkql
//
LOCUS       WP_010734370             458 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MATE family efflux transporter [Enterococcus].
ACCESSION   WP_010734370
VERSION     WP_010734370.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..458
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49463
     Region          11..438
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mrdltkgspa klillftvpl lignvfqqfy nmvdmiivgq tlgknslaav gatggltfli
       61 igfaqgltag laiitaqryg akdfrglkks fatsvmisvi vtviltvlsl vfirpmlqlm
      121 qtpadiidea qtfiviilwg ifaavsfnll snviralgds rtpllfliva viinvvldli
      181 fiinfgmgve gaaiatviaq iassllcivy ikkkipmlql rkkdfsfdkq eirthlnval
      241 pmafqssiia igaivlqsal nslgtdvvaa qaaagridqf avqpmmsfgi amatfaaqny
      301 gakqygrilk gvrqtlvmsi gfsflagaiv iflgrplvsl fvspnetvvf dlaqtyfnin
      361 gslywilail filrytlqgl gqskvptiag mmelimrsfa aiiltgiwgy pgaalaspla
      421 wagsvivlly syiravkhlk qldaeqqqfs iedaeisy
//
LOCUS       WP_010733209             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: urease accessory protein UreF [Enterococcus].
ACCESSION   WP_010733209
VERSION     WP_010733209.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..231
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26582
     Region          10..231
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mnkdnilkyl lmvqvcdstf pigtfnhsyg metylrenki nnsqdffdwl kaylntqfyy
       61 seglllkacy eklpqnidev wnldsliths tqsretrdgt rmvanqmisl iqllypidll
      121 dkykyridnn lshgnpaivf aifaqkngfs fdeafcfygy svistliqna vraiplgqkd
      181 gqiillesys ilkemltnih ntdiddlgat vpgielaqir heiqifrlfm s
//
LOCUS       WP_010734371             432 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [Enterococcus].
ACCESSION   WP_010734371
VERSION     WP_010734371.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..432
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48323
     Region          1..432
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mvlnfvilfl miaitaffva sefalvkirr srleqlekdd vknaklalhv thhlddylsa
       61 sqlgitltgl iigwvgegsv aallepwigq lpigrgisat isvalgfilv tyvdvvvgel
      121 lpksysivnt eqvvlfvvrp lhyfylamfp fiwvlnhsaa slgkllgvkl vsegeetlsq
      181 eeltlvalns yqqgeltkde yqylenvfef ddtlakdiqv drtsmqvfda sdtvkqaike
      241 sierghtryp vileskdnvl gyvtlpalik qsleddqitv eslieepivt aetipikkll
      301 timrrkgkhi ailkdeyggt sglvtiedil eeivgeirde tdvdqaliak qedgsyivsg
      361 kltlddfery fnedvpefee tnfitlagfm ssyqkdieag tvitidqfqf tvleydhahi
      421 dyfslvilpt np
//
LOCUS       WP_010734437             334 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010734437
VERSION     WP_010734437.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..334
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37178
     Region          6..319
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msdnqlldvq nlhtgfrlkd eyydavddvs ftldkneila ivgesgcgks tlattimgll
       61 dpnntkitge imyndlnlie lnetlynkir gndigmifqd plsalnplmr iedqikegls
      121 yhtkmtaeqr qaralelleq vgipnparvg rqyphelsgg mrqrviiaia iackppiiia
      181 depttaldvt iqaqildllk dlqeetktgi ilithdlgvv aemadrvavm yggqfvevag
      241 vkelfenpkh pytqsllnsi pqegnheael hviegvvpsl knmprtgcrf apripwipas
      301 aheenpvlhe iapnhmvrcs cykhfhfrde kgev
//
LOCUS       WP_010734477             194 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Enterococcus].
ACCESSION   WP_010734477
VERSION     WP_010734477.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..194
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22115
     Region          3..129
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,67..68,71)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(66,110..111,113..114,118)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(72,77..78,106,109..110,113..114,117,120)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95..97,106..107,110..111,114,118,121,125)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95,111,114,118,121,125)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(119,125..126)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mkiigyartt indvdstaqm qklsdfgche ifhetygqkd slsdaiclek viekmeqgdt
       61 lvicqlhhlg kstrqlteft klfkdrglhl vsitekidtr epmgtvyfql meglaemeca
      121 likertligl dearkkgkig grpkidakti kkirrlyyek ketiqfissk cgvsvgtcyk
      181 yinlpekelq qlfn
//
LOCUS       WP_010734536             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus mundtii].
ACCESSION   WP_010734536
VERSION     WP_010734536.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..248
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28565
     Region          1..242
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 maifeslnln klsaveqeiy rfivnnleki pymrvrdiat dahvsstsvf rfiqkvgfds
       61 fpefrfyikn hlekahyetd dkqlmleeri nqlnmtifhp dieyqikkma ktlrqadfil
      121 fmgmgasgal aqyvarklan igyfcislde ltypirsflr pdqknalvfl svsgetkeri
      181 evisglahay svhkycitah kesslaqlcd ysidyaikee rkdifldlts qlpsmailet
      241 ligylede
//
LOCUS       WP_010734545             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ZIP family metal transporter [Enterococcus].
ACCESSION   WP_010734545
VERSION     WP_010734545.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..272
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28747
     Region          8..270
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mvdwllklep wqqaltgtaf tyfmtalgag lvfffkeikk dvlnlmlgfa sgvmiaasfw
       61 slldpaitka eengdiawlv vsigfglggl flyiadktlp hmhfgpahek eglpthlkrt
      121 illvfsitlh nipeglavgv afgaaatadn qttavlaais valgigiqnf pegaavsipl
      181 rqeglsrtka fvygqasgvv epiagvigai lvtkvavllp yalafaagam iyvvveelip
      241 eaqqtlsskr hyavfgvmtg fiimmildva lg
//
LOCUS       WP_010734698             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010734698
VERSION     WP_010734698.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..233
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27273
     Region          7..231
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mkrtrvlyle vadkikedif sgkypvgsml pteneleelf qvskitvrka iellatdeyv
       61 ekksgrgttv lsnrpynrls kaesftqilk dsqyevrket iglekisikk dhplysmfgs
      121 aavcfkrlyy lndqpyiyfv hylpkdmnkm kqkefdkesl yrlltqnnhi idsfsddfsa
      181 tfltdeekal lkttseigik rvrrsttedr evveyseaiy htdlhpyhin yet
//
LOCUS       WP_010734728             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus mundtii].
ACCESSION   WP_010734728
VERSION     WP_010734728.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..279
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30215
     Region          1..273
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkklirytvl afvaliwlag csqgnaetdt nkqttvklgi igedtdvwdd vkarlakedi
       61 dleyvkftdy nqpnaaladg sidlnafqhq ffldnynteh gtdlvsignt vnaplgiysn
      121 tiqsiddikd gakvaipndv tnggrallll qtaglikvdp akgqtpttsd itentknldi
      181 seldasqtar alndvdlsvi nsgvavdagl nptsdaifle pvddsarpyv niivarkede
      241 nneiyqkivd tyqteetakv ieetskgssv pawetfgek
//
LOCUS       WP_010734760             289 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus mundtii].
ACCESSION   WP_010734760
VERSION     WP_010734760.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..289
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31171
     Region          4..281
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,214,236..238,240..241)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mikliasdmd gtlldahmsi stenteairm anelgiefmv atgrnaqear aaldeagidc
       61 amitlngaqv fdrsgkslft vpipspqamt imdildangi yyevatnqgl ysesqpkrie
      121 sfassiathm phltykmaia masanlellh ityvdsirel llddklevlk iicfhtegpr
      181 ilgpvgkeis nlgelavtss gqnnlevnhk naqkgiavah vahergitld evmtigdnfn
      241 dvsmlqtagv sfamgnaeie vkdyakyltd tnlesgvgka ilrainenl
//
LOCUS       WP_010734801             307 aa            linear   BCT 01-JAN-2025
DEFINITION  permease [Enterococcus mundtii].
ACCESSION   WP_010734801
VERSION     WP_010734801.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..307
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=33689
     Region          5..307
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mfsfipnsvs qmgtiflsiv iealpfvllg ciisgalqvf ltpervkrwl pknrflsiiv
       61 gsilgfffps cecgivpivh qfvkkgvpvh tafafmltap iinpvvifst fiafgntwkm
      121 aglrmlgsfi valivgvwla yiqkgtilks sfdsamvepn shtheheeve aiapqkwgyr
      181 ilhvlthsid effdtgryli iggliaagmq tylptrvmlt lgstkllail imlvlaftms
      241 lcseadafig ssllslfgta pvvaflvfgp mvdiknllmm khyfntrfiv sliglialsv
      301 igftlfi
//
LOCUS       WP_010734847             593 aa            linear   BCT 01-JAN-2025
DEFINITION  V-type ATP synthase subunit A [Enterococcus mundtii].
ACCESSION   WP_010734847
VERSION     WP_010734847.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF003220.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK04192
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..593
                     /product="V-type ATP synthase subunit A"
                     /EC_number="7.1.2.2"
                     /calculated_mol_wt=65354
     Region          1..584
                     /region_name="NtpA"
                     /note="Archaeal/vacuolar-type H+-ATPase catalytic subunit
                     A/Vma1 [Energy production and conversion]; COG1155"
                     /db_xref="CDD:440769"
ORIGIN      
        1 mqigkiikvs gplvmaknms dasiqdmclv gelgvigeii emrgdvasiq vyeetsgigp
       61 gepvrstgea lsvelapgii sqmfdgiqrp ldtfmeitqs nflsrgvqlp aldhekkwwf
      121 eataevgqev stgdvlgvvd etkiiqhkim vphgvkgkik kieagsftid evvcvieted
      181 glreltmlqk wpvrrsrpik aklnpdapmi tgqrvidtff pvtkggaaav pgpfgagktv
      241 vqhqiakwad vdmvvyvgcg ergnemtdvl nefpelidpn tgeslmertv liantsnmpv
      301 aareasiytg itiaeyfrdm gydvaimads tsrwaealre msgrleempg degypaylgs
      361 rlaeyyersg rvialgneer egsitaisav spsggdvsep vtqntlrvvk vfwgldssla
      421 qkrhfpsinw iqsyslysse vgrymdqilq adwaemvaeg mrilqqeerl neivrlvgvd
      481 slsdndrltl evsksiredy lqqnafdevd tftsrekqfk mlklilsfge earqaislga
      541 ylseimkgtv glrerigrsk fvpetelekl deiqanikpt iqaivseggm tdd
//
LOCUS       WP_010734905             235 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010734905
VERSION     WP_010734905.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..235
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26937
     Region          2..234
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 msnqlpvyiq ihdqikseie qgvwkigdrl pserelaikf nvsrmtlrqa iqnladegil
       61 erkigsgtyv arekvqekms gatsfteime sqnrvpssrt isyfltspss semeklqlkk
      121 ddtilrmeri rfaddipicf eiasipqkii dgyskaeite slyrtleekr gnkigaakqt
      181 isavlaseki aeylevkrgd avlrlrqisy fedgtpfeyv rtqyvgdrfe fyler
//
LOCUS       WP_010734958             323 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PhoH family protein [Enterococcus].
ACCESSION   WP_010734958
VERSION     WP_010734958.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..323
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=35786
     Region          5..319
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 mteasssldi rltatddism llgshdkhik lieettetti htrgeviqii geetdislaa
       61 svirtlqeli krgihismpd vvtalkmaqk gtldyfvemy eqeivkdrng kpirvknsgq
      121 kkyvdsvakh dvvfgvgpag tgktflavvl aiaalkkgev qkiiltrpav eagenlgflp
      181 gdlkekvdpy lrpvydalyq ifgldhtnrl mergiieiap laymrgrtld dafvildeaq
      241 nttvaqmkmf ltrlgyqskm ivngdtsqid lpkgtmsgli haertlkqik kidfvnfeas
      301 dvvrhpvvae iikayekadl hqe
//
LOCUS       WP_010734978             397 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Enterococcus
            mundtii].
ACCESSION   WP_010734978
VERSION     WP_010734978.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..397
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43405
     Region          1..394
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,206,235,237..238,246)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,199,244..246,275,278)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            238
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mkqskrverl kpsvtlataa kakalkaqgk diisltvgep dfatpeniqe aaiaaikngk
       61 asyytptagi pelrqaivsy letyygltyd asqtivtdga kfalyalfqt ildpkdevii
      121 pvpywvsyge qvklaegvpv fvtgqevndf kvtleqleqa rssktkavii nspsnptgmi
      181 ytkeelqvig ewavkndili vaddiygrlv yndneftpia tiskaireqt iiingvskty
      241 amtgwrigya vgdqkiidgm iaiasqstsn ptavsqyaav ealqgeqdtv eelrkafeer
      301 ldivfplvad lpgvsvkrpq gafylfpnvk etlaicgyeq vtpwvedlle eagvalvtge
      361 gfgapenvrl syaanlatle egirriqrfi esksqne
//
LOCUS       WP_010735005             184 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [Enterococcus].
ACCESSION   WP_010735005
VERSION     WP_010735005.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..184
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20346
     Region          3..161
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtkkigffig slrkdsynkk vaetfadllp egyesvfvki ddlpfynedi etpeqtpaew
       61 trfreevkdl dgvifvtpey nrsvpavlkn aldvgsrpyg qsvwdkkpgl vvtaspggvg
      121 gfganhhlrq slvflnvptl qqpeayigni tnlldeegni iqgtvdffqt ildayldfag
      181 klna
//
LOCUS       WP_010735029             482 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus mundtii].
ACCESSION   WP_010735029
VERSION     WP_010735029.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 482)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..482
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55082
     Region          26..471
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mkknesikvl lrhtswlmls laitpliisi alythylfsy eksihnisia nqiasnveet
       61 iieealglty gqitpeefqk snqinrikee isaikvstqn sqelatlniv lrsldnvsdy
      121 ldkiianihq ketfaenqal mlhvesavkl ahdilqdfvk ieidtasvks eevrsslvil
      181 stieaviial iflmtrkfnm kmmyqiqqpm demikmadal aeghlnhrik tpqnnelkkl
      241 snsmndmadn lvilleenal kqynlaqsev rtlqaqiiph fiynsldail vlaemgqiek
      301 vkemtyslsd ffrislsqgk dwipveqeir hcdnylkilq irygdqlsyq ltidpkvnnh
      361 pilkmilqpl ienavyhgtk lvrrpgkiiv kayidqeefi hfwiidngkg itetkleein
      421 qeladgldtn fhkgyglfnv nkrlllyygt dasikitsri dhgtvihvvv ptknidrnea
      481 nv
//
LOCUS       WP_010735036             509 aa            linear   BCT 01-JAN-2025
DEFINITION  xylulokinase [Enterococcus mundtii].
ACCESSION   WP_010735036
VERSION     WP_010735036.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..509
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55695
     Region          2..448
                     /region_name="ASKHA_NBD_FGGY_BaXK-like"
                     /note="nucleotide-binding domain (NBD) of Bifidobacterium
                     adolescentis xylulose kinase (XK) and similar proteins;
                     cd07809"
                     /db_xref="CDD:466809"
ORIGIN      
        1 mlidqhyepi aagsydwenq lengiwtysl deiwkglqss yqqlvdvvse eydttlttig
       61 aigfsammhg ylafdqhdel lvpfrtwrna itaeaeekls kafhytipqr wsiahlyqai
      121 lnkethlkdl syfttlagyi hwqltgqkvl gvgdasgmfp idrqtkgyda qkiaifdqla
      181 qaegfmqple tllpeirlag evagpltekg aklldlsgnl sagipvcppe gdagtgmvat
      241 nsvglrtgnv sagtsafami vldkelvnih peidqvttpd gspvamvhtn ncsseinawv
      301 kifkefsesl gvtidtqqiy etlflkalqg esdcggllsy gyhsgenitk meqgrplfvr
      361 qsdskfdlan fmrmhlssaf gamrlgieil kseqvtidrl vahggifktp kvaqtilasa
      421 meapvtvmet ageggawgia llaaylrsad gmtleeflak evfstseglt iepkeadlkg
      481 yekfielyek glpieasaiv smeegvrec
//
LOCUS       WP_010735111              65 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Enterococcus].
ACCESSION   WP_010735111
VERSION     WP_010735111.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..65
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6968
     Region          1..63
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mnngtvkwfn sdkgfgfitg edgqdvfahf saiqgegfkt ldegqavtyd iedgqrgpqa
       61 vnink
//
LOCUS       WP_010735128             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase [Enterococcus].
ACCESSION   WP_010735128
VERSION     WP_010735128.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10082841
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..163
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005542 - folic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18927
     Region          2..161
                     /region_name="DHFR"
                     /note="Dihydrofolate reductase (DHFR). Reduces
                     7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH
                     as a cofactor. This is an essential step in the
                     biosynthesis of deoxythymidine phosphate since
                     5,6,7,8-tetrahydrofolate is required to regenerate 5;
                     cd00209"
                     /db_xref="CDD:238127"
     Site            order(5,22,27,58,98,104,117)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(7,14,44..46,65,99..102)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mfismwaqdk ngligkdgll pwrlpndmrf frehtvdrll vmgrktyegm gdlslpyrhi
       61 ivlttqedfe vkenaevmhs idellafaet vsediyvsgg srifqellpq tgiiwrtlid
      121 gefegdtyig eidfsdfela eehigitdqe nhyahrfqkw vrk
//
LOCUS       WP_010735146             131 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Enterococcus].
ACCESSION   WP_010735146
VERSION     WP_010735146.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..131
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15074
     Region          38..123
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mvlwiiniil lliilaivfw evylrvmakr satmleeeef regmrraqvi dvrekdvfda
       61 ghilgarnip ytvlknslgs irkdqpvyiy dqkkslsirt anqlrkagyq diyilkggyd
      121 gwsgkikskk i
//
LOCUS       WP_010735226             245 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Enterococcus
            mundtii].
ACCESSION   WP_010735226
VERSION     WP_010735226.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..245
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27219
     Region          5..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mtekilvehl vkkygdntvl ndinvsineg dvvcvigpsg sgkstflrcl nrledptsge
       61 iiidgahlmd kntdinlvrq higmvfqhfn lfphlsvlen ivlapmdlkk lsreeaekka
      121 iklletvgle dkkdmypdnl sggqkqrvai aralamnpdi mlfdeptsal dpemvgdvln
      181 vmkklakqgm tmvivthemg fakevanrvm fidggnfled gtpqqifenp qnertkdfld
      241 kvldi
//
LOCUS       WP_010735332             635 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus mundtii].
ACCESSION   WP_010735332
VERSION     WP_010735332.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..635
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=73511
     Region          9..635
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mikerekaii qyilmneytk vtkiakhmnl snktvsqslk lidelfsgtt ielirkprvg
       61 vsingdpnev lsgldtttmv tvpaskkeri qflcfellkk ktyftrqelq dtlfiskstl
      121 egdmnqvhei frhfnvsidr lpgkgsflnl seqekrhlaf dliyyfwgsn wkitkknqly
      181 lhsiqgippf vnefidmkni tlvdtllqey lkeaqirlnd ttyhslllhl limidhvred
      241 nylesegvfg kvrenkpfdl firklektfl ltlpssevcy illhlegdtl leqtkqmhev
      301 tdehirqlih envtlynesi ilglvthike avlrikkgll ihnpflqdvk knfpmaftea
      361 iqlanalsqd fsinvpedev aflavhiqam keqkeekhqk kvsvllvcss gkgtsqllaa
      421 rlrrnyekie isrilsiqel mqtsidedlv istvnlnlet iptinvspvl nklerqkieq
      481 flknaqnkpi kstnhfgkli kddlifldhs ftdyqeviqf vgqqlikkgy aeekiisssl
      541 ereqlsftsf gkfatphgvp kyvkksaivf lrlanelmwg etkvkylffi cikdetaqel
      601 eeiydvmlei iesgeknyll kgtkneikny lkeef
//
LOCUS       WP_010735349             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NusG domain II-containing protein [Enterococcus].
ACCESSION   WP_010735349
VERSION     WP_010735349.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009210
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..135
                     /product="NusG domain II-containing protein"
                     /calculated_mol_wt=15151
     Region          9..132
                     /region_name="COG5341"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444125"
ORIGIN      
        1 mhnfrksgik pwdiiiisvl vvasfvptiv falsfdnaes gnsvkyavvk idgkeverfd
       61 ldeisskmvt yhpsdtqyni veiqegkirv kednspdqia vrtgwisepg qtsiclphrl
      121 vitieqegqs dyhiy
//
LOCUS       WP_010735435             393 aa            linear   BCT 01-JAN-2025
DEFINITION  NupC/NupG family nucleoside CNT transporter [Enterococcus mundtii].
ACCESSION   WP_010735435
VERSION     WP_010735435.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..393
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42317
     Region          1..393
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 msqfigiigl llifglavli ssdrkaikrk pliimlvlqf afgfvllrtt fgtavvamla
       61 klfdhllafa gegvnfvfgg vanvgsapff lnvlmpivfi saiigilryi kilplfmkav
      121 glglskingm gklesyngva sailgqsevf isikkelpfl tekrlfsmsv samstvsmsi
      181 vgsymalids kyvitalvln lfggyilasi vnpyeldeke delvieedke qtffqmlgey
      241 ildgfhvait vaamligfva liaminalfs gifgitfqqi lgyifapfaf isgipwkeav
      301 dagsimatkl vtnefvamte lstgtfefte rttailavfl vsfanfssig iisgamkgln
      361 eekgnlvakh glkilftasl vsflsaivtg ill
//
LOCUS       WP_010735463             357 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010735463
VERSION     WP_010735463.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..357
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38985
     Region          16..177
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          121..357
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflaikemry aklrygliig imfliayvvf mltglasgls eefkkaivdw qaqeivlsed
       61 ankvfaasql tredldqvda kdkapiglfs gavkaeeken itvfgttrda fllpdllege
      121 mfkqkneiii sknmadlgfs igkkikigsy deeltivgif petyytvgpv vytdldtwtq
      181 lkfgdqpfas dekkpinaiv tkqaatiqsd gasktlqkls iddfiqslpg ysaqnmtlna
      241 miyflfvvva avvgifmyvi tlqktaifgv mkaqgirnsf iarsllaqaf ivgvvgvafa
      301 vglafltsli lptampfaim wpqwllysgi lilvamiggl fsirtvakvd pviaigg
//
LOCUS       WP_010735472             748 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-galactosidase [Enterococcus mundtii].
ACCESSION   WP_010735472
VERSION     WP_010735472.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 748)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16044983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..748
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85551
     Region          27..285
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          290..638
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Site            order(337,368,412,477,481,529,548,551)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          652..741
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mieqlnkrif hmnnsqvsfi lhvmqngqie qiyygkplhg lsveeidylv tdqnksagtv
       61 kffeddpnft ltdhpqaypv ygssdfkega ielssnqtpy ytdfrfveat tkkgkkrtln
      121 cpatygneee tetlslrlmd qerqlelilh ytlfydstai vqsqtlinqs eaelqihrml
      181 sgvlnlstka ydfthfsgaw lkerhekkrp leqgvvaigs lkgasshqhn pfirlehqns
      241 tldqgevygm nlvysgnfla qaevdewdkt rvmigihptq ftwalvpkes fttpeavlmy
      301 saagtnglak qlthfienyl idrqwqdapr pivfnnweat yfdfteekll slatigkelg
      361 mecfvlddgw fgkrnndrss lgdwtpdkqk fphglasfat klknmglqfg mwfepemisp
      421 dsqllekhpd wvvkhpysri svgrgqyvld fanpavvegi yeqmakiiee tnltyikwdm
      481 nrniteaysa ylekqgmhqq effhryvqgv ytlygkllts ypdlliegca ggggrydlgi
      541 lfyspqiwps dtsdglerls ilsgtmagyp lssfsnhvsa spnhqvlret slsfrqdvam
      601 fgplgyeldl ltlteaekqq isdritfyka hrqllthgef lqilpnhpyd neicwgvfnh
      661 drseaiigfy qklgranpaa qaylplpecl nkdsyyqine ketisghflm nvglkkphlf
      721 nganhttyql agdcqsfvyh lverremk
//
LOCUS       WP_010735566             141 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Enterococcus mundtii].
ACCESSION   WP_010735566
VERSION     WP_010735566.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..141
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16410
     Region          4..141
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 menkkveaai eqlkkeniri tpqryavley liehrshpta deiykalehr fpnmsvatvy
       61 nnlrlftsig fvqemkygda ssqfdfssqr hyhvicqnce tivdfhypgl ediemaagrl
      121 tdfeihdhrl elyglcpnck k
//
LOCUS       WP_010735696             321 aa            linear   BCT 01-JAN-2025
DEFINITION  aromatic acid exporter family protein [Enterococcus mundtii].
ACCESSION   WP_010735696
VERSION     WP_010735696.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10532842
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..321
                     /product="aromatic acid exporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37079
     Region          1..141
                     /region_name="ArAE_1"
                     /note="Aromatic acid exporter family member 1; pfam06081"
                     /db_xref="CDD:428756"
     Region          148..306
                     /region_name="ArAE_1_C"
                     /note="Putative aromatic acid exporter C-terminal domain;
                     pfam11728"
                     /db_xref="CDD:432028"
ORIGIN      
        1 mrigmrtvkt visvfasmlv anyfsllfwp sagiiallsv gntrrstlmt giyriaafiv
       61 atliaymcft llgyriisfs vfllffipia vrfkltegiv vnsvlithyl seqsmswqli
      121 tneaalmiig vgfallsnvy mpdskkslke nqmiieerfr lllknmadfl lsgeayenqg
      181 lckelqvyir esqayarnhq ennllrqnqy yetyfsmrra qinviqdmqe nlayiqdpvp
      241 ysdhiyglli ytaetfsesn dgkeiltrie evygmyrqmp lpttrsefed raelfqflqs
      301 fksfieikve fsqqmivdae k
//
LOCUS       WP_010735721             221 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YitT family protein [Enterococcus].
ACCESSION   WP_010735721
VERSION     WP_010735721.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..221
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24051
     Region          5..>190
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mkqvkflldl cgiifgaaly glavtginlp skladggvtg ialllnhlfg fapsitslii
       61 nlplllislf ifgkhafirt ivgtfslvff lhvwenlnvh favgnllvns lmtgilsgig
      121 cglvfrfggs tggtdivyqa iekyyhvnig kslfvitfgi lvvsllyldf thfaytllsc
      181 silsytlnkv kyfrfanpfk kitapsptvn qlepvedsyi d
//
LOCUS       WP_010735766             419 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Enterococcus mundtii].
ACCESSION   WP_010735766
VERSION     WP_010735766.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18643657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..419
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47975
     Region          33..62
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          38..301
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          67..93
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          177..200
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          196..>413
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          208..233
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(209..210,213..214,216,240,243..244,247..248,
                     250..251,274,277..278,281..282,285)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          238..268
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          273..300
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          339..365
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          373..400
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mmtnsekmlq aladenltea neylakalqe dpadvlhelg eellaigfle eakaifehll
       61 tvspendewn iplaeiaied neidqafdyl ekiqqdseyy pqallaiadl yqvigipevs
      121 eaklkeaakl lpeepliqfa laelyysvdr fneasalyem llangieeis sismqerlgq
      181 slsmqgdfea aippleaala eertddrlfq laftnlqlhe nekainylqe lrelnpqyqs
      241 lylylgqalq eeemieeaqq vledgikenp fqvelyhlas enafrlhdke kaekllldal
      301 nvgdkqdetl ltlsnlyldq eryedvvqtv nqmeevanpy aewnlahayn qledfavaav
      361 hyeqaaheld hkpdflkeya lflreegqla ktrelleqyl tyepgdmevl sllddlter
//
LOCUS       WP_010735779             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [Enterococcus].
ACCESSION   WP_010735779
VERSION     WP_010735779.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26597
     Region          1..226
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 merlqkviah agitsrrkae eyilagrvkv ngqvvkelgv kvgkhdtvev dqvpiyqeey
       61 gyyllykpkg visavaddkg rkvvtdllpm vkeriypvgr ldydtsgill ltndgdfaqr
      121 lthpkhevdk vyvakvkgia tksalnpltk gikiegkkts pakyailsvd phtnhsivel
      181 tihegrnhqv knmlqavglp vqklkrekyg eltlqglrpg eyrelnkkei sqllnqsk
//
LOCUS       WP_010735809             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Enterococcus].
ACCESSION   WP_010735809
VERSION     WP_010735809.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..240
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27660
     Region          45..125
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mdkeewntfa kdyyesqkes sttivedvva ylksedllpa gsfadvagga grylplakei
       61 eqyelidfse emlvyaehea qilglnncqf ilkdftnflq eektyelvfs aanpalvsce
      121 qleklrgkam raclilrvvs sedsvfvple rylgieesdp ntsstimdrf etylskkhls
      181 ykrteftyds qeevtpsflr ayyeemqddp rfqsalqelf knsetiqstn kltyrlltiy
//
LOCUS       WP_010735890             458 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [Enterococcus].
ACCESSION   WP_010735890
VERSION     WP_010735890.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..458
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51517
     Region          24..429
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mnadpesqsl laqillliil tlinaflaas eiavvsinkn rieqkaeegd vkskkllkil
       61 qnpnnflsti qvgitlvnil sgaslantls vrlapllggg aaarsianii vlailtyvsi
      121 vfgelypkri alnkseevan ftsgmirmig vvakpfvwll sastsllari tpmtfddeds
      181 kmtrdemrym lenegvlnne elemlqgvfs ldtkvarevm vprtdafmid indsieenvn
      241 evlsenysri pvynedkdkv vgilhtknll kaahkfgfen leikkimqep lfvpetifid
      301 dllyemkktq nqmailldey ggvvglvtle dlleeivgei ddesdevenl yeqvgdyeyi
      361 iqgrmlidef neafesnlhm sdvdtmagyl italgmipde geklsfdven itliseemeg
      421 srvlkirvif hdpeeieaep eeerryfkkd feddeprr
//
LOCUS       WP_010735910              66 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Enterococcus].
ACCESSION   WP_010735910
VERSION     WP_010735910.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7046
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mehgtvkwfn nekgfgfitv dggddvfvhf saiqgdgfks leegqevefs ivegargpqa
       61 aevskl
//
LOCUS       WP_010735949             376 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MraY family glycosyltransferase [Enterococcus].
ACCESSION   WP_010735949
VERSION     WP_010735949.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..376
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41896
     Region          41..290
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            94..95
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            216..219
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133463"
     Site            order(266,280..283)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 mlvsfsivik ifltillsli ltpifkiisv qtgmvdkpne rrinkvpmps agglpifvsf
       61 visslflfkd iipkfyilpi llaasvivlt gllddkyels pkqksigill aaliiyfvad
      121 iridsftlpf lgyiqlgwls fpvtifwifg itnavnlidg ldglaagisl iglmtigiig
      181 yfflhastvy ipivifclva siigffpynf ypakiylgdt galflgfmma vlslqglknv
      241 tfvssislli imgvpvtdtf faiirrkanr vsfstadkkh lhhrllalgf thkgavltiy
      301 sialmfsfta mimnytgslg tialflvmlf aaillfelig linekyqfil ktlrflgnke
      361 yrtqvmqkyf kkwkrp
//
LOCUS       WP_010735953             189 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010735953
VERSION     WP_010735953.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..189
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21598
     Region          2..>113
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 markktitke qilaaayeva anegfskfta rniankmncs tqpiylefkn mddlkhalfe
       61 qiydylkyev fpvehtgnti vdlalnyihf anrekklyss lyleeygggr emqnfsynyf
      121 mdvvkedpky mdlsddklvs lhngtwiiat giaalmssni ihptdtqiek miqdsinail
      181 slkdpievd
//
LOCUS       WP_010735966             337 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Enterococcus].
ACCESSION   WP_010735966
VERSION     WP_010735966.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..337
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38025
     Region          1..253
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mihlgiigtn withqfvqaa latrkyelta vysrhlekaq qfgaeyegdi afatdltvff
       61 elehmdtvyi aspnslhfqh akqailagkn vivekpafst pkemeeiihl anqekvfffe
      121 aarniheagf kkiaeflplk deiiganfsy mkyssrydqv ldgeepnifs prfsggammd
      181 lgvylvyaav gwfgkpqevh yfprkiatgv dglgwgilry atfdvaiqpg kigdsylpse
      241 iyfdsgtvim ngvnaieqae yhdrnheqie kleivasenp mseeaedfan vimnpkdpqw
      301 glqyeewvel arnvnqvvyd lrisggiefd adkegte
//
LOCUS       WP_010735996             273 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TlyA family RNA methyltransferase [Enterococcus].
ACCESSION   WP_010735996
VERSION     WP_010735996.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..273
                     /product="TlyA family RNA methyltransferase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30259
     Region          4..245
                     /region_name="YqxC"
                     /note="Predicted rRNA methylase YqxC, contains S4 and FtsJ
                     domains [Translation, ribosomal structure and biogenesis];
                     COG1189"
                     /db_xref="CDD:440802"
ORIGIN      
        1 mekervdvla vkqglfetre qakrsvmagl iyneknerfd kpgekipvss elkvkgkklp
       61 yvsrgglkle kalkqfdltv kdkvlldiga stggftdaal qngakmsyal dvgynqlawk
      121 irqdpkvvvm ervnfryakp edfdqgvpev avidvsfisl klmlpplhai lkpegevial
      181 ikpqfeagre avgkngivre atthqqvieq iltfateqgf dvldlsyspi tggegniefl
      241 ahlkkvsdkg tiyanvdpah ivemaheqft hkr
//
LOCUS       WP_010736015             124 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010736015
VERSION     WP_010736015.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..124
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14142
     Region          1..112
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(49,52,56..57,66,84,88,94,98,101..102)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mnikqvseek gisadtlryy eriglippvn rtnggirdyt eedlrwvdft lcmrsaglsi
       61 eslteyirly sagdetilar rdllmeeseq lakkiaemqa cqerlqkkia rynqdlvkgd
      121 pila
//
LOCUS       WP_010736116             502 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus mundtii].
ACCESSION   WP_010736116
VERSION     WP_010736116.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 502)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..502
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52722
     Region          199..500
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnffkralks tkvkwgrsll llavftailv fvlagltirs aaqeaaeqaq kdvgatvtls
       61 anreaafqkq tvatdtesgg rpdpgsfslt pvsvsdaeki aaldnvasfs fessasalan
      121 sgitaisssd tsetseetdt atdaapngen mggamgggkp qmiqadfqis gvsntaqtsg
      181 ftdgtakiie gegitdsdkd tnnvvidstl asandlsigd tfiitstede ettyemtikg
      241 iyessetsss mgmnfnfmnp antlytyytf antlngsted dtidsavytl tdpnkmtdfi
      301 neaenlidts tfslqsndtm fqamleplnn vasfsqnvvl lvavagiiil tliimitire
      361 rrhelgvlls lgesrskivl qlfaevaicm ivalgvasfs gnvvanavgq qlldqqtets
      421 tdspaeqqge qmpgggnrgp ggqpggtsnp ftvseqvsdl eitvqpaqlg llaavafgis
      481 llsvflasig ilrlnprkil ln
//
LOCUS       WP_010736139             440 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Enterococcus].
ACCESSION   WP_010736139
VERSION     WP_010736139.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..440
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46970
     Region          1..436
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mkgklkrein lfgalstvmg tvigagvffk taavvastqs tsltllawll ggflticagl
       61 tvaelataip etggavkyie aaygklpsfl lgwaqsliyf paniaalsii fatqlinllq
      121 lspdyllvia iitalsitgl nllgtkvgay vqsitlvvkl ipiaviiiwg lltpgqgtvq
      181 lfpveagqgv swaeglsgal latlfaydgw lgvgamagem krpekdlpka iilglsfvtf
      241 vyllinfvfl ktlpidqiag nlnassdasa vifgelggki vtigilisvy galngytltg
      301 irvpyamale nelpfsnqlt klskkftvpy vpalfqlaia cimmslgsfd fltdmlifvm
      361 wlfsllifig vfilrkkape mprpykvply pvipiiailg aifilgmtli tqtnlaligi
      421 lvtllgvpvf yykkrqtesn
//
LOCUS       WP_010736199             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Enterococcus].
ACCESSION   WP_010736199
VERSION     WP_010736199.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 187)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..187
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21180
     Region          45..181
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mleyeqfeek tiqrkeiyhg aiidvavddv rlpdgnigkr elvfhpggvg iiafdekdrl
       61 llvkqfrkpl ekvileipag kidpgekqap eitaarelee etgyraerld hltsmylspg
      121 fanellhiyh avniekveqp laqdedevle lyaltlaeak qamsdqvicd aktiyaiqyw
      181 esmnkgk
//
LOCUS       WP_010736202             459 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus mundtii].
ACCESSION   WP_010736202
VERSION     WP_010736202.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..459
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49418
     Region          10..458
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mdlfrkkeis lnhtsemkke lktsdlimlg igaiigtgif vvtgvaanqn agpalslsfv
       61 laaivvilsg lsfaefasrv pviggpyayl yvvfgefaaw ltgwlligef llavssvasg
      121 wsgyvqgfie slgfglptal tggynpangt yidliavlvv ifvtyivsle akkalrlnnm
      181 mvyvkfgiia lfiivgiffv kpenwqpftp fgfegvldga alvffaflgf davamaaeev
      241 knpqkdvprg iigsiliatv lyiivtlilt givpytelgv ndpvafamry vghgtvgaii
      301 avgailtllt vtismmysla rllfavskdg llpqfmteid kkhrtpkkat yaagiaalff
      361 agffplnila eltnimalay lmlvslgllk lrkmfgkpka gefkvplvpi lpiisilscl
      421 vlmsrlqavt wlvfgitmvi glviyfgygy khskintek
//
LOCUS       WP_010736267             168 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: shikimate kinase [Enterococcus].
ACCESSION   WP_010736267
VERSION     WP_010736267.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..168
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=18897
     Region          4..165
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 maaivligfm gagkttisrk lsmqlkkpli dmdtklveef gcsisqyfel hgeaafrqee
       61 tkllknslqe eaiiatgggv ilqeenqrll tdhlvvylka dpdllikrir qdhkqarpla
      121 ldkddtelke lffsrkkhye tladltiett gkspaevvse iikqvmnr
//
LOCUS       WP_010736376             121 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system PemK/MazF family toxin
            [Enterococcus].
ACCESSION   WP_010736376
VERSION     WP_010736376.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..121
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=14179
     Region          4..104
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 msykprqrdi vlfyfepskg yevkkrrpal imskdaynla tnliivcpit tsdknrpflv
       61 piqsdkfkld evkrskvntl qvfsldytek akrnvkyidt leeeaffdia qrflknfsfp
      121 i
//
LOCUS       WP_010736379             490 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Enterococcus mundtii].
ACCESSION   WP_010736379
VERSION     WP_010736379.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..490
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52552
     Region          23..477
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,279,282..283,286..288,291,319,323,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 msknqpvdiy gkpynrtllv vvlligtfct vlnqtlltta fpalmkafdi sasdvqwltt
       61 gfllvngimi pitawlinkf ssrklylsam tifligtitc ftapnfstll igrliqacgv
      121 gvsmpllqni mlsifppekr gsamgmsgiv iglapalgpt lsgyiidnyh wrdlfgmvip
      181 ivvlvlvlaf flmksvipls npsidifsai lstigfgsll ygfssvgdag wgstkvisfl
      241 ivgvifiaaf awrqlhlehp flelrvfksp tftiaailag vtnmamvgae mvvplyiqni
      301 rgesafhsgl mllpgalimg ammpitgaif dkhgakrlai vgmfiltaat apfafltett
      361 pvlyivilya irmfgismvm mpvttsgmna lpnnlishgt avnntfrqia ssigtailis
      421 vltnvtkdnl ptdavlkstp laykdqaina tlsgyhaaff vaiifgligs aiafflkrke
      481 pvvvevgdna
//
LOCUS       WP_010736381             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010736381
VERSION     WP_010736381.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..182
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21680
     Region          3..89
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          98..178
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 markntlryi llgllskknq tgyelnqafk neigefwqak hsqiypelak meelgiikhe
       61 vgitgvklek kiyqlteegr vllnewihts pnelpvnrde fvlklyfvkd indptwieil
      121 eqqkelheek rqhlfarqqv ifptekdqhe nyghylilsh ainreteyin wltqvleqei
      181 rk
//
LOCUS       WP_010736386             764 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus mundtii].
ACCESSION   WP_010736386
VERSION     WP_010736386.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..764
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87927
     Region          4..757
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mkqikrlfqi dpwkistttl dkenlrlqes ltsigngymg mrgnfeetys gdhhqgtyla
       61 giwypdktrv gwwkngypey fgkvinavnf iamdiyindq lidlasldpe dfsweldmkn
      121 gvlsrqftit tatnkvrfsf erflsivkse aayirvkvel iagsatvkfg skldgnvqne
      181 dsnydehfwn qtdrgtkdsi gylttktipn afdieqftvt agmrhfingk ettpifeeqt
      241 lalqgvfsyd ltpndpvvvd kevlvltsrd ipeaqqvatl mdefdqltth ydeakkeqtt
      301 awakrwelad vviegddeaq qgirfnlfql fstyygeder lnigpkgftg ekyggatywd
      361 teayavplyl aladpevtkn llkyrhnqlp qaihnaqqqg lkgalypmvt ftgvechnew
      421 eitfeeihrn gaiayaiyny tnytgdtsyl kneglevlae iarfwadrvh yskrqnkymi
      481 hgvtgpneye nninnnwytn tiaawvlryt renylafkee ttieiseeel akwadivenm
      541 yypideeqgi fvqhdtfldk dlmpvsdlpl selplnqkws wdkilrscfi kqadvlqgiy
      601 ffneeftkee kqrnfdfyep mtvhesslsp sihailaael glekkavemy qrtarldldn
      661 ynndtedglh itsmtgswla ivqgfaqmkt ahgelsfapf lpntwnaysf hinyrgrlif
      721 iavsdeqvtf tllngealel tvygqaqelt dqltiplrkd dahv
//
LOCUS       WP_010736418             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MIP/aquaporin family protein [Enterococcus].
ACCESSION   WP_010736418
VERSION     WP_010736418.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..238
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24455
     Region          5..238
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mnadmtqimg efigtmilil lgdgvcaavn lnkskaqasg wiviafgwam avtmavfisg
       61 fmgpahlnpa vtlgmamtga igwnlvfpfi iaqllgaivg avlvwlsylp hwsatkdqga
      121 ilgtfatgpa irnypanfit eligtfvlvl gllafgqtef aggtnvfavg glilaiglsl
      181 ggstgyainp ardlgpriah ailpiankgg sdwgyswvpi agpmvgaiva vgmytlmv
//
LOCUS       WP_010736527             151 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Enterococcus].
ACCESSION   WP_010736527
VERSION     WP_010736527.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..151
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16746
     Region          5..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 meqaykkilv gidgseqafa afkkavevar rnegtvyatn vidqqfyqfm gytpidqsli
       61 dqqtesakel ieecknygks vdyqkiegiv aygsvresma vklpkkyqid limigqsgln
      121 averfmtgsv asyvirqapc dvlvvsepre a
//
LOCUS       WP_010736531             319 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus mundtii].
ACCESSION   WP_010736531
VERSION     WP_010736531.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..319
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36502
     Region          9..184
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(12,14,88)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(41,87..88)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            86..88
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mnhtekiavl ipcyneeati ptviadfkre lpeadiyvyd nnstdntydl avvagaivkk
       61 eprqgkgnvi rqmffdidad yylmvdgddt ypaeavhgll eklrsgeadm vigdrlsngt
      121 yfeenkrafh dfgnnlvknt itrlyktkir dvmtgyrgfn rifvksfpim sagfqietel
      181 tihaldkkfk lvelpidyrd rpegseskln tfsdgfkvim miikmckdyk pilffniwtv
      241 ifflaglftg ipvirefmlt sfitkvpsai lstglmilal lslvtgmild tvvtnakkey
      301 elnlyhvyhe yhqnkkeer
//
LOCUS       WP_010736578             335 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar kinase [Enterococcus].
ACCESSION   WP_010736578
VERSION     WP_010736578.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..335
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36844
     Region          <1..335
                     /region_name="trifunc_aldol"
                     /note="KHG/KDPG aldolase/sugar kinase fusion protein;
                     NF041633"
                     /db_xref="CDD:469516"
ORIGIN      
        1 mgrvvtlgei mlrlsteqgq rlqdsdhfca hygggeanva islanyghmv sfmskvpehs
       61 lglavekhlr sygvdtslll kggprlgtyy metgigeraa sviydragss favmdrlews
      121 ledcfkgvdl fhvsgitpal senwrwltke lmeaakqagc qisfdinyrg klwtqqeagk
      181 vleqllplvd icsagemdal yllgiakape ttvnpliyyy ekmqerfpni qtfystkrtv
      241 hsasendlqg tlwmkdsyfe splhqvtsiv drvgggdafa ggllhgilee mqpqaiidfa
      301 taasalkhti hgdcnqfnqa evasfitsgs gkiir
//
LOCUS       WP_010736585             159 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease [Enterococcus].
ACCESSION   WP_010736585
VERSION     WP_010736585.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..159
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=17233
     Region          3..152
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mkkgisrlle flgaclligm iiivlwqvfs rtilgnpntv teelvrfglv wfamlssayv
       61 vgqkghlavt llsekltgkk anvleivvqc lflafaitim vyggwnavtl tmgqispslg
      121 ipmgyvylsv pvsgvliiiy slinlieamn rksvvqekg
//
LOCUS       WP_010736604             120 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Enterococcus
            mundtii].
ACCESSION   WP_010736604
VERSION     WP_010736604.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..120
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=12921
     Region          1..112
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mvkrgdiyfa dlspvvgseq ggtrpvlviq nnlgnhfspt vivavitakm akpklpthig
       61 ikatgtgier dsvilleqir tidksrlkek vchlersiml dvdralkisv giealvpvsk
//
LOCUS       WP_010736660             102 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Enterococcus].
ACCESSION   WP_010736660
VERSION     WP_010736660.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..102
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11612
     Region          1..88
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 miksitvhel yfvyqkkdvv ildvrktney ikkhlshsis ipitslpaql nnldtkkqyy
       61 ivgasnhsaq eitsylieng lqatyvidnm klfesrelts pl
//
LOCUS       WP_010736781             287 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DegV family protein [Enterococcus].
ACCESSION   WP_010736781
VERSION     WP_010736781.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..287
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=32093
     Region          1..281
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 myqivtdscc dlpyqvlqaa kvdylsmkiq ldeeelvddl gktfnydhym eqlrngatpt
       61 tsqinvgqyl effrpyveqn ipilyvafss alsgsyssal qavellkeey pdpqvkvfdt
      121 kaasvgegll vleavrlkne gktleenlew lennylkvhs wvtvddlkhl erggriskts
      181 atlgsilnvk piitvdqegr ltniskvrgr nksiqkivee tvktivaple qtvyiayagd
      241 lesaektkql leenikmkev klyplgptia shtgygciai fsmgitr
//
LOCUS       WP_010736782             540 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus hirae].
ACCESSION   WP_010736782
VERSION     WP_010736782.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..540
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60886
     Region          4..527
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mitvndvslh fsdrklfddv nikftpgncy gligangagk stflkvlsgd lqpstgtvsm
       61 gpdermavlk qnhydyeeyt vletvimghk rlyevmkekd aiymkedftd edgiraaele
      121 gefaelngwe aepeaavllq glnipeelhh qlmseltggq kvkvllaqtl fgkpdvllld
      181 eptngldiqs inwleeflie fentvivvsh drhflnkvct hmadldfgki klyvgnydfw
      241 lessqlaakl qananakkee qikelqefia rfsanasksk qatsrkkmle kitlddiqps
      301 srrypfvgfk pereigndll qvenvsvmid gkkilndisf nlskedkvaf vaenditttt
      361 lfkvimgeit pdtgtvrwgv ttsnsylpkd ttkefdnelt ildwlrqyas keeddntflr
      421 sflgrmlfsg eevlkpvnvl sggekvrcml skmmlskanv lvlddptnhl dlesitalnd
      481 glmaftgsil fashdhqfiq tlanriiavs dkgvidradt tydeflenkd iqkqledlwk
//
LOCUS       WP_010736807             334 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010736807
VERSION     WP_010736807.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..334
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37213
     Region          6..319
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msdnqlldvq nlhtgfrlkd eyydavddvs ftldkneila ivgesgcgks tlattimgll
       61 dpnntkitge ilyndlnlie lnetlynkir gndigmifqd plsalnplmr iedqikegls
      121 yhtkmnaeqr qaralelleq vgipnparvg rqyphelsgg mrqrviiaia iackppivia
      181 depttaldvt iqaqildllk dlqeetktgi ilithdlgvv aemadrvavm yggqfvevag
      241 vkelfenpkh pytrsllnsi pqegnheael hviegvvpsl knmprtgcrf apripwipas
      301 dheenpvlhe iapnhlvrcs cykhfhfrde kgev
//
LOCUS       WP_010736842             451 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Enterococcus].
ACCESSION   WP_010736842
VERSION     WP_010736842.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..451
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50110
     Region          3..449
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mveeqqelqr glknrhvqli siggaigtgl flgagktiql agpsillayl itgcvcffim
       61 ralgelllsn tnnhsfldfv aeylgkkvaf vtgwtywfcw vaiamadlta igmyvrywvp
      121 gvpqwlpeli alilllglnm vavslfgele fwfalikvvs iiafiivgiy milthyktsa
      181 gpasitnlws hggffptgtk gfilsfqmvt faftgielvg lvagetknpe kvlpeainni
      241 piriilfylg slfvimsiyp wnsldannsp fvevfseigi tvaaslinlv vlsaaasacn
      301 saiystgrml rslsqegsap kkfrqltshr vpgnalvfst ivifisviln yvmpsevftl
      361 vssiattcfl fiwgilvyth lkyrksmlgk kehtfkmpfy pysnflvfay mificlvlfl
      421 gkdtrialll tpvwfiglli iyrmkyekqs l
//
LOCUS       WP_010736852             461 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MATE family efflux transporter [Enterococcus].
ACCESSION   WP_010736852
VERSION     WP_010736852.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..461
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49895
     Region          11..412
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mrdltkgspa klilmftvpl lignvfqqfy nmvdmiivgq tlgknalaav gatgsltfli
       61 lgfaqgltag laiitaqryg akdyrglkks faasvvislv vtialtvlsl vfirpmlqlm
      121 qtpveiidqa qtfisiillg ifasmsfnll snviralgds rtplffliia vvvnvvldli
      181 fiisfgmgve gaaiatviaq vcssllclvy ikkkipllql rkkdfhfdke eirvhlnaal
      241 pmafqssiia igaivlqaal nslgtdvvaa qaaasridqf anqpmmsfgi aiatftaqny
      301 gakeygrilk gvkqtlmmsi gfsivagaiv iffghslmql fvsptetrvf elaqtyfnin
      361 gslywilail filrytlqgl gqskiptlag mmelvmrsfa aiiltgllgy tgaaaaspla
      421 wagsvavlly sylrsmkqlk sfeneqqyam ddpeiqynsi q
//
LOCUS       WP_010736860             450 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
            ligase [Enterococcus].
ACCESSION   WP_010736860
VERSION     WP_010736860.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..450
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=48928
     Region          1..447
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mkltvqeiaq avgsvmndlt eitgvefdsr kiekgglfvp lkgardghef iqqamdngav
       61 atfwsleatk apsgirvilv ddplkamqdl akyylakvga evvaitgsng ktttkdltas
      121 vlaqkyktyk tqgnynnnig lpytilhmpm dtekivlemg mdhareitel sliarpkvaa
      181 itmigeahie nlgsragiaq akmeivdglr edglliipee epllkpltes ltqkietfgl
      241 ntgelqaevt seektathfi vndesfmipl pgsynvtnal iayavgqffg lpteairlgl
      301 asvtvtqnrt ewlsagngag ilsdvynanp tamglvldtf anlptkgrrl avladmlelg
      361 pdalkmhasm aehldpadfa gvylygpqmk alyeklneky pdlyvqyfet dkeqliatvk
      421 eeirpedsiv lkgsngmgli dvvkqlqgmk
//
LOCUS       WP_010736868             878 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus hirae].
ACCESSION   WP_010736868
VERSION     WP_010736868.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 878)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 878)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 878)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 878)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..878
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..878
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95056
     Region          6..869
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mddfkktvke lesetkttie qglttqeaek rsqeqgknkf eeapkeslak kflrslsdft
       61 tiillvaavi sfytafateh gdlfegllii aiviinsvla ivqegnaeka leslqdmnkq
      121 tatvirdgkv ekvdaehlvv gdvlvlesgs aiaadarlve tsqlrveesa ltgeseavek
      181 dadyvsqedd algdqinmvf kgctvaagrg kaivtaigmk temgkiagll ndntaqktpl
      241 qirlnqlgkr isfialaaaa lvfiigelqg epllemfmts islavaavpe tltvivtltl
      301 aygvqkmakk haiirqlpav etlgtanvic sdktgtltqn kmrvrrvwsk edevtdveds
      361 mtnsameilk maalctdvtv ekendelivk gnpteaaivr aveenyhtke eleekyprva
      421 elsfdsdrkm mttvhqmgek yisitkgafd vlasrftsgd ieqativnds fgkkalrvia
      481 vgyatykeep qeitsealek dlrligligm idpprpeskg aikrakkagi ktvmitgdhv
      541 vtasaiakel gilsnpaeal sgselqalsd deldervkdl svyarvtped kirivkswqr
      601 tgavvamtgd gvndapalka sdvgcamgit gtdvaqsasd miltddnfat ivdavsqgrs
      661 vyqnirkain fllscnvsei fivliamlvg wgapftavql lfvnvvadgl pgfalgrepa
      721 ekgimdeapi pknegifarg llqkiainat iftivtlfgy ylgsyvdtis pwvdagqevg
      781 qtvaflvlay ssilhvfnvr ssqsifkvnl atnksllema vlslvittvi allpftqelf
      841 glvhvslnhw llvgflsvvp vavnelikfh qlpeaeee
//
LOCUS       WP_010736923             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endonuclease/exonuclease/phosphatase family protein
            [Enterococcus].
ACCESSION   WP_010736923
VERSION     WP_010736923.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..277
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31934
     Region          4..273
                     /region_name="RgfB-like"
                     /note="Streptococcus agalactiae RgfB, part of a putative
                     two component signal transduction system, and related
                     proteins; cd09079"
                     /db_xref="CDD:197313"
     Site            order(7,39,151,185,187,238,265..266)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197313"
     Site            order(39,265)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197313"
     Site            order(151,187,266)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197313"
ORIGIN      
        1 mkmmtlnths wleespeekm rqivdkicqa dydvialqev nqlitsesiv neelnkfcpv
       61 ieqspvhvdn fayclvryla kqgkdyywsw emshvgygiy eegnallskt pltseaiyvs
      121 etkqkedyht rkilicqtmi ddqtitlasc hfswwidetk gfafewhclm ehlanlsnpl
      181 flmgdfnnpa geagyrlvek splaivdsyt vaqevhgqat ieqkidgwet nteqlridyi
      241 yvpqefsvpf yrsifdgkqe iivsdhygve itvspiq
//
LOCUS       WP_010736978             241 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [Enterococcus].
ACCESSION   WP_010736978
VERSION     WP_010736978.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..241
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=27287
     Region          1..229
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrldkfladv glgsrkevka likkghikvn dqtiksdkfq vdewkdqvty egeqfiyqkd
       61 fyyilnkpag visatqdnyd qtvldlfddt syredlfpvg rldkdtegll vvtndgglah
      121 rllspkkhve keyfaevngi mteadvqafs qgltidggee trpaqlsivs vnsedetsvi
      181 hlilhegkfh qvkrmvkavg kevtylkrir mgnfllpedl algeyrpmta eevkqlegke
      241 m
//
LOCUS       WP_010737009             439 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Enterococcus].
ACCESSION   WP_010737009
VERSION     WP_010737009.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..439
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48785
     Region          2..434
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 merttmkktl tnrniqmial ggaigtglfl gsakaiklag pavlltyfvc glaiyglmya
       61 mgelflsnne fqsigdfiqy ylgerwaflv nwtywlcwmg aglteltaig lyirfwlpal
      121 splisgifal ialviinvva vrwfgelesl fstikifgil lfillgigvc flyfksprig
      181 vrenfdqlqt ifpfgltglv aafpmvlfsf agvemigltv getadpqknl kkaiqclpar
      241 ilffyigtiv aillvvpwqs ldlkesplvt mlqfihcskg agvinliilv aslsstnsai
      301 ystsrilynt akeknlskwf ltlssrgvpl hgilftggmf llglclhffv sdsrilfqll
      361 agmttisflf vwsailfahl kltksqlkkw kdrlilcffg lvgislffep ttrvipvvsv
      421 vwfgalnliy qrirqtspk
//
LOCUS       WP_010736730             235 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: XRE family transcriptional regulator [Enterococcus].
ACCESSION   WP_010736730
VERSION     WP_010736730.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..235
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26654
     Region          3..69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          127..234
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mkknilgsvi kdarkkkklt qeqlskltgy sqntisnhen gnrsldedni ktyataldlt
       61 pddlfealdi knslenkmmi idkkqtkidn lldlysqlee srqtkvynfa eyqlreqnkr
      121 pkttieirgy vsagtgewle deivdevsye gvipehdfav kvngdsmlpl fedgqvifik
      181 stsdvrdgqi ivcqvnneaf vkklsgnklv slnkkyedis icdtddfkiy gvvvl
//
LOCUS       WP_010737017             437 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Enterococcus].
ACCESSION   WP_010737017
VERSION     WP_010737017.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..437
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45879
     Region          1..436
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mkekllsyfe ieklgttvrr eilagfttfi smayilfvnp tvlgasgmde gavftatala
       61 saigcilmgv larypigtap alginaffay svclgmgipw etalagvfva slifilitif
      121 klremiidai padlkyaisg giglfiaflg lneggvivsn estlvglgsl svgstwltif
      181 glvvtailli rrvpggifig mvastilglv tglipmpsql vsaapslkpt flvalkhigd
      241 inslqmwvvv ltfllvtffd tagtlvglan qagfmkdnkm prvgkalasd stamlagsll
      301 gtspvgafve ssagiavggr sgitavttgi lflfglffsp llsvvtsqvt apaliivgvl
      361 maqslrqiew gkleiaipaf liligmplty sisdgialgf ifypitmiaa krgkevspim
      421 yllffvfigf mwilnis
//
LOCUS       WP_010737027             486 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Enterococcus].
ACCESSION   WP_010737027
VERSION     WP_010737027.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..486
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56889
     Region          77..161
                     /region_name="Mga"
                     /note="Mga helix-turn-helix domain; pfam05043"
                     /db_xref="CDD:428276"
ORIGIN      
        1 mkieqllekk eqlqvlilrd mvlhggtvgt nqlreqvnls ktsfdqyiae ipmigrmmgk
       61 kvaikrnefq vtlelaedvs lekiilflvq qslkfnllvy llehhqasiv rlatafnise
      121 ssvfrkikel nqllqefslq ikngqlygee lqvryfyyvl fqfisesqrp lflqqtpdka
      181 plilgleral ettfsqesas kiacwlgitr krllsekttf atlkekkily qkdrlyqald
      241 pvislylsrt aaeisgyepl mfysffvsfa vlseehfyqy dltrskklpt avldtyiret
      301 mlwhyrprkl kikeekavgy qlaqidnefy ffrgvmmiye pehllqqqkk mlgrslsqll
      361 erlkettltq lpakqgeeaa lsylmiqyan ilmmidfyia ksvtigidie tlpiyrvafq
      421 qfllrelkgi sgieienrrp gkkydlvitf nqedphqnyy ylsefassyd iarlkqkiee
      481 ekkakn
//
LOCUS       WP_010737041             292 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Enterococcus].
ACCESSION   WP_010737041
VERSION     WP_010737041.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..292
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31836
     Region          12..291
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mnkdrykqlk qaelgaiisi vayivvsilk ltignlanse alradglnnf tdilasvavl
       61 iglrisrkpa dtehryghwk aeniaslits fimllvglev lyssilsitd kkmespdmta
      121 aivgivsali mygvylfnkk latkvnspgl laaakdnlsd awtsigtava vfaasfnlgw
      181 ldsaaaivvg llilktavdi fressfslsd gfdqqklery kqavnnipev qsvksikgrt
      241 ygsntyvdit vtmdpnltvk eshdisdlie htlfeqfqvh etdvhvepve ks
//
LOCUS       WP_010737053             632 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Enterococcus].
ACCESSION   WP_010737053
VERSION     WP_010737053.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..632
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=73934
     Region          9..625
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 matkrqreii aylakrqqhw vtatelatfc ncttrtirnq itkineteqq iissnqgyri
       61 kqptqdnqvi qatndrqsql fltllksnhg idlydladtm flsestlknd iqllrneiqn
      121 kqlkltikan qiylegsesd krrymislly eegdyqeklk yhvqdmigtl slidlertih
      181 dvlashkiki nrysmnnivl hfaisierir qgndlksvkd fplrndatef qlcveitell
      241 sntyhihfsd aevkqlsllf iglqneyltn rkelslskiv earvietlne vlekvketyl
      301 idlqdeaffn klaihlqnly drsqyerftr nsslldikta ypltydiavy lsmlvqekla
      361 iwfnedeisf ialhigayle skkekrpklr vlvdhnnyhd feetnvqnir smlgedveiv
      421 avdhhevsvq endvyvssdr drvteingav yvhpiltrkd fakiqkrvta krksnwrkqm
      481 fhlidrfiie dlyfnqfdpt dqtpkmirek lfdrllvtgy veeefsqrme kreamsstsf
      541 psgiavphsl eqqakksals imtlqetlkw deypvqival vaisqdeake fndffemfie
      601 ivsdpinvrl lagaenftef ilkmkmlvet ee
//
LOCUS       WP_010737058             433 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 125 protein
            [Enterococcus].
ACCESSION   WP_010737058
VERSION     WP_010737058.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..433
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49141
     Region          6..430
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 maykdipksv qqfmdeitak cgeehadwat nfsaafantl lttvkrhedg ttflltgdip
       61 amwlrdstaq vrpylviake dedlasmisg lvkkqfeyin idpyanafne eangaghqsd
      121 htemndwiwe rkyeidslcy piqlayllyk ntgrtdqlnd sfvegikkal hvfkteqdhn
      181 qspytferdt trkedtlvnd grgstvaptg mtwsgfrpsd dacqygylvp snmfavvvlg
      241 yieeiftnil teetsskail eeakrlkedi qkgiedhalt knqqgetiya yevdglgnas
      301 imddsnvpnl iaapylgycs ttdeqylatr ktllskenpy fyegkyakgi gsshtpenyi
      361 wpialamegm ttedkeekkr ildllvatda gthlmhegfd vddpnnytre wfswanmmfc
      421 elvmdyfdir vak
//
LOCUS       WP_010737112             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010737112
VERSION     WP_010737112.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..248
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27010
     Region          1..241
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mseaiiniqq ltvayqgkla lnevdvmiqp kkitgiigpn gagkstfmka ilalipkvsg
       61 eisfggsllk earkkiayve qrneldlsfp idvlgvvllg typslrlgqr pgkkekeraq
      121 qalekvgmas ygkrqisels ggqlqrvfia ralaqqaewi fldepfvgid avsekkifsi
      181 lkelkaagkt iiivhhdlhk vteyfdevil lnqqliaagp vattftsenl kiaygevigq
      241 lvkgakek
//
LOCUS       WP_010737113             283 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Enterococcus hirae].
ACCESSION   WP_010737113
VERSION     WP_010737113.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..283
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30618
     Region          4..273
                     /region_name="ABC_perm_SloB"
                     /note="metal ABC transporter permease subunit; NF040927"
                     /db_xref="CDD:468860"
ORIGIN      
        1 miqsfiegmm nyqflqyalf tsmlvglasg vigsfiilrg mslmgdaish avlpgvaisy
       61 mfgfsyilga tvfgmltagl igfvtqrsrl kndtaigivf ssffalgvil isfaqsatdl
      121 yhilfgnvla vresdlqmta ivsgivllfv fifykelkit sfdpmmakay glnitlihyl
      181 lmffltlvav vslqtvgtil viamlitpaa taylltnslv kmiaisstvg vlsailgvff
      241 sysynwpsga tivlacalff llafcfspsk giffahkrli kse
//
LOCUS       WP_010737156             358 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010737156
VERSION     WP_010737156.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..358
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39474
     Region          4..324
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtkvlevknl qisfdtyagk vrairgvnfh lnkgetlaiv gesgsgksvt trsimrllss
       61 natidsgeil fkgknivdqs ekamqkirgk eiamifqdpm tsldptmtig kqvaeslrkh
      121 nkvskkegqk aalellnlvg ipeaekrins yphqfsggqr qriviaiali cypeiliade
      181 pttaldvtiq aqilellkei qtkidtsiif ithdlgvvan vadrvavmyg gkivevgtse
      241 eifyhpqhpy twgllgsmpt ldsanerlya ipgsppdlln ppkgdafypr neyalqidae
      301 eeppffelsk thqaatwlla pqapkveppe eikrrwaife ekqkanggmt nakktarg
//
LOCUS       WP_010737222             366 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FAD:protein FMN transferase [Enterococcus].
ACCESSION   WP_010737222
VERSION     WP_010737222.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..366
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=40603
     Region          50..343
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mlkkrllsfv aflslftlaa cstatkqtts esktttkilq epysdeqfll gtyvririyd
       61 egkeaalkpa farvkelgdk itinqegsei davnqqagik pvkvsddiyt llkrayeysq
      121 dsqggfdmai gavtqlwrig fddarkpaqe eidqalklvd yhkielndkd ktvylkekgm
      181 iidlgaiakg yitdevvkvl kqqgvttaiv dlggnvyvlg hsprgedqdw tvgiqdpnla
      241 rgsvlgtike rnktlvtsgi yerylevdgk kyhhlfdpdt gypfdndias vtiitdksid
      301 gdglstavfs mgvkkgleyv eselndgtea ifvtkenkvy vtdpikdtfv ldkdskytmg
      361 nrselk
//
LOCUS       WP_010737240             171 aa            linear   BCT 01-JAN-2025
DEFINITION  YjbQ family protein [Enterococcus hirae].
ACCESSION   WP_010737240
VERSION     WP_010737240.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Morett,E., Saab-Rincon,G., Olvera,L., Olvera,M., Flores,H. and
            Grande,R.
  TITLE     Sensitive genome-wide screen for low secondary enzymatic
            activities: the YjbQ family shows thiamin phosphate synthase
            activity
  JOURNAL   J Mol Biol 376 (3), 839-853 (2008)
   PUBMED   18178222
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..171
                     /product="YjbQ family protein"
                     /calculated_mol_wt=19255
     Region          5..169
                     /region_name="YjbQ"
                     /note="Thiamin phosphate synthase YjbQ, UPF0047 family
                     [Coenzyme transport and metabolism]; COG0432"
                     /db_xref="CDD:440201"
ORIGIN      
        1 mttyteqlvl tsngqrvtyh niteqvkemv aksgikngic lvqsphttcs vifeefmhdl
       61 dfngdeflqv dlnrildrii preltentny cypgpkhldf llslddpdya gdagtilngd
      121 ahirasffga senfivkeet lmtgavgsiy fidfdqnrvr nrkchilvmg e
//
LOCUS       WP_010737242             371 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Enterococcus].
ACCESSION   WP_010737242
VERSION     WP_010737242.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..371
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42397
     Region          160..369
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msffekhiff pkrfgiapyf wlvfliptiy slfpltswfd wlfilllvif lkayrdgyev
       61 hkfltgdvfl qlliaclfgi fqkngylfif vaweigslpv tkrlfyhylt gyyvsvmisl
      121 gamlwttrft hsssyinvgi tiiaaiitpl aaksvgesyr riyrlnqqnk rleavvrqne
      181 rdriardlhd hlgqafsiis lkaelaekli aidsrqatne lhdiaetsrk nlslvrgivs
      241 nlqertiaqt mleeeknlvl tniqlhsvge elaekwptni qhtvsavike aitnmirhsk
      301 asiamidfte nidtyfitiq dngqgftqlk stgygisgmk eriqtekgql titgtqgvki
      361 vislpkeneh d
//
LOCUS       WP_010737300             315 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar-binding transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010737300
VERSION     WP_010737300.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..315
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35362
     Region          11..311
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mskseernmv kvatlyykeg ltqaqiakkm gvsrsliskw lidarkagfi effinseniy
       61 aieletelek kfalsfvkvv dttnlsypei ekmvgqiaai slkdkiaaak tigiswgksi
      121 kslvtqfpfe nypdttfipl iggmgydhfd ihsnqlchef arktrgssky lytpalvsne
      181 iirqefegni yidkilseak kvelalvgis spdhfntmee igytnkkema qlrgigavgd
      241 insrfydkdg qevnhpinkh vvglsleelk aipetiaiay ddakwqgiyy acknqlvdsi
      301 ittdtiadhl ihmdi
//
LOCUS       WP_010737334             258 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphatase PAP2 family protein [Enterococcus].
ACCESSION   WP_010737334
VERSION     WP_010737334.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..258
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=29282
     Region          26..203
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(106,113,129..131,173,179,183)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 msdyqqkalk lsivplclli glilcvkinp pwfetldlav ytkidlpnfp qlttivrlfa
       61 klatigptlc faflfafyiw kknyhllaiw nicnifavsf fgyilkklia rirpavsqle
      121 irtsysfpsg hsllsfalfl tiilslsiiw srqdtrrvaw yfisypllia atrlylrvhy
      181 psdilagfsl savvvllsyv vcfsfistds ilktrqlekk ktlfskkqkv vlgllvllla
      241 viisgvayel nvfyhahg
//
LOCUS       WP_010737385             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010737385
VERSION     WP_010737385.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..255
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29103
     Region          2..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 metrrtsdll sylvkkkqat skelcthlhc sistlrrell elekrklirr twggailnet
       61 tnmeytylqr easnipekki iselardfia pgmcifldss stvlhlipll vkipnliiit
      121 nglrtalkls ecqneslkiy ltggevklna stvisntldp itssfrfnaa flscrgldhe
      181 giyeanfnqa qikkemmnka qeivlladet kfdsthffki gdyydydaiv tnkkppkiyh
      241 riiekndihl vypte
//
LOCUS       WP_010737401             221 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YitT family protein [Enterococcus].
ACCESSION   WP_010737401
VERSION     WP_010737401.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..221
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23920
     Region          2..>190
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mkkinllidl vgisfgaaly glavtginip akladggvtg ialllnnlfg fapsitslii
       61 nlplllvslf ifgkqsflrt ivgtfalvff lhlweglnvh favhslllns lmtgvlsgig
      121 cglvfrfggs tggtdiiyqa fekyfhikig kslflitfgi lvvsllyldv thfvytllsc
      181 silsytlnkv kylevkgsln pfsanrskep fdtldsaeqf e
//
LOCUS       WP_010737423             317 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aromatic acid exporter family protein [Enterococcus].
ACCESSION   WP_010737423
VERSION     WP_010737423.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10369318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..317
                     /product="aromatic acid exporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36460
     Region          1..141
                     /region_name="FUSC_2"
                     /note="Fusaric acid resistance protein-like; cl19401"
                     /db_xref="CDD:450298"
     Region          147..306
                     /region_name="ArAE_1_C"
                     /note="Putative aromatic acid exporter C-terminal domain;
                     pfam11728"
                     /db_xref="CDD:432028"
ORIGIN      
        1 mrigmrtvkt vvssmlsmvt aqmfsllfwp sagiiallsv gntkrstlrt gmlritafil
       61 atviafisff ifdytilgfg lflllfiplt vglkltdgiv vnsvlvthyl seknmswsli
      121 gnaaslmaig vffalvaniy mpdikkqlqk nqqlieeefr iilnnmadfl ltgrntnnql
      181 lcdkllafvr esqsdarkyq enywvkqtqy yetyfsmrrt qinvikdmqg nldriqdpvp
      241 ygkhiygllv ytaetfsekn dgkellkrie evyelyrdma mpkerlefed raelfqflqs
      301 fksfieikae fsqqsig
//
LOCUS       WP_010737453             388 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Enterococcus hirae].
ACCESSION   WP_010737453
VERSION     WP_010737453.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..388
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=42524
     Region          3..383
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mpkkvkkrhl lnysilipyl ilcilglimv yssssyllle ngsspsasff nqslfwgvsl
       61 vaigllykmk tsvlknqrli maaiavltil llivlffgke ingakgwlqi agfslqpaey
      121 lkiiviwyla ltlskrqrsv qkdfvstvkr plllvlalta lvailpdfgn atvifliilv
      181 lllasginyv ytlivggggv glsalaiwli nithgkifpg rlqyiynrfa iyqnpfsdel
      241 nkghqlangy yamfngglfg rglgnsiqkk gflneaqtdf iyaivveelg vimgililal
      301 lffmivrifl vgirskdpfn sllcigigam fmiqifinlg gitgvipltg itfpflsqgg
      361 ssllmlsicv gfvlnisade krkslgly
//
LOCUS       WP_010737481            1176 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Enterococcus hirae].
ACCESSION   WP_010737481
VERSION     WP_010737481.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1176)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1176)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1176)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1176
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..1176
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=137527
     Region          4..1159
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mslqfilgta rkdhrtalid esvewlakds mhqvfflvpn ynkfeqeqei ltelrqrsgk
       61 tsfsttnvqv fsfyrlawyl lqqttllsgn elsesgsami lrqileknee nltifrgein
      121 kkgfirqlqe lhnelrigni spedlvfsel adtvkaenqq lkmkdlqlif tafeeelvqr
      181 alqsedalti lanylqtqdm skvkfivsgf trvnaqeyql lqvmmekgql vidllldrpy
      241 itdmpevltl fhetgklyfq linsakerrv pvlvekfape herplalmhl qkmweetssn
      301 kksqplkvgq qealriweae nateevrqla veirrlvsee nyryrdiqvl tkdmafygnl
      361 lqpvfkemai pfyideeqlm enhpliewin slfaldryay rlndimrffk telficeadd
      421 tldlaswreq rnqfrakldv tenvalayny qgsywtrekd wqfvsydfea eqledvqele
      481 krsndirhff kekvptffdk ikkckngqeg atvfyrflvn sgvqqqlvfw rnqeiergnl
      541 aaarnheqtw galidlldey sliygesefd whlfqeiits glenlsygki ptaidqvrin
      601 rlelvrsnqa kvtfaiglnd qvfpdrhetk gllsseeret lnarlakekf lfdpakenls
      661 feplqaylvf asatqrlyls yaqsydtntl kispylkrim eylmipaerk ehlvldsdps
      721 cyigtyrsgi ntinhiyrla keekkkvpvy wrqlreqilq sqwrnfalri fesqehlnvp
      781 vslpkkmaee lygkdiytsi srlenfynce ykyfvqfglk lkermvyglt paatgdfyhe
      841 sldrffkllf snqislvemt dtqrkeftek vlqdvfgelr feildssarm nyiryqlgqt
      901 iqkvawalqk qskntgmkpl qteilfgqia gaqgipglel plnnggklhv rgkidrvdva
      961 veqadtwlsv vdykssgrsf dvteayygma mqlltyldva lmdavkltgk alvrpagsyy
     1021 lhvhnpilse aneieketlk kfsydgifvd epellevldh sleakensli ypikknakdv
     1081 yqkgsfskek fyteqelqlf mahnranmrl agdkitsgei klnpaykdke rlacqmcpfr
     1141 svctfdvmlq ennyhrlekl nkeealrrie krseee
//
LOCUS       WP_010737526             379 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Enterococcus].
ACCESSION   WP_010737526
VERSION     WP_010737526.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..379
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42916
     Region          17..295
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mskeqktisg qertkkgiia gilglitnil lfvakfaigl fsgsvsimad ainslsdtas
       61 siltlvgfki aakpadqehp fgherfeyis glfvsiiity vgfqfldasi rkifrpehlv
      121 ltpivflvli fsillkllqg rmytrfskti qsealkatak dsyndvfttl avlvsagier
      181 ftgwridgyv gfvlagyiif sgimmlrdfv yellgsrpta eeiktmekql ssyksilgfh
      241 dllvhnygpn kkfasvhiev ddslnlneah kiidiiekdf kktldvdlvc hldpvaihne
      301 qyrkilkqlr qiikelgeel rlhdlriirk gkelqfdivv pqnfklpddv leekirqaie
      361 kkvgsfeldi tfdhnylly
//
LOCUS       WP_010737570             339 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Enterococcus].
ACCESSION   WP_010737570
VERSION     WP_010737570.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..339
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=40051
     Region          20..291
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdqktrkhiq eklkqriaql ppifqeflke nqkklslssr yeyakdfhlf tdylhealdq
       61 eitdevilrl ekqdylnfld kvyqhtrsfq ttadqqtnql fknsyyglsr kqyslnhflr
      121 flyqkgllte eisllgktlp ettaaaprfi daslfqdfeh lfipmngfns srearfeirn
      181 rprnlaiaai llycglkihe vvelkrkdid lnkqiihlsr kknrlnqspi pnealpfikn
      241 ylaitdtgtg pdsfafrssh dqqisprtir qilskitvyk nispelcrkt ygyyvslyfd
      301 dldivnflyg nryinehsfe evqqkmlefs ykeitsnkk
//
LOCUS       WP_010737572             266 aa            linear   BCT 01-JAN-2025
DEFINITION  hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
            [Enterococcus hirae].
ACCESSION   WP_010737572
VERSION     WP_010737572.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..266
                     /product="hydroxymethylpyrimidine/phosphomethylpyrimidine
                     kinase"
                     /EC_number="2.7.1.49"
                     /EC_number="2.7.4.7"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008902 - hydroxymethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008972 - phosphomethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=28667
     Region          3..246
                     /region_name="HMPP_kinase"
                     /note="4-amino-5-hydroxymethyl-2-methyl-pyrimidine
                     phosphate kinase (HMPP-kinase) catalyzes two consecutive
                     phosphorylation steps in the thiamine phosphate
                     biosynthesis pathway, leading to the synthesis of vitamin
                     B1. The first step is the phosphorylation of...; cd01169"
                     /db_xref="CDD:238574"
     Site            order(3,10,12..13,15,19,22..23,26,29..34,36,39..43,48..49,
                     51,53..54,57,60,64..65)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238574"
     Site            order(9,21,42,78,212)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238574"
     Site            order(103,140,174,209,211)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238574"
ORIGIN      
        1 mrkiltiggs dpfagggiqs dlktfenfql fgmsaltcvg mldennafll enlpakwleq
       61 qlasiqkmtd lagikigllh sleaiiivrd flkkhpqipi vldpvlafke ttslanqqyi
      121 eclvkelfpl vdlvtpnlke aallsgkkki ssineviett kfihtlgska vvvkggsgih
      181 gdeaidvlys hdglttftme kltrstvnga gctfssaita nlvhgytlpq aiqrsktyvy
      241 qcilngvemn dqtgsvwsgg nikggi
//
LOCUS       WP_010737601             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Enterococcus].
ACCESSION   WP_010737601
VERSION     WP_010737601.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..290
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30626
     Region          <100..279
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mvqlllglls vlllyflfff vldllankgn wgggnylisg tiglitdfld tlgigsfapt
       61 tmlleftkql dndrqlpgtl nvahsipvii eafifitvvk vspitlfslv aaaivgsfvg
      121 sktvsklpek kvqffmglal ivtailmglk qagmldllgs gneataltgl kliigvignf
      181 llgalmtigv glyapcmalv ymlglsplva fpimmascag lmpvasgnfi ksgdyarkvs
      241 laitiggvig viiavkfvts ldlnmltwvi iaviiysgit ymrkgmfskk
//
LOCUS       WP_010737617             129 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Enterococcus hirae].
ACCESSION   WP_010737617
VERSION     WP_010737617.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Song,F., Zhuang,Z., Finci,L., Dunaway-Mariano,D., Kniewel,R.,
            Buglino,J.A., Solorzano,V., Wu,J. and Lima,C.D.
  TITLE     Structure, function, and mechanism of the phenylacetate pathway hot
            dog-fold thioesterase PaaI
  JOURNAL   J Biol Chem 281 (16), 11028-11038 (2006)
   PUBMED   16464851
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..129
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14099
     Region          7..124
                     /region_name="PaaI_thioesterase"
                     /note="PaaI_thioesterase is a tetrameric acyl-CoA
                     thioesterase with a hot dog fold and one of several
                     proteins responsible for phenylacetic acid (PA)
                     degradation in bacteria. Although orthologs of PaaI exist
                     in archaea and eukaryotes, their function has not...;
                     cd03443"
                     /db_xref="CDD:239527"
     Site            order(36,65,72..75)
                     /site_type="other"
                     /note="CoenzymeA binding site [chemical binding]"
                     /db_xref="CDD:239527"
     Site            order(37,39,42,66..70,72)
                     /site_type="other"
                     /note="subunit interaction site [polypeptide binding]"
                     /db_xref="CDD:239527"
     Site            order(38,46..47,50..51,65)
                     /site_type="active"
                     /note="PHB binding site [active]"
                     /db_xref="CDD:239527"
ORIGIN      
        1 mnlieylqie tmsiskeqve lllpisdihl qpfgflhggi ngilietacs iganqhlssp
       61 qyavsvdlhv nhlnsaqngq lrviarptki grsiqfwaae iylekenept pahliangsc
      121 tltvrnest
//
LOCUS       WP_010737630             383 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Enterococcus hirae].
ACCESSION   WP_010737630
VERSION     WP_010737630.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..383
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41424
     Region          1..380
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mefigilcli lvattigshi srrfgipavi gqllvgvllg qaglgwvhpn ilvhdfseig
       61 villmflagl esdlsllkky fkpgmfvall gilfpvffgw ltgeafqvan neaiffgiil
      121 aatsvsisve vlkelnvvnt kegstilgas vvddilvvlv lsfslsfltg kstsnlplpl
      181 llleqlfyfl fifllvkwia pflmslaeki yansaiiims lviclgmsyl adliglssvi
      241 gaffagiavs qtkvkhevyn nvealgyavf ipvffvsvgl evdfskfseq ilfililtlv
      301 ailtkliggy igakfssfss nsalmvgagm isrgemalii lqigqqsnli enhyysplvi
      361 vvllstlisp lilkyftkkv yan
//
LOCUS       WP_010737635             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FtsW/RodA/SpoVE family cell cycle protein
            [Enterococcus].
ACCESSION   WP_010737635
VERSION     WP_010737635.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..397
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=43680
     Region          2..378
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mwknrkidwl ilgpylalsi vglleiysas syrllvagsd pkslfirqfl fiilswgviv
       61 ltysirlqvl lkpriikagl ivsglllamm klgifavtvn gaqrwvsiag iqfqpseiat
      121 iflilylsrf frndrsvpek lhipvlivgg iavlvlfqpk iagalmilai agaifwaaai
      181 pikkgliiig aaiaslilva glvlllekhh llpsffehay driamvhnpf ldehgagyqm
      241 snsyyalyng glfgrgmgns itkkgylpes etdfifsvia eefgligall vlfllfllcm
      301 rifqkstkqk nqqanlilig vgtwilvqts inigsilgli pmtgvplpfv syggtsylil
      361 sfaiglalni ssrqvkeknk qverlqlkkp kllnknn
//
LOCUS       WP_010737637             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Enterococcus].
ACCESSION   WP_010737637
VERSION     WP_010737637.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..256
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=27845
     Region          67..255
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          67..94
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          97..127
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(98,102..103,106..108,110..111,115,118,127,163,165,
                     169..170,173..175,177..178,182,185,195,197,199,203..204,
                     207..209,216..217,221,224,233)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          163..195
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          197..233
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mkpysilwlf ptllvfagca dhssqsngtn tstnsivlds tasvplptnp nhpskeetpm
       61 siapgrllqa vsaedlnlvq tlldqstami deqnekgesp lliavhhnmi diakilvdhg
      121 aninlqdhiq dspylyagaq gkteilayml ensepdqsiv nrfggnalip aaekghlanv
      181 kllltdgrvd idhqnhygyt alieavalrd gskiyqdivr ellahganke lrdnqgktae
      241 dyarelgydq llsqlt
//
LOCUS       WP_010737699             450 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010737699
VERSION     WP_010737699.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..450
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=49070
     Region          1..423
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mekleaflgs kllplsqklq qnkvlaalme gfirtspitl gialitivgn fpipgwidyl
       61 tslgiyphve aitngatgvf slyvvyslaf syakqlgtne rnaaiislas fvmlmpqtva
      121 tmamqngeav dstiaalrld flggqglfig mivalvvtql yaylskkniv lklpdsvppm
      181 vtqslapvfv vtiifvfvfi lrilfgltks gsifqffidv inaplnalva splsiiiime
      241 vlavlwffgi hnavlqgplg aismtmvvsn iaafqkneal pylipsviym gmyaagfmgf
      301 vtffmirsks akmkqlgkls vipaifnite plmfgmpiil nplffipqvf tqliagfvtw
      361 gltttilpis lnpmisllpw ttptfvkmpl sgginytilm vicmgigilm wypfikiadk
      421 keyelelkae aeakeakekm agviaeevqa
//
LOCUS       WP_010737708             745 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha-galactosidase [Enterococcus].
ACCESSION   WP_010737708
VERSION     WP_010737708.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 745)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 745)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 745)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 745)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11245829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..745
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85831
     Region          41..298
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          302..648
                     /region_name="Melibiase"
                     /note="pfam02065"
                     /db_xref="CDD:307952"
     Site            order(349,380,424,489,493,539,558,561)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          661..738
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 meqvmknqrv alitfdeqek vfhlsnseis yilqieesev lahvyfgkrt thyhnhkkyp
       61 rrdrgfsgnv plnedrtysk dtlpqeysgh ggmdyrlpal mirrengsnl ldlryesfqi
      121 qegkpnlsgl pqayikndte aetlivtlkd reekiyvdls ytiyreravi trslkvrnet
      181 ndpvmiekaa sfqldftnsg rfdevialpg ahvkerqmsr qsitdgiksf esrrgssshq
      241 mnsfialtnh atteftgeai gihlvysgnh sfeiekdaiq qfrvigginp ynfswelqpy
      301 esfqtpeill tysdqglngm sqvthhllre rvargrfqyq erpilvnnwe atyfdftskk
      361 ieaivdeane laiemfvldd gwfgkrdsdq sslgdwfeyq gklknglkgi adyvhqkglk
      421 fglwvepemv ssdsqlnrnh pefmmkepgr qpsasrsqhv ldftrkevrq tietqlrhll
      481 dsveidyikw dmnrslsdvy svslgkqnqg evlhryllgl yemmenltnd yphilwegcs
      541 ggggrfdagl lyympqswts dntdaverin iqygtslayp isamtahvsa vpnhqtgrvt
      601 slktrgdvam ggvfgyeldl tklsseekqe vaaqvefykk irqtvqygdf yrlqnpfeqn
      661 iaswefvskn qqevllfinr rlanaqpefh evrlvglsee klyqnqidgk vysgselmti
      721 glyfpdfygd fqtelihfms idege
//
LOCUS       WP_010737725             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010737725
VERSION     WP_010737725.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27858
     Region          1..242
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlteerrqki lhlleqnkiv ksqdlvtlln asestirrdl qelendglle rihggakkgq
       61 llgfeqnmse ktlknvqekq tiarlaaqli ndddviylda gsttlemipy lqekkvtvvt
      121 nsvkhaaslv dlqlptiilg gqvklstnav lgnstisqlk nfyfnkvfmg mngvdlnrgf
      181 ttpdpeeaav krlamanaee sfvlidhskf nklsftsvap leaativter cplefvadyr
      241 erttikeaai q
//
LOCUS       WP_010737750             176 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010737750
VERSION     WP_010737750.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..176
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20245
     Region          4..83
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mmnelfvlge lmespqngyh lrnamqaslg knrkvsfgvl yplldklakn glititvnee
       61 grtqktasit dkgrqrffel mkqdvpsgah teeiylikld smqhlsldeq kellmvyire
      121 kqitvdeikg ylkkldevkk idhwyatkkl elllgkaqla iqwaedflse lpyvee
//
LOCUS       WP_010737758             573 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Enterococcus].
ACCESSION   WP_010737758
VERSION     WP_010737758.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 573)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 573)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 573)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..573
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=67429
     Region          164..569
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mtksmtrikh nllkhafyry mlwmsvsllv lffiiylitv sfhqkrdenl keinlnfyte
       61 immmknatdn mlallyaeqp dledlrqitn lslaeyyeyk tttymkhags kyngtqnfvn
      121 qsfkmndyls tvviyhaqtk rsvvfqkdqt ttmkkvdefh ladpndiekt kkqifkinkn
      181 rnligfhkel hketdlsyaa dvyfyynisp lfekihyqvl rnngniqvfy knkpippeik
      241 pkyvldqrqa ehyvvtattk yanvfteysl iytvysffai lvflgffpfl fqylqkiegr
      301 lsqltqkitk vktgnfdpek faqsddyksd daislisssi delayqlndq ihqvykskik
      361 qkdyqiqsir sqinphflyn tleairmkae lnedhavagm llnaatlyrk likgkdvicl
      421 aeeleycday lslfeirfed alfydivcdp sleslliekf tiqpiienfi hhgidsqrqd
      481 nfieihcfek ddrlyievvn ngkpipkvek qriqkqlaqn shdlemtapt glfgvdyrik
      541 qrfghqygvt fttqedyvkf qitmpkkrgg eiv
//
LOCUS       WP_010737780             266 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Enterococcus hirae].
ACCESSION   WP_010737780
VERSION     WP_010737780.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..266
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29184
     Region          1..266
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mkqrvitaai alvlfipiiw iggitiefva allavvgvye lfrmkgltll sfegilsaig
       61 avilvlpker wffflpekts tfmifylivm illgtsvisk ntytideagf pvitslyvgi
      121 gfqnfvnart eglavllfgl fvvwatdiga ymvgrqygkh klspdvspnk tiegalggit
      181 salvvallyf lfypakelfg hglffmllvt mllsivgqfg dlvessikrh ydvkdsgnil
      241 pghggildrf dsllfvfpim hlfgli
//
LOCUS       WP_010737785             262 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus hirae].
ACCESSION   WP_010737785
VERSION     WP_010737785.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..262
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31150
     Region          1..226
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 misviiptfn aeksieravn svlrqsyqdf eiiivddrst dhtwelltkl kkqdqririy
       61 qnarnsksay trnqaikhar gnyimqlddd dychvermak qvafleahpe fgfvgsnayl
      121 wdqegvyger vvkerpeikd llktspfinp samfrkhile svagyrvskd tvrgqdydly
      181 mrlyakghkg ynlqenlvyy yqdkeyykkn swknrlgesr lkyrnfkelq vakvhylyvl
      241 kpliaimipr hllfwhqhrk qg
//
LOCUS       WP_010737800             131 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Enterococcus].
ACCESSION   WP_010737800
VERSION     WP_010737800.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..131
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15002
     Region          31..123
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mvlwviniil lliilaivfw evylrvmakr saktleeeef rdgmrkaqvi dvrekdvfda
       61 ghilgarnip ytvlkdslgs irkdqpvyiy dqkkslsirt anklrkagyq diyilkggyd
      121 gwsgkikskk v
//
LOCUS       WP_010737807             167 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase [Enterococcus].
ACCESSION   WP_010737807
VERSION     WP_010737807.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10082841
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..167
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005542 - folic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19451
     Region          2..161
                     /region_name="DHFR"
                     /note="Dihydrofolate reductase (DHFR). Reduces
                     7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH
                     as a cofactor. This is an essential step in the
                     biosynthesis of deoxythymidine phosphate since
                     5,6,7,8-tetrahydrofolate is required to regenerate 5;
                     cd00209"
                     /db_xref="CDD:238127"
     Site            order(5,22,27,58,98,104,117)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(7,14,44..46,65,99..102)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mfismwaqdk ngligkdgll pwrlpndmrf frehtmdkil vmgrktyegm gklslpyrhi
       61 ivlttqkdfk veknaevlhs idellayakd ipediyvsgg srifqallpe tkiiwrtlid
      121 aefegdtfig eidftsfelv eehegivnqe nqyphrfqkw qkmskvv
//
LOCUS       WP_010738018             239 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Enterococcus hirae].
ACCESSION   WP_010738018
VERSION     WP_010738018.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..239
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=26410
     Region          16..238
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mlpiigiagn qliratdtfq gnqvtytpqg fvnavqqadg lpivlpissp ktasayidqi
       61 dklilaggqd ispqlyhepp hpklletnlq rdlfeaalis ealkqnkpif avcrgmqlln
      121 vvlggslyqd lttypkwsvk heqhptapqf atheveilpd tllyqllpdt ylvnsyhhqa
      181 lkelapslka tafspdglve giesldkdvr lfgvqwhpel thssnstdqg lfdffvqef
//
LOCUS       WP_010738040             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: permease [Enterococcus].
ACCESSION   WP_010738040
VERSION     WP_010738040.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..316
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=35083
     Region          5..316
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mfsfipnsvl qmstiflsiv iealpfvllg clisgalqvf ltpervkrwl pdnrflsilt
       61 gsvlgfffps cecgivpivh qfvkkgvpvh tafafmltap iinpivifst fiafgnswem
      121 agwrmvgsfv valiigiwla yfqkesvlkt kiqqtidhnh hhnhhhdhth gtnkheevki
      181 grikqlsqqt ghvlthside ffdtgryliv ggliaasmqt ylptrvmltl gstkllaiii
      241 mlllaftmsl cseadafigs sllslfgtap vvaflvfgpm vdiknllmmk ryfngrfilm
      301 ligliavsvi gftlfi
//
LOCUS       WP_010738058             130 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010738058
VERSION     WP_010738058.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..130
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15134
     Region          12..110
                     /region_name="HTH_GlnR-like"
                     /note="Helix-Turn-Helix DNA binding domain of GlnR-like
                     transcription regulators; cd01105"
                     /db_xref="CDD:133380"
     Site            order(14..16,30,47..48)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133380"
     Site            order(60,63,67..68,89,92,96,102,106,109..110)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133380"
ORIGIN      
        1 mgekelrrsm svfpigtvmk ltdltarqir yyeeqdfvhp ersegnrrmy slndidllle
       61 ikdylsdgln magikrvyem aqakkqeeks kkpltdhdvr qifrdeilaq gglsktghyq
      121 sqgmqrqffd
//
LOCUS       WP_010738121             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Cof-type HAD-IIB family hydrolase [Enterococcus].
ACCESSION   WP_010738121
VERSION     WP_010738121.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..269
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30135
     Region          5..264
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,195,217..219,221..222)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mnrkliaidl dgttlnpdsi itskteetlk kainaghhvs iatgrpfrms yhyyqqlgls
       61 tpmvnfngal vhipnqywah eketsidkri vfeilaqkrq lnldfiaaen retyfidsfd
      121 ffdekifaas npspqnllsp knlttdptsl lvrtekcyae qvsaeltrqf gnfvdvrtwg
      181 gpmaileivs kgiekakgvh rianyldidq kdviafgdeh ndlelleyag wgvamkngtd
      241 qlkgvandvt ehtnqedgla tyledllal
//
LOCUS       WP_010738088             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Enterococcus].
ACCESSION   WP_010738088
VERSION     WP_010738088.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..305
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34612
     Region          3..301
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mskkfvignf kggvgkstca qmlgfesava kkqktliidl dmqgntsdvm slthmnfpve
       61 dgggdgepld yqytitdvlv gtpplelgle kngkvnwdkv vvndtrvdpe kavykvvdnl
      121 yilpadmsfe lyddwikdqf sdssdkllym ekrlapllee fdviyldvpp sisvysksam
      181 yiadfaivvl qtqvksmrna mqyleymdff vdefdttlkv agvipfmles gdavdqemya
      241 eaqkiygdhl lknvvlknar lkrydgsgit meltkagklk qwdrrshelf iniydelveh
      301 etwye
//
LOCUS       WP_010738141             745 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Enterococcus
            hirae].
ACCESSION   WP_010738141
VERSION     WP_010738141.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 745)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 745)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 745)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..745
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83383
     Region          1..>78
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          93..736
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mlcqncgkne atihlyatvn gqrtqldycq scyqkiknqq nggltsmaqn dpfgfgsldd
       61 lfrsmsrqmq qqgnyeqtpp tqfggnnnfn ggqppqqgns egllgeygin iteqarqgdi
      121 dpvigrddei krvieilnrr tknnpvlige pgvgktavve glaqkivdgd vpqklmdkev
      181 irldvvslvq gtgirgqfee rmqklieeik qaenvilfid evheivgags agdgnmdagn
      241 ilkpalarge lqmvgattln eyriiekdaa lerrmqpvrv vepsveetis ilkglqkrye
      301 dyhhvkytde aieaaailsn ryvqdrflpd kaidlldetg skknltiqiv dpktidkkle
      361 eaqeqkiqas keedfekaay yrdqisklek mkerqltdee tpvitekdme kiveertgip
      421 vgdlkekeqt qlknlatdlk ahvigqddav drvakairrn rvglskknrp igsflfvgpt
      481 gvgktelakq lafelfgsed smirfdmsey mekhsvskli gsppgyvgye eagqltekvr
      541 rnpyslilld evekahpdvl hmflqilddg rltdaqgrtv sfkdtiiimt snagtgkvea
      601 nvgfgaareg vtrsvlnqln nyftpeflnr fdgiiefsal skenlmtivt lmldevneml
      661 aaqqlhievp tnvkeklvdl gydpamgarp lrrtiqeqie dgiaefyldh psihelkakl
      721 dkeekivits kqerlvkett neptn
//
LOCUS       WP_010738161             202 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Enterococcus hirae].
ACCESSION   WP_010738161
VERSION     WP_010738161.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..202
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22643
     Region          4..197
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mtytlpdlpy afdalepyid eetmhlhhdk hhntyvtnln aaiekhpelg ektieellsd
       61 mdavptdikt avrnngggha nhsffwkima pnaggeptga ikeaidetfg dfatfkeefk
      121 kaaagrfgsg wawlvmengk laitstanqd splmegktpi lgldvwehay ylkyknvrpd
      181 yieafwnvvn weevnnrlss ak
//
LOCUS       WP_010738191             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Enterococcus].
ACCESSION   WP_010738191
VERSION     WP_010738191.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..429
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48456
     Region          7..408
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnefvknfpq awqekwqekg fqtpsliqqa vfqplkekes iigisptgsg ktlayllpll
       61 lnvpkeggst llilvssqel aiqvaevare wskglalkvq slvgganvkr qieglkkrpe
      121 vlvgtpgrvl elmktkklka hqlqtivfde adqlfdegnr slveqilrqa pvdyqlvffs
      181 atadrsiski eeitnasipv vdvtkdddsr kgqqhyylri pprkkeeylr rlayvtdfhg
      241 lvffnqlnel gtmeeklqfr gvsvgslasd qnkllrkaal dqfkdkkitm lfttdvaarg
      301 ldieqlpyvv naeiplteea ylhrsgrtgr mgkdgtvitf vqdhtvkelk kltrhmaidm
      361 eeiflhggql vkelpqkels qkeeandknt kktapfgpsk keqveknstp kkklknkqkk
      421 qknkgarrk
//
LOCUS       WP_010738276             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010738276
VERSION     WP_010738276.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28323
     Region          1..227
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mdkmievkhv sksygnklsp vkvldnisft vekgefvgim gpsgagkttl mnilstinlp
       61 tmgsvliqgn eitkmknnel sdfrrkklgf ifqefnlidt lnakdnillp laveriskee
      121 meksvlhvaq llgieeilkr ypdelsvsqr qriaaaralv iqpqvifade ptgsldsksa
      181 tellnylttm nrvekstill vthdpytasy cdrilfikdg vifsevvrrg srneffervi
      241 dmqatigggg klnal
//
LOCUS       WP_010738295             327 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-quinone oxidoreductase [Enterococcus].
ACCESSION   WP_010738295
VERSION     WP_010738295.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..327
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35430
     Region          1..323
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,120,124,127,145,148..150,170..171,175,190,
                     214..215,236..237,239,262..264,312,317)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mraitikhpg saevlqeida pkpiaekgql likvhtaain rtdimrrett nqqtpypilg
       61 vevagevven rsdnpdfvpg trvcglvnlg gyaeyavmpa draillpdtl dnvaaagiae
      121 vfltayqtly wlgnlqeget vlihagasgv gtaaiqlakq ltkatvivta gsseklafcq
      181 klgadeqiny ktqdfsteva ritngkgvdv ildfigasyw eknlasiaid grwvligmlg
      241 gtivpeidla tlitkriqli gtlltprsdq ykaqltqefm qvvgpyladq rvkpiidrtf
      301 tlaqvqeahe ymeanknigk iiltite
//
LOCUS       WP_010738329             278 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Enterococcus].
ACCESSION   WP_010738329
VERSION     WP_010738329.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 278)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..278
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30385
     Region          1..272
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkvirfavv tfvalfwlag csqgkadtkt kettvklgvi gedtdvwddv karlkkenie
       61 leyvkftdyn qpnaaladgs idlnafqhqf fldnyneehg tnlvsigntv naplgiysnt
      121 ikkieevkeg akvaipndvt nggrallllq saglikvdps kgqtptisdv tendkklklt
      181 eldasqtara lndvslsvin sgvavdagft ptkdaiflep vddrarpyvn iivarkedet
      241 nrtyqkivdt yqteatakvi eetskgssvp awktfgrk
//
LOCUS       WP_010738335             691 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus hirae].
ACCESSION   WP_010738335
VERSION     WP_010738335.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 691)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..691
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78420
     Region          14..632
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mthlkklcqn rllivltasf ffwlktifay yvdfslgveg siqyfilwin piattllffg
       61 lalyikklkp alivlliidi lntlllylni ifyreftdfv tvksilgfsk vsqglsgssf
      121 almrphdily wldilvfvgl iiwmfvkkip vkspavskpv aiavtclsal ifsgnlalse
      181 anrpqllqrt fdrsyivkyl gidaytiyda iktgmtssvr ahassngvee vrkytenhya
      241 apnpatfgva kgkniivlhl esfqqflinm kvdgqevtpf lnsiyknqst isfdnffhev
      301 gqgktsdaen mletgtfglp qgslftelgs dntfqaapai laqqqgytsa vfhgnvgsfw
      361 nrdhvyknlg ydnffdrsyf nssdetlgyg ildkdlfres akylehlqqp fytkflsvtn
      421 htpyytddkh fnfpslktgn srvddyvrta hyldqsleqf ftylkksgiy qnsmfviygd
      481 hfgisntdnk dlakalgkdp atwndfdnaq mqrvplmfhi pgykkgeinh eyggeidvlp
      541 tllhlvgind kdyihfgtdl lspqhdqlva frngnfvtpk ytvldgktyn nqtgeiidpk
      601 kagiqkevek dqnqvktals lsdklnqenl lrfyvpdnfk tidpkkydyk ndaeknetie
      661 kqkgskstsv yskngnkttt nlypaetden n
//
LOCUS       WP_010738388             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Enterococcus].
ACCESSION   WP_010738388
VERSION     WP_010738388.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..282
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30623
     Region          3..277
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkkifgfaa avlltvglaa cgnnsdskga ssksddttlk vgasptphae ilehvqpllk
       61 deginleivk fddyilpnqs laegdidany fqhipylnke ikekgydfvn agavhiepmg
      121 lyskkikdia dlkdgatvit snsesdwgri itilqnaglv kvkdgvdlet atfddiaenp
      181 knlkfnhsid psllastyqn degdlvaina nfaygaglnp lkdsvlleed nspyvniiat
      241 rkgdenseki kkllevlhre dvqkwiedkw ggsvkpvaad ak
//
LOCUS       WP_010738444             199 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SOS response-associated peptidase [Enterococcus].
ACCESSION   WP_010738444
VERSION     WP_010738444.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..199
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=22906
     Region          1..173
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgryffdla sdelkkyyeq vkpqaesrqi higkneifps nhvvtlglnq esvvvpgitr
       61 wgftgfkkgq lminaraetv eekktfshpf ketrcvfpms gfyewdsdkh kvmftdsqts
      121 vlyvggfyri hkneagfete siilttqpsq svlpvhdrmp lilakeqikd wlndldfars
      181 qltakmpels rrnvdenhi
//
LOCUS       WP_010738456             379 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Enterococcus].
ACCESSION   WP_010738456
VERSION     WP_010738456.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..379
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42296
     Region          37..360
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mqakfknskl lfwtvelvlt iigvyfilqm pnvfspvlkm lsaillpllv agffyymfdp
       61 vvvflekrki prvygyiltl vvlvvlavla imnvipqlae qtiqltkslp myaeetskwl
      121 nelaqreeik nfnieeqlas anlslsnlfn ivlvslsssv skvfsfmmqf fvllftvpfi
      181 llfmfkdghk fidalakffp qgirgevrqt vkelnetlsa yisstivdav iigimsfiam
      241 tifkqpysll lavfcgitni ipyvgpfiga vpavivglfv spfqalymal silviqqldg
      301 nvikpllfgk nmnmhpltii lvligagsva gilgmlicip vyaviktlvl nirkiyllrk
      361 fdsgveptiq eiktngren
//
LOCUS       WP_010738459             509 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Enterococcus].
ACCESSION   WP_010738459
VERSION     WP_010738459.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..509
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57374
     Region          6..508
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mslltltnit qqfgdkilye nvqlqvnage hlgligqnga gkstlikiit geilpddgqv
       61 hwqknihrgy ldqyvavdet ltieeflkta ysdefkkeal itqlyqeyse tmeeelleka
      121 gklqteldqg vfyqidtlva emssglgidv lglstplkkl sggqrskvil aklllenpdv
      181 lildeptnhl ddqhiqwltq flqsfegayi vishdqefld kitthiadie fgkitkytgh
      241 lkqalrqkeq nresylrqfh aqqkhiekte ayirkykags rstmaksrqk qldkierltp
      301 pastakpifd fpyspivttl avettdlvig ydrpllspin ltirfgekva irgfngigks
      361 tllktligei eqlageyhfp dntainyfsq dliwekplet plqylgaqfp katvkelrrq
      421 laksglvnql aseplstlsg geqtkvklaq ltmnqgnlli ldeptnhidh etkdslqtgi
      481 khfpgtviiv sheqefyqdl vdrvieieg
//
LOCUS       WP_010738520             176 aa            linear   BCT 01-JAN-2025
DEFINITION  shikimate kinase [Enterococcus hirae].
ACCESSION   WP_010738520
VERSION     WP_010738520.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..176
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19936
     Region          4..167
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 mtslvligfm gagkttiskk laarldqpvi dmddylvqql gcsieqyfat fgeaafrdhe
       61 tallktilqk kaviatgggv vlqkenqell kqqqviylkg eadilierir qdqtnirpla
      121 lknsdtklre imwerekiyk slakitidts kklpdeiite iikwvennde nwvsrs
//
LOCUS       WP_010738533             321 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus hirae].
ACCESSION   WP_010738533
VERSION     WP_010738533.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..321
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37056
     Region          38..121
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <217..320
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mekwiselfk eteieklqkk sgknintmnl nyhrsivpei pkskffefgs iainkhprfs
       61 ytpahthhfi elnflfngqc tqrlngdvfh lekgqlllld skviqqidyv gaedilinfl
      121 ldipaiqnil lpnlpksnnl itdfffqatr sptehtsyil ldlsmsplay qlikslmmtt
      181 yqkesvhkql llnllfsslm vesaqapvii tnkktirnep liqildyind hyaeitlqql
      241 getfgynkky lsnllknktg ssfqelidqk rlseakrlml etndslstia lkigyksvps
      301 ifklfqketg ktpdyfrkkr m
//
LOCUS       WP_010738648             379 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Enterococcus faecium].
ACCESSION   WP_010738648
VERSION     WP_010738648.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..379
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42766
     Region          37..366
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mqsrfkqskl ffwtvelvlt iigvyfilqm pnifspilkt lsavflpllv agfiyymfdp
       61 ivvflekhri prvfgflltf lvviilvvlt vmnvvpqlme qtiqltqslp myadetskwl
      121 nelaqreefk nfnleeqlas anlslsnlfn iilvslsasv skiisfmmqf fillftvpfi
      181 llfmfkdghk fidalshffp kairkelrqt vkelnetlsa yisstildal iigvmsflam
      241 rifdqpysll lavicgitni ipyvgpfiga vpaiivglfi spfqalymal silviqqldg
      301 nlikpllfgk smnihpltii lvligagsva gilgmlicip vyaviktiil nirkiyllrr
      361 mehvseklds pkvleetse
//
LOCUS       WP_010738743             279 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            faecium].
ACCESSION   WP_010738743
VERSION     WP_010738743.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..279
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=31746
     Region          128..220
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mkiikktvvi lippilsffi affglfissy lesifyeqlf pnlqgnlfvs limdvffflm
       61 isflfilltk iiykdirilg fskknffknf ffgyltgafi itfivagyvl vggadfqevf
      121 sksswsklli sivfylaqgs qeevisrgfv lggiakktnl lwgvivsslf fmlmhlsntg
      181 gftlelldyf ligmvwallr ilfsntwvaa ashgaynffm sdffglansp kdsegilfqt
      241 iyhssidyms iiissivlvi liilvwrkrn ilnkplefe
//
LOCUS       WP_010738850             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus faecium].
ACCESSION   WP_010738850
VERSION     WP_010738850.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..279
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30471
     Region          1..273
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkiirfvvi tfvaiiwlag csqgkadttd kketivklgi igedtdvwdn vkdrlkkeni
       61 nleyvkftdy nqpnvaladg sidlnsfqhq ffidnynkeh gtdlvsignt vnaplgiysn
      121 tlkdvadikd gakvaipndv tnggrallll qtaglikvdk akgqaptvsd itenrknldi
      181 seldasqtar alsdvdisvi nsgvavdagf npasdaifle pvddharpyv niivarkede
      241 nnktyqkivd ayqtedtvkv iektskgssv pawetfgrk
//
LOCUS       WP_010738878             453 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Enterococcus faecium].
ACCESSION   WP_010738878
VERSION     WP_010738878.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..453
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=52158
     Region          226..349
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mpqqksftry lashhedely navadfvatn pdtldlrshr vdvdnidsid sidsieldkv
       61 slkttyiqds dtmnlefdil vvvelifqei trhddfddsc eawfrvtcta yldgsledfk
      121 vlevdtydqn kgrrfgslls eqlvpilyka dhdkaaevfl rkyqpealer pmrvnpyqla
      181 skmglqvvea dtcedsttlg qiyfqdvdgi kagtikivtd ledefnlgak nntiihecvh
      241 walhkkafel ercydlglss istrvdlekc qekttatdwm ewharsltpk immphdmfkq
      301 eadyifwqya dehghvsspd iieqviekla dyfgvsrlsa kirmvevgye eaigafnyvd
      361 gryvqahswk kgtveknqtf cidemsavfe lftnlefgkl iqsgqyvyvd shfvlstpky
      421 vvqdfvgrmv ltdyarhhfv liikyrncse ant
//
LOCUS       WP_010738899             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus faecium].
ACCESSION   WP_010738899
VERSION     WP_010738899.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..282
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30855
     Region          3..277
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkkifgfaa allltvglaa cgnnsdskds ankaddttlk vgasptphae ilehvkpllk
       61 degidleivk fddyvlpnqs leegdidany fqhipylnke ikekgydfvd agavhiepmg
      121 lyskkvkdvs elkdgatiit snsesdwgri itilqdaglv kvkdgvdlet atfddieenp
      181 knlkfnhtid psllastyqn degdlvaina nfaygaglnp ledavllekd nspyvniiat
      241 rkgdedsdki kklievlhrk evqewitdkw ggsvkpvkad ak
//
LOCUS       WP_010738939             313 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus malodoratus].
ACCESSION   WP_010738939
VERSION     WP_010738939.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..313
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35067
     Region          16..311
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 meqdqlelmq vvtekyyyqd inqaqiatel nlskptvsrl lkrakkdgyi kvelnfptty
       61 qkslgdqlat afgirkafvy dtqltnkqli ieemseqisl flddliqdgq tiglawgrtl
      121 yqlsehlkgr qkkdtkviqi tggaarnsmv tnseaivlnf sisygsewfq lpvpafvdse
      181 eialalkkdr qikhvldsfd kldialfsvg eihknaivve agyfgeedfl dllekgvvgd
      241 ivgtfldkeg qvldlglskr higisaqqlq kvenkvcvai geekrdvlka tllggyvdyl
      301 ftdtvtakem lmq
//
LOCUS       WP_010738929             703 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus malodoratus].
ACCESSION   WP_010738929
VERSION     WP_010738929.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..703
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=82204
     Region          233..555
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtqnnqnhpi svyerinndl shflektihs nksvttnqiy tdvflendiw tidmfqdinq
       61 fvasvekhri sseagrnklk fksvnsnins elkyvfyrrl fddlwtiyga fhtysgplys
      121 vtvflnekyp nlnslldldi daaekryffw lnakgisshy qkknsenrey ktirpsaafl
      181 rrlhdflfey tdfreewekd kwniknlhrn ygleynrsts nyyidftkvn ekmidplrky
      241 fkhrllgkrn ftvgtaqmti lylkkfinfi fmiephwndl kdlnrshieq yieylnkyta
      301 dsrdsisnpe gyinrslhyp qkflediqif nydvapkini nhlmfpedkp krkkksidqi
      361 dyipdfvlnq lfenindlsp eivpivwial ktglrisdvl glrkdclkki nnkywvqtdi
      421 ektfvkdhri pidnelalii aslidksgkl snqennllny ifvcyhgnrk gnplpqksva
      481 fhlnnfaqkk gitdesgnif hfkthqfrht yavkmlngga diltvqqlla haspemtvqy
      541 akilddtkrk afesvvkqgi fsfdsvgqvn evalqsevss tslkllwqdy klhaidnpfg
      601 tcharlkgnc pymdsppcls cgtnqtpckd laigfsdldi skyelhvktv traielatkv
      661 erpelisank knleryqnil stlyegnfif grknrlnqek ing
//
LOCUS       WP_010738955             279 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterococcus malodoratus].
ACCESSION   WP_010738955
VERSION     WP_010738955.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..279
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31542
     Region          3..235
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 maatiyvtgn fkggvgkstt aqmlsyesal kkerktllid mdpqgnasev meltsenitg
       61 kevsfknget iwegittykd ltkviypvae nldiipanik fsaypqyiig klkntteqlk
      121 yfaefivplr emydviyidv pptisvysda amyvadwvil ilqtqvkslr ggqdyidymk
      181 ffkkkhsakl dvlgivpfmv qkrdsvdiev ydmakelype hlistvvlnn grlkrydgdg
      241 itetltkkgh inkkdahthr ifldildeld eneealgdl
//
LOCUS       WP_010739008             189 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RDD family protein [Enterococcus].
ACCESSION   WP_010739008
VERSION     WP_010739008.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..189
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21352
     Region          32..168
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mteetsqrpp avgpvsqlle kkkrkaqfhh ypdyfyagfw irffaylldl lcvsaitgil
       61 lglpanllnv tkssellsiy gflalliyla yfilmtklnh gqtigkmafg irvvcfseed
      121 lswqtvfvre gacrfvlrgs ifmlgylvti ftpnkqhigd yfsdtsvvtl nllaaregly
      181 knesdrisq
//
LOCUS       WP_010739098             396 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FtsW/RodA/SpoVE family cell cycle protein
            [Enterococcus].
ACCESSION   WP_010739098
VERSION     WP_010739098.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..396
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=44210
     Region          5..384
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mptkikkrhf ldysilipyl iltviglifv ysstsyllis nnvsptslvm nqgifwalsl
       61 vmislmykmk tdvlksqqli ifatylifil livvffigde ingakgwiri gsfsmqpaey
      121 lkimvvwyls yilskrqeti qnnftndmkr plmlvfamif lvavqpdmgn aaiitllali
      181 lllasgvnwi yslivggvgi vgsflaiefl thfggaifpk rlqyifnrfe sfknpfkyel
      241 dqghqmvngy yamfnggwfg rglgnsiekk gflseahtdf ifsivieevg ligaliilai
      301 lifmiariyl vgirskkpfn slicigigsl lllqvfinlg gilgiipltg itfpflsqgg
      361 nsllvlsvgv afalnisade krtklaieye ylksqe
//
LOCUS       WP_010739161             394 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LCP family protein [Enterococcus].
ACCESSION   WP_010739161
VERSION     WP_010739161.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..394
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=44811
     Region          154..393
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 msrmdkykki heesqkdekk plgfrremkk dpkaasekar yedpvyeqpk epfrepeeef
       61 yyedhyqepk kkqfgfklps iknpfkrkpk npyepkpkkk rrwrrtlvmi liailgysvi
      121 sfgignfaak hdssmpkiet qefngvksen gkrnilllgs dtrdnisgrs dsmmvlqvdg
      181 fgkpklvsfm rdmyvnipgv gqnklnaaya yggadlvrqt lkenfgidcr yyamvdfqtf
      241 ekgvdalfpr gvqidaekdm ssyidapisk gpqrmnghtl lnyarfrmde egdfgrvrrq
      301 qqvmqsvfgq linplvllrg pyaagkiwgy lstdmpntyv vshllnfaka vggidrltlp
      361 vdgswsyidt dnagsalavd tnqnaqsaqg flgk
//
LOCUS       WP_010739230             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptidylprolyl isomerase [Enterococcus].
ACCESSION   WP_010739230
VERSION     WP_010739230.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..249
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=27040
     Region          58..246
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mqlkklivga slllsiglfa acgsnnstkd tkessaktte ssvdlnklsl pqlndkvtdd
       61 eylvelvtte gnvkiklfpk qapkavenfv khakdgyykd tpfhrvikdf miqggdpkgd
      121 gtggesiwkk gfktedskql ynirgalsma rsesrssngs qffivtnkdd vsdglavqyy
      181 pkkmieqykn ggapqldgey tvfgqvtegm dvvdkiasge vkdggsgeks tpvepvkvte
      241 vkvlqepkk
//
LOCUS       WP_010739252             420 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Enterococcus].
ACCESSION   WP_010739252
VERSION     WP_010739252.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..420
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46050
     Region          27..323
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mheliviggg paglaaavaa hekgitdili ierdqklggi lnqcihngfg lhyfkeeltg
       61 peyaarfinm vqeanievll dtmvlevten kevhivnkeq gyqiltakal vfamgcrert
      121 rgaigiagsr pagvftagta qryvnmegyi vgkkviilgs gdiglimarr mtlegadvla
      181 cievmpysgg ltrnivqcld dyaiplllsh titeirgknr veqvvvskvd ekrqpisgte
      241 qtfdcdtill svglipenel srdahldlds ktngpfvyen metsvpgifa cgnvvhvhdl
      301 vdfvtaesik agtsaatyil eqekestqyl tikngdhvty vvpqkiradn idrrtelffr
      361 vnkvfddsqi likskgevla kqkksyivpg emekmklskk vldkvtngel eicveevaks
//
LOCUS       WP_010739303             270 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus malodoratus].
ACCESSION   WP_010739303
VERSION     WP_010739303.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..270
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29761
     Region          1..269
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkiglaili iscitflaac gsgsaektdk ikigasptph aeilehikpe lkkkgidlei
       61 vkfddyvlpn kalengdida nyfstvpyfn lqkkengykf snvgaihlep mgiyshkikk
      121 vsdipngakv vvsnvpsewg rvlnifvknn likiksgvpi dkatfddite npknlvfdhs
      181 vdptlltsay ennegdlvai nsnfayekgl npvkdslmie qndspyvniv atktsnkdnk
      241 dikkivevlh eskvqkwike kwggsvvpvn
//
LOCUS       WP_010739387             345 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Enterococcus].
ACCESSION   WP_010739387
VERSION     WP_010739387.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..345
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37395
     Region          165..345
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mnrsikralv llglllflas acsrnpggtd sftteskrsi iteekgseqa tmqkftlnst
       61 vgevladpaf enfghllfpv drsvtenmsl advstsrvfv wynnlqpekt veiinhlksr
      121 alegqrifyp iyeekeiaad sakantglfh fggeagkpfa imnagggfsy vgamhdsfph
      181 alavtdhgyn gfaliyrpnd ayadlakaie ylydhaeeln lsgenyslwg gsagarmaat
      241 lgnaaslfql tgrkdipqaa avvmqytgys vyspadapty anvgtndgia swqtmesrlq
      301 rleslgitte fhvydgllhg fglgtgtvae gwfddavafw asqmk
//
LOCUS       WP_010739416             624 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Enterococcus].
ACCESSION   WP_010739416
VERSION     WP_010739416.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..624
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71014
     Region          6..531
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          553..619
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mkelkvtely ktfgdktlfd risflihekd rigligvngt gksslltila gqdsgdgdvs
       61 aiekasdyri gylaqeqifs adllvldavf qgdnplmqtv rnyekallel sndnnaesqr
      121 rftvaeeamn kqdawtadse akailnklgi dtldkridel sggqikrval aqvlidapdl
      181 llldeptnhl dydaiqwles ylksytgsll mvthdryfld rvtnrifels fgklyeyqgn
      241 yeaylvekae rdriageqeg krkqlykqel awmragakar ttkqqarinr fedlkdnlhq
      301 vktdgqlemn iattrlgkkv lelkqasyai agktilenfd llvqskerlg itgkngagks
      361 tllnilagrl pldngviemg etvrlayytq qnetldpnkr miaylqeaae evkqrdgsqi
      421 svaeilerfl fprfmhgsli gklsggekrr lyllklliqq pnvllldept ndldiatltv
      481 ledylqefsg avitvshdry fldkvaekll ifegngmits yfgsivdfle qqapvkeekv
      541 skvkpqpker kkklsykeqk ewetieddia lleknidelt eamnhqgddf tklqdlqkei
      601 dqteqsleek msrweylsel iedn
//
LOCUS       WP_010739436             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [Enterococcus].
ACCESSION   WP_010739436
VERSION     WP_010739436.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26767
     Region          1..226
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 merlqkviaq agiasrrkse eyitggrvkv ngelvkelgt kvgkkdivev dgvpiyqeep
       61 vhylfykprg visavsddkn rkvvtdyfta vseriypvgr ldydtsgili ltndgdfsqr
      121 lahpkhqidk vyvakvkgya ekrnllpltr giriegkkta parfeilstd kkaetsivel
      181 tihegrnhqv knmlaavglp vqklkreryg dltlqglrpg eyrrlnskei ngllnqsr
//
LOCUS       WP_010739527             173 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus malodoratus].
ACCESSION   WP_010739527
VERSION     WP_010739527.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..173
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20649
     Region          1..84
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mipllilgll kekpasygye llsdmeanyf qyfvkftkgs fyynlqqlee kgmiqkilie
       61 qglvekeknr ytltelgeke ferrfvqygs knepitfpfy tpmlfvdqvs teemeqllkk
      121 qiqqtqekih lielaltspd qlrpnfvkmm enskrhhevn lewfqeqltd ykq
//
LOCUS       WP_010739572             225 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010739572
VERSION     WP_010739572.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..225
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24502
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnaievkdvk kvygsgqatf ealkgvsfti kkgesiaiig ksgsgkstlm hilalldrps
       61 sgkiallnqd trqiknsaln kmrnetfgfv fqqffinpkd tvlsnvllpl kiagitnrqr
      121 kqmalealea velsdkannk andlsggqkq rvciaraivn qpeiifadep tgnldsatge
      181 kiekllfnln hkkgitliiv thdpelaarc drqihikdgl llegi
//
LOCUS       WP_010739607             280 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus malodoratus].
ACCESSION   WP_010739607
VERSION     WP_010739607.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..280
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30692
     Region          57..234
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mnalvyrgll lffknkqavi gsfigalimi ilyvflldds lvnslsvlsh pklvvdtwml
       61 agvigissas stlgsvslmi rdkersvytd fmispisksk imlgyffstf lisllvtsvv
      121 iivaeiyivt lskgtllslp qfgllflvsl ltvfcssafm ffiasffrri dtfstmtsii
      181 gpligfltgc yvpigslpet aqtvvqyfpl tsgvvlirri ltenvftaad kpamdtikee
      241 lgivmngqnd vllpiailil ssllflvlal wnvkrvevkr
//
LOCUS       WP_010739609             126 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010739609
VERSION     WP_010739609.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..126
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14737
     Region          12..89
                     /region_name="HTH_GlnR-like"
                     /note="Helix-Turn-Helix DNA binding domain of GlnR-like
                     transcription regulators; cd01105"
                     /db_xref="CDD:133380"
     Site            order(14..16,30,47..48)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133380"
ORIGIN      
        1 mrekelrrsl avfpigtvmk ltdltarqir yyeeqelihp ersegnrrmy slndidvlle
       61 ikdylsdgln magikrvyqm rqeeikaake kpsltdkdvr rifydemltq gglqqqnpyq
      121 sqgpkl
//
LOCUS       WP_010739620             314 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SPFH domain-containing protein [Enterococcus].
ACCESSION   WP_010739620
VERSION     WP_010739620.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..314
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34753
     Region          24..296
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mvvfniillv lavvvvlfvv sqlivivqqg evkvvesfgk yvktldpglh flvpilyvvr
       61 rrvslkqtpi qiepqsvitr dnviveidea ikyhvtdara fvydnedsvt smiqdcqsnl
      121 rgiigkmeln evlngteein vnlyesvkdi tagyglsidr inigeisvsd eivnsmnkli
      181 tasrdkesli tisegkkqsv ileseaksse mqidaearar qtkidadara drtridaaae
      241 adriakitea etarikeink aiaesnltde miaylgieaf khvvenngnt vimpsnltel
      301 gnvpaikeiw qqtk
//
LOCUS       WP_010739784             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            malodoratus].
ACCESSION   WP_010739784
VERSION     WP_010739784.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..251
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28453
     Region          14..243
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mlflayqvel ksieidiydf iiknldavpy mrireladac hvststilrf ckkfecngya
       61 dfrlrlqlya kelhelaepi qtidelpfie flkrthtnef qerinsaasi lkesdlvlfv
      121 gigtssifas ygallfsslf tlalniqdpl ntplynisdr ldnkvclval svsgenedii
      181 dyinhiklhk sgviaitnss ntpiaklsdv dipyyantem yketnitsql svtyileila
      241 rtvhqlknke n
//
LOCUS       WP_010739700             205 aa            linear   BCT 01-JAN-2025
DEFINITION  putative ABC transporter permease [Enterococcus malodoratus].
ACCESSION   WP_010739700
VERSION     WP_010739700.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 205)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..205
                     /product="putative ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23323
     Region          7..185
                     /region_name="COG4905"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443933"
ORIGIN      
        1 mkaaklfwif ilssmigfli engyrflltg nfvwhrgvii gpflpiygmg acvftlvlrr
       61 vhstiklfil galiggvtef lgslikevll giklwdyshh pfnllgrisl vylcfwgilc
      121 vlfikiilpf lsdlieksgv grmknmtriv flvftlnltf sglalqrwne rqsgasaenq
      181 ferrmdklfp dkvlekvyps leqsn
//
LOCUS       WP_010739810             444 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Enterococcus].
ACCESSION   WP_010739810
VERSION     WP_010739810.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..444
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48801
     Region          2..436
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 menklqkqmt srhimmlalg gaigaglfkg sgeaigiagp svilafllgg lvlfivmngl
       61 grlvlnsdnv qglsgiikpf lgertadfid wlywslwmvn iiaeavaaas fmqlwfphvp
      121 swifvlllai mttainlysv rlfaeteywl afikiaviii liafgtylvg reifnigfld
      181 tisrmnshgg ftphglkglv nsllvviysy ggseliaitv setedpktai pkaikgvmgr
      241 iisfyivpmi llliiyrwdt laatsvspfv mvfqkmhipf atdivnfviv lalfssinsg
      301 vyassrtlyf rvkdnpgfts klavlnkhqv pqravlfctg tlylgvilsy flgnklfnyl
      361 vgslsysvll twllisvaaf vlalkkgtns erlfsglvil vlglifigil innpigvtif
      421 taciyliiff syrkkqtdvi seqv
//
LOCUS       WP_010739825             249 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Enterococcus
            malodoratus].
ACCESSION   WP_010739825
VERSION     WP_010739825.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..249
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27455
     Region          1..236
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 metirvenls vayrgkvalq qidlelsagk ltgivgpnga gkstlmkgil qliktqsgki
       61 fygeqplndh rkkiayveqr qdidlsfpid vfgvvlfgty phlkmfqrpg kkeksfaavc
      121 lekvglsdfa drqiselsgg qlqrvfiara laqqaewill depfagidat sekiiiellk
      181 elrdegksiv ivhhdlhkvt dyfdevilln kgliasgpva qtyttknmek tygseitqml
      241 rmggagfat
//
LOCUS       WP_010739921             245 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus malodoratus].
ACCESSION   WP_010739921
VERSION     WP_010739921.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..245
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27239
     Region          3..244
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mslaiqhvtg gyghlpvlkd infevhngem igliglngag ksttikniig lltpqkgtit
       61 vddltlqqdp enyrkkigyi petpslyeel tlrehievta maygipkeea meraesllkt
      121 frlenrldwf pvnfskgmkq kvmvlcafli qpslyiidep flgldplain allelmvamk
      181 eqgaailmst hilataekyc drfvvlhege vraqgtlqnl qtefnlpgss ldeiyialtk
      241 ekeha
//
LOCUS       WP_010739977             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010739977
VERSION     WP_010739977.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33604
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(106..107,109..110,113,117,121..127,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mnlqhlkyfd vlareqhytr sskllnvtqp slsnaiasle delgitlfek kgrnvvltkp
       61 gkifqdyvtr tlgtlddgie titkiskgsg fisfaflpvl gttfvpklvr dfhnahqdqe
      121 ilfdfhtssg vskeivdgik nmhydigias ylpdepsief lpiasqelvv iapldhplaq
      181 fdaiyleqtq pyeqigfsks sglrnvidev fqknncsyni vyevtvdqvi aglvsqgfgi
      241 avvpnmyilk hlplktihlk nvmldrsfyl vtnkdayltp avinfkefvv ahsdskeivy
//
LOCUS       WP_010739993             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010739993
VERSION     WP_010739993.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..228
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25776
     Region          1..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mielkninky yrndeeslhv lkdinlkada gemiavmgps gsgkstlinl lgfidtkfeg
       61 eylfedenlv tttddrlsqt rnemvgfvfq nfslienytv yenvelplly ngygfhqtke
      121 kvmsalekvg iadkaekhpr qlsggqqqrv aiaralinqp kfiiadeptg aldthtsnei
      181 melfkelnhr dhatiflvth dpevvpyctr lvrirdgait edraviee
//
LOCUS       WP_010739992             399 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010739992
VERSION     WP_010739992.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..399
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42974
     Region          6..399
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkfyvnwrss igsifknkkr saltmfgiii giaaviails igrgferdti esltaeesdk
       61 levdinfvpg ndalyysnvd miqasdfsll knvegveavs ypkndlsyiy keikvkdktk
      121 nyrvgvvsks geavsygrai saydnqtqnk vvtidaslak dlygsakgav grgfeldkqv
      181 ftiigvfpag aeetmfsqgt tkillprqty ihffgneqdt ssvvltladg sklnkvadka
      241 ikklesagam rqqgeyqvsn mammtdgise vlssitlfis avagislfia gvgvmnmmyi
      301 svsertkeig irralgatrg airmqflleg mtltlvggii gyllgmivay aignvmdisv
      361 svdlftvcla vgvssgigli fsvmpaseaa kkdlidilr
//
LOCUS       WP_010740124             703 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LTA synthase family protein [Enterococcus].
ACCESSION   WP_010740124
VERSION     WP_010740124.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..703
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80059
     Region          16..638
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkklkapafl nkrlgfyall tfllwaksif aylfefnlgi esltqyfilf inpiastmfl
       61 lsialyvrrs kasyltmmii yalasfllfa nvvyyreftd fitvntflga gkvasglges
      121 avrlfrpydv lylidivilp lllwrkrike eerpvrarma famtalsvmi fsgnlflaea
      181 drpelltrtf srdylikylg vnaftvydgi qtyktnqvra easpndlkev esyvkehyaa
      241 pnsdyygiak grnvitihle slqqfvidyk lkdengqehe vtpflnsifh snstfsfdnf
      301 fhqvkagkts daetlmensl fglnqgslfs qlggkntfqa apdilkqtag ytsasfhgns
      361 gsfwnrtety knlgydyffd ssyydvnden sfqyglhdkp ffqqsvkyle rlqqpfyskf
      421 iavsnhypys efkndeagfp mantsdetin gyfatanyld kaveeffnyl kasglydnsi
      481 ivmygdhygi snsrnsdlap llgksketws nfdnaqmqrv pymvhvpgqd kgginhtygg
      541 evdalptllh llgtdtskyi qlgqdllskd ndqivafrdg dyvtpeytyy sgslysnsng
      601 mpitepsetl qhqaetwkea vskqlstsdn inngdllrfy sasglkpida sqfdykngln
      661 kmekienklg dkstslfdqn gkkstqelyk tetykqyqeq gqq
//
LOCUS       WP_010740186             185 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            malodoratus].
ACCESSION   WP_010740186
VERSION     WP_010740186.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..185
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21942
     Region          10..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          88..180
                     /region_name="TetR_C_8"
                     /note="Transcriptional regulator C-terminal region;
                     pfam14278"
                     /db_xref="CDD:464123"
ORIGIN      
        1 mkendlryyr trksilsamt rllqtkkfeq itvtticeea eisrsgfylh yvdkydliev
       61 nlkefrdqan qfvqadnens kkklffnmlt ylrndgklia alisengsie vqnyikrmmr
      121 enartnifpq mdlelendie ehyaliflsn alfgvlqdwi nrgqkesiee lvqimdrlit
      181 fdfrk
//
LOCUS       WP_010740231             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            malodoratus].
ACCESSION   WP_010740231
VERSION     WP_010740231.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..248
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27996
     Region          7..246
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 miidikkevy qslsesekkv idflnrneql ipelsitkia ektftssati srtiqkcgfs
       61 giselrykis qqkesaesan apyvvnnila ksyrecteti nsisstdiyq tieylknadr
      121 ificargfta liadelqmyl qllgynaiiv kdvmwmkkfh riitakdtlv iislrnstpe
      181 laitakaard ceakviticc ktptelekys ditlvghsek imeaseqivy sriplliitr
      241 tiieyigl
//
LOCUS       WP_010740232             299 aa            linear   BCT 01-JAN-2025
DEFINITION  carbohydrate kinase family protein [Enterococcus malodoratus].
ACCESSION   WP_010740232
VERSION     WP_010740232.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..299
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32415
     Region          2..291
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 msilcvgqav ydltfpvnep lvenqkyrip drhecmgapa anaaylcgsw gaeaaliarv
       61 gedlfgqeiv rtlvaggvda asiycdpkqa tsiscivvnq qnghrtilns pmreqrfpiv
      121 wpdkapqvll vdghelsatl ealkkypaal simdagtykp elaevvqavd ylvcsedfay
      181 qatglpiqld epdqikevfk qlrtlngnql vitigdqgcl wqeqeiihhv pafkvapvdt
      241 tgagdifhga fafcleqkks lretiifssa asalsvqkig gqtsiptlae vrafiskee
//
LOCUS       WP_010740246             233 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus malodoratus].
ACCESSION   WP_010740246
VERSION     WP_010740246.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..233
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27266
     Region          7..231
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mkktrvlyle iaekikedif sgkypvgtml psepelerlf dvskitvrka iellaadeyv
       61 ekksgkgttv lserpynkls kaisftqile nsnlsvkkmi ldvkkitlde sqkayeyfgs
      121 eaiwfqrmyl lddkpyicfd hylpvglkrv tkedleqesl yrilyqngle ierfmddfva
      181 ialnqeqqkl lqteetialk rirksydydq kvveyseaiy ntsnhayqie yet
//
LOCUS       WP_010740300             170 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase family protein
            [Enterococcus].
ACCESSION   WP_010740300
VERSION     WP_010740300.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..170
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19357
     Region          5..168
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 maravfygai sldgyladka drldwlyqqe ggelvpydtf yqtidytimg rrtydavkrd
       61 aeleiiypek enfifshsai evdenmqvvn gdpvefiekl psdktvwvvg ggallrpvie
      121 aglidewwiq ivpiligegv plflpqtnqq kfqlleteqf gqfaqihlkk
//
LOCUS       WP_010740253             383 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Listeria monocytogenes].
ACCESSION   WP_010740253
VERSION     WP_010740253.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..383
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41284
     Region          13..380
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,138,
                     141..142,145,259,262..263,266..268,271,299,303,356..357,
                     361,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mkrekfgvil pitllayfli lmdnsiifts sveigeslgl satalswvss aytltfggfl
       61 llsgrlsdll grkrifligl fifgisslvi glsqtaemvi amravqgigs siiapttlal
      121 imdayqnnmr qraiayygat agigssigll vgggltslis wragflinvp ftlvlfiltl
      181 kyvtpsvrrk eridylgsil sifgligiiy gftegkiglv flgvvflgif ilwegksaap
      241 ilplalfknk irsgayvtrl lfmmamlpfw fflpqmmqsq ygfsalesgf aflpltivnf
      301 iiamqlprlt gkfgnnkvll ageiilaigl mllaisnpan gywqtvfvpm vilglgqgli
      361 lapvtsagvy eapdelagiv lve
//
LOCUS       WP_010740319             246 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus malodoratus].
ACCESSION   WP_010740319
VERSION     WP_010740319.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..246
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26188
     Region          60..246
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mnkvislakv egklairsid gilfgigmpl gvlllttmia gskqagdasy tfldssfssl
       61 lvvgicataf mgiplticdy rdkkilkhff vtpaspghli atqvlvamit avtsatvval
      121 vsvvflgyrm qgnwgllias yflvmiamys lglliaslck nikianlvcs lvyfpmlfls
      181 gavipfelfp sglqkvanvl pltqgvqllk svslnqpvgn pqfvlvllvv itivgfglaa
      241 klfrwe
//
LOCUS       WP_010740442             329 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus malodoratus].
ACCESSION   WP_010740442
VERSION     WP_010740442.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..329
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37702
     Region          10..223
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkensensfk lsivvpvynv edtieravqs lfdndfgnie vlliddgstd ssgqiceelt
       61 ktsekiycfh kengglssar nyglervsgd lvafldsddy ylpgcidkvm ndfqintpdi
      121 vcfglkkgkt eansiefigd rqiscsnaea iellfnskav dfyawnkifk kklfdnvefp
      181 egklyedmmp vyqtfraart idildfagif yfqnsnsivy qdfnpkqydn itqrkvllde
      241 vtkdfpefin lanarlidgy lstgfkigls kkdnpernhf yntskmeirs llkkikgsre
      301 vsytkrlaly lylvnpnlys ilykqilkk
//
LOCUS       WP_010740434             318 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus malodoratus].
ACCESSION   WP_010740434
VERSION     WP_010740434.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..318
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36439
     Region          7..181
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(10,12,86)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(39,85..86)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            84..86
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mtdsiaillp cyneamtikk vindfqkelp sadiyvydnn stddtyqial negaivrkep
       61 rqgkgnvirq mffdidadfy lmvdgddtyp aeachellka lkenradmvi gdrlsngtyf
      121 nenkrafhdf gnnlvknsin wlykanikdv mtgyrgfnrl fvksfpvmss gfqietefti
      181 hsldkrfklv eipidyrdrp egseskldtf sdgikvlmti fkmckdykpl fffsmwfalf
      241 filgllaglp visefirngf itkipsaila tglmilslll lvtglildtv vtddkknyel
      301 nlykiygekn drykkgpy
//
LOCUS       WP_010740467             392 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus malodoratus].
ACCESSION   WP_010740467
VERSION     WP_010740467.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..392
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43434
     Region          8..378
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnnqdfvpfl qenwneagfq kpaliqskvy tpiieganlv giaptgsgkt layllplinq
       61 leagkpsqvl iltssqelam qvvevarkwl agsgmkvqpl igganvkrqq dalkkkpell
      121 igtpgrvlel itakkiktpn iktlvfdevd qliqgqslql iqkilkasdn daqhlyfsat
      181 adtvldelnn fesdllvidv skeddsqgev qhfyletsdr kkvdqlrrll nlpafwgmif
      241 fnqlsdmgsa eekllfhhlp vvslasdqsk msrksaieqf kkhqalgllt tdlasrgldi
      301 eslpfvinan vplseesylh ragrvgrmgk tgvvitfvtp qektdltkia kklnltlapi
      361 ylfggellte epikqsdpkk kkskkskgkr rk
//
LOCUS       WP_010740468             333 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus malodoratus].
ACCESSION   WP_010740468
VERSION     WP_010740468.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..333
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37406
     Region          1..254
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 minlgiigtn witdqfvqaa hetgsyqlaa iysrrletaq kfgekygdve yatnldtffg
       61 iehlntvyia spnslhfeqa kqgilagknv ivekpafstp kemdeiiela nqkkvfffea
      121 arnihekafk vvadflpmkd qiigadfsfm kyssrydqvl dgqepnifsp hfsggaladl
      181 gvypiyaala wfgmpkesiy fgqkistgvd gigtgilrye nfditirtgk igdsfqqsei
      241 ylangtlvln avnsideaif hdrnhqrrek lnvhqlenpm veeaaefaqv ilnptdrklg
      301 tdyeawvels rnvnqviydm rksagiifda dek
//
LOCUS       WP_010740540              69 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010740540
VERSION     WP_010740540.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..69
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7588
     Region          8..69
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mseeklvlkn rlketrkskq lsqaalaklv gvsrttissi etgqfsptak lalilciald
       61 vkfedlfyf
//
LOCUS       WP_010740598             102 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Enterococcus].
ACCESSION   WP_010740598
VERSION     WP_010740598.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..102
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11375
     Region          4..98
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mnysvttkef mmlaakepvd vldlrdpefv dsfdlsegsn vthipltqlp nrlgqldrgk
       61 tyylftqfgg rsktmaqflr negfqvvnvi ggtsaykqyl as
//
LOCUS       WP_010740575             344 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methionine ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010740575
VERSION     WP_010740575.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..344
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37433
     Region          4..341
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 malielnqvg ksfagktgpi havnginlai eekdvygivg ysgagkstlv rllngleapt
       61 ngqvlvnged vaklqgaalr tfrkkvgmif qhfnllwsrt vieniqlple lagvakeqrr
      121 kkaeellhlv gldgrgdayp sqlsggqkqr vgiaraland pdillcdeat saldpqttee
      181 vlellaninq qlgltivlit hemnvirkic nkvavmelgk iveegsvrev frhpqqevtk
      241 ifvqqdlepk adpselleef vkenptgtla tlhflennan epvvsqairk fpvnisivyg
      301 nieratgssf gtltvqltgd prevdqaisf iesqqvgvev lhrg
//
LOCUS       WP_010740600             387 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Enterococcus].
ACCESSION   WP_010740600
VERSION     WP_010740600.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..387
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42964
     Region          52..380
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mdkkkltqkt swfwkwflns qvvvaliivl llllialvft kvsylfepvg qffaivglpi
       61 viagilyylm npvvnflekk glnrtlaiil lfivvvalii wgivviipqi reqigsmiks
      121 lpgyfdtisd kaseifkdps fkpfqqhidn slqkileslt etaqnisrvt lqglgsvvst
      181 latvvialit apiilffllk dgdqlapyil kflptrtrkp tlrvmtemns qlasyirgql
      241 tvafavavmf iigfslvgmn yaitlgilag flnlipylgs flamvpvvfi aivtgpimlv
      301 kviivfaieq tiegrivspl vlgnqleihp vtimfvllta gkifgiagvi lgipfyavak
      361 viaihvfewy krvsrfyedd eknpvde
//
LOCUS       WP_010740615             213 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010740615
VERSION     WP_010740615.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..213
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=23925
     Region          114..206
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mnekkysfit iftyglvlfs pllflrvfqa sssqiiqltt lsyfigavlm ifyriksqsf
       61 elegrkksll isiligivgi paslllqmli lqieqrllgq svasqntqni vqlimnnmif
      121 ilattiagpi meefvfrrai fgslekrfgf ilpallssvl fafahndghy llyaglgflf
      181 cgmyrysgri wtsmithvgm nllviltqla lqs
//
LOCUS       WP_010740617             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Enterococcus].
ACCESSION   WP_010740617
VERSION     WP_010740617.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..269
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30194
     Region          11..198
                     /region_name="YycJ-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Bacillus
                     subtilis YycJ and related proteins; MBL-fold metallo
                     hydrolase domain; cd07733"
                     /db_xref="CDD:293819"
     Site            order(63,65,67..68,128..129,150,198)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293819"
ORIGIN      
        1 mlemnnafni silasgstgn slylespqkr ilidaglsgk kitsllaevd rkpedldail
       61 vthehrdhih gvgvlarkyk lpvyanektw eamapligkv dveqkhifem gkvltfgdld
      121 iesfgvshda aapqfyrfyk dghsfvmltd tgyasehvrg tirdadaylv esnhdlemlr
      181 mgaypwslkq rilgdrghls nddgalvmtd ilgdrtkriy lghlskennm kelahmtmee
      241 tltrydlgvn yqfqifdtdp dsatelfai
//
LOCUS       WP_010740644             219 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus malodoratus].
ACCESSION   WP_010740644
VERSION     WP_010740644.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..219
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23949
     Region          2..219
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 milkirdlvk hyddgnsivk avdhidlevg kgdfiavvgk sgsgkstlln liggldrpds
       61 gqviidgknv frmkdeelai frrqkigfif qnynlipsln vwenvvlpig ldnrkvdkaf
      121 vedllttigl sdrkkalpsm lsggqqqrva iaraiasepa iiladeptgn ldtktelevm
      181 sllkksvekf gqtlimithd egiaqtadhi vhiedgrvi
//
LOCUS       WP_010740732             331 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Enterococcus malodoratus].
ACCESSION   WP_010740732
VERSION     WP_010740732.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..331
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36256
     Region          3..309
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,89,104,106,136,169,270,273,309)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(234,246,261,270..272,275,297,301)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 makvvclgei mlrlsaeagt rlnqtqqlev fygggeanva vslanyghav qfvskvsdng
       61 fgqaaerhlr sygvatdhll kavgrlgayy veqgtgqrat sviydrqasv falmdelewp
      121 laelfagadi fhisgitpal seqwqnltle likaakkagc kvsfdcnyrq nlwsqkaaga
      181 flnkilplvd ycsagkmdai yllgvpevea datyyyqklq elfptiqafy stnrivhstc
      241 inelqgtlwi ngkcytsknh vidpiidrig ggdaftggil hgllkektpn eiiefataaa
      301 vlkhsvkgdc nqfsekevlk fiksdnakie r
//
LOCUS       WP_010740784              66 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Enterococcus].
ACCESSION   WP_010740784
VERSION     WP_010740784.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7083
     Region          1..63
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 meqgtvkwfn sekgygfita engndvfvhf saiqgdgfkt leegqavtfd vedgqrgpqa
       61 tnvnka
//
LOCUS       WP_010740809             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AzlC family ABC transporter permease [Enterococcus].
ACCESSION   WP_010740809
VERSION     WP_010740809.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..251
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27887
     Region          9..229
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mpvkkrtpwl ealyaamplc fsyipvglac gmllqkagfn ifltallsml vfsggaqflv
       61 vsmisvhasf vstilmvffl emryallgss lsqffkkekr sfialfsqsm ndenyavnyl
      121 kystdpewnr kkalyvnwfs maswtgstvl gtifgsvihv dtelvhfalt amfifmfmmq
      181 lsnglllatg llsgglavif mlvfkntfgl ilatllasfv gylierihkt antkndgpdh
      241 ydltggevhh e
//
LOCUS       WP_010740813             316 aa            linear   BCT 01-JAN-2025
DEFINITION  aromatic acid exporter family protein [Enterococcus malodoratus].
ACCESSION   WP_010740813
VERSION     WP_010740813.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10369318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..316
                     /product="aromatic acid exporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35743
     Region          1..141
                     /region_name="FUSC_2"
                     /note="Fusaric acid resistance protein-like; cl19401"
                     /db_xref="CDD:450298"
     Region          147..307
                     /region_name="ArAE_1_C"
                     /note="Putative aromatic acid exporter C-terminal domain;
                     pfam11728"
                     /db_xref="CDD:432028"
ORIGIN      
        1 mkiglrtikt aaaapialli anglslesaa saaiitiltv tntkrstakt alnrifsltl
       61 atiiaaicfs llgfhplvfg lyllffipls lrldlaegia vssvlithyl vagemplsli
      121 fneyllmiig vgcalianly mpntekkiqe dqmvvevsmk kmlgqmsayl nqpakeeelr
      181 qeclslrdfv reaqiraqey eenrffsgns yyfeyfamrr lqlkiladml qilnrltaap
      241 edvqelrelf eftsqtlaed ndgsailiki setdrryqqk qlpdsrqafe eramlfqlfq
      301 lfqdfieika gfyrnk
//
LOCUS       WP_010740822             223 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus malodoratus].
ACCESSION   WP_010740822
VERSION     WP_010740822.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 223)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..223
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25028
     Region          1..219
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msdilrmeni ikkfgqghte vtalknidft vaqgefisvi gpsgsgkstf ltiagglqsp
       61 tegkitinga dfgqmnekdr skarfkeigf ilqssnlipf lkvqeqfqlv ekieqeknta
      121 kieellksld iwelreqypk elsggerqrv aiarslfndp qliladepta sldsdhaydv
      181 vkllakeahe rskaivmvth dermtqwsdk vyqmkdgkll mke
//
LOCUS       WP_010740823             356 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus malodoratus].
ACCESSION   WP_010740823
VERSION     WP_010740823.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..356
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38598
     Region          18..179
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          126..356
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflawkeiry aklryglivg imilvayvvf mlsglangla dgnrtaiddw gasaiilsed
       61 snkianasql qksdtdrvta kekagvgiys taaekknnge ktnvsifgts ndafvvpkvi
      121 kgrlykndne iivsenllse gyklnqqikv ndqtlkivgi tkettytlap viylnsttfk
      181 nlkygaqptg nepinliatk gqttidnqeg qtkldkmtpe tfienipgyt pekltlntmi
      241 yflfvvvtai igifmyvitl qktsifgvmk aqgvatsylv rsilaqaflv giigvavaig
      301 lsvltslilp sampfavhws ewalysvilv lvvmigglfs mravtkvdpv taigge
//
LOCUS       WP_010740838             519 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010740838
VERSION     WP_010740838.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..519
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59348
     Region          7..138
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          279..517
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mgaklkelmg lpslreaqlm sgqnclnqtv tsltfldian mddyaallet neyhsgelal
       61 tsffnikddv akqcetirrl hkmgelgiil yyvgvvlprl sseviktaed ldfviiqmpk
      121 nqnqirysev ivevmaeilk erstenlvne vlekasllpe hlrtvevtlk llsdllrtni
      181 iltnpdnevi nqikwprnss vdlerilrrv vvedgeqvqk ndfaifykel yhkengvlrf
      241 yllkehdllt eaecgqsvel lqvamnlwgk khgevseyal vqailndese kmyrlanhlk
      301 vdvkgielmw llqvndlree kklkqdilay askfyktcva qlmddqlivl lgnychtdse
      361 lelgeaylqt spyqdmidsi vlcprlrntt evrttyqlvn kvalqlpklf hgkksfsise
      421 irqvvcaskl iqsgeaevee tlsvlapimd skeqlmtlcs flldagadfq vcseqlfihk
      481 ntvkyrikki sealgynvmr fsesyecyla cltyrlisl
//
LOCUS       WP_010740840             477 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus malodoratus].
ACCESSION   WP_010740840
VERSION     WP_010740840.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..477
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53378
     Region          9..476
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mieekksfis wpilammsfv tvigfddiiy nfanqglgvi tswlilllly vipyslmvgq
       61 lgsvfnhegg gltswvrgts gdrlgyftaw tywaasipyv vdtanavvvg fgwlingnds
      121 medkmsnsmf alltfcvfla fiflqrhfkk slevlstlgg gamfimailf vfmtfaslfm
      181 pnghietqpm nlgavipkfd lhylttigll iyaingaelv apfvtrmrkp qrefpkamim
      241 ltvmtifltv fgsfslgvff nahhlpnnlk mngsyyafqr lgeffhlgnt lmyvfavtqi
      301 iymcallavl ldamtrmlis dtgkqfmpkk ltklnddglp ingyilttal safilllgvf
      361 lpemndifnw llnlngiisp gvtcwifyaf ikirldsrkf qsdyifiknd rmavfvgawc
      421 lvvtiiatlf gilpqdaayg sslfwhelii nvvgivvlig lgfimpalak rerekav
//
LOCUS       WP_010740921             199 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Enterococcus].
ACCESSION   WP_010740921
VERSION     WP_010740921.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..199
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22196
     Region          15..198
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 meylyqagkp ngkkfillhg tggdetslie lakfldadst ilsfrgtiee egmnrffkrn
       61 glnqfdfesl eketdhllea ineisaekai aledwilvgy snganiaahm lleretalae
      121 giffhpmsle vhtqsfnlsd kriwvsygga kdpivsddsf aelvaafrdr sgevtvvetn
      181 yghqltmdev qsarewlkg
//
LOCUS       WP_010740925             187 aa            linear   BCT 01-JAN-2025
DEFINITION  VanZ family protein [Enterococcus malodoratus].
ACCESSION   WP_010740925
VERSION     WP_010740925.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..187
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=22406
     Region          97..178
                     /region_name="VanZ"
                     /note="Glycopeptide antibiotics resistance protein
                     [Defense mechanisms]; COG4767"
                     /db_xref="CDD:443799"
ORIGIN      
        1 mkriiagivs lllsygmvyy lvmptlqnyp rldrmaqrfe ytdealwlfi flslwlfywq
       61 weqkrlwniy lylfyscyfl llfimlftka rayhsfnlnp felylnndqq iielflntay
      121 fiplgclygl rakkleaavi alitiigiet iqyvfyigtf diwdvitnft gcmigyflct
      181 qikrrma
//
LOCUS       WP_010740952             261 aa            linear   BCT 01-JAN-2025
DEFINITION  putative ABC transporter permease [Enterococcus malodoratus].
ACCESSION   WP_010740952
VERSION     WP_010740952.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..261
                     /product="putative ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30499
     Region          9..178
                     /region_name="COG4905"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443933"
ORIGIN      
        1 meqiftivvl lffcysfigw lwetvycsik akhfvyrgfl lgpitpiygf gvvgvlylie
       61 pyqrnivllf flalilvtal eyltsfllek ifhltlwdyk evplningrv avpvsifwgl
      121 acvfivrvln pylmsliidw qqrfgiflpm illmstsfdl gftlanlasl rqainkmsat
      181 iqdkkeqvqt dlgelkvaae erlqnrqwla emkeqpewrk qlpklnfqer rflnsfpnmk
      241 skeiksplte irqlskelrk k
//
LOCUS       WP_010740980             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010740980
VERSION     WP_010740980.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..272
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30071
     Region          1..269
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 maitytiqen ystltksekk iadyilssge kivhstmsdi reatkvgdgt iirfcqkigf
       61 sgfsdlkiai akedfskqqe dsqesdlfdk rtktinnalk ttnqrldsek lqqavqlitn
      121 anqiyifgvg ssgntgndle amllrvgvqs ravidphfqa qiaslltekd lvigfslsgr
      181 tkdtydsmdi akknkakvia itnyqlspia qladivlqta ieefldgasl agkisqlylc
      241 dllvqryeie nnvnsielre tvlrsildks ld
//
LOCUS       WP_010740991             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Cof-type HAD-IIB family hydrolase [Enterococcus].
ACCESSION   WP_010740991
VERSION     WP_010740991.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..268
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29771
     Region          4..263
                     /region_name="HAD_YbiV-Like"
                     /note="Escherichia coli YbiV sugar
                     phosphatase/phosphotransferase and related proteins;
                     belongs to the haloacid dehalogenase-like superfamily;
                     cd07518"
                     /db_xref="CDD:319820"
     Site            order(9..13,44..46,67,151,153,187,195,217..219,221..222)
                     /site_type="active"
                     /db_xref="CDD:319820"
ORIGIN      
        1 mtikmiavdm dgtflddqke ynrerfekif hqikekdikf vvasgnqydq lksffpelhk
       61 emsfvsenga niivegndyy naqlpiekvm kvltgleale ptvtvvcgkk sayvsqempe
      121 evfnnvqfyy psnkkldrle eiaaeedeif kfaltfpntg ieaklaaltd ilagemipvs
      181 sghgdidlii pgvhkafgla klsdkwginp aeiaafgdsg ndiemlkyag esfavdnaqe
      241 kvkqasneii gsnnqesvld kielllks
//
LOCUS       WP_010740997             608 aa            linear   BCT 01-JAN-2025
DEFINITION  vWA domain-containing protein [Enterococcus malodoratus].
ACCESSION   WP_010740997
VERSION     WP_010740997.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10646251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..608
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=68968
     Region          330..>456
                     /region_name="VWA"
                     /note="von Willebrand factor (vWF) type A domain;
                     smart00327"
                     /db_xref="CDD:214621"
     Site            order(336,422,452)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238119"
ORIGIN      
        1 mkrlrkwltf vmafsclini lpikqlqafa ekkeetslid tdqlqvsfet eslkgnnvwr
       61 iktkrksdaq rqrlkvkvlt dekkeidypk ikgmevqegw lvdqeftvse kremtfklse
      121 kqkslllyvq ldeqqlhsee gedeirkdil ettepfvlkl qdrkedkqeh satstsnekr
      181 kkteasketd keqegprisg sqianaalps pvqragtygi nrytnkvpvy kkdtkgtypt
      241 nswqpdnqtn vinhqggien qkgsddleiw dgkknwdvta dryensyihy gganapsisl
      301 rkyaketdke daftvklnvr ggtvqkpgid ifflldnsgs miqnkignlt rkevandylg
      361 klltalndqq tvtggriqig ghifsdyrqw pnepklhsls ptysnwlqmq nqyaslssag
      421 dtytqrglie sdnylskstd akrrkvlfvl tdgtptlsat pkggyvdnnm yydkiminnf
      481 dyqenytygs rfqgvndpsp tkikpgnypn gykmadgkyi nshitttnst aktlkdkgie
      541 ihtvaiginp amdpprvveg htkeelrssk llgtsrsknn gratnersey rcfqksgngg
      601 ikcresve
//
LOCUS       WP_010741006             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            malodoratus].
ACCESSION   WP_010741006
VERSION     WP_010741006.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..305
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34329
     Region          1..282
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mllsekmrqt dfsnaeaalv nyvldkgiei epltikeiae anfvhpstli rvakklgykg
       61 wlelrtefla eqtylqtyfe dvdanfpfqt ndglmtiank iaslerttvd dtlsllnhdd
      121 lqnakqllln akqikifgsn anllisqdfa lkmrrikknv vtsqtmgedt yeafnsqedt
      181 cailisytge nnfilrlaki lrkqnipvia ltsigdntla sisqatlrit trerlyskia
      241 nftinssicy lldvlyscvf aedyqknlnh liaigeladt rktsseimae spesmiqise
      301 sfrpn
//
LOCUS       WP_010741042             156 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Enterococcus].
ACCESSION   WP_010741042
VERSION     WP_010741042.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..156
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16985
     Region          5..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mdqeyskimv avdgsneael afkkavnvak rnqaelllah vidtrafqtv ssfdnvlaeq
       61 atdmakqtld dyeadaksag vehiskviey gapkvmianq ipennqidli mlgatglnav
      121 erlfigsvse yvirnaacdv livrtdldnk vpeede
//
LOCUS       WP_010741152             311 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfurtransferase [Enterococcus malodoratus].
ACCESSION   WP_010741152
VERSION     WP_010741152.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..311
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33896
     Region          53..304
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mkktiiglla lvtlglvgcg gggdktdsad saktakkett aftgeyivna dyvkknldei
       61 ilvdargeee ankgtvkgat aigwqnlaav eegasgdekw glvlepvela krlgekgiak
      121 dkvvvlfaga qkgwgddgri awellatgyk dvkmvdggfa alkkaglkte vestklepvt
      181 vkidsidqkh iirtdelkke yddykivdvr ddkeykgevl ygeakgghlp eaiqvrftdl
      241 fnskgmlksk aeltklfeda glakndkivt yctagirsay melvmemcgf kqvknydgsy
      301 yrwakvedve k
//
LOCUS       WP_010741167             184 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Enterococcus malodoratus].
ACCESSION   WP_010741167
VERSION     WP_010741167.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..184
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20860
     Region          2..173
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 miylarhgqt qwnvekricg radiplteeg ykqaellaeq aktltdpitq iicsplirak
       61 etaqvvaiql glpiivderl iemdfglydg lpiqteefqn rrnefslpfe qgesildvag
      121 riypllaelt gqekelpllv chnavsrvvd nyfngktmse flgfniente lvryiqrtpi
      181 shek
//
LOCUS       WP_010741341             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Enterococcus].
ACCESSION   WP_010741341
VERSION     WP_010741341.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..190
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21025
     Region          6..190
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mkrkgsgiiv glvvialaig aylmttynsl asaendvdak wsqvenvmqr radlipnlvn
       61 svkgsmnhee kivkeitdar ksynsaktpa eknaannqie qslgtmvnvi qenyptlasn
      121 envktlmvql egtenrisve rknyieqvnd ynqslvrfpk nmaakvlgfd kkanfkaddk
      181 akevpdvsfe
//
LOCUS       WP_010741365             233 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus
            malodoratus].
ACCESSION   WP_010741365
VERSION     WP_010741365.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..233
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26909
     Region          145..220
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mtkvliitkn llaeqdlqav lqrsnaevyc sydlmldaqh fpqvisyfsv vifsdtistl
       61 evskyystfk qnglfilrkg npehlkqtel sylfdeiddw idpvtsnlgi iekiakltsk
      121 qsiypssekr tnskidinse tfffslssne kkllyhlyqf qkdgailsre klcsllwetq
      181 vtksnlcqls nltnrirkkl stynfpegel itswnkgyfl gdllfnevkn yld
//
LOCUS       WP_010741391             307 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus malodoratus].
ACCESSION   WP_010741391
VERSION     WP_010741391.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..307
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31970
     Region          4..297
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mnvitlllsa tsqgmlwsll aigvymtfri ldiadltaeg sfplgggiaa igivngihpv
       61 latllafggg mlaglvtgil ntkfkipall agiitmtgly sitsrvmgap niallgesti
      121 ftaaqdmglt knnavilvgl livllvilll vlffrteigl avratgdnpd mseangikte
      181 nmklvgymis ngsialsgal laqnngfadl nagvgtivig lasiiiaevl lhnkpilirl
      241 itivagaiiy rfilalvfem nveptdskla saivlvicls lpqirskftl ktkkkgadtd
      301 atslknq
//
LOCUS       WP_010741401             277 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus malodoratus].
ACCESSION   WP_010741401
VERSION     WP_010741401.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..277
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30216
     Region          6..270
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,206,228..230,232..233)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mdikaivldi dgtllttgkv isektkqali aaqekgikvi lasgrpttgm lelaeqlemt
       61 kyegylvsyn gsrvtdcltk evvfnqamsv etgqailehl kkfdvmpmid kedylyvndv
      121 ynntlhlpdg dfniieyesr ggnfklceid dlaafatfpi nkiliaaqpd ylqenadaih
      181 apfdetvtaa fsapfyfeft dkgidkakal ntvfpdlgih synmiafgdg hndrsiieya
      241 gigvamgnav ddlkaiaddv tltcdedgia aglakyl
//
LOCUS       WP_010741402             454 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus malodoratus].
ACCESSION   WP_010741402
VERSION     WP_010741402.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50313
     Region          20..439
                     /region_name="MFS_MelB_like"
                     /note="Salmonella enterica Na+/melibiose symporter MelB
                     and similar transporters of the Major Facilitator
                     Superfamily; cd17332"
                     /db_xref="CDD:340890"
     Site            order(30..31,34..35,38,71,132..133,135..137,140,161,
                     164..165,168,246,249..250,253..255,258,286,290,339..340,
                     344,348,371,374..375,378..379,382)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340890"
ORIGIN      
        1 mettqtnqvk nkrtnkwqqr igygvsdlac nliwqmisly llyfytdimh lsaasislmf
       61 vvtrfvdgmt dllvgylidh tntrwgksrp yflfgaipfa lfaflcfnvp dfsasgklvy
      121 ayvtyfglsl aytlvnvpma silpsltndt eertalstsr kffaflgati vsstaltlva
      181 ffgngnerig fkivmgifgi igcllffftf fsvrelpmrs sksvslktvf tslkqnkpwl
      241 ifavnilfmw tsffiqssal vyyfsvvvgn ktlsitvati msvvpmfanf fvpmlakkig
      301 krnlyilsss iqliglviim faakavagil fgafisaigy gikesiyfsm qadpvdygew
      361 ktgvnvsgsl saingflgkv aqaisgglag allawgmykp geavqtgkam faiqamylyv
      421 pmilifcsii tmlfynldki yptikaelee rrna
//
LOCUS       WP_010741430             382 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Enterococcus malodoratus].
ACCESSION   WP_010741430
VERSION     WP_010741430.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..382
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41151
     Region          1..376
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mefigvlcli listtiashf srrfgipavi gqllvgillg saglklvhpd ilvedfseig
       61 villmflagi esdlsllrky frpgmyvavl givfpvllgt lggnvfhiaw nesfflglil
      121 aatsvsisve vlkelnvint kegstilgas vvddilvvli vslsmsflga ksgndnplgi
      181 mlieqvlffa aifflirwga pylmrlskkl laessviivs lilclsmsyl adfiglssvi
      241 gafftgvaig qtnvwkdvqh nveaigyavf ipvffvsigl eisfngisnq lllivivtil
      301 aiiskllggf igsklagfsn hsslmvgsgm isrgemalii vqlgyqaqlv tkeyysafil
      361 vilfttlssp fllkyftkki ys
//
LOCUS       WP_010741406             323 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus malodoratus].
ACCESSION   WP_010741406
VERSION     WP_010741406.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37685
     Region          39..125
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <157..322
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnyeelkeil rqeneiekiq rtkgynvndq nlpfedvaip kmpssnffke gnifinkhhr
       61 ysampnhthe fvefnymisg sctqyvnekk vvlqegeiil ldkdivqrid plseddllvn
      121 illkdesitt diiinmvkst glvneflmna snktgkhdaf ihfhcggkde vqkiiqnlis
      181 eylqkrryym raanlllsll lieltrmiee esldnyqkkd eeiicilkyi dihfrqlslk
      241 dlakefgyns nyignklkke tgrtfqdlln sakyqtalel mketdksiee iayevgfnsl
      301 pslyklfarf tdktpkqvrn klt
//
LOCUS       WP_010741439             497 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus malodoratus].
ACCESSION   WP_010741439
VERSION     WP_010741439.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 497)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..497
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52218
     Region          190..495
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnyikratqs lwakkgrsii miavfsaili fvlagltirs gaelattnak ksvgatvtls
       61 tnreamfnqq setdsdeett rpdpgsfert pvnlsdaeki aklsnvksys feastsadks
      121 tgitpissds dseeassdeq asgfggqgap dgmsqgdfqi kgvsqssays efssgtaslv
      181 kgeaitskde gsnnvlieqs laeandlsvg dtfkikdsnd kdveatvkgi yktsnsgdsm
      241 sarfnfmnpa ntifssytmv ntlagsdgkt idsavynltd pkdmdsfvkq anklidtdtf
      301 sletndqmyq qmlqplnnvs sfaknivilv aaagviiltl iimlsirerk yeigvllslg
      361 esrvkvisqf fveifvcmif algiaaasgn vvgnavgnql lsqqttsqnt dgqadaagng
      421 gpgqgqapgg gnggprgggq mgsnpftqse eiqelnismq pteilslagi glgislfsiv
      481 lssagilrln pkkilis
//
LOCUS       WP_010741458             323 aa            linear   BCT 01-JAN-2025
DEFINITION  sialidase family protein [Enterococcus malodoratus].
ACCESSION   WP_010741458
VERSION     WP_010741458.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..323
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36306
     Region          152..>289
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mknrkptsss ykshspwstv lrdipftirv ivltivigls vvsynigkav teakatsqte
       61 vtfpskrtkk ttvddvkirr nndrwefssd egiswsttpp dgiyedadgr lryknskser
      121 inntssedtf kfpfsdkkgn smimkreedk wkfssdggkt wseekpegve idkngkltwk
      181 stdgkkvsef dpkenqwkys edggktwsdp lkeiedwlen gftvpvedgv smkikdgkiq
      241 ystdggktws eeapegfndk iqsvitkqsd dgktlystdg gktwseekpe gyeipsvqdi
      301 ldsipddlvp kdedlgeges tai
//
LOCUS       WP_010741518             692 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus
            malodoratus].
ACCESSION   WP_010741518
VERSION     WP_010741518.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..692
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=80721
     Region          12..671
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnmnledrnn qilmelinnp qitskvlyer fdlsrsqlny alkkindfle dgklpqikrt
       61 kkgyflvpnv visafgggke kehekiehyi fsgqeriwvi ellilakdey lsldhfilel
      121 kvsrntilrd lrkvgedvgk ydlelkytrq kgyhfhgdew nkrellsvtl mnlaeihdgi
      181 ncisqfskid idlvevfkkr iglveeklni qftddrlkvl pllviliirr akrgkqisyn
      241 fkindfelad tkeflaaehi iwdvdkisrn ervyltllll ttnlsqanil svremdklke
      301 allqvlnnfe kisglsverk erllerllih mrpayyriky hlnlqtrfyq enkdsdlfsl
      361 fylvkessep lenffgeaip dpelflislf igshiveste iirdenrrra iivcpngisi
      421 slllkntlqn llpeidfvel iserkfyrnn yevdfifsai pletekpvfv vnnfltdqek
      481 rqlrervlrs vslsqntvin pekimslikk yavisdeenl yhelltlftp kdfemvekkr
      541 ihlidtlkid tiqlfddeie wlelldklaw plekqnvisn nfvnalkqem pilpqytvlr
      601 ntiglphtmc eagalgvgls mgivkkgilt engskvhtvv llasndkdkh vdlifelmnl
      661 agseqlkeie eatsineilt llvdfsdeyw rn
//
LOCUS       WP_010741562             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_010741562
VERSION     WP_010741562.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..146
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16630
     Region          <39..135
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mkiemaelfs kehtgavklr kqvlggkidw dneknlsvfv avendevvgt aaiqlypfgi
       61 arvrqvavsp dyqgqhigdq lmssleefaq eqghfriilt grktaqlfym krdyhrvlgy
      121 ftkhdiefiw mtkvlpavev pvfsen
//
LOCUS       WP_010741626             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Enterococcus].
ACCESSION   WP_010741626
VERSION     WP_010741626.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10084616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=15815
     Region          7..142
                     /region_name="USP-like"
                     /note="universal stress protein (USP) and similar
                     proteins; cd00293"
                     /db_xref="CDD:467483"
ORIGIN      
        1 mirkyqnilv aidgsehseh afdeaveaak rydaklnvis iindselsts afsfskiyaa
       61 ekeqiekeml kkvhdasrke ldnvepfvel gspkekivef akdneidmif lgatgkgeir
      121 lsrigstaay vvnhapcsvt vir
//
LOCUS       WP_010741575             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Enterococcus].
ACCESSION   WP_010741575
VERSION     WP_010741575.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..282
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32103
     Region          5..271
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mpkkaetyvv gnfkggvgks ttvqmlsfes afrknrktlv idldpqgnts dvlsltaenf
       61 gnenlpeefd stiweavrsg niqssiyqim pnldlipani sfsdfpdymi ekypsdklsq
      121 fkymekliep lkdiydviyi dvpptistys naamyvaeyv ivilqtqvka lkgaqnyidy
      181 msffieqydt dlevvgivpf mmqkrdsvdq eiytaakeiy gahlldtvvl nqsrlkrydg
      241 sgitydinkn gkveqwdkra hevfvnilde idehrlilsg ee
//
LOCUS       WP_010741639             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Enterococcus].
ACCESSION   WP_010741639
VERSION     WP_010741639.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..145
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15507
     Region          5..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mvdeyknilv avdgseqskk afdeainiak rnngkltlat vidtasfsgt tggnsiplmq
       61 evhekaqkii telehhriae eqevhltsqi iagnpkreiv elaekleidl ivmgatglga
      121 lslllvgstt ayvvnqapcn vmvvk
//
LOCUS       WP_010741682             312 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus malodoratus].
ACCESSION   WP_010741682
VERSION     WP_010741682.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..312
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34967
     Region          6..180
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(9,11,85)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(38,84..85)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            83..85
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mdkiavlipc yneaqtiqav iddfkkelpe gtiyvydnns tddtyaiaka agvkvkkesr
       61 qgkgnvvrtm freidaecyl lvdgddtypa kdarnlcrev lengadmvtg drlsstyfse
      121 nkrpfhnsgn vivrnlinyf fkgnikdilt gyralsplfa ksmpvlskgf eietemniha
      181 ldknfviknv evdyrdrpeg sdsklntvsd glrviktifq lfkdyrpllf fsalaafltv
      241 lavilgipvf ldyfrtglve rmptlitagf lmlaallnls cgfildtenk karqnfelql
      301 nvlhqlikgg na
//
LOCUS       WP_010741649             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010741649
VERSION     WP_010741649.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 205)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..205
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21903
     Region          1..203
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mfdnlvqyls enssylitqf gvhvyisvig vvltfligfp lgillserpk lsdivigiin
       61 viqtipsiam ltvllilmgl gqntvvatvv lysllpivkn tyvglvnvdp myvdsakgig
      121 mnryqilymi kiplampvil agvrnalvis vgittigsfv gaggvgdvil rgiaitdggp
      181 iiivgavlca fiammmdwlf dwimk
//
LOCUS       WP_010741706             496 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BCCT family transporter [Enterococcus].
ACCESSION   WP_010741706
VERSION     WP_010741706.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..496
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53984
     Region          3..493
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mkknivfyvs llitavivlv glvapkpfaq amngtkaflv dtfgwfylia mfvfvifsll
       61 iafsrfgkik lgpddsvpey snrswfamlf gagmgiglvf wgvaeplnhf atfggtekaa
      121 dlamqksflh wgfhpwaays iigmalayfq frkktpglis siflpilgee gvrgpigkii
      181 dicavfatva giatslgqgt lqinsglnyl fdipttrlvq iviivsltvv ytwtavsgid
      241 kgikllsdin lflavaillg afligpkims lniftnsfgg yinnlvsesf sinpfgdnaw
      301 lgswtifyws wwiawgpfvg tfiariskgr tikefvlgvi iapsmvsfiw fsifgslgln
      361 ldieiinkak avtetalfvv laeyplgmff siiaicllct ffitsansgi fvlsmfsseg
      421 dlnpgndkki lwgviqalla lvllmtggld alqtcsivaa lpltvimllc avclfkallq
      481 ekpkpeelsk saelek
//
LOCUS       WP_010741725             164 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010741725
VERSION     WP_010741725.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..164
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18943
     Region          7..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 meqskrkqll kliesdcrls meeyavmlge devivsaeik rleeekiicg yralidwdkv
       61 eddwiealve vqtipkgeeg yreiaervrk fpevksfffv sggfdfilll qgrnikeisk
      121 fistnlasip dvsgtqthfl ldkykewgid myqddsdpri qvsp
//
LOCUS       WP_010741729             462 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Enterococcus].
ACCESSION   WP_010741729
VERSION     WP_010741729.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..462
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51103
     Region          2..445
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mesheelerg lknrhvqlis iggaigtglf lgagktiqlt gpsillsymi tgiiiflimr
       61 algelmlsnl nyhsfldfia dylgnkaafv tgwtywfcwi aiamadltat gmyvnywlpg
      121 ipqwlpeiia lvlllglnlv avglfgemef wfalikvvai ivlivvgafm iftsfktsag
      181 tvnvsnlwsh ggffpkgmng fvlsfqmatf afcgvelvgl iggetsdpks vlpkaintip
      241 lriilfylgs lfmimsiypw sslsadqspf vqvfseigia aaasivnlvv lssamsacns
      301 aiystsrmvr slaqegsaps rftkltrnrv pgnalvfstl vifiavilnf fvpsriftmi
      361 ssiaticfif iwgmivlthm ryrktkpela akgsfklplf pytsylifaf lafvlfvlal
      421 addtrealff spiwfitllg iyyfkfeqni pifnkifrns dd
//
LOCUS       WP_010741755             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Enterococcus].
ACCESSION   WP_010741755
VERSION     WP_010741755.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..316
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35297
     Region          81..288
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mterisleqa aiefseanap hpriyelppe egralleqvq espvaklavq iedqtistgq
       61 wgeinvrfir pegavgplpv ifyihgagwv fgsakthdkl vrelavrtns ivvfpeysrs
      121 peakyptaie qnfailqqlp nlaaeknmdi drltvsgdsv ggnmatvmti mtkqrggvpi
      181 kqqvlyypvt danfetdsyn qfaedyfltk egmqwfwdqy tkdrgeraei tasplrasle
      241 elsglppami lngeadvlrd egeayarrlr eagvevaqvr fqgmihdfvm vnsldqtnaa
      301 raamtlstew ikqknk
//
LOCUS       WP_010741769             175 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus malodoratus].
ACCESSION   WP_010741769
VERSION     WP_010741769.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..175
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19648
     Region          4..175
                     /region_name="COG3981"
                     /note="Predicted acetyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443180"
ORIGIN      
        1 metiqlvhpa kkheaavldy ieehfsngen flhgssllte mesydawleh lakqsdktsv
       61 ssdwvvsttl lairkndqki lgtidirhel ndflqafggh igcgvrpser rkgyateilr
      121 lglaycqtlg lekvmvacyk enspsaqmiq knggvleref thvdgkmvqv ywinl
//
LOCUS       WP_010741774             104 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010741774
VERSION     WP_010741774.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..104
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12059
     Region          1..91
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mdsqlkkgli eycvlaslvd vdsygyqivk eihpriaite stlypilkrl etnkkvatys
       61 kvhngrlrky yhltdlgfas iqkflqewnd veavhnyirr svee
//
LOCUS       WP_010741783             374 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LCP family protein [Enterococcus].
ACCESSION   WP_010741783
VERSION     WP_010741783.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..374
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=42142
     Region          59..301
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mkraqkiill cltailmcti svsayfllan qhlrktldng yhpikneyht knkkdteafl
       61 imgldntier klgttrtdam mvvtlnnktk kitfcslprd sfvpidskny hgnqrieaay
      121 tfdgptasin tvekllnipi dhycvfnfls fikfidaigg ididvqhsfd gvtkdgpgai
      181 hfdegkqhvd gtkalsyare rhsdndimrg frqqeiiqsv gnklkskeav knltgiidsf
      241 nnniqtditt dqllalmkng lvysdyekqr ltfdwrtfsn qgrsmvelyp dsidyvshel
      301 rvslgidkkn eqdkkgfvfh tdgdylyqsd ysvqdeaaed kestslngnt yigtpdntet
      361 galptvktkn gfvp
//
LOCUS       WP_010741807             366 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            malodoratus].
ACCESSION   WP_010741807
VERSION     WP_010741807.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..366
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=41382
     Region          180..283
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mymkernekk qlaifsmiaf glpvimglfm wygysnnknl dlfsmahmyy paagamiall
       61 lsnsnhklip kpfficyllq tammigislf slfsnsealp qlsgllmivg glllwlclli
      121 akkdrraayg lsrknwkati wmvalyvily tarmvvayaa egnfsgmlei ftksavwial
      181 lstlvsyipl fvpyfgeeyg wryffqpilq krygslkgvl ilgvlwglwh lplnfffyts
      241 padglisvtn qvvvcltlgi fyayaymktd niwtvvamhf lnnnlvpifs gdltgesakg
      301 ysitwsmvgm mailmticya wpaltkffkd rgnlnptpeh radtvaynle neneqktatl
      361 nqspak
//
LOCUS       WP_010741859             261 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010741859
VERSION     WP_010741859.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..261
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28776
     Region          1..255
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mlkieqlsvq yqgnpqptlh dfnlsidkgg ivcivgesgs gkstvlktii galpkktqis
       61 gmiqfeemsl lqqsvsewqk mrgtvfsmif qdstaalnpi rkigkqyeey irqhesvsse
      121 darkqaeaml kkmqlrdars imdsyphqls ggmcqrigia lamtfnprll ladeptsald
      181 vvtqeqiveq llqvreqfsv svllvthnva maahmadrli vmengkivdq gsplevitqp
      241 ksaytkklla svpelkgaay v
//
LOCUS       WP_010741829             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010741829
VERSION     WP_010741829.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..218
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24390
     Region          4..216
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mvyqlnhteh kiyqkimkai akgelpkltk vaeenyvstt yivkfakklg ysgfsemiyv
       61 nkykqrlgnt asnseialfd qedvhklaal isqfsdkiif vfgigysaii adylqkklsk
      121 lglfvnsssp idmtipyqey lvifisksge tddvleiakk ikstvsasil ltaasdstig
      181 rhvthtqvve terepnapdl fdskclalfe yillelnq
//
LOCUS       WP_010741880             271 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Cof-type HAD-IIB family hydrolase [Enterococcus].
ACCESSION   WP_010741880
VERSION     WP_010741880.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..271
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30130
     Region          6..261
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(10..14,44..45,194,216..218,220..221)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mseiqlivid ldgtllnaqk eitarnieai rqssakgiki aiasgrlypd ivrlfnrelq
       61 vsgykiclng syilneenqv isktriersl lnkifeiayn nevslfcngl iysvnfagid
      121 sdesvlngrt lwvkdsdefn qkldemalni ykfglhstnl drlkeavedl ralgismvrt
      181 etyffeganq ginkfegikq vaqslgistk nilaigdqen dfemirnvgf gvamgnaipa
      241 iksvakyitn tnerdgvaqi ihdlilkedd a
//
LOCUS       WP_010741922             353 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus malodoratus].
ACCESSION   WP_010741922
VERSION     WP_010741922.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..353
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38293
     Region          123..352
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflaineikh sklrytlvmg vmfliaylvf fltglaygla qdnrtavdkw dadsilltee
       61 annnlnmsmi plktfdevka dekaylaqta gvikgeggek idvsffgidk dqflapklts
      121 gkmfssddea vadislkdey dlkigetvkm agndktlkiv gftnnakfnv apvlyttiga
      181 yqeirfetqg tsentrinai itrgkvqstp ddldktdiks findlpgysa qvltfgfmig
      241 fliviaaivi gifiyvltmq kaeifgvmka qgissryisn sviaqtflla tvgvviglaa
      301 tlgtalvlpd avpfqvnmlf fggislmmia valigaffsv rtivkidplk aig
//
LOCUS       WP_010741943             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010741943
VERSION     WP_010741943.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..239
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27523
     Region          1..227
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mpkyeeiant lrnrikndty pagsllpkqi elvkefsvsr mtvqkaleil tlegllaskk
       61 gvgttilnhp fltkdtsvls yyeglsteme kanrkleskv iefnvefpda aiqeklhise
      121 eepvykiirl rilddkpfil ehtympiqav pnlkkeiies siyqyikkel gikitgayrt
      181 iradksseyd qtyldcavdd pvleirqiay qqngdpieys rsrnrfdvrd ysyldmkgn
//
LOCUS       WP_010741950             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010741950
VERSION     WP_010741950.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..249
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28023
     Region          1..248
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlkeerhqki vdllnieqkv iasdlsqrfn vsedtirrdl keldnqgllk rvhsgalrvg
       61 ppitdfnyre tvasdrkkel ahkalpflke dsviiidgst tnlalakeip qdfratiitn
      121 sppialelaq hsnleiinig gvfykqsmin igvqaykqlq niradlyvmg iynldleagt
      181 svpttqesei kremvriste vlgmitndkf gtisnhivgp vddltylise eipdkvrkey
      241 nkqkivlid
//
LOCUS       WP_010741986             282 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Enterococcus
            malodoratus].
ACCESSION   WP_010741986
VERSION     WP_010741986.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..282
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29383
     Region          31..279
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlsqiglllv tgvlagilgs ilgigggiil tpfltlimgl dikyaiaasi vcviatssga
       61 tiaylkddml nlrvamflei attigaivga llsgvvptgf lfilfggfll fsvsnmiqkl
      121 rgkankqvkk atedsladkl klngsyydkv leeqidyqve kvpggfammf gagiasgllg
      181 igsgvfkvta mdtimkmplk pssatsnlmm gvtaaasatv yffsgailpq iaaplalgvl
      241 vgatigsrim qrlkpivirl ifipillfmg iqmvlrgfgv ii
//
LOCUS       WP_010741969             212 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            malodoratus].
ACCESSION   WP_010741969
VERSION     WP_010741969.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..212
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=23309
     Region          105..201
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mdkilnkqva fknigiatai liaglaillf gpgylgffsv aatslialli vypkksvqai
       61 fgkplhpvki iigyfllnwl vsivvsllln yglgwhlqgn pindnpswll lftipimlmg
      121 eellsiyfls vfsskfslpi asllsalifg lihystyndg nvlhtlahil liqgvarlif
      181 nraaiktnsi wtswiihvlf dsstillvll qh
//
LOCUS       WP_010742001             483 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein/permease
            [Enterococcus].
ACCESSION   WP_010742001
VERSION     WP_010742001.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 483)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11705690
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..483
                     /product="ABC transporter substrate-binding
                     protein/permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52753
     Region          37..261
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Region          271..480
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mkkkigalvt vllmllsflp akaqgaekde iyeriqqsge lvvglsadya pyefhadvdg
       61 tdkivgfdis iakkiakdmg vklkieelgf dallgalktg kidlvisgms iteerlkevd
      121 fsdpyfvvqq kvlvrkgdkn kykttadfng vpvgaqkqtt qedlvknelt gadptslqkv
      181 pdlinnllnk kveavvleqp vaeayvqqsd nvelapvkfe qgekvtaiam skntpelkkh
      241 vnasiktind kgllkgyqke anelmfqgek sflqkygpyy lngakytill afvgvlfgli
      301 fgsllalmkl skskilkala viyieyvrgt pllvqifivy fgtgvigldl skllagciav
      361 slnsaayvae ivraginavn kgqmeaarsl gmnqkeamry ivfpqaikni lpalgnefvt
      421 iikessvvsv igvselifqt gvvqgasfkp flpyvlvsli yfvltfcisr llglverrmg
      481 lnd
//
LOCUS       WP_010742069             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus malodoratus].
ACCESSION   WP_010742069
VERSION     WP_010742069.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44271
     Region          7..399
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(17..18,21..22,25,57,111..112,114..116,119,139,
                     142..143,146,225,228..229,232..234,238,262,266,326..327,
                     331,335,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mrknknfnll igsqlfsvlg ttivqfvisl yvlditksaf tfsviaslsv vgrliclpfc
       61 gvladrlpkr nlmlfmdcly lvlsvglflv trlanpvtai giltviigmv safetpvvqs
      121 aipvictdee iprangiiss igtlgtvlgp iiagiiyrfd avyqifvitg vlfliaifce
      181 vlltiptqsq avtegslfqv vagdlkevtq ylkaqkvivk vamvafllnf flasfiqvii
      241 pyvsriqlgv sdaqfglmnt ilaigsllgt vvygvianrl netsitknli lvailfgllv
      301 ipfgliqnaa lafwvmtiiv acamgvvtvv svqlivyiql vsdkallgri mslvmivttl
      361 avplgqvmyg gfaavaseam lliliagtsl vtvliaffsi kifkqmrven el
//
LOCUS       WP_010742093             311 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010742093
VERSION     WP_010742093.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..311
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34550
     Region          5..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mkslievknl eksyknkqvi hgisfsiyqg eilcllgpng asksttinil cgalgfdrge
       61 vtckgdpidq nlqafkqqlg vvpqdlalye dltaeknvqf faslyglkgk eleagvtfal
      121 nsvgltshrk ekvatfsggm krrlniacai ahrpallimd eptvgidpqs rnhiltsikn
      181 mqlkgmtvly tthymeevee issriiimdh griiaegtke alkeknderk itieisdsnd
      241 isldtfyqie gvkevtlnkd elritsikgi enldhiigkl islqqkiqnv fvqeanleti
      301 fldltgrslr d
//
LOCUS       WP_010742103             209 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            malodoratus].
ACCESSION   WP_010742103
VERSION     WP_010742103.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23698
     Region          4..>80
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrvskdptvr kneildvagr lfaekgfdqt stgeiitqag iargtlyyhf kskeeimdal
       61 verttsllfd aakkvaddhs ipvyqrfvqt vlalrldtsk ddtmmdyvhk pqnalmhqki
      121 qtalvreitp vltgivedgi qqgifqtdyp yesvelvvvy asvafdeqem vpdsrakkeh
      181 rvksffylle rllgveegkl aremegmfd
//
LOCUS       WP_010742128             171 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010742128
VERSION     WP_010742128.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..171
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20075
     Region          12..>98
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maktnysisl qedsknfite atlqlldsks fnkltvmevv kragvsrmaf yrnfesiedv
       61 lkqyycpkfe affdkikkth geeelvilte ffsvmksdli kainhdydsi ffdilsqqte
      121 lfiqpqnrse yyqmkfiiag tftvwkvwlt eedetslaem wallsnltkk y
//
LOCUS       WP_010742131             144 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Enterococcus malodoratus].
ACCESSION   WP_010742131
VERSION     WP_010742131.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..144
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=15971
     Region          10..143
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mvkqvlkaev eslgglqlkc sargfefmid epenvggtne amnpleallc slgackmmvv
       61 rffyqakqik lksmrveilg eidsdrlkgk pdvkvgfski itnyyidadn tdeeiqdlva
      121 fiektcpvkd tivnapemel hinp
//
LOCUS       WP_010742138             192 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            malodoratus].
ACCESSION   WP_010742138
VERSION     WP_010742138.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22255
     Region          10..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkrkqdsllt kqrlletafq nfyevgfent sldkiskdan vsrgaaywhf knkseifgev
       61 vrmtiekikd ekreimlses lefkekvvqi livpshnqig fkfmqqslkt levypefsel
      121 lenfretrar lynffltglr negltendaa aissmlynyf egmygsgtpe evtknytpea
      181 ikrsitiifk na
//
LOCUS       WP_010742141             386 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Enterococcus].
ACCESSION   WP_010742141
VERSION     WP_010742141.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..386
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43543
     Region          22..303
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mltilinkit erwkgnkrts vgilagilgl isnlilflak ffigslsgsv simadamnnl
       61 sdtassvitl agfkiagkpa dedhpygher feyisgfvis ilvtyvgvrf ldssfvkimh
      121 pssvllspiv yivlilsilm kfwqshmyqk lsreinsdtl kataqdsind vyttiavlvs
      181 aivewfsgwr idgyigflia lyiiysgikm ilgfindlmg vrppeaevla irkhldhypd
      241 iigyhdllih sygpnsifas vhievdqdws lphahevids ieyevkeslg vdlvchldpy
      301 plddpdfkri apelkktlkd ihpqlrfhdl rvdktttpet iyfdlvvpeq lkkvkntqlh
      361 dqisqhfisq selaklvitf drtyll
//
LOCUS       WP_010742279             250 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            malodoratus].
ACCESSION   WP_010742279
VERSION     WP_010742279.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..250
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28735
     Region          1..234
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlktdrfqai msllevsgtv rvneimekls vsdmtvrrdl delekqglle rvhggaklkd
       61 fyrhvelsht ekqimlqaek qrivekanel indgdtiflg pgttiellsk iikadglriv
      121 tnclpvfeel nkhkgnrkiy llggelrett qcfvgeitnk slndmnfhka ffscnalneq
      181 kimtstfeeg qtqqialnns verfllidhs kigkrdfsvy ynlhdvtavi idedeqkhye
      241 kiekeeryiv
//
LOCUS       WP_010742196             404 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus malodoratus].
ACCESSION   WP_010742196
VERSION     WP_010742196.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..404
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43211
     Region          8..388
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(20..21,24..25,28,60,111..112,114..116,119,139,
                     142..143,146,218,221..222,225..227,230,258,262,314..315,
                     319,323,339,342..343,346..347,350)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mgkskinrsl iliflgytcv yldkniisls vipiaqdlgi nagqkglils afflgytlfq
       61 ipfgflgnrl gsrkimtlai lligvlmicl gfgfsliyll mirfaagsfa hagypsavsa
      121 fvtrevepak rgsvqssmia ssgfagivgp llvaplltlv gwkttyfvyg vivlvigflm
      181 ikgipktage pivsanqsni sffqvikdrn vwimvlaaff inaavygmtg wiasylvdef
      241 nltmnrmaml saligfvmmi samfagsmig rhfkdrekqv iliasalggl vafllskshs
      301 lvlsmlflal avaaasigfa tlmslpvklf aerevstkys iinavgvsgg ffapmiigwl
      361 vntsgsygga fsfialvfvl aglvslaiqt kdskqaigel erqk
//
LOCUS       WP_010742285             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010742285
VERSION     WP_010742285.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28700
     Region          1..235
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlkkerqeki ldllhvndyl sipeisakld vsdmtirrdi nelaensllv kiyggaqkle
       61 kieqelstqe kidtnvpekq figkvmnsii sdndtiyiga gttmlhalpe ikkanlfvit
      121 nsllafnyli yntdyrvllt ggefsrttee fygeiaersf enlnidlafa atngvfdnnv
      181 ttansiegsi qrvafkhark kcvvadsskf nrsdvytfys lsdidylvtd dklsettfdy
      241 ynsyttiike eqe
//
LOCUS       WP_010742350             215 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            malodoratus].
ACCESSION   WP_010742350
VERSION     WP_010742350.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..215
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=23898
     Region          121..203
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mnslfhkqid lkkgffatli vilgyigqly gslfintvsl vvttligfsi vytpkellll
       61 fskplhplkn tikyfllswi ismaigvalt vifglnlkan pidtinvkpl lllvlpislm
      121 geelfciyfl siftskfglf isnvfsalif glahystyyn gsvvitlihi iliqgvtrll
      181 lsqaaiksns iwtswiihvl fdfstialpi likll
//
LOCUS       WP_010742301             126 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus malodoratus].
ACCESSION   WP_010742301
VERSION     WP_010742301.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..126
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14750
     Region          5..115
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(5..7,21,38..40)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(52,55,59..60,69,87,91,97,101,104..105)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mmgdkigdis krtglstytl ryydqkgllp fvardkngrr hfkeedfefl siitclkdtg
       61 mqlsdirqfv ewsmdgdptf ekrlnfftdh kqevekqlaq tqtylnkidr kigkytrahe
      121 aamtkq
//
LOCUS       WP_010742388             273 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            malodoratus].
ACCESSION   WP_010742388
VERSION     WP_010742388.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..273
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=30274
     Region          111..217
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mhkfrslakr fpiifsvivi sismwliflp ddgslgwgli ltnlkgrfav svllvvlmfl
       61 lgmgkglfra sgivkvffdg wvllligavy lvvqvlsldf safgeglnal ilmaflfdmf
      121 ctglfeevlm rgvvfqsmas swrdkkngil isaivssilf glvhllnytd glliatmtqi
      181 ifstfigiyl cgvflkrgnm wsvillhsvf dfltlffqqe ftespkvvea astvtdlpls
      241 mglimimatl plcilgirti rryanvnkpi els
//
LOCUS       WP_010742478             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010742478
VERSION     WP_010742478.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..262
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29927
     Region          30..262
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mninnlglln slssilnegi mdsdyaitvy lvenldrise msvneiidet ftsrsairrf
       61 cnrlgysnfs dlkdsvtkli fpsnlqyrsq ddllnhrtql nkliftmiqd idrvftiaiv
      121 delsdliheh kdvvllcann tsgdlirfqq eliygnkeik ivsnaytnne niksltaesl
      181 iitvsasgkf aeianewvse ikgrkilita srseefqtiy nkifyiskhs fsndylgiyg
      241 kygiayifdl isssyiskyk rr
//
LOCUS       WP_010742481             179 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Enterococcus malodoratus].
ACCESSION   WP_010742481
VERSION     WP_010742481.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..179
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19680
     Region          1..169
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 myyhsnyssp igqitlagtd dkliglwmkd qkyfgdtlpe nsvennhlal fdktkkwldk
       61 yfagnnpeis elplhpigne frqtvwsvlr qipygetity kqiaqktaei lekdsmscqa
      121 vggavghnpi sviipchrvv gtngsltgfs gginkkikll elegvdtaqf kvpikgtal
//
LOCUS       WP_010742580             691 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus
            malodoratus].
ACCESSION   WP_010742580
VERSION     WP_010742580.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 691)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..691
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=79661
     Region          14..658
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnleertnqi fvelvnnpqi tskalcekfd ltrgqlnyal kkindsllde nlgeikrtkn
       61 ghflianeil stykggddql gvstesyvfs gkeraaiiel mllskedyls lnhfidelkv
      121 srntvlrdlk evdhelqqne lslkytrlkg yfiqgdewnk rnllsdlldn lammhngvnf
      181 iihfanidpk qieafrtrve lveeelevqf tderlktlpl liilmirraq kgklisysfk
      241 inyreladtk eylaadrviw dvdglsener vyltmllltt nlsrgdilsv keltkmkeal
      301 ekvianferi agvtledkek lldrllvhmr payyrikyhl nlqtrfyqen kdanlfslfy
      361 lvkeasgple tyfeqpipda elffislfig shivesseiv hpenrkravi vcpngisiaa
      421 llentlrnll peidfvttms arefyrtnyd vdfifsavpl ktekkvfvvd sflpekekrq
      481 lrervlrata iiqteivtpe kiltvvkkha eildetslye ellglfvpke srilekkrph
      541 lvdllkgeml qifeeevsws evltalgepl erqkiitpey ikalkkempi lpaytvlrhk
      601 ialphtvkea gaigvgislg ivkkgivted gkkihtvill asndkeehld lifemmslag
      661 adqlarleka ttkeevretl idfndeywra k
//
LOCUS       WP_010742637             334 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Enterococcus malodoratus].
ACCESSION   WP_010742637
VERSION     WP_010742637.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..334
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36558
     Region          14..334
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mmaatknisi pnragltden lvelyrrmwe iryfdekvdq lfakglihgt thlavgqest
       61 aagsgavlrk tdwitathrg hgqtiakgtn inemmaelfg rttgtnngkg gsmhiadldt
      121 gnlgangivg ggfpiatgaa ltsklkkndt valayagdgs tnegsfhesl nlasiwdlpv
      181 vffiennqyg msgpfktmmn verlseraka ygiegitieg ndiievintt ydavekarrg
      241 egptlieamt yrwkghsksd akkyrtkeee edwrknrdpi klarekfvaa gifteeeaee
      301 lrlaakqaie davtfaeesp mpatesmyed vysd
//
LOCUS       WP_010742609             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Enterococcus].
ACCESSION   WP_010742609
VERSION     WP_010742609.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..308
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34514
     Region          59..306
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mnkttkiilg ivlvlvivli aagnyfysya vvpakkdfla dgsakkstel itaeswfnnk
       61 dnrsdwklts ddglklsayy lpaeknqhkt ailahgymgq asdmpqyaki yhdlgynvlm
      121 pdarghgkse gdyigfgwpe rkdylqwidr iiekdsqaei vlhgvsmgga tvmmtsgekl
      181 pdnvkafved cgyssakgel nyqlkemfnl psfplipvts lvtkvragyf fgeadaikql
      241 nknhrpmlfi hgdkddfvpy smldevynat kgpkekyvvh gakhaealsk dpdmyqkkvt
      301 efvqkyvh
//
LOCUS       WP_010742639             405 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Enterococcus
            malodoratus].
ACCESSION   WP_010742639
VERSION     WP_010742639.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..405
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43064
     Region          1..405
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 manevlmpkl sstmdvgtit twlknegdsv evgeaifevm tdkiaievea ydegillkky
       61 igdgdsapvn sviayigeag edvpaempga eaeaaeetea eevaevaept esneettvtt
      121 tkvratpaar riarekglnl qkvqgsgpkg riqaldvkey qeptvaaapk aaegelipws
      181 gmrkaiadkm seskhtiphv tmnaevdltk vielrkqllp mveertderl sfleiiakaa
      241 mvalkaypef nanayaegik rfdhvnlgva vavsdglvvp vveqadqkgl sdltaavkav
      301 tkkardgqlm paemsggtft isslgrskvq tfnpiinlpe vailgvggsy dklvvadtse
      361 gsqvatital nlclsfdhrv adgapaaafl smivdllenp mslll
//
LOCUS       WP_010742670             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010742670
VERSION     WP_010742670.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23669
     Region          8..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mekkklqrrr gdrldaeifr vtyqlleneg yqavtfaria reaetsrsvl yrhwdtpfdl
       61 vfeavhdrnr svefdmhdld fdqgsleedl yyvgdnfltw ltsvptsfnq mmlleiqnqp
      121 krikqimqea riynisvmeh vlknarrrge ltkfppeetk lalfqiirck viiesadvtk
      181 kelrvlvrsv vkpaiqhfdy
//
LOCUS       WP_010742717             239 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus malodoratus].
ACCESSION   WP_010742717
VERSION     WP_010742717.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..239
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26512
     Region          1..220
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mepvikatai tkkyaqqevl kgidiaiapg dftcimgrsg cgkttllkil glmhpptage
       61 iffedkltye lfpdeisdir rrkigfvfqd fnlmesitvg enillpaild kqdpveaeek
      121 mkpffqvlri ehlldklphe lsvgekqraa icralinape iiladeptgn ldsnagaevi
      181 kifqrinqel gitivmithd skvaqaakev iflkdgqiyd rlvnvigsev qiaekmlev
//
LOCUS       WP_010742720             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010742720
VERSION     WP_010742720.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..247
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27301
     Region          4..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mnsiieierl kksfgdnlvl kdismnvnkg evvtiigasg sgkstflrci nlletptdgk
       61 imyqgenvla pgynlpkyrt hlgmvfqsfn lfnnmnvlqn cmsgqvtvlg rkeeeakkia
      121 ienlekvgmd rfidakpaql sggqkqrvai aralsmdpev mlfdeptsal dpemvgdvlr
      181 imkklaesgl tmvivthema fakevsdrvi fmdqgviaee gspedifgnp keartkeflh
      241 rvlhpep
//
LOCUS       WP_010742800             271 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus malodoratus].
ACCESSION   WP_010742800
VERSION     WP_010742800.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..271
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29468
     Region          4..264
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,195,217..219,221..222)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mikliaidld gtlltdakti sdtnktilak akargvkivi ctgrpliaik dylaelnlld
       61 addysitfng gliqtntgei lgktamelad vkhihellke idlpmdvlsd alcfqfetaa
      121 ghpsiystln kaltyvpkti dslkedtlyn kvvaavnady ldqkiplips eeydkfeifk
      181 trpnllefmp kgvtkafgls vlgehlgiea hemmalgdea ndlsminyag mgvamenatd
      241 giksaanfvt rtnqadgvah aiqkfvfdel n
//
LOCUS       WP_010742863             109 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010742863
VERSION     WP_010742863.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..109
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12666
     Region          3..102
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 meidkevlrg yidpiilsil akadsygydi arqakkssne tfelkegtly vafkrlekng
       61 yvvsywqdgq aarrkyyhlt ekgaaflqhk kqewqfikdl mdgfykgde
//
LOCUS       WP_010742843             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010742843
VERSION     WP_010742843.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 220)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 220)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 220)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..220
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23669
     Region          8..214
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 menmntfqqf idyfqtngay vfsqfvrhfl isiygvlfaa ivgipigifi skhyklanwv
       61 irianviqti pslamisilm iglglgvnvv iltvflysll piikntytgm rqvdknaldv
      121 gtgmgmtswq rlymielpls vsvimagirn alvvaigita igafvgaggl gdiiirgtna
      181 tdgtslilag alptalmail tdwilsiver kldpatktsk
//
LOCUS       WP_010742867             344 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Enterococcus malodoratus].
ACCESSION   WP_010742867
VERSION     WP_010742867.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..344
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38643
     Region          200..313
                     /region_name="FUSC_2"
                     /note="Fusaric acid resistance protein-like; pfam13515"
                     /db_xref="CDD:433273"
ORIGIN      
        1 meqsffkeli hynkpkespf rllgaglcmi svlftgylth qlaissfgsl giftflyyqr
       61 lplkqlimrl sivgsfltva nflgmlstha awtapivvai vgflgrfffr lygiakpgpf
      121 fivmvtamga stkipltrip vmsgyffigv lfsllvatil hfvenkplpa iearktvksr
      181 idddpavvid sllysgflff avylsmslql knpywlvvsc asilqadnlr amahrnvqri
      241 fgtiiglaia afllylplsv fetlliitvl fvtveyfvkr nyaiaqfftt pmalmlsmlv
      301 rqqylysliq frflgivlgs llgllagwlm stslefynrk fhsn
//
LOCUS       WP_010742966             441 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus malodoratus].
ACCESSION   WP_010742966
VERSION     WP_010742966.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..441
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=48618
     Region          4..411
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mfakfeafmn rffvplahkv dnqrhlsaik agmvamtpft ilgsffailp alpnmlgesn
       61 afsqfilnna elfnlpvtls tgliglyaca aisynlgnhy klyipgavtl slfgflfmta
      121 tfdkngmldi tnfgakglft smfvalitve lynfckkhnm tirmpdgvpd fvsksfelip
      181 vtlivggtfi igrfalmqta gelpptiltr flsplvgsmd npwsvlalnf ciclifffgi
      241 hssvfspitr pimvafiaen isafqagqpi phfytagass affgftgcgi sigcivaclf
      301 skskryrqig kvslfpalfg inepilfgap iilnplmfvp hvfggaiigt lpmffmhwgw
      361 lnkpifdppy vgiflegflt ngdwrtilvn alqlvlavai yvpffkimer nelkdeakkk
      421 ekktifdqgd tdildgldld f
//
LOCUS       WP_010742999             257 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010742999
VERSION     WP_010742999.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..257
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28827
     Region          1..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlteerrmkl leaienkqfi svaqlseifq vhettirrdl delesqglvv rihggvvpas
       61 ikhdepvfed ratenmlekt rigkyatkyi ksgeaiilds gtttlqiakt lndmpqlqdi
      121 tiitndvnia svlrsnrnit tivtggtlfh dsymlngqia netlhqlsvd kafiatpaln
      181 vekglthfne lliatkknmi dasvkkivvs dhtkigrral ytflpidqid llitdnqteq
      241 klidemykng ikriesv
//
LOCUS       WP_010742979             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010742979
VERSION     WP_010742979.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..305
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34625
     Region          5..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtyaleindl kkvyatgvea lkgidlsvee gdfyallgpn gagksttigi itslvnktsg
       61 nvkvfgydld kelvmakqqi glvpqefnfn pfetvqqivv nqagyygvpr kealvrseky
      121 lkqsdlwekr dvrarmlsgg mkrrlmiara lmheprllil deptagvdie lrremwkflr
      181 elnangttii ltthyleeae mlcrnigiiq sgelientsm ksllaklqfe tfifdlepfd
      241 kepditgfah tftdeqtlev evvrdqgine lfeqltnqgi kvlsmrnksn rleelflkit
      301 eekhv
//
LOCUS       WP_010743047             237 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010743047
VERSION     WP_010743047.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..237
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26938
     Region          6..234
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mrknakymei yldvkrkved gtyaigdklp tgielakhyn tskltvkkgl dmlvsegvlh
       61 srsgfgtevl rkpidnskvf gpseglmsvv gedhvdseih tfsielpskk vaerlqlnek
      121 eyiynivrsr fvdqqpysle qtfmplsiip glepkhlkks vysyirdelh leinashvwm
      181 kgvlatefda kilgidvgdf mieieksvsl angtpfeysi trhlykdfif eavfmen
//
LOCUS       WP_010743050             459 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010743050
VERSION     WP_010743050.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..459
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=50392
     Region          1..448
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mkfdmqklqe pllkasawve gntilqaikn afvrtipftv vgsfsnlikm qldaliksqh
       61 idnviltnis elfgylgnat lgivalivvf ssaysyaiel krkennerln piiatllafa
      121 ayfvmvpknv nflepkakvi egfstsffsy egmftglivg misvalfakf trskftikmp
      181 gnvpqnvfds ffslipisev llifgavril ieslgyvsll qmiseilikp llsvgtglpa
      241 ilivillqqi lwflglhgfn ivwgvvsafw lplflenvak faetqsfagi tispntmtnv
      301 yamiggsgat fgliiamlif tkkgekerev aklalipgcf ginepvifgl pivlnplmfi
      361 pwilvpiina viayivtsig wvvplvvlns gnepiflstw vlgafhispv iltavlvvld
      421 vvlyapfvvl nqrheraeql ieeqtkeett aqlmaenag
//
LOCUS       WP_010743060             644 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus
            malodoratus].
ACCESSION   WP_010743060
VERSION     WP_010743060.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..644
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74117
     Region          12..644
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 msklayqrld dllellakqt tplpmkelak sfsisertvr tdianlndll snvgatitlv
       61 rgqgylltil skeqfndwwt ksmssadsfl ttseerqayl lfllfknetp lplddfldql
      121 fiskntfysy lktardnlmt yqlkivnrpn igfellgnef akrqaisdll iekdlqeyli
      181 gftemelalf dnidlellqd leltylaple lldsdyyhkn ilshfalais rflaghemtg
      241 fplrvpilkq haqkalchfl deidqafdiq lssgekeyft yylalnaprl vetastsnss
      301 setakaivdd llhaikrtsn fdwvedkmli edltshiegf inmnlmearr snpllatikk
      361 sfpqaydlcl thleilgkqh glyfsqdevg yialhiagam ernsssahrk yrvilvcgtg
      421 ramsriieak inknyqetie vvdrlsyvel qqhnlstvdf vittvpleql siphiyinma
      481 kldkeivkie hfienfkgsk aeiyslfyed fflhedfdtk dqllkkmtqq lfqkdfvpen
      541 fhasimkrea inqtninewl aiphpmslla kqsavsvavi pngvdwgegd lvkfvflfai
      601 skedyedtee iyslllelme rediqqailq nseyknfleh ikql
//
LOCUS       WP_010743053             291 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Enterococcus malodoratus].
ACCESSION   WP_010743053
VERSION     WP_010743053.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..291
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=31432
     Region          4..284
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 msqkilaidi ggsaiksglw gnealtelps yptpktwdem kaylkllvee hqitdgvais
       61 apgavnveeg viygvsavpy lhrfpikqel adflsvpvsf qndancaala eiwqgnakgl
      121 esaalmiigt gigggiaing klrsgtnlfg gefgyqvmnd dtletlsdlg spvamskrfs
      181 nikaddrsyt skeifdlaea gdelaqeqid yfynalsigi ynilvsldpd rvligggist
      241 redllfniee rvqqlllkkg akelkasimp ckflsqanli gavyqfleeq d
//
LOCUS       WP_010743087              70 aa            linear   BCT 01-JAN-2025
DEFINITION  tautomerase family protein [Enterococcus malodoratus].
ACCESSION   WP_010743087
VERSION     WP_010743087.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..70
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=7951
     Region          2..51
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mphlsvrlyp grtkevkqdf aeklqdlvvk elgcepnvvs vsfkeiekek wddvidveia
       61 gediyieadf
//
LOCUS       WP_010743095             324 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Enterococcus
            malodoratus].
ACCESSION   WP_010743095
VERSION     WP_010743095.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..324
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35429
     Region          3..313
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 meividqvnk sygeqiiled isltipagsi mgilgvsgag kstllrcing lekgqsgsik
       61 igtqaleels ekqlrevkkk igmifqgnsl ieqktifknv alplecsgys kedikarvde
      121 llkevgiadk aqmkprqlsg gqkqraaiar altmspeill cdeatsaldp nitngildll
      181 lklnqkmglt ivvvthqmev vkkicdrvai lqsgkiveen tvqqvffnds evlktitgeq
      241 qtgfgklkad hrlvklftql dkdvlallrq asietphllk aateqfknet istlllsipd
      301 edvekltqla dqghficqev kvge
//
LOCUS       WP_010743123             232 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus
            malodoratus].
ACCESSION   WP_010743123
VERSION     WP_010743123.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..232
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27045
     Region          142..215
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mkkviiltrn iiieqefqde lqrldyevfv lkeffdvdkp qyfeeilslf divifsetlt
       61 nqefneilpi vvekdlhylr rtdepvpnid enhclsidct ltelreflll sdkregqnes
      121 lskglvrqse mkkqdlvlfy sslnniekki isalaegsgk iisrdelcnk vwnnevsksr
      181 lvqmsttvgn ihkkiahahi dnvriitywg ngyrlhdvpn glmnehikey sm
//
LOCUS       WP_010743202             327 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Enterococcus malodoratus].
ACCESSION   WP_010743202
VERSION     WP_010743202.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..327
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36154
     Region          4..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meifditivg agpvgmfaaf yagirqaktk lidslpqlgg qlttlypekn iydipgfpiv
       61 kaadlvgnle kqlrtfshty cldeevlelk qhedylevit aknshytksv vlalgngsfq
      121 prrlmidgae qfenkgidyy isdimkyagk kvaiagggds aidwalmlep iaaevsiihr
      181 rdnfrghehs vqklkdssvn iytpyilkdl rgenyledlt lqkaksdeti tlnldylivn
      241 ygfsssldhl rswglestrq ailvesdmrt sipgvyacgd iatydgkvkl iatgmgeapt
      301 avnnalhyvn pknrtqpghs tslfpqn
//
LOCUS       WP_010743184             475 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus malodoratus].
ACCESSION   WP_010743184
VERSION     WP_010743184.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51986
     Region          21..469
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,146,
                     149..150,153,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mktyqedsvv qknrwwilvs vamftfmstl dssivnialp tisrdlavpm nkaewvvsiy
       61 lmvvcaclll fgkvgdsfgk ikvyrigtii ftlgsllcgf nhslamllfg rviqgigasm
      121 tmatntgitt evfpmkergr algaigafvs lgsiagpgig glilahfsws yifwinvpvg
      181 iltiligekf lpkditmskk kidwlgfatf aitimsffga vfigqevgyi halplsllav
      241 aivffilfiq vekrkenpll vfsilknkmf tmslitalli fsanffvnvv mpfylqnarg
      301 ltasyagllm mvfpflmvig splsgyltdk igpqklvlmg llllsitqlm yvfmnelspi
      361 wyyvlataim gmgnalfqsp nntivmssvd kenlgvagsm nsfarnlgmv igialsttil
      421 yggmsvsygr rvttyidgrp dififgmrvt fiaslaicat alvislvrfr kkavn
//
LOCUS       WP_010743353             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010743353
VERSION     WP_010743353.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..247
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27682
     Region          3..247
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 msreeeilai vskkkkievn qlsellnvsk vtirkdldkl eargllhrqh gyallnntdd
       61 inyrlaqnyd lkrkialeas kivhdgevim iesgstcall aeelafnrnd itiitnscfi
      121 asyvrkaesv kviliggeyq kesqvnvgpl vkqvinefyv dklfvgidgf dkrrgftgsd
      181 itrcdttrml ataanqtivl tdsskfsqng vvsefafsev skvytdgmie dearkflqke
      241 nievftv
//
LOCUS       WP_010743351             291 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010743351
VERSION     WP_010743351.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..291
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32680
     Region          2..269
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mllqerletq pfttsekqvv dylleqqrni qnkttaeiaa atfsskstlv riakklnysg
       61 wtalkadfln eldyleksvs cidanypftk rdslmtiank iarleiesie dtlslithdd
      121 lrkvvdmiak sseinifaas nnllvaqefs hqmsrikrev kihsiqgeil fnaylakqds
      181 cgliitysge tgslnqvakl lveqnipvit itsmgentta ryadailrlc treklyskis
      241 tystdaainy llnviyscvf aldydanval kiasskkien drfsdseilr e
//
LOCUS       WP_010743358             323 aa            linear   BCT 01-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase [Enterococcus
            raffinosus].
ACCESSION   WP_010743358
VERSION     WP_010743358.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..323
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35126
     Region          2..312
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 miltitlnps mdynylvssl tldqvnrven phtsiggkgi nagrviaqsg egvvltgilg
       61 gpvgemildt liaegryqle flpvegnsrn aitimhdgnt htelvekgly lskeneqlff
      121 qhvasllkky aidticisgs vnsddsnfhl hllsfirsiv gtefpilmdi sgkqlenvlt
      181 qqavrpsfik pntheleelv gkeilsteel itilkeplfd nietimisqg gdgaivkhhs
      241 tiydvqipqv eivnttgcgd stvggmafai srgyamedai kyamacgisn slfetngtid
      301 pkqvekftev vklteinels ikg
//
LOCUS       WP_010743367             250 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010743367
VERSION     WP_010743367.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..250
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28702
     Region          1..234
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlktdrfqai msllevngtv rvsdimdkls vsdmtvrrdl delekqglle rvhggaklkd
       61 fyrhvelsht ekqimlqaek qrivekanel indgdtlflg pgttiellsk iiradslriv
      121 tnclpvfeel nkhkgnrkiy llggelrett qcfvgeitnk slndmnfhka ffscnalneq
      181 kimtstfeeg qtqqialnns ierfllidhs kigkrdfsvy ynlndvtavi sdedeqkhye
      241 kiekeekyiv
//
LOCUS       WP_010743377             258 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010743377
VERSION     WP_010743377.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..258
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29025
     Region          1..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlkterqqsi lamcdrygti tvkfiqevld vsdmtirrdl eelaqsqkll rvhggaqkin
       61 etkeivssie anelshkekk klhtkekeyi aknaaayinq eddtiflgsg ttielmtqyi
      121 dspslrivtn slpvfnllse tksfelylig glyrektgaf vgsianeavq kigikkafvg
      181 vnglkgpevs nfsieegtlq kivldnaaek clvsdankfd hsdfynfydl rkidalftds
      241 tlspelksyy qqytriiq
//
LOCUS       WP_010743436             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Enterococcus].
ACCESSION   WP_010743436
VERSION     WP_010743436.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..282
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=32170
     Region          1..189
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mendqerllv easlagnsda laelltsvkd svfnlslrml gnvfdaedat qeillkamtn
       61 lssfkqysrf stwvyriain ylinnqkkrs fkekltfdlm aedleqsipv tdenyfglee
      121 delaeelkls ctnimlqcls pqdrcvfilg tmfkmnsqla ggllemtpea yrkklsrtrk
      181 rmgsflsthc gvaggsceck kripfaiqqk rlnpsqldys slkksklgti fhqkqnmefl
      241 deqtlifetl shyqstfdpq qflkellgsq qlseltqede ll
//
LOCUS       WP_010743463             723 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha-galactosidase [Enterococcus].
ACCESSION   WP_010743463
VERSION     WP_010743463.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 723)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 723)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 723)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11245829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..723
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=82734
     Region          33..282
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          286..632
                     /region_name="Melibiase"
                     /note="pfam02065"
                     /db_xref="CDD:307952"
     Site            order(333,364,408,473,477,523,542,545)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          646..719
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mpilfdhqrq ifhlsnsqis yvigiekdkf ithryfgrsl pfytgsnelq ridrgfatnp
       61 dlsdrtfsln alpletstqg tgdhrignyq irrenganvt sfsyksytis sgkptleglp
      121 slrgeqaetl aillvddvqr lemvlnytly kdypvvtrsv rflnrgkekv fienagsmll
      181 dltrtdfdml tlngshtnea tigrqalheg iqkiessrgt sspqhqpfla lmdsttnefq
      241 gevyafhliy sgnftaqvev eqygssrvql giqpetfewc lepnasfqtp eavisysdag
      301 lngmsqtfha lyqkelipvq wkdqerpilv ntweanyfdf headllqqae vakdtgielf
      361 vlddgwfgqr nddtsslgdw fenreklpqg iaglaekiqq kglkfglwfe pemisensrl
      421 feshpdwvlq vpdypktegr rqlvldlsqt vvqeylieml dsylstgkid yikwdmnrhl
      481 tevgsfafpa yqqkeiyhry vlglyrvlev ittkypnclf encssgggrf dpgmmyymaq
      541 twtsdntdal crskiqygys llyppimmga hvspvpnhqv grrtslhtrg liamsgnfgy
      601 emalthlpad eqkeireqit fykkhrslfq fgkfyrlqsa ddffatawlf tndeeaiviy
      661 fnglarpavp vkyvktryle eqaifkntat gtlvsgaeln qagitiprik edfstllfhw
      721 kki
//
LOCUS       WP_010743524             209 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010743524
VERSION     WP_010743524.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23610
     Region          4..>80
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mriskdpiir kneildvask lfaekgfdht streiidqag iargtlyyhf kskeeimdal
       61 verttaelfa aakkvaadqt ipvyqrfvqt vlalrldtsd gedmmdfvhk pqnalmhqkm
      121 qtavvteitp vlasivedgi qqgifqtdyp yetmemaivy ataafddqel vpqseeiqlq
      181 rvsgffylle rmlgveegkl akemegmfe
//
LOCUS       WP_010743497             124 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Enterococcus].
ACCESSION   WP_010743497
VERSION     WP_010743497.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..124
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14382
     Region          6..112
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mnrayiehva iyvtdidwyi dffentlnft ermrkvengq prqvwlyggi qlieveknhl
       61 tgklghlgim aenqqealkk ikqydvepmp qgnnwwqlpd glcieilqak pgtvkdildv
      121 tpwn
//
LOCUS       WP_010743467             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010743467
VERSION     WP_010743467.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..233
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25777
     Region          1..220
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msaiefkqve ktfkdgdsti ealketnfsv ekgefvaiig psgsgkstfl tiagglqsps
       61 sgevlinded fsekkekera klrfkeigfi lqasnlvpfl tvkkqlklvd kvskndntqv
      121 aeklfeqlgi aslenkypee lsggerqrva iaralyhdpt iiladeptas ldsekayevv
      181 kilaketkek nkatimvthd trlvkfcdri lemkdgtlke ksvsedekes dsv
//
LOCUS       WP_010743550             148 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Enterococcus].
ACCESSION   WP_010743550
VERSION     WP_010743550.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..148
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16339
     Region          10..143
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 makqvlkaev eslgglqlkc sargfefmid epesvggtne amnpleallc slgackmmvv
       61 rffyqaknir lksmrveilg eidsdrlkgk pdvkvgfski itnyyidadn teeeiqelva
      121 fiektcpvkd tivnapemel ninskkas
//
LOCUS       WP_010743560             386 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Enterococcus].
ACCESSION   WP_010743560
VERSION     WP_010743560.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..386
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43561
     Region          22..303
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mltflinkit drskgnkrts vgilagilgl isnlalflak ffigslsgsv simadamnnl
       61 sdtassfitl agfkiagkpa dedhpygher feyisgfvis ilvtyvgfrf ldssfvkilh
      121 pssvllspiv yivlvlsilm kfwqsfmyrr lsreissdtl kataqdsind vyttiavlis
      181 aiiewfsgwr idgyigflia lyiiysgikm imgfindlmg vrprdeevaa irqhldnypd
      241 iigyhdllih sygpnsvfas vhievnqdwt lphahevida ieydvkqnlg vdlvchldpy
      301 piddpdfkri apvlkrilkd ihqnlrfhdl rvdktttpet iyfdlvvped lkkrtntqlq
      361 dqissqfisq sepaklsitf drtyll
//
LOCUS       WP_010743562             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010743562
VERSION     WP_010743562.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28167
     Region          1..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnellkveni kkiyqtqfkg mpvealrnid ltvekgdyva imgesgsgks tllnliatld
       61 kpssgtilld gmdlntikek naaafrrdhl gfvfqdfnll dtfsvkdnil lplvlsqtpv
      121 kqlmdelkpv vkalgiekll ekypyelsgg qkqrvavara iitnpellla deptgaldsk
      181 tseqllqifq rlnyngqtil mvthssiaas harrvlfikd gqvyhqlyrg nkdnyeflet
      241 inetltalls kea
//
LOCUS       WP_010743638             111 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010743638
VERSION     WP_010743638.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..111
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12817
     Region          12..106
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 msdkdivqny vtelkrgslv lavlgslttp hygyallqtm qekgieiean tlypllrrle
       61 kqellvsdwd ttesrprkyy sispiglevr selleewkkm qkniaeiyrg r
//
LOCUS       WP_010743656             293 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010743656
VERSION     WP_010743656.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..293
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33763
     Region          1..288
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          <164..>238
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
ORIGIN      
        1 mdqqklrlfl dltetlnyte taernymtqg nvskkinale relqvplfdr knrqiqltee
       61 gqlllpairr ivedyqalad tlsdyrekke rvltvhtipt mpnylgfdrl atflkqhpev
      121 hlnlkeseem algafeiekn tvyffrsmsq iveknaipte kdhfvavlsk dhplvdqapi
      181 nlaalakenf lllgqaqnsy ysveqlcrea gfdprityqg tridlilrmi eeglgislmm
      241 ekslgdslse elvvreilpt kesylyfcls eetdaqaska ffnflhsyhs kle
//
LOCUS       WP_010743650             252 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010743650
VERSION     WP_010743650.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..252
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27996
     Region          2..238
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mieltgvtkv ygqkkaldnl sltikageif gflghngagk sttikslvsi ieptsgeilf
       61 dgknlkedrl aikkkiayvp dspdmflqlt aneywdlisa ayelkgqehr rqelielfdl
      121 vghedetles fshgmrqkti iigallpdpd iwildeplqg ldpqaafdlk emikrhaekg
      181 ntvifsthvl dtaqqlcdel ailkkgeliy ngsvealled ypneslesvy lkmagrqang
      241 eliseieeda he
//
LOCUS       WP_010743657             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Enterococcus].
ACCESSION   WP_010743657
VERSION     WP_010743657.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 190)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..190
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22089
     Region          44..173
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mkriidaita ykpyteqeaa dkklfldklq fqdnlltren qeyhfsssaw vvnptydkvl
       61 mvyhniyqsy swtgghadgc eelltvaqke leeetgikey qliydglfaf dilpvnahyk
      121 kgqfikahhh inttylfmas enqdlqvkad ensavkwiev adldqavtek emrpyyhklm
      181 ekalikrnng
//
LOCUS       WP_010743663             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010743663
VERSION     WP_010743663.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..240
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26321
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 minvkqlskq fgenevlkai dltvkegevv viigpsgsgk stilrclnll eeptsgeiff
       61 egqnitapds nidqirqkmg mvfqsfnlfp hmsvlenlti tpvkikkedp tkakdqalal
      121 ldqvglkeka dsypsnlsgg qqqrvaiara lamnpdvmlf deptsaldpe mvgevlavmq
      181 dlakkgmtmv vvthemgfak evadrvifma dgiiqeegtp eeifdrpqns rtqdflnkvl
//
LOCUS       WP_010743664             483 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein/permease
            [Enterococcus].
ACCESSION   WP_010743664
VERSION     WP_010743664.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 483)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11705690
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..483
                     /product="ABC transporter substrate-binding
                     protein/permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52909
     Region          37..261
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Region          271..480
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mkkrigvlla vvlmlfsflp vkaqgaekde iyeriqqsge lvvglsadya pyefhaevdg
       61 kdkivgfdvs iaekiakdmg vklkieelgf dallgalktg kidlvisgms iteerlkevd
      121 fsdpyfvvqq kvlvrkgdkn kfkttadfng lavgaqkqtt qedlvknemt gaeptslqkv
      181 pdlinnllnk kveavvleqp vaeayvqqsd nvelapvkfe qgekvtaiam skntpelkkh
      241 vnasiktind ddllkgyqke anelmfqgek sflqkygpyy lsgakytill afvgvlfgli
      301 fgsllalmkl skskilkala viyieyvrgt pllvqifivy fgtgvlgldl skllagciav
      361 slnsaayvae ivraginavn kgqmeaarsl gmnqkeamry ivfpqaikni lpalgnefvt
      421 iikessvvsv igvselifqt gvvqgasfkp flpyvlvsli yfvmtfcisr llglverrmg
      481 lnd
//
LOCUS       WP_010743674             137 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NusG domain II-containing protein [Enterococcus].
ACCESSION   WP_010743674
VERSION     WP_010743674.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009210
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..137
                     /product="NusG domain II-containing protein"
                     /calculated_mol_wt=15205
     Region          11..137
                     /region_name="COG5341"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444125"
ORIGIN      
        1 mklkdfakns llrpwdgiiv vilillsfap vlvfslnras sptqeavlsv dgkeiktfdl
       61 sdnsqaytyr yedkdgdynl ievkgnriri keadcgdqic vrrgwieqsg etivclphkl
      121 lievkssdgg epgsviy
//
LOCUS       WP_010743755             509 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Enterococcus].
ACCESSION   WP_010743755
VERSION     WP_010743755.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..509
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57197
     Region          6..507
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msildltgia qqfgdkilye dlelhlnkge hlgligqnga gkstlikiit geqlpdegti
       61 awqknihvgy ldqyvevdpt lsikeflkta yaadfekeak igelymayse smddklleka
      121 grlqteldqg dfyqidtlia emssglgldv lgmdtpledl sggqrsklil aklllekpdv
      181 lildeptnhl ddehvawlsq flqdfagtfv vishdrdfln qitthiadie fgkltkytgn
      241 ltkalkqkeq fqetymkqya aqkrqiekte ayirkykags rstmaksrqk qldkverltp
      301 pssnavahfe fpyapivttl alettdleig yqkpllapin itlrygekva irgfngigks
      361 tllktligai pkiagefhfp antkinyfeq dlqwenpyqt plqylsehfp ketvkelrkh
      421 lakaglpnqi aqeplstlsg geqtkvklcq mtmqkgnlli ldeptnhidq atkdslresl
      481 anfagtvivv sheegfyqdw idrvieisq
//
LOCUS       WP_010743767             104 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010743767
VERSION     WP_010743767.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..104
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12050
     Region          1..91
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mdsqlkkgli eycvlaslve idsygyqivk eihphleite stlypilkrl etnkkvstys
       61 kvhngrlrky yhltdlgvas iqkflkewnd veavhnfikr svee
//
LOCUS       WP_010743750             464 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Enterococcus].
ACCESSION   WP_010743750
VERSION     WP_010743750.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 464)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..464
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52881
     Region          102..441
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 mtefllflks lpfhapplfv tdlisfffll kvfnlhvdgr kqravnlfti gsfsivqsvf
       61 vfllsdsslt llarivvfst ysaffvfams llihlnakhf plykitmlsi lilhlnilve
      121 misgffllli vlianradil pisnafaplf fylfdallll gafaillrtr fsnylneife
      181 qrslciklcw vaaviqiasy sllhamkntl ywslaisgii visfllclfl iavysknlsk
      241 tlelkqsrll llqqqaymkq leaiqnelra iqhdhknlit glylhakdgd tkeiqryiek
      301 fllnmdegiq eqmkwsnqlt siaspelkgl llskmllaqq hdvffnleva ttveeikmat
      361 ndfircmgil ldnaveaaqc edenrrvdil fykeedkltl vvknpcqekv nlakirnrgv
      421 stkgsgrglg lsiyqevvqk ysnilsetkq qngefiqela ifds
//
LOCUS       WP_010743805             473 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Enterococcus].
ACCESSION   WP_010743805
VERSION     WP_010743805.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..473
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51842
     Region          1..418
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 meekkkkfsl msailsvicv vfvaeaaapv aaignsqffw wifllvafll pyglisselg
       61 ttyigdggiy dwvtqafghr wgsrvswyyw inyplwlasl avvcpdlltt itgiefstlp
      121 ailielvfiw vivwisfypv adsvwilnga avikmllail igalglytfa tkgaaneftl
      181 ssmlpsfdln slsfisviif nllgfevict faddmenpkk qipqsiiagg lviaaiyifs
      241 afgigvaipt dqistgsglm dsfklltgst ggwfiiamaf lflltlfgnm iswslgvnnt
      301 acyaaengdm pkifakrggk dempigaaim ngvvasvvvv iapilpnqdl fwaffslnlv
      361 mflmsyvpvf pafyklrqid pdtprpfrvg ggdgflkllv vlpmimivis liftalplqf
      421 daetlsqqlp itigavvftl fgeaiiwvkk ikkkgviyng eenrkdntet rrv
//
LOCUS       WP_010743828             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010743828
VERSION     WP_010743828.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..190
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21842
     Region          1..>184
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mesgpkyekq slsdlvvshl knrilsgtlk ggdrliemei snhfnisrap vreamrilse
       61 qglitfsprk gnqvielkpa eilevfeirt sletqilrki lrnqmlseed fqqlteiame
      121 mkdgeercrn eedkafllna ldlsfhkylw nlsgsvkrtq ilesmfyqll iamnedltsl
      181 gileknrksi
//
LOCUS       WP_010743858             481 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FGGY-family carbohydrate kinase [Enterococcus].
ACCESSION   WP_010743858
VERSION     WP_010743858.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167356
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..481
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=53409
     Region          5..451
                     /region_name="ASKHA_NBD_FGGY_YgcE-like"
                     /note="nucleotide-binding domain (NBD) of Escherichia coli
                     sugar kinase YgcE and similar proteins; cd07779"
                     /db_xref="CDD:466798"
ORIGIN      
        1 mekkyivgid ggsqsakivi fdlegnivge gkealrpmhl gedvvvehpg ddlwdalcsa
       61 smkamdefgv rkekivgigl gfirccrvll kkdgtlaqpv iswmdkrtst pyvhdnpdvq
      121 yvtstsgyit hrltgefkdn ignnfgqwpv dyetwdwstd eqvlkqynlp eemlfetvkp
      181 gdklgtitke askktglpeg vpvfattsdk avealgagli qdtsavvslg tyicsmmmgk
      241 qmppsdavny wgilssmpgr yiyegygirr gmwtvswfkd llgekisirs nyqgiseeey
      301 lneqaanipa gsdglmtkld wlanpwepfk rgvmigfnah hdyrylyrsi legiaytmkn
      361 nvtnmtdelg hpidevivtg ggsnsdllmq ifadvfnlpi krnvvngsas vgaainaavg
      421 lgiyetyeea vekmvkvkdv ftpkpenvsi ykrlneevyq sltdytdevl kksynilhpe
      481 g
//
LOCUS       WP_010743863             237 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010743863
VERSION     WP_010743863.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..237
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27365
     Region          27..234
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mkiqldrlnd leisihnrlt leskenpnlt iteaaklsgv spskisklvk kmgfsgykey
       61 frfltgkeli kqkklnsefa rikdfmenfd estvdylagl iqqsdkillf gygptnfcme
      121 yfeyklnftl nknvirvsqp slipdllted slllifsvag kfanfdplfe eakkhhaksl
      181 lvmeemntdl tldaseiifl tkshqdehlk shektrtill myieevirql tkedlre
//
LOCUS       WP_010743864             205 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus raffinosus].
ACCESSION   WP_010743864
VERSION     WP_010743864.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 205)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..205
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21944
     Region          1..203
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mfdnliqyls enssylitqf gvhvyisvig vvltfligfp lgillserqk lsdlviglin
       61 viqtipsiam ltvllilmgl gqntvvatvv lysllpivkn tyvglvnvdp myidsakgig
      121 mnryqilymi kiplampvil agvrnaliis vgittigsfv gaggvgdvil rgiaitdggp
      181 iivvgavlca fiaimmdwlf dwimk
//
LOCUS       WP_010743871             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pyridoxamine 5'-phosphate oxidase family protein
            [Enterococcus].
ACCESSION   WP_010743871
VERSION     WP_010743871.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..135
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15531
     Region          1..80
                     /region_name="Putative_PNPOx"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam01243"
                     /db_xref="CDD:426149"
ORIGIN      
        1 mdkgmeallt kadtftliti dnrgfphaia vspplerngf yyfkfyingd grtaenirqn
       61 rsgslfcfdk ekhesialkg ylfaeelvey kklaaqlnef qkelnyehpm iavfetlsvk
      121 hyenmhgefl dvpek
//
LOCUS       WP_010743898              66 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Enterococcus].
ACCESSION   WP_010743898
VERSION     WP_010743898.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7026
     Region          1..65
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mnkgtvkwfn adkgfgfitg edgndvfahf saiqgegfks ldegqavtfd veegqrglqa
       61 snivkd
//
LOCUS       WP_010743888             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Enterococcus].
ACCESSION   WP_010743888
VERSION     WP_010743888.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15652
     Region          5..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlnnyknilv aidgsehseh afaeavevak rhdaklnvis iindselsts afsfskiyaa
       61 ekeqvekell kkvhdasrke feniepfvdl gspkekivef akdndvdmiy lgatgkgeis
      121 lsrigstaay vvnhapcsvt vir
//
LOCUS       WP_010743970             315 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Enterococcus].
ACCESSION   WP_010743970
VERSION     WP_010743970.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..315
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35457
     Region          81..287
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mterisleks aldfsianek epyiyqlpvn daralleqvq dspvnklead ttdekwdlgn
       61 hgiinvrsvk pkhateklpv ilyihgagwv lgsahthdkl vrelavrtns ivfvpeydrs
      121 peakypvaie qsyavllklv eeaegrydtd rltiagdsvg gnmatvltml akdrkgpkik
      181 qqllyypvtn hgfdtesyhq fatnyflake gmkwfwdnyl pegqdasikt isplqatked
      241 ltdlpaamil ngeadvlrde geeyarhlrd agvdvtqirf qgmihdfvmv nsmdqsnatr
      301 aamdlstdwl nkrnk
//
LOCUS       WP_010743906             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cell division ATP-binding protein FtsE
            [Enterococcus].
ACCESSION   WP_010743906
VERSION     WP_010743906.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Hung,L.W., Wang,I.X., Nikaido,K., Liu,P.Q., Ames,G.F. and Kim,S.H.
  TITLE     Crystal structure of the ATP-binding subunit of an ABC transporter
  JOURNAL   Nature 396 (6712), 703-707 (1998)
   PUBMED   9872322
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..222
                     /product="cell division ATP-binding protein FtsE"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=24816
     Region          1..222
                     /region_name="FtsE"
                     /note="Cell division ATPase FtsE [Cell cycle control, cell
                     division, chromosome partitioning]; COG2884"
                     /db_xref="CDD:442130"
ORIGIN      
        1 mivlenvtkc lavskqkkrm pvlrqlslhi sagefvyitg ssgagkstll kllykelspd
       61 qgevyvgqyp lsqlrkkdlp yfrrrigvvf qdfrllpnmt veenlayald avgtppevmd
      121 rritqvlklv glshrrhave lsggeaqrva iargvinqpk llladeptgn ldaknafqil
      181 rllerihrkg vtvvvtthnd allhrfphrv itlekglils dr
//
LOCUS       WP_010743985             688 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LTA synthase family protein [Enterococcus].
ACCESSION   WP_010743985
VERSION     WP_010743985.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..688
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78058
     Region          14..633
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mnrvkraftn rwlilltvsv lfwaktilay yvdfslgveg siqyfilwin piattlllfg
       61 vflyvkkikp alivlflmdl lntlilylnv ifyreftdfv tiksilgfsk vsqgisgssf
      121 almkphdify wvdvlaflgi liyifakrke ivskpvkktf avavsclaal tfsinlslse
      181 anrpqllqrt fdrsyivkyl gldaftvydg ikteqtnsvr ahassngltd ilkytkshya
      241 apdpskygia kgkniivihl esfqqflinm kvdgqevtpf lnslendnkq tlafdnffhe
      301 vgqgktsdae nmletgtfgl pqgslftqlg sdntfqaapa ilnqqagyts avfhgnvgsf
      361 wnrdhvyknl gyqnffdrsy fnqsdenlgy gildkdmlke tvghlehlqq pfytkfltvt
      421 nhtpyltddk nfnfpalktg nstvddyvrt ahyldeslrq ffdylkasgi yqnsifmiyg
      481 dhfgisdsnn kdlakalgkd pttwdkfdda qmqrvplmfh ipgytkggiq hqyggeidvl
      541 ptllhlmgid tkkyiqfgtd lfspqhdqtv afrngdfvsp nytelggety dnktgekvdp
      601 kalniepeid kqqkqvkqal slsdklnqen llrfytpegf tpvdpkkydy hdldkkntei
      661 ekekgsqsts lyskngnktt anlyppiq
//
LOCUS       WP_010743988             600 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010743988
VERSION     WP_010743988.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..600
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67396
     Region          <46..186
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mllklsltgi kgrlrdyvvl fsglvvasgi fymfeglatn eaflknnsmi nsvvmifhlg
       61 tvllsiitfv yilyansflm smrqkdyamf mmlgakgrki aqlifietfv vgvgatlvgv
      121 ilgiglsgvv qqllvkqlei kithfmains saalftliff tvifliaafv namtivrkpi
      181 lnllrasetp lpanrkvitl ileviagiaf lgvgyymmtq vmtlaflali ialvtivlgt
      241 yfvfhsilif vldllkrsds ialkklnnft lsqlsfriqd ytrilsmvam lfalalgait
      301 vglgfhneim kmtdatsayd lvlnngqafn tselqkidat sdvayqqked kdtiyydrgq
      361 fnqtpfmake fttsretkkk sydgetlakd ltasdqlrsl elpeqstkkh qflsseefaa
      421 lpmkatelrl ihvsdftkdk aalkqlaeen fvknptinkd mgsmnqkalv yelynalfsg
      481 fefmgfflgi afltmlascl mfkilsgaks diqrysmlek igtrrkllkq sirkeigilf
      541 lvpgllgvth vlfglqlfkt lmsdpysniw lpfliffvly fiyylltvwi ytgivmkhed
//
LOCUS       WP_010744025             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Enterococcus].
ACCESSION   WP_010744025
VERSION     WP_010744025.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..282
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32102
     Region          5..271
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mpkkaetyvv gnfkggvgks ttvqmlsfes afrkdrktlv idldpqgnts dvlsltaenf
       61 gndtlpdefd atiweavrtg dikssiyqim pnldlipani sfsdfpdymi ekypgdklsq
      121 fkymedliep lkniydviyi dvpptistys naamyvaeyv ivilqtqvks lkgaqnyidy
      181 mnffieqydt dlevvgivpf mmqkrdsvdq eiytaareiy gahlldtvvl nqsrlkrydg
      241 sgityeinkn gkveqwdkra hevfvnilde idehrlilsg ee
//
LOCUS       WP_010744032             391 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Enterococcus].
ACCESSION   WP_010744032
VERSION     WP_010744032.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..391
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43384
     Region          45..367
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mekekpskii qffggktsyy ligliilssl aiyllntvsf ifrpivviit tvlppmvfal
       61 llyyllnpvv nflskrglsr tisivltyvv ifgllffgga rlvpviqdqa qdlikqfpky
      121 vddfqngikn ildttpfaas sgealdsidk lakealnylg snwqdgakgl gtifsavsst
      181 aitlftgpii affliqsphk lyravidmip prfrkdsqsl ikianqqlga flkgqviasl
      241 llgliywvvf lllglqyatv ialaagilsi ipyigsflaf lpglfiafqd stfmvvkfvi
      301 awfvvqllhg dlvvprvmgd klkihpitil vvllvmgdll glvgvifgip iysmikllvv
      361 ftfrkfkqry nkyfsdegay rntgfseddy l
//
LOCUS       WP_010744037             290 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Enterococcus
            raffinosus].
ACCESSION   WP_010744037
VERSION     WP_010744037.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..290
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31734
     Region          12..290
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mvnnryeqlk kaelgaiisi aayilvsamk liignmanse alradglnnf tdilasiavl
       61 iglrisqkpa daehryghwk aenvaslvts fimllvglqv lyssilsvvn kktespdmta
      121 aivgivsaai mygvyffnkr lseevkspgl laaakdnrsd awtsigtaia vfaasfslgw
      181 ldsvaaivva llilktaidi fkesvftlsd gfdqeeldqf nesirhiqqv qsvknikgrt
      241 ygsniyldvt vtmrpeltvk eshdvadqie sllrdkyqvf etdvhvepse
//
LOCUS       WP_010744039             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_010744039
VERSION     WP_010744039.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..146
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16738
     Region          10..135
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mriemaelfs kehtsavklr kqvlggkidw dkekklhvfv aieneevvgt aaiqlypfgi
       61 arvrqvavsp afqgqhigdq lmtrveefaq eqghfrivlt grktaqlfyl krgyhrvlfp
      121 ftkheieflw mtkalpavev pifsen
//
LOCUS       WP_010744078             433 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010744078
VERSION     WP_010744078.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..433
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=47499
     Region          4..433
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 menstfimkl ndllspvaak ignqrhlkai ssgmmfglpf ivigsfflif anppinidry
       61 npetanffmk fmagwkdfav anydlitapy nltmgiigli svfgiafsla seykinpsmn
      121 gmvasviflm vctpvmegti nlnylgtngl fvailigllv vevnrvfevr niklklpdtv
      181 ppmvatfint lvplltniil fygvnlifli ttkkifpetv mqiltpatni agslggflli
      241 vtlgnilwlf gingssiifp ivftlgmaqt glnaeqmang etmthlmnlq mfrisvlgga
      301 ggslglvllm irskvseyrt igklslipgi csinepvifg lpivfnpila ipflitpvis
      361 llltyiaqsv slisvgfivd psftpffaqa ylssmdwrni vfcfvlilis vviyypffkv
      421 mennktklve eeq
//
LOCUS       WP_010744097             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF805 domain-containing protein [Enterococcus].
ACCESSION   WP_010744097
VERSION     WP_010744097.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..205
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23560
     Region          16..132
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mikikkrasy vnfptaikdf fvgyfdfkgr ttragywwvm vgylilsllf ipiivyqfai
       61 iinmliqgvd deqalsygtn nimtmmlvvl viyflfffvp slalltrrcr dvglkgrgff
      121 vlwivslvsg llaamdffln ialvyfsyrs gadiifvyln yaiglfffil tllptdaltv
      181 nsnhsvmrff frskhahekd qsfsn
//
LOCUS       WP_010744119             227 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar transferase [Enterococcus].
ACCESSION   WP_010744119
VERSION     WP_010744119.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..227
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25944
     Region          <26..226
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mnniyennss ieefvlsnqd dfgtsdffgr rtkrvidifv sivslailli plaftallik
       61 ledpkgpiff tqtrvglngk pfviykfrtm yvgaekqlad lmakneiegp mfkmkrdpri
      121 trvggflrkf sidefpqlvn vlkgemsivg prpalpreve qysayhclrl rvkpgctglw
      181 qvsgrnklhf eemiqldlry lnrgsflldv qimlktllvi vthygay
//
LOCUS       WP_010744165             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010744165
VERSION     WP_010744165.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..238
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27522
     Region          13..218
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mkiyhlskll pdntlreedk piieyivkki erneevdirs tamenytsps sisrlskrag
       61 fknfkemiff ltqksnetqi aerslnqqkf lntkqnweei dqifelikeq gqvylsgegf
      121 cdllvkyayr klmlkkiyai dlkdmeikli sdgqpkslii fsqsgenrda lrrikeckel
      181 ggkvitftas pnstflkegd asfqvdpess vinsenstln fffgnclnal eylfdryl
//
LOCUS       WP_010744253             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Enterococcus].
ACCESSION   WP_010744253
VERSION     WP_010744253.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..228
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26131
     Region          146..222
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mcrillltks mmaeqqleek ikhlgyevfc ttellsrien qhipldflsc fqvvllsesi
       61 pteeqgllle rlnktalivi qkrdneqsek mepvlegidy fipinasiei lrdtlsdciq
      121 stentkyisq pfsyrqegva ndsrlerirf sgleiiflkl lidadgetvs rellcqeiwn
      181 snlthskqah lsnlakrirs kmheagidss mlttlwgegy rldraldl
//
LOCUS       WP_010744203             441 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus raffinosus].
ACCESSION   WP_010744203
VERSION     WP_010744203.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47181
     Region          21..377
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mskkseskns lvkrysplat aagigsmlgs gcivglsati pvwqkglelt tgqvgilsgs
       61 ltfaiafgsm fagniskgfg lirsfnwlnl fyaigaaicl fsnsflmlla gviimgassg
      121 adlpisltvv shdapdeats aklvsstqif wqigvfisyi csfllsgieg vlgarivfai
      181 lfgfavvtwl wrtlskkfql fheegnarqa anktiteqgq evsfktvlfg qdknkylgff
      241 laiitfyvcw nllantwgqf qtyaltnaga sqtqatglgi ilnivslatt ivfasisggk
      301 yrnkaffiga fvqfaamigm allgggagfi alaitiafyn fgnplageai ykvwtqesfp
      361 aetraslqgf ingfsrlccg lfafvtpylv mpdriqssmi gfagivvvat iagiimmrlq
      421 kkygtsenre metihdsdvt v
//
LOCUS       WP_010744317             325 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Enterococcus].
ACCESSION   WP_010744317
VERSION     WP_010744317.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..325
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36084
     Region          1..250
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mklaifgsgk ivqeflpitk dlpeidvkai lgtkrsqekt ekiqaeygie asytdidecl
       61 ksdafdtvyv avpnhlhygf akkaleagkh vicekpftlk haelldleql alkkdvvlve
      121 aitnqylvny qgikeasqki gklkiiecny sqyssrydaf kegtilpafn pkmgggalmd
      181 iniynihlvv gllgkpkhvq yyanieraid tsgmlildyg dvkvvcigak dseatirsti
      241 qgtegsvvvn gptntldsyt teslsgeket fdhkdhphrm ydefklfsqv iknkdmdfvk
      301 kqlehskivm eiveasinda givlg
//
LOCUS       WP_010744347             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010744347
VERSION     WP_010744347.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..249
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28458
     Region          3..245
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdhklseteq ylwdyieshi levpnysivk lseqanvsta tivrtmkkkg yegftafkhh
       61 lkeqenknin fssldkvdeg irrailkneq evirtinmmk igniedaiqk ikfadrvflf
      121 argfsemigq emmvkfqltg kncqmhtdpe iiknisrklt kqdivifisl ngetkelvva
      181 akncydaeig silltannts slmnyceial vgfksegsyf pdyevrsrlp lqiiarilld
      241 syalrvtdn
//
LOCUS       WP_010744390             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010744390
VERSION     WP_010744390.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 429)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..429
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47223
     Region          20..223
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          165..428
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflikimihs ifrnkrhsll igvttiigit lsvsmlstml giqekinlel ksyganievt
       61 pktteiisdl ygtkkhmkqr dsfinekdii kvksmfwgfn ildiapylit svqidqthqp
      121 vemvgtwfnk kltltnndtm vtglpkikkw waiegtwlkd ndltgllvge giaknknwqi
      181 gdiivlkgig tekkleikgi fhsgegddqr lfvnlrvaqq lsgntgkvsk fdvsalttpd
      241 nelakkaain pnqltvkere iwyctayass iayqiqevmp dvvakpvrri aesegkvlek
      301 nklllifvsi isvlgaavga anlvsvtlms rnievglkea lgitmgmlcw ellssiflin
      361 cvagvigfil gqgvtqiigh ivfgsgvpfs iysvpltigl ilfisvigsi ptihylrtfn
      421 padvlhgrs
//
LOCUS       WP_010744442             286 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010744442
VERSION     WP_010744442.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..286
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31832
     Region          1..282
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 msspihlqik smyndfspke qaiadyilen pskvshssis dlaaelgiad stffqftkkl
       61 gfngfkdfkm allkqendlt aitihenvqk ddselvmaqk vfdsnmstlv dtkkllkeqd
      121 lkravkmisd srrlyffgvg gseivatday hkflrspipv ghstdyhlql measllteed
      181 calfishsgk sketihiaea akkngakviv mtsqahspla klgdvvfisi seeiefrsea
      241 lasriaqlsi idslyvilmf hnrenaqnti tkvrtviqsl kenkge
//
LOCUS       WP_010744496             271 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aldo/keto reductase [Enterococcus].
ACCESSION   WP_010744496
VERSION     WP_010744496.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..271
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30886
     Region          9..267
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mdkmkklang lemprlglgv wrvndddatn svkwaisngy qlidtaavyk neegvgegir
       61 qagvnrgdlf ittklwnadq gyesahqafn dslerlgldy vdlylihwpv egkfndswra
      121 meeiyengra kaigvsnfhq hhieelmtta kikpmvnqie lhptltqvql rdflskedia
      181 ieawsplgqg kilqnetlve igqkydktaa qviirwhlqs diivipksvh enrikenfdv
      241 fdfelseedm nqidslnine rlgadpdnfd f
//
LOCUS       WP_010744458             229 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010744458
VERSION     WP_010744458.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..229
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=26162
     Region          117..214
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 metnkkqwlg llivpaelli gdflfplihl drdpklalla stvlfligfv mmlylfhdfl
       61 kaqwhlfrqk lftkllisiv lvagafwllr vvrgmipsel lqlrsstsyt sqkldpswtv
      121 laaitpfiap faeeltfryl llgkfqntil rmlmlfvqgi lfglvhwnnf sgnlyamipy
      181 mvlgvylgai yllskniwss imvhwmintm ngmlpalllf ilslfgitt
//
LOCUS       WP_010744510             453 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TrkH family potassium uptake protein [Enterococcus].
ACCESSION   WP_010744510
VERSION     WP_010744510.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..453
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49032
     Region          13..433
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mnkekrwpfk iypiqfialg fggiilfgsv lltlpmftns gegtpfidal ftatsatcvt
       61 glttlttseh wnmggqliil glievgglgf mmmpfiffav mkrkvglvtr iiiseslnld
      121 glsgviklmy yilrfaigfq llgaillavd fiptygigkg iwyaifhsis afcnagfdlf
      181 gdslvgfqgn ayvllvisgl iiagglgfiv wqdlmafrkt kklslhskla ltvsisllvf
      241 gtivfyvses ggrfivndts pinrfanmlf msvtartagy fsvdygnvsq agilftivlm
      301 figgtsgsta gglktttfgv lliqtismlk grvhaeafhr tirpsvvsra ltlffitltl
      361 ciavtmvmsv tevlprfrgi eyllfetfsa fgtvgltmgl tpslslmgkl liialmyigr
      421 vgiltvgfsl tmrlmkkang ghyklpeesv iig
//
LOCUS       WP_010744499             225 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010744499
VERSION     WP_010744499.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..225
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24472
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnaievndvk kvyssgpaaf ealkgisfti kkgesiaiig ksgsgkstlm hilalldrps
       61 sgkiallnqd tqkinkrtln kmrnetfgfv fqqffmnpkd tvlsnvvlpl kiaglssrqr
      121 kemaidalea velsdkannk andlsggqkq rvciaraivn qpeiifadep tgnldsttge
      181 kieellfnln qnkgitliiv thdpelaarc drqihikdgq llega
//
LOCUS       WP_010744539             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010744539
VERSION     WP_010744539.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..240
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26959
     Region          11..211
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdlelvtkgk qlsendqail tylathinel egvslrkiat tlytspativ rlaqkldfsg
       61 ylelfyflkn qyqpqnqlve atvdisipte kiapsiqnmk qiyqenqdkf itiyatgfss
      121 iiaeylykkl lvngiktlfv naadssgiin nnagnismli visksgetqk viekmqfsqe
      181 rsiptilftg nsqsratkaa tiifevader pldsqnikyn gffgkllllm eyivqeftre
//
LOCUS       WP_010744543             311 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphotransferase family protein [Enterococcus].
ACCESSION   WP_010744543
VERSION     WP_010744543.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..311
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36031
     Region          19..249
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mdkqsavnqi nleypdffie kieflgsgfd seaflinqiy vfkfprhqka aknlykeali
       61 lkeikgqvpl kvrdicfvge sdalnelqfv gyekmegvpl vaeilatltk erkdklakel
      121 aaffkalhgi dlsitiegle vekkskakhe ykvikesayp flkdsvknqi dkvyqrllnq
      181 efhdknclih ndfgasnvyy dlstneingv idfgdsaiyd rdmefvclmy dyeegfdqef
      241 vqklidyygv dpaslinkfn ftgfynqlen iylgkefemk elldesihsi qkgiegyeen
      301 ilkedktkyy l
//
LOCUS       WP_010744551             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Enterococcus].
ACCESSION   WP_010744551
VERSION     WP_010744551.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..322
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34591
     Region          2..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydviiiggg pagltaalyn ararlkvlll ektklggqiv stheianfpg sikttekets
       61 gpelikrmad qaqqfgaeiq lrkevtdldl egsvkkikck dgsvyeshav icangafpre
      121 igcagerela gkgvsycatc dgaffedmev fvigggnsav eeamfittfa ckvtiiqnls
      181 dltadaiave qvkandkidy ifdsvvesie gdgmveamti rntktdevtr feadeddglf
      241 gifvfignvp stklyegkip lneygymitd damctkvpgv faagdmrpkv lrqvvtatgd
      301 gaiaafsaqk yvekikrevp tt
//
LOCUS       WP_010744614             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [Enterococcus].
ACCESSION   WP_010744614
VERSION     WP_010744614.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26800
     Region          1..226
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 merlqkviah agiasrrkae ayitdgrvkv ngevikelgt kvgkkdivev dgvpiyqeep
       61 vyylfykprg visavtddkn rkvvtdyfss vperiypvgr ldydtsgill ltndgdfsqk
      121 lahpkhqidk vyvakvkgya ekrnllpltk giriegkkta parfeilstd kkaetsiiel
      181 tihegrnhqv knmlaavglp vqklkreryg dltlqglrpg eyrrlntkei ntllnqsk
//
LOCUS       WP_010744678             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010744678
VERSION     WP_010744678.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..233
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25406
     Region          4..220
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mayidvides khykmgetvi kanekinfsi ekgevavilg psgagkstvl nilggmdscd
       61 egkvvvdgtn iaafsdkelt tyrrndvgfv fqfynlvpnl takenvelas qivadamepe
      121 avlrsvglge rmdnfpaqls ggeqqrvtia ralakrpkll lcdeptgald fetgkqilki
      181 lqdtarengt tvviithnsa iapmadrvir indarvrsee lneqpqsied iqw
//
LOCUS       WP_010744688             163 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Enterococcus
            raffinosus].
ACCESSION   WP_010744688
VERSION     WP_010744688.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Leiros,H.K., Tedesco,C. and McSweeney,S.M.
  TITLE     High-resolution structure of the antibiotic resistance protein NimA
            from Deinococcus radiodurans
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 64 (Pt 6), 442-447
            (2008)
   PUBMED   18540048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..163
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18422
     Region          1..159
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 mrrkkrqvtd rksiqnlvee aqvvrialng edypyvvpvn ygyewendql tlfvhgateg
       61 kkvsmikndp rvavelegnh klvegtmnaa tysyayqsli gfgkaeived leekrkalhv
      121 lmdhaakgaa fdeipesmlk rtgiikivld sytmkenvhp dek
//
LOCUS       WP_010744690             169 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleoside 2-deoxyribosyltransferase [Enterococcus].
ACCESSION   WP_010744690
VERSION     WP_010744690.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..169
                     /product="nucleoside 2-deoxyribosyltransferase"
                     /calculated_mol_wt=18586
     Region          9..162
                     /region_name="RCL"
                     /note="Nucleoside 2-deoxyribosyltransferase [Nucleotide
                     transport and metabolism]; COG3613"
                     /db_xref="CDD:442831"
ORIGIN      
        1 mttskhiyfa aplfaqsdlf ynqylvkkir elddnltiyl pqenegindk sayadskmia
       61 ladtdevlks dlmvalldgl tidagvasei gvayakgipv ialytdsrqq gadnqqkida
      121 lqtpaenqfh ylnlytvgli klngtivsne ealleaiksy legsdfrdl
//
LOCUS       WP_010744698             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010744698
VERSION     WP_010744698.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..254
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28667
     Region          7..253
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mknsiinidk rhkdildile kkehmttlel sealdvslst irrdlhllee kndiirkfgy
       61 cifnyenkpd teqsgpvrik qalaqeasky ihdydtvfin ssstaiktvd ylhsehltii
      121 tnnlkinyat qnpeynfvlt ggemrfpkea lvgdvvinll ssinadvcvv gcsgidieng
      181 vttkfmneat inemmvqrtt rckilvadhr kvgqtskfkm adisafdyli tdqfsseevl
      241 tkiqhmgvtv vqvt
//
LOCUS       WP_010744713             223 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010744713
VERSION     WP_010744713.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..223
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25234
     Region          23..210
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtpqlkqhhl dllnkyglld hqsvcevqqf ksgetifsqg veykyimivv sgkakvctsa
       61 psgkdlvlay ylssgligdv elmsnttyat asvitlspfe viivpfqddq dsifknltfm
      121 ttlakglsen linsshnyts nalysgeqrl ctyilqgsyk nyffdnltdm aatigisyrh
      181 llrllnklcd dgilkrekrk fqitdmeqlk yrsseaeyfk tny
//
LOCUS       WP_010744715             184 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_010744715
VERSION     WP_010744715.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..184
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21850
     Region          31..166
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mldksvpfip ftmfrpsdap plpeiqlpkd yrivfyqpgd ekewckieta vlefetekda
       61 mdyfqrsfap yqdelkkrml fvenaegkkv gtftawwted hsprlhwlgv lpeeqrkgla
      121 kalairvtql lheyyphqdl ylntqtwshh avklyeklny qifqnqnyqk ildvlkeanq
      181 pqke
//
LOCUS       WP_010744717             126 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PH domain-containing protein [Enterococcus].
ACCESSION   WP_010744717
VERSION     WP_010744717.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10547098
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..126
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13986
     Region          3..121
                     /region_name="bPH_1"
                     /note="Bacterial PH domain; pfam08000"
                     /db_xref="CDD:462337"
ORIGIN      
        1 msifdglmgn asqhnnkave eklkdvlitg etvslafklv rdlivftdfr lilvdkqgmt
       61 gkkveyksip yrsisrfsve tsghfdldae lkiwissael paetiqfrkd knivavqkal
      121 alalsk
//
LOCUS       WP_010744725             331 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010744725
VERSION     WP_010744725.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..331
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37345
     Region          3..331
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mglnvsevql sygkkrilde lsfelndgei valfgpsgvg ktsllkmiag iqpvnkgkii
       61 fsegysqest vlvfqdfwlf phmnvvdnia fglkarkfsk erirekinki laafdlkgle
      121 kqfpdelsgg qkqrvalara ivlepkllll depfanldsh lkeamreylr rlqktycfsv
      181 ilvthdrdea fqladrmill ldgkiqqigt pqeiyfyprn kkvaksigen nfipgvvsdh
      241 iftlenthlt vrnptniqga aslfipygae ievceagvpa lvehhewtpn gqrtqvkign
      301 tsciftnlsk kiidqrqifl kfnddlqvmp r
//
LOCUS       WP_010744751            1160 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Enterococcus raffinosus].
ACCESSION   WP_010744751
VERSION     WP_010744751.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1160)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1160)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1160)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1160
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..1160
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=134391
     Region          4..1143
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mplqfllgag qndatermiq taqawleqns enrvfflvpn ynkfeqeirl lsamkqdnka
       61 vefstirtqv fsfqrlawyf lqkngqipgn ilseagnami lrkilheqre eltifrgevn
      121 kagfiqqlvr fyqemqignv tvedlvengn dqdqvlklqd lkkvfsayee alfkykvand
      181 dplqllqqyl stkkmsnnlf ivsgftrfna relgvlnelm vcgellvsle ldrpypseep
      241 nplnlfaepg ktyfqlkksa daykipvrpd qfaqmnqtvf nqvgefwanq krrnleqndq
      301 vqikifstla deirktgeei rrlvrdegyr yrdiqillrn sqaynsilpd lfnkldipfy
      361 ldetqemaah plieflqalf ltdsyhyrin dvfrmlrtel fapfdwtadt wfnlqqeyre
      421 kidqtenvcl aynfrgsawt keadwefvdy dfeadvfnda keleattnev rrsvqqvipv
      481 ffkkiknskn gleaatffyh fleasgvkrq llfwrdqeva kgsldkarnh eqtwqalldl
      541 ldeyvliyge dsfdwetfqe iflaglmnvt ygkiptaidq vrvndlelar idqtkvtfai
      601 glnsndfpar fddkglltae ersafnqnlp egkflpesng skvnrepfla ysvflsasek
      661 lylsmattve gekkleispf lrqlsqglkl piqeneplrl msdpenhlgt mrtllsdlia
      721 lnrfaqdenr aflpawrelq kfiqnsslss maqrvfkslq dlnvprellp etaerlygkn
      781 lyvsvsrien fyncqykyfa nfglglkert vygltpaaag dfyhealdyf frlikeqglr
      841 lselneeert nladqvlkei fgelkfails ssarmnyiry qlsrtiqkvs wglvnqgart
      901 kfepqqtevi fgsiggqkgi pginlplsng gevairgkid rldqlqsaen dwlsvidyks
      961 sphsfnvada yygialqlit yldvavtdfs qssgkaikpa gayylhvhnp vlkepknier
     1021 dmlkayqydg lfakepelyd qldqsleeke nsllfpikkd kngqivavlq srdkfydlse
     1081 idllrkynre kiqeagnqiv sgeiklnpty kdnqriacqy cpfrsvckfd amlkennyhr
     1141 leklskeevl krmeeelhdn
//
LOCUS       WP_010744775             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [Enterococcus].
ACCESSION   WP_010744775
VERSION     WP_010744775.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..304
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34121
     Region          43..296
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mflfttqtid ssntnvvdqa teqlsawqky whaidwdrvf siliqkglti lavlilfyli
       61 rkignflinr sfdrqkkkia dnvtrietih tltlnvfsyt lfffflysil dtlgipvgsl
      121 lagagiagia iglgaqgftn diitgffiim eqqidvgdyi rlvnlniegt vtsvgirmlq
      181 mkaadgtvhf vpnrnittis nlsrahmqvk vdvriqpdeg ydkisqlidk anqklakdfk
      241 deifdgptlf gmvdlgnsny airtilyvtn gkqyklqeef lttyvkvlnq ngftipnnpi
      301 tigk
//
LOCUS       WP_010744802             215 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HD domain-containing protein [Enterococcus].
ACCESSION   WP_010744802
VERSION     WP_010744802.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..215
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24677
     Region          6..213
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 mqknkveeir hysieklggd hsghdfyhve rvakianqla eqegisdtli ieaasylhdi
       61 iddkvvadvg lekrnlkkfl keldfstkei qeifeiienm sfskeieegk adltvagqiv
      121 qdadridalg aigilrtayy gghtdsplyd pailpqefks kqeyrkkstv inhfyeklfk
      181 lpetmntkag kleaerrkkf menflevfyt ewnls
//
LOCUS       WP_010744813              66 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Enterococcus].
ACCESSION   WP_010744813
VERSION     WP_010744813.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7395
     Region          1..65
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mnngivkwfd ekkgygfity eenqevfvhf taieedgfks ldpgdevtfv ivegargmqa
       61 ahvkkk
//
LOCUS       WP_010744877             511 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease/substrate-binding protein
            [Enterococcus].
ACCESSION   WP_010744877
VERSION     WP_010744877.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 511)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..511
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56075
     Region          2..204
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          235..502
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(241,243,292..293,296,341,343,422,446)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mnelintfse rkddllsaif ehlaislsal liaiviaipl aillsqrkkl aevvlqitsi
       61 lqtipslall gllipfvgig tvpalialvv yallpifqnt yiglseidps ieeaadafgm
      121 srmrklirve lpmampviis gvrtalvlii gtatlaalig agglgtfill gidrndpnlt
      181 ligaissall aiifstlirf lqnrsgkvtl ialgviclsi ggiffaqnnp igtetvtiag
      241 klgsepdili nmykevikde dssinvelkp nfgktsflfs avksdqidiy peftgtvles
      301 lvevpkntpd nltpektyte anklldsqfd mrllkpmdye ntyalamkks eaekrgitki
      361 sqlqaqqdql kagftlefid rqdgyrgiqd kygvklssvq smepalryqa intgdvdvid
      421 aystdseikq ydlmtleddq hlfppyqgap lmkkefaekh pkvvkalnrl agkitedqmi
      481 emnylvnvkk eqpakvahdf lvkekiigee k
//
LOCUS       WP_010744992             250 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010744992
VERSION     WP_010744992.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..250
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27592
     Region          1..232
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlteerhrki ierlerdgvv ksqdlvqwld ssestvrrdl qeledlgile rvhggakrpq
       61 hleqelgmfe kssknvqqkk lvakyaveci aegdviylda gtttsemipf lkertvtvvt
      121 nsvglaarlv eaeiativlg griklttdav vgsqaleqlk qyrfnkafmg mngvhtdsgy
      181 stpdpeeail kraaiqqaee afilvdhskf nqtsfvsvap lsaasiltdt cplvihdqit
      241 eqttlkevsv
//
LOCUS       WP_010745119             422 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010745119
VERSION     WP_010745119.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..422
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=46764
     Region          1..409
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mkkfmdwlan sfapkakklt qkpsvaglss amqklipfim tgsivffynv frsyipqlpd
       61 lgnisnysfg migliaafmv anqymekfkh pnyaitagiv svcvlmmtlh pvaakegvyd
      121 mgrigptgil igvivgavvs vifhyfsklh llqhselpdf vvewinniip iflslalwst
      181 lifalkidvf eviinlfepi qsfgqslpgl illvlipaff ysmgistwlw saiqnpifia
      241 giaanalamk ngdvgmnivt netvyslgli mmggtgatlt lnllmcfska kklktlgric
      301 igpslfnine pivfstpvvm npilmmpmwi nsitgscvvw famrggllni pqdlmqvaqi
      361 papissvmil qdfrailwyv llfamylltw ypffkvyeke vlaeehqqek vnepmtapae
      421 av
//
LOCUS       WP_010745133             235 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus
            raffinosus].
ACCESSION   WP_010745133
VERSION     WP_010745133.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..235
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27369
     Region          152..225
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mkplliltkn llveqtiqar lqelgyevfc setflrklyq rlnikevken fqgvilngti
       61 tdreaesiis tleqqipcfr kldrdpteqe eenirkigfc gwisdsqssd rlreslstqf
      121 ttldhqknsq vssllqtsee lqkknlqvfl rkltnrewkf fqklmeanga ivsrtemcly
      181 iwekapnhsy laqlsvlvkr ikgklksvgi deesletiwg kgyrlllens keeky
//
LOCUS       WP_010745174              67 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010745174
VERSION     WP_010745174.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..67
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7633
     Region          1..67
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mnvkfeshlk kyrtlkgltq eqladlvgvr retimrleka qynpslklal diakvvdtpv
       61 tdlfife
//
LOCUS       WP_010745176             341 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LLM class flavin-dependent oxidoreductase
            [Enterococcus].
ACCESSION   WP_010745176
VERSION     WP_010745176.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..341
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38342
     Region          36..340
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mkkigflsfg hwmdqgslvk taqdsylqsi dlaveaekig idgayyrvhh fadqigspfp
       61 llsaigakts kieigtglid mryenpymma enagltdiit qgrvelgvgr gspeqvldgw
      121 kyfgydysee eikditrert leflkllege rfaeqnpqpm fpqapgklrl epyseglrqr
      181 iwwgagstqt aiwaaqhgmn lqsstlvnye tnepfhiqqa kqlraykeaw keaghdfepr
      241 tlvtrsiqpi ttdldrqlfg hqgddanydq vgflayhqnp tifgktfage pdkiakelae
      301 deaikeadtv lvtipntlgv dynihlldti vkdvapelgw r
//
LOCUS       WP_010745218             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SGNH/GDSL hydrolase family protein [Enterococcus].
ACCESSION   WP_010745218
VERSION     WP_010745218.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..193
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=21127
     Region          4..186
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mkeivlfgds lltgvmnget sdildtyild eltemgfpgy qlvklgkrge tssdglarvs
       61 eavdaegdfv visfgtndsl khetsleafg enlkeiiesf daskvilltt gyintevypk
      121 gdnerqqlfa qkakmvaaes gvnvidlyhh mtvypkpnef vqtfdgihps degyhflgal
      181 iardikeill aeg
//
LOCUS       WP_010745221             315 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar-binding transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010745221
VERSION     WP_010745221.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..315
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35363
     Region          11..314
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mqkeedkllv riaemyyqed knqsqiskel nihrstisrl lkrsrnegiv nisinydkag
       61 tysiekelqe kfdlekaiiv qagadlsrtq kdkllaqgvg eylteiikdd mifgfswget
      121 msaipeglsn ydvnnilcvp miggpsgrli sdyhvntity easkklngra llidspafpe
      181 tvalkkalme nefnqelidy wrkidiailg igsptlkase swkqfygedv laylegkkvv
      241 gdvvsrfyni egehidntld drligidisd lkrtpyrigv aeavdkadai asalkgryin
      301 vlvtteetaq evlkr
//
LOCUS       WP_010745276             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfurtransferase [Enterococcus].
ACCESSION   WP_010745276
VERSION     WP_010745276.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..308
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33681
     Region          50..301
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mkktiiglla lvtlgltacg ggsdettdta kakketeaft geyivnadyv kknlddvili
       61 dargeeeank gtvkgataig wqnlasveeg asgdekwglv lepkelakrl gekgiakdke
      121 ivlfagaqkg wgddgriawe llaagykdvk mvdggfaalk kagletdies tkldpvdvti
      181 dsidqthiir tdelkkdyde ykivdvredk eyegdvlyge akgghlpdai hipftdlfns
      241 ngklkskkdl tklfedagla kedkivtyct agirsaymel vmdmcgfkqv knydgsyyrw
      301 akvedvek
//
LOCUS       WP_010745374             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cysteine hydrolase family protein [Enterococcus].
ACCESSION   WP_010745374
VERSION     WP_010745374.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..181
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19895
     Region          3..181
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mrallsidyt kdfvatdgkl ttgeagqaie gelvaitedy fqqgnfvvfa idghdpsdqy
       61 hpenklfpah nvigtsgrel ygsladfyqa nqaektvywi dkrhysafsg tdldirlrer
      121 gitelcltgv ctdicvlhta vdaynlgyql vipekavasf datghtwaln hfkntlgati
      181 i
//
LOCUS       WP_010745424            1088 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: vWA domain-containing protein [Enterococcus].
ACCESSION   WP_010745424
VERSION     WP_010745424.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10076759
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..1088
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=120575
     Region          321..>457
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cd00198"
                     /db_xref="CDD:238119"
     Site            order(328,415,451)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238119"
     Region          628..>1005
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mrkskflvlv lllfsiviem amplisvqak tneielvdde slklsytyee kkettkwqlt
       61 fdrqsekgyq qrlkfkltda kdktidystv dmdhlieedg wlkeknfses indqlswels
      121 ssvkklnvyv qldqektate dgkkasslqe nilkreepfv letksttesq tkttqssekt
      181 atqatkttse afigpqkegv naaqraatat ngisrmyanh ydaktptyld nggthpensw
      241 qptgqtnvin hqggqegqng wdnnagwdvt qdnhtnsyih ygqdlnnsnv alrklaqqtd
      301 kedefkvkln vrgnttykpg vdivflldns gsmtdglpgk pngrktdaia amtkivdelk
      361 kvyvpsaeni rigahifsdy qysawgnkpg qqrtfpltsn taawsnmvtv ysgatatgat
      421 ftqrglkeaq difddagdtt grqqllfvlt dgapnyswdt ddtgtpnldm fvdllhfknf
      481 ktgtkgsykv gtplgtsgyk ttiipayngv inshitttns tamdiknagi eihtiavelt
      541 lnvnepeskr aeqlrglykm stkkanatng plndvasdfh fynvenaddl vdtfkawydt
      601 virtvdrgii sdplgdmvel vgdptwrqvd stgkaieada epqisvssdr rkievnninl
      661 tanqeievey tvrlktsdpt fasstwypan ktttlkptpe rtgdrldfgv psvrlktadf
      721 vipvkkiwsd khqnqenywg lrpnkvtatl qrldgatwqd vesidlkstn nwegnfsave
      781 ggedktyrvv egsrtagyka pvvnqqnfts eniasggiti tnellrgnhq fwkfmedgtt
      841 kftsdlpkfk vtrrdgkvla enltpdatgk vaindfpigt ytveetyvpe gfqkmadfei
      901 vvtennppts lvfkvngrtd dyhainrlkd fsvkvekidp ngnaltgavf kltgpngyee
      961 tistgstftf tglrpgiysl kevdnpegyq riqepiafvi nqdgsfdvss hpnvsdssgg
     1021 tgsnntitlk vtnkkvkpgt lprtgnsgik gffliagmla vtggtvggfc fykvrkelar
     1081 trekmnee
//
LOCUS       WP_010745453             258 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Enterococcus].
ACCESSION   WP_010745453
VERSION     WP_010745453.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..258
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29383
     Region          2..254
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mifdshthln aeqfekeipe tverarelgv temavvgfdt ptieksleln qqyegiysii
       61 gwhpteagsy tkvieedlik kltlpkvval geigldyhwm edpkevqdsv frrqiaiake
      121 mnlpisihtr eamedtykil keedirdigg imhsfsgsge wakyfldlgm hvsfsgvvtf
      181 kkaldvqeaa tivpmdkllv etdapylapm pyrgkrnepg ytryvvekia elrnlpmeei
      241 aqqttenahr lfrinahd
//
LOCUS       WP_010745565             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010745565
VERSION     WP_010745565.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..305
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34100
     Region          6..222
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mdnqivslsk vekkfgkfqa lkdvtfdvkk gevlgfigpn gsgksttiri llgmlkksgg
       61 eatifgkdvw kedteihkgi ayvpgdvylw pnltggeiid lllrlngqkr tqkteeliek
      121 fqldpkkkar tyskgnrqki aliaalsqea elyifdepts gldplneksf qeevlklkea
      181 gksillsshi lsevekmcdr iaiiregeii etgdlasmrh ltrieitvet kstldgidql
      241 tgvhkvvfse enhhqavlsv dreqmtqimi fladkqivnl tstpptledl fmryyekqgv
      301 dsyga
//
LOCUS       WP_010745566             536 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010745566
VERSION     WP_010745566.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..536
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58327
     Region          1..536
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 mghsgtktsy llkanlkqnr ikhviwlvll vglfaaaame fhvlfgtqed inaivetlkt
       61 pamvslfgef saeksyttat vfahemlvfl amfmvfmnis laisntrtee dsgllemvrs
      121 rtvgrlapiy atileillin gsmgslyvis lfvadlngat iqgnflmgig lascgmmfgf
      181 isllmaqlan nsrsasfmsy glygffyiir mitdvtdprw twlspvgwiq ktaiythdhw
      241 lpialmiglg liclliavki verrdigsgi laarngkpka gkllssplgl vltiernsii
      301 gwvfggvilg aaygsvfsti gdiigsnpty rkilgvtqin aanrelilny lnmlalffva
      361 iaaisgilii frlksddkkg yleilhsksi sktrlalsyf gvgtfvsilv ftgtlagaff
      421 igngmmddpl aikyfwqvll gflpatlffv giaifftgaf pkltnilwly laasvlvkml
      481 gpllnlsddv anispfgwvg kvptenadnt vvifltaafl vltvlgilgy nkrdlg
//
LOCUS       WP_010745582             477 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Enterococcus].
ACCESSION   WP_010745582
VERSION     WP_010745582.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..477
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53308
     Region          9..477
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mieekksfis wpvlammsfv tvigfddiiy nfanqglgvi tswiilllly vipyslmvgq
       61 lgsvfnhegg gltswvrgts gdrlgyftaw tywaasipyv vdtanavvvg fgwlvngnds
      121 medkmsnsmf alltfcvfla fiflqrhfkk slevlstlgg gamfimailf vfmtfaslfm
      181 pnghietqpm nlgavipkfd lhylttigll iyaingaelv apfvtrmrkp qkdfpkamim
      241 ltvmtifltv fgsfslgvff nahhlpnnlk mngsyyafqr lgeffhlgnt lmyvfavtqi
      301 iymcallavl ldamtrmlis dtgkqfmpkk ltklnddglp ingyilttal safilllgvf
      361 lpemndifnw llnlngiisp gvtcwifyaf irirldsrkf qsdyvfiknd rmavfvggwc
      421 lvvtviatlf gvlpqdapyg sslfwhelii nivgiavlig lgfimpglak rerekea
//
LOCUS       WP_010745597             893 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010745597
VERSION     WP_010745597.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 893)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..893
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=100806
     Region          246..>334
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          <353..494
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          649..891
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mknktylkas lreiiyskgr fiaivliill gtllyvgika tgpilnhsas qfvdkqelsn
       61 lqivstgglt krdeeaaaei pdaevesgyq lfyadskknq vvklysynkk sqqnqlivks
      121 ghlpkkenei vldekakeeg yrlnqtykid qpdqlkrktf kivgfvqspm yisteergls
      181 nvgkgnvdff aylpesnfss eiksviyvrf knvqgketyg sayeqtmdkn iaaseklfkd
      241 rpeeraaeir keaqaellpk knevadglak laegqkeidq akdqleqqqa migtespqla
      301 qaqtalenqq keldnnreql lsaqkkiren eqaihdlktp sytfdqraen pgfqeygdls
      361 eriaaianvf pvffffiaal itfttmtrmv eenrreigtl kalgysrfei aikyiiyals
      421 aaiigivlgs vigthtlprl vfelssdryn fpgveafyls rpivqatiaf lfaslgaall
      481 vlmrelhekp aellqpkapk pgkrifleri tpiwsrmsfn skvsyrnlfr yksrmimavi
      541 giagcaalmv agvglkdsls svgdkqfgpi idydaivtlk dqpdraavek iftdkekits
      601 hlgmmnqtve lkqkgqanqk ltmmvpesrk afdqylhlkq qekkftlpee gavitqkiae
      661 lfdlkkgdsl tvydedqqpf kirianisdn ylgnflylsk dyyqkvrgts favnsyllks
      721 kkmskseeed lsktllnseq vtntsfistq ietqehsmdn ldgivwifvv lsgllafivl
      781 ynltninvse rlrelstikv lgfydrevts yifrenfvft ilgilfgygl giiltkfild
      841 qasmetitfp lviragayll aggltilfsv ivmvathfrl qhinmidalk sne
//
LOCUS       WP_010745609             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aromatic acid exporter family protein [Enterococcus].
ACCESSION   WP_010745609
VERSION     WP_010745609.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10532842
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..316
                     /product="aromatic acid exporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35796
     Region          1..141
                     /region_name="ArAE_1"
                     /note="Aromatic acid exporter family member 1; pfam06081"
                     /db_xref="CDD:428756"
     Region          147..307
                     /region_name="ArAE_1_C"
                     /note="Putative aromatic acid exporter C-terminal domain;
                     pfam11728"
                     /db_xref="CDD:432028"
ORIGIN      
        1 mkiglrtikt avaapialll asglhlesaa saaiitiltv tntkrstakt alnrlfsltl
       61 atliaavcfs llgfhpivfg fyllvfipls irfdlaegia vssvlithyl vagempisli
      121 ineyllmilg vgcalvanly mpntekkiqe dqmvvevsmk kmlgqmsayl nqpakeeelr
      181 hecltlrdfv reaqvraqef eenrffsgns yyfeyfamrr lqlrvladml qilnrldaap
      241 edvqelrelf eftsrtlaee ndgseiltki aetdqryqqk qlpesrqafe eramlfqlfq
      301 lfqdfieika gfnrkk
//
LOCUS       WP_010745611             171 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VanZ family protein [Enterococcus].
ACCESSION   WP_010745611
VERSION     WP_010745611.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..171
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=18860
     Region          45..130
                     /region_name="VanZ"
                     /note="Glycopeptide antibiotics resistance protein
                     [Defense mechanisms]; COG4767"
                     /db_xref="CDD:443799"
ORIGIN      
        1 matkklskil lliysllliw illfklslsf seiteslahp mrsinlipfq dsmivngkva
       61 lneillnavi faplgvllgi saknwsflrk igfiflfsfv iemlqfilgi gatdatdllm
      121 nfvggflgli fyqglkqvip etkldkrliv igtiagifcl gvilllifgn r
//
LOCUS       WP_010745656             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010745656
VERSION     WP_010745656.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28375
     Region          1..227
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mekiinvqhl sksygtrnnk vtvlndlnft vekgefvgim gpsgagkttl mnilstillp
       61 tmgsvkiaga ditqmresrl tdfrreklgf ifqdfnlids ltvkdniilp ltvsklsnne
      121 ieermlrlag ilriehilar ypeeisvgqq qrtaaarali skplvlfade ptgsldsksa
      181 teflnylddv nlheettilm vthdpytasy cnrvlfikdg rffaeivrrs srkdffekvi
      241 dmqatigggg kanad
//
LOCUS       WP_010745506             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 32 protein [Enterococcus].
ACCESSION   WP_010745506
VERSION     WP_010745506.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Yoko-o,T., Tsukahara,K., Watanabe,T., Hata-Sugi,N., Yoshimatsu,K.,
            Nagasu,T. and Jigami,Y.
  TITLE     Schizosaccharomyces pombe och1(+) encodes
            alpha-1,6-mannosyltransferase that is involved in outer chain
            elongation of N-linked oligosaccharides
  JOURNAL   FEBS Lett 489 (1), 75-80 (2001)
   PUBMED   11231017
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..253
                     /product="glycosyltransferase family 32 protein"
                     /EC_number="2.4.-.-"
                     /calculated_mol_wt=29613
     Region          1..129
                     /region_name="OCH1"
                     /note="Mannosyltransferase OCH1 or related enzyme [Cell
                     wall/membrane/envelope biogenesis]; COG3774"
                     /db_xref="CDD:442988"
ORIGIN      
        1 mipkrihycw fgnkpipdsv kkcimswkin cpeyeiirwd esnydinkit fikeayqakk
       61 yafvsdyarl diiynnggfy ldtdveliks ldrfcedkcf mgcelpgkva tglgfgatkg
      121 stilkrnmdi yekssfyeng hqnsitcvey tsnllleygl kksrdiqyld sgnitiypte
      181 ffcpynmitk kttitnntys ihhydatwys enillkkwkk milpmkvylk rivnslfgeg
      241 iyekirnslk rdl
//
LOCUS       WP_010745667             366 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus raffinosus].
ACCESSION   WP_010745667
VERSION     WP_010745667.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..366
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41932
     Region          111..355
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mkhlnkywad ffffeiigiv llfqqefkpq mvvfllasil laapalllkk slgqamsvfp
       61 llilsffwpm lliflpanlr iswreeviws wglivlvipl fqdgysyseh llifclscfa
      121 illawrgkkq meleeaflql kddswekqel lkqknqeliq sqetfidlei seernriard
      181 ihdnvghlls saiiqlgaie ainqadslke pltqlkvtih tgmdniresv hdlhetslsf
      241 kkgldfliad fqfcevilrg nipenltqeq drtllmvmke alanvmkhsn atnvtlsfne
      301 lpafyrlqil dngtlakksg sgiglksmqq rlekiggqmh lsqtpnhfmi hvilpkntrs
      361 alrein
//
LOCUS       WP_010745703             314 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ROK family protein [Enterococcus].
ACCESSION   WP_010745703
VERSION     WP_010745703.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..314
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33099
     Region          7..306
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mekqnkkiig vdiggtaikf almdtqgiie kkwsiptnis ekgryipaei gssilssidk
       61 nalravegig igvpgaissd gavvvqavnl gweqlplkkm iegeigleac llndanaaal
      121 gemwkgaarg renllfvtlg tgvgggiiln gevlngchsa ggeighipir tdenrlcgcg
      181 grncletfas anglmlsmrk kleqlgeswt evtppiifkk aaqnntaake vinefatvla
      241 qalagimnti dveeiiiggg vseagadlld plmeklemyv fpsikdhfsl rkallgndag
      301 iygagyfylt ksar
//
LOCUS       WP_010745695             351 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Enterococcus].
ACCESSION   WP_010745695
VERSION     WP_010745695.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..351
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39500
     Region          1..269
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkkrvglvgf ggmgkqhikr ikesqyveit gifdidsdkd ystisskikk ydslsalldd
       61 stieivliat pndthktiai qalqsgkhvi sekpvtlnts elkeilttae kcgkkftvhq
      121 nrrwdenfli tkklleekkl gellyvenrv qgsrgipkdw rrnknqgggm lldwgvhlid
      181 rilflfpnqk iislhatlty flnhevddgf kieivfdslk kaylevgttn fielpewyvv
      241 gsigtavied felngkfvtl tgelakeavp vetgagltkt maprnddsve tfplpyvesn
      301 vvefydnfaq tidgkaepfi kdeelirltt iidacfeasr knevlhfpng l
//
LOCUS       WP_010745788             152 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus raffinosus].
ACCESSION   WP_010745788
VERSION     WP_010745788.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..152
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17771
     Region          6..116
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(6..7,21,38..40)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(52,55,59..60,69,87,91,97,101,104..105)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mkkfligdit kmygisqdtl ryydkagllp fvkknkagrr efteddlgyi evidclkrsg
       61 ipvkeiakfm dwcvegdetl pqrytfmieq eaalekkiyd lqtqldflrw kkwyyqtane
      121 agteevffke gtrqvdgkwh qkylasknpg sv
//
LOCUS       WP_010745853             388 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Enterococcus].
ACCESSION   WP_010745853
VERSION     WP_010745853.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10478446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..388
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43119
     Region          1..>23
                     /region_name="YifL"
                     /note="Small periplasmic lipoprotein YifL (function
                     unknown) [Function unknown]; COG5567"
                     /db_xref="CDD:444309"
     Region          253..388
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
ORIGIN      
        1 mkkflgfisl iflsilltac gnkvsvedlk andwqmdkee nkedinfkvs fsdhimtwap
       61 dmssvkseas newekmgedf gkqiveniky kveyklkgtt ihlkekdlnl dddysiekdg
      121 nnivltpedk daqklilkpy skkakskeas ttsstsknkn vadlskvien fkndglevne
      181 prkmtkddyg maplkakdgm ifgvqvgtdg eyqnarifsf envddlndtk kyyddlgkes
      241 smtfsytaan edklvlmqfn gdlpkevvdk yvdkadltlt pvsfntnsss sqdtqdgntn
      301 sstataspeq qtqqeqaapq qdpaqqeqaa eqndssadtg tqygtvqpge gpkevagryg
      361 msvedfldan gmdadnyyfd pgqqvvvk
//
LOCUS       WP_010745881             205 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            raffinosus].
ACCESSION   WP_010745881
VERSION     WP_010745881.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24355
     Region          12..>104
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdfntndpk iqriinaalk efslrgydea stnriakaag lskplmfhyv kskedlfwll
       61 vdycqktide dylkqmdfqe kdlfkrlrqs yvlqielmkk npwiidfsnk tfesksetin
      121 akltdrskqd cfhcknplfe qideskfrse ltvdqykqli ywgnigftte vlaelknvky
      181 eaidyqeitd kliqylenls rifyq
//
LOCUS       WP_010745935             333 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Enterococcus].
ACCESSION   WP_010745935
VERSION     WP_010745935.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..333
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37663
     Region          1..254
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 minlgiigtn witdqfvqaa hetgqyqlaa vysrrletaq kfgekygdve yatdlktffd
       61 iehlntvyia spnslhfeqa kqgilagknv ivekpafstp qemdeiiela nqkrvfffea
      121 arniheqsfk tvadflpykd riigadfsfm kyssrydqvl dgqepnifsp hfsggaladl
      181 gvypiyaala wfgmpkesiy fgqklstgvd gmgtgilrye nfdvtirtgk igdsfqqsei
      241 yltngtlvmn avnsiseavf hdrdhqrrek lnvhqlenpm veeanvfaqv ilnptdrklg
      301 tdyeewvela rnvnqviydm rksagivfda dkk
//
LOCUS       WP_010745976             365 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus raffinosus].
ACCESSION   WP_010745976
VERSION     WP_010745976.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..365
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41060
     Region          146..351
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mmgkysrlqv slysglisfl lilttlflym yaigkkqlfa qlfiarifyi plfvhiivia
       61 ltvsavvyfl vtfiekrqlg kiegklqsla sgnydqpsld vaisqnkeml lvdhdikrik
      121 eklvsmsrel qqlssqpqmv dgttkekile eerhrlarel hdsvsqqlfa ammmmsalne
      181 qsqhseelep ykkqlamvad iinaaqsemr alllhlrpis legkslrqgi eqllkelqtk
      241 iqiqlkwdvq dicvsasied qlfrvvqell sntlrhakan elevylkivg qnillrvidd
      301 gvgfeskdeh agsyglrnir eriagvggst kiisfkgqgt sieikvpvva dtsavadksl
      361 enqae
//
LOCUS       WP_010745989             144 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus raffinosus].
ACCESSION   WP_010745989
VERSION     WP_010745989.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..144
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16330
     Region          16..144
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mkilitkdtm sdiyldavri rqkvfvqeqg vpanleiden eaysvhfvly teeekpaatv
       61 rllplddqtf klqrmavlke yrgkklgaei iaesetfakq qgfktielga qltaeafyqk
      121 lgyvaygeif qdagidhvhm kkel
//
LOCUS       WP_010745990             374 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Enterococcus].
ACCESSION   WP_010745990
VERSION     WP_010745990.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..374
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41415
     Region          40..370
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mfekiknskl mfwsvellvi atlifvsski dfvfqpigtf fttlfapili agflyyllnp
       61 lvnllmkmgv krllaialif illigmivli fmsvipnlve qlvslaknip gfisnmqdwl
      121 qqaadnatrf plfkeldvdk yisnldvsag siiqqsltgv tnglgsligk ittvvlllvt
      181 vpfilfymlk dgeklvpnie rlfpekqrdn ikgllqqlnk tlsdyisgqa ieclfvgtft
      241 flgylligvd yaflfgviag ltnlipylgp ylglapaliy tffdsptkal lcilivlivq
      301 qvdgnviypn vigkslnihp ltiilillva gnlsgilgvf lgvpvyailr tvvifivkiv
      361 kqskqeereq efln
//
LOCUS       WP_010746042             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhomboid family intramembrane serine protease
            [Enterococcus].
ACCESSION   WP_010746042
VERSION     WP_010746042.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..220
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=24754
     Region          5..190
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mrkdrpyvmy tlfaintivf imqyllpgls ienqlgmfap sviwqhqywr fitpmfihfg
       61 lmhfalngvv lyymgqqcea ifghwrfaii yllsgvmgnf asfafnqptt lsggastaif
      121 glfgaflivg lhyrdngaiq altrqfalfi lmnlafglfd stidiwghlg giiggalsgw
      181 alavpysqdr fttrarvtav lffifaivlf vffglrkfsm
//
LOCUS       WP_010746045             133 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Enterococcus].
ACCESSION   WP_010746045
VERSION     WP_010746045.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..133
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15484
     Region          32..123
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 msiwwkiniv lisvlvlfgl yelvvrimmr rsakiitqee fqagmrkaqv vdvrerdefn
       61 akhilgarsf pfsmlketys slrkdqpiyl ydhnkavsar aanmlrkkgy kdlyilkggm
      121 qewtgkvkqk kid
//
LOCUS       WP_010746081             275 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010746081
VERSION     WP_010746081.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..275
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32125
     Region          13..116
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(14..16,30,48..50)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            51
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(62,65,69..70,79,89,93,99,103,106..107)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          123..268
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mdyecekiee klyrigmfsk mnqvtiktlr yydevgllrp rfidpdngyr yysssqlepl
       61 hrllalrrig ysieeikqvq dgvseqrilr rkkqqlmkei sermsmlsqi egylqqeees
      121 yhmvvkrlpe vivasmkkvi pnfeslssim pemgammeka gcvcampeyc fniyydneyk
      181 denigvevce avteqkedfg dlkfkvipev pmavctmhkg pytsipkafa aaikfteeng
      241 yeiidsiren yidgmwnkdn eddwlteiqi pvkki
//
LOCUS       WP_010746136             246 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus raffinosus].
ACCESSION   WP_010746136
VERSION     WP_010746136.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27038
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mqtiingidi iksfgegeek ntvlnhvniq vqsgqfvaim gpsgsgkstl lyaisgmdkv
       61 dsgkisvngr pidqmtekql aamrreelgf vfqqptllkn lslidniilp slkgkkqtaq
      121 qeqranslmk kvdiqelrer kitqvsggql qragicralm shpsiifgde ptgalnskaa
      181 qeimnillki neegttiviv thdmkvaaqs eqvffmedgq itdtlylggy nghsiearme
      241 ksmrky
//
LOCUS       WP_010746171             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010746171
VERSION     WP_010746171.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..254
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28396
     Region          7..254
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mknslinidk rqkeilellq qseqmttlel aqslgvsist irrdlnllee kndiirnygy
       61 csynydnktd fdqsgperik qaiareasky indydtlfin ssstalktld fihsnhltiv
      121 tnnvkvnysp hkdncsyilt ggemrfpkea lvgdialnti ssmnadvcvi gcsgvsvedg
      181 vttkilnest inemminktt rckilvadhr kigltskfki adisvfdyli tdqfcsqkgl
      241 seimnagvkv iqie
//
LOCUS       WP_010746184              68 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF378 domain-containing protein [Enterococcus].
ACCESSION   WP_010746184
VERSION     WP_010746184.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..68
                     /product="DUF378 domain-containing protein"
                     /calculated_mol_wt=7167
     Region          14..68
                     /region_name="YuzA"
                     /note="Uncharacterized membrane protein YuzA, DUF378
                     family [Function unknown]; COG2155"
                     /db_xref="CDD:441758"
ORIGIN      
        1 mkyldiiali llivgginwl lvglfeydlv aaisggstai lakiiyivvg icalyclkfi
       61 pgianrae
//
LOCUS       WP_010746191             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent rRNA methyltransferase
            [Enterococcus].
ACCESSION   WP_010746191
VERSION     WP_010746191.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..389
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=44162
     Region          2..389
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mkieltnygi kriqqgnpli qaedlkvnik kiplewvhfv dnknkyiatg ylgkqnkgfg
       61 wvidqtqrpi dqaffmekfq qaiakrqsff adetttafrl fngegdgvgg itidyyadyl
      121 viswynetih yfkkmivdsl lqvfpnakgv vekirfksel vesrwlagek pqeplivlen
      181 gvsyavylde gymtgifldq kevrgrlteg laagqkvlnm fsytgafsva aayggalett
      241 svdlaqrslp ktqeqfevng lplaqqkiiv mdtfdyfrya arknlsynli vldppsfarn
      301 kkktfsvakd ygrliedsvd ilteegmiia stnaanlplk kfkksietal nnknvsyrlt
      361 esyrlpadfp ashfeesnyl kvlfysikk
//
LOCUS       WP_010746298             166 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavodoxin family protein [Enterococcus].
ACCESSION   WP_010746298
VERSION     WP_010746298.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..166
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=17810
     Region          2..163
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mklaviyysk tgqtkemaei iaggmrktgs dvkafsvdes mdreylkess gvvfgsptyl
       61 atshwrlsqw lledssnlsl agklggafat ahyaqggsds tilsmlgill vkgmlvysgg
      121 safgkpfihh gpvaldavgd hyeeskaqfe ifgqrfaeka lelfea
//
LOCUS       WP_010746306             244 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010746306
VERSION     WP_010746306.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..244
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=27280
     Region          114..210
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 menhltrlkl yffyfviiig ylilpsiasa itgfssgavv tafsqvvfiv lsfmminryr
       61 lnkfwhfekl sgakmpplll llpaifpiaa dllfmrvgdf sfqklgisli tssltgitee
      121 fvfrgvllsg fllvyqskgi wkpimissfl fgavhflnll sttqvspklv ilqvvyatfl
      181 gvflasqflv sknlllpivt htlidlfsfv ehplngtqtv vflllygivp lifgvyflmr
      241 gksk
//
LOCUS       WP_010746299             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Cof-type HAD-IIB family hydrolase [Enterococcus].
ACCESSION   WP_010746299
VERSION     WP_010746299.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..268
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30206
     Region          4..264
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,194,216..218,220..221)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mkkliaidld gttlnqdski tdktartlrr aiqdghsvvi atgrpyrmsk nfyqelqltt
       61 pminfngalv hlpdkqwdge qetsfnrkiv fdlmaekknl kldfiaaenr etffiddlnf
      121 fdqhffasdf atnenlltvn tlrtnptsvl lrsqpenvgs vseelkqqyg hevevntwgg
      181 pnpilevvak giqkahglrr vidhlnmkqe dilafgdehn dvemlkfagw gvamangtdq
      241 vksvandvtd kpntedgmad yltkyldl
//
LOCUS       WP_010746410             281 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010746410
VERSION     WP_010746410.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..281
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31689
     Region          2..267
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrrskfswan iylifvfill yipifylify sfnqggnmst ftgftwehyq nlfsdrrlis
       61 ivvqtfvlaf lsallatiig tfgamgiyyt rkrnsrnvll glnnilmvsp dviigasfli
      121 lftmlggvlk nfqlgfvsvl lshiafsipi vvlmvlpklk emndsmidaa rdlgannfqv
      181 lsniilpflt pgiiagyfma ftyslddfav tffvtgngft tlsveiysra rqgisleina
      241 lstlvfifsl llvvgyyfis rdtskkarkr krefeevavl k
//
LOCUS       WP_010746431             287 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Cof-type HAD-IIB family hydrolase [Enterococcus].
ACCESSION   WP_010746431
VERSION     WP_010746431.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..287
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31439
     Region          4..283
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,214,236..238,240..241)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mikliasdmd gtllndqmqv ptanieairk aqaqgiefit atgrgmshak isldeanihv
       61 pmillngahv vnaeretift ipigkektfe vmdaleeadl yyeiftaehv yssnqpmrie
      121 ffsehilekm pgiskkmaia assrhlsltp itfvkdmrqt lieknedvlk iiafdkngpe
      181 qlkevtgvle kmgdlaiaas eltnieinhv naqkgialkq faeergftad qvmalgdnfn
      241 dvsmltyagt sfamgnaata ikkiakhvtd tneengvata idrilse
//
LOCUS       WP_010746444             186 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: histidine phosphatase family protein [Enterococcus].
ACCESSION   WP_010746444
VERSION     WP_010746444.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..186
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21270
     Region          2..169
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mlyvarhget ewnrkgiisg rsdislsevg ykqaeflaee vaalktpitk iihsplerar
       61 etarivaekn qllmnmderl ieldygdydg tsdksegylk frtqfavryp ngeslmdvya
      121 rivplleele qdsentyllv chnsviraik nyfeplenek vfnyrtpnak ligfdwkkva
      181 stiksa
//
LOCUS       WP_010746454             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010746454
VERSION     WP_010746454.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..283
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31653
     Region          1..279
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 msvlshmksm qkemsaaekk iycfirdnse kaasmtanei aeasgasapt vvrfskkmgf
       61 nsltdfkiel saetmqersn ntysdvdhde sfhslknkla snarytidet talfneeefl
      121 eactlleeke fcyvlgigas nlaatdivqk wsrlgkniis epdyntilpq lvlhqkeavi
      181 wlvsnsglts elialaetak dlgipiitlt qfgqnplakl sdvclqtsrp teatyrsaat
      241 dsilaqfiti dllfyvyisr nkenaekiyt traivqeyrk kyf
//
LOCUS       WP_010746461             444 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Enterococcus].
ACCESSION   WP_010746461
VERSION     WP_010746461.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..444
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48872
     Region          2..430
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 menklqkqmt srhimmlalg gaigaglfkg sgeaigiagp svilafllgg lvlfivmngl
       61 grlvlnsdnv qglsgiikpf lgdrtadfid wlywslwmvn iiaeavaaas fmqlwfphvp
      121 swifvlilai lttminlysv rlfaeteywl afikiaviii livfsaylva hevfnigfvd
      181 tisrmnshgg ftphglhglv ssllvviysy ggseliaitv setedpktai pkaikgvmgr
      241 iisfyivpmt llliiyrwdt lsattvspfv mvfqkmhipf atdivnfviv lalfssinsg
      301 vyassrtlyf rvkdndgfts klaalnkhqv pqravlfctg tlylgvilsy flgnklfnyl
      361 vgslsysvll twllisiaaf vlalkkgtrs erffsglvil vlglifigil mnnpigvtlf
      421 taciylvilf syrkkqtdpv seqi
//
LOCUS       WP_010746585             417 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010746585
VERSION     WP_010746585.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..417
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=44204
     Region          1..417
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdgfinfmek hfiphaskig nqrhliaird aftvtmplmi lgalavmlnn lpidafqnfm
       61 ngifggeawk gfggavwngt fgvlsvfiaf lvaynlahhy gkdpigtgvv svasfftlga
      121 atsgmnssgl fvalivgiav aeiftrlvgn eklvvkmpdg vppavarsfa slfpamitvs
      181 ifgliaavia gfgvedmfae fyalvqepfm glansygsal liafitpflw ffglhganmi
      241 dpfmqainap aieannaals agkaapyivn kpfidsfvnm ggtgvtigli iaiylvgrkn
      301 kpfmvvnnla aapgifnine plmfglplvl npimfipfil tpmvcvttay fatslgwvpa
      361 atvmppwvtp piiggflatq sfsgailaav nlvisivmyv pfvslatrqe lkkvaea
//
LOCUS       WP_010746646             399 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010746646
VERSION     WP_010746646.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..399
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43203
     Region          6..399
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkfyvnwrss lgsifknkkr saltmfgivi giaaviails igrgferdti esltasdsek
       61 levninfvps nqalyysnid miqasdfsil knvdgvesvs ypkndlsyiy kdvkvkdktk
      121 nyrvgvvskk gkavrygrti smydnqtqnk vvtidsalak elfgsakgav grgfelenqv
      181 ftiigvfpsg adetmfsmgs tkiqlprqty ihffgneqdk savvltladg sqlnkvadka
      241 ikklesagam rqqgeyqvsn mammtdgise vlnsitlfis avagislfia gvgvmnmmyi
      301 svsertkeig irralgatrg airmqflleg mtltlvggli gyllgmivay aignvmdisv
      361 tvdlftvcla vgvssgigli fsvmpaseaa kkdlidilr
//
LOCUS       WP_010746654             313 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Enterococcus].
ACCESSION   WP_010746654
VERSION     WP_010746654.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..313
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34902
     Region          1..313
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mvsayiniff ifvlmfigyv ltykqwfsnq igdafsklvl qialpcnmfl titknfsrse
       61 flhlvggmvi plismlltfl vsfiycrifr itparkgifs tmftcsntif iglpinlaif
      121 geqavpyvll yyivnttifw tlgiyfiard npqieqatvk fhlipilkki fspallgfll
      181 glcavlvnls vsdsiatflg ylanlttpls mfvigiivyn vgiknltlnr diigvlvgry
      241 visplivwll gqwisvpplm lsvfiiqaam pvqnsvpila rsygadqqfa asslgysvll
      301 ylayiplllk lil
//
LOCUS       WP_010746690             795 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: transglycosylase domain-containing protein
            [Enterococcus].
ACCESSION   WP_010746690
VERSION     WP_010746690.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..795
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=87502
     Region          34..686
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mahkkkinkq pkksskskar palggpfaln vslrvvksll lglivvlflg gmlvvgigag
       61 yfahlvegtp tptksemkqk vgdiaesskl lyadnqelat iqadpireki nsdeisqwvk
      121 kalvateden fyehhgvvpk avvrallgev vgfgagsggs tltqqlikqq vltnetsfkr
      181 kaneivlald lekylskdei ltaylnvspf grnnkgqnia gveeaaigif gvhakdlnlp
      241 qsafiaglpq spivyspytn tgdlkqdysl gmarkddvlf nmyreqmisk keyedakkyd
      301 lakdfqarqd vevqqhgfly ytvyneaini varqqakedg vsdadynked vqnryieqak
      361 vkmqnqglvv kstidkniyd amqlgvaeyg qylddgsgat vepgtvmmdn ktgriygfvg
      421 srdyntnqnn hafdtarqag ssikpvlvyg paidqgligs asriadfpmk yqhgenagke
      481 lgnaenkgsk tfqttrqalv estnitsyhv yqdlltnkgs dqfaydnylk kmnypssntw
      541 gvesaplgtt nvttltevng fqtlanggvy qqgylidsit dstgkeiykh keapvqvysk
      601 atasimndlm rsvineqhtt pfktilsgvn yqlstadwvg ktgttdnyad nwlivstpsi
      661 tlgtwtgrdd nkpmndgagn rtatymayla griyqvnpnv fgeneefels ddvkqikvsd
      721 ftglkpgkvs hdgtnyqvps geatslwakd gpgdntyefg iggtdddykt ywntrnkvna
      781 knkedkedee tktdd
//
LOCUS       WP_010746702             186 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010746702
VERSION     WP_010746702.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..186
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21334
     Region          7..131
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mktsrlnkei viacamdlvy esginglrln kiadrldvks pslythtgsv telrqavvrr
       61 amedfreqlv dsllgranlc afielgktwa dfaknknafy tvfyekeyid syeksiavfl
      121 raaferifse celtdkeilq vervmtnyfr ghadgftenn fnetdlisdl eiiyngilqn
      181 ftkvpq
//
LOCUS       WP_010746759              91 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_010746759
VERSION     WP_010746759.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 91)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..91
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10202
     Region          1..88
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 meikeekerf vllndaneea gemtwsnags eimiidhtfv dptyrgqgla eklvaagvek
       61 arnegkkiip lcpfakkefe ekseyadvlr k
//
LOCUS       WP_010746767             169 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010746767
VERSION     WP_010746767.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..169
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19745
     Region          9..>100
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvrtqrvqrs hiidgayqli inegfkkfha rniakhiacs tqpiyreftn laelksvltn
       61 riivkyqdfi edqepktlka lstaimnyat dypdefhrff lqdsdtiqmv kqvtketfss
      121 lqpnrsdslf feffwqycig kaalatndan htedleedqf fqyslensh
//
LOCUS       WP_010746768              66 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Enterococcus].
ACCESSION   WP_010746768
VERSION     WP_010746768.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7139
     Region          1..65
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mengtvkwfn aekgfgfitr edgsdvfvhf saiqgdgfkt leegqavtfd veesdrgpqa
       61 anvvkq
//
LOCUS       WP_010746799             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010746799
VERSION     WP_010746799.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..243
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27967
     Region          10..242
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mensfknkal yhqlvdllke rmetgmiphd klpserelta qygvsrttvr lalqelestg
       61 yiyrrhgkgt fvsdikkeaa dlaaaysfte qmkslgrnpe trilsfekve adkfisqhln
      121 lslgesvfkl srlriadrep lmiedtylpv kfflsltdql lrskplydlf sedfdqtvrl
      181 adeelyasia skddakqlmi pegapvlhla rqtynmknei ieftlsvara dqfhyqirhi
      241 rns
//
LOCUS       WP_010746810             327 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Enterococcus].
ACCESSION   WP_010746810
VERSION     WP_010746810.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..327
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36176
     Region          4..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meifditivg agpvgmfaaf yagirqaktk lidslpqlgg qlttlypekn iydipgfpiv
       61 kaadlignle kqlrtfshty cldeevlevk qhedflelvt tkdshytkav vlaigngsfq
      121 prrlmidnad slenhgidyy indlmkyagk kvaiagggds aidwalmlep iasevsiihr
      181 rdnfrghehs vqklkdssvn iytpyilkel hgeqnledlt lqktksdeti tlnvdylivn
      241 ygfsssldhl rswglestrq ailvesdmrt sipgiyacgd iatydgkvkl iatgmgeapt
      301 avnnalhyin pknrtqpghs tslfpqi
//
LOCUS       WP_010746827             475 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus raffinosus].
ACCESSION   WP_010746827
VERSION     WP_010746827.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52131
     Region          21..469
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,146,
                     149..150,153,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mktyqddpvv qknrwwilvs vamftfmstl dssivnialp tiskdlvvpm nkaewvvsiy
       61 lmivcaclll fgkvgdsfgk ikvyrigtiv ftlgsllcgf nhsltmllfg rviqgigasm
      121 tmatntgitt evfpmeergr algaigafvs lgsiagpgig glilahfsws yifwinvpvg
      181 iltiligekf lpkdltmskk kidwlgfatf altimsffga vfigqevgyi htlpvlllva
      241 aiiffilfiq vekrkenpll vfsilknkmf tmslitalli fsanffvnvv mpfylqnarg
      301 ltasyagllm mvfpflmvig splsgyltdk igpqklvlig ltllsitqll yvfmsqsspi
      361 wyyvlataim gmgnalfqsp nntivmssve kenlgvagsm nsfarnlgmv igialsttil
      421 yggmstaygq rvttyvndrp difiygmrvt fiaslvicaf almislvrfr kkplt
//
LOCUS       WP_010746829             560 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease J [Enterococcus].
ACCESSION   WP_010746829
VERSION     WP_010746829.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..560
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=62369
     Region          1..551
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mstvkiipfs gvrengknmy avevdndifv ldcglkypen ellgidvvip dftylienad
       61 rvagvflthg hadaigalpy lvsevavpvf gteltielak lnvsqneesk gfkdfhvide
      121 hteidfgtav isffrtthti pdsvgislkt degnvvytgd fkfdptaipm yatnyrrlae
      181 igsegvlall ssssnaenai qvasereias evydvinewn griivacvas nlqrvqqiln
      241 aaekagrkvv ltgqdldrii ktamrlkkle vpedilvtik emkkypaeel iiletgrmge
      301 pikslqkman rshrnlkied gdlvyitttp tiamettvak tedmiyragg ivksisenlr
      361 vsghanprdl qmmmnfmspk yfipvqgeyr qlaahaslan elgmpfkdif itgrgdvley
      421 knkhmsaags vpadnimidg igvgdigniv lrdrkvlsdd gifvvvvtid rkqkkivsap
      481 qitsrgfvyi kasrdlikes adttseivek hlhsddfews klkqdirdql srylfeqtkr
      541 rpvilpvime anqrrgrrnk
//
LOCUS       WP_010746851              99 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Enterococcus].
ACCESSION   WP_010746851
VERSION     WP_010746851.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..99
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=10905
     Region          1..93
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mtssitmrdf yqlanhkele iidvresyey qmghvphakn lplsslsssm telddskdyy
       61 licqsgarse nacaflagqs ynvinvlggt aawpgelvr
//
LOCUS       WP_010746871             291 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Enterococcus].
ACCESSION   WP_010746871
VERSION     WP_010746871.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..291
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=31302
     Region          <3..150
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; cl46157"
                     /db_xref="CDD:480497"
     Region          <100..285
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; cl46157"
                     /db_xref="CDD:480497"
ORIGIN      
        1 maqiifyvli glmifqaiml vrdvvthred lgpgnwling iigfiadfad tigigsfalt
       61 tmmlnvtkqn dddrklpgil nvghaipvlt eavifvtvik vdsltlvsli laaivgswfg
      121 skyvtklset avqkwigwal litailmllr qteviallgk gntamgltgi klivgiignf
      181 ffgalmtvgv glyapcmamv ymlgmtplaa fpimmcscag lqpvasinfi rekaysrkia
      241 laitiggipg viiasqflmn ldismvtylv iviifytgiq yilksrktat a
//
LOCUS       WP_010746925             441 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010746925
VERSION     WP_010746925.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..441
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=48557
     Region          4..420
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mfakfeafmn rffvplahkv dnqrhlsaik agmvamtpft ilgsffailp alpnmlgesn
       61 gfsqfilnna elfnlpvtls tgliglyaca aisynlgnhy klyipgavtl slfgflfmta
      121 mfdenglldi anfgakglft smfvalitve lynfckkrnl tirmpegvpd fvsksfelip
      181 vtlivggtfi igrfalmqta gelpptiltr flsplvgsmd npwsvlalnf ciclifffgi
      241 hssvfspitr pimvafiaen isafqagepi phfytagtss affgftgcgi sigcivacmv
      301 skskryrkig kvslfpalfg inepilfgap iilnplmfip hvfggaligt lpmffmhwgl
      361 lnkpifdppy vgvflegflt ngdwrtilvn alqlvlavai yvpffkvmer nelrdeakkk
      421 eqknifdqgd tdildgldld f
//
LOCUS       WP_010746862             324 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methionine ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010746862
VERSION     WP_010746862.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..324
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35858
     Region          3..304
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 meividqink rygeqtiled isltipsgti mgilgisgag kstllrcing leqsesgsir
       61 igtqalekls ekqlremkkk igmifqgnsl ieqktiyknv alplecsgys ketikarvee
      121 lltevgiadk ahmkprqlsg gqkqraaiar altmnpeill cdeatsaldp nitngildll
      181 lklnqkmglt ivvvthqmev vkkicdrvai lqkgkiveed tvqqvflnns nvlqtitges
      241 pinfsegkig yrivkivtkl ekdilvlwrq agieaphllk atteqfkeet lttlfvsvpd
      301 adsekllkla dqdhflyqev kfse
//
LOCUS       WP_010746939             715 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-dependent helicase [Enterococcus].
ACCESSION   WP_010746939
VERSION     WP_010746939.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..715
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82553
     Region          41..713
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mftklsnyik sdlieaerdt lddkdtlqql iaqnnghsfs edqlaairfp mqthlriiag
       61 agsgktqtic akaaylvlek svdpkaimmc tfsrkaklem earvnhylgg farvkvqtfh
      121 gwfnaeynel lrknpdlkqw giegqinedq yyqvvnhlik kyrlynfdkl edrtiasris
      181 ywrnmgysdq emvgfvakyf dgqelllnqk lsevfqqflt elaltkktqh fitfddmlfn
      241 lklilendrt aqqtlqekyr yifidefqdi nplqkqival icppdkevmq knsskliivg
      301 dddqsiyyfr gaepsyikdf eqehkqtslk lmtnyrsdap iveagnrlir fnahdrlekt
      361 mtaskktiah dcygigfpdd edeaawigqk iqklaneapl kdgspdyrdt mvlyptrvql
      421 rsllkqlkky kvpfvtpsnd dllgifglpl fktlfqqlem lasataiqqk ndalkkiiqq
      481 yaffhfikfn ssakfsdelf sknkfkindl vaflvsernl spssqdhakv ffkemyffyq
      541 qgrlnltala dallatpkfk kdlseeeadw lhkelsaagd wpglleafqq asqqnegmkk
      601 rlrvydqekl navyllsiha skglgkknif ikgvyqdalp nhhtvkkadc dlqkareega
      661 ppttleeqrr lmyvaitrak enlyvtypkt vnnktiepsp flkeaglplk eyrkk
//
LOCUS       WP_010747038             672 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus raffinosus].
ACCESSION   WP_010747038
VERSION     WP_010747038.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..672
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=77155
     Region          9..667
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mlskretqil kllfdhrhty ltsqeiasgi dvsnrtarky lhlledalkk eavatidakq
       61 gngyqlkied skkfdvfyln evkeqstskd ittiqesndr qyyilnrlff eqsavyvdai
      121 adelfvsrst isndlveikk litpyqielq sksnkgifvv gneqnirhfi mnyffmdrlh
      181 dnlfafsmya nllegisvee iviivldecr esqlklsdfi vynlvlhigl aikriqngfl
      241 mdiqapiafd edsieyqtal kilarieqam gltfsseead fialhlknki taktifqkad
      301 ateaeirsql letlkaidqd tpfdlehdti lidglmihfi plltrlqnns sienplleei
      361 ksqypdlyel tvnyfskmpi fssyrmtege waylaihita averyfndqk thvlvicatg
      421 lgssqmiknr lerefgsril iekvisyyei aeqdlsqidl vissinlgni vlnapivnvs
      481 vflgeedikk inheisstkg ghfntceenk qvemveekve likrsfqsel fyfadkrltk
      541 etvlkeligk ieaveqndlq esflnqlklr esyssvvfse fmavphpiea ltnegyvava
      601 vvpegidwse eyqkiqlvfl lspdklgkfe idkvsqmlve imeddsfrka lafsdtfdnf
      661 ikafidqfek ts
//
LOCUS       WP_010747121             345 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Enterococcus].
ACCESSION   WP_010747121
VERSION     WP_010747121.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..345
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38537
     Region          201..327
                     /region_name="FUSC_2"
                     /note="Fusaric acid resistance protein-like; pfam13515"
                     /db_xref="CDD:433273"
ORIGIN      
        1 mehsffkeli hynkpkespl rligaglcmi silftgyllh qltissfgsl giftflyyqr
       61 lplkqlmirl aivgsfltvg nflgmlstha awtapivvai vgflgrfffr lygiakpgpf
      121 fivmvtamga stkiplhrip tmssflllgv lfslgfafll hlvekepspa aserlktvke
      181 rinddpavvi dsllysgflf favylsmglq lknpywlvvs casilqgdnl ramahrnvqr
      241 ifgtiiglai aafllnlpls vfetlliita lfvtveyfvk rnyaiaqffs tpmalmlsml
      301 arqqylnsli qfrflgivig sllgllagwl mstslefynr kfhsn
//
LOCUS       WP_010747122             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Cof-type HAD-IIB family hydrolase [Enterococcus].
ACCESSION   WP_010747122
VERSION     WP_010747122.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..269
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30220
     Region          4..265
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,196,218..220,222..223)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 myrliacdld etlldksrhv skrtqetikm aeaqglvfap atgrgfysik qtleeldaan
       61 kknhymigfn ggvvvenhgp tiikdfpmpf eilaqlfefg snydvaihly tfdqtyvyhs
      121 npeedayltt iphekrldde isflkdqvcy kalfqnldrs ylerleqemp kplhdvleis
      181 yssnryiefn pkgvskgval qtladhleip mketiaigdn tndlamihaa elgiavanav
      241 pavkeaaqht tiadheqsvv aevietfil
//
LOCUS       WP_010747167             123 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system PemK/MazF family toxin
            [Enterococcus].
ACCESSION   WP_010747167
VERSION     WP_010747167.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..123
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=13205
     Region          1..112
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mvkrgdiyfa dlspvigseq ggirpvlviq nnlgnhfspt iiiaaitakm akpklpthig
       61 iksngtgier dsvilleqir tidksrlkek vchldrclma evdaalrisv gietmsavts
      121 nlt
//
LOCUS       WP_010747238             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: transketolase family protein [Enterococcus].
ACCESSION   WP_010747238
VERSION     WP_010747238.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..316
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33945
     Region          12..312
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mftlaenhev gkelratvvd alkaamsvde kiialdadlg gaskwtelaq stperfinvg
       61 iaeanmvgva aglsltgytp fihtfgpfat rrvldqiyls gayadntini ygsdpgftag
      121 hnggthttwe dvallrsipe viicdaadev qmdwiikefa rlkgvhyvrg nrkgvkniya
      181 pgstfklgkg nvlregqdyl ivatgqlvse alevanalea kgesvevidm ftikpldkel
      241 llerfigkkv vitienhsit gglgsavaev ladnglaipl krvgvderfg qvgtpaflqe
      301 efgltttkil eqlnsl
//
LOCUS       WP_010747127             367 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010747127
VERSION     WP_010747127.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..367
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41119
     Region          1..366
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mvelnlkhin kkypnnnays vknfnlhikt hefivfvgps gcgksttlrm iagleditdg
       61 dfeingirmn dtppkdrdia mvfqnyalyp hmtvfenmaf glklrkypkd dikqrveeaa
      121 kilgltelld rkpadmsggq rqrvamgrai vrdakvflmd eplsnldakl rvqmraeiak
      181 ihqnlgstti yvthdqteam tladrivimn egviqqvgsp qelynrpank fvagfmgspa
      241 mnffevtfkn gritnhkgld lplpegqvkt ltgqgyegkt vtfgirpedi taeevaleay
      301 ensvvsatvv vsellgyesm lystigntef iskvdardfh npgeqiclaf nlnkarffdf
      361 eteeaiy
//
LOCUS       WP_010747247             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010747247
VERSION     WP_010747247.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..239
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26852
     Region          1..220
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mepiikasdi tknygqqevl kginlainyg dftcimgrsg cgkttllkil glmhppttga
       61 vmfekrathe lfpdeisdir rrkigfvfqd fnlmesitvk enillpaild kqdtkkaeer
      121 mnpffkilri ehllaklphe lsigekqraa icralmnepq iiiadeptgn ldsnagaevi
      181 kifqrinqel eitivmithd skvaqaanei iflkdgqiyd rfsnrvgses qiaekmlev
//
LOCUS       WP_010747314             121 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus raffinosus].
ACCESSION   WP_010747314
VERSION     WP_010747314.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         1..121
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14375
     Region          2..113
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(3..5,19,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(49,52,56..57,66,84,88,94,98,101..102)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mykisevskm igfsvptlry yeelgisapa knksgyreys eadvewlrfi hrlkhtgmdl
       61 esikkysqlr sqgdqtiekr mkllatqrnr lltekrkieq hltfleekqk tykemladrd
      121 r
//
LOCUS       WP_010747345             647 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Enterococcus].
ACCESSION   WP_010747345
VERSION     WP_010747345.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..647
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74698
     Region          19..629
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mektmrrrnq llslllsesd ykttdyfsek levstrtiln dvnflnkela gkaieivkvp
       61 rhgikligte geinritdlt vesdrdiydv lgrregifrq lfmtpegqll etleadffis
      121 dstlkkdldy lqrylrhfdv kicqsrrkvs lrgaeadiqq ayqnflmtkf pdallvnnee
      181 lliqlenyfp valiqlvkdt lekfsdmfys nisnkyfsai fltflclltr aengchmtie
      241 ekkksdledl alytqtyeic afistnssie lwypdiyhls etlyamnvkp fykstktynd
      301 syqeaveeli adlgnllnid fsgdqelhds lmshivpmiy rlrrnilikn pfmediknry
      361 lllysmmcya issigqrfsi evtgdeisfl viyfqvaler kygvsfrniy vvlsrglits
      421 dliytkirri iphtdkviql ttkefeqvtl nsrdvvvttd psvkatnvvy ispmikdeei
      481 srivhtyykr yhatakektq vnqqwinpel vflqqhvenk eaclnfmier yqalgiaken
      541 fgesvwtrek lgdtsfsvsv aiphadpsev nqtsigimtl dkkinwginn vnvilffais
      601 dtdinaaksk itgllefiek eenvekliqv tdkqalldlv mgegsai
//
LOCUS       WP_010747350             618 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Enterococcus].
ACCESSION   WP_010747350
VERSION     WP_010747350.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..618
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=71638
     Region          10..615
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnisqrqeki leklslnqqp stagqlskel gvssktirnd iqqlnqlseq pmilskagtg
       61 fyinpennhl qqlasdkqst nltfdllmrl ldqkacdfye ladeffises tldrmvkeln
      121 rliakrdqrl iikrkqnrll iegdeaakrr vftlflnqei etnklsldny sdyfeqidla
      181 kltkvvinvh qkegffvndf stisfilhla vllervskks ylnpsqaslk etksrqmtla
      241 mvkeletnfe vkipeeeyay iyrlysgslv sdedladkkl kqaiegvltn idsiffidft
      301 qdkkitdyll thvsalykra thkqylvnpl leeikskfpf vynvsvyasg ylqeklsiqf
      361 pedevaylsl hflsalenir ahkkkrvllv spygvgnqri vrnqlnkiqe feielfvaes
      421 ifavtnette ekslilttek lnlpttvpvy qydsfltdad lkkiqnllie enqspsvltt
      481 flkeelffpq etftdrdevi rflcqelykk gyceknyvek vlqrealsst afgdfyalph
      541 aikreakqna vaicslekpl qwkekkvrlv lllalkeerd nsfeqlfeel vkmlndaarv
      601 kklsrqtsfq efmaicqn
//
LOCUS       WP_010747364             320 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar-binding transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010747364
VERSION     WP_010747364.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..320
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35397
     Region          11..313
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 maikhnrdiv kvatmyykks lkqseiakrl gisrslvsky lndaknegiv difiksesay
       61 sielelalee tfglkkaavl dtsslrkdev erllvqtait afqkeiakak tiglswgkml
      121 rgivdeypye nhadatiipl igglgsemvd vhsnqlaydl skklrakcky lyapalvdna
      181 fikksliend gihdvleagk nvdfalvgia spfsknntmt eigyvdqqdi delekldvig
      241 dvnskfidqa grevaceine nviglgvedv rkianvavac yedskkdvly vgtktkifth
      301 itvtdslaey lleqakneth
//
LOCUS       WP_010747363             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Enterococcus].
ACCESSION   WP_010747363
VERSION     WP_010747363.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..308
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34678
     Region          59..306
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mnkstkiilg iililvivli aagnyfysya vvpakkdfla sgsekksaer iraedwfndk
       61 nnrsdwqlts ndglklsayy lpakkeqhkt aiiahgymgq atdmpqyaki yhdlgynvlm
      121 pdarghgkse gdyigfgwde rkdylqwinr iikkdpqsei vlhgvsmgaa tvmmtsgekl
      181 pdnvkafved cgyssvkgel gyqlkemfnl pafplipvts lvtkvragyf fgeadtikql
      241 kkntrpmlfi hgdkddfvpy fmldevykat kgpkeqyvvh gakhaealss npsmyqkkvt
      301 efiqkyvp
//
LOCUS       WP_010747400             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ZIP family metal transporter [Enterococcus].
ACCESSION   WP_010747400
VERSION     WP_010747400.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..272
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28627
     Region          10..270
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mvewilslav wqqalvgtlf twgmtalgaa lvfffkninr nvlnlmlgfa sgvmiaasfw
       61 slldpaieaa eengsipwlv vslgfglggl flyladktip hmhfgpnkek egfpshlkrt
      121 illvfsitlh nipeglavgv afgaaneaan ptaavlaais vslgigiqnf pegaavsipl
      181 rqeglsrtks flygqasglv epiaavigal lvtsvepllp yalsfaagam iyvvveelip
      241 eaqattdskh hygvfgamsg fiimmildva lg
//
LOCUS       WP_010747404             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Enterococcus].
ACCESSION   WP_010747404
VERSION     WP_010747404.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..321
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34604
     Region          3..321
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 miffqsiqsv lsiiimialg yilkgqgwfd dsfgksissl itrvalpasi fvsvlknltk
       61 eslfqlsgsl iypvgaviis yilayalvki lkirpgrrgi fmnavvnant ifiglplnia
      121 lfgekslpyf lvyyvtntvs twafgvflis nddptkvkge nkaklnwkkl lpppllgfiv
      181 aiifllvgip vpsfinatlg yvgsivtpls llyigivlyd aglksirfdr dtivallgrf
      241 vlapavlval ialgsnafga slapllkqtl ivqsatpmla vlpilaneah gdvkyatnlv
      301 ttstvlfviv vpilmelvqf i
//
LOCUS       WP_010747436             488 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MDR family MFS transporter [Enterococcus].
ACCESSION   WP_010747436
VERSION     WP_010747436.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..488
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52185
     Region          23..477
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,279,282..283,286..288,291,319,323,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 msnnqtvdiy gkpynrsllv vvlligtfct vlnqtlltta fpalmkafdi sassvqwltt
       61 gfllvngimi pisawlinkf sskklylsam tifligtitc fvapnfstll igrliqaagv
      121 gismpllqni mlsifppekr gsamgmagiv iglapalgpt lsgwiidhyt wrdlfgmvip
      181 ivilvlvlat flmksviqls npsidilsal lstigfgsll ygfssvgndg wgsvkvigfl
      241 vvgviviglf vwrqlhlehp flelrvfksp iftiaailsg vvnmamvgae mvlplyiqni
      301 rgesafhsgl mllpgalvmg lmmpitgsif dkygakrlai sgmliltaat lpfafltset
      361 piamivilya mrmfgismvm mpvttsgmna lpmnlishgt avnntfrqva ssigtailis
      421 vltnvtkgnl paahllktlp ltyknqaisa tlsgyhaafy vavifgvigf iitfflkant
      481 kaeggvak
//
LOCUS       WP_010747605             188 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF1836 domain-containing protein [Enterococcus].
ACCESSION   WP_010747605
VERSION     WP_010747605.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10556141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..188
                     /product="DUF1836 domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21385
     Region          21..121
                     /region_name="DUF1836"
                     /note="Domain of unknown function (DUF1836); pfam08876"
                     /db_xref="CDD:430279"
ORIGIN      
        1 meklqadmkn wgnsllkfhl prweelptle lymdqvitli dqylspviqt ekhplltssm
       61 vnnyvkkgmi papekkrynq khlafliait mlkqvltipe iktgilfqgk vvgirnaynv
      121 fceeqekaih lvgkeamgep eqmtsepipi elvamkgatr sfankllaek tieleviyle
      181 thkgeahe
//
LOCUS       WP_010747604             405 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus casseliflavus].
ACCESSION   WP_010747604
VERSION     WP_010747604.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..405
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47448
     Region          89..397
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mlfsvlggfe lklranivek rgtlqvvvti kddfgktsqr wrdtklkkkg nkkraerikd
       61 qfiseieqei amkqedylvl kqertetpfv dylysyleta kpqlsktsyf sykryidiri
      121 kdyfgpsgim lsdlkpvhlq rfyqkilddg ctgntalhyh afvrkalqea fmteqidkni
      181 adrvrrpkkd sfvpnfytkd dvlkllqifk geklypiill tvfygfrrse vlglkwdaid
      241 fvnktitikh vvlenkedlt tvlkedrtkn assyrsvpli etveeelvkl arwkeknkkl
      301 fgaeynyedd dylftmengn iirpdfvskr fakvikrnni krirfhdlrh ttasimigng
      361 ehmkkvqewl ghasytttan lyahldpsfk yasaenlant fgfkk
//
LOCUS       WP_010747610             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010747610
VERSION     WP_010747610.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..245
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27648
     Region          4..244
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mfdeekikrl nelemavyky ivqhfeeidq ltirelsaac hvststilrc itklgyrgys
       61 elkyaicqkk eqdarafdlf ydatiqvntf lkkvnnedyr kfiqpaveli lsarhvafsg
      121 igtsgilgty gsryfanlgi naysivdpfl pvpprgment laiilsvsge tiqmikqted
      181 fkrygakvls itndekstia qmadynisyy mpvvsggkev dlnlttqvpv itliellahq
      241 vykqi
//
LOCUS       WP_010747680             525 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010747680
VERSION     WP_010747680.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..525
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61672
     Region          5..123
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          <315..519
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mklkelvelp lfekskvltg sigltnsvgs vmvleamdie kwskahqlil tsfyafkdqs
       61 peelrvffek mqqigvsglv ikvdrlipmi pdwvielsfa yqiplikvqq evsyeaimla
      121 vyepllnhqt qllrtyyevr qrfmkvernh ssfdqimqef yqliekpcsl riphldvhvs
      181 vgqsfknfvv tkqepmktie ftknhyeyle lfshennqyv taikveiinp yndlctlivy
      241 qkdsqipeak vmiienvidv iyerlqmeyl lkkerynrmn nladailqnt psnlaeldll
      301 leeaqldryd fyqgiafasn sfkdkerksv vlhklralkt phvffehhny lvilynfqsi
      361 ahqvtkqmlq thfdnallad ehgclvvsev lrkeqikeil pecldairfn rqfylapiia
      421 ysdlgifssf ikenqleklq qsippklyql seeneelfkt lytffitnrn ykntaetlfl
      481 haktiryrls kieqlleidl tspiqlvnye igtyllelqk rsqak
//
LOCUS       WP_010747683             405 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dicarboxylate/amino acid:cation symporter
            [Enterococcus].
ACCESSION   WP_010747683
VERSION     WP_010747683.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..405
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43159
     Region          4..405
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkakklpmvt qiviavllgi lcglffgqaa sflkilgdlf lrlmqmaipl livgqiiqav
       61 ggiapkeltr lggktiavfg isslfaaawg vlmalffapg kgidfsqaag eplqaqeisi
      121 setvinfipt nifdalskgs iiqiivfglf fgvalnrfvq kkpesalygl ivdlnevvia
      181 iiryvmivap igifaliast isslglqiil plgsyllvyg latvtflglw lvlltvycri
      241 nplrliknmk nmsvmalatt ssaitlpiam eesqnklgls sritnlvlpl gmslnsngsa
      301 mhmaitvmti aqmyqinfdg iqmvtvavta tfvslanavv pgaglvslai ivpqlglpie
      361 sialfagvew fvgmlrtiln vnsdvysall iaksadeldh rvfnq
//
LOCUS       WP_010747699             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADPH-dependent F420 reductase [Enterococcus].
ACCESSION   WP_010747699
VERSION     WP_010747699.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..238
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25197
     Region          5..209
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mpktigilga gklglalanl gaqagyrvli astkpaekia lsvsvlapga iaknavevmt
       61 eaqtillaip lskyqqlpae alagklvida mnywwevdgk eteyssieqt sservqryfs
      121 qskvvkgfnh mgyhdiqees lltrtaaqgt akkaiaiagd dqtaldqiae ivaafgfdpf
      181 pigalangim lepgspffga nqtkegltal mkafwssekg qaflarpsav snkqqvpq
//
LOCUS       WP_010747694             534 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amidohydrolase [Enterococcus].
ACCESSION   WP_010747694
VERSION     WP_010747694.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..534
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58623
     Region          23..534
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mslllksehi fdtktkttfa gflliedqki tavgplsalp tlaedtqvid lkeqmiipgf
       61 idahvhfyls allhqgalth ltgvteeava qqvpalpith gwkigigwfs sdfgqqvypt
      121 kdsidnycad tpvmlisgda hsiwlnsqgi aalgitpenl pagisgeall densgqlsgc
      181 fleaiaihyl akvlqsfqaq spaafltymk qlnqygitti gdvaltgesw ddlvyptlyr
      241 qteaeatlra vfypamredi tqlkktyrty rsekvqmggv kqffdgvtst htaflkeeye
      301 tpyfagdvgm plidvqrmrr filqanqqdw pmrihtigde airqallfyq esaaahplsk
      361 gkantlehle vmdaadlplv rqeqlvlsvq pshllvgyet ldeevgpqra sqmfpfqsfl
      421 eqgatlafgt dtpvvidvtp ldslyyavar qekngqpagg lmpqekisia dalyahtaga
      481 akalsrqdig rlevgcladl cilsqnilpl taeellqttv eatvfdgqfv yrgn
//
LOCUS       WP_010747719             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010747719
VERSION     WP_010747719.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..135
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15526
     Region          1..>104
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdiideqila ilkhnsklsn keigemvhlt gqavgnrilk lqdegiiqrf sivvnypstq
       61 yirffmdsnr ytdfeafvnq ykeievfhkv sgqacyllvs hftdvtfplf ieslskwgry
      121 svetfvadkl nhgdd
//
LOCUS       WP_010747740             420 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010747740
VERSION     WP_010747740.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..420
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=45148
     Region          1..408
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mnrliegfqe nfapklvris enrflvavrn gvavtmplti igslflilan lpfpgwtefv
       61 gefgvklgaa snftfgilgl aacigiayyl aasyeidrig svvlavcafl llqageewti
      121 dpaslgasgl ftgivtaiat vvihrfflkh rlvirmpaev ppavaksfsv llpgaaiitg
      181 awvirvllef nvnqfvqaif splavglntl pgmllytfli lllwclgihg snvmgsigdp
      241 iflallaant eaytageplp nifaggfyim flcyggtgst lgliinmlvs kkkayrslgk
      301 malpsaifci nepiifgfpi vmnpimmipf iltplvlcvg tyflsvtnvi grimfnppwt
      361 tppfintyla tggnipavlw siasllisva iyypffkise rslteeekgv tdavaakgen
//
LOCUS       WP_010747742             325 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [Enterococcus].
ACCESSION   WP_010747742
VERSION     WP_010747742.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..325
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35125
     Region          9..309
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mkktilasil alfavgaaac gntgetasts nsstssteaa vtdqpltigv lpaesaipii
       61 lakeegffek qgltvelksf tspndrnvav qageldgtis dvmteatfkq ngidmtitsd
      121 ilenfkilas pnsgitemkg ladkkitlvp nfileyimdq faqendftyd ivdiasfsar
      181 seallndqvd gavytepqas mlaaqgaivl gsskdagikg gtlqfmdevi qnrpqdlkaf
      241 ytayneaidy mnahsakdya diladyqfpd amstyldsqe dypyaqavpq eqfdaiiawt
      301 kdkgqidqay syneltnfdf lpade
//
LOCUS       WP_010747781             582 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus casseliflavus].
ACCESSION   WP_010747781
VERSION     WP_010747781.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 582)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..582
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=66813
     Region          185..569
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mtkqrfrlfk hdflinqlmq lysvllviis iiimlvltay tgadrfnsse rlveatsmql
       61 dayvqdqnav vsavlgelts sdtafeslrn ylqlslpdyf sysndifrqt gqsvylpnil
      121 yrlirnhpsi eeiiiqldes netlvatpdt pygekrsgkq idlknrlffv rsiaqpsnya
      181 qplgqvyvif hsddvlanrq ednqahgins flytsngqrl ykdaanlskq tlakidqava
      241 hgtihdtlsk dfyikkqttv sgelslills kgviwrdifs saiwifsfgi gilllvlwvl
      301 hrtfkrytsq vqqivyatke vsqgnfdkri dtanvqqelk eiaeainqmt ysineyikdi
      361 ytleikqrda dmralqaqin phflyntley irmyalsrnq eeladvvyaf sallrnnttq
      421 ektktlkeei dfcekyvylf qmrypdkiay hvtidsaleq lelpkftlqp lvenyfvhgi
      481 dyqrndnais ikaykeveqi vievkdngkg adaqqlamiq eelqnqeiga qtsigiknvh
      541 erlrgmfnga yqmdvtsqag agftvkirld ekrlqrghet dv
//
LOCUS       WP_010747783             443 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Enterococcus].
ACCESSION   WP_010747783
VERSION     WP_010747783.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..443
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47040
     Region          1..443
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mksqlkkeis ffgalstvmg tvigagvffk aaavvqqtqs tgltllvwll agflticggl
       61 tvaelataip etggpiryie riygklpsfl lgwaqsiiyf panvaalsii fatqclnlfh
      121 lpsnyllpls iltgtsvtli nllgtkaaaq vqsvtlavkl ipiaviivag lltpgqvsvs
      181 lvdfssntqg slaagissal latlfaydgw mgvgnvagem krpekdlpka iifglsfvtl
      241 vyvlinvafl ktlpidqiag nlnsasetam alfgsfggkl vtigilisvy galngytmtg
      301 lrvpyamale deipfsktfa tlskttnapy aaaflqlgia cimmllgtfd lltdmlvfvm
      361 wffsvllfvg vfrlrktepq mkrpykvpfy piipliailg gcfilimtli tdtwlavvgi
      421 gvtllgipvf ygkakgkarg ake
//
LOCUS       WP_010747806             276 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Enterococcus].
ACCESSION   WP_010747806
VERSION     WP_010747806.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..276
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29907
     Region          1..275
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkrnvvnvlt tgviglfalf slaacgtnqa deettvvklg vvgeqneawe hvqeelkene
       61 nidlqlvkfi dyrqpivale dgsidlhaal teifmdnvne esgysnttia yttlnplgiy
      121 sdkitdvsel adgatvalpn dvsnesrall llqtaglitl deskgllptt sdvtenpkal
      181 kfelldsnqt aramtdvdis linngmavda glvptedaif lepvadsstp yynviaarad
      241 eaendvyqtv vayyqtdevk aiidevtkks sipvwe
//
LOCUS       WP_010747845              90 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_010747845
VERSION     WP_010747845.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 90)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 90)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..90
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10308
     Region          1..87
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 meileentrf vlkdgdkeig emtwseaget rliidhtfvd payrgqglae klvakgveka
       61 rkeqkkiipl cpfakkefer kpeyadvwnq
//
LOCUS       WP_010747864             255 aa            linear   BCT 01-JAN-2025
DEFINITION  putative ABC transporter permease [Enterococcus casseliflavus].
ACCESSION   WP_010747864
VERSION     WP_010747864.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..255
                     /product="putative ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30063
     Region          8..185
                     /region_name="COG4905"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443933"
ORIGIN      
        1 mvqfewiill fflysfigwl wetiycslka khfvyrgfli gpitpiygfg ilgvvyllrp
       61 lheqviplff aaallvtvle yvtsyllerf fhaswwdyke vplningrva lpislfwgvc
      121 cvlivrfvhp qmleivqili arvgfllpvf llmvlsfdmg ytlanlvafq kavqqvnqaf
      181 eqhkkelaen ieqykndwqg rfaafpeewr vlkqnlprln fhqrrllknf qkleinqiks
      241 sqelsrfiea irkkk
//
LOCUS       WP_010747892             525 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Enterococcus
            casseliflavus].
ACCESSION   WP_010747892
VERSION     WP_010747892.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..525
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58365
     Region          320..499
                     /region_name="CE4_CtAXE_like"
                     /note="Catalytic NodB homology domain of Clostridium
                     thermocellum acetylxylan esterase and its bacterial
                     homologs; cd10954"
                     /db_xref="CDD:200578"
     Site            order(325..328,378..383,416,418..419,437,443..444,467,469)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:200578"
     Site            order(327..328,378,382,416..420,437,469)
                     /site_type="active"
                     /db_xref="CDD:200578"
ORIGIN      
        1 mkkssnysnn sqhreatsek qapisrvesh qkqttgttrr tptanrqvsk kkpthrkylf
       61 slmtlltivi iatggyiaft lkqqealare kyeaaaqkll asiqeeqake gipakletls
      121 dgdkkelifr pkeesaipvk dasqklstma nklckkhadk etvtiariqa qavaskvsty
      181 slkadsyvwn retgrfedad svvadpifis ektgnelslk dlvpdegsll giqqviqqkl
      241 ldqakeptki ldavlgmdri tydskftydp ekitlqlpqn qtgvseitla ykeiapfidp
      301 elvnadqlke qqamldenkk yvaltfddgp ndtstldllk ilkdndvkat ffelgqmvdr
      361 ypevakkvhe egheiashsy shpqlntlsp eevkaeitkt dkaiyqatgv lpknlrppyg
      421 aidqqsaqaa gksiiqwsvd tedwklkdpn kilkvvqnnv ydgsiillhd ihpksvqavp
      481 giikalkaqg yefvtvdqll ncsmaaknqc intlvrkmna vlans
//
LOCUS       WP_010747723             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LOG family protein [Enterococcus].
ACCESSION   WP_010747723
VERSION     WP_010747723.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..192
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20666
     Region          2..182
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mrvtvycgtr lenaeklakt araignalak nhielvycgp laglmreivk gvfekegavt
       61 giypsgsfae dlppiitgss tytefytdtr eeqtqqllem sdaylvlpgg fgtleelssv
      121 csfmtlgklp vkpigvlmne glkdglkpll tmfeassfaw aelsetlfvl sdvetliqrl
      181 aakgskkecl ag
//
LOCUS       WP_010747940             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            casseliflavus].
ACCESSION   WP_010747940
VERSION     WP_010747940.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..256
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29442
     Region          8..256
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mlfldynpel taleyevyrf vsknlasvsk mkmkelaket htstasisrf ckkfecntft
       61 efkinlrfyl dslvkskisd sdesqtidfl krvnqpflse ridrateilk nksfvlfigs
      121 glsetiaeyg alyftdfgkt alkvddlsny pidwfpedil cktgiivlsi sgetqemiry
      181 lqklnqkdcq iiaitnteds tisqlsdltv pyyieretif kasqkkekti eltsqlpaiy
      241 liekiakrir lseell
//
LOCUS       WP_010747953             238 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus casseliflavus].
ACCESSION   WP_010747953
VERSION     WP_010747953.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..238
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26390
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msaiefkqvk ksfkdgdati ealketnfsv ekgefvaiig psgsgkstfl tiagglqaps
       61 egevfindep fskqkekqra ktrfkkigfi lqasnlvpfl tvkkqlqlvd kvsketqeqs
      121 atelfeqlgi eklqnkypde lsggerqrva iaralyhdpt iiladepaas ldskkavevv
      181 kilaketkek qkatimvthd trltdycdrv lvmkdgvlee kehtkkeaes ddsqkeqa
//
LOCUS       WP_010748033             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010748033
VERSION     WP_010748033.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29285
     Region          1..195
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mltliknewi kltkkrstwi mllllvlmtf gltyvvrlgs peigandlfa slsdmtsfln
       61 lfvvivaass vaeefsrgti kfllirpfsr sqilaakain tflfallgta vllisslaaa
      121 nlflaaespf aatgynglaa ilvalvfagt nlllivfyia ltifisavir sqslavglgl
      181 gmlfgssiin simlfaqeky pwlkwnpfnf mnikeqipsl lnspdmqmta fdpglgywem
      241 aigilvysvl iylltnwlfn krdvals
//
LOCUS       WP_010748134             122 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010748134
VERSION     WP_010748134.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..122
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=13936
     Region          1..116
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mselsrseyq imcyfyelnq sltkhellei lpelnkntta avissllnkg yltvaeikys
       61 qnvlarayrp sipyvdfikd eygevvvqkl vnhavsslnt kqqteyflnl ikerknainn
      121 ng
//
LOCUS       WP_010748305             259 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Enterococcus casseliflavus].
ACCESSION   WP_010748305
VERSION     WP_010748305.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..259
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30216
     Region          1..>150
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          90..>237
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(102,104..105,108,115,117,118..122,225..230,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mqfqqliyfn eiikaksmnr aannlylsqp slsksmqlle eeigtklfir tnkgvilten
       61 geklaqyskt ilaqlemikk ipqeksrkvl niasyplitv ekviadfynv ydfhplvinf
      121 eqcrlndvie kveksdaeig iimyneaqsr eiknilrhkh llytewmtdt wyvnlgkknp
      181 lyhskmisme elrsfpvirk pddyysslsf yleidgirla eldkviytnd nssiitmlqk
      241 tdvfrfgpsi rkksstnme
//
LOCUS       WP_010748413             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptidylprolyl isomerase [Enterococcus].
ACCESSION   WP_010748413
VERSION     WP_010748413.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..249
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=26646
     Region          61..246
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mkkilftlta aasllllaac tgssttdpss snsaeststs esvdlnalel pqlstdvqen
       61 ealvemvtee gsikiklfpe iapkavenfl thakdgyydg ltfhrvveef miqggdpngd
      121 gtggesiwge gfgeeysnql yhlrgalama kssapnsqgs qfyivqndqd vsdglaiqhy
      181 pekiieaykn ggtprldgsy tvfgqviegm dvvdkiaqae tqdsgngens qpvepvkiet
      241 ikvlqeake
//
LOCUS       WP_010748435             366 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Enterococcus].
ACCESSION   WP_010748435
VERSION     WP_010748435.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..366
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40506
     Region          39..358
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 meflkkskif aglvivcllg iavwiysnil fvfrpleaif ssvflpvlis ififyiflpf
       61 fnwvkrrtkk ksialyatll livfaaylii qvigpalaye mgrfinqipv iinlvidnid
      121 hsyleelfgp fidsidisqa snfalqfitg atnsltslis ivshsaivlf tiplllvymf
      181 kdgekvpdfl anktpkkyqg lmrqlcsdfh qaasayiggk llvcsyvavs sylifsllgl
      241 qnalllglic gvldiipyfg pfigaapafl falsldirta illvvgitii qlgesylvsp
      301 lvmnkvlhih piiavfllli agnllgfvgm ivalpvysii mamsgtllrf fqerklersv
      361 idkesl
//
LOCUS       WP_010748456             208 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010748456
VERSION     WP_010748456.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..208
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24089
     Region          30..>115
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          <153..198
                     /region_name="TetR_C_8"
                     /note="Transcriptional regulator C-terminal region;
                     pfam14278"
                     /db_xref="CDD:464123"
ORIGIN      
        1 mltylslnrq ilikctekrg ndmvgtvgnr rtiyskkvir rafqelllek eyrkitikei
       61 aeradinrgt fykyykdtaa lleeiegelv eqiasnlqqe nlsldlwlek lltilyenps
      121 tthlillnns hllnlllsei kpetlkrfaq yfqdaseeel elclsffvcg siglierwlk
      181 dfstmspkav aelliqifvt nvyedkkg
//
LOCUS       WP_010748706             482 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Enterococcus].
ACCESSION   WP_010748706
VERSION     WP_010748706.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 482)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..482
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55375
     Region          77..473
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mktksikgif qqtnklmilv afiplvvssv fysrqifiyq ntinnieean qlsekvdaiv
       61 leemwdlvfg qktvaqvqet nvidelrsdl qhiqentsta kelnilavaf rtldsletyq
      121 qqlidnilnd epveqnqyvm iqvdsvidll sdilqqfvgv eislasqtnh elvqsvllli
      181 lfqvvlllii faiinknrrf vrdnlqypld rlldlsnels qghlsyrael petpelrtlt
      241 sslnrmaddl trlleenalk qyhlaqsevr vlqaqitphf iynsldaivs lieaaryeqa
      301 temtyalsdf frislskgqd wiplekelrh vddylkilqi rygrmlsyti edqtvspelq
      361 vlkmvlqplv enavyhgtkf vrrvgmirit vselphqiqm tisdngvgid perlqeirrn
      421 lkettdpase sgyglynvyr rlqlnygsea qltihsqyqe gttinvtvpk reepnhvqsv
      481 hs
//
LOCUS       WP_010748867             826 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-dependent Clp protease ATP-binding subunit
            [Enterococcus].
ACCESSION   WP_010748867
VERSION     WP_010748867.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..826
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91838
     Region          1..812
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mdelftqrak avlaiaqeea kyfkhqavgs ehillalvie qngiagktlr emnitendir
       61 eeiehltgyg tvrqypenay laysprakht fayagdeakr lgapqigteh lllgllrded
      121 ilasrimlnl glslakmrql lkkkmgfnes ktngsagrrr paqakaqqgt ptldslardl
      181 tklarekrld pvvgrakevk rliqilsrrt knnpvlvgep gvgktaiaeg laqkiingev
      241 pedmqnkrlm mldmgalvag tkyrgefedr mkkiideiyq dgqiilfide lhtligagga
      301 egaidasnil kpalargelq tigattldey qkyiekdsal errfarvqvd eptpeeaeei
      361 lrglrpryee hhgveisdda lhaavqlsvr yinsrqlpdk aidlmdesaa kvrldktdes
      421 seladlqnei anlieekeaa irqqdfeaaa rlrikekklt qqltevafme vkeasgyads
      481 vtaedvatvv sqwtgvplqq mekkeserll dlekilhqrv vgqeeavkav arsirrarsg
      541 lkdpnrpigs fmflgptgvg ktelakalae amfgsedalv rvdmsefmek ystsrligsp
      601 pgyvgydegg qltekirskp ysvilldeve kahpdvfnil lqvlddghlt dakgrkvdfr
      661 ntilimtsni gaqqireeks vgfnvtdltk dhqamqkril eelkkafrpe flnrvdetvv
      721 fqslgegeih eivkimskai ikrlsnqdiq lkitpsaidv igkagfdpey garpirralq
      781 kevedrlsea llsgqihlgd kvtigaskgs itlnvkegqa rvlqqv
//
LOCUS       WP_010748871             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NusG domain II-containing protein [Enterococcus].
ACCESSION   WP_010748871
VERSION     WP_010748871.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009210
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..135
                     /product="NusG domain II-containing protein"
                     /calculated_mol_wt=15230
     Region          11..135
                     /region_name="COG5341"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444125"
ORIGIN      
        1 mklkefirda hlkpwdgvii lvlilssflp ififgqtqta dkeavlrvdg teikrfdlve
       61 gqktytylye dedgdtnlle iegdririke adcgdqicvr rgwasknget ivclphklvi
      121 eiqaadgset ddliy
//
LOCUS       WP_010748942              99 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Enterococcus].
ACCESSION   WP_010748942
VERSION     WP_010748942.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..99
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11173
     Region          1..97
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mikaismeef aqkekreple ildvrevdef aqghiktaqn lplselteqi sdlekdknyy
       61 vichsgarsq maseflsqqg fqvtnvlggm sawrgeikr
//
LOCUS       WP_010749061             754 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus casseliflavus].
ACCESSION   WP_010749061
VERSION     WP_010749061.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 754)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 754)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..754
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=86468
     Region          4..753
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mkkiqrlfei dpwkiatstl dkenrrlqes ltsigngymg mrgnfeeqys gdhhlgtyia
       61 gvwypdktrv gwwkngypdy fvkvinavnf iamdlfvndq lvdlakisps dfrleldmet
      121 gilrrnftvt lagatvkfsf erflsivkre lalikmdaei iegdaeikvv skldnnvhne
      181 dsnyderfwk elahgqtetf hylttrtven nfdierftvt samrhsqtpi dsvkselcva
      241 dtfafsgtag dtfslikevl ivtsrdvpah dhpakvtelg tlykadydal raeqvaawka
      301 rwdladviie gdaaaqqgir fnlfqlfsty ygederlnig pkgftgekyg gatywdteay
      361 avplylalak pevtrnllky rhnqlpqahi naqkqglaga lypmvtftgi echneweitf
      421 eeihrngaia yaiynytnyt gdtsylkkeg levlsaisrf wadrvhyskr qqkymihgvt
      481 gpneyennin nnwytnkmat wvlaytlasy eafkdeatvt isdeeqakwq diidnmyfpe
      541 dqelgvfvqh dtfldkdlmp vsdldpkhlp lnqnwswdhi lrscfikqad vlqgiyffgd
      601 qfskeekqrn fdfyepmtvh esslspsiha ilaaelgmee kalemyerta rldldnynnd
      661 tddglhitsm tgswlaivqg faqmktdhdh lgfapflpkt wsryafhiny rgrllfvsvn
      721 dstvtlkkis gealpiklyg kdyvledeis aain
//
LOCUS       WP_010749113             430 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Enterococcus].
ACCESSION   WP_010749113
VERSION     WP_010749113.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..430
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48732
     Region          8..217
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd07732"
                     /db_xref="CDD:293818"
     Site            order(92,94,96..97,167..168,189,217)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293818"
ORIGIN      
        1 maskdkttit fhsgiltigg tvievaykda hiffdfgsey hpetplpdee lqtlvahrwi
       61 pelknvydpr ldytyqgset keyqetavfl shahldhskm infldpnipm ytlketkail
      121 evlnqkgdfl lpvpheeksf vreligleph dvirvgeiev eiipvdhday gaaallirtp
      181 dhfiaytgdl rlhgyhpert kefcqlakht dllmmegvsi sfperepdpk vitvesetel
      241 ietfvrlvke npqrqitfng ypanverfma lveaaprtvv leatqaallk eifnkdvpfy
      301 tiddqvpatl dpafaisyqa lcadtsqylw qavahfenlq tgglyihsda qplgdfdpay
      361 qvfldqlaal eiefvrlpns ghakpadldq iiawiepqrl vpihtlkpen lvnpygeril
      421 pqrgekiile
//
LOCUS       WP_010749094             494 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010749094
VERSION     WP_010749094.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..494
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51415
     Region          196..405
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnflkrglqs lwakkgrsll liavfsaili fvlagltirs aalvatenaq ksvgatvtlq
       61 anreqafqqr ssssdsddqs trpdpgsfqs tpvaitdaqa iadldgvasy sfevstsada
      121 vsgiepisss dssteseatd ssesgqmggm pggmpggsms tgdfqitgvs tsaayttfse
      181 gtatitdgeg itsedegtnq vliesslaea ndlavgdtfs itdaedneve vmvkgiyets
      241 evgnsmsqmf nflnpantit asytlantls gnedtidsat ytlsdpsamt afveeaegli
      301 dtetysiqtn dqmyqsmltp lnnvasfakn iivlvaaagi iiltlivmms irerryeigv
      361 llslgesrak vilqffteif vcmvfalgia aasgnlvgna vgeqllaqqt etttdqaate
      421 nagpgggemp qmggnrggsf psftqsaeve sleitvspqq igllallglg isfgsillss
      481 agilrlnpkk ilvs
//
LOCUS       WP_010749160             201 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus casseliflavus].
ACCESSION   WP_010749160
VERSION     WP_010749160.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..201
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23082
     Region          3..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,65..66,69)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(64,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(70,75..76,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94..96,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          <166..195
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
ORIGIN      
        1 mgkigyirvs sqdqnldrql ammedlhidk lfqekasgkd tqrpefqkll syiregdcvi
       61 vasldrlgrd yedikntvaf mkqkkvalki ldaqfldfnt gnelldtamf dmflsllsyi
      121 aqnerekire rqrqgvllaq kagrykgrpi eyssnstdpq krlvyktvvd mlkqrvpvae
      181 iakengisrp tiykikkand l
//
LOCUS       WP_010749210              62 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial [Enterococcus
            casseliflavus].
ACCESSION   WP_010749210
VERSION     WP_010749210.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 62)
  AUTHORS   Munoz-Lopez,M. and Garcia-Perez,J.L.
  TITLE     DNA transposons: nature and applications in genomics
  JOURNAL   Curr Genomics 11 (2), 115-128 (2010)
   PUBMED   20885819
REFERENCE   2  (residues 1 to 62)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 62)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..62
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..>62
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          9..57
                     /region_name="HTH_28"
                     /note="Helix-turn-helix domain; pfam13518"
                     /db_xref="CDD:463908"
ORIGIN      
        1 makypfelkl kivkeylsgv ggyrylanky vissksqvsn wvnayreyge egllrkhqnq
       61 ky
//
LOCUS       WP_010749163            1049 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Enterococcus
            casseliflavus].
ACCESSION   WP_010749163
VERSION     WP_010749163.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1049)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1049)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1049)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1049)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..1049
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=121111
     Region          8..941
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mkishreeae veeqlirvlg eghnqwtyrp dlkseedlwv nlrqkiisnn qaelndfplt
       61 dkefetikte lllrtktpfd aakwlkgeng maritiered sqlgsvslil ysnqdigggi
      121 styevvhqia krgrnidard rrfdvtllin glpivqielk qvsakdgvyq afnqikkyae
      181 egmfrnnifs tlqlfvvsne qttryfanal pkdlhakflf swrtkdnkkv enlyefckqv
      241 lnipdahrli adytivsedq dnktlmvlhp yqvhaiqalf iaankhqsgy vwhatgsgkt
      301 ltsfvstkll arksgidrti mlvdrkdldn qttteftkfa sefntgissg nakanslivg
      361 tgsakelset lladananvv iittrqklda alkyakkqee kkgtnrfqkl mgqhivfvvd
      421 echralsaen meeikkmfpk stwfgftgtp ifpenrkqak gqlartthdq ygevlhtyti
      481 knaledgsvl gfqvehentv eptslenkiy rklkevetya eysseqinrm idqmepvkke
      541 syldpavfea dehiqkvihk mfrpdnaytk fdfrngrptk sailttssid makkyyraik
      601 emtkepdwlt kefpdqpire grtmedpdfp riaityslee nnqdssaqqe emkkiieeyn
      661 qyfdtawsla dieryngdin nrlarkraef kqfgkqidlv ivvdrlltgf daptiqtlfv
      721 drnleyagli qafsrtnrty pdktkglivt frkpatmekn vedatklyse akeesgliyp
      781 syqeskkrfk qayrklkevs smesidehtp letrieyvka fqelnrayes lvtyddyndd
      841 mvksptlnnq iqlleeqigv yetvkgslme eepekegedf stiefysent tklydidsty
      901 idqllgtyaa nssdareeie kaltklnkte gvkevyrqil nafdvgtlds nedifvikrr
      961 yftqasddli hafsnewfvs ekelhasnlq ympgedpipn mkaiinskdy egykanhpea
     1021 kpfkypqemk rawrkmldde liplenelr
//
LOCUS       WP_010749295             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YitT family protein [Enterococcus].
ACCESSION   WP_010749295
VERSION     WP_010749295.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..301
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=33180
     Region          4..285
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mraffswrti rdivliifgt siygfglvyl nipndlaegg vtgitlilra lwginpaist
       61 lilnipiili ggkilgrrsl vytilgtfgl sfwlafwqsv pllidlqhdl livallagli
      121 agigsgivyk vggttggvdv larileknfg vtigrsllif dvfvlllslt yidlnrmmyt
      181 lifsyvftrv idsildggys akgilvisnh seemapvlmd elergvtflq gegaysrvsk
      241 qiiymvvsgr eisevkrivh dfdpqafvsv invhevegeg ftylrpksrf lqrktavskt
      301 k
//
LOCUS       WP_010749353             409 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010749353
VERSION     WP_010749353.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..409
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46179
     Region          1..241
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mnneiavkvd higksfrlpt esttslkrti vnyfkgikgy neqkvlrdis fevnkgdffg
       61 ivgrngsgks tllkiisqiy tpekgsvevn gklvsfielg vgfnpeltgr envylngaml
      121 gfsekevdgm ysdivefael tefmnqklkn yssgmqvrla fsvaiqaksd ilvldevlav
      181 gdeafqrkcn dyfmkakden ktiilvthsm esvrkycnka lmidkgevki igtpddvanq
      241 ysldnvtqtg tstviektdd idvkkeeend yikdfkvrll sdeliekdqk riafevsyev
      301 leemktyiaf sltdidrniw vyndnsldhm ttglgkktlr ytcnlnemng cklrlgvsvr
      361 nesdqpfafs dkenspiiii spkkemskse risssglvrr ngsweeiei
//
LOCUS       WP_010749431             278 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Enterococcus].
ACCESSION   WP_010749431
VERSION     WP_010749431.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13303805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..278
                     /product="AraC family transcriptional regulator"
                     /calculated_mol_wt=32382
     Region          30..269
                     /region_name="PRK13503"
                     /note="HTH-type transcriptional activator RhaS"
                     /db_xref="CDD:184094"
     Region          190..270
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnlvnprtfn peiiylfdpw tqseshgemh hhdfleisvl legestyyfe kepakkirag
       61 svmlfnpgvd hcelqpkgtr shqlhiglkn islegfkrnf fpnkhpllel gkyhhqvlek
      121 awqlvresse erdefqlmqk avlmemlvyi lrglnedhin vvpylsksqr rqqqivnytv
      181 yylenhykee itleklaqdq flsptylski fkeatgvspi nylieirlkr akdmlknenl
      241 tikevasavg yqdayhfsks fkklygvsps gvlpkpkn
//
LOCUS       WP_010749546             332 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Enterococcus casseliflavus].
ACCESSION   WP_010749546
VERSION     WP_010749546.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..332
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36325
     Region          <1..332
                     /region_name="trifunc_aldol"
                     /note="KHG/KDPG aldolase/sugar kinase fusion protein;
                     NF041633"
                     /db_xref="CDD:469516"
ORIGIN      
        1 maniltlgei mlrlsttlsd riahssmfaa hygggeanva islanfghhv sfaskvpgna
       61 lgdavfhhlr sygvdcrhll rggsrlgsyy ietgigeraa rvvydragss faqmkenewq
      121 sdlfdgvdiv hlsgitpals ttwqtllltl ikeakaagck isfdinyrgk lwttaearvf
      181 lqevlpyvdy csagqldaqv fmdvsaptee veddyyyqem hrkypniqlf ystsrqvlsa
      241 shnqltgslw hngnyvvsat heinpivdrv gggdafsagi lhglvtkkqd qeiidfataa
      301 salkhtihgd cnqfsaneiq efiatgsgki ir
//
LOCUS       WP_010749693             188 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010749693
VERSION     WP_010749693.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21260
     Region          1..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrrkvytreh ilkaayelin regfgnftar niakhmgist qpiylefenm qdlkntlvea
       61 vfkdlsenvf pvvrtgdklv dlglnyirfa qeqhnlyial fiddygggkl mhdfsstyfk
      121 slikseekya dlsedavnal hngawivvtg laslmsagii tptddqiiki inetiegvie
      181 kkdsyifd
//
LOCUS       WP_010749809             456 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HD domain-containing protein [Enterococcus].
ACCESSION   WP_010749809
VERSION     WP_010749809.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..456
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52706
     Region          13..425
                     /region_name="YdhJ"
                     /note="HD superfamily phosphohydrolase [General function
                     prediction only]; COG1078"
                     /db_xref="CDD:440696"
ORIGIN      
        1 mslpykyqtl aiekvfrdpv hnyvhvqhqv ildlinskev qrlrrikqlg tasftfhgae
       61 hsrfshslgv yeisrricdi fqrnysiekv gpngwddker lvtlcaallh dvghgpysht
      121 fehifhtdhe aitvaiitsp etevhqilnr veagfpekva svitktypnp qvvqmissqi
      181 dadrmdyllr dayftgteyg tfdltrilrv irpyeggiaf smngmhaved yivsryqmyv
      241 qvyfhassrg mevilahlld raaelyqvdq emfqshsqll lpflkqeftl deylklddgv
      301 lntyftqwte endpilsdla krflnrkplk sarfddetql pmieemqglv ekvgfnpryy
      361 tainssfdlp ydfyrptsgk hrtqielqek dgslvelsqa sqlvaalagq tqgdqrfyfp
      421 kemidpniqn hydlfgetyq efakhirnga likpsh
//
LOCUS       WP_010749909             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010749909
VERSION     WP_010749909.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..222
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26017
     Region          10..203
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mlnltnfqsq ayesikelil taklipgqki sekeleqrlt igrtpireai irlrrealih
       61 vvpqsgtyis kisikqieea rfvretleke vfvaacqavt eeqlkelekl vilqrtyaql
      121 kdeieffqld eafhqliyki adkenvwnwl qtinlplnrf rflrleveel sweiilrdhe
      181 eilatlkekd qakiaplvgq hidvidndlv fvekafpdyf te
//
LOCUS       WP_010749925             626 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Enterococcus].
ACCESSION   WP_010749925
VERSION     WP_010749925.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..626
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=72532
     Region          14..626
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 meklsllllr tlskhdgfmt skaaaaelgv srktvrryae einqhqeryg cmiqakkgsg
       61 lylqitneea fqrrkeqash nddfvsriie ffiqeetyik semlcerlfi sqsklsqelk
      121 klrrilshyq lsiqtkpyyg mklsgsefdl rrfmasnylq rthikqleeg tisedtpsll
      181 hqqikaivss efsqkaypms eailnnlvnh laiavlrmqs gryldrnlpi sgrtndeqtl
      241 lgeriiarie kecavhftey ernyvlgqiv gkrvvprnek mtvsdeaael vskilkaike
      301 srqidfskdl dlqtmlmlhf aplidrielg ielknpllne vkvhcnvayd laiiagqvia
      361 kqfektisdh elsylamhfd valnkknsqt qrkyilvvnd lgraantflk ekfefyfrny
      421 ikkvtvcnqy eflqmieeqe fdfifssipl pyegtipvmn vdyfmqpdmi kkietalaav
      481 fteevllnyf keslficeqe fetkeavlhf lcqqikeqys mpenfetlvf ereaffgtdf
      541 lpsvafphpn aligsetvia vanlkkpvfw ykqsvrlvfl lviaeqdhlk vkplndhlik
      601 qcssldkvnk laattdfmsf inylke
//
LOCUS       WP_010749955             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010749955
VERSION     WP_010749955.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..222
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24187
     Region          124..218
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mkavknlfil iglfllsqvg mtvfsvvkiy yleageprip ammsyglial llanigllmy
       61 larklglatf dfgwstkrnw lwiiggfvlg rvvavggtmy lqyisdqeat andallgelf
      121 tgenpllifl liavaapime eivfrggfig llfkkypivg iissvavfsi ihsvtnlvef
      181 liygamglim aliyvktkrl etaiamhfln nalaaiamil lg
//
LOCUS       WP_010750037             827 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Enterococcus
            villorum].
ACCESSION   WP_010750037
VERSION     WP_010750037.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..827
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92451
     Region          1..813
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 meelftqraq lvleiaqeea kkfkhqsvss ehillalvie pngiagkvlr evglnetdvy
       61 eevehligyg tmtayppgvf lpysprmkqi falansevkk mgaqkvgteh ilisllkdes
      121 imatrmminl gvsltkvrqs lkqkmglknd srnnsirrrn sqekrqltkg tptldslard
      181 ltklakegkl dpvvgrssev krliqilsrr tknnpvlvge pgvgktaiae glaqkiilge
      241 vpeemqekrl mmldmgslva gtkyrgefed rmkkvideiy ndgqvilfid elhtligagg
      301 aegaidasni lkpalargel qtigattlde yqkyiekdsa lerrfariqv deptpeeaee
      361 ilrglrsrye ehhgveitdd avraavnlsv ryitsrqlpd kaidlidesa akvrldqtgd
      421 ltesavtkie ieeivkekea aiqkqsfeta aqlrrqeksl rnklaklliv eekhekgyad
      481 rvteedvatv vsewtgvplq qlekkesqrl leleallher vvgqdeavka vsrairrars
      541 glkdpnrpig sfmflgptgv gktelakals evmfgdensl irvdmsefme kystsrligs
      601 ppgyvgydeg gqltekirqk pysvilldev ekahpdvfnl llqvlddghl tdskgrkvdf
      661 rntimimtsn igatqireek nvgfnvqdit kdhkamqkri leelkktfrp eflnridetv
      721 vfhslskdei hsivqimsra ivkrlkeqdi qvkitsaavd vigkagfdpe ygarpirral
      781 qkevedrlse allggeihlg dhvtvgaskg kitlttrlpk kqavkts
//
LOCUS       WP_010750062             153 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus villorum].
ACCESSION   WP_010750062
VERSION     WP_010750062.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..153
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17863
     Region          3..117
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(4..6,20,39..41)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(53,56,60..61,70,88,92,98,102,105..106)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 myltihevak ktgltpytlr yyareglfdf verssnsigt rlfkesdlef iyiikclkha
       61 glsikdiksf vewtmqgdat iedrlhmfke rqielekqls elqevldvvk yktwyyetak
      121 dagtcaihdt laedevpkqm lktkkklief hns
//
LOCUS       WP_010750076             153 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus villorum].
ACCESSION   WP_010750076
VERSION     WP_010750076.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..153
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17619
     Region          5..116
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(6..8,22,39..41)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(53,56,60..61,70,88,92,98,102,105..106)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mnktysigev aemfhlsist lhyydkkgll pfvekndsgh raftesdlqf iqticclkdt
       61 dmpikdirty inycmegpst iekrkallla hkrqvlakqe kiikslegid qkiehyslkn
      121 adsfieeqla yameekrinh lanpfkkvsf ssk
//
LOCUS       WP_010750080             527 aa            linear   BCT 01-JAN-2025
DEFINITION  gluconokinase [Enterococcus villorum].
ACCESSION   WP_010750080
VERSION     WP_010750080.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..527
                     /product="gluconokinase"
                     /EC_number="2.7.1.12"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046316 - gluconokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /GO_process="GO:0046177 - D-gluconate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58917
     Region          5..488
                     /region_name="ASKHA_NBD_FGGY_GntK"
                     /note="nucleotide-binding domain (NBD) of gluconate kinase
                     (GntK) and similar proteins; cd07770"
                     /db_xref="CDD:466790"
ORIGIN      
        1 mkisigvdig ttqtkavafn eqaevvasny flnpmiqetq gmaeqdpdli fhgvcivire
       61 vmknlpkkvt ievisfssam hslilldenk lpltrmitwa dnrakdqaee lkheplgkqf
      121 yqqsgtpihp mtplikikwl kethpelikq tayfigikey ifyrffgrlm cdystasgtg
      181 yfdihrftws geiiaylkin qnqlpelfpp ttkisglkkd mrellglgnd isfvlggadg
      241 plsnlglgaf gehivaltvg tsgairfitn epylhpemet fcyvldqthw iiggatsnga
      301 gifdwasqtl mqevtqkaia hgenpydell ssiafvppga ngllfqpyll geraplweae
      361 asgsflglqr nhtekemmra ilegiclnlk rilsgickee qfiqvratgg fsnsvifrql
      421 madvlgyplv fptvtessal gavflgwqsi gkitelsevt ekiqletqvl vqenvhevyq
      481 kvypvfvetq kqlartyqpl tqlrkilnie kkkrvnnrsg gcclvtr
//
LOCUS       WP_010750102             173 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus villorum].
ACCESSION   WP_010750102
VERSION     WP_010750102.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..173
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19607
     Region          9..153
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
     Region          85..172
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtlvfqktte edvpavmkii ddaksllaat gspqwqngyp nietiekdie eaisyvllvd
       61 gevagilalq qtpdknyqei fegrweeead pyttihrial skafrgqkla yrliefaqae
      121 tktlgitqir vdthrmnsgm qrimahcgfk fcgivyvddy vdnerlayqk llq
//
LOCUS       WP_010750213             196 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Enterococcus villorum].
ACCESSION   WP_010750213
VERSION     WP_010750213.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..196
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21517
     Region          1..>182
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mlkelkktsv iligvlfiai glnwfllphd iasagvgaig hlvetaflip kaitvwvvni
       61 tmltlailll gkiifvkavi gsllfpiile iipktalfys qflslivgsl lfssgvytly
      121 tvgasnggvt ippiilqkff ripvsrglll tnliivwlny lvfgwretvy vlfsivlssf
      181 flkllgriyp itknle
//
LOCUS       WP_010750134             144 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus villorum].
ACCESSION   WP_010750134
VERSION     WP_010750134.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..144
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16674
     Region          13..143
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mehyvkkfad lttqefyeiv keriavfvve qncpyqevdd vdaqswhtyf kdeegnvaay
       61 triyeeagti hfgrvlvnkd hrkeglgrki vqrtidviea nypampivig aqvylqsfye
      121 sfgfkaisdv yleddiphid mkra
//
LOCUS       WP_010750054             366 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Enterococcus villorum].
ACCESSION   WP_010750054
VERSION     WP_010750054.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..366
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=40424
     Region          50..343
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mlkkqllfvv alfslltlaa cgtsskeatt qsqtankilq epysdeqfll gtyvririyd
       61 egkkdalkpa farvkelgdk itinqsgsei davnqqagik pvkvsddvyt llkrayeyse
      121 dsqggfdmai gaitqlwrig fddarkpsqe eidqalklvd yhkivlndqd ktvylkekgm
      181 iidlgaiakg yitdevvkvl kkqgvttaiv dlggnvyvlg hsprgndqdw tvgiqdpnla
      241 rgsvlgsike rnktlvtsgi yerylevdgk kyhhlfdpdt gypfdndias vtiitdksid
      301 gdglstavfs mgvkkgldyv eselndgtea ifvtkenkvy vtdpikdsfv ldkdskytmg
      361 drselk
//
LOCUS       WP_010750229             417 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus villorum].
ACCESSION   WP_010750229
VERSION     WP_010750229.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..417
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=43982
     Region          1..414
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdkfvafmek hfipvaskig aqrhlvaird sfmvsmplmi lgalavminn lpipgfqelm
       61 nsifggeawk gfgaaawngt failsvliaf llayhlangy rkdgvsagvi slgsffalgg
      121 algmssnglf iaiivgiist eifvrlsgne kliikmpdgv ppavakafas llpamitisl
      181 fslvaaifaa fgvddivgaf ytavqepfmg lansypsall lafitpflwf fglhganmvd
      241 plmqtinapa ieanvnaiaa ghsapfivnk pffdsfvnlg gtgatlglll aiylvgrknk
      301 pymvvtnlsi apgifninep tmfglpivln pimfipfilt pmvlvsvayf atstglvpaa
      361 tvmppwvtpp iiggvlatks iaggvlaavn lilsiliylp fvkvatiqer rkealng
//
LOCUS       WP_010750220             575 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus villorum].
ACCESSION   WP_010750220
VERSION     WP_010750220.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 575)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 575)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 575)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..575
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=65982
     Region          194..575
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 msrwrilfsq gtllnrllrk yalvmilltt vatviisvht wiqsqnqaeq mtsealqsts
       61 rtlndkatls kiiknqllgs sekienatty ltkpideylm yaydqqqkts dflsfpyqmr
      121 diyvsyeevs tvyvvfsqlp eyfessrnnk ggiiksgtpk lsdafyikms itqggsevgs
      181 mfvgfekeel daalaslntf sglslymisg ttnrlytfhd kglaettlas qeqlitaslq
      241 qnsklpiqal eknnfiqyqk lpddyriltt ldrqmvsrtv irnlaplvlg vflldsslll
      301 llyktfnrys qqidivmaam netakgnlet ridttkteye lkdlsigine mldsinqfve
      361 diykleikqq eahmralqaq inphflyntl eyirmyalse gseeladvvy afsallrnnt
      421 nqektislke eldfcekyvy lyqmrypnri ayhfsidptl ekievpkfvi qplienyfkh
      481 gidftrvdna lsvkvfregq rvmiivkdng rgitparlee iesrlvqtkv eltqsiglqn
      541 vnerlrayfg ssyqmklcen keggltvtii fkeke
//
LOCUS       WP_010750307             144 aa            linear   BCT 01-JAN-2025
DEFINITION  HIT family protein [Enterococcus villorum].
ACCESSION   WP_010750307
VERSION     WP_010750307.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..144
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16706
     Region          2..136
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mencifckii nqeipsykiy edevvyafld isqttkghtl vipkqhvsdi feydkalaat
       61 ifsripkiar sleqafpemq glnilnnnre layqtvfhsh ihlvprysek ddfsihfgnh
      121 qadytpeeli diqhkieeqv nkid
//
LOCUS       WP_010750308             245 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus villorum].
ACCESSION   WP_010750308
VERSION     WP_010750308.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..245
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27367
     Region          3..244
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mslivehvtg gyghlpvlkd isfsvksgem vgliglngag ksttikhiig lleqkkgsit
       61 indrslkkdp eayrkqigyi petpslyeel tlkehievta maydipidea mkraekllqt
      121 frlenrlewl panfskgmkq kvmilcafli epslyiidep flgldplain allelmvemk
      181 negsgilmst hilataekyc drfvvlhnge irangtledl qkefhlpgss lddiyisltk
      241 eqehe
//
LOCUS       WP_010750325             428 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A [Enterococcus
            villorum].
ACCESSION   WP_010750325
VERSION     WP_010750325.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..428
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47227
     Region          1..427
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mqqplayrmr prnidevvgq ehlvgegkii rrmvdakmls smilygppgt gktsiasaia
       61 gstnfafrml naatdtkkdl qivaeeakms gtvillldev hrldktkqdf llphlesgri
      121 imigattenp yitinpairs rtqifevkpl deqdiqkavk ralhdkergl ghlliqlden
      181 allhlsratn gdlrstlngl elaarstkpd esgtihltlt iieecvqkka lthdkdgdah
      241 ydvisafqks irgsdvdaal hylarlveag dlasicrrlm vigyediglg npaaaartvn
      301 avlaaerlgl peariplada vvdlclspks nsaysaldea isdihagkag dvpdhlrdsh
      361 yqgakalnrg igyqyphnfd qawvnqqylp dklknttyyh pkstgkyeqa lkqqydrine
      421 wkkkatkk
//
LOCUS       WP_010750323             157 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus villorum].
ACCESSION   WP_010750323
VERSION     WP_010750323.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..157
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17163
     Region          5..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlqqykkimv avdgsaeael afkkavnvam rnngelllah vidtrsfqtv ssfdgmlaeq
       61 atemakqtla dyeenakkag lnhvstviey gspkqiiake ipednhvdli llgatglnav
      121 erlfigsvse yvirnatcdv lvvrtdlenk lpekkkd
//
LOCUS       WP_010750352             235 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Enterococcus villorum].
ACCESSION   WP_010750352
VERSION     WP_010750352.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..235
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27234
     Region          2..228
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 miksvvfdvd dtmydqqqpf rnavkkvvpl vsdedmssly lrfrhhsden fpkvmagnwt
       61 leymrahris qslkdldyph iteadglyfq qvyeeelnni clheevkktl dflaeleipl
      121 giitngptdh qtkkleqlql akwiptqhmi vsqatgyqkp ekeifqlaee rfnlspqetl
      181 yvgdnydndv lgakgagwkt lwfnhrerki egtstcdiei tsfdqlletm kvifg
//
LOCUS       WP_010750361             301 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus villorum].
ACCESSION   WP_010750361
VERSION     WP_010750361.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34499
     Region          16..96
                     /region_name="cupin_MmsR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MmsR, N-terminal cupin domain; cd06986"
                     /db_xref="CDD:380391"
     Region          <113..273
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 meqaiflkke hqqvkkeldf dfcgfsktlp yhsfgpairq dyvlhvvmeg kgtyhvkeqq
       61 yhlkkgdlfl irpgdstfyl adgddpwmyc wlsfngplaq kiiqrslfke dqytmvssgi
      121 sayidiilec mhhsqedlvn eleltaltyr flslllkdgg kvglgeqkvy sslvietvky
      181 ieghyphhlt veeiaqqlsi nrshlsrvfk nqlgtsikey ligvrinraa fllsltndsv
      241 esiayqvgfn slvvfsrmfk kttgetatsy rkrmkneesr nlsldtlkke laeqaiisws
      301 t
//
LOCUS       WP_010750390             187 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Enterococcus villorum].
ACCESSION   WP_010750390
VERSION     WP_010750390.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 187)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..187
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21312
     Region          45..181
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mleyeqfeek tikrkeiyhg aiidvalddv qlpdgnhakr elvfhpggvg iiafdeqdrl
       61 llvkqfrkpl ekvileipag kidpgesqtp ertaarelee etgyraeklq hltsmylspg
      121 faneimhiyh athlkqvanp laqdedevle lyaltfeeak qaiidqlicd aktiyaiqyw
      181 ellikgk
//
LOCUS       WP_010750394             635 aa            linear   BCT 01-JAN-2025
DEFINITION  M13 family metallopeptidase [Enterococcus villorum].
ACCESSION   WP_010750394
VERSION     WP_010750394.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..635
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72393
     Region          8..635
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mnkerlkqdf feavnedwlk takipadkpa tggfqdlvdg iddllmkdid rmladpsivq
       61 sdmmlhflhf yqlandydsr nqlaekpllp lleqiekits feelnqqfpe wtldslplpf
      121 sldvdadmkn aqtnalfayp pslflpdkty yssehpngaq llniffdmmv qlvqlagkdk
      181 nqaeaiveqa iqfdklvaph vksaeekady skmynpqdfd tfiahtnqld lkklvtglig
      241 tipdkvivtd pvyfeqlsei lttdhfqlfk swmivrtirs lsgylseefr qvsgifsrtl
      301 sgtdeamppk kaayylatgq fdqvigdyyg ktyfgevakk dveqmiqkmi lvykkrleen
      361 nwlsdatrkk aiikldklgv qvgypekipt lfqqyktipk eeggtllsna ltfskvalkd
      421 rfarwnkpvd rtewemsadt vnayyhpfrn iivfpaailq apfysleqss sanfggigav
      481 iaheishafd nngalfdeyg nlnnwwteed lahfqekaqa mieefdglpf adgkvngklt
      541 vseniadagg lscaleaakt eqehsleeff iswatiwrtk akkeyqqlll qidvhapakl
      601 raniqpqnlv efyetfaite kdamylppek rvhiw
//
LOCUS       WP_010750467             258 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Enterococcus villorum].
ACCESSION   WP_010750467
VERSION     WP_010750467.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..258
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29506
     Region          2..254
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mifdshthln aeqfnedipe tierakelgv tkmavvgfdt ptiekslqls hdypniysii
       61 gwhpteagsy tkeietklqe qltmpkvval geigldyywm edpketqatv frrqiaiake
      121 mnlpisihtr ealedtynil keedirdigg imhsfsgdfe wakrfldlgm hisfsgvvtf
      181 kkaidvqeaa invpldrmlv etdapylapv pyrgkrnepg ytrytvekia elrnlsveev
      241 alqtwenahr lfrlsend
//
LOCUS       WP_010750515             332 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Enterococcus villorum].
ACCESSION   WP_010750515
VERSION     WP_010750515.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..332
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36344
     Region          4..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meiyditiig agpvgmfaaf yagmrqaktk iidslpqlgg qlatlypeky iydipgfpai
       61 kaselvnnle kqlttfnhsf hlneevlslt kddelieitt tkgihyskav iltlgsgsfq
      121 prklklpeak tyenhgldyf vndlmkyagk kvaiagggds aidwalmlep iasevylihr
      181 rsefrahehs vnllkassvn lltpylieel sgengeltdi rlkmvksdet idlmvnslii
      241 nygftsnleh lsawgldstr naitvnsdms tsipgiyaag dicsypgkvk liatgfgeap
      301 tavnnalhfi npkvrtqpgh stslydnanl nk
//
LOCUS       WP_010750641             879 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus villorum].
ACCESSION   WP_010750641
VERSION     WP_010750641.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 879)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 879)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 879)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 879)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..879
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..879
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95346
     Region          6..869
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mddfkktgke veketkttie tglttqeaek rsqeqgknkf deapkeslvk kflrslsdft
       61 tiillvaavi sfytafateh gdlfegllii aivlinsvla ivqegnaeka leslqemnkq
      121 tatvirdgkv ekvdaenlvv gdvlvlesgs aitadarlve tsqlrveesa ltgeseavek
      181 dadyvsqeed algdqinmvf kgctvaagrg kaivtsigmk temgkiagll ndhtmqktpl
      241 qirlnqlgkr islialaaaa lvfiigelqg epllemfmts islavaavpe tltvivtltl
      301 aygvqkmakk haiirqlpav etlgtanvic sdktgtltqn kmrvrrvwsk edevtdveds
      361 mtnsameilk maalctdvtv ekegdelivk gnpteaaivr aveenyhtke elekeyprva
      421 eipfdserkm mttihqmgek yisitkgafd vlsprftsgd ieqatavndr fgkkalrvia
      481 vgyatyeeep qeitsealek dlrligligm idpprpeskg aikrakkagi ktvmitgdhv
      541 vtasaiakel giltnpteal sgselqalsd deldervkdl svyarvtped kirivkswqr
      601 tgavvamtgd gvndapalka sdvgcamgit gtdvaqsasd miltddnfat ivdavsqgrs
      661 vyqnirkain fllscnisei fivliamlvg wgapftavql lfvnvvadgl pgfalgrepa
      721 ekgimdeapi pknegifarg llqkiainat vftivtlfgy ylgsfvnsis pwveasqevg
      781 qtvaflvlay ssilhvfnvr ssqsifkvnl atnksllema ilamvittav allpftqelf
      841 glvhislnhw llvgllsiip iavselikfh qlpeveeee
//
LOCUS       WP_010750677             288 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Enterococcus villorum].
ACCESSION   WP_010750677
VERSION     WP_010750677.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..288
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31881
     Region          22..>287
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mltiteelke iylnkietkn lrvgvigmgy vglplavefa kyglkvvgid lneqkvssln
       61 qgkshildvp dyevnqlven rnllatsdfs iiseldalsi cvptplnenq epdtsyieat
      121 vkeivryqek pllvvlestt ypgttrelia gtfeknglvl dqdyylcfsp ervdpgnkny
      181 qtkqipkvig glsensthig qalyekvida vvpvsspeta emskllentf rsvniafvne
      241 malmcdrmgi diwetidaaa tkpfgympfy pgpgvgghci pldpmyly
//
LOCUS       WP_010750281             318 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus villorum].
ACCESSION   WP_010750281
VERSION     WP_010750281.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..318
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36655
     Region          9..184
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(12,14,88)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(41,87..88)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            86..88
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 meqqekiavl ipcyneeati stviadfkre lpeaeiyvyd nnstdrtyel avacgaivkk
       61 eprqgkgnvi rqmffdidad yylmvdgddt ypaeavhgll dklrsgeadm vigdrlsngt
      121 yfdenkrpfh dfgnhlvknt itrlyktkir dvmtgyrgfn rifvksfpim ssgfqietel
      181 tihaldkkfk lvelpidyrd rpegseskln tfsdgfkvim miikmwkdyk plmffgiwtl
      241 fffvfglftg vpvlreymlt hfitrvpsai lstglmilal lslvtglild tvvtnakkdy
      301 elnlyhvyhe ckkkeqrk
//
LOCUS       WP_010750693             201 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Enterococcus villorum].
ACCESSION   WP_010750693
VERSION     WP_010750693.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..201
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23061
     Region          <19..185
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mylqikrlld llasmlllii vtpflvviav tlyfcngkqv lfkqprvgkn ekifliykfk
       61 tmndqkdeeg nllpdvqrlt kfgaflrkts ldelpqlwni fkgdmsfvgp rpllieylpl
      121 ytkeqarrhl vipgltglaq vngrnaltwe ekfqydvtyv dqaslktdsf ilvktvlivl
      181 krkgvnsgkq etmerfmgvs k
//
LOCUS       WP_010750890             296 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Enterococcus villorum].
ACCESSION   WP_010750890
VERSION     WP_010750890.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..296
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33918
     Region          27..290
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mkkskglgrg idalfqdlen letmdvkdet vvqlplnelr pnpyqprktf eeislqelan
       61 sieqsgvfqp iivrrsavkg yeiiagerrf rasklaekat ipaivrdfde eammqvavle
      121 nlqredlnpl eeaeaydmlm knlqltqaev akrlgksrpy ianylrlltl pelvkemvqd
      181 qrlsmgqart llglknksmi lklanravte nltvrqleqi vsqlnqndgk ekkkiprlak
      241 ekpyylrese drlmdkfgtn vaiqekdgkg kieieylsqn dltrildiln iqfdee
//
LOCUS       WP_010750928             341 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Enterococcus villorum].
ACCESSION   WP_010750928
VERSION     WP_010750928.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..341
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39010
     Region          18..330
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 msvyqrfitn ekirrmtvll siivvlflvk smittilltf iftylmihlv hiiqrfikip
       61 tgvltilvya lvvyliylal tiyvpllihq tvdmiqsvin fyehqpkdad pvlqyihtyi
      121 erndffeqlq ngasialgyl qdvgklavaf tmsfilsfff miekkktivf sklflkgefa
      181 wffqdiyyfa dkfvntfglv leaqfiiall ntllttiala afgfhqllsl aimifilsli
      241 pvagvivscv plsfiaysqg gikdvvyill tilivhlies yvlnpklmss ktelpifytf
      301 ivlllskrfl gvwglivgip iftffldvlk vkeipnhplk e
//
LOCUS       WP_010750931             282 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Enterococcus villorum].
ACCESSION   WP_010750931
VERSION     WP_010750931.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..282
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30856
     Region          1..281
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mkqiksitwi ytkivfalti lgvsinmflg phhiaaggvs glgillesaf gfnralvilv
       61 lnsvmlvlal vflgkkpffk vlfgslvfpl iialipetmv tpdrllsvif gsaifalgva
      121 ilyknnsssg gttipplifk kyfhlntsig llvtdafvvs lnlfifgfee flyailsivi
      181 tsivmtyiet gmnrkkslmv msenyleeir qrlsaeigrg ltlleakggy nrkskevlli
      241 vvtdhefski kpiieeidpt afvivssvae vtgsgftyhp ie
//
LOCUS       WP_010750943             283 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar ABC transporter permease [Enterococcus villorum].
ACCESSION   WP_010750943
VERSION     WP_010750943.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..283
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31705
     Region          3..283
                     /region_name="MalG"
                     /note="ABC-type maltose transport system, permease
                     component MalG [Carbohydrate transport and metabolism];
                     COG3833"
                     /db_xref="CDD:443045"
ORIGIN      
        1 mkkinssakf qrrvsqffty vfliilsiii iypllitast afksgniaaf sldlssdwtl
       61 nnfsrlfset lygtwykntl iisiltmviq vtvvtlagyt ysryrfigrk sslmfflviq
      121 mvptmaalta fyvmafllna ldrywfltmi yigggipmnt wlmkgyfdtv pidldesakl
      181 dgaghfrifl qivlplvkpm iavqalwafm gpfgdfmlak fllrtpenqt vavglqtfis
      241 dvtnqrvslf aagailialp icllffflqk nfvtgltsgg tkg
//
LOCUS       WP_010750954             284 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus villorum].
ACCESSION   WP_010750954
VERSION     WP_010750954.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..284
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31478
     Region          58..236
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mralckrnlk iyfsnsatvf fsllgalivf glyllflrkn mvtqfdrltd gpiiadfwvl
       61 ggilattslt tsftglsqfi kdkaenkfmd fiitdkkash lligyflsgl iisfcmqvav
      121 lifclvyfsc qensqftfmm elkafgiill sslnatainl iictfiktes tlrtissilg
      181 aisgfmctay lpigsfsgft eiiikilpis yasssfrrif ispiitdmph eqllalkeyl
      241 gigytwddhl ttattdisil iittifcllv lslcgkkiaq vsms
//
LOCUS       WP_010750979             357 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus villorum].
ACCESSION   WP_010750979
VERSION     WP_010750979.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..357
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38917
     Region          16..177
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          122..357
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflaikemky aklrygliig imfliayvvf mlsglasgla eefkkaiddw gaqeivlsed
       61 annvfaasql tredlnsvka kekapiglfs gavkgnkken vtvfgttnea fllpkvssgr
      121 lfekeneiii sqnlaegnyk lgdqlkigsy dqkltivgif petyytvspv iytdldtwtq
      181 lkygdqpfss pskkpinaiv tkqkatitke gasktlqklt ipdfiesipg ysaqnmtlna
      241 miyflflvva avvgifmyvi tlqktaifgv mkaqgirhtf iakslvaqsf iigvfgvsla
      301 vlvafltsli lpsampfaii wpqwlmysgv lilvavlggl fsirtiakvd pitaigg
//
LOCUS       WP_010751005             293 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus villorum].
ACCESSION   WP_010751005
VERSION     WP_010751005.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..293
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31183
     Region          1..291
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mivsaisqgm lwailglgif mtyrildfpd mttegsfplg gavcvtaith gvspflatil
       61 gvlagmiagl vtgllytkgk ipvilagilv msglnsvilf vmrtpnlsll nypilqdifh
      121 glhlpnyfdt vllgfialgi lisvllfffn tdlgqgyiat gdnetmarsl giqtdrmkil
      181 gltlsngvia lsgaliaqnd gyadvnkgig viviglasii igevifhelt laerliaivv
      241 gsiiyqllil vviklgfdtt ylklfsaiil alclmipqlk nalklktgfe kev
//
LOCUS       WP_010750901             747 aa            linear   BCT 01-JAN-2025
DEFINITION  LPXTG cell wall anchor domain-containing protein, partial
            [Enterococcus villorum].
ACCESSION   WP_010750901
VERSION     WP_010750901.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Novick,R.P.
  TITLE     Sortase: the surface protein anchoring transpeptidase and the LPXTG
            motif
  JOURNAL   Trends Microbiol 8 (4), 148-151 (2000)
   PUBMED   10754567
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01167.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         <1..747
                     /product="LPXTG cell wall anchor domain-containing
                     protein"
                     /GO_component="GO:0009986 - cell surface [Evidence IEA]"
     Region          <505..589
                     /region_name="Mucin_bdg"
                     /note="Putative mucin or carbohydrate-binding module;
                     pfam03272"
                     /db_xref="CDD:460871"
     Region          708..741
                     /region_name="LPXTG_anchor"
                     /note="LPXTG-motif cell wall anchor domain; TIGR01167"
                     /db_xref="CDD:273478"
ORIGIN      
        1 ggsagafsli dgkalagtts sskvlkisag ldtpldekin adnepntyys ieitrngssi
       61 ysqnmpgrat lqqimnnfgn gsnlvtvqtg diitvnqpqk iegssvlwqd etekdytygs
      121 ntaryqvtdy glepapelgg ttankqlnlt eqpenvelnq llsavtvngh avtddlytik
      181 qltdfdtkti gkrevklqid lkdgyatkev dipyevkwgd slvmkglnga tvgvysfikk
      241 ndqwylsatq gdpdadlnnw vnnefgrndy yrievdegen slpvpsqpev fedssvntgn
      301 fvysvtgnmt fgqaiarfnn gqplpistga iikvyhaeps knnlfiqddv vrdytaglny
      361 ayyrvtdsgi epitdmkanf vkmsltlged atakdikali qnvkfndqel ntdlytvepv
      421 dtfdtstvge kelkvkltts devttkevav pytvnwgntl vmknkdgdti safsltkedk
      481 klqiaslpgk nksnlskrit naddsdvyys ievfshnasq ykyevhgkqt ieqaisrfng
      541 gepltvsagd qvkvyhadps gnvfmsdeqe gnytygsnya yynvtdygfe ptgdlsvtpa
      601 epnitvgtke vdlkdllkev kvndkavpkn sytvtldpet emdtssvgtr taklvvkvdr
      661 aygafsttte atyhvveega agdnatggdq egnadndgan adgsadgslp ktnetknatf
      721 silgaflvsv agmtlfwkrr ktneekk
//
LOCUS       WP_010751037             449 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus villorum].
ACCESSION   WP_010751037
VERSION     WP_010751037.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..449
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51329
     Region          1..391
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msnfeqfnfk pyinealmek gfnqptevqe rlipliakgk niigqsqtgs gkthtfllpl
       61 fqkinaekae vqvvitapsr elatqiyeaa nqiakfstpe irvtnfvggt dkqrqlnrln
      121 hqqphivvgt pgrildmmne qalkihtafa fvvdeadmtl dmgflnevdq iasrlpeklq
      181 flvfsatipe klrpflrkym enpiieeikp kavisedien wlistkgkdk nrmiyqllti
      241 ghpylaivfa ntkqhvdeia dylknqglkv akihgditpr erkrvmrqvq nleyqyvvat
      301 dlaargidie gvshvinaev pddldffihr vgrtgrsglk gtaitlyspn deqaidsiek
      361 igvtfepmei kndeivktyd rnrrtkreks kdtldptlig lvkkkkkkik pgykkkidwa
      421 iaeknkkerk lerrqqtrta rknkknsnk
//
LOCUS       WP_010751076             251 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Enterococcus villorum].
ACCESSION   WP_010751076
VERSION     WP_010751076.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..251
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=27028
     Region          65..248
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mktkklllsm glaatfllaa gcsqnntdks assaesstek ttdsstkesv dlnsltlpql
       61 snevaadedl vemvtskgti kiklfpeiap kavenfmtha kdgyydgltf hrvikdfmiq
      121 ggdpkgdgtg gesiwgkgfe teisnklyni rgalsmaraq dpssngsqff ivqnaddvhd
      181 gllkddypqa iidaykkggs pnldgeytvf gqviegmdvv dkianvetds sdkptedvki
      241 ekinilqeak e
//
LOCUS       WP_010751097            1177 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Enterococcus villorum].
ACCESSION   WP_010751097
VERSION     WP_010751097.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1177)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1177)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1177)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1177
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..1177
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=138059
     Region          4..1159
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mslqfilgta rkdhqamlid eavdwlaedr nhqvfflvpn ynkfeqeqei laqlrkksgk
       61 safsttnvqv fsfyrlawyl lqqttllsgn eltesgsami lrqileknee nltifrgein
      121 kkgfikqlqe lynelqigki apedlvfsqp tespkeenqq lkmkdlqlif tafeeellkr
      181 alqvedalti lanymqtqem sevkfivsgf trvnaqeyql lqvmmekgrl vvdllldrpy
      241 itempelltl fhetgklyfq lissakerki pvfvekyapa hslpfalqnl qkmwedtssn
      301 kkikpiklee qealkvweae nateevrqla veirrlvsee hyryrdiqil tkdmgfygnl
      361 iqpvfkemai pyyideeqlm enhpliewin slfsldryay rlndimrffk telficeedq
      421 tldleswrkq rnqfrtkldm tenvalayny qgtywtrekd wqfvsydfea eqledvqqle
      481 nysneirhff kekvptffee ikrcktgqeg atvfyrflis sgvqqqllfw rnqevergnl
      541 aaarnheqtw galidlldey sliygdtdfd wslfqeiims glenlsygki ptaidqvlin
      601 rlelvranqa kitfaiglnd qvfpdrketk glltseereq lntrladekf lfdpakenlt
      661 feplqaylvf ssaterlyls ysqsydtntl kmspylrrih dylgvsierk ehlllesdpd
      721 chvgtyrsgi ntinhiyria keekkkipvy wlelrerilq skwrnfalrv fesqdhlnlp
      781 vslpqkmaee lygkdiytsi srlenfynce ykyfvqfglk lkermvyglt paatgdfyhe
      841 sldrffkllf snqlslvems ekqrkeftek vlqevfgelr feildssarm nyiryqlgqt
      901 iqkvawalqk qskntgmkpl qteilfgqia gakgipglel plnnggklhv rgkidrvdva
      961 veqadtwlsv vdykssgrsf dvteayygma mqlltyldva lmdavrltgk aavrpagsyy
     1021 lhvhnpiltd tkeieketlk kfsydgifvd dpqllevldh sleakensli ypvkknakee
     1081 yqkgsfskek fyseeelqlf mahnranmrl agekitsgei klnpaykdke rlacqfcpfr
     1141 sictfdvmlk ennyhrlekl nkeealrrii krseeee
//
LOCUS       WP_010751182             436 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            villorum].
ACCESSION   WP_010751182
VERSION     WP_010751182.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..436
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45960
     Region          14..420
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 meketqngka avlglqhlla myagavavpl ligtglgfnq eqmtylisid ifmcglatll
       61 qltvnrffgi glpvvlgcai qavaplilig snegvgaiyg siiasgifvv lvagffskik
      121 rlfppivtgt vitvigltli pvaiekmggg sataanfgdk tnlllafvti alivgvqmfa
      181 kgfirsiavl iglvggsila almgqvdlsa igqapvfhvp qpfyfgkptf diwsillmii
      241 isivsmvest gvyfalgdit gkkvgeeelk kgyraeglav vlggifntfp ytgfsqnvgl
      301 vqlsgiktrk piyfsaifli ilglfpkiga laqiipepvl gggmlvmfgm vavqgirmlm
      361 evdftndknl liaavsigfg lgfnimptlf sqlpqtvqmf tgngivmssv taiilnlvfn
      421 glkkdekiik kalmdk
//
LOCUS       WP_010751188             318 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus villorum].
ACCESSION   WP_010751188
VERSION     WP_010751188.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..318
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35900
     Region          1..246
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkkyqwgiig lgtiahkfae tfdqetsela avasrtseka knfaeryhip kaygtyqell
       61 mdedidivyi avpnrqhiqh ilqalhankh vlcekaitmn kveldeamrl aeeknlilae
      121 amtifnmply qqlrslmdtn klgalkmiqa pfgsykepdp tnrffnpela ggalldigty
      181 avsfarffls sqpevmastm ipfetgvdeq sitilrnken elatvsltfq akmpkvgiva
      241 fengyltisd ypradraevi fndgtrewie sgstaqamny eianmvkiik gelpnrslfl
      301 tkdvieildt mqkiwqnq
//
LOCUS       WP_010751216             218 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Enterococcus villorum].
ACCESSION   WP_010751216
VERSION     WP_010751216.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..218
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23850
     Region          2..>190
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mkklklftdl igiifgaaiy glavtginip akladggvtg ialllnnlfg fapsitslif
       61 nlplllislf ifgkqaflrt iigtfslvff lhlweglhih favqsllins lmtgvlsgig
      121 cglvfrfggs tggtdiiyqv fekyfqikig kslflvtfgi livsllyldi ihfiytlvsc
      181 silsytlnki kylditnpfk fissarenet iksfdsae
//
LOCUS       WP_010751295             773 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus villorum].
ACCESSION   WP_010751295
VERSION     WP_010751295.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..773
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=85059
     Region          3..654
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(293..295,358,377..379,404,456..458,502,505,508,527,
                     530)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(587,591..592,594..595,620,623..624)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
ORIGIN      
        1 mngltqeevn qkialgqqnd yqedaskstk qilsdniltl fnflnfgigv cllwvgaysn
       61 maylaiiavn iiigiyqeih arnlvrklsi vsqsevqvir dgkeqsiatt qlvlgdivki
      121 gageqipsdl kvisgraean ealltgesdl ivkemgdell sgsfltsgsv faetirvgad
      181 nyavqltnea kthkaihsel vdsirkvskf tsfviiplgi ilflealfir dasiklsvva
      241 saaallgmlp kglvllisia lttgvtklak krilvqdmys ietlahvdtl cldktgtite
      301 gkmslqrvep lhsvyekaip eimgtyltes sdnnltmral rdyfelsnry tvtkklafss
      361 drkwgamefp elgvvyigap erlvekdqlp eslmtaqang frvlmlgiap gqqlvegkpq
      421 gvepvalfei ddpirknaee tlaylhdegv dlkvisgdnp ftvsniarra glpnydsyid
      481 lstlteeesv rkavheytvf grvspqqkkl lvnelkesgr tvamtgdgvn dvlalreadc
      541 siamaegdga trqianlvll dsdfttlpev lfegrrvvnn vtkvsgiffi ktiysfilsi
      601 lcaitaigfp fipiqitlid laiegypsff lsfeqdkrki tyrylptali talpnallvv
      661 lniivvyllg kvlpftalqt ttlmyyllig iscmavikac ypfnplrifl atttvigiyv
      721 aamlfhhlle vdlglgnawt yfvglmiini ilrllywkan iqnhllnkfa aak
//
LOCUS       WP_010751301             395 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu [Enterococcus villorum].
ACCESSION   WP_010751301
VERSION     WP_010751301.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     gene            1..395
                     /gene="tuf"
     Protein         1..395
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43100
     Region          1..393
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makehydrsk phvnigtigh vdhgkttlta aittvlgkkg lanpqdyasi daapeererg
       61 itintahvey etdkrhyahi dapghadyvk nmitgaaqmd gailvvsatd gpmpqtrehi
      121 llsrqvgvky livflnktdl vddeelidlv emevrellse ygfpgddtpv ikgsalkalq
      181 gdpdaedaim elmdtvdeyi ptperdtdkp lllpvedvfs itgrgtvasg ridrgavrvg
      241 deieivgikp etqkavvtgv emfrktldyg eagdnvgvll rgiqredier gqviakpgsi
      301 tphtkfkaev yvltkeeggr htpffnnyrp qfyfrttdvt gtivlpegte mvmpgdnvti
      361 dvelihpvai engttfsire ggrtvgsgiv teiea
//
LOCUS       WP_010751329             889 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus villorum].
ACCESSION   WP_010751329
VERSION     WP_010751329.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 889)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 889)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..889
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=96622
     Region          5..886
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 menkeqaqrt vyketidslm qktqssadgl stsqakekle rdglnqlkea pkkptwklfl
       61 etfkdamviv llivaliqmv mgdyieffvi favlmlnsvi sviqtkkaeg slealknlsa
      121 pdarvirdgk ektipanelv vgdivlldag dyvpadgrll eagslkvdeg mltgesvase
      181 kevtsitqtv pigdrvnmvf sgtiitygrg kflvtatgnn teigevagll estteqvtpl
      241 qrgldkfskk lslailglsl vilgiqlfri ylgegtgdlt adivsavmfa vavavaaipe
      301 alqsivtivl slgtnkmakr haiirklpav etlgstsiic tdktgtltqn kmtvvdyyla
      361 ngstgdftnd ptkwtdderr lieisvland asisedgtkl gdptevafid fseklnqpyq
      421 eirnnyprqa elpfdsdrkl mstahninkn qylfvkggpd ivfarskkvl ldgevvpmtd
      481 elmqkfkeqn eafsnkalrv lafayrpien inlsfededd lilvgllami dpprdevtqa
      541 vkearsagik timitgdhkt tavaiakeig ifangdqalt gteldelsee qlneilekvt
      601 vyarvspenk irivrawqtk ghisamtgdg vndapalkqa digiamgtgt dvakdaaamv
      661 ltddnfasiv savevgrnvf dnikkaisyl fsgnlgaiia iifalvadws npftalqllf
      721 inlvndslpa ialgtekaep atmkrpprdp nsgiftdktl isvtyrgvli gisvifsqwl
      781 gmqhspefgv amsfstliwc rtlqtfpars ntqtaiqagf fsnrsvllav vvcsalyclt
      841 mipglkevfs ipeafgltev ltcmgialvt iilmeitkli lvkvqkeqv
//
LOCUS       WP_010751337             239 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus villorum].
ACCESSION   WP_010751337
VERSION     WP_010751337.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..239
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27627
     Region          1..227
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mpkyeeianv lrerirskey ppnsllpnqv clveefgasr mtikkainil ameglvysqr
       61 gsgtkildhp fiekdtspan eyeglshqmk rrqrlltsqi iqfdvefpap fiqeklmiga
      121 eqpvynihrl rilenepyil ehtfmpvhlv pglkkehllt siydylhqel nlhfagayra
      181 isadksttfd qeylncaktd pvlevqqvvy lkdgqpiefs tsrnrydvrn yslldvrsn
//
LOCUS       WP_010751388             295 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Enterococcus villorum].
ACCESSION   WP_010751388
VERSION     WP_010751388.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..295
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31807
     Region          1..284
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mklgfigtgv mgsaiafhlm naghevtvyn rtksktdeli kngarwadtp kevakdsevi
       61 fsmvgypqdv eeiyygdagi faadvkdril idlttstptl aekiaktake kgakaldapv
      121 sggdlgakna tltimvggek ntyekvlplf rvfgstftlh gtagkgqhak manqimiagt
      181 mtgmtemlay askanldmek viatlsggsa anwslsnysp rilredytpg ffvkhfikdl
      241 kialdeankm slnlpataqa lklyeqladq gfendgtqal iklwwpagkn pekks
//
LOCUS       WP_010751398             144 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus villorum].
ACCESSION   WP_010751398
VERSION     WP_010751398.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..144
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16420
     Region          16..144
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mrvvqtkdtl ndiyldavri rnqvfvveqd vpltreidkd eahcvhfvly sekkqplgtv
       61 rllplengkm klqrmailln yrhqglgkil vaeaesfakr qgyntillga qstakhfyek
      121 lgykaygelf edagithism kkel
//
LOCUS       WP_010751471             427 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus villorum].
ACCESSION   WP_010751471
VERSION     WP_010751471.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..427
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48358
     Region          8..403
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnefvqafpq twqekwqnkg fsepsliqql afnalkekes mvgisptgsg ktlayllpll
       61 lnvskgeghs llilvssqel aiqvaevtre wakelelnvq slvgganvkr qieglkkhpe
      121 ilvgtpgrvl elmktkklka hqlqtivfde adqllddgnr klvvqilhqa pvdyqfvffs
      181 atadrsidki neitnakipi vdvtkednst kgqkhyflrv psrkkeeylr rltyvdgfhg
      241 lvffnqlsel gmmeeklqfr gvsvgslasd qnklvrkaal eqfknkklta lfttdvaarg
      301 ldihhlpyvv naevpltees ylhrsgrtgr mgkdgmvitf vqentirdlk rltrnmtvei
      361 eeiflhsgql vtalpekeel aiekkqhkna pfvpskkekk taekdkllkk ksknkqkkqk
      421 nkgarrk
//
LOCUS       WP_010751513             323 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus villorum].
ACCESSION   WP_010751513
VERSION     WP_010751513.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..323
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37083
     Region          31..232
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mfvetfsfdk tahasltvyl heekpefsrv gkrpfvlvip gggynfcser egepialqfl
       61 ahgyhagvlr yhvgehrhfk kaledgekal akidalaqdw aidtdkvavl gfsagghlaa
      121 amsnllerkp slcllgypai lksfsevmqi dapslettvs hntpptflfs tfednvvpie
      181 nslrylvale enevpfetmi fqkgkhglsl asewygakee mvdqrfarwf nsctewmeln
      241 wnqpkqdnen rkiserpikv fwrkatsrel ildyfphwkd ksrynlvknl sftdlanmfp
      301 erfqekeleq lfkklalinn env
//
LOCUS       WP_010751534             255 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus villorum].
ACCESSION   WP_010751534
VERSION     WP_010751534.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28222
     Region          1..227
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnkmievkhv sksygnklss akvldnisft vaegefvgim gpsgagkttl mnilstislp
       61 tmgsvmiqgs eitkmknsel sefrrkklgf ifqefnlidt lnakdnillp laveritkee
      121 mekrvlrvaq lldiedilkr ypdelsvgqr qriaaaralv irpqvifade ptgsldsksa
      181 tellnylttm nqvekatill vthdpytasy cnrilfikdg vifsevvrsg trneffervi
      241 dmqatigggg klnal
//
LOCUS       WP_010751550             361 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus villorum].
ACCESSION   WP_010751550
VERSION     WP_010751550.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..361
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41134
     Region          1..344
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mgkpiisfdq vvkryddeti lkkvsfeleq gkfytllgps gcgkttilri iagfteateg
       61 emyfegkrln dvpankrqvn tvfqdyalfp hmnvfdnvaf glkikkmnkr diekkvkdal
      121 rmvqlpgyen reisemsggq rqrvaiarai vnepkvllld eplsaldlkl rtdmqyelre
      181 lqqrlgitfi fvthdqeeal amsdeifvmn kgkiiqsgtp vdiydepinh fvadfvgesn
      241 ivngvmiedn lvefvgkkfe cvdggmrpne pvevvlrped ltittpdkgk lvvtvdtqlf
      301 rgvhyeivcy deqqnewtvh stkkakegsk vglsfdpedi hvmrfnetee efdarldsye
      361 e
//
LOCUS       WP_010751563             306 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus villorum].
ACCESSION   WP_010751563
VERSION     WP_010751563.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..306
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35398
     Region          1..226
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkigvigvgn iaekaylpty aknqgivdfy fatrnketkk rihamygfnh lyetldella
       61 qnieacmiha atkvhytlak kclenhihvy idkplsvnln evrelqelad knqvilmvgf
      121 nrrfapmvdr lkkvpdkrli qlqknrvaaq ettefviydl flhlidtavy lldepilrtn
      181 yqiretkeyl dfailqleta hqtailtmdl asganteryq itsrngiyev selteltiqq
      241 apelkietfg dwentlvkrg fepmiqaflt eikkekpdln alkqqqivqs halceemlik
      301 hmrqqm
//
LOCUS       WP_010751574             256 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            villorum].
ACCESSION   WP_010751574
VERSION     WP_010751574.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..256
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29100
     Region          1..247
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mnqqkrlmii merlekeksl tlqdimqltg vsrdtarrdt ikltdsnlvi rtyggislan
       61 sfnkidgylg rtdqelqvkk qiakeaskll lekqtvyldv sttisllpqy lanrninlav
      121 tnsidiadqf lkttsiptti lggtlnresr svtggypiwe ltkyrfdssf lscaginnqg
      181 iyyaheedia mkqavreksn kivllcdhtk inlshnylvy sfeeidylit dkkipeelvv
      241 rigkskiiyt kensyd
//
LOCUS       WP_010751628             695 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus villorum].
ACCESSION   WP_010751628
VERSION     WP_010751628.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..695
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78939
     Region          14..632
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mthlkklcqn rlfivltasf ffwlktifay yvdfslgveg siqyfilwin piattllffg
       61 lalyvkkikp alflllfidi lntlllylni ifyreftdfi tiksvlgfsk vsqglsgssf
      121 slmkphdvly wldilvfigl liwllvkkip inspavskpi amavsclaal ifsgnlalse
      181 anrpqllqrt fdrsyivkyl gidaytiyda iktgmtnsvr ahassngidd vlaytkkhya
      241 tpnpetfgla kgkniivlhl esfqqflinm kvdgqevtpf lnsiyknqst isfdnffhev
      301 gqgktsdaen mletgtfglp qgslftelgs dnvfqaapai lsqqqgytsa vfhgnvasfw
      361 nrdhvyknlg ydnffdrsyf krtdetlgyg ildkdlfres aqylehlqqp fytkflsvtn
      421 htpyytddkn fdfpslntgn stvddyvrta hyldqsleqf ftylkksgiy qnsmfviygd
      481 hfgisntdnk dlatalgkda dtwdaydnaq lqrvplmfhi pgytkgeikh tyggeidvlp
      541 tllhlvgidd knyiyfgtdl lsdqhdqvva frngnfvtpd ytvlngktys nqtgeiidpk
      601 tagiqkeiek eqeqvknvls lsdklnqenl lrfyvpegfq tidpkkynyk neaekneaek
      661 neaieqqkgn kstsvysrng nktttnlyps ddltk
//
LOCUS       WP_010751621             357 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Enterococcus
            villorum].
ACCESSION   WP_010751621
VERSION     WP_010751621.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..357
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40233
     Region          1..342
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mielqnisvh fyqkekvira veevnlsiak gdiygivgys gagkstlvrv mnflqkpteg
       61 eviihqtnlg klspkelrke rksigmifqh fnlmenrtif dnvdfslkyt gkskqerrqk
      121 vnellelvgl eektssypsq lsggqkqrva iaralanepk vllcdeatsa ldpkttqqil
      181 kllkklnrql gltivlithe mqvvkeicnk vavmengrii engssvqifs hpkeeltkdf
      241 irtathldqa lekiqehevf adqlankwli elsyvgtqtn epliaqlysk yqvtanilyg
      301 nvewlqetpl gslivtlage tiqkqkaldy lkrlgvrvni lqkhesqdai klieggv
//
LOCUS       WP_010751631             443 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus villorum].
ACCESSION   WP_010751631
VERSION     WP_010751631.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..443
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=50211
     Region          13..369
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(16..17,20..21,57,60,118..119,179)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(116,119,208..214,243,270..275,302,327..331,333)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mldyskepin dyflidiksf yasveciern ldplttplvv msqadhtggg lilassptak
       61 kkynitnvsr prdlpqpypk elyivsprmn lyiqrnlevn nvfrkyvade dlliysides
      121 ilkvtkslnl ftkaktrser rrqlaklike qvqketglva aigigdnpll aklaldneak
      181 nneefiaewt yqsvpekvwn isemtdfwgi gshmkkrlnh kgimsikdla nwdpyalksq
      241 lgviglqlyf hangidrtdi aippeptkek sygnsqvlpn dytrkdqiel vikemaeqva
      301 irirqhnckt gcvhlsigts iletrpgfsh qmkvpvtnnt kelqnyclyl fnkyyegqev
      361 rhvgvtyskl fytdslqldl fsepqkqidk enldkiidli rqkygftsiv hasslldgar
      421 sikrsklvgg haggnggmmd dgv
//
LOCUS       WP_010751639             356 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus villorum].
ACCESSION   WP_010751639
VERSION     WP_010751639.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..356
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40034
     Region          1..355
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mievidlkkv fdngfealks vdfqiekgdl vcllgpsgcg kstilnliag llspshgdir
       61 fngesvvrte pkdrnigfvf qnyalyphmt vlenimfplp vgenkikkae akkisqeymk
      121 ltnieelqdk kpgtlsggqq qrvaitralv qkpevlllde plsnldarlr lkireeirrl
      181 vkevgittif vthdqeeals isdkiillne giiqqndipq nlyldpanlf vanfignpii
      241 ntlpievvng kiihsefefp lstldttrlk ksladghyvl girpedvfpt nqglfeakis
      301 gieligreqi lnfmlaskrl ksivaieemm eegavfsfdf qykkmfifdd kgervy
//
LOCUS       WP_010751649             335 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Enterococcus villorum].
ACCESSION   WP_010751649
VERSION     WP_010751649.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..335
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37525
     Region          5..313
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(33..34,37,88,103,106,136,169,274,277,313)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(240,251,265,274..276,279,301,305)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mkfgafgevm lrltppehlm leqthtlrma ytgtgvnlvg nlahfdmesy lltalpdnrl
       61 gsaalanlks igvqtkyviq keqhigtyfa emgygvrpte vtyqnrkhss fglskeedya
      121 iqefintvdl vhicgislsl sdqcaqtais lakrahacgk kvcfdfnfrp tlnqekdkks
      181 klkkryqeil pyctilfgsi rdliellews svdsaldepi ryiqsflahy giewfagtkr
      241 itqdgkkqlk gylitlnetv etafydlfil drigagdafa agillgygek wslektvefa
      301 lgnarlahai qgdvplttrk qvlqlldapd idlir
//
LOCUS       WP_010751655             233 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus villorum].
ACCESSION   WP_010751655
VERSION     WP_010751655.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..233
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27377
     Region          7..231
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mkrtrvlyle vadkikedif sgkypvgtml pteneleemf qvskitvrka iellatdeyv
       61 ekksgrgttv lsnrpynrls kaasftqile nsrhevrket ielrkitlkk enplfsafgt
      121 tatyfkrlyy ldekpyiyfi hylpsdlldf krkefdqesl yrllmqkgyl idsfsddfsa
      181 iflskeeqem lntsstiaik rtrqsksihg emieyseaiy etnlhtyhid yet
//
LOCUS       WP_010751759             393 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Enterococcus villorum].
ACCESSION   WP_010751759
VERSION     WP_010751759.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..393
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43736
     Region          50..371
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 meeknkrtrp iswfwrwfln nqvvtallvv llillivflf tkvsylfapi wqflavvglp
       61 iilagilyyl mnpivdylek qkiprlysii glfvtvvali vwgsvviipk iqeqtisfid
      121 nfpqyvktid qklteilsdp lfnqfreqle sagdkfmssa gdmlqdisks tvqslgsfvg
      181 tiatifvaii tmpfilfyll kdgkrlapyf vnflptrmrk ptlkvlsemn aqvssyirgq
      241 ltvaftvaim fmigfaligl dyavtlgiia gflnlipylg sflaiipaif lgivagpaml
      301 ikvlivaale qtiegrlisp lvlgnqlaih pvtillvllt sgklfgivgv ilgipvyaaa
      361 kviithifew yttisslyee knkdgieisn sen
//
LOCUS       WP_010751688            1051 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Enterococcus villorum].
ACCESSION   WP_010751688
VERSION     WP_010751688.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1051)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1051)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1051)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1051)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..1051
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=121129
     Region          8..978
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mriihrdeae veshlihllg egrnqwvyrp dlkseadlwq nlrekithnn lseigehplt
       61 dkefetikte lllktqtpfd aakwlkgeng iariridred aslgsmslil ysnqdvgggl
      121 styevvnqia kkgssadard rrfdvtllis glpivqielk qvtakdgifq afnqvkkyae
      181 egvfrnnifs tlqlfvisne qttryfanam pkdmhrkflf swrtrdnkkv dnlyefykqv
      241 lnipdahrli anytivsedq dnktlmvlhp yqvhaiealf iaankhqsgy vwhatgsgkt
      301 ltsfvatkll arkagidrti mlvdrkdldn qttneftkfa sefntgissg nakanslivg
      361 tgtakelgkn lladananvv iittrqklda alkfarkqea kngtkrfekl igqhivfvvd
      421 echralsaen meeikqffpn stwygftgtp ifevnkkqaq gqlarttrdq ygdvlhtyti
      481 knaledgsvl gfqvehenti eptsldnriy qkmrevetya kyspeqinli idnmdqikke
      541 syidssvyes dehiqkvihk ifrpnnaytk fdfrngrptk sailttssie makkyyraik
      601 emtkasdwlq kefpdqpire grtmedpdfp rmaityside naekakekqd dmqqiiseyn
      661 eyyhtawnia eidryngdin nrlarkraef qqfgqqidlv ivvdrlltgf daptiqtlfv
      721 drnleyagli qafsrtnrty peknkglivt frkpatmesn vteatklyse akeesgliyp
      781 tyeeskarfe kaykqlqtfs vlpeitenap ieprvnyvka fqelnrayea lvtydnynee
      841 meesdilkeq vsileeqvgf yetvkgslvd kekddgdktd dfssiefysd nsirlydids
      901 syidqllgty aanssdvrke iekalkklnk tecvkevyrq ilnaidagei dvkedifaik
      961 rhffmqakdq kihefsnewn vstnelhyss iqyvigevpi pnmkgiiesk nfeaykekhp
     1021 aakpfqypqq mkrawrkvld etliplenel r
//
LOCUS       WP_010751802             660 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus villorum].
ACCESSION   WP_010751802
VERSION     WP_010751802.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..660
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=75972
     Region          15..646
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mrlkerells hlvdhqgefv tsqylasels lsdrtvrtyi hnlkglveek ggkitskqgy
       61 gyrlevlnkl nfdlflaqkg lilndeksap lisditdrkn yilnkllled atinlddlae
      121 elfisrssls kdiqeiklkl kpytltlvsk hglglwvkgd ernkrhfild tffgknytns
      181 lkkylinspf fqdisfeelt iiildeirea klklsdiiiq nlilhlvlsi krlkegfeik
      241 elgmiadish kveyqvarki vkrievfsef pfppqevsyl alhlmaksnh pvveenqklg
      301 selnqaiasl skslgyslna dyqlksglld hlkpmlirle rkrtlvnplt heirnnysla
      361 ygltkkhlgq mpvlqnyqmt ddewayltlh vmaamekvkd mqkvhaliic atgygsaqll
      421 knrvvnefek hitvtnikgy yeidnaclke adliissidl stmffpipvv hvsvflnded
      481 vakirktiqq ictknrqlir pqlsvekdqy kqnilleqtg eqyfkfydnk ttkvqvlqel
      541 trllsvneak dyphellkqi nhrqkmgqmi fsdsivvphp alpvgistki avalipkgmr
      601 wdeeknirfv flispsyien keitmmtkai vklvdclsfq ekilakptft nfsklflqlm
//
LOCUS       WP_010751775             222 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            villorum].
ACCESSION   WP_010751775
VERSION     WP_010751775.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..222
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24434
     Region          118..211
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mslkkysfas ifcyglvfls plifpyigiv hnisgvitat aimyvigaiv laffyfkqne
       61 plsieaiipk asllriilyg lvgifialii qaiavaletf lfgnsgpsen tqdiiqmilk
      121 apafilatti agpimeefvf rrsilgivek ytnfwvgavi ssllfafahn dghlliyffl
      181 gfffslqykt tgriwtsmit hvgmntlvvi vqlaiqkgli sa
//
LOCUS       WP_010751863             259 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus villorum].
ACCESSION   WP_010751863
VERSION     WP_010751863.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..259
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28475
     Region          1..254
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrkqkgmsii aglvfiflfl plliivvtsf gksstiqfpi defsldwyqk alssetfmns
       61 fklslfigig atllallvgv ptsyalsryh inskqlfksf flsptmipgi vvgyslfqya
      121 vikfnlpviq allighflis lpyiirvvgs smeqldfsie evawtlgctk trafmqvvlp
      181 nvssgifaaf mlafvnsfnn vpvsmflsgp gvtmlptsll syieyaydpt vsaisvmimv
      241 ltvflmfiie ktlglasia
//
LOCUS       WP_010751926             269 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus villorum].
ACCESSION   WP_010751926
VERSION     WP_010751926.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..269
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29723
     Region          3..267
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(7..11,41..42,198,220..222,224..225)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mklaaidldg tlldrsgkip qeniealqnf dqhggivtia tgrnsisakd vfeelgvggy
       61 lissngsfva emrkgtivkv lkrskielst lkrafflaqe akisiiasre tqddqltfde
      121 snlvkddpyy qhfnlqnqsf deitkllegp svsylklalt dkdenklqkl qqdlkkdgid
      181 svfsdphfle itpknvtkah slifladylg iepnqivafg dqendiamlk vsgtsiamgn
      241 akkqvkniad evtktneeag vayiinnyy
//
LOCUS       WP_010751931              66 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Enterococcus villorum].
ACCESSION   WP_010751931
VERSION     WP_010751931.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7056
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mnngtvkwfn adkgfgfita edgndvfahf saiqgegfkt ldegqavtfd iedgqrgpqa
       61 vniyka
//
LOCUS       WP_010751962             164 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside 2-deoxyribosyltransferase [Enterococcus villorum].
ACCESSION   WP_010751962
VERSION     WP_010751962.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..164
                     /product="nucleoside 2-deoxyribosyltransferase"
                     /calculated_mol_wt=18018
     Region          5..>107
                     /region_name="RCL"
                     /note="Nucleoside 2-deoxyribosyltransferase [Nucleotide
                     transport and metabolism]; COG3613"
                     /db_xref="CDD:442831"
ORIGIN      
        1 mkiyfaaplf aksdllynam lvkeirtlse didiylpqen eaindktaya dskmialadt
       61 qkvceselmi alldggtidp gvaseigvay akgipiigly tdsrqqggth pkkidalqev
      121 aenqfhyinl ytigliklng mivssekalf hkiktyldgg lfre
//
LOCUS       WP_010751988             433 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus villorum].
ACCESSION   WP_010751988
VERSION     WP_010751988.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..433
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=47528
     Region          4..432
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 menstiitkl ndmlspiaak ignqrhlkai ssgmmfslpf ivigsfflif anppidlnqy
       61 hpetanlfmk flagwkdfav anydlitapy dltmgiigli svfgiafsla seykinpsmn
      121 gmvasviflm vctpvkdgti nlhylgtngl fvaiiigllv vevnrifevk niklklpdtv
      181 ppmvatfint lvpllinill fygtnlifls mtnnmfpeti mniltpatni agslggflli
      241 vtlgnilwlf gingssiifp ivftlgmaqt glnaeqmang eemthlmnlq mfrisvlgga
      301 ggtlglvilm mrskvseyrt igklsiipgi csinepiifg lpivfnpila ipflitpvis
      361 llltyfaqki gligigfivd psftpffaqa ylssmdwrni vfclilifis aiiyypffkv
      421 mennktklvn eel
//
LOCUS       WP_010752011             625 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Enterococcus villorum].
ACCESSION   WP_010752011
VERSION     WP_010752011.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..625
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=72898
     Region          46..>620
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mkamiewldd pqvyrmnqmn ahsdhlfyan reevqkgssr iqslngrwkf hysknalerp
       61 vnffekefds sgfdqinvpg hielagydki hyintmypwe ghefrrppft tasqeetagm
      121 fsqaeynpvg sylttfrlke emkghsisvf fegveqamyv wlnghfigya edsftpsefd
      181 ltpyleeenq lavevhkrst aafledqdff rffgifrdvk lvargcnhlk dmwikpqvdn
      241 sfqngwvdih laienkttkg qlgvrildgt gyeifqkkvv lkdelsihip ieniklwdhf
      301 qpnlytaefe tfdetgitey ssypfgfrki eikdkviyln grrmiingvn rhewhpetgr
      361 vitiedmkkd letikkanin gvrtshypnq ipwyylcdka gvhlmaetnl eshgswqkmg
      421 afepsynvpg nilqwreivl draksnfetf knhtsilfws lgnesyaeen irlmndyfke
      481 kdpdrlvhye gnfpnpafee sisdvkscmy aspteiinyl eneaqkpfil cefmhdmgns
      541 lgglgsymel lkkypmyqgg yiwdfkdqai qvtdpitqqk vmryggdfdd kpsdyefsgn
      601 givfadgqek palqevryyy gkysn
//
LOCUS       WP_010752012             752 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-galactosidase [Enterococcus villorum].
ACCESSION   WP_010752012
VERSION     WP_010752012.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16044983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..752
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=86525
     Region          41..298
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          303..648
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Site            order(349,380,424,489,493,539,558,561)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          661..738
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mrpvneerra tlitfdtnek vfhltnqkis ylfqveesdi lahiyfgkki qkyhhhkkyp
       61 rrdrgfsgnv plnddrsysk dtlpqeysgh ggmdyrlpsi mirrengsnl ldlryekhqi
      121 qkgkltldgl pqayvkeene aetlivtlkd rqediyvdla ytiyrdraii trsvkvrnes
      181 essimlekaa sfqidftnsg rfdevialpg ahvkerqlsr qtisdgiksf esrrgtsshq
      241 mnsfivltnk yttefvgeai gihlvysgnh sfeiekdqin qvrlvggina ynfswelqps
      301 dhfqtpevil tysdqglngm sqvthqllqe rvargthqyq qrpilvnnwe atyfdftskk
      361 ieaivdeakt lgiemfvldd gwfgkrdsdq sslgdwfeyq ekltrglkgi adyvhqkglk
      421 fglwiepemi sidsklyrth pefmmqepnr vpaasrsqhv ldftqkevrm aiekqlrqll
      481 dsieidyikw dmnrslsdvy saslgkqnqg evmhryvlgl yemmgnltka yphilwegcs
      541 ggggrfdagi lhympqswts dntdaverin iqygtslgyp isamtahvsa vpnhqtgrit
      601 rlktrsdvam ggvfgyeldl tklsadekva vktqvdfykq irqtvqygdf yrlknpfeqn
      661 iaswefvskd qnevllflsr rlanaqpdfh evclvglvpe klyknqktgd iysgselmtv
      721 giyfpdfygd fqtelihfis idkgeevnes nd
//
LOCUS       WP_010752014             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus villorum].
ACCESSION   WP_010752014
VERSION     WP_010752014.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..255
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30340
     Region          5..97
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(6..8,22,39..41)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(53,56,60..61,70,82,86,92,96)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mqklytigev sellnvprst irfwdeqgli hslrqeenny rmfsiedifq iydinfyrkl
       61 dvpikqmkdl ygktmeelye tiaeteqrim reknnlqkkh eeilarkkql klmidqknke
      121 lsvekipfea ivivesedil dskaylenya sfggyfdfse gkemiygfct ekesqniqls
      181 kvvwqndpdk nyhrfllqve vnhtennnie evkkqltsqg yetgnvigqy lltnrtkegk
      241 dyeyyqawie tsnke
//
LOCUS       WP_010752094             365 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus villorum].
ACCESSION   WP_010752094
VERSION     WP_010752094.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 365)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..365
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42772
     Region          <145..361
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 mfyifkkkdq enftllnall isatvpyvvs llisvgvlnn yflgelkdpm yilleillel
       61 tvililrris klinlkyfly qysslsstll lsfyyltiql flyvaeyfka yenfifnial
      121 flimqiifla iflvkeikkk kheyenkile kqlldfkvya vqleanqlel rkfkhdyknl
      181 llslkqlate sdpkvfekri milekysecy ftsidwnynd ienikdiyle ilfiskvyfm
      241 kesdimfqie ckvpvdvvpi qvfdlvrilg vcldnaieaa iqtnnpfinv siikdrnqie
      301 fiiqnsaiet kegipkllka gystkkghsg lglsniedik kkysnvyvqy ektkeqftvq
      361 ivllc
//
LOCUS       WP_010752134             266 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Enterococcus villorum].
ACCESSION   WP_010752134
VERSION     WP_010752134.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..266
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29178
     Region          1..266
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mrqrvitavi alalflpiiw iggmaiefva allavvgvye lfrmkgltll sfegilsaig
       61 avilvlpker wffflpekts tfmlfyfivm illgtsvlsk ntytideagf pvivslyvgi
      121 gfqnfvnart egiavlifgl fivwatdiga ymvgrkygkh klspdvspnk tiegalggia
      181 salvvailyf llypskelfg hgmfvmlllt illsivgqfg dlvessikrh yevkdsgnil
      241 pghggildrf dsllfvfpim hlfgli
//
LOCUS       WP_010752206             169 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Enterococcus villorum].
ACCESSION   WP_010752206
VERSION     WP_010752206.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10628024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..169
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=19322
     Region          21..119
                     /region_name="bPH_3"
                     /note="Bacterial PH domain; pfam14470"
                     /db_xref="CDD:464181"
ORIGIN      
        1 mtldtknkki akqlkyaqeh lepgekvveg vfgayetksm gtdtikngvf latnkrlfff
       61 gkrtfgfdse sfpysnissf efakkamgyk isfyasgnkv nmkwisigdi nsfvnyvkek
      121 meaknhknie qnqsltspiq kmkelkelld meiitkdefe kkkkellgl
//
LOCUS       WP_010752320              96 aa            linear   BCT 01-JAN-2025
DEFINITION  putative quinol monooxygenase [Enterococcus villorum].
ACCESSION   WP_010752320
VERSION     WP_010752320.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..96
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11287
     Region          2..90
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mivinakfti kpekrnefle evkqlvestk keegclgyql yesidfenef mmienwrdlq
       61 aieghnqnpl lqklfknmsq ygnkkteini sktlee
//
LOCUS       WP_010752335             211 aa            linear   BCT 01-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Enterococcus villorum].
ACCESSION   WP_010752335
VERSION     WP_010752335.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..211
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=23904
     Region          24..210
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mkiippkisp klmnkdfsti fheedpilem cqisgdeytd sfldrprfyn tefdhchftn
       61 sdfsqiemvd vrfkncdlan vdmtkaaihr tefinckllg tafpeatikn vsfkdsllnl
      121 aslgdaklen vqfvhcllen adfyhckfkg vsfdqcelne atfhqtslkg vdlstskfet
      181 lsisieevkg cqvstyqalq fssllgliik e
//
LOCUS       WP_010752334             256 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            villorum].
ACCESSION   WP_010752334
VERSION     WP_010752334.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..256
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28949
     Region          1..250
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlmevrlkki kqiineqqha tmdelaeqln vskdtirrdl ikleeqhiir rthggavlve
       61 keasifdydq rstklhqvkt qlgkiaeski ktnssvifds sttvekviqy lfnkritait
      121 nslihatlla kmkevtisvl pgklhktqlf lhgadtiekl kqyhvdytll gvfalsnegv
      181 fihteeeglv krqmikqant viaiadhtkm gktgffkicd lseidllitd lmpnpslkqa
      241 lienhvacli ldkike
//
LOCUS       WP_010752359             224 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus villorum].
ACCESSION   WP_010752359
VERSION     WP_010752359.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..224
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26394
     Region          5..192
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtlnslqfqa fkairkkiiy cdlepgkkis eknleemlki grtpiresli qlrqqelvyt
       61 ipqsgtyvsk idlkaaenar ftrehlerqi mveccakldk qtsiilqtvl eeqekaaaak
      121 nerdffaadn lfheicfeia drreiwtwld dhnthlerfr wlrvltnglp wetileqhyn
      181 ifhallaksp eevnfltafh shmmlyeket vvgrfpeyft ttee
//
LOCUS       WP_010752384             173 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Enterococcus villorum].
ACCESSION   WP_010752384
VERSION     WP_010752384.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..173
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19695
     Region          2..170
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mgkivfygai sldgylatke dslqwlfdtp tggnttyeaf yqtidttimg rktyeeakki
       61 mgteslypek knfvfssnkk lllndaevvh depayfvkkl kentkqtvwv vgggkllkpl
      121 iedhlideww iqlapvllga gkrlfeegdy kerlklvdtk sfgafielhy vke
//
LOCUS       WP_010752392             821 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus villorum].
ACCESSION   WP_010752392
VERSION     WP_010752392.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   5  (residues 1 to 821)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 821)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18941298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..821
                     /product="cation-translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0043169 - cation binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /calculated_mol_wt=91053
     Region          27..682
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(318..320,387,405..407,434,486..488,531,534,537,555,
                     558)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(615,619..620,622..623,648,651..652)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
     Region          638..782
                     /region_name="Cation_ATPase_C"
                     /note="Cation transporting ATPase, C-terminus; pfam00689"
                     /db_xref="CDD:376368"
ORIGIN      
        1 mkifdrkpkd ersqinlary tpdykeglte kqvlervnaq atnktidtsf ktnkqiyfqn
       61 iftyfnlifi vlavllclvg syknltflpv iiantgiaiy qeirskkild nlnvlnsakv
      121 tvvrngtesk idledlvldd vvlletgqqi padgivlsgk lqvnealltg eadeitkevd
      181 dylmsgsfiv sgsayvrldk vgydsyisql takakkmgeg eqsemiasln klikwvgiii
      241 iplgitlfsq syffngdtik esvvameaal igmipeglyl lttialamsa arlakqrvll
      301 hdmksietla rvnvlcvdkt gtitenqmsv qklliatndq arqkadriee lisdyakmma
      361 ndnatmeaik eafphgsdke vlamlpfssv qkfssvtfsd gvyvlgapem vlrdhfltyk
      421 nefshytsqg yrvlvfgsyq gklekavlee eviplaylli anpirkeapa tfayfeeqgv
      481 aikvisgdnp qtvssvalqa gianadkyid asqlaeedyl eavekytvfg rvkpeqkmaf
      541 vqllkqqntv tmtgdgvndi lamkeadcsi amasgneati qaaqvallds dfsrmpeiva
      601 egrkvvnnie rsaslflvkn ifsfllsifs vlfaltyple psqitlislf tiglpsflla
      661 leenkqrikg kfifnvmeka ipggltdmtv vgmlviggvi lnlnktdvst astmlliavg
      721 flvlykicqp lnqfrgriil fcaggivfsv vflhtlfsis aispvsilll vilffaadsi
      781 frqythyiek ysrlkneqkk rtigewfkal fsveihnekn e
//
LOCUS       WP_010752403             486 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus villorum].
ACCESSION   WP_010752403
VERSION     WP_010752403.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..486
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53607
     Region          4..481
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mnnkqlrwft valiafnmvw gmgnvvnnya qqgisvvtsw llilaiyfip yalivgqlgs
       61 afkdskggvs swventtsnk rlayyaawty wvvhipylaq kpqailiagg wavkgngniv
      121 ntmsvqmvav isliiflafl ylstkglstl kvigglagta mfvmsllfil mavtapfins
      181 smefattgmn evktyipkfd fsyfttvsml vfavggaeki spyvnstrnp akefpkgmif
      241 laamvgvcav lgsvamgmlf asdnipkdlm angaysafqi lgnyygigns lmiiyaltnm
      301 vgqisalafs idaplkilla dadpefvplw lrkrnrkgtl vngylltgil vgiiillpif
      361 gikdmnelvk wltnlnsvvm pmrylwvfla ymmlnkaykk ftseykfvkn pkvgfifgaw
      421 cfaftafaci lgmvpkveya adpkawwfql isnivtpiil imlgmilpai arrdknkevk
      481 ktivea
//
LOCUS       WP_010752435             204 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Enterococcus villorum].
ACCESSION   WP_010752435
VERSION     WP_010752435.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..204
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23383
     Region          <1..190
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mykdnlkrgi gfllslvgii glspvflilc ilikldskgp iifkqkrigk nksyfyiykf
       61 rtmkvdtpqe ipthlllnpd iyitrvgrfl rktsldelpq lfnilkgema iigprpalwn
      121 qydlieerek yqannirpgl tglaqisgrd eleihqkakl dgyytanmtl wvdlkcffgt
      181 iisvfkrhgv ieggtgyrkk eeve
//
LOCUS       WP_010752525              91 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus villorum].
ACCESSION   WP_010752525
VERSION     WP_010752525.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 91)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..91
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10519
     Region          1..88
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 meikeeqnrl vllnddaqei gemtwsdagp dvmiidhtfv dpeyrvqkla eklvfsgvel
       61 arregkkiip lcpyakkefe rkseyqdvlh k
//
LOCUS       WP_010752536             396 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphoglycerate kinase [Enterococcus villorum].
ACCESSION   WP_010752536
VERSION     WP_010752536.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..396
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41869
     Region          5..396
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 makktvkdid lkdkkvlvrv dfnvplkdgv itddtrikaa lptinyvleq ggkailfshl
       61 grvkteedka gkslapvakr lgellgkevt fvpetrgeel etainnmkdg dvvvfentrf
      121 edvdgkkesk ndadlgkywa slgdvfvnda fgtahrahas nvgiastgip tvagflmeke
      181 ikfigeavee pkrpmiailg gakvsdkigv ienlipkadk iligggmtyt fyeakgikig
      241 nslveadkva lakdliekag dklvlpidnv capefsndve tqviegdipe glmaldigpa
      301 svklfadtlq gaktvvwngp mgvfemsnfa kgtigvceai anledattii gggdsaaaae
      361 qlgfadkfth istgggasle llegkelpgl aaindk
//
LOCUS       WP_010752716             428 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Enterococcus asini].
ACCESSION   WP_010752716
VERSION     WP_010752716.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..428
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47095
     Region          8..215
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd07732"
                     /db_xref="CDD:293818"
     Site            order(92,94,96..97,165..166,187,215)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293818"
     Region          <379..403
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cl23716"
                     /db_xref="CDD:451500"
ORIGIN      
        1 mdlkgktsvt fhsgiltigg tvievryeda riffdfgtef rpelgltees lgtlldnrli
       61 palsgvydsr lsgaeglaap teevetavfl shahldhskm inyldpaipl ytlketkail
      121 aslnrdeqfl ltnpfapgtr dmigleagse vvvgkihvti lpvdhdayga aalliktpda
      181 fltytgdlrl hgydrdltea fcaqakhtdl lmmegvsisf ddreeeadte tlpseqalit
      241 rlvelvaanp qrqltfngyp anvkrfaail ssaprtvvle anmaallqev lgldayyyyp
      301 tgatkisslk pelaisyetl ladqgqylwq vvdhfealqp gglyfhldae plgdfdpayq
      361 vfldllakqd iiflrlacsg hafpedldri iamiqpktlv pihtlkpekl vnpygerilp
      421 srgdtivl
//
LOCUS       WP_010752718             635 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus asini].
ACCESSION   WP_010752718
VERSION     WP_010752718.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..635
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=73664
     Region          1..>43
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
     Region          25..635
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mfahkrlnqi fhrlyieknc ssgilatefs vsertirndi telntdlkky qakiisrrnl
       61 gyellqkenv kqlfseidkq iissnqqlet sedrirqlll llllsehels ldelcttifv
      121 grttllgylr qlrlllasyn lkitskmnig ykisgdesai rqvisdqlie knfesyisqf
      181 sasekelfde idlenlatav asyfppnqfr isdynrknfv ihlaisilrt tkkhkletis
      241 nfftidkkiq samdellsti endyqitfdl qerywlynhl fsdlqqevhs nsqttkiyqf
      301 idqmlleine iigenllqde ilrqdlfvhf ssylslkell knkknpllpe ikknfsyafe
      361 lavlatnnsk wlsefefted digylalhia aaierkkels ihkkrvliic gqgvstsrli
      421 eamikkrfsd kleivdiisy atfqlsepqn vnliistipl qnqqipivqi dfldikqgme
      481 kideilaiee khlaltklfd asmfvinnqk ttrdtlinsi gnileeqevv nigftkkvle
      541 rehiaptnit dliaiphaid anikqtkifv yisqspiiwr ddktvkiifl lavaeedken
      601 lhtffeylsd lvenkklqqk ignsqnfemf lsslf
//
LOCUS       WP_010752730             490 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Enterococcus asini].
ACCESSION   WP_010752730
VERSION     WP_010752730.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..490
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52208
     Region          14..407
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(21..22,25..26,29,60,110..111,113..115,118,138,
                     141..142,145,269,272..273,276..278,281,309,313,365..366,
                     370,374,390,393..394,397..398,401)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mkketnvklv tvavfvatfm taiegtivtt amptivgslh gieimnwvfs iylltnamlt
       61 piygkladti grkpvfifgt llfvigsalc gmsnsmetli varaiqgmga gammpvalti
      121 igdlysmekr akvlgfnsta wgiasvvgpl agglivdtig whwiffinvp igailiamiw
      181 rylvepkrek tgkpmdlkgs ltlaatllal llafqflgdq gfsmpvilli vvsvfglayf
      241 ifvekraqdp vialnlfhsr lfvvvnlvaa lasgflmavd vyipmwmqgv lglpagiggl
      301 vlaplsilwm vgsfiagrwl vqksvkevli vflaviligg aglflipisa swlwffliss
      361 vlgvglggti vvctvtaqss vghdqlgvat sfntlartig qtimvsvfgi imnsitanal
      421 qkgsltkdpd imnklvnpqt akllpeklla plreilfsgl hgvfgvalll vaialvmtll
      481 iskksatike
//
LOCUS       WP_010752734             216 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Enterococcus asini].
ACCESSION   WP_010752734
VERSION     WP_010752734.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..216
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=24848
     Region          25..202
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(105,112,128..130,173,179,183)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mknklyyqfa gscfllvfvf ltyvvkfypq wlqgfdtqlt nlvrgpypdw hpfyltvtkl
       61 gnpsmiialt iflvallllt krylegiwls agfvivagiv nplikhaiyr qrptlehlvt
      121 etsysfpsgh satsmvvfgt lifilpgivk skywrlalqi llgllillig csriylgvhf
      181 psdilagfll slswlcftyp yyderrfiwr fqgkqr
//
LOCUS       WP_010752744             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010752744
VERSION     WP_010752744.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..277
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29987
     Region          1..275
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnvllqiqqn iqsytageqk ianyiienpe kllpmsvhel agrldvssat lvrfskmlgl
       61 kgftelkqrv saalttisst eslkevekgd svedikkkvs lrmnhmveqv nkvlaneqve
      121 qaaqlirnae nvftfglgas slaaqdisqk fsrigkhclv ntditlmats mtllkesacl
      181 iaisnsgeta evvklsslae slgipvigit gqlkskvaak aqvvlmpssg esipmrtaat
      241 mslmaqlyvv dilfynyvan nfedsmsgiq qtkniei
//
LOCUS       WP_010752761             634 aa            linear   BCT 01-JAN-2025
DEFINITION  M13 family metallopeptidase [Enterococcus asini].
ACCESSION   WP_010752761
VERSION     WP_010752761.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..634
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71551
     Region          7..634
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mssllkddfy eyvngawlet aeipedkpat ggfqdlvdei drllmkefed fsqhpetipp
       61 grlqdavayy dlakdyesrd rlgaaplrpl lervtalenl edlnrqlvdw vleglplpfd
      121 vdvdqdmknt rfntffagpa gtilpdktyy dednaqgpql ldafgtmtra vlekldyske
      181 qaativseal afdrlivphv rsseenadys knynprtfde ftnysqffdl rsltlgligq
      241 epekiivtep dyftaldeia nptnfplmks wlliqvalaf tgylseelrv lggtysrqls
      301 gatapkpqdk aafylangrf sqvvgeyygr kyfgpkakad vehmvkemia iyqerlehnt
      361 wlseatcqka ivklgtlgih vgypekipaf ydrfhtkpks eggtlvgnar rfarivredr
      421 fskygqakdr eewemsaatv nayyhpflnv ivfpaailqa pfysleqsks anyggigavi
      481 aheishafdn ngakfdefgn mnnwwteadl aqfeklsqam iaefdglpya ggkvngtltv
      541 seniadaggl scalaaakke dqvsledfft nwakiwrska rpqyeqllla idvhapaklr
      601 gniqlqnidd fyttydineq dgmylapekr vhiw
//
LOCUS       WP_010752865             291 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Enterococcus asini].
ACCESSION   WP_010752865
VERSION     WP_010752865.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..291
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=32145
     Region          1..289
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mkkwftalph hdyaqkfsfs vvyallasis vnvfyqpgqi yssgitgiaq ilntlshnlf
       61 gldipvslwl lllnlplfif gwfaighkft fftgitvvlt slfmqimpee vlstdpiica
      121 ifggavmgag igyalrngls sggldfvtia mrkrtgrtig slsiffnili maaagvlfgw
      181 qyalysaiai fvsgkvtdav ytkqkkmqvi vitrhpdrvi hnvqkslrrg itiineaega
      241 ynhdkqtvll tvvtryelpi lrqamksadp kafvsiadnv qilghfyeee l
//
LOCUS       WP_010752887             353 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Enterococcus asini].
ACCESSION   WP_010752887
VERSION     WP_010752887.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..353
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39271
     Region          205..>337
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mtlyqkmqls pavlrqhire sfaqekkqyv talvlrsvll llfaiayisi ftslfgqkns
       61 yvgvgslcml lsirfvnygy hiidslvalf fisslylins fflaglpvil yfvvqlasls
      121 fillmttthp eygnggvyaf syilitsntv sgqheilqrt gavylsflfc glvflqkhsq
      181 anrtirfhhi ckgyslhqtt yqwqlrlalg iafalsigky lgiprsmwmg fasmslllpq
      241 thqvlsrgfs rmmgvtigsv ifvlclhlfp iewvfllgpl agfclgltph ygwasilncf
      301 galsaayvll gilpagviri qnnflgilcg lgiallfqll qrkstkrvge sqc
//
LOCUS       WP_010752895             151 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus asini].
ACCESSION   WP_010752895
VERSION     WP_010752895.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..151
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17620
     Region          15..126
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mlnvkkykst dktiyhaalq lrdvllrqpi gksiyeedlt ieqdndfygi fqgeeligtl
       61 sffekrprva qltvfavkqe fqrrglgktl vafliadlrk rryrkiivda rsearffyqk
      121 cgftiekgpv inqklgvkdy qmkyviekit d
//
LOCUS       WP_010752900             341 aa            linear   BCT 01-JAN-2025
DEFINITION  LLM class flavin-dependent oxidoreductase [Enterococcus asini].
ACCESSION   WP_010752900
VERSION     WP_010752900.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..341
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38349
     Region          36..340
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mkkigflsfg hwmnqgslvk taqdsylqsi elavaaeqig ldgayfrvhh fadqigspfp
       61 llaaigakts kieigtglid mryenpymma enagltdiit qgrvelgvgr gspeqvldgw
      121 kyfgydysee dvkevarert leflkllegh hfaepnpqpm fpqapgklrl epyseglrqr
      181 iwwgagsket aiwaaeqgmn lqsstlvnye skepfhvqqa nqlraykeaw kkaghtfepr
      241 tlvtrsiqpi ttdfdrqlfg hqdeelkyds vsflayhqnp tifgktfage pdkiakelae
      301 deaikeadtl litipntlgv dynihlldti lkdvapelgw r
//
LOCUS       WP_010752918             241 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010752918
VERSION     WP_010752918.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..241
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27799
     Region          3..235
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mayfqviate lrkkivdgty pkdsrlpnqs tlakefrtsr vtiqralntl qvegliegrq
       61 gsgsyvkgpe slfdydasiy ggmtrklghl gnlkneiisf evsfpnekeq eklrikkndp
      121 vydiirlrif egeplaleyt impvliipgi teeilkgsiy ryiqqdlnkp fgsshrrika
      181 drpdtydqky lhceptdpil efeqivflkd gtpfeysqtr hrfdkgdvtv tyqssrhdyh
      241 l
//
LOCUS       WP_010752959             241 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Enterococcus asini].
ACCESSION   WP_010752959
VERSION     WP_010752959.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..241
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27961
     Region          2..228
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 miqaivfdvd dtlydqqqpf rnavyqivpd fqaedmhdly irfrvhsdei fpkvlagewe
       61 lvtmrnfriq qslkdlgypt idddtalafq aiyeneldhi tmhdevkktl dylkklgvpm
      121 giitngptdh qfkkikqlgl fkwvrpehil isqatgfqkp eadifqlaee rfdlngettl
      181 yvgdsfendv vgsksrnwqa lwfnhrdrcl pegaeaiydi elhdfdqlyp ticnictplt
      241 v
//
LOCUS       WP_010752984             200 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010752984
VERSION     WP_010752984.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23043
     Region          5..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mngfekrtqq kmqtikdtaf allnqpagvd glrmdtlake agvskatifk yfhskekliq
       61 qvfmdfldrm gaesmtflsq dlpfeeklma lakvkiqyld tvdqqffldl maqysqkada
      121 elatkmhayn qryydvmvql lqqgrkegki dlkysdefll lylesmvqgv sdpaiyqkin
      181 vhyaeywaem llkalaptek
//
LOCUS       WP_010753018             284 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Enterococcus asini].
ACCESSION   WP_010753018
VERSION     WP_010753018.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..284
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=30688
     Region          3..280
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mnkkivilad sgsdvpqdfc eahdvftlpl kviypdreyt dkvditsedv iarmpqeipk
       61 tslpdgasiv acfdeikaag yeqviavtis sglsgtfnmv rmmakdydgl eifvldtkni
      121 giasglqair avelvdsgle faaicqtlen evfknkvffn vatleylqkg griglvtaif
      181 gtalklnpii scneegvyyt vaksrgrkks lakslelvkd fagsskkyrl avahagakee
      241 aqammerltt llpnaveryf geispalvvh tgpgllgvgi qvld
//
LOCUS       WP_010753058             363 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus asini].
ACCESSION   WP_010753058
VERSION     WP_010753058.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..363
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41183
     Region          1..346
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 maksiisfeh vtkryedted avlkdicfdi eegkfytllg psgcgkttil riiagfseat
       61 agdiyfdgqr indipankrq vntvfqdyal fphmnvfdnv afglkikkls kaaiqekvme
      121 alrlvqlkgy ekreisemsg gqrqrvaiar aivnepkvll ldeplsaldl klrtdmqyel
      181 relqqrlgit fifvthdqee alamsdeifv mnkgkivqsg tpvdiydepi nhfvadfvge
      241 snivkgtmie dnlvefvgkq fvcvdggmrp nepvevvlrp edlnittaek gklvvkvdtq
      301 lfrgvhyeii cydedgnewm vhstrkakeg sqvglyfepe dihvmrfnes eedfdarles
      361 yee
//
LOCUS       WP_010753065             644 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus asini].
ACCESSION   WP_010753065
VERSION     WP_010753065.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..644
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72856
     Region          6..530
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          569..641
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 millqanqia rlfgaevlfq niqleiadha riglvgrnga gkstllkiia gleapdegai
       61 aknktatigy laqdtgltsd ktvweemlaa fdalrqqerr laeleqaiaa stpntpeair
      121 ilkeydqlqh dflaangygy eaeirsvlhg fqfdesfynq tidtlsggqr trlalarmll
      181 qkpdililde ptnhldietl swlenylqny sgallivshd ryfldkvvse iyeisrhkmr
      241 hykgnysryl dlkaeqlqse wksyekqqee ihkledfvar nlvrasttkr aqsrrkqlek
      301 mermdkpqgd eksvhflfdi dkpsgnvvcq veaaaigydk evlaspidld irrkdsvalv
      361 gpngigkstl lksligelpf lagsahlgtn vsigyydqgq telnprktil qelwdehptt
      421 peveirnvlg gflfsgedve kpiallsgge karvalakla mnkenflild eptnhldidn
      481 kevlenalid yegtllfvsh dryfinrlas kvvelspegs klylgdydyy lekkkeeeel
      541 kellaqetap tttlsqgkqs fqnskeqqkl lrslqrkvtq veedlaklee tmgqlesema
      601 kpeiqadhla ltelnqqlee aqekqealle eweaaslele eyen
//
LOCUS       WP_010753067             119 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Enterococcus asini].
ACCESSION   WP_010753067
VERSION     WP_010753067.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..119
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12711
     Region          12..99
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(29,32)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 minvtdfetg ltqlqeapla iayismpncs vcvsvkpqlv krlgptgipl lhfdaaalpe
       61 vagsfqvlta paillyaqgk evdrqarfid fnrletevkn ylaagsapvd yaalfasee
//
LOCUS       WP_010753078             169 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Enterococcus asini].
ACCESSION   WP_010753078
VERSION     WP_010753078.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..169
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18196
     Region          1..166
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mltktnypsp lgqlilvsde tallglwfed qkyfgagfdl raipekqtai sdqvttwlde
       61 yfkgnapsse alplnpqvta yrqrvlqvlc qvpygqtity aelahrlskq gaatspraig
      121 gavghnplsi vipchrvvgs dgsltgyagg lerkiallkl egadfshlk
//
LOCUS       WP_010753085              91 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus asini].
ACCESSION   WP_010753085
VERSION     WP_010753085.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 91)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..91
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10254
     Region          1..88
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 meikeeknrm vlltddgqea gemtwsqagd dliiidhtfv ddayrghqya qqlvaagvem
       61 areknlkvlp lcpfakkefa ekpeygdvlr k
//
LOCUS       WP_010753107             325 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Enterococcus
            asini].
ACCESSION   WP_010753107
VERSION     WP_010753107.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..325
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34140
     Region          39..306
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mkkvakynli wlafilvsyg illvlynvgi vdlfidnalv niginvilav glnliigysg
       61 qfslghagfm aigaytgaif amqnptyggf flgmlvgall sgilalgvgi ptlrlkgdyl
      121 aiatlgvaei irilivnldg itngpagifg ipqfttwemv fafavltili vvnfihsgpg
      181 rgvlavrede iaaesmgvnt tkykvmafvv gamtasvagt lfagykqsvf pgdygfmksv
      241 diliivvfgg mgsttgavis aivlgvmntf lqdtgslrmi iyalaliiim ifkpsgllgt
      301 wefsvknilt kitgkgagsd atidr
//
LOCUS       WP_010753116             493 aa            linear   BCT 01-JAN-2025
DEFINITION  multicopper oxidase family protein [Enterococcus asini].
ACCESSION   WP_010753116
VERSION     WP_010753116.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..493
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=54645
     Region          63..493
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mikqkwrila gvvllvgggf flgknltqkq gttdsqgshg mmgqmmtdes aplqvseqke
       61 qklaipplle pteeegnhvt yritaqkgay qiksgkktqt lgyngdflgp virlkkgqdv
      121 tfitenqlpt etsfhwhglk lassadggph qviapgqtkt vnftveqeaa tlwfhphpmg
      181 ataaqvyqgl agllyieddh skqlrlpdey gvndfplivq dksfdqdnql nyqedttgdg
      241 iqgdtllvng tlnpyletee rwlrlrvvng snarnfdfsl segqpfyqia tdggllnqgv
      301 kltslrlspg ergeilvdtq qfrsgesfrl lanqntalti kingqkataf dsketlneik
      361 hvaqkdlqgl krqeitlkgm shmvsindqk fdperidlqa ktgtqevwev snvggmmggm
      421 ahpfhlhgvq fqiisrngqp pseneagwkd tvlvnpeeqv ellvtfdhpg lfmyhchile
      481 heengmmgqv nvv
//
LOCUS       WP_010753169             345 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010753169
VERSION     WP_010753169.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..345
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38304
     Region          25..341
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mldelkliea vapdilavlq erfkilqniy wmqpigrrnl aesmemteri lrsetdqlkk
       61 lqlievsksg mtltekgeaa ynglgkmmdq lfgmhrlekr ladhfgiarc vistgdsdrq
      121 rkiieefgdy lnealdfllp egnniiaamg gttmaivaer ltnlesekrh nlfvparggi
      181 geavnlqans vssvmamran gdyralyvpe qlspatyrsl lqepsilevl nlishancvi
      241 hsigralhma arrkmseeei lmlkqknava esfgyffnen geviykvpki gielnelqdv
      301 pvilavaggk skakaikaym knapkqtwli tdeaaaneil kgatl
//
LOCUS       WP_010753207             225 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010753207
VERSION     WP_010753207.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..225
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26056
     Region          4..215
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 milnlqgqay kairkkiiys elepgakise kelekalnig rtpirealiq lrnqelvyti
       61 pqsgtyiski dlksasnary vretlersil aecsakiddk dkkaleaill etenatarrg
      121 isdffqldsa fhrtcfeiag rgevwtwied hathfdrfrw lrlevteldw qkvtdehqal
      181 ydaivshdld elaflitlhl hmaideqeqv mdhfpnffte dsqiy
//
LOCUS       WP_010753221             229 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Enterococcus asini].
ACCESSION   WP_010753221
VERSION     WP_010753221.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..229
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23617
     Region          3..218
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 melfrkifge figtfmlvfi gtgmvvfstn pdpltiglaf glsitiadya vghgglsdgh
       61 fnpavtiamv lnkratikea vffiiaqfvg aiaasacvgg fgsalgleag tygqtdfpdi
      121 sagaafafet lisflfifvi lmvtskkygs kqmasiaigl tlgflvaial nltggslnpa
      181 rsfgpaifag gsalshywvy lcapilggii aavvakfmgs eqglteqda
//
LOCUS       WP_010753241              66 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Enterococcus asini].
ACCESSION   WP_010753241
VERSION     WP_010753241.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7371
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mikgkviwfn dqkgygfiag ddgheyfihh tgiimpgyrk lekaqsvefe sedtpqgkka
       61 fnlspv
//
LOCUS       WP_010753244             187 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010753244
VERSION     WP_010753244.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..187
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21318
     Region          1..>114
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrrkvytkdq ilkaaydvis tegfskftar niakkmgist qpiylefknm qdlkntlvet
       61 vmkdlhenaf pkphtgneli dlginyinfa renrnlyvsl yvdeygggel mhqfsydyfk
      121 nlvkrdpays hlnedqiall hestwitvsg iaslmssgii npteeeiikl ieraiestld
      181 skafkal
//
LOCUS       WP_010753287             236 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Enterococcus asini].
ACCESSION   WP_010753287
VERSION     WP_010753287.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..236
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25057
     Region          9..232
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 metvgyrrfr egvqacvptm mgylgigfaa gvvekgvgls lwqiaalsll vyagsgqfii
       61 cgllalnapi psiivtvflv nfrhllmsls vtsyfrgkgl wqtigigsll tdesygvltt
      121 alqaghkvsv awchglnvaa ylvwlvanvl gglfgqfltd parfgldfal tamflglwlf
      181 qvdlplkkrt sqsvrillav vvtlvvgmrl fsgeiaviaa tlvgcmvgll teggvq
//
LOCUS       WP_010753297              74 aa            linear   BCT 01-JAN-2025
DEFINITION  ferredoxin [Enterococcus asini].
ACCESSION   WP_010753297
VERSION     WP_010753297.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..74
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=8108
     Region          6..71
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mtslakikpe lciscglcav yapdifdyde egillfkeep eahqqfipqe qeaalrkaag
       61 kcpvrailme klad
//
LOCUS       WP_010753300             229 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Enterococcus
            asini].
ACCESSION   WP_010753300
VERSION     WP_010753300.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..229
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24596
     Region          <184..228
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
ORIGIN      
        1 mskrddlknd nqepweqpiy dtegedlgsr tqrrsnkngn kvflislvvl lvlciglimg
       61 fwmivtrdtd raavsestte tttaisstke sstkesstke sssesstves sssssetvps
      121 ssetepssse etpaaddtvq qadgtnngtt nndttnnatn ngnttnngtt nnqttqnant
      181 egdytlvrdg egpnqvaart gvsvdtlfql ngldpnnyml ypgqqlrir
//
LOCUS       WP_010753322             232 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Enterococcus asini].
ACCESSION   WP_010753322
VERSION     WP_010753322.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..232
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=25951
     Region          14..179
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mnptikrtln qwrngpyity sliaiqtivf llnyllpslq lqekgvmfgp fvayyhqywr
       61 fitpiffhfg lshyaintiv lyfigqqvea lyghsrflal yllsgilgna fsfgfnaigv
      121 qsagsstsif gifgaflilg vyfrhnpaiq gmvrqfalfv llslvfgmfd qsidiwghvg
      181 giigglllgn tialpnnpgr ysmhtriltg ivygflfvic lfyglkkygi lv
//
LOCUS       WP_010753411             243 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Enterococcus
            asini].
ACCESSION   WP_010753411
VERSION     WP_010753411.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..243
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26737
     Region          4..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mealiqvkgl eksfgkqqvl kgidteiqkg evvviigpsg sgkstflrcl nlletptkgq
       61 vifegvdita akndlytmre kmgmvfqnfn lfpnltvmen ltlapvkvkr qskseaeayg
      121 ehllkkvglq dkagaypqsl sggqkqriai aralamqpdv mlfdeptsal dpemvgevlq
      181 vmkdlakegm tmvivthemg fakevgdril fmdegiimee glpqelfeqp qnprtcdfls
      241 kvl
//
LOCUS       WP_010753446             592 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus asini].
ACCESSION   WP_010753446
VERSION     WP_010753446.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 592)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..592
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=67887
     Region          167..582
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mnqrkwikrf kntsfktqlq iaflvtillv llvtllmtlv wrnaylektk vsaykdisll
       61 akdtgeklta vedlslnvid sptlqslltd ftqqtdndts itlknqlvre vnqitrnnsn
      121 irnvyllspk keslisfids kkniinqlsv ddlirdlpdh pakgkwffsd tlsqgvyvrk
      181 ifasdnlsln higtviffvd ttffqlerqn faalaedsff lldyenalys panqvdaqnf
      241 itqydqiept lsesfgitkl sqdsyyyvta dspmdqgrfi ylipenqila dlyqlqwlfv
      301 liflpfllai iwgihkisnq ltrpitnlan qmlainetke lqslktlalp adpqeeiail
      361 ydsynimied intlikdnye mrilsqevef kslqsqldph flyntldsin wlaiannqsq
      421 iaemvtslay lfrkkidtns efvtlqdeld ivdayiriqk vrfekriefi slilvddlsl
      481 pvpklliqpl ienvfkyavs nmkttcqlvl svemaqdnlw vtvsdngpgf kphfsierdg
      541 giglkniqkr lalhygptsr lqiaksipfk ktvvkfnipl nksqsytake sl
//
LOCUS       WP_010753470             433 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus asini].
ACCESSION   WP_010753470
VERSION     WP_010753470.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..433
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=46687
     Region          7..431
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mnesnpivdk mllfankfss qrhitairdg fvtlipmtii asfwvlinnl ilsptngllk
       61 nvpaaarwmd lgnqvynatl gimalliamt igyklaqsyg eegliggvmg lvsylivlpa
      121 qvvltdvegk svtaaavmtq tqtsatgmfl aiiatlfsvt wlckftkmek lkirmpesvp
      181 psiaksfnvl ipaflvttil glievlivwv fatdiptiia kffqaplvas fqsigglvly
      241 vflsnllwaf glhgtfilgs igepimltai qenmdalkng ealpnivtkp fldafgwmgg
      301 ggmiiclvia imiaskredy rsitkvgivp slfnvseplm fgipvvfnpl lgipliivpi
      361 vtvtlayyat afgliaktsv lipwttppii sgylatngdw kasllqvili aigvliyipf
      421 vkmankaaqk eti
//
LOCUS       WP_010753494             212 aa            linear   BCT 01-JAN-2025
DEFINITION  RDD family protein [Enterococcus asini].
ACCESSION   WP_010753494
VERSION     WP_010753494.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..212
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24607
     Region          59..199
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mteqwnpdee qqsqtieptt kpktflnerk vlgrkkatde eqrklrkkwr pyeepketep
       61 gfpryfyagf wmrsfaflfd liciaairts tlglvyrlag lvdtgdyfgl ynlfsiaiyl
      121 ayftgltrfn hgqtlgkmvf glrvvslsek eltwttilmr etvcrfilmg fpwivgylpa
      181 afsknkqhlg dyfcetsvvt inlikafnqe lv
//
LOCUS       WP_010753536             253 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus asini].
ACCESSION   WP_010753536
VERSION     WP_010753536.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27731
     Region          1..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 meelltvanv kkvyqgrfha tpvealknit ftvaqgeyva imgesgsgks tllnllatld
       61 kptagsihlg dadfkaikeq eaaafrrdhl gfvfqdfnll dtlsvkdnil lplvltrlpv
      121 aqmeerllpl vnnlgienll ekypyelsgg qkqrvavara iitepellla deptgaldsk
      181 tseqlldlfq rlnesgqtil mvthssiaas hakrvlfikd glvfhqlyrg dksnqaflet
      241 isetmtallt kgv
//
LOCUS       WP_010753537             662 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus asini].
ACCESSION   WP_010753537
VERSION     WP_010753537.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 662)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 662)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..662
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74731
     Region          543..656
                     /region_name="FtsX"
                     /note="FtsX-like permease family; pfam02687"
                     /db_xref="CDD:460652"
ORIGIN      
        1 mfygklalsn lkknkraylp fllsmlflva intmvqlvvt nqgmkelpga gealqmfslg
       61 qwvilffsll falytnsfll kqrkkefgly nilglgkrel fhllfwesca sfalvillgi
      121 llglvltrls flllirfmal qsgfafqvnp sdlgwiillf avlflllfal nclqmwrmnp
      181 iellqgsktg ekmpkanwfm avlgivtlga gyyisvtiqd pidalllffv avilviigty
      241 clfmagsial lqmlkkrkgy yyqtkhfinv ssmiyrmkqn aaglasicil stmvlvtvat
      301 taslyfgqrd ildyryptdv aiemkeepte llekvhqkse aagvtlrnek qlitsdpilf
      361 lqksnrsfqv akqemgsmkd aamvtftdld nyqtlsgekp tldkgevlvf tvsgptpqkt
      421 inlsgqefti kenltelpgy edewegmvnv ylvvmpdwat iqnmlddwfa tagpdfaknr
      481 lpnyrvsfdf tapkgqrlaf angleteltn tyggfeegfs vnsrdafeen skqitggfff
      541 lgilfgvtft iatgmiiyyk qiseglddqd rfailqkvgm srqevksvih tqvlmvfafp
      601 llvaivhlaf afpiirnlli lfglvnwqlf llttvvvval fgllyffiyr itaksyyqiv
      661 er
//
LOCUS       WP_010753573             110 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010753573
VERSION     WP_010753573.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..110
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12219
     Region          3..103
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mketqmlkgl legcvlaliq qgageiygye lvqrlkasgf ttivggtiyp llqkleknql
       61 ikgemrkspe gpdrkyftlt tlgeqsladf qrqwremegk vnrllggnea
//
LOCUS       WP_010753645             792 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Enterococcus asini].
ACCESSION   WP_010753645
VERSION     WP_010753645.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..792
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=86175
     Region          35..675
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mttdtpsraa rnqnkksgkq ppkkngknnk pkkkrsvgti ifrvvaslfi lgmlaflggv
       61 glfwyyakda pkiddtnles avsstlyasn gdsyaelgae rretitsqev pqlledaivs
      121 vedkrfykhi gvdpiriigs aisnltsntt qggstltqql iklsffstka sdqtlkrkaq
      181 eawmaiqlek ekskqeilty yinkvymsng isgmqtaaka yfgkgldeln laqtaliagm
      241 pqapesydpy knpelakkrr divlytmken nkisekeyke avdtpvtdgl ieftnssqnw
      301 vkydgyvkev iqqvkdltgk nvytdglevy tnldldaqnr lydivntdqy vqypdsdmqv
      361 aatlvdthtg kvsaqiggrn idssvvlgnn lavntsrdfg stmkpvtdyg pafeylkdst
      421 gtriddepyt ypgtdikvnn wdlkymgnis lrtalsqsrn vpsvklldev gidkahdflk
      481 glgieyknmv isnaissnta qdgtkygvss eklaaaysaf anggtyykpm yiskivyqdg
      541 sydefnpdgt kameagtaym vtdvlkdvit egtgynaeip gliqagktgt snytdeelak
      601 lgissnvypd vmfagytpdf slsvwtgynn rmtpitndsn mvasdvyrnl mqyitrnstv
      661 sdwempedlv rvgselywrd tykapepess vtpsssssss ssvveststt esttsssses
      721 sttessssss ssssssesst ttpssstpes sttpssetpe ssseenpgnn nnqgqgngng
      781 ngnangdgnn ng
//
LOCUS       WP_010753671             112 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010753671
VERSION     WP_010753671.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..112
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12806
     Region          2..103
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 missdglrgy ndalilsvla egdsygyeis keirrrtkdv ylikettlys aftrlekkgy
       61 lhsypgevth gkkrtyyqlt tagrghlaek wqewqqtkni vdsfllpkgs nr
//
LOCUS       WP_010753683             593 aa            linear   BCT 01-JAN-2025
DEFINITION  V-type ATP synthase subunit A [Enterococcus asini].
ACCESSION   WP_010753683
VERSION     WP_010753683.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF003220.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK04192
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..593
                     /product="V-type ATP synthase subunit A"
                     /EC_number="7.1.2.2"
                     /calculated_mol_wt=65431
     Region          1..584
                     /region_name="NtpA"
                     /note="Archaeal/vacuolar-type H+-ATPase catalytic subunit
                     A/Vma1 [Energy production and conversion]; COG1155"
                     /db_xref="CDD:440769"
ORIGIN      
        1 meignivkvs gplvmaenmg hasiqdicyv gdlgvigeii emrgdvasiq vyeetagigp
       61 gepvhstgea lsvelapgil sqmfdgiqrp ldefiaqths nflargvqik aldhekkwlf
      121 eailepgaev atgdivgtvq etkiiqhkim vpvgvkgtlk avypgehtid etvfvittae
      181 gdkefsmlqk wpvrrprpvk eklnpdvpmi tgqrvidtff pvtkggaaav pgpfgagktv
      241 vqhqiakwad vdlvvyvgcg ergnemtdvm nefpelidpn tgeslmerti liantsnmpv
      301 aareasiytg itiaeyfrdm gysvaimads tsrwaealre msgrleempg degypaylgs
      361 rlaeyyerag kvitlgqegr ggsitaisav spsggdisep vtqntlrvvk vfwgldstla
      421 qqrhfpsidw lqsyslysne vgqyldqqmq vnwstlvrda mrmlqkesel qeivrlvgid
      481 slsakdqlll evtksiredy lqqnafddvd tftsrekqfq mlhniltfgq eatralelgs
      541 ylnevmdgtv ilrdklarmk yipetdlqki idleqeiknt lkdiiqqggm tnd
//
LOCUS       WP_010753687             193 aa            linear   BCT 01-JAN-2025
DEFINITION  SOS response-associated peptidase [Enterococcus asini].
ACCESSION   WP_010753687
VERSION     WP_010753687.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..193
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=22675
     Region          1..193
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgrylfdpm tgelkeyykl afqmkqddlk tgeifpseev itlgsgpdqk lrvalttwgf
       61 snhqnkqrli narsetveek ptfreefrrh rclfpmsgfy ewnkdkeril ftypderemy
      121 vaglyrvkdg qtesviltte pnelvepihn rmpliidkkd ardwlentek aalllhktde
      181 sklvlqkipk dkn
//
LOCUS       WP_010753704             372 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Enterococcus asini].
ACCESSION   WP_010753704
VERSION     WP_010753704.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..372
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42117
     Region          37..363
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mqsrfknskl ffwtaewvli iigsffllqm rsflrpvltm astiilplfv agflyymfdp
       61 lvrwlekrgl srmvsflivf aavviflvll imnvvpqlve qsvqltqslp syaekandwl
      121 idlsqqedfr nfnieqqlen mnltlnniin wlitsvttsl shilsaltkf fvllftvpfi
      181 lifmfkdghr fmnsldvffp qslrselrat vkdlnntlsa yisstmldav iigvmsfiam
      241 tifkqpysll laficgltni ipyvgpfiga vpavivglfv spwqalymal silviqqldg
      301 nvikpllfgk tlnihpitii lvllgagsvf gifgmlvcip vyaviktlii ngrkiyllrk
      361 qensiltdnr ee
//
LOCUS       WP_010753728             295 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus asini].
ACCESSION   WP_010753728
VERSION     WP_010753728.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..295
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31414
     Region          1..292
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mivstigqgl lwsllaigif mtyrilnfpd mttegtfplg gavcvvaitq gihpllatll
       61 avlagmgagf vtgilytkgk ipvilagilv msglnsvilf vmkspnkglg hqyskiqdlf
      121 salhlpdyfd illlgalvvl lviglllfff ntelgqayia tgdnetmars lgiktdrmki
      181 lgltlsngvi glsgalisqn dgyadvskgi gviviglaai iigevlfgel dfwerliavv
      241 vgsiiyqlii fliiylgfdt tylkiissgi lalclmipql kqalhlktgf ekegh
//
LOCUS       WP_010753772             339 aa            linear   BCT 01-JAN-2025
DEFINITION  inorganic phosphate transporter [Enterococcus asini].
ACCESSION   WP_010753772
VERSION     WP_010753772.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..339
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35697
     Region          17..339
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 msialvvtvv lvmgvifvng wtdapnaiat avstrvlkpn vaiwiavamn flgalvmtyf
       61 nsqvaetisn ivsfegggni qasqvalaas lfsivvwsva awyfgiptse shaliagltg
      121 samalggiga vngqewikvl iglvvstvfg fgggylitkl ivliftnvrr rtankfftig
      181 qataaaanaf lhgaqdgqkf mgvfmlglfy nglaeksgng fvipiwvmaf csltmgfgts
      241 vggmkiiksv gmdmvklery qgfsadlsaa iclfaasvfg ipvstthtkt taimgvgasr
      301 rlssvdwriv kemvfawvmt fpgcgliafv maklfiaif
//
LOCUS       WP_010753793             487 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus asini].
ACCESSION   WP_010753793
VERSION     WP_010753793.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..487
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53688
     Region          1..478
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msqnqkqlrw ftvgliafnm vwglgnvvnn yaqqgisvvt swililalyf ipyalivgql
       61 gstfkdskgg vsswventst krlayyaawt ywvvhipyla qkpqaimial gwavqgngdm
      121 lsnmsmttia lvslvifllf lylstkglst lkvigglagt amfvmsilfi llavgapavs
      181 ngmqfatpdm gniktyipkf dfsyfttism lvfavggaek ispyvnqtkn pakefpkgmf
      241 llagmvgvsa ilgsiamgml fasnnipadl mrngaytafq qlgeyygvgn flmivyaltn
      301 tvgqisalaf sidaplqill adadpmfvpn wlrkrskkgt lvngylftgi lvsiiillpi
      361 lgignmdelv kwmtnlnsvv mpmrylwvff aymmlnkawk nykseykfmk npklgfiagt
      421 wcfaftafac ilgmvpkldy avdpkawwfq latniltpiv lillgmilpa iarrdkdkgi
      481 vpdlkev
//
LOCUS       WP_010753856             651 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Enterococcus].
ACCESSION   WP_010753856
VERSION     WP_010753856.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..651
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73510
     Region          10..>395
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mtsnlfeinf dknqskttnd lgmremqerv yekrasqyll vksppasgks ralmfvgldk
       61 lhnqgikkvv iavpersigk sfkdtelskf gfywdwevkp snnltiggge kskvqhfvkf
      121 mnstdpsdni liathatlrf afeelddslf dntllaidef hhvsrddksv lgnalrsims
      181 nsnahilamt gsyfrgdsvq ilepadedkf dkvtytyyeq legykylksf amgysfyrgk
      241 ytdaldkvid vnkksiihip nvnsgestkd kyaevdeild lltdggnitq nedgiyeier
      301 pdgkkllvad lvneegrekv saylasitdd iqdldkldii valgmakegf dwpfaeyalt
      361 igyrnsltev iqiigrvtrd spnkthaqft nliaqpdaqd devlfavnsi mkaisasllm
      421 eqvlapvykf kpkddkpekp gdlsirglkp adttertkki iendmedlks silqsqdiqn
      481 aivsgadakm inktliprvi ierypdltne eletvrqhtv adiniaagrt ttsedgsrei
      541 ikmadrfini delnidlidq vnpfqrayev isrdidaptl rfiqdylssn kydftdeqlv
      601 aayqaakkfr aengrnpdrn skddgekyla fallrlaeik rereaakedg e
//
LOCUS       WP_010753943             632 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus asini].
ACCESSION   WP_010753943
VERSION     WP_010753943.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..632
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71771
     Region          6..532
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          562..628
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mqelkviglt ktygektlfq disflihekd rigligvngt gkssllkila eldagdgdvt
       61 yiqkagdyqi gyltqetdfp eeltvlesvf qgdapmiqtv rryeqallal aeagdnpenq
      121 kayaraeeam neqdawlvdt naktilqklg itqinqkike lsggqkkrvg laqvliqepd
      181 lllldeptnh ldyqaiqwle gylrqyrgal lmvthdryfl drvtnrifel shgqlieykg
      241 nyedyvvaka ererqaiqqe ekrqqlykqe lawmragaka rttkqqarih rfedlkenln
      301 qvqtdeqvam elttkrlgkq vleikegnyr fdekvilknf dllvqardri gitgengagk
      361 stllnilagq laldsgtliv getvriayyt qltepikedq rviaylqeva eeakqkdgts
      421 isvaellerf lfprhthgsl isklsggerr rlfllkllis qpnvllldep tndldiatlt
      481 iledylqnfp gavitvshdr yfldkvaekl lifegqgeid ryygsimdyl ekapevtpev
      541 akptpvktve aaapaankpk qkltymeqke watiedeiad leaqvetlta gmnnqgsdft
      601 klqelqnqln tvetqleekm nrweylsefa ed
//
LOCUS       WP_010753948             199 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Enterococcus asini].
ACCESSION   WP_010753948
VERSION     WP_010753948.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..199
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22010
     Region          4..197
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mtftvpdlpy aydalepyfd tetmhlhhdk hhatyvsnln aaiekhpelg dksvealiad
       61 ldslpedikt avrnngggha nhsffweila pnaggaptgp vkdaidaafg dfdtmkaefk
      121 taatgrfgsg wawlvkdgdk laimstanqd splsegkkpi lgldvwehay ylkyknvrpd
      181 yieafwnlvn wdkvnelfa
//
LOCUS       WP_010753979             396 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Enterococcus
            asini].
ACCESSION   WP_010753979
VERSION     WP_010753979.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..396
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43186
     Region          1..394
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,206,235,237..238,246)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,199,244..246,275,278)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            238
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mklskramql epsvtlaaaa kakqlksegy dvlsltvgep dfptpenire aavtairsge
       61 asfytqaagi pelrravvdy mktyygldyg ieetivtdga kfalyalfqa ildkgdevii
      121 pvpywvsyae qvklaegvpv fveglqeadf kvtvpqleaa rtektvavll nspsnptgmi
      181 ytkdelraig ewavehglli iaddiygrlv yngntftpma tvsreirknt ivingvskty
      241 amtgwrigfa ignkeiiaam akitsqstsn ptaasqyaal ealtgeqdsv elmrqafeer
      301 lnklyplvaa ipgvkltkpq gafylfpnma gtmelcgydn vttfvndlle dalvatvtga
      361 gfgapenlri syaadwdtle eavrritafv ekkrlk
//
LOCUS       WP_010753984             443 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus asini].
ACCESSION   WP_010753984
VERSION     WP_010753984.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..443
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=50035
     Region          15..369
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(18..19,22..23,59,62,118..119,181)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(116,119,210..216,245,272..277,304,328..332,334)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mlnfdyekep lrdilfvdvk sfyatvecav rgldplttml vvmstadntg kglilasspa
       61 akerlgisnv trannlpnhp dlwqvpprmn lyiqenvkfn qllkeyvaee dhlvysides
      121 lidvtdsmql ffpdtglsrq ekrwrfakri qkeaeeklgl vlsvgigdnp llaklaldng
      181 akhnpkfraq wqyqdipetv wkiprmqdfw gigsrmeknf yrmgidtiwq lahtepelly
      241 qkfgvmgqqh yyhangidrt ilseaspvak eksysnsqvl prnytdasei elvvremaeq
      301 vaarirrhgc ltqcvslfig gamgeksgfs hqmkipatdn tkklmnyclq lfrkyytgqv
      361 vrhvgisysr liftqsrqld lfsspeesak eehldqiidr irekygftai vhatskvnga
      421 rsikraglvg ghagggpggl dgl
//
LOCUS       WP_010753996             336 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus asini].
ACCESSION   WP_010753996
VERSION     WP_010753996.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..336
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37624
     Region          1..258
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mlalgvigtn wishqfveaa lasgkyqlkg vysrklatae efggkyegec fyetdlekff
       61 arefdvvyia spnslhfaqa kaallagkhv ivekpafsnp qemaaiiela nqqglfyfea
      121 arnlhekafr kvgdflpvqe ailganftym kyssrydqvl aggepnifsp hfsggslqdl
      181 giytlyaalg wfgmpeevhy farkiatgvd gigtiilryd lfdvtiqqgk iadsflpsei
      241 ylengtllls ginsfeeatf ydrdsgekrp ldimqaanpm ieealdfaki mnhpkdpelg
      301 lryeewvels rnvneviyql rkqahvvfda dttnee
//
LOCUS       WP_010754007             313 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Enterococcus asini].
ACCESSION   WP_010754007
VERSION     WP_010754007.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..313
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35369
     Region          1..313
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mlqayinifa ifalmflgyf lsykqwfnnq vadafsklvl nlalpfnmfl nmtenfsrde
       61 flslfsgmii pllsmaatfl isllyrrlfh isktrqgtfs tmftcsntif iglpinlavf
      121 gekaipyvll yyivnttffw tigiytmaqd npeieqqrls fhpvvllkkv ltpalmgfii
      181 gllwvmttrp vpsflqnfgg yladlttpls mfiigiivys nglanlkfnk dilgvligrf
      241 visplivwgl gfvfpvpalm lsvfmiqssm pvqnsipila rnyqadedya asslgysvll
      301 ymiyipillk iil
//
LOCUS       WP_010754016             147 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Enterococcus asini].
ACCESSION   WP_010754016
VERSION     WP_010754016.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..147
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16253
     Region          1..147
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mtllstlntd mktamrakdk erlavirmlk aslqneeikv ghelnadeel tilsremkqr
       61 rdslaefeka gredlsekvk ieiaivenyl paqltdeeir qivaqaitdt gatsakefgk
      121 vmgavmpkvk gkadgnqvna ivkellq
//
LOCUS       WP_010754088             226 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Enterococcus asini].
ACCESSION   WP_010754088
VERSION     WP_010754088.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..226
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=26268
     Region          46..226
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mhcnycqkpi vrnlkvkeil fpwtlpisel cddcrksfvp lkkagscpgc mrqaasfcld
       61 cqawqrqypd yefahealfa yedsfaqwla mykftgdyrl rwtfaqevrq alkkypgfil
      121 cpiplakerw qergfnqttg flqaagssyq ellhrtkqdl pqskktreer lrlaqpyrla
      181 vspekiygkk illvddvytt grtlfhaari lltahpaqir tfslar
//
LOCUS       WP_010754096             201 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010754096
VERSION     WP_010754096.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23384
     Region          7..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkktdlrvrr tnkmiieafi qlveekgydq itvqdisqra minratfyah ykdkqdlydt
       61 ifdfaieaft svlspkdlvq gnrlrvkqie vllthiykni qrnrrfylti mdgaametlr
      121 kkiadildae yahifnrlki tendievpmd fiieymtsif igtlhwwltt dspmapedla
      181 klvikligng hltvlgieie n
//
LOCUS       WP_010754102             311 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Enterococcus asini].
ACCESSION   WP_010754102
VERSION     WP_010754102.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..311
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33642
     Region          1..288
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mkwlqklrnn eslkrllaig kqrfsdaelg nssvvvayyl llslfpllia ignllpffri
       61 dpngilpyle nvmpaeiysf lgpaihsllt qssggllsis aiaavwsasq sinalqgamn
      121 kaygvpnren fiivrivsvl illlllaggl gativlgvgk avldalqpif gfsgeiiktf
      181 qtlkwpatil alllimtviy wlvpnarvrv faafpgavia tigwlllgql fglytrffaa
      241 rvsgyqiigs fivlmiwlnl aagitlfggi vnaiiatykg ggsvekrhgp lsrmttklkk
      301 rltkdtpske e
//
LOCUS       WP_010754172             404 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Enterococcus asini].
ACCESSION   WP_010754172
VERSION     WP_010754172.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..404
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42248
     Region          1..402
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mdtgnigfmi lctglvfvmt palaffyggl sqkkhllntm mmvivtmgla sllwiiigys
       61 lafsggnsfi gnldkvffng vssesssglp eglfaafqmm fvlittailt gavagrmrfs
      121 alliflsgwi ilvyapiahm vwgggfldqi gsvdfaggnv vhissgisgl vlamvlgqrk
      181 rkenesftph nvpfvvlgtg llwlgwfgfn agsalaadgl avhallttnt aaaagmmswm
      241 mlewlvkgkp sivgsctgav vglvaitpga gfvsigsali agllvspicf ygtrfvkekl
      301 gcddaldafg chglggifgg litglladpa iggetglffg gvdlfvaqil silftilfag
      361 gvsfilimvi kkfmpirvss sqeekgldha lhneqayqdl lgne
//
LOCUS       WP_010754185             288 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus asini].
ACCESSION   WP_010754185
VERSION     WP_010754185.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13403879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=33095
     Region          <90..276
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
     Region          230..284
                     /region_name="HTH_30"
                     /note="PucR C-terminal helix-turn-helix domain; pfam13556"
                     /db_xref="CDD:433305"
ORIGIN      
        1 mdsnqlpaif ptgrvdqqph gseqeltipv dqgffhvakt eltprelqll elfaphtthh
       61 aekehlwyqi lfegapvpat palrviqvkl kiqpgflkke wlaeiddmfl rlvdrffiqd
      121 dllllieekg dtnypveeif glfqaldtdf diytqvfvga fhgdptslaa nfqeeqkift
      181 gelatrnrqk dfpftstain yfigepvkas pmmnglyqdw fsdsemidil ralwqsqgnv
      241 ssaakelflh rntvlyridk fqeatrldlk nmndlvfchl lieifadk
//
LOCUS       WP_010754193             202 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Enterococcus asini].
ACCESSION   WP_010754193
VERSION     WP_010754193.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..202
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22400
     Region          3..161
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mvkivalvgt nsenstnrql lqymkahfan qaelellein hlplfdkpad kkvpevvrqm
       61 altiesadgv vistpeydha ipaallnaln wlsygiypfv dkpvmiigas ygtlgssraq
      121 ahlrqvldap elkarimpss efllshslqa fdennelidq dmvaqleglf edflvfmqit
      181 sqlghahsvn qklaesvswe nr
//
LOCUS       WP_010754240             202 aa            linear   BCT 01-JAN-2025
DEFINITION  VanZ family protein [Enterococcus asini].
ACCESSION   WP_010754240
VERSION     WP_010754240.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..202
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=23251
     Region          105..179
                     /region_name="VanZ"
                     /note="Glycopeptide antibiotics resistance protein
                     [Defense mechanisms]; COG4767"
                     /db_xref="CDD:443799"
ORIGIN      
        1 mrviknvval lvavgvsgll ihfialpvla gypriaqtme rfvytelvli sflalviwlf
       61 ylqwslgkls vvylylffsv ylfllfvvlf tkapryqali lnpidflmgg rlswlealln
      121 vcyfiplgll ygmkaryref vivalltivg iemiqfvfyl gtfaisdifl nfigcllgyh
      181 lypplhehfd vrmiswtrfg ri
//
LOCUS       WP_010754314             137 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010754314
VERSION     WP_010754314.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..137
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=15515
     Region          4..115
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mvaidksssk pyyeqlmlsi kadifhgilr pgdrlpsvre lakellmnpn tvskaykile
       61 neqvlvtirg kgtfvkkeed lprdelrirh lkeqlsalvv eaahlrvsqe elmkwlaenf
      121 selggsqdes qqptknd
//
LOCUS       WP_010754326             560 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus asini].
ACCESSION   WP_010754326
VERSION     WP_010754326.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 560)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..560
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62475
     Region          2..524
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 malvtmqnfn fsypetdqpa lqdvsltlfp gsfnvlfgks gsgkttllrq fkpvlaphgq
       61 vsgeiffadq plnqlalrqe asqigfvlqn pdnqivtdkv whelafgles lgydtptirl
      121 rvaemasyfg iqhwfekdvk elsggqkqll nlasvmvlhp qllildepts qldpiaasdf
      181 letlqkinre igttillteh rlqdvlpmad qvllmdqgkl iaaaspreig qqlqksqgdl
      241 fvampapmqi aaqftpdqlp ltvregrnwl tnlsltplak qveqprkite amielkdvwf
      301 rydrseadvi kglslqvakg effaivggng tgkstslsli srirqpyrgk iklggrplrk
      361 yseqelyrnf lgvlpqnpqs lfvkktvled lyevidgpke kksaayqaqm qkeqavqgiv
      421 eltqlihlvq rhpydlsgge qqrlalakvl lmrpqillld eptkglddfy krqlgeilcq
      481 lkaqgvtilm vshdvefvae fadscglffn gnvvssksaq dffagnsfyt taanrmarty
      541 fpdavtvkdv ieclktqeis
//
LOCUS       WP_010754355             323 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Enterococcus asini].
ACCESSION   WP_010754355
VERSION     WP_010754355.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..323
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35120
     Region          4..295
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mevydvtilg agpvglfaaf yagmrkrkik vidsldqvgg qlaalypekv iydipgqpei
       61 aagtliknle qqltkfpvty algqrvenyr eegdllaiet dqeihytktl ilatgqgsfa
      121 prkltvpgad tfegrgisyf vtapeqyrnq rvliagggds aldwalslea lgaevglvhr
      181 rdkfraheyq venleksgvk rytpyviael hgdtrlrqvt lvhkktgeqv ilptdellvn
      241 ygfvtdrksh wpleqdtagi tvssnmatsf pgvfacgdaa sypgkvnlia tgfgeaatav
      301 nnavafldpt srrqpahsts lfa
//
LOCUS       WP_010754385             414 aa            linear   BCT 01-JAN-2025
DEFINITION  M20 family metallopeptidase [Enterococcus asini].
ACCESSION   WP_010754385
VERSION     WP_010754385.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133889
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..414
                     /product="M20 family metallopeptidase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43924
     Region          32..382
                     /region_name="M20_Acy1L2"
                     /note="M20 Peptidase Aminoacylase 1-like protein 2,
                     amidohydrolase family; cd03887"
                     /db_xref="CDD:349883"
ORIGIN      
        1 mtttttnplt tkttntpaqt aiikefiakr lpeyqalald ihehpevsny efyssgalva
       61 qlekegftva qdvaghrtgf daryqgkkpg ptlaflaefd alpgighacg hnlfgtysvl
      121 aasalkelid evggelrvyg tpgeeggeng sakgsfvkhg yftdvdaalc ihpgyryqkt
      181 saslandpvd ikfygvasha agapeagisa leallqvfng inglrlslpk dvnihgiitd
      241 ggqaanvipe fasarfylra anrktldqvy ekvenivkga alatgatyef glfqnavddv
      301 ivtplfdevf frhaeeagvp eteiqerdsg skgssdvgnv sqviptiqpt vsiadeyiag
      361 hseefkaaar stkglasigi aaellattal dllqdpella aikeehqkqv akgn
//
LOCUS       WP_010754406             138 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010754406
VERSION     WP_010754406.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..138
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16033
     Region          1..115
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(49,52,56..57,66,86,90,96,100,103..104)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mnikkaaemf dlsvdtlryy ervgvippvn rnesgyrdyq tndlnwiyla knlrnaglsv
       61 esliefahla qlretqnvee aqkqilhdql aeldeklaqm rqvrellvyk ietydehvgk
      121 fqagtippak veklwern
//
LOCUS       WP_010754426             206 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Enterococcus asini].
ACCESSION   WP_010754426
VERSION     WP_010754426.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..206
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22837
     Region          13..169
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 miefsaqels glqnykfltg sviprpiawi ttkdpttqvv naapfsyfnv vssqpplvsl
       61 sinraqglak dtarnllaqk egvihivned vlaimnqtaa slppeisele qqpvtlipsq
      121 qvevpsiqea airlevrvhq yvpvtdqnqr ivsdlfilev lhyafdpaif saerqyilpe
      181 kldpiarlag ntyanlgdtf dirrpy
//
LOCUS       WP_010754022             451 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 28 protein [Enterococcus asini].
ACCESSION   WP_010754022
VERSION     WP_010754022.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Abbott,D.W. and Boraston,A.B.
  TITLE     The structural basis for exopolygalacturonase activity in a family
            28 glycoside hydrolase
  JOURNAL   J Mol Biol 368 (5), 1215-1222 (2007)
   PUBMED   17397864
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..451
                     /product="glycoside hydrolase family 28 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50224
     Region          4..366
                     /region_name="Pgu1"
                     /note="Polygalacturonase [Carbohydrate transport and
                     metabolism]; COG5434"
                     /db_xref="CDD:444185"
ORIGIN      
        1 mseyvitdfg ivaeenivtk eiqkvidqaa aagggrvivp agrfitgalq lkdnielhll
       61 pgavlqfsdd qkdypvvtsr wegveravya aclyafdakn iavtgfgtld gngekwwqvf
      121 rhereklayp rpmlvsfegc ervtlkdftc inspswtihp qccrnvtidn lnihnpadsp
      181 ntdgidpesc qnvriancni dvgddciaik agtedtpqri scenititnc tmvhghggvv
      241 lgsemsggik nvtitncvfq dtdrgirlks rrgrggfied iridnlvmer vlcpfilnly
      301 yfcgprgker yvwdktpypv teetprfrri hfanitarnv haaagfiygl aeqhieevsf
      361 dniaiemaee avagrpamms giedmqrrgf yigfgdnllf knvsirnheg paftqegckd
      421 lrfvecqsla prdqaplvye qevvtletet l
//
LOCUS       WP_010754429             251 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-glycerol glycerophosphotransferase family protein [Enterococcus
            asini].
ACCESSION   WP_010754429
VERSION     WP_010754429.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..251
                     /product="CDP-glycerol glycerophosphotransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=29926
     Region          4..>239
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mnaklrrtle rmyhkvvtat ftvvgrlpkr elfffesfhg rqysdnprai yeyiqsqype
       61 atcvwavkkg feqpfidndv pyvrrmglnw lltmprakyw ifntrmpkwm kkttgttfvq
      121 twhgtplkrl gldiqqvnmp dtdteryren frqesarwdy llspnaystt ifkrafaytg
      181 pvleigyprn dilqdeehla anrqqvlqkl glqegqkiil yaptwrdnqf hrkgaykydn
      241 qfplsalsrw w
//
LOCUS       WP_010754432             383 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-glycerol glycerophosphotransferase family protein [Enterococcus
            asini].
ACCESSION   WP_010754432
VERSION     WP_010754432.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..383
                     /product="CDP-glycerol glycerophosphotransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=43028
     Region          <84..374
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mfdvknayla flasrakkht lnkrvcylls fadndggaid alqqqygtdf llaytpqmte
       61 vaksyaakgv vitpfspraf cmerswrqia scqiiiadny ypelaalsqp qrkiiqiwha
      121 tgalkafgwq dpktkkrsqa dqvrfqkvyg sltdivvgsq amgkvfeaay hidparvryl
      181 gaprtdvlqp talaitvlta epttvlyvpt yrdsleemrt vltsafrafq nsdmqvlvkl
      241 hphlarqlsd vktptnvrlv tgnllalfdq seylvtdyss cvfdfmlrrp gqgiclycpd
      301 lehyadttgl qpdfkvdwqp wlaqsseela vklqaasqpn nektetlllq qqalsqkwqe
      361 yntgqavegl lalvdrylqt ens
//
LOCUS       WP_010754451             317 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010754451
VERSION     WP_010754451.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13303752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..317
                     /product="AraC family transcriptional regulator"
                     /calculated_mol_wt=36479
     Region          44..310
                     /region_name="PRK13501"
                     /note="HTH-type transcriptional activator RhaR"
                     /db_xref="CDD:184092"
     Region          <182..313
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkpflfqnye evliddfvpe lkeydriwqd gkisldkqlk avdlakdhpv ffighrmsqd
       61 apfhshsfye ivcvlnglve nctkkstfym gsgdicimnl asshslkvvd pqaivfnigi
      121 eatemesgtf kniyrstsfl gnflrekedl dylyfpsngs lrlaqliqtm lttharksag
      181 mpfllasevm qllgelvdln eysywgvnnr vmelldfvek hyatvslael aqefnysesy
      241 lsrfvkkqtg qqiskiimgk kmekaglllq ntdlsvneia levgyqsysh fhkifkkwyr
      301 qtpndyrqhy speiatn
//
LOCUS       WP_010754446             261 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Enterococcus asini].
ACCESSION   WP_010754446
VERSION     WP_010754446.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..261
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29128
     Region          3..255
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mkifdshthl naeqfngeea qivsqaqalg vtemavvgfd tptiaktlel nqqfpgvysi
       61 igwhpteags ytaeiertle kqltlpkvva lgeigldyyw medpkdvqer ifrrqiaiak
      121 ehnlpisiht rdatpdtyri lkdegvparg gimhsfsgdl ewaqrfldlg mhvsfsgvvt
      181 fkkaldvqea atgvplerll vetdapylap vpyrgkrnep gytryvveki aelremtped
      241 vaaitrknal tlfgldkeld s
//
LOCUS       WP_010754435             258 aa            linear   BCT 01-JAN-2025
DEFINITION  putative ABC transporter permease [Enterococcus asini].
ACCESSION   WP_010754435
VERSION     WP_010754435.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..258
                     /product="putative ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29631
     Region          8..185
                     /region_name="COG4905"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443933"
ORIGIN      
        1 matfiqivll ffcysfigwa wetvycsika rkfqyrgfli gpitpiygfg ilavlyflep
       61 lhdnllllyv aatiivtvle yvtsfglekl fhaswwdykd vplningrva vpvslfwgvg
      121 cvfivkilnp qvlhleewla shfgfllpvf lialisfdlg ytlanmaafq aavkrlnatv
      181 dnrkeelkga wetskedvqq rlnwgkylgd hpeeasnlpr lnfnqrrllk nfphlrlsnv
      241 kngqelrqlv edlrkgfk
//
LOCUS       WP_010754463             218 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Enterococcus asini].
ACCESSION   WP_010754463
VERSION     WP_010754463.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..218
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25753
     Region          20..214
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mdhhvlqeyl tahqfpvvkk tykkyltyeg iqdsyvyilk ngviktsvis kdgrqfnlry
       61 inqleivsll kdeysqyida pfniriespe aelyridrvq fwkdinrsmd lqlyvkdyyr
      121 vrllhnmkkl qqmlmngkfg avcsqlyefq elfgvpteeg ilidfvvtne eiarfcgitt
      181 assvsrmlqq lremnaicie nhkilirdle kikeniif
//
LOCUS       WP_010754482             442 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus asini].
ACCESSION   WP_010754482
VERSION     WP_010754482.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..442
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=47425
     Region          13..442
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mneeknqkse ariekfvtia qkvgnqihlr slrdglapmm plfilagiav linsvfldps
       61 gfmnnvlses tmvtwqgfgn liinatlnva ailfvislsy qlsknrgytn pigaamavlp
      121 afftflpmlv tvtvdekatq iggmiaysnv gtsgvfaail vgiigtelfi klttvkrlqi
      181 slgenvppav ansfnvmlpa iitvslfall sfliqlggsd lmslisrfiq eplravgtsl
      241 pgylllvclg nllfsfgihq sviagpildp llllnmndnm aakaagtepp hiitnafhqv
      301 fgslnmasgs tvaliiaifi fskyqpyrnl aklslgpnlf ninepiifgl pivfnlpmii
      361 pfvlspiigt vigyaatslg lvsktvvmip wttptlisgy latagdwrap viqvliivil
      421 vffylpflki sekvaianae ka
//
LOCUS       WP_010754532             515 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus asini].
ACCESSION   WP_010754532
VERSION     WP_010754532.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..515
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57691
     Region          23..483
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mkpkenkksn eseknwvyqp kditvargig ygltdlmggg wnnivsgvif afvlsqginp
       61 afagaitgig rivdaiftlf fgaitdgfyk tklgqrfgrr hffmllggil favlfplfwi
      121 qsddwhyyli iyiaieiaia milipwetlp temtddynkr tvlsgsrmfi satgtaivfl
      181 vlaalkrmen pnaylitgii wtvifvvaif vsyrttwerp ltpefiaele sqpklslgaf
      241 vkktvsdyfs tfknkafrkh laiyllsftg kdfystmlpt fiiccihgak adtpwtlqal
      301 svfgilatlg aaklmlthgp kylftlsytt liitmvgyfl twafqvknav wvliiisily
      361 qcaraileft pwnvfpfipd vdrimtrgdr agvyasvmtf frkstgalas wiagillaei
      421 gfdsktmldl nstphnvqvg ialiffvapv vlfalslfta wkfrlnreth avlkaeinrl
      481 eaggskddvt peakevveel tghpyqeswp dqplt
//
LOCUS       WP_010754565             504 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus asini].
ACCESSION   WP_010754565
VERSION     WP_010754565.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 504)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..504
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52556
     Region          201..502
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnfmkrglqs lwakkgrsli liavfsaili fvlagltiks aadtatdtak ksvgatvtls
       61 tnreqmfkkd sdsddasdes tsrpdpgsfq mtpvnladae kiaaldgvks ysfevstsat
      121 kgddiepiss sdeedtteds atdeasqgan gmpgggmmgg aggmdqgdfq itgvlesaay
      181 ssfsagtatl tsgealtaed vdtnnvlies alaeandlav gdtftlvdan denvevtikg
      241 iyetsdtgts mgmqfnfmnp antifsaytl antiageegd tidsavytla dpnemdsfvk
      301 eaeslidtdt fslqtndqmy qqmltplnnv ssfakniiil vaaagviilt livmmtirer
      361 ryeigvllsl gegrgkvilq ffteifvcml lalgiasasg nlvgnvvgnq lleqqttqta
      421 sadqgapgge gqgqapsggr gqggpgqmis stfsqseeik dlditvsgeq iallaaiglg
      481 isfvsillss agimrlnpkk ilis
//
LOCUS       WP_010754572             317 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus asini].
ACCESSION   WP_010754572
VERSION     WP_010754572.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..317
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34763
     Region          1..244
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mirygiista qvvhrfvagv kessngevva iasrnltkak emaqdldipq aygsyeelyq
       61 dsqvdivyia tynkghysaa kaaleagkhv llekpftlha aearelfdla kaqgvflmea
      121 qkalflpvtl avqeaiaagk igevrrvvsq taylnsdmip wfrdleaggg vlygsgsypl
      181 qyvefvtgek itdlsgtavi kpgesevqad lslqlgahat gnvfltvqld lprglwiygs
      241 qgtiqvpnfw rgdqaritvg dqveelffpf asefvyeieh vneclsagyl tspvmtpelt
      301 ietvarmeql hqawhkk
//
LOCUS       WP_010754644             441 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus asini].
ACCESSION   WP_010754644
VERSION     WP_010754644.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..441
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=47601
     Region          1..426
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mnqwinekll ppvlkfvntk aitalrngml ytmpftivgs iflllanfpi edvsnwvnds
       61 glagyfneaf gasfaimaif avmgiaysyv kddgyeglpa gmialvvfll tqrstvtdae
      121 agvtignvin ktwtggqgmi aailvglfvg wayvwflrrd iriklpeqvp anvansftal
      181 ipaaviivvs lviyalfdal lnttvvewiy kviqspmqgv tdslggaimi gflvpflwff
      241 gvhgstivgg imgpilqans lenteilnag keltvanggh ivtqqfmdqf ttvtgagmti
      301 giviymvlla rsaqykqlgr lslvpalfni nepiifatpi vmnpimalpf iltpvvsaiv
      361 tyfalytglv plftavqvpw ttppiisgfl vggwrtallq avvlgigfll ylpfirkadq
      421 lnyleetgkt paeaaealea e
//
LOCUS       WP_010754651             496 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease/substrate-binding protein [Enterococcus
            asini].
ACCESSION   WP_010754651
VERSION     WP_010754651.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 496)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..496
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54083
     Region          1..189
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          220..487
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(226,228,277..278,281,326,328,407,431)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mqaifehlai slsalliail iavpcaills krqkiaevvl qftsvlqtip slallgllip
       61 fvgigttpal ialviyallp ifqntyigls eidpsieeaa eafgmsrmrk llkvevpmam
      121 pmivsgirta lvliigtatl aaligagglg tfillgidrn dpsltligai csallalifs
      181 glirflqkrs wkvslaalgi iflgiggvya aqqttltket itiagklgse pdilinmcke
      241 vieandeqvt vtlkpnfgkt sflfsalksq qidlypeftg tvleslvkvp aaedqihspe
      301 ktyqlanell geqfdmelle pmsyqntyav amkrsvaeek gitkisdlva hqgelragft
      361 lefidredgy kgmqkkyglk lgsvqsmepa lryqaiqngd vdvidaystd seikqydlvt
      421 leddrqlfpp yqgapllrgd fakehprvve alnllagkii eeqmiemnyl vnvekqqpad
      481 vahdflvkek iiqegn
//
LOCUS       WP_010754715             225 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            asini].
ACCESSION   WP_010754715
VERSION     WP_010754715.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..225
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=25260
     Region          125..216
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mnqrrslpgr igifialvfi qnlstmimgi egligrplse iayalvislv flavmvyfik
       61 yyqgqlqeyn prgfgenlsf kgkvgwiilt vvgiyaflil vspllpqgta enqqvvdqmf
      121 lnhvlgvtly gavlgpiiee llyrgifmnf fwnqkgrmyd vlavlssgll fgllhepqls
      181 lylvvysaig vflgmlylkt kdircnmiah ilyngitflv mfqtl
//
LOCUS       WP_010754836             104 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Enterococcus asini].
ACCESSION   WP_010754836
VERSION     WP_010754836.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..104
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11286
     Region          7..96
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mfglfnrips istselagkl gknlilldvr tpgeyrgghi asaknvplnk iadyrqkeaq
       61 pvyvicqsgm rskqaarilk qkgyqvinvt ggmnrwtgpt rggk
//
LOCUS       WP_010754847             278 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Enterococcus asini].
ACCESSION   WP_010754847
VERSION     WP_010754847.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 278)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..278
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29777
     Region          6..265
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 malfsyefmi kalwaavfia giapmlgvfl virrqslmad tlshvslagv algfflnlnp
       61 slttlivvvi aavlmeylrs lyrtyseisi ailmagglal alvlmnlspg nsatsiqsyl
      121 fgsivtittg qvitlgvlfv ltailfalfk rpmyvltfde dvahvdglpv hlmsmlfnvl
      181 tgvaiavmip iagallisai mvlpaaismr igksfnivil isivvglvgm lgglvgsfyw
      241 nsppaatitl vfiglfllvn lakrivisfq rkhrlken
//
LOCUS       WP_010754957             679 aa            linear   BCT 01-JAN-2025
DEFINITION  beta-galactosidase [Enterococcus asini].
ACCESSION   WP_010754957
VERSION     WP_010754957.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 679)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 679)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 679)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..679
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=77712
     Region          1..618
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
     Region          621..676
                     /region_name="Glyco_hydro_42C"
                     /note="Beta-galactosidase C-terminal domain; pfam08533"
                     /db_xref="CDD:400716"
ORIGIN      
        1 mnaynqeprl lhggdynpdq wldypeilkk dlelmkeaki ntvslgifaw salepregef
       61 hfewldqimd dvaamggnvi latpsgarpa wlsekypevl rtnanrqkmr hggrhnhcfs
      121 spvyrekval inrklaeryg qhpavimwhi sneyggdchc eycqanfrkw lqarygtlea
      181 lneawwgpfw shsfsdwsqv espspigesa vhglnldwkr fvtdqtidff eheikdirhi
      241 tpdipvttnf madtmdlipf qslnyerfak hvdilswdcy pawhndwett adlaskvgfi
      301 ddlyrslkdq pfllmestps gvnwhpvnkt krpgmhllss mqhiahgsds nlyfqirksr
      361 gssekfhgav idhdnssdnr vfqdvkevga lmekiqgvkg ggkkakvail ydwennwald
      421 daqgyaqgtk rypqtlqehy ryfwnqdipv dvvtprydls gydlvvapml yllsetdmra
      481 lkeyvaaggt lvstyitgvv neadltylng wpqalqelfg lqvketdvyy pkdhnriqta
      541 tgdygvkdya alievqdaev laryqegfyq geaavtrhhf gegdayfiap rteqafldef
      601 yglrtkelhl anplvvagnp dvsiqsrkqa grtyhfvmnf seevqevtla qelqdlltge
      661 tmpktlhlqp yqvrvlvae
//
LOCUS       WP_010754959             428 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar ABC transporter permease [Enterococcus].
ACCESSION   WP_010754959
VERSION     WP_010754959.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 428)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15767475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..428
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47883
     Region          13..>103
                     /region_name="DUF5683"
                     /note="Family of unknown function (DUF5683); pfam18935"
                     /db_xref="CDD:465918"
     Region          <174..394
                     /region_name="malF"
                     /note="maltose ABC transporter permease MalF; PRK10999"
                     /db_xref="CDD:236816"
ORIGIN      
        1 metmsqstnq kqrgrkaalf slipglgqfy nrqyakgglf lfffvayilv fkdlfnmglw
       61 givtlgvevp rdnsifllae glialiviaf giffyylnlr dayktgelig mgqkphtikq
      121 syqallaegy pylisspafl llvfsvifpi lfsvalaftn ydlyhsapan ladwvgletf
      181 akiftvdiwr stffgvmgwt vvwtlvastl qvaigvflai vvhqkelrfk kffrtilvlp
      241 wavpgfvtil ifaglfndsf gavnnvildf frispipwln danwtrlall iiqgwlgfpy
      301 ifivttgtlq sipadlyeaa tidgasviqk fknitlplvl ysmapiiitq ytfnfnnfni
      361 iylfnaggpa vpgstaggtd ilvswiyklt mqnsqyalaa altillsifv iaialwqfrr
      421 tnsfkeev
//
LOCUS       WP_010754996             281 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Enterococcus asini].
ACCESSION   WP_010754996
VERSION     WP_010754996.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..281
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32332
     Region          10..207
                     /region_name="HAD"
                     /note="haloacid dehalogenase-like hydrolase; pfam12710"
                     /db_xref="CDD:432733"
ORIGIN      
        1 mkkpiiafmy dfdrtlctrd mqeysfipel gvdaatfwqq vahlaetehm dhiisylyhm
       61 iksanakglp lrredfvalg kdvelfpgvt twfkrmndlg aelgleiehy iissglteii
      121 egtpihgefk kiyacefhyd eagnadwpal tvnytnktqf lfrinkgvlp mnddealnef
      181 ledrdrripf rnmiyigdgl tdvpcmklvk vnggqsiavy enkervvdll tdrrvdfitp
      241 anyeagseld eicqtilrkm alvdklvtln hrqrdqetpk r
//
LOCUS       WP_010755011             258 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Enterococcus asini].
ACCESSION   WP_010755011
VERSION     WP_010755011.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..258
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27445
     Region          1..244
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mtgvlyfiii ilantvgais gmgggvlikp vfdaigahsv paitfystva vltmsvvstl
       61 rqrknlvidy pvaglislga iiggmlgnvv fesllnwlvv eksvqliqiv ltivtigisy
      121 lvsegkwslh lkgwywysli glslgflasl lgigggpinv amlllcfgmp iksatvysii
      181 tilfsqlaki ltiasttgfg rydlkllyyv ipaaviggfl gallsgrlkd qsvrrvyqvi
      241 lflvlcingy ngiqillg
//
LOCUS       WP_010755056             289 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Enterococcus asini].
ACCESSION   WP_010755056
VERSION     WP_010755056.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..289
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=31914
     Region          1..281
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 myqivtdscc dvpyqllaek dvafipmivn ingqeyfddl gksfdyeqfl qslrdkqqpt
       61 tsqinvgryi effmpycekg eailylcfts gmsgsynsal qavdilkedy peaniqvvdt
      121 laasmgegfi vleaakrkqa gasmeevmaw vnehkmnlqs wvtvddlshl yrggrlsrsq
      181 aamggllnik piihvdakgt lqnvgkvrgr nkalqkvvde tvdhlvsken qtvyvaysgd
      241 leaaekvmgl lkekidvqds gifplgptia shtglgciai ftfgqervd
//
LOCUS       WP_010755057             540 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus asini].
ACCESSION   WP_010755057
VERSION     WP_010755057.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..540
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60631
     Region          4..527
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mitvsdvslh fsdrklfddv nikftpgncy gligangagk stflkvlsge iqpstgsvsl
       61 gpdermatlk qnhfdyeeyp vietvimghk rlydvmkekd aiymkedfsd edgiraaele
      121 gefaelggwe aepeaavllq glnitedlhq lpmkeltagq kvkvllaqal fgkpdvllld
      181 eptngldiqs inwleeflid fentvivvsh drhflnkvct hmadldfgki klfvgnydfw
      241 lessqlaqkl qsqqnakkee qikelqefia rfsanasksk qatsrkkmld kitlddiqps
      301 srrypfvgfk pereigndll qvdnvsvtid gkkildnisf tlnkddkvaf ianndivttt
      361 lfkvimgeit pdtgtvrwgv ttnqsylpkd nsrefdndlt ildwlrqfas keeddntflr
      421 sflgrmlfsg devlkpvsvl sggekvrcml sklmlskanv lvlddptnhl dlesitalnd
      481 glmgftgsil fashdhqfiq tlanriiais dkgvvdraet tydeflenpe vqkrvnelfa
//
LOCUS       WP_010755081             255 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010755081
VERSION     WP_010755081.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..255
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29525
     Region          155..230
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mqhvliltkn slaeeplvqk lqrmnceilc stdlfkrlka gtispflsyf qwiilseslc
       61 nsevehilqm lknhpllvlr vvetipneee qaywqerglv dwisketsye llrekmnelq
      121 qqvkqdavtg nqilnfpttp geettpnnlk llikslskte krvfecliqs ystsgvlsrq
      181 elcnylwqdg stssnmsqls clinklkhkf elhgikgeti ttlwgrgykl sssfyeywle
      241 nsqqleelky ysamn
//
LOCUS       WP_010755083             422 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus pallens].
ACCESSION   WP_010755083
VERSION     WP_010755083.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..422
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=46542
     Region          1..411
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdnimkfmte sfapkvnkvv knpwisaiqd simialplvf vgslvtvvsl lgnifsgmpd
       61 fsmissfsfg myglvvafli pyylmekkgh ggqklisgst slvlfmmllf ptitedgeai
      121 filsrfgstg mflsivtglf vafvmnlavk ksffdedtpi pdfvvgwfns llpitfvlfv
      181 gwlitfqmqv dffdviilif splakivqsy pgfvlsvfip vflytfgisg wvmmpviypv
      241 ymsglaenaq avasggeamh iatqetcyaf ssmggigttl alsvmmlils rsaqlkaigk
      301 aiivpsifni neplvfgapi afnpylmvpm winsiivpti ayvtmslglv nipsqtfllw
      361 ympypitsyl atqdwraivv sviifavtwl iflpffkayd nsllkqeekd aleeaqmnaa
      421 aq
//
LOCUS       WP_010755131             279 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus pallens].
ACCESSION   WP_010755131
VERSION     WP_010755131.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..279
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30740
     Region          6..275
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,206,228..230,232..233)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mtlkaivldi dgtllnekke ispatkkali eaqqngikli lasgrptsgm liyadelemk
       61 qhhgllvsyn gakvidcqtn eelfsqamtv eegravlehl kkfdvkvmid kddymyvnnv
      121 ydcdithkgn kiniieyesr ggnyklceid dlaaflnepp skiltagepe ylathyqemm
      181 apfsdslncv ftadfyfeft aegidkakal dtvlrplgit peeiaafgdg hnditliqya
      241 gkgvamenav pelkaaadhi tlshnadgip hmleqlvnv
//
LOCUS       WP_010755086             632 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus pallens].
ACCESSION   WP_010755086
VERSION     WP_010755086.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..632
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=73029
     Region          16..627
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mltekekelv gflekkqpqw vtskelaafc qcttrtirnr vakinqqtpe lvltshlgyq
       61 lnsavaiaee gvedrksrif lellkhsskg vdvfelaekl fvsestlknd iqqlkkeitn
      121 daiqiafeqd fvkltgpera krrylislly nesdlqeklk hsiqqmigyi sleelqqtiq
      181 qtlaaheiqi nqyslnnivl hyaisierir qghslnigps ipllqekpef llaeeigdsl
      241 aqeydihfsk meleqlsllf igmqnenlak esdqqlstfv dpkiirvlkd vlyeveqtyl
      301 velhdqdffn klaihiqsly yrshyetftr nsslldikta ypltydlavy issliqerld
      361 iwfnddeisf ialhigafle tkrhhqnqit irlivndyhd igqqlskqiq ekfsdslvvl
      421 vterqaenla acdlllttdr rvasahagsv fihpflttkd ikkienriea vksqrekkrm
      481 yqaidafilp elyfnqidps elnpeeirqq lcqqmvaadl vdeyfiqrve krermsptsf
      541 psgiavphsv eleakksgva imtlqepliw anypvklvaf iainkeeant fndffekfie
      601 ivsepvntkq lsmsedydef ilklkmmvea de
//
LOCUS       WP_010755132             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010755132
VERSION     WP_010755132.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..283
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31744
     Region          1..283
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnlfkkfaem dhltnnekal vayiladpak tltfraqela daafvsvaal yrfinklglt
       61 gmgelkvela sslkesqssa aidydypile sdtpfqiten lnkiykrtid etltfsdpee
      121 laaigqalqk aktidiysas anlffaknfk fqmqeigvlv nvpeedymqr lsaansdadh
      181 laivvsyggr gqtlnavvei lhenqipivl itsvqdnpla sfadykifma sienhydkvs
      241 sfstrmsllm ifdtlyavyf nhhyeqnvaf kianyqkink elk
//
LOCUS       WP_010755140             223 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010755140
VERSION     WP_010755140.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..223
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25878
     Region          134..210
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mkkivvltnn vyaeqsfqdk llvlshevyc skclleelps elityfdill fsetipdqdv
       61 skllsgikdq nivvirksve rlsteekadw veqgiagwld ytvtieklre sldeiiranp
      121 tpltktvaks tvsrkikfsk ieyriictll eqedffmtrp dlcwhlwnek psnsrlvqls
      181 tmvnnirrkl rlegveadai ktlwnkgyql sqsldwkafy qqv
//
LOCUS       WP_010755279             269 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Enterococcus pallens].
ACCESSION   WP_010755279
VERSION     WP_010755279.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..269
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=29816
     Region          5..269
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mrrkimigll lllvfipfya fkiepnlavv hrlelgdqsk paelkvvqls diqvsesyat
       61 nrldkvikkv nqenpdiivf tgdlfdnyaq ynheqeiidk lsqmkatmgk yavwgnhdyg
      121 ggasrvyqqv mnaanfevlq ntgetitlan gkqvfiggld dsllgnpsis gtlayrqgyd
      181 ysillthepd vadgfigtnt qlvlaghshg gqvrlpfyqv knvlaekyvr glyelsdytq
      241 lyvntglgtt aiharlgvpp eissftlhf
//
LOCUS       WP_010755284             236 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010755284
VERSION     WP_010755284.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..236
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27720
     Region          3..236
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtipkyqiik delkqqiiag rfengdkfyt eaelvkmfnv ssitviraln elvkdgfivr
       61 hqgrgsfvsr arkgklvefs dielfpinhd qvkvlsitrg ndpeylnrlg ltetafyyci
      121 ervrttgdvp yiyhqtylpe qyvnpnypdl syynsiyqrf kldynihmnd esfvetneik
      181 fpapakacek lqiikeepvv lqvritkrkd teqileyvet fkkwnfykie lvsnsn
//
LOCUS       WP_010755313             234 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Enterococcus pallens].
ACCESSION   WP_010755313
VERSION     WP_010755313.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..234
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27003
     Region          4..234
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mkktaiffdv ddtlldnhna frqtlcqlwp nwqvsqgelm rlyqkfrads etiyaqaqte
       61 kahvflsshe rwahlikeig asgeqspqqa dqlyhkyqqq enlspewvql fkqlqnqtsv
      121 qvgvftngfk kvqqkkiaql klanylvpew lliseafgda kpnvscfekl kiclpstieq
      181 fiylgdsyrn divpslaagw qpiwinrfee trtqkgviea tsipeavrql qqll
//
LOCUS       WP_010755328             563 aa            linear   BCT 01-JAN-2025
DEFINITION  molecular chaperone HscC [Enterococcus pallens].
ACCESSION   WP_010755328
VERSION     WP_010755328.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10178812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..563
                     /product="molecular chaperone HscC"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
                     /calculated_mol_wt=62844
     Region          4..343
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mavigidlgt snslasfwdg eqvvlianrf gsyltpsvig vdenndilvg eiakqrlvsh
       61 pqktaaafkr fmgtekmyql gsysfspief sslvlsslke daelflqepc devvisvpay
      121 fnniqreatm eaaklaglnv lnliseptaa amayglhqee dlsilvidlg ggtfdvslle
      181 mfegimqvea iagdnqlgge dftqliirdc lvkskleqea lpaavlsviy qkaemlkrel
      241 sfqarsgfef ekdgtiysye ltkpqyeklc epllakmrlp vgrvlndkkm tveeidrvil
      301 iggatkdpvv rsflakllrt ipytsinpde avgigagiqt alkkdhsmvs elmltdvcsh
      361 tlgvesvrel gnewingvft piiernttip vskvetfytv rdqqpkirfa vyqgesprvs
      421 enlkigeiii pldpapkdyp vdcrftydts gilevlvtvk qtgethqlii eespgklspe
      481 eiqhslnkle klkihprdra enrlltarle rlyaettgek reyiqtlllr feaelakqdd
      541 qiikklvkel tetlnefekg mwl
//
LOCUS       WP_010755332             400 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Enterococcus pallens].
ACCESSION   WP_010755332
VERSION     WP_010755332.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..400
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=44393
     Region          51..383
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mfqlgkgdek vkrkewndal llpillllil svwvqyqaal ldgravqpvi fkqlifsgla
       61 lgallvmrri pflflvkfap iwysfslgvm lllhwyydpt mylltgtkrw lrigplslqp
      121 semvkisfil mlvhftlkye kqarphslka dggyiiksla ialptfllmf mqrdfgtslv
      181 fisvlaalfi vagvdkrill agagaltllg gclllfvfte wgrgilqalh fkeyqlnrve
      241 awidpfkyqd sisfqqvrsm lsvavggfag ksselasiyv pvresdmift viaeksgfig
      301 ssgvlflyfy lfyqmltagi qtnnrgclyf svglvfallf qtvenigaai gilpltgipl
      361 pflsqggtsm itvcvglgiv lgmekpkkgr rvaalstlkr
//
LOCUS       WP_010755393             472 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus pallens].
ACCESSION   WP_010755393
VERSION     WP_010755393.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..472
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51821
     Region          2..417
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 meqkkkfslm sailsvicvv fvaeaaapva aignsqffww ifllvafllp yglisselgt
       61 tyigdggiyd wvtkafghrw gsrvswyywi nfplwlasla vmcpellttm tgiefpvips
      121 iiiqlvfiwl vvwisfypvs dsvwilngaa vikmilavli gglglyvaft rgmaneftvk
      181 smlpsfdlns lsfisviifn llgfevictf addmenpkkq ipqaivaagi viaaiyifsa
      241 fgigvaiptd qistgsgmmd sfklltgstg gwfiilmaff flltlfgnmi swslgvnnta
      301 cyaaengdmp kffakrsqkn empigaalmn givatvvvvi apilpnqdlf waffslnlvm
      361 fllsyvpvfp afyklrkidp dtprpfkvgg gdgmlkllvi apmlmiiisl vftaiplqfd
      421 aatlaeqlpi tigaiifilf geaiivfkki tkegadnnge enrsdntetr rv
//
LOCUS       WP_010755454             255 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010755454
VERSION     WP_010755454.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..255
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29515
     Region          <74..158
                     /region_name="PLN03094"
                     /note="Substrate binding subunit of ER-derived-lipid
                     transporter; Provisional"
                     /db_xref="CDD:178642"
     Region          155..230
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mqhvliltkn slaeeplvqk lqrmnceilc stdlfkrlka gtispflsyf qwmilseslc
       61 nsevehilqm lknhpllvlr vvenipneee qaywqerglv dwisketsye llrekmnelq
      121 qqvkqdvaig nqiltfptiq geettsnnlk llikslskte krvfecliqs ystsgvlsrq
      181 elcnylwqdg gtssnmsqls clinklkhkf elhgikgeti ttlwgrgykl ssafyeywle
      241 nsqqleelky ysams
//
LOCUS       WP_010755481             299 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010755481
VERSION     WP_010755481.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..299
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33707
     Region          1..292
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mknhyldqri rikrpklsdt eqkianylvh seegvahktl delaneigvs qssvyqfvkr
       61 igyggfqefk idiarnsnyq pnfqavntms gtsgtddits edssidiakk vlqsnlhsls
      121 nsthfiteel ldnalaliys aktlhffgqg gstivafdsf hkfirtkyrc nyvfdyhmql
      181 sfatkltsed cvfifshsgq tkesinlarq vkktdaklit ltgnggselv nlsdeaiivv
      241 tdeslfrtea lssrigyltv mdilytnvmh hnydqntdsl kkirdnistt kidphnfmm
//
LOCUS       WP_010755504             723 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-galactosidase [Enterococcus pallens].
ACCESSION   WP_010755504
VERSION     WP_010755504.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 723)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 723)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 723)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11245829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..723
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=82330
     Region          29..282
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          287..632
                     /region_name="Melibiase"
                     /note="pfam02065"
                     /db_xref="CDD:307952"
     Site            order(333,364,408,473,477,523,542,545)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          646..719
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mpilydsekq ffhltnsqis yvigiekdry lvhryfgsal pfytgsnalq ridrgfatnp
       61 deldrsfsln alpmetstqg ngdhrisnyq irsangsnvt nffyrshkit sgkpvlpglp
      121 slrgeqaatl evslydavqd lemvllysiy ddqpvitrsv rfenhgtntv flenagsmml
      181 dlpstqfdli tlngahtnea nlsrqplhag iqkiessrgt sspqhqpfla ladpstnefq
      241 gevyafhfiy sgnfaaqvev eqygssriql giqpetfewr lepkqdfqtp evvinystag
      301 fngmsqtfhd lyqqhlvpaa wqkqerpill ntweanyfdf hetellrqad laketgielf
      361 vlddgwfgqr nddtsslgdw qenleklpqg iagladkihq kglqfglwfe pemisrnsql
      421 fkthpdwalq vpdypltegr rqyvldlsqt vvqdylieml ssylatgkid yikwdmnrhl
      481 tevgslafpa nqqkeishry vlglyrilei itskypeclf encssgggrf dpgmmhympq
      541 twtsdntdal crsqiqygys ylyppimmga hvspvpnhqv gritnlqtrg liamsgnfgy
      601 eldltnlpan qqaeiaqqit fykahrslfq fgrfyrlqpa neffatawlv vnkeeaaviy
      661 fnglarpavp vkylkthyle dqaiyqdlat gqqisgaeln yagitiprik edfatllfhw
      721 kkc
//
LOCUS       WP_010755518             375 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Enterococcus pallens].
ACCESSION   WP_010755518
VERSION     WP_010755518.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..375
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40373
     Region          1..373
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfteeqvmi rdmvreftkk eveprdawmd vsgfdhdlhk kmsetglmgi hlpeeygggg
       61 gdavtsaivi heiakgsase alfldahwla adcilhhgte eqkkkylpma aagqifafgl
      121 teacagsdva giksiavaed dgwvlnggka witnsgiadv yvilaktepd agargvsafi
      181 ieantpgliv gkhenkmgmr gtsttelsfd nlrlpkdall gnlgngfkia mialdgaris
      241 igaiatglae hamelarkya nerhtfgrpi gkhqgvmfkf admsagiram tlmtynaaqi
      301 kaagkrhtle aaevklfsge tcfnicnecl qvfggygysk eyhverfvrd akllqigegt
      361 seilrmligs tvlaq
//
LOCUS       WP_010755524             424 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010755524
VERSION     WP_010755524.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 424)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..424
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47364
     Region          26..246
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          160..349
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mmfiqhafln lkrnkrndff igllffgill sffcllqvyg avehslaetk kqtdtlinvk
       61 pdfekqehvt nlneadlqal nelpnveesv lmgysavevt glvmdagenv etvhsgavst
      121 mrtpqmgvta ldnaslkryf qaskkvsfqg elpleqgtcl vteqvakgnk lklgdelsig
      181 ngskklkivg ivsgkqelqe vfggifinlq tneylaegkq ssfntvtvrl ssqqaarafe
      241 kelrklpafd qyqiyadqey lqvfdsfvsq qelllngvia agvlslffvv lfysqlfkrr
      301 esdifalrlm gmrpmqligs nileitlial lssclayvca sfiseglvan wlrglrqtst
      361 tqiplitikq anlsaaeirq llenskflkf llpyfasmll vivgltsrmi fvfgeysfql
      421 rrsi
//
LOCUS       WP_010755527             224 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010755527
VERSION     WP_010755527.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..224
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25147
     Region          2..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtilkaknvs yfyqdgdqkr iilqdtsisf eqgqfytilg dsgsgkttfl slisaldepk
       61 sgqilyhdkn ikeigydeyr rddisiifqn ynlvpyltal envlvamtit dnklpaaqqe
      121 vaynlldyig itktkadrlv tqlsggeqqr vaiaralstn vdiiladept gnldeemeqe
      181 ivdifkdlaf thnkcvivvt hskeiakqsd ktfflkqgel vsye
//
LOCUS       WP_010755526             489 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010755526
VERSION     WP_010755526.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 489)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..489
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53291
     Region          165..488
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnywkrawss vsrrkgksli lfavifvlgn viagaiaiqq stgnvekkmk qqlgatvsae
       61 vdldklmqgs dstaamkgpe plkeelvkki gessyvkdyd ysytgyltld sfktyqleqd
      121 sisinggmnm ltlkgsnkte padfknkkvk lvegsfpsqe dikngqstav iskkvadeng
      181 lsvgdqmvld ttfvsqkadg stdsqeslkh svkivglfep ikldkkkndg kgggiqeqfm
      241 emdqfntaym pnklvksitq aefekgkeid paayddasst dqitpiytlk spddveafke
      301 emstmlpegy katastdefd kvgasvkkls tisgyvvils iiaslliisl vvvlflrdrk
      361 hewgiylslg errknimrqv vlellvislv amclslvtgn flgklisesl vssdalaevq
      421 saagsqmiva gsqslgsglt tddvinnyev tfslsyivtf lvsglatvll savlpltyvm
      481 rlnpkkimm
//
LOCUS       WP_010755549             217 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010755549
VERSION     WP_010755549.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..217
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24738
     Region          1..202
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtqsiessay qeikqailyg riepdeilse aslskklghs rtpirsalkq leqeklvvyk
       61 knrgvtlrea svkemvdvtq icvewmilat kkaqtglsil dvdaiqerlt aaknyraald
      121 yaqyinqmpk vytkimeaag nelliptyen lwarvistsl yrkmadphns pkktistvqf
      181 fqeylalien nqfdqaiakl mdyqeyanhq ilhygtl
//
LOCUS       WP_010755641             363 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF917 domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010755641
VERSION     WP_010755641.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..363
                     /product="DUF917 domain-containing protein"
                     /calculated_mol_wt=39097
     Region          26..356
                     /region_name="COG3535"
                     /note="Uncharacterized conserved protein, DUF917 family
                     [Function unknown]"
                     /db_xref="CDD:442756"
ORIGIN      
        1 mewitvddln diatgatllg tggggdpfvg klmalqalqk ygpvkvlsvd elddkamvmp
       61 vgaigapsvs nekiaaeeel fapvealkdf fqektqaimp ieigggnsml piacaakmgl
      121 pivdadamgr afpesqmvtf flkgyqpevv amadsqgnri iyypkdgews ekiarsitdv
      181 mggnanmvdn vfpgeivkec airgtlslak eigatlsrlt dsaspvasll nklkgyslfe
      241 gkinhiernv eggftrgrtt lsginqnkge elevlfqnel llakkngevv astpdlical
      301 dhetgrpitt etlrygarih mialpcdpkw rtekgievag pkyfgydidy vpveklmgek
      361 vhv
//
LOCUS       WP_010755665             310 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010755665
VERSION     WP_010755665.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..310
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34894
     Region          3..224
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mmieienlvk rygdflainh lnlsvkqgdi lgllgpngsg ksttincvls llsydrgnik
       61 ifgeemgpnk ynikqkigvv pqeiavfeel nvkdnidyyc glyindkktr aqyveevisl
      121 vgleefckff paqlsgglkr rlniacgivh kpelifldep tvavdpqsrn kilesikeln
      181 rqgativytt hymeeveilc nqiviidqgq viaegtkeql knmvrtsekv imevpdisqv
      241 qlkavselpg vsdvsydemy ltlytkelkq smlpvlsyfe qenipyanlv teeatlndvf
      301 leitgkelrd
//
LOCUS       WP_010755712             825 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010755712
VERSION     WP_010755712.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 825)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..825
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91057
     Region          122..402
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          587..>768
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mkmvntvawa ntkfhrrkni ltgvaiilts vlvflivtig lgtvntqnaa vnkifptwht
       61 myrsvseenk dklaqhaaie tyglrqdvgq igldegsail lhldenaqrl nktaidegra
      121 pesgneavfs ltmlkqighd qaklgdeltl pfqrytedgm glaeptafki vglmddtqta
      181 ngnnmyailv skefmeanip sdqrayrmmi rlaaeefatt devekeakki gksfnvlesd
      241 vvinqeylfa nyvdpafysg miivigiilv agaltiysiy yvsliskvqe fgklkalgat
      301 kkqvhqivlr enllvaciai piglvigmia tklffgrivg ilqegsvltt tmqqivrdne
      361 vqliipwvia ltigislvtv lvaslkpmrl askimpieam rytgqneskq kkrsgfteln
      421 lerltganla rnkkrtliti vslgligilf vavstvfncm qpeeiahqli aedfrlglet
      481 wsgdqmnper ewrklqqnnp ltpetiaair qlpgvekvdt qeiisgelts ikevdtgepl
      541 avsiagikes qmkeitkhle kgsatyeklt egnyliaggf mlknypdlel gkptevivfd
      601 gdkrsvekmt iiaagylpek ivhsaslias ektvralsdn nlikfvdika nsqqlpavkk
      661 eleaikgese fyqlesyedl lrtwesatlm tvgagysill vlavvgimnl vnttidsils
      721 rkkelgvmqa igmsnkqmrk mlqleslfya ggiillsvgi gsiagyliyr yaaanalmqi
      781 qnyyypfvqv gllilvtvvv qllltiattt ivnkesviqr iqaae
//
LOCUS       WP_010755744             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Enterococcus pallens].
ACCESSION   WP_010755744
VERSION     WP_010755744.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..269
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30178
     Region          11..198
                     /region_name="YycJ-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Bacillus
                     subtilis YycJ and related proteins; MBL-fold metallo
                     hydrolase domain; cd07733"
                     /db_xref="CDD:293819"
     Site            order(63,65,67..68,128..129,150,198)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293819"
ORIGIN      
        1 mlemnhafqi svlasgstgn slylesaekk vlvdaglsgk kitsllaevn rkpedldail
       61 vthehrdhih gvgvlarkyk lpvyanektw eamaplignv aleqrqifem gkvltfgdmd
      121 iesfgvshda aapqfyrfyk dgrsfvmltd tgyasdhvrg tirnadaylv esnhdlemlr
      181 mgpypwslkq rilgdrghls nedgalvmtd iigdntkriy lghlskennm kelahmtmee
      241 tltrydlgvn yqfniydtdp ecstelfai
//
LOCUS       WP_010755768             129 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF805 domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010755768
VERSION     WP_010755768.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..129
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15469
     Region          3..117
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 miqaykeywk nitvmdarat rsqywwpqva nylvlflysw ltnlsryydf stesvkelni
       61 rvliflvlsf liwlanftvr arrlhdtnks nwwillyiip ilgpiimfvl lilpskpfsr
      121 wtinqsels
//
LOCUS       WP_010755801             256 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            pallens].
ACCESSION   WP_010755801
VERSION     WP_010755801.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..256
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28724
     Region          1..256
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlsviedrqq qivnylkvnq farvvdliel vnyseatvkr dlimleksgl irrtrggami
       61 vdnkkidvpy lmkvtrldee dnkqyianva atlikddmvi fldssttslh liknlskfdg
      121 lqiitngvlt aamlseftsa hvsilggsiv pkratingsk ayndslsyna dmafigcrgl
      181 dfehgvteth egeafmkkaf rrqanqlvvl atadkldhky myqgiachei dylitdqpla
      241 aekmkklhnh hikcly
//
LOCUS       WP_010755795             344 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Enterococcus
            pallens].
ACCESSION   WP_010755795
VERSION     WP_010755795.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..344
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37692
     Region          4..341
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 malielrqve ktfsgksgqi havsgvdlsv epkdvygivg ysgagkstlv rllngletat
       61 kgevvikgqd vakmhgtdlr sfrkkvgmif qhfnllwsrt vleniqlple lagvakeqrk
      121 qkaeellklv glegrgdayp aqlsggqkqr vgiaraland pdillcdeat saldpqttee
      181 vlelladine klgltivlit hemnvirkic nkvavmeqgk iveegfvkdv frhpqqevtk
      241 lfvqqelepk sdtseltkef lkenpdgtlv tlhflennag epvvsqairk fqvdisivyg
      301 nieradgnsf gtltvqltga steidqalaf irsqnvdvev ihrg
//
LOCUS       WP_010755812             759 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus pallens].
ACCESSION   WP_010755812
VERSION     WP_010755812.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 759)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 759)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 759)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..759
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87712
     Region          4..755
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mnqiqrlfdi dpwkirtttl dkqnrrlqes ltsigngymg lrgnfeetys gdhhkgtyla
       61 giwypdktrv gwwkngypdy fgkvinaidf lqmkifinev evdlakqemv dfelelnmqn
      121 gvlsrsftvv lgdakvrfsf erflsivkke lavikltaec lsgdatikii ssldnniqne
      181 dsnyeemfwi ekerghkeei sfltaqtvpn nfgieqfsit aamkhlgtle aqvqhddqli
      241 vseqfewtlt ageaaevekr vviltsrdlp eakqreaaae llttydqtyd elykeqsaaw
      301 akrweladvl iegddeaqqg irynifqlfs tyygdderln igpkgftgek yggatywdte
      361 ayavpmylal akpevsknll kyrhnqlpea kinaqkqglk galypmvtft giechnewei
      421 tfeeihrnga iayaiynytn ytgddnylkq eglevlteia rfwadrvhfs krnqkymihg
      481 vtgpneyenn innnwytnti arwvlkytle nylryqdsts viitkeeqvk wqdiienmyl
      541 pedkelgvfv qhdtfldkdl mpvsdlaped rplnqkwswd kilrscfikq advlqgiyff
      601 ndqfsieekk rnfefyepmt vhesslspsv havlaaelgk eeksvemyqr tarldldnyn
      661 ndtqdglhit smtgswlaiv qgfaqmktfn nklsfapflp skwqsysfhi nyrgrliava
      721 vngdevalsl kegtpfnvdi ynqtvelvne vtvplikeg
//
LOCUS       WP_010755847             281 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010755847
VERSION     WP_010755847.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..281
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31465
     Region          2..267
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mkkrrfswsn lylilvfvll yvpifylify sfnaggtmts ftgftwehye tlfsdtrlis
       61 ivlqtfvlaf lsaliataig tfgamsiyyt rkrgsrnall glnnilmvsp dviigasfli
      121 lftmlggylr sfqlgfvsvl lshvafsipi vvlmvlpklq emndsmidaa rdlgannlqv
      181 lsnivlpflt pgiiagyfma ftyslddfav tffvtgngfs tlsveiysra rqgisleina
      241 lstlvfifsl ilvigyyfis rdntkkakkr krefeevavl k
//
LOCUS       WP_010755860             644 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus pallens].
ACCESSION   WP_010755860
VERSION     WP_010755860.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..644
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72938
     Region          6..532
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          566..629
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mlllqanqia ryfgaetlfe nihleidsra riglvgrnga gkstllkiia gidppdagqi
       61 tknkqatlgy laqdtglasc etvwnemlka fapviamekr mrevelaisq asesdnnyds
      121 lmkeydqlqh dfnesngygy eneirsvlhg fkfdesfyek pidtlsggqk trlalarmll
      181 vrpdililde ptnhldietl awledylqgy tgallivshd ryfldrvvne iyeisrrkmt
      241 hyngnyskyl dqkaaqlasd wkayekqqae idkledfvar nlvrasttkr aqsrrktlek
      301 mdrldrpdgk eksarfmfai ekasgnvvlq ledaaigyed ilsepvnldv rrqdaialvg
      361 pngigkstll ksligqipfi kgeahfgtnv sigyydqtqa elsgnktila elwdehpttp
      421 ekdirtvlgg flfsgedvek tipllsggek arvalaklsm drenflilde ptnhldidnk
      481 evlenalidy egtllfvshd ryfinriatk vielspegsk lylgdydyyl ekkreeeeia
      541 ellaeetaea apppknkfyq dketqkmirs lrrkveatee alaaldttia qleqamvqpd
      601 vlndhvrlme ltqeleqhka dqeeqmaawe elsleleemd eats
//
LOCUS       WP_010755891             875 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus pallens].
ACCESSION   WP_010755891
VERSION     WP_010755891.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 875)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 875)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..875
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=101688
     Region          566..765
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mrkelaaakk elfvpakdgk vhffvttcsg nnrgkvwqts gdnfeqgwlk veqyletfpl
       61 fpkwvkieri dtankmsaed gqqafyqtqr dnyfpygvaf nedndltflp eeitgnallv
      121 phpehriarr darlmiseah vqaysqyrdq cdlssplhfg kewtfftkkg vfieegkmys
      181 metegygqgv reinddnqwt mleqgirrga hylidqitet gkfiygyfpi ggrkinsyns
      241 vrhysslyal leaydylreq elveadflek ieqglqwglm hltkvteday yvvdgeelkl
      301 gaqamvilal tkyqtvtgnq qflpsiekfl ngmksfiaed gstthvlnee lteseafrii
      361 yydgealfai mrayplvgkk ewldlaellm nhfiqkryer yhdhwlsysv nelttylpkr
      421 kyfefgvrna lenlafiekr dtayptmlel vvaavkmfdr iqeidfeepl fsaeeftwlk
      481 rvmekralhe lrtgtmwpel amffaqpeti aggfyvrhdr crmriddaeh flsglinyql
      541 yhspevvset ltnekdenpe edslaisvii pvynrekeia kcltqlaqat fdhsqfeviv
      601 addastdqti evvekfqkdf ehlrvlrlpk nsggasvprn eglkqakgrw vvfvdsddyl
      661 tphaledayq laieeeetdl vcmpyfraag srralsrscf qsstavtgmd fletklynsl
      721 nivgklmrke vvdryqlefp tkirvrednw fsmklyavvr kiaflgnkkd yyfcgewdtv
      781 slskigtppr damkiyaevf rfifsleevp qkrkadllai ylnryaamik rgkyaptrlf
      841 qqighslyli kgstyldqea kqfindlysg ryevq
//
LOCUS       WP_010755931             163 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Enterococcus pallens].
ACCESSION   WP_010755931
VERSION     WP_010755931.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..163
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=17677
     Region          2..162
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mkigiiyyth gghtheiaec iakgihskev evrlfslseq ldteylneca giifgtptym
       61 atshwrvvew ltkdrsiklg gklggcfata hyaqggsdsa imslvgilmt kgmlvysggs
      121 algkpfihhg pvaldavgnh feeskelfei fgqrfaakal elf
//
LOCUS       WP_010755954             593 aa            linear   BCT 01-JAN-2025
DEFINITION  V-type ATP synthase subunit A [Enterococcus pallens].
ACCESSION   WP_010755954
VERSION     WP_010755954.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF003220.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK04192
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..593
                     /product="V-type ATP synthase subunit A"
                     /EC_number="7.1.2.2"
                     /calculated_mol_wt=65170
     Region          1..584
                     /region_name="NtpA"
                     /note="Archaeal/vacuolar-type H+-ATPase catalytic subunit
                     A/Vma1 [Energy production and conversion]; COG1155"
                     /db_xref="CDD:440769"
ORIGIN      
        1 mqegkiikvs gplvmaenma eaaiqdicyv gdlgvigeii emrgdvasiq vyeetagigp
       61 gepvkttgea lsvelapgiv sqmfdgiqrp ldtfkeltks nflargvqlp aldhekkwwf
      121 eaivevgkev tagdiigtvq etklishkim vpfgvsgkvk kvasgeftid dtvyvletvd
      181 gdkefsmlqk wpvrrgrpvk eklnpeapmi tgqrvidtff pvvkggaaav pgpfgagktv
      241 vqhqiakwad vdlvvyvgcg ergnemtdvl nefpelidpk tgeslmerti liantsnmpv
      301 aareasiytg itiaeyfrdm gyniaimads tsrwaealre msgrleempg degypaylgs
      361 rlaeyyerag rvltlgegsr egsitaisav spsggdtsep vtqntlrvvk vywglsatla
      421 qqrhfpsidw iasyslysse vgkfldnamq sdwsamvadg mrilqeesql seivrlvgid
      481 slsekdrltl evakqiredy lqqnafddvd tftsrekqfk mlnniltfnk egqralelga
      541 ylkeiidgti tlrdriarsk yiaeteldil dqinqditle iqaiiaeggm tnd
//
LOCUS       WP_010755972             345 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010755972
VERSION     WP_010755972.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..345
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38371
     Region          26..341
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mlseirvlea iapdvlntvk rryrvlqnif wmqpigrrnl aeslnlterv lrgetdylrd
       61 qrliettksg msltergkei lqqldllmdq ftgmdqlekq lalmfnidrc livsgdsdeq
      121 pkvigdfgel vnealhrllp dgrnviavmg gttmaeiarh itpletnnrk nlfvparggi
      181 gesvsiqans vsavmaanak gnhrvlyvpe qlsqeayhtl lkepsimdvl atikqancvv
      241 hsigralhma arrkmleeei vslrqrkava esfgyffdes gqivyrasrv gltledvqki
      301 pivlavaggk skakaimaym knapkqtwfi tdeaaaneil kgvtl
//
LOCUS       WP_010756119             708 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus pallens].
ACCESSION   WP_010756119
VERSION     WP_010756119.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..708
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80610
     Region          16..638
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mknlksptfl nkrlgfyall tfllwaksif aylfefnlgi eslrqyfilf lnpiattmfl
       61 lsialyvrrp kaayrtmlfi yalatillfs nvvyyreftd fitvntllga gkvasglges
      121 airlfrpydl lfvldlvvlp illwkkvikr eerpvrarma famtalsvmv fsanlflaea
      181 drpelltrtf srdylikylg vnaftaydgi qtyktnqvra easpndltev esyvknhyaa
      241 pndelygiak dknviyihle sfqqflidyk ltdengqehe vtpfinsifh qnstfsfdnf
      301 fhqvkagkts daetllensl fglnqgslft qlggkntfqa apdilkqeag ytsaafhgns
      361 gnfwnrtety krfgydyffd ssyydvnedn sfqyglhdkp ffqqsvkyle rlqqpfyskf
      421 iavsnhypys efqndeagfp mantddetin gyfatanyld kaveeffnyl kasglyensv
      481 ivmygdhygi stsrnselap llgktkeswt nfdnaqmqrv pymihipgqe ngginhtygg
      541 evdalptllh llgidsskyi qlgqdllspe ndqlvafrsg dyvtpdytyy ggslydnhtg
      601 fmvtapdenl qakadgwkqa vsdqlstsdd inngdllrfy tgsgmetidp sdydyknglq
      661 qlqktesklg dkstsvyskl gtstenlynt qtykqyhste esatpvqe
//
LOCUS       WP_010756129             148 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus pallens].
ACCESSION   WP_010756129
VERSION     WP_010756129.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..148
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16344
     Region          3..140
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mdfqkilvav ddspssvaaf nyavefaqlv naqlavatif eidqlnvyey lspdvlrkqk
       61 dktinlaeey vrkakekglp apeafvyegg paeviikqil payqpdllic gssvrkkhkn
      121 llgeqadymv rnaicsvfiv kndpsvkp
//
LOCUS       WP_010756163             151 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Enterococcus pallens].
ACCESSION   WP_010756163
VERSION     WP_010756163.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..151
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16678
     Region          3..149
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mkfetslgtl wldaneqalt avsyteises kianqdilkq akeeillfle gqltiftvpy
       61 eftygtafqq evwqalaqip ygktccyqdi aeqiqrpkav raigqanrkn plpiiipchr
      121 vigksgqltg ysgssaegla ikqqlltiel n
//
LOCUS       WP_010756185             833 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Enterococcus
            pallens].
ACCESSION   WP_010756185
VERSION     WP_010756185.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..833
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=93309
     Region          5..818
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mdqlyterak avlaiaqeea kyfkhrsvgs ehlllalvie qqgiagktlr qmnanendir
       61 eeiehmtgyg smqtypegsy lpysprakqi lifaddeakr fnaklvgteh illgllrdde
      121 ilashilvnl glslpkmrql llkkmgvten asqnhqgmgr rkpaakssqq ntsqgtptld
      181 slardltkla rekrldpvvg resevrrvvq ilsrrtknnp vlvgepgvgk taiveglaqr
      241 iisndvpedm rgkrlmmmdm galvagtkyr gefedrlkkv ideiyhdgki ilfidelhtl
      301 igaggaegai dasnilkpal argelqtiga ttldeyqkyi ekdsalerrf arvqveeptp
      361 eeaeqilkgl rpryeehhgv eitdealhaa vslsvryins rqlpdkaidl mdesaakvrl
      421 dttdeiseld elqreiqnlv eekekaiqnq dfeaaarlrm kekqmtqele qaaiteakqe
      481 ngyinrvtde dvaavvsqwt gvplqqlekk esqrlldles vlhkrvvgqd tavkaisrai
      541 rrarsglkdp nrpigsfmfl gptgvgktel akalaeamfg seealirvdm sefmekysts
      601 rligsppgyv gyeeggqlte kirqkpysvi lldevekahp dvfnillqvl ddghltdskg
      661 rkvdfrntil imtsnigate ireeknvgfn vkditkdhda mekrileelk kafrpeflnr
      721 idetvvfqsl dqeqiheivk imsrsiverm teheikvkit ssafdvigkv gfdpeygarp
      781 irralqkeve drlaeallsg qiqlgdavti gaskgkitlt vrapkenkvp qev
//
LOCUS       WP_010756227             269 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus pallens].
ACCESSION   WP_010756227
VERSION     WP_010756227.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..269
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29454
     Region          4..263
                     /region_name="HAD_YbiV-Like"
                     /note="Escherichia coli YbiV sugar
                     phosphatase/phosphotransferase and related proteins;
                     belongs to the haloacid dehalogenase-like superfamily;
                     cd07518"
                     /db_xref="CDD:319820"
     Site            order(9..13,44..46,67,151,153,187,195,217..219,221..222)
                     /site_type="active"
                     /db_xref="CDD:319820"
ORIGIN      
        1 mgikmiavdm dgtflddqka ynherfqqlf hqmqekgikf vvasgnqydq lksffpdnhe
       61 kmsfvaenga nivlegehfd narldmkvvl aalakietld ptaivlcgkn sayvsaqlpa
      121 erfesvqfyy psikrlenla diqtesddif kfalsfpnin ipgkvaaltd llaedlipvs
      181 sghgdidlii pgvhkaygls klcqvwaisp selaafgdsg ndiemleyag fsfamenaqp
      241 avkkaagkvi gsnnqesvfd iiealllkv
//
LOCUS       WP_010756260             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010756260
VERSION     WP_010756260.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..264
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29987
     Region          1..264
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mqedifilie scrlnftave qviadyflsk qqapknidql sedlavskas itrfckkigl
       61 nnykelifly klsldkdetd lsvsskvtaa yhslatrsds tyskevvdaf cgylhqhkii
      121 hffgkgfnsy agadfqfkfs rvgkyvrvia densilmsan fankdelivv stlrgddeel
      181 leamkiakkr dvpillitsn qfsqlipyan vvllaasftr eeslgnispq ipiliqldmv
      241 yeryihlysd slkqwleseq ilhk
//
LOCUS       WP_010756325             277 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010756325
VERSION     WP_010756325.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 277)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..277
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29610
     Region          6..266
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mallsyefmi raflagifia giapmlgvfl virrqslmad tlshvslagv algfflnlnp
       61 tattllvvvi aaiimeylqn myssyseisi ailmaaglai alvlmklapg ssavsiqsyl
      121 fgsiitvtwp qvgflgalfv lvsilfllfk rpmyvltfde diaavdglpv rlmsmifnvv
      181 tgvaiavmip iagallisai mivpaatgmr agksfnavil isviiglvgi isgltgsfym
      241 dippgatitl cfiglfllmn vfrrvkmmlq rkrnqnd
//
LOCUS       WP_010756298             182 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010756298
VERSION     WP_010756298.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..182
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21213
     Region          3..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 myqkiletae qlfmnqgyea tstrqiadal gitqpnlyyh fkkkediyva vmralaeevg
       61 qqlrqlaken estlteklte mmvylrqrhp fdfymmmhdm hyalskesae elyllwqqsy
      121 eapfievlkk egvalrseiq velavkqlfi llaaylqpet ydkqgnsfpa aidmflygiv
      181 kk
//
LOCUS       WP_010756331             247 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Enterococcus
            pallens].
ACCESSION   WP_010756331
VERSION     WP_010756331.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..247
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27385
     Region          4..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mdsiiqiehl kksfgdnlvl kdinmnvnkg evvtiigasg sgkstflrci nlletptdgk
       61 ilykgenvla dgynlpkyrt hlgmvfqsfn lfnnmnvlqn cmsgqltvlk rneeearkva
      121 ienlekvgms rfidakpaql sggqkqrvai aralsmnpev mlfdeptsal dpemvgdvls
      181 imknlaesgl tmvvvthema fakevsdrvi fmdqgliaee gspedifvrp keartkeflr
      241 rvlhpep
//
LOCUS       WP_010756409             678 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus pallens].
ACCESSION   WP_010756409
VERSION     WP_010756409.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..678
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=77761
     Region          11..654
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mdnrlsnlys llakqetkvk iselaarfhv strtiyndid klnelletve aaeimiekgh
       61 iqyecetpvd iekilfknnd fissdqrirk irmlesvlll pdnfssdtll qqtlvsrntl
      121 lndlravrke lenneiflet ipfrgyrvig eetrirnflv atlgqdplvf etesfqmerk
      181 slveidrlie aicqeigiql sdesfqkvvl hfwvtkkrle vnktikqwpk kdiynkeeqv
      241 llaneetism lfnrsvtqne llhlanklse asitkyqell tdkwltfnli veqfikavdq
      301 dfppidfttd qklyegllnh lrpaykrtla hepienpmyd yvmenyqelh vsvraqvpll
      361 etklkvrftd qeisfftlff aaslerkkff tpqrtriiii cnagvstsei lkskiqntfh
      421 vevlgtfgtr egikwlkenn vdlviatipl elksvpvvqv npylseqdre sinrfvkpif
      481 revnidqllt ivkkyaplsf qaskslsdel ttylnlpksq kkkeyqpmlk eiltpnliel
      541 nylaknrdea vrksgellvh sglatnsyvd gmienvevng tyiviapgia mpharpeega
      601 ldvgfsivtl kepvvfghpk ndpvkivigl caidhqthlk alaelveils heenvacftk
      661 avskteimdi ieggeatc
//
LOCUS       WP_010756362             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010756362
VERSION     WP_010756362.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..264
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30645
     Region          1..261
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 memrtsvlsl llryvnnrek rdnnyhiara mldhfdqipk itiydlselc fvstaaisrf
       61 irqlgfstft afkeacaeki ditndyssky naaapdvypt fvkqfteniq dnvqiianql
      121 dfeqflrine yihqskdvgv fglefasfla qhfqikmael nkytrigltk eeqltaaqem
      181 aegstvlifs leggyfyyne kildilkekk tkiivftlnk tamiertade ivlcgthnen
      241 tegrlsilyi melliyqyfl hyhh
//
LOCUS       WP_010756479             322 aa            linear   BCT 01-JAN-2025
DEFINITION  dipeptidase [Enterococcus pallens].
ACCESSION   WP_010756479
VERSION     WP_010756479.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..322
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36545
     Region          1..319
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mkaidmhcdt imklyqtpea elkendfqid llrmkesgtd lqnfamfipl devddpytvc
       61 remidcyqse igkntdlira ittmaeyeen qaagrlsall tmeegaplag rldrlqefyd
      121 lgvrmltltw nfenelgfpn alywneveqt lnpdqrglte kgieivqrme elgmiidvsh
      181 gsdqlvrdvl tytkrpfvas hsnarticnh prnlsdelih giaerggvig mnyyeafirp
      241 pgsqqslaag linhikhfiq iggiecvglg sdfdgieehp eladirsiek ieqalraagf
      301 saserekify qnverlyref ll
//
LOCUS       WP_010756494             124 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010756494
VERSION     WP_010756494.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..124
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13640
     Region          3..116
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 meiiiqhssm tpiyeqlvqq vkraiiqgsl kendplpsvr slakdlkisa ltvkkaydtl
       61 dqegmiatvh gkgsfvlain pvqkreeqlk vvqseleatv nkariagisd edikelltiv
      121 mees
//
LOCUS       WP_010756522             321 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Enterococcus pallens].
ACCESSION   WP_010756522
VERSION     WP_010756522.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..321
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35675
     Region          10..311
                     /region_name="AKR_AKR13C1_2"
                     /note="AKR13C family of aldo-keto reductase (AKR);
                     cd19078"
                     /db_xref="CDD:381304"
     Site            order(19..21,52,57,81,127..128,157..158,177,205..211,262,
                     279..284,287,290..291)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381304"
     Site            order(52,57,81,127)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381304"
ORIGIN      
        1 mkmrrlgkta ieisaiglgt mgmdhaygpq adrsemikll rkavelgcnf fdtavvygea
       61 neellgeafe plreqvvlat kfgiigqeiv dgepqnilns qpksireqle gslkrlrtda
      121 idlyyqhrvd pnvepeivaa tmkeliaegk ikawgvsnap inyikrahav cpvsavenqy
      181 smvwrepeke lfdlceaygi sfvaysplgn gflsgkiskd tkfpegdfrn fmgrfkpevi
      241 dhnkalldii advaarknat saqivfawel aqkpfiipip gttklhrlke nlgsadiilt
      301 qtelnelnea laklevdeth f
//
LOCUS       WP_010756516             220 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010756516
VERSION     WP_010756516.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 220)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 220)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 220)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..220
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23735
     Region          8..214
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 menmntfqqf feyfqvnggy vfsqfyrhfl isiygvlfaa lvgipvgifi skhyklanwv
       61 irianiiqti pslamisilm lglglganvv iltvflysll piikntytgm rqvdrnaldv
      121 gkgmgmtsfq rlymielpls vsvimagirn alvvaigita igafvgaggl gdiiirgtna
      181 tdgtaiilag alptalmaii tdwllglver rldpatktsk
//
LOCUS       WP_010756619              69 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010756619
VERSION     WP_010756619.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..69
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7804
     Region          1..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mkvinhikei reakgipqya madavgvsrq tmtaiekgky npslelslki aeyfelpfee
       61 ifylegkkk
//
LOCUS       WP_010756616             462 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus pallens].
ACCESSION   WP_010756616
VERSION     WP_010756616.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..462
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50738
     Region          4..443
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 meekkvslvk silfticsvl vldsfvassa igvssitiwl ittvlfflpy glvtaelgsn
       61 ypgdggiylw ikrafgdkig vlngwfywvn vafwmpavfv afsswfsyaf mpeaspifla
      121 glalvmcwli vyigirgvdl svtvtniaai fkvavllifg fmgiayalqh gsandfsvas
      181 fmptpgntvr yisviiynll gfeligsign qidnpgktip kmtvvagvii salyifgtyg
      241 vlvaipanqi dtvdgfyyal lelckvfgsf qmpvfyviil vamstlisnm vswtlganev
      301 fiaakldqrn rflkhrsaky gtpdglyyfm givatfliiv nyattgdana ifwtifsfsv
      361 iilmipylfm fpaaillrkk datmqriyqv pggmtglvvc svlgeaclil siilmfitae
      421 ssfvigtyvv gtiitlllgi wlyhskeqlp keetphlpde th
//
LOCUS       WP_010756624             270 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010756624
VERSION     WP_010756624.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..270
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30817
     Region          2..109
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(3..5,19,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            40
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(51,54,58..59,68,81,85,91,95,98..99)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          120..263
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mfkigefskl snttvrtldh yavlgllipe kidtqsnyry ysagqlglln qikmlqqtgl
       61 plktikeiie tndleflerh ytlqeqklqe dldevmkkqr misllqqtmk egiemtkynv
      121 vvkevaernv lsvreriady tlegelwmkl qqgmqetkak mtqpamnmtv fhdkefvekn
      181 pdvevqttvi geypeaqsvq fkkapsfima svtfsgpfeq mpqvtqalge wieandykvv
      241 gpminighvs paedpnpenw vteagfvvsk
//
LOCUS       WP_010756654             252 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010756654
VERSION     WP_010756654.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..252
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28540
     Region          <57..192
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mkhavkqevf klmkqhvilk qtlkvsglil lvalvtkfgn femlspnklv rtcfnsgwli
       61 vffmvylasq tfsmefrfgt iknllqknqq rrtiffskli tlvgysiyln vvavvvtisl
      121 smilfpevsl eqteiirtlf anllgnfvgm wlfaslalmi slivtnesla smlgiatyfl
      181 ssmlagmqfi lldkfswlrw nplnmlnlsn qlinsgmekl tqlatnqlli gnivyilgfl
      241 liadvvfsrk ki
//
LOCUS       WP_010756679             274 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010756679
VERSION     WP_010756679.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..274
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32041
     Region          10..113
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(11..13,27,45..47)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            48
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(59,62,66..67,76,86,90,96,100,103..104)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          122..267
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mideskenly rvgifsqmnq vtikalrhyd ekgllvpryv dpengyryys asqlpdlhqi
       61 malrkigfsl eeirkvqqgv gknkllrmkk krileeiaer trelsviesy lsdeeelvey
      121 diiekalpei tiasmtltid nygelirymp qmdqelerlg csytnpqycf nryldgeyke
      181 edvrveicea vtamksgetf lefsiipkve navctlhkgs yeqlplsyqa ilsfidqndy
      241 eladlpresy idgmwnkesp eewlteiqip vrrk
//
LOCUS       WP_010756680             246 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010756680
VERSION     WP_010756680.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..246
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26657
     Region          58..246
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mskyltvlri egklslrtpd glffgigmpm avlllismla gnqpagdggy tfmqssypal
       61 atvgicataf mglpltisdy rdkkilkhff ttptspflll gvhvtvcvlt alasalgvtl
      121 vamlvldyrm pgswlgfigs yflvmlamys igmmmaslcq tikqanlvcn lvyfpmlfls
      181 gavipfeifp egmqkiasvl pltqgirllk lvslegissl plfallylli fgilgilvsv
      241 ktfrwe
//
LOCUS       WP_010756704             425 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A [Enterococcus
            pallens].
ACCESSION   WP_010756704
VERSION     WP_010756704.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..425
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=46918
     Region          1..425
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mqqplayrmr prnldevvgq qqlvgpgkii rrmvearmls smilygppgt gktsiasaia
       61 gstnyafrml naatdtkkdl qivaeeakms gtvillldev hrldktkqdf llphlesgri
      121 imigattenp yitinpairs rtqifevkpl seediqlavn salkddergl gsypveldee
      181 alrflsqatn gdlrsalngl elatkstpen degqihltlp iieecvqrka lthdkdgdah
      241 ydvisafqks vrgsdvdaal hylgrlveag dlpiicrrlm vmgyedigla nppaaartvq
      301 avqaaeklgf peariplana vvdlclspks nsayvaldaa itdiragkag dvpdhlrdsh
      361 ykgakdlgrg idyqyphsfe nawvdqqylp dklknahyye pkatgkyeqa lgqqyqriqe
      421 wkkkk
//
LOCUS       WP_010756805             227 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010756805
VERSION     WP_010756805.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..227
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25990
     Region          155..225
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mirillltkn vlseqellqk lqrlnfevfa ssstlellla gdegaelaey fsviilseti
       61 schevesilp rlvndgrlif rkadrsfvee eksilnqeqi tgwlhsdast eeirelislp
      121 yynlgvenqg nhsfasgqfs kldskhmenv lasfsasefk vfqklkqerg htvsreelcq
      181 llwtestqsr mvqlsslikn mrmkfesndi dgeiiqtvwr kgyilkq
//
LOCUS       WP_010756797             458 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Enterococcus pallens].
ACCESSION   WP_010756797
VERSION     WP_010756797.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Kaatz,G.W., DeMarco,C.E. and Seo,S.M.
  TITLE     MepR, a repressor of the Staphylococcus aureus MATE family
            multidrug efflux pump MepA, is a substrate-responsive regulatory
            protein
  JOURNAL   Antimicrob Agents Chemother 50 (4), 1276-1281 (2006)
   PUBMED   16569840
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..458
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50153
     Region          12..439
                     /region_name="MATE_MepA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Streptococcus
                     aureus MepA; cd13143"
                     /db_xref="CDD:240548"
ORIGIN      
        1 mdesknplgt ekvsrliiqf sipaiigmiv nalynvvdri yignapslgq nglagitigf
       61 pimiiliaig llfgvggatl fsirlgekkv qeaeealgna fslliisgll fmllgqlflt
      121 rvltlfgasp tvlpysieym riiffgaifq ivslgmnnfm radgqpklam itmfmgagvn
      181 ivldpvfiyv fdmgmagaal atilsqfism vwilayflgk rshhkihvrn mrlkwqtstr
      241 ltalglpsff iqlansllnv vlnvnlttyg gdiavsgmgi vnsiqtillm pitglvqgtq
      301 piisfnhgak kfqrvwqaqk iaitsataiv vlgwiitria pellvsmfnr dpelmsfsaf
      361 alqawffclp vigfqivasn yfqatgkttv aiiltltrqf lmllpaifif sniwglegil
      421 yaapfsdaas viltgslyli amkklrqeir lnnqldfe
//
LOCUS       WP_010756827             189 aa            linear   BCT 01-JAN-2025
DEFINITION  VanZ family protein [Enterococcus pallens].
ACCESSION   WP_010756827
VERSION     WP_010756827.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..189
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21945
     Region          100..178
                     /region_name="VanZ"
                     /note="Glycopeptide antibiotics resistance protein
                     [Defense mechanisms]; COG4767"
                     /db_xref="CDD:443799"
ORIGIN      
        1 mkkiiagils liasygiiyy lvmptlmhyp rlagmmhrfv ytdealwafl flslwlfyvq
       61 werrqlwtvy lylfysvyal lmfivlftka ehyhalnldi rqvplesgaa viefvlnigy
      121 fiplgilygm rarlveavvl slvtilgiet lqyvfylgtf diwdvltnfa gcmigyglcn
      181 qlkkqfrkg
//
LOCUS       WP_010756892             253 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010756892
VERSION     WP_010756892.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27980
     Region          3..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 maeviieaet ivkevttgst knrildsvsl qlykndftvi mgasgagkst llyalsgmdt
       61 issgivnfqk qditklneke laslrsnsfg fifqqthlvs nltlfenvlv agylsknisk
      121 dsvqkkaahl mtqmnveqar nrlpnqvsgg eaqraaiara mihqpeilfa deptgalnkq
      181 nteevlnllt elnnseqsil lvthdvkaai rgnrilyled gkiiaelllp sfeveeiqkr
      241 erqvtqwlls hgw
//
LOCUS       WP_010756958             297 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010756958
VERSION     WP_010756958.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..297
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33757
     Region          1..286
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mylfqrieea afkqsdarrt igefilenre qlqdlsmeei akqtftskpt lvrfakyfgy
       61 sgwkefmyaf nhevayhddt ayadvdpnfp fsaeedtlei ieslvnlkmq sikdtvslia
      121 aedlnkaagm ihraenvvvy gtspnyyyge lfkrnlltir kkafmaksge sgvishslnq
      181 rdcaiiisys gnnpdenpss nvkillknrv pvisitsggk nylrdysdvv lnisskekly
      241 skianfatqe simlildalf akvfamnyee nkankiasak llesrrqatf kdleerf
//
LOCUS       WP_010756971             262 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010756971
VERSION     WP_010756971.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..262
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=27913
     Region          69..261
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(98,100,104..105,108..110,112..113,117,120,129,165,
                     167,171..172,175..177,179..180,184,188,197,199,201,
                     205..206,209..211,218..219,223,226,235)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          98..129
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          165..197
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          199..235
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mkifqltaaf alllllsgcq aasqqsqasd ssknvpakss stqaasqpqt etttqseedq
       61 smsysagsli qavtannldq tkailssany pldevnehge tplliavhnn qvdiakalid
      121 agadinkqda iqdspylyag aqgrseilsy mlahatpnqa itnrfggnal ipaaekghld
      181 nvkilladkr vdinhqnnyg ytalieaval rdgsqvyqdi vaellkngad ptlvdnygkt
      241 aldyanqlgy gnmakmlqea qr
//
LOCUS       WP_010756985             445 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus pallens].
ACCESSION   WP_010756985
VERSION     WP_010756985.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..445
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=48242
     Region          9..431
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdnqkktmmd rvteftnkis gplarfantd iissvvaglv avtpiimigs iflilyvlgs
       61 pdvgtsgkpl igflaplagk fawmnsltmn mmslycsiai pynyaqkkkm ntltcsllgl
      121 atflifting ydeaggisvt sfsasglfvc iitsivgvqi lkffldknit ikmpdsvppn
      181 ignafgallp fatifgiawl irtimnfdmv awlntllepi itssdslwma mlvtficlll
      241 wsvglhgdnm fialftpfgl twvnqnasal adgvsnydlp nilaglgntg lirltiwtaa
      301 vwpllflmit skrkqfktig ltalapgift ivepviyglp ialnpylmvp filsgtistg
      361 vgyllmstsf fgkfyavvpw atppfllgpl gtgdmktali pflsfaiglv iyvpfwkvyn
      421 qsldaieqqe veeapsvemi qgnea
//
LOCUS       WP_010757005             327 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Enterococcus pallens].
ACCESSION   WP_010757005
VERSION     WP_010757005.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..327
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36053
     Region          10..306
                     /region_name="AKR_AKR13C1_2"
                     /note="AKR13C family of aldo-keto reductase (AKR);
                     cd19078"
                     /db_xref="CDD:381304"
     Site            order(19..21,52,57,82,123..124,153..154,173,201..207,258,
                     275..280,283,286..287)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381304"
     Site            order(52,57,82,123)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381304"
ORIGIN      
        1 mktrrlgtsn levseiglga mgmsyaygav pdkkkmikvl qeavelgehf idtaevygpf
       61 tneeliaeal apykkdvvia tkvgikiidg kqvvdgrpev ieksvegslk rlkreaidly
      121 ylhrvdpntp ieevaltmqk likagkikhw glseagvqti rkahaieplt aveseyslwt
      181 repeeellpt leelgigfvp fsplgkgflt gsldvttefd agdsrrslpr fqkdameanm
      241 qlvnlvkqva ekkqatpaqi alawilaqkp wivpipgttk iervkenmga asiqfsekel
      301 qeltaaanqi qivghrytpe lakrvgl
//
LOCUS       WP_010757016             222 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            pallens].
ACCESSION   WP_010757016
VERSION     WP_010757016.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..222
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24312
     Region          126..218
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 merknqmniv lriilwlvmm ivatlpttvv mltgmiegia gvligavill amlalaafva
       61 dkgdiwtkng rsfmgrgmkl gpaiglaiga glflrvwvvi lnmiipikta ndqalqglag
      121 getssillff smvvmapvle elvfrgyifk fffrenrlaa yllssllftl ihvptdlisf
      181 vtygslalvm gfvyyktnri emsmlthain nllpaivlaf lh
//
LOCUS       WP_010757035             148 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Enterococcus pallens].
ACCESSION   WP_010757035
VERSION     WP_010757035.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..148
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16411
     Region          10..142
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mtkqilkaev esvgglqlkc ssrgfeflid epenvggtnq amnpleallc slgackmmva
       61 rffyqthhiq lktmkvellg eidsdrlkgk pnvkvgfski itnytieadn sqaeieefin
      121 fiertcpvkd tivnspemet hlsfhsas
//
LOCUS       WP_010757086             107 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010757086
VERSION     WP_010757086.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..107
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12301
     Region          1..91
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mnsqlkkgli eycvlaalah qdsygyeivk qinhqieite stlypilkrl etskrvttys
       61 kihngrlrky yqltdegqns iqqflndwkq veaihqyikg svknaas
//
LOCUS       WP_010757102             248 aa            linear   BCT 01-JAN-2025
DEFINITION  YdcF family protein [Enterococcus pallens].
ACCESSION   WP_010757102
VERSION     WP_010757102.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..248
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28073
     Region          <53..205
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mfkdlallvd ylttfpknat fesntlliag nsipelteaa ahfcqqktei tqvifaggig
       61 hgtqrliesi kkrgpeislp dwekkseaei taalfnkyyp theltfyldt qstntgenaq
      121 fsrdlftnen rpksfwlvqd pllqlrsyvt llqewtlske aiqpiplepp vlisydnapq
      181 fansvmndww sseyflslvi geirrlqdnp ngygpkgagf iphvdvpsev idsyqrcqql
      241 lqndvrkv
//
LOCUS       WP_010757132             748 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-galactosidase [Enterococcus pallens].
ACCESSION   WP_010757132
VERSION     WP_010757132.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 748)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 748)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11245829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..748
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85624
     Region          35..292
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          296..642
                     /region_name="Melibiase"
                     /note="pfam02065"
                     /db_xref="CDD:307952"
     Site            order(343,374,418,483,487,533,552,555)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          657..745
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mtkqrkasie ylanckqfhl snkhisyifc vsedgkllql yygkkvpqek sythlieqhy
       61 rqqapcrkkd dllysldslk qelpeygtsd yrhpairlrq pngsaiselv ysfhkikagk
      121 eslpglpaty teepleaetl kvclkdeltg vvvevmyaif sdlpvitrnv nvinqgseni
      181 flthlmslnl dlpdsnyewl qlsgawgrer hvkkrtlqqg iqsiestrgi sspqqnpfva
      241 laraettefs gevigatlvy sgnflvqaev dtfdvtrlql ginpfnfewk lapketfvsp
      301 eavlvysdqg lngmsqtfht lfrkhlvrge wrdrerpvli nnweatyfdf nedkllaiae
      361 kaqqvgvelf vlddgwfgqr thekaglgdw yvnkdrlpdg mgalankirg lglkfglwfe
      421 peminldsdl yrkhpdwmlh tpnrkashgr hqyvlnyanp evvdnifqqm clviddsklq
      481 yikwdmnrvl sevyavnlpa dqqgevfhry vlgvydlyer lttkypnilf escssgggrf
      541 dagmlyyapq awtsddtdav erlkiqygts flyplssmgs hvsvipnhqt nrlvpldtra
      601 nvayfgtfgy eldlsklsad eiteikeqia ffkkyqsvfh ngtfyriqsp feknrtetsw
      661 mvvsedqtia iagyykmlne vnrsfhrmkl qglkadwdyv idghvhsgae lmyaglvssd
      721 assgflidqs plppthdyds rlwvieka
//
LOCUS       WP_010757152             256 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            pallens].
ACCESSION   WP_010757152
VERSION     WP_010757152.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..256
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28799
     Region          1..250
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mnsaarrdfi ikeleenhtv kilelsrqlk vtretirkdl yflekkgiik kvhggavlei
       61 tnqetdyekr knefhdekai iakkaasyie egdtvyldyg tttlalakei vkmknltvvt
      121 ntipivnlll knktinlimp ggivrnness lygpfasnni keiyvsigff gcsgidmerg
      181 itshhtgenl vskemiqhsq ttviladhsk fgtvafnrta tfdqvdivit drprnkeeqq
      241 qltqqgveli dgseee
//
LOCUS       WP_010757165             445 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus pallens].
ACCESSION   WP_010757165
VERSION     WP_010757165.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..445
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49165
     Region          1..425
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mrkkmylrek igfaltnlgn ipimtllnty llifytdvig inpavvatlf lvsrmfdgis
       61 dpilgyfidk fpqtrlgkyr vilvlgtivc cinylfvwfa plllvqhqvl vigisylllg
      121 vtfdlmdipl nsmipiltkd enernvlssi kgvsytvgpt ilnvlaplai aaftdktdgy
      181 lllisgtvlt vlfftivgaa clkernleae epekaavhys fkdivaifki rsvsvlfvsm
      241 lfvtaatnif ngtilyyity llgderifsm aslvgffgal fagmivpsvs krigkenvyi
      301 lglfiascmm vailffrqqv ilfivfylfi qfglglinti qysisadnvd rvyetmhiqs
      361 agliaslnsf vmkvamalgg aapgfilnhf gyvsnqdqsp eaqtgillaa fivpfilyii
      421 tilvfkigyk nieagklttv vdkvd
//
LOCUS       WP_010757168             324 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010757168
VERSION     WP_010757168.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..324
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37370
     Region          46..124
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <235..324
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mmhelrellq kelpvetlqr qsgkninemn lnyeesivpk ipvvdffeeg nifinkhprf
       61 shtpahthsf vefnyvytgs cvqwingdrv alsqgqlilm drniiqqidy vgeedlilni
      121 lvqdssipte llnnlaqsed ivtqfivqas qkqashnnfm vfdlteqkia kqlielmalk
      181 ffqpqrnkar slnlllsall velsntttly tnntysekke ifqllkyind hycevslkql
      241 gdhfgynkny isnmikaktg stfqelidqk rlseakimlq ntnysiseia eaigykstps
      301 ifklfqqktg qtpndfrqkk ksqe
//
LOCUS       WP_010757206             191 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010757206
VERSION     WP_010757206.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21988
     Region          14..>118
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpkfndserl iindllleng eqlftafglk kvtvsdlaks aniskgsfya fypskehlym
       61 tinfsmqqai faemndelak hrsmeteklt lyifkwmfek vkeyplllnm dnetiqhllr
      121 rlpkkfmdah tlddakmidn lkkygivfrs etvviakvvq gifsctklfm ndtdgdkvlt
      181 illeglvnql v
//
LOCUS       WP_010757219             284 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010757219
VERSION     WP_010757219.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..284
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30977
     Region          8..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mpnstpsivv sslkksyqdk svlkdvtfsv psgtiyallg sngagkttvv kilstllkpd
       61 agtaaingfd vinqadevre wisltgqfva vdevlsgren lnligqlkrl pnaqrktdew
      121 lalfdltdaa drkvstysgg mrrrldiams llgdpevlfl depttgldpq nriamwelvk
      181 qlsakgttvf lttqyleeae yladnvailh ngrilvegtp hylkqilpar gaklnfdsek
      241 qaakaveiln ehhiavanle qslpsledvf lslidekted sqng
//
LOCUS       WP_010757221             201 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Enterococcus
            pallens].
ACCESSION   WP_010757221
VERSION     WP_010757221.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..201
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22073
     Region          15..187
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mekrkinkli sfnspvilgl tiasfvvlil nvvtngeink lfavyytswa dpmmyirlft
       61 htlahqdlsh ysgnflllla vgplveekyg sknvlimilt asaiiglinv iffprtmllg
      121 asgivfmfil lasfanmkdg ripltvilvg tlyigneivs gvissdnisr mahiiggllg
      181 alfgylfhtn glknkmeksr y
//
LOCUS       WP_010757225             273 aa            linear   BCT 01-JAN-2025
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Enterococcus pallens].
ACCESSION   WP_010757225
VERSION     WP_010757225.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..273
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30532
     Region          3..232
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mkieitnlth qypsgdnals eintvfegte piaiigqnga gkttfvkhln gllrpttgdv
       61 lingesiknh ttafwsrkig yvfqnpdnql flesvkkefe fgpkqqgipq keinerlkkv
      121 adlvgladkl sihpfdlngt ekkfctigsi lmmnpemiil deptcgqdle gnkrleriit
      181 alkenhqlci tithdmkfvv knfdqiivma kgrivkratk evifssreil qassvspppi
      241 trvgqalgle kpvftqqdfh qqfenkktgn tyi
//
LOCUS       WP_010757226             282 aa            linear   BCT 01-JAN-2025
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Enterococcus pallens].
ACCESSION   WP_010757226
VERSION     WP_010757226.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..282
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30603
     Region          13..243
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mdrdtiiesi sfsyryneap evalnditfd vqkgeiiaii gangagkstl cnalaglipn
       61 yfvghtdgvi qidgkkttec tvgelsqtvg lvfqnpfnql sytadtvsee lafglgnrgv
      121 pkeimiekin kvadivqied lldknplels ggqvqrvala saiilepevl vldecttqld
      181 pagsqqimkt vkrlnqngmt iimvdhdmek vaeladrvlv lhngnlilnd speavfsnpn
      241 iaeygiaapd yyeltkdyds ssvilteeqa ikkledvlas en
//
LOCUS       WP_010757233             201 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Enterococcus pallens].
ACCESSION   WP_010757233
VERSION     WP_010757233.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..201
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23625
     Region          23..198
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 milaagllly seefrkrvil ikdyllvlki kkgdpeawel lveryyqtiy sycfrrcfgq
       61 vklaedltqd iflkliksid kyqftgkffn ylftiavntc nnyyskkkfd lteladylpd
      121 qqqksslqli seeersdeiq qalnqlpdiq reaiilkfyh dlkvkeiakm tevsvptaqs
      181 rinqgikkls klldkealyf e
//
LOCUS       WP_010757247             902 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010757247
VERSION     WP_010757247.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..902
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=100101
     Region          54..725
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 maerrkdrrk keskqkqvlp llsgekkrpk pkktgnkrnn ntkskkpsgs glsrvtkisi
       61 aaltlmvial vaagvfffrq ygqvitaavd agqqqaksiq esdfkqfrpt tildvnggtl
      121 kelktqerdy lsykdmdplv sqalisiedk rfyehhgvdt qglltvglna vlgrgvrgas
      181 titqqlvkni yltpevsisr kveemvmaqs leqkfskeqi leyylnnvyf ghgayginaa
      241 srvyfdksin dtsllekavl vgitnnpgly dpvsnkenal krgktilnem lsqgyitqad
      301 hdkavkddft asihsdalnn dlgdnevala vdsatkilme qqdfrfqyqf dskeeedryn
      361 qeyqdaynkv yqrilsggye iqtkidptih qqlqeivtrv mqswpdmdpe knihvkqaam
      421 tvidnatgsv vasiggrgee gntynrafls yrqpgsaikp lvsyapayer glletstvsd
      481 drpnnnypnn iymgsrgnlt lrnalaissn vvayklamdn qtelqepvyq plaqmqftgl
      541 dvaddnpiia vggmtygatt qemasgiatl vnqgnyrmpt niqsikrkdn dqevfnlnda
      601 pqrkvyseda ayltidtmka vhqdadgtat dtnlahnqyw aiktgttdea kdlwtvgatp
      661 hytvavwagd dtpqpqdnts vgkatrqifq eamdllndgk edvdfqmpas vtnqngqlvt
      721 rssqakqvla trsnallatt qnidalaktk aneliaekln spmvseassf stqlladriq
      781 tlsqfelivt dtqdnwktfd qyaqqvwali qnvepaggtl snqytsvyrt keaqyaqeka
      841 altsdvdrve geitaneeqs kdldkqiedl kkelnirdtt rpssssntsg ssssssesqe
      901 rd
//
LOCUS       WP_010757263             164 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010757263
VERSION     WP_010757263.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..164
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18641
     Region          8..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mekakqhqll kliekdcrlt tqeyaimlge eesivaaeik rledakviag yralvdwdkv
       61 eddwiealve istlpqgedg ykkvgdtirk fpeveslyfi sggfdfivlv qgrnikeisk
      121 fissnlapip evtgtrthfl ldkfkqwgid leddntdhri mvsp
//
LOCUS       WP_010757288             234 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010757288
VERSION     WP_010757288.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..234
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26309
     Region          5..233
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mekvvtitrl eknygtksvl kgidltvdqg eifvllgkng agkstlfkvl tglaiktngs
       61 fqffdkdydr qidsrkigfn indpvfyenl sgrenliihc aymqisnvnv dywlnqmgle
      121 indipvktys tgmrqrlala rclvhdpalv iideplngld pkgirefrql ieqivemnkt
      181 vimsshilae veaiatriav isngeivlnq tkrqlmaehg snfedyliek megn
//
LOCUS       WP_010757328             343 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010757328
VERSION     WP_010757328.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39357
     Region          2..331
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mfleihdlhl ffdekqilai deiqiekgel vtllgpsgcg kstllrcitg lekpksgeiv
       61 ldnehiadkp tkdrnigfvf qnyalfptmt vfenvafglk vkklsaeaiq ekvlkmlalv
      121 dmtehadknv qflsggqrqr valarslvte pkvllldepl saldarirkq lqrdlrkiqq
      181 slgmtmifvt hdqeeamris drifvmeagr vaqvsnsrel yqnpqsrfva efignynrfe
      241 wfeldqytre fsakgnryiy ylrpeliqfe pipqgvkipi hlkesfilgn iqryvfqtle
      301 gkeilvdrln dqeekigdal yiqlkdilai pveldaqrla qks
//
LOCUS       WP_010757332             363 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Enterococcus pallens].
ACCESSION   WP_010757332
VERSION     WP_010757332.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..363
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=39653
     Region          68..346
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 mkkirtmtig licvttlslv lagcgsgeat nqsaaeddsl dtiiekakee geiaslgmpd
       61 twanwvgtwe dleeeyglsh vdtdmssaee lakfesegen gtadigdvgi sfgplaeske
      121 ltlpyktsyw eeipdwakdd ngdwllsytg tisfitdkdn vdqaptswke lqegdyqvsv
      181 gdvtvanqaq favlaaaian ggdekdiqpg ldyykkmaek grlstvdasv anlekgeidv
      241 avvwdfngln yrdqidserf evtvptdgsi isgyttlink naphpnaakl areyilsdeg
      301 qinlakgyar pirevelpke vaekllpeda yqaavpvedn eawdktsvel pelwqsevlt
      361 yak
//
LOCUS       WP_010757344             406 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus pallens].
ACCESSION   WP_010757344
VERSION     WP_010757344.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..406
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43796
     Region          17..400
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(25..26,29..30,33,65,123..124,126..128,131,151,
                     154..155,158,235,238..239,242..244,247,271,275,328..329,
                     333,337,353,356..357,360..361,364)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mskaiydekn wkrniayllt sqaismigtm lvqyaiiwhv tlstksgtmi glmscigllp
       61 mvlvmpfaga ladhynrkkl aivsdscvav vslmmaiill vnirmennil lllavtfirs
      121 vgqgfqtpai ssiipqltpk khlvrvngvd qtiqavmlla spalaaalla vlplagilmi
      181 dfvtaaigit tmffkvkvpl lqsaevkkin vfeeiktgin ylrthkilia livagfagsv
      241 fstpasnlgp lqitrkfhdg lwqlstieig falgmllggs vmstwgglkn kietvalgys
      301 llvipfillg itsvfwlyla mmaaigfvvp isrtamvsff qsetddehmg rvmsivtmai
      361 siaspatmll lgpladvisi dyimiasgis miplavwllf gksfrs
//
LOCUS       WP_010757347             281 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010757347
VERSION     WP_010757347.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..281
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31964
     Region          1..278
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mlltqrmkdy pfspnekvvi dfilekksli kdysvkaian etftspsilv qiaqkldcag
       61 wvefketflt einylqkhfq sidadhpfyv kdplmtiidk mgqlhvesih dtlslishde
      121 lhqairimer skkvrvfavd nlnyageefv fklrrinkea eisadpfhda amttdadcai
      181 clsysgetsa llksvkllke nhvpiiaits ignnrlaewa dvvlntttre tsyskiadfs
      241 slasinfild tiyacyfsln yqqnldykiq iaeivetkcd q
//
LOCUS       WP_010757351             113 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010757351
VERSION     WP_010757351.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..113
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12497
     Region          5..104
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 msdkidsqml kgvltgsill llskeelygy glsksldsfg ftniskgtiy plllslekkn
       61 likgsmrase ngpkrkyyai teegtaekek flaqwsdlkn nmeriiegve gnd
//
LOCUS       WP_010757388             250 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010757388
VERSION     WP_010757388.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10248821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..250
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28877
     Region          3..99
                     /region_name="HTH_MerR-SF"
                     /note="Helix-Turn-Helix DNA binding domain of
                     transcription regulators from the MerR superfamily;
                     cl02600"
                     /db_xref="CDD:470628"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133389"
     Region          125..206
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(126..128,142,158..160)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mtyytsevak lvglhpntir ryeewelipk pqraangyrm ftqyhvelir lariafqiev
       61 lqsglrrkmv dvikalalyd feaagqlimd yqrladqeit qaheaieive eiinnntakd
      121 khetltrsda aeylgvtvda lrnwelngll tvkrsanryr iynqedlkrl kiirtlrgan
      181 ysleailrll ltmdqkrvss ikevldtpkp dedivavcdq lltsleqakk navaimkrid
      241 dleqidrftq
//
LOCUS       WP_010757404             308 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Enterococcus pallens].
ACCESSION   WP_010757404
VERSION     WP_010757404.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..308
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33493
     Region          19..306
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mfkalilidq eavnysvdli eaarrlaged elevfglgin lpnkelkgfd slicvddpti
       61 qtrdsrvvtd ileqvqnnwh fdsviilatd fgrmvaprla mrlraglvad itaievdekg
      121 rklirpafsg nilasilcds tpimasvhpn vfhakelski peridfpvte lkassievla
      181 veeqaknqdi reakvlvsag agysaevkql telahqlnga vavskplveq nrapreiqvg
      241 qsgktvspql ylalgiygsm qhveglknvt diisvntdkg apmnylanis vigdaaefae
      301 rltarlnq
//
LOCUS       WP_010757398             205 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010757398
VERSION     WP_010757398.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 205)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..205
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21719
     Region          1..203
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 miqnlmnyls dnssyiisqf lshiyisivg vvltcligfp igiflsdnkk aatfvigfin
       61 vvqtipsigm ltillilmgl gkntviatvv lysllpivnn tyvglnnvdp vyidsargig
      121 msrfqvlyli kiplaapvil agirnalvis vgittigsfv gagglgdiil rginitggep
      181 iifvgaflcv vialgmeglf nwlmk
//
LOCUS       WP_010757400             207 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010757400
VERSION     WP_010757400.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 207)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 207)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 207)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..207
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22425
     Region          11..199
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 meifwkqygi eillklwehf yisfsaillg tlvavplgal ltrikkgset iinivgffqt
       61 ipslallsim vpflgigkvp aiaalflysl lpilrntyvg iqsvdatyld aakgmgmskw
      121 qrllqielpl assviisgik vsavyviswt tlaayigagg lgdfifnglt lyrmdlimmg
      181 tipitllalg tdavlryveg hlavdrg
//
LOCUS       WP_010757405             262 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Enterococcus pallens].
ACCESSION   WP_010757405
VERSION     WP_010757405.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..262
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29288
     Region          1..260
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkiiclikyv pdteqfeydy ktdkinreks klilnpddrn avawalqkkk qqpsveveiv
       61 smgpskveke lkdlirlgad ravllndrqf agsdslatsf ilagylsqqk ydliltgtht
      121 ldggtghigp qvaellavdq fsniseieet asdyiiakav qeervfrlki ptpcvlsvth
      181 qmnlrlgfvr yenmdknvda qfslvtneel klaqdeigrk gsptkvikni vakrtkvenq
      241 evavddagie tvvqfltekg yl
//
LOCUS       WP_010757452             311 aa            linear   BCT 01-JAN-2025
DEFINITION  transketolase family protein [Enterococcus pallens].
ACCESSION   WP_010757452
VERSION     WP_010757452.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..311
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33093
     Region          5..310
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mskqtvanrq amcevlveea kqnadivvlt sdsrgsaslv efakqlpeql ievgiaeqnl
       61 vsisaglahm gkrpfaaspa cflsmrsieq ikvdvaysnk nvklvgisgg vsygalgmsh
      121 hslqdfavtr aipnlqvlvp adrretkkmf qalaasdepa yirlgrnpve dcyvedygfe
      181 igkavtmkeg tditliatge tvrqamdaae llkeqsisam vlnihslkpf dqaavkaaaq
      241 atkrvlsvee hsiygglgaa vaetlseetg ikhkivgfpd ealitgtsge lfkhygldga
      301 slaeqaaamv k
//
LOCUS       WP_010757543             641 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus pallens].
ACCESSION   WP_010757543
VERSION     WP_010757543.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..641
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74193
     Region          12..640
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mrkisnsrrt nllkylines dykpakyyad rlnistrtlf keiekinqel knhqleikkk
       61 ahfgikisgn wqeklsylnn erdiasddse vaernfaimk rlilesqivt fdslaerfft
      121 sktsikssld liertfitpf slvlsktnhg tvvvgdeadi qkaiyafvld rftalneqve
      181 myehyvayla alfphkliqr vnnliqekli eleytldshy krnfltylsi llyrksigkq
      241 idldkhllty kkimslesyf vakelleels deygafdeqe liyvslllva nkiqkattsk
      301 hisqtletli drsiqkmsel vqvdlcqdql lkdalvehip saifrmsnqi siqnsliddi
      361 rdeyavtfrt tviamneiee tyqinltdde igfimvhfqc aierntrvrk vfvicpngig
      421 taelislrlk kylplldive vtsidklqkn eitendlvis tiplpdetlp fiqvsplmne
      481 tdiksvtgyy qhllsetast itlekfqdyl deeliffnqn fttkeevltf ianrlyekgl
      541 vkqgfsenll qrellgrtdl nsgvaiphan pafvlktqlv viinnrpirw ttqnvkavfl
      601 iciseqdlkl arkllselyn ivntkenvqk yifdeasrif n
//
LOCUS       WP_010757563             734 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-galactosidase [Enterococcus pallens].
ACCESSION   WP_010757563
VERSION     WP_010757563.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 734)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11245829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..734
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83321
     Region          32..291
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          296..641
                     /region_name="Melibiase"
                     /note="pfam02065"
                     /db_xref="CDD:307952"
     Site            order(342,373,417,482,486,532,551,554)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          655..731
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mskalitfne eqrvfhlsng eisyimkiea dnvlshiyfg kkvasygdhk nyphrdrgfs
       61 gnvpghpdra yskdtlpqef sshgsmdyri pasiirreng snlhdfryfd yridegkpal
      121 tglpaayvnd aaeastltit lkdrdqeiyl dllftiyrdr aviarstkvr neltatinie
      181 kiasmqldlt nsgiyqevis lpgahvrerq iarqeistgi qafesrrgas shhmnsfvai
      241 vgkdtneftg eaigfnlvys gnhafelekd qidqlrivag inaynfswel kpaeefqtpe
      301 vllvysdkgl nkmsdtyhhl lrervargqh qfqerpilvn nweatyfdft skkveeivde
      361 aadlgiemfv lddgwfgkrs sdnsslgdwf efegklengl kgvadyvhrk glkfglwfep
      421 emismdsely rehpdflmte pgrapsssrd qhlldmgrke vreniqaqme qlldkvaidy
      481 ikwdmnrsms dayslalsag nqgetahryi lgvyellenl tkkypsilwe gcsggggrfd
      541 agflyympqs wasdntdave rlkiqygtsl ayptsaitah vsavpnhqtg ritslktrsd
      601 vamcgvfgye ldltlmsaee klqvkqqvay yqeirklvqf gdfirlqspf egnlaswmfv
      661 seeqdeallf igrvlanaqp vfnevrlagl aenslyedte sgavysgsel mniglyypdf
      721 ygdfqtqlih lkrk
//
LOCUS       WP_010757567             369 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010757567
VERSION     WP_010757567.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41083
     Region          1..366
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mvemklqnvy kryennpnns vtdfnlaiad kefivfvgps gcgksttlrm iaglediteg
       61 elsidgkvmn evapkdrdia mvfqnyalyp hmtvfdnmaf glklrkyske kikdrvenaa
      121 ailgltdyls rkpaalsggq rqrvalgrai vrdakvflmd eplsnldakl rvamraeiak
      181 lhrrlettti yvthdqteam tmadrivimk dgfvqqigsp kevynkpknv fvagfigspa
      241 mnffkvslnq giitdgyglq lripegknkv lvekgyegke lifgvrpedi hseqialdaa
      301 ldstvtaevv vsellgaetm lytklgetef iskvdardfh npgemvdlaf dinkahffdk
      361 eseevitlp
//
LOCUS       WP_010757619             369 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010757619
VERSION     WP_010757619.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41166
     Region          1..366
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mtelslkhih kkydnadkys vtdfnleikd kefivfvgps gcgksttlrm iaglediseg
       61 dftidgqrmn evapkdrdia mvfqnyalyp hmtvfdnmaf glklrkynke eiskrvenaa
      121 dilglteyly rkpaalsggq rqrvalgrai vrdarvflmd eplsnldakl rvsmraeiak
      181 lhhrlettti yvthdqteam tmadrivimk dgviqqvgsp qevynkpnnv fvagfigspa
      241 mnfftvtlkd glltndhglr laipegknkv lkekgyegke vifgirpeai hgeqialdaa
      301 pestvrakvv vsellgaetm lysvigdtef vakvdarnfh epgayvdlaf dlnkgnffdk
      361 etevviqlp
//
LOCUS       WP_010757663             333 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Enterococcus pallens].
ACCESSION   WP_010757663
VERSION     WP_010757663.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..333
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=37283
     Region          96..>275
                     /region_name="ASKHA_ATPase_ROK"
                     /note="ATPase-like domain of the ROK (Repressor, ORF,
                     Kinase) domain family; cd23763"
                     /db_xref="CDD:466849"
ORIGIN      
        1 mksqkpndlk qhnvqairkl lsqqpngltk seiaqsisls vvttnklise mleteevitl
       61 qkpvttggrk alayklnpny rylltiqfle qakqpialft lstieqeaif qqtlpmlqdd
      121 gqeivatvrn ilqrypktav isigipgvei egifqiidfp siskadlrna lsretnlpil
      181 iendinaatf gfsklngthd ivaglyflen yapgsglvik dtifrgangl sgelkhlsyf
      241 ekltfpitke aqiiqlaeqs lrtiislydp qqivifdteh llsadhldql rrqlekvfpy
      301 gylphlilhn dlstyylkgl nelavkviqe spv
//
LOCUS       WP_010757684             363 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010757684
VERSION     WP_010757684.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..363
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40668
     Region          170..362
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mirfkamltr vvkeltrdkr tlalmliapi ivlslmnvvf dtnaethvki gvdetvptal
       61 tdhfpadqvk vkryhdakds edkmltdnld afvtlkgstf hilyenedps ntakvkalfq
      121 niittsklne lstdlqklam qtgqkvqven fsiknayvyg gadssffdki fpiligffvf
      181 ffvflisgia llrerttgtl erllatpikr seivlgyltg ygifailqtl iivffsiyil
      241 dlqivgnllw vilinslial talsmgifvs tfansefqmi qfiplvvipq vffsglipld
      301 smadwvrkis yifplsygge altnvmikgq gwsaisfdlg ilvlfiigft llnivglrry
      361 rkv
//
LOCUS       WP_010757699             192 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010757699
VERSION     WP_010757699.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21543
     Region          4..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkeeaarkt iasliqiark hftqygyhqv slekiaeegq vtrgavyhhf knkqglflav
       61 lnqvqqdvav qieqealtse dpwqqlilgc vgfikgansp ecrrillvda pavvgweawr
      121 kadqensmda lqrhllelke qnylaeevnp twmtfalsga lnelalnysa tadaeliiyd
      181 tiarmvagfk qe
//
LOCUS       WP_010757730             282 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterococcus pallens].
ACCESSION   WP_010757730
VERSION     WP_010757730.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..282
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32095
     Region          6..238
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mvekqaqtyv vgnfkggvgk sttvqmlsfe safrknrktl vidldpqgnt sdvlsltaen
       61 fgnselpdef dstiweavrt gdisnsiyni mpnldlipan isfsdfpdym ismfpndkls
      121 qfqymdklis plksvydviy idvpptisty snaamyvaey vivilqtqvk slkgaqnyid
      181 ymnffieqyq televvgiip fmmqkrdsvd qeiyetakgi ygdhllntvv lnqsrlkryd
      241 gsgitydink ngkveqwdnr ahevfvhild eidehrylls ge
//
LOCUS       WP_010757801             144 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus pallens].
ACCESSION   WP_010757801
VERSION     WP_010757801.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15601
     Region          4..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mfgkyesilv avdgskqaer afeeavaiav anqatltiaw iineedlsns afsyskilhe
       61 ekemvekeml kkihdakqaq ieevasviei gnpkeylatl ipesqsidli vmgptgkgmi
      121 rralvgstts yvvnnascsv lvvk
//
LOCUS       WP_010757337             674 aa            linear   BCT 01-JAN-2025
DEFINITION  CocE/NonD family hydrolase [Enterococcus pallens].
ACCESSION   WP_010757337
VERSION     WP_010757337.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 674)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 674)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 674)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..674
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=76632
     Region          10..533
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mvkkivtefp yqvtvienew ftlsdgtrls crrwqpesee plptileylp yrktdgtrgr
       61 dnpmhgffsg hgynvvrvdm rgtgesdgll edeylkqeqd daleiidwis kqpwcdgqva
      121 mmgkswggfn slqiaarrpp alkavmvvgy tddrynndih ykgglilnds fwwgaimlgy
      181 qsraidphvv gdrwremwle rlknmplwma nwlehqtrdd ywkhgsvcen yddiqvpvfc
      241 mdgyadsytn tvlsllkgls vpkkgiigpw ahvyahdgvp epainflgeg vkwwdhwlkg
      301 kdngamdgpm iqawiedsmp psthmpvskg rwvgledwps kdvtpksygl tygrlvherg
      361 eqeeqavlht plnhtllane wmgagvpges pgdqridngl smtfdseile eeleifgypk
      421 vevklssdkp namiyaslcd vapdgastrv sygvmnlthl eghdkvvhlt pgkevqafvd
      481 ldccghrfka ghrirlslan tawpmfwtmp eeysltlnlk darftlpifh gediagpdpe
      541 aqsapltptt vlsegkvere inydlvsdtw tcmtngiggv fgegiyrfde vdvtvehnlk
      601 reltlsnrdp lsahytitqn mrigregwwt naditttqts dkeyfyitgq mdvseneqhv
      661 ytkkwdqkik rngm
//
LOCUS       WP_010757962             142 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010757962
VERSION     WP_010757962.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..142
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16287
     Region          1..119
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdqtdwhila lleenarlsl kelsskvnls tpavkerilk leeqgiiegy ttkinypklg
       61 keievfilme tincqafref cwshpdviec hriagkysyl vkfatesmat letfidqtlk
      121 yghpstqivf sshynqktfk ap
//
LOCUS       WP_010758008             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010758008
VERSION     WP_010758008.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..228
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25076
     Region          1..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mellrienvr kiygtgenqv aaldgvslti ekgefvaiig ssgsgkstll hiiggvdvpt
       61 sgkvyvdgqd vyaqtnekla ifrrrqvgli yqfhnliptl nvvenitlpv lmdkrrvnqe
      121 rlkellellg lekrqnhlpn qlsggqqqrv svgralmnap avmladeptg sldsrnghei
      181 iqllklsnrk ygqtlivvth desialqadr iigisdgkvv rdertvrp
//
LOCUS       WP_010758050             250 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            pallens].
ACCESSION   WP_010758050
VERSION     WP_010758050.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..250
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27704
     Region          1..250
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlkserqeli lnrveqygkv vvnelteela vtedtirkdl qelskaglvr rvhggairtd
       61 kslkpfeqri nqdssrkqai akeavqflhp dqviyidsgt tnlsfsseip lsfkgtvvtn
      121 spsialnlsd hselrirllp gelnketkvi egsdtisair ninfdlcilg vssidinkgi
      181 tvpmmeesll kqqvikqssh vitiitadki gssstyfvde akaldvlvte kdipdnlitp
      241 yqqegiqviy
//
LOCUS       WP_010758064             364 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus pallens].
ACCESSION   WP_010758064
VERSION     WP_010758064.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..364
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39499
     Region          1..364
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkklkfgiig cggianqkhl palakladqv elvafcdtii eraeaaaaty gtadalvtad
       61 yqevvkqkdi dvihvltpnv shseitvasl eggkhvmcek pmainyaeak kmldaanrtg
      121 kkltigyqnr fradslatye acskgelgei yfakahairr kgvptwgvfp dkakqgggpl
      181 idigthaldl tlwymnnykp kmvlgstyqk lkdnpmgnmf gpwdpesfet edsafglikm
      241 engatiflea awalnminpk eaqvtlcgte ggaemfgkaf ldqgyvvfnq aahnqleqtq
      301 psdaggvfgf egssleqkda eakqwveail ndteplvkpe qaivvtqile aiyqsaetgk
      361 vvel
//
LOCUS       WP_010758115             172 aa            linear   BCT 01-JAN-2025
DEFINITION  YjbQ family protein [Enterococcus pallens].
ACCESSION   WP_010758115
VERSION     WP_010758115.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Morett,E., Saab-Rincon,G., Olvera,L., Olvera,M., Flores,H. and
            Grande,R.
  TITLE     Sensitive genome-wide screen for low secondary enzymatic
            activities: the YjbQ family shows thiamin phosphate synthase
            activity
  JOURNAL   J Mol Biol 376 (3), 839-853 (2008)
   PUBMED   18178222
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..172
                     /product="YjbQ family protein"
                     /calculated_mol_wt=19289
     Region          5..170
                     /region_name="YjbQ"
                     /note="Thiamin phosphate synthase YjbQ, UPF0047 family
                     [Coenzyme transport and metabolism]; COG0432"
                     /db_xref="CDD:440201"
ORIGIN      
        1 mkviheqlsi ktqagkvsyi ditadlrkti esaglkngfc aittphttcs vifeeyvhdk
       61 dwkgdeylqv dqnrilekli prqltesdyl ypgpehvefl kelaaadpny lpdpvsilna
      121 dahikgslfg asetvivkdg qpligsvgyl yfvdwdqnre rtrtcnlmlm ge
//
LOCUS       WP_010758100             669 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus pallens].
ACCESSION   WP_010758100
VERSION     WP_010758100.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..669
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=77124
     Region          9..669
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mlskkethil kllyenqpdy ltsqemavrl gvsdrtarky lhlledtlke kglgtieakq
       61 gygyrliven qdsfqvfylq etksqhcskd kgaiheaqdr qyyilnqlff eqkavyvdnl
      121 aeelyvsrst vsndlveikk llkpyeiels sksnrgifvv gseknirhfi mnyfflqrlq
      181 dniytfstyt nlldgisiee iviivldecr earlklsdfi ifnivlhigl aikrlqagfe
      241 ieyaqmiqlp edsveyqtal rivqritqsm svafpqeean yialhlrnkl takrvfqktk
      301 yteaeikaql lealaaldee tgyqlqqdti lidglmmhft pfllrlqnnm sienplleei
      361 rqhygellel tikylskmpi fqsyeitese wayltihlta averyhkdqk arvlvicatg
      421 lgssqmiknr lerefgskil idkvisyyei adqdldqidl iissinlpnv ihhtpivyvs
      481 vfvgeedikk inhelsgfmp ahclipndsg adaekkaqqi aliqqcfrpe lflqletast
      541 keeildqlid rleaveqtpi keafgqqlrl resyssvafs pylavphpie avteeayvaa
      601 aivpkgvfwe eeypdiqlif lmspdklgrv elekvshmlv piiedddfrk klvasrdyqe
      661 fianliesl
//
LOCUS       WP_010758125             315 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010758125
VERSION     WP_010758125.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..315
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34610
     Region          12..314
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 msladdkrll veiaslyyeq glkqeeiaqr vkisrslvsk ylvrsreegi veiiihddla
       61 spfhaleekl aaayeleevi ciesagrglq nkllgitaak ylsrvikpwd tisvsagttv
      121 heaaanfpkq sqmtnvrfvp lvggmgmehi tiqsnkvcel fasrcgghav elhapitvdn
      181 peakevfmqq sfiknvfdeg eaatialvgi ggipiystlt dayladqvni nseysqeria
      241 gdicynfidh sgqladcswn krvlaidler lkniprriav sggkekvegi raalkgklvn
      301 vlitdektar elvdk
//
LOCUS       WP_010758136             271 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus pallens].
ACCESSION   WP_010758136
VERSION     WP_010758136.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..271
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29763
     Region          1..269
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkivsflvl tgllllagcs nkasgsdaet lkvgasptph aeilehikpl lkkegvnlei
       61 vkfddyilpn kslaegeida nyfstvpyfn lqkaennydf anvagihlep mgiyshdikk
      121 vadipegatv ivsnvasewg rvlrifeqng likvkegvai dkatfnditd npkklvfkhd
      181 veptllatay enkegdlvai nsnfayekgl npvkdslmle dkdspyvnii atrtkdkddp
      241 rvkklvaalq dkevqawiee kwggsvipvs k
//
LOCUS       WP_010758163             253 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010758163
VERSION     WP_010758163.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28015
     Region          1..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnellyvkdv rkvyqsqmng lsvealrsin fsvdsgeyva imgesgsgks tllnlvatld
       61 kptagtmtln nmdltkipek naaafrrdhl gfvfqdfnll dtfsakdnil lplvlsqvkv
      121 aemdkrlepi akalgihqll ekypyelsgg qkqrvavara iitepellla deptgaldsk
      181 tsdqlleifq qinqngqtil mvthssiaas hadrvlfikd gqvfhqlyrg qrqnfqflet
      241 inetmtalls keg
//
LOCUS       WP_010758190             369 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus pallens].
ACCESSION   WP_010758190
VERSION     WP_010758190.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..369
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42586
     Region          71..365
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msrrgeniyk rkdkrwegry ikgrknngki kygyiygkty kevklklypy kmqyqmiqet
       61 qgtssimmlv wanewlsdie ktvktstyng ysykvfkyii pyigeiplne indtllnnmv
      121 aaweennlsp ssikvifrlv nnclekaven glllknpaak vvlpkesfkk vgalnmdeqk
      181 llekaaldkl dgiglavllg lrtglrigei aalkwenidf qrgiiriekt lqripiksae
      241 yktkiiidkv ktrasnriip msdsvkewls krqlktkndf vlssnekpce prlityhfhq
      301 ireiaglkhi hfhqlrhtfa trcletrana vsvssllghs sikmtldtya dsmieervat
      361 irnmetyvi
//
LOCUS       WP_010758266             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010758266
VERSION     WP_010758266.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..228
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25273
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mivmkdinkf ytadqekihv lknisltide hefvavmgps gsgkstlint isfldgdfeg
       61 sytfngenay rykderlsal rnqsvgfvfq afqlienntv menvalplly ggmksrqtkp
      121 lvmealkkvg iadkynklpk qlsggqqqrv aiaraivgnp kfivadeptg aldshtseei
      181 mhlfkrlnee ekvtilmvth dpdaaaycqr viivkdgeil eegvayav
//
LOCUS       WP_010758265             404 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010758265
VERSION     WP_010758265.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..404
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44015
     Region          5..404
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mrfsevwkts fkaigknkrr sfltmiglvi gvsavitvfs igrafenyas efigldqfdg
       61 svgltfsptd eafaanhldg fteedisrie alpgvenaty ytgqrngvky geqkiddavn
      121 dqrwscfkll kgqgtevlyg rsiqesdsln enpvividev aaeainkeep aalvgqaiki
      181 gghlfevvgi mperesngii steednvvae mpekvyqkyf dtedrsmvqv kmtstanvet
      241 vtketetmlk kygsqkdlgs ytsqdlagqv dtlrtlltsi tllisvvggi slfisgigvm
      301 nmiyisvser tkeigvrram ggtkgnimmq fllegisltl iggtigylvg mvfaylislf
      361 tplsvqpdlf tvllafglsv ligivfswlp aksaaskdiv sllr
//
LOCUS       WP_010758291             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010758291
VERSION     WP_010758291.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..264
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30914
     Region          1..>188
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mktnrlslly niekiynenk igstdyqlar yllenyadip rlniydvaeq nhmsratvrr
       61 fcnhlgyanf kemksqfkef edgqekyvsf ysgedfrivl qrqinemide laermntsek
      121 knivnrlika deviilasst vassirifqq nlaifgkris livsedelkq lkqytsknsl
      181 livlsisgll aeslsdeidk lemqkvifti krnpefnrqy nkiyhlcgqd shqvnevlfy
      241 tygitfvldl lfkeyldinq krgh
//
LOCUS       WP_010758403             230 aa            linear   BCT 01-JAN-2025
DEFINITION  putative ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010758403
VERSION     WP_010758403.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..230
                     /product="putative ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26083
     Region          3..168
                     /region_name="COG4905"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443933"
ORIGIN      
        1 mtfivysfig wlwesiycsi karhfvyrgf llgpycpvyg fgvsavlllv psnagtllnl
       61 yfnivvivti iefvtswlle klfnmklwdy thvplniegr vavpvslfwg vgclllikii
      121 npmiqemihd fitatnhlgp iilaalvasd vlstlfftlt tkkeveavvd tsdpenaaik
      181 efrlkhlvtn hkssasrnkv lkllesrpkq lkhhnlsrii knypnlkfhk
//
LOCUS       WP_010758430             253 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            pallens].
ACCESSION   WP_010758430
VERSION     WP_010758430.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28407
     Region          1..243
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlkqerqtkl ldlvqqhtyl siveiasrln vsemtirrdi telaqqkklt klyggaqkld
       61 ildkelstge kidtnvtqkk yigkiinsli kdnsiifiga gttlyyalpe iqrknlfvit
      121 nsliaftylk ehtdyriilt ggefshttee fvgevavrsf dnlnidiafa atngifddnv
      181 ttaqfdegav qnaafekakv tcivadsskl gvsdvytftr lsehdylvtd neiseelaah
      241 ysqyttilke elq
//
LOCUS       WP_010758436             176 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010758436
VERSION     WP_010758436.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..176
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=19718
     Region          1..90
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 matidlivlg mvkqqplsay diqklveyrn isrwvkistp siykkviqle nkgyikstlv
       61 kegnkaekai ygltdagqte fqrlmqeisq qpihifldfn avmvnlasla pneqrqcian
      121 ieenivnlkn ylaenqaake hsaeipetgl avlqqqiila eaiekwlhsv kegleg
//
LOCUS       WP_010758447             536 aa            linear   BCT 01-JAN-2025
DEFINITION  BCCT family transporter [Enterococcus pallens].
ACCESSION   WP_010758447
VERSION     WP_010758447.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..536
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59188
     Region          3..498
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mdkkpkytly kvaffpamai llveiifgif fqeqfgslln naiyfvgdnf gwfintlsvv
       61 svfaalaiil fkfgdikigg peakpdfkfh nwcfmaicgg igcgvlfwal gepmfhfmtp
      121 pvsagveags reaaifavsq amfdwtfvqy clyslcgvvf alisynlkmn lsfgsliect
      181 fkrripwlna lvhiiaifcl asavsnsmga gllqlgagfe sifniqqgpl iwlilavgvg
      241 mffiltciag mskglknlsn itmvifacll vyilfagdaq figkistesv gymfdnfftm
      301 itrnntlapq dqwanewsit iwnsffiyap vigmflarma kgrtvrqfll vnifvpsifc
      361 ivwigvfggm amqvqtsgql niwemihtsg mqttvyqvlt tlpfgqiaif ifliavicsf
      421 ctladpmcsv lsslcvctmq iddeppknik ilmgvivtsi ayllvssggm dsvkgllnig
      481 gilmtiptaw cfielfrqss ylltlkgnmp pekqsnaekk ikstlvenki ineesi
//
LOCUS       WP_010758456             194 aa            linear   BCT 01-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Enterococcus
            pallens].
ACCESSION   WP_010758456
VERSION     WP_010758456.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..194
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=21662
     Region          42..188
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mkgqwrnrli sagvvlicll agffvflgsr dmedvelgvp eievrstsit qegkllltcg
       61 sdkskndpag dnqspqvswn qvmgaksyvv vmvdedaswi hwyvddltvt elpqgaynke
      121 yegpyppall gsrhnyriev falrqppdiv tvkldkrnsy peiindldta kgerrnilar
      181 gyivgsyqhg dkte
//
LOCUS       WP_010758466             332 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Enterococcus pallens].
ACCESSION   WP_010758466
VERSION     WP_010758466.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..332
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36625
     Region          3..310
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,89,104,106,136,169,271,274,310)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(235,247,261,271..273,276,298,302)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 marivclgei mmrlsaevgt rlnqasqldv fygggeanva vslanyghhv qyaskvadna
       61 fgqaverhlr sygvatdfll kepgrlgtyy veqgigqkat kvvydrqgsv falmnelewn
      121 ltelfaevdv fhvsgitpal sedwcqltiq lmqaakavgc kvsfdsnyrq tlwtqqaaga
      181 flrkalpyvd ycsaghmdai hllgiqeeae advthyyqam qklfpnievf fstkrtvhst
      241 svnelqgnlw ikgqcytskn yaidpivdri gggdaftggm lhglltamnp qeaiefataa
      301 avlkhfvkgd cnqyseeevr qfmnsdsaki sr
//
LOCUS       WP_010758525             466 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus pallens].
ACCESSION   WP_010758525
VERSION     WP_010758525.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49003
     Region          22..458
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(29..30,33..34,37,69,119..120,122..124,127,147,
                     150..151,154,279,282..283,286..288,291,318,322,376..377,
                     381,385,401,404..405,408..409,412)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mrtdsvtqeg sfrgnnrlli givfsvltyw lfaqsllnma pdvqsdlgis sgilsigvsi
       61 tglisgifiv vaggfadkfg rvkvtylgil lnilgslali ltgnaamfli grvlqgfsaa
      121 cimpatmaiv ksyyhgkdrq ralsywsigs wggsglcsff ggavdsslgw ryvfvfsivi
      181 silsailmlg tpesvstddk kqafdslglv lfvismlsln vvvskgtelg wgnpitlgli
      241 vvvlvgtflf yriersrdns fvdfslfenk gylgatisnf llnavagtli iinsyvqqgr
      301 gltaaktgll sigylvtvlv tirigekllq nigakkpmiw gallsglgvl lmsltfiqgi
      361 tylvlvfigy sffgtglgiy atpstdtais svplekagva sgiykmassl ggalgvaiss
      421 siysglsqsa sfaagatsgl fvnilfclla ivsvvliipt kvedak
//
LOCUS       WP_010758537             337 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus pallens].
ACCESSION   WP_010758537
VERSION     WP_010758537.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..337
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37489
     Region          11..332
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mnkpadkatk ileikqlkvk fpihkkwlpa vdevdltiha geiigivges gsgksvmsqs
       61 ilrlrdhdta vkyegeilfe gndllqdsla qlreirgndi siifqdplns lspvhtvekq
      121 lsevitlhkq vskdeakkrs iemlhltgip dpaaclkkyp felsggmqqr vmiamalace
      181 pklliadept taldvtiqeq ilrlikelne tlgmsvlfit hdmgvvaklc hrikvmylgq
      241 ivenaateel faeplhpyte glisciphle tkrgeplpti pgtvpslsei pkgchfctrc
      301 kyadercfqe qppmiearpd hfvkcwkyde aanvgeg
//
LOCUS       WP_010758597             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010758597
VERSION     WP_010758597.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..240
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27082
     Region          5..239
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdldiimkgk klsaneqeil eylishvdql egvslrelaq rlftspaaiv rlaqklefsg
       61 ylelfyylkn qfrpsgqgvs atidfnidtk riepsissmk diyahnkdkf vtiyatgfss
      121 ivadylhkkl lvngiktlfv sagdssgiis nntdnismli sisksgetqk viekmtfcqe
      181 rnipnilftg nlhsraeqla tisfeveder pldsqnikyn sffgklmlll eyivqefvqe
//
LOCUS       WP_010758598             380 aa            linear   BCT 01-JAN-2025
DEFINITION  CapA family protein [Enterococcus pallens].
ACCESSION   WP_010758598
VERSION     WP_010758598.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..380
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=42435
     Region          36..335
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mkkllagial vivlagcskg evekrslrid srsddepvev sfsavgdnli hdfiymnnqn
       61 pdgtyrfdym yeptryltsd advsyinqet icggealgls gypafngpte ildavhgagf
      121 nwlaaasnhs mdrgengivs qlnyldqnyp dmmvtgsqrs akdsrlkvke ingvkvgftt
      181 ytyglngyal pygkeylvnl iddeviqadm eelnqisdvq vvsmhwgqey qfvpdseqer
      241 laqllsdaga dvivgghphv iqpmdyitgs ggnetlviys lgnflssqnv ndqmlggmar
      301 wkisfnkatd evsfkdvtfw ptityigdny qtyevyalkd ytdelanqhm lhlyggqdts
      361 reyfinrvne imndkvelvy
//
LOCUS       WP_010758618             190 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Enterococcus pallens].
ACCESSION   WP_010758618
VERSION     WP_010758618.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..190
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=21218
     Region          16..189
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(95,102,118..120,160,166,170)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mmwialssfi afflvlilvq skrmqsvdas lakqviaqrr dgwtsiflff tklgkavpti
       61 liclllvlfp ttrtaialnv ginvmattgl tyiikrifkr erpkgdrlve eldhsfpsgh
      121 sstaaalylg iflnsflyls iswwwiipal licfligfsr vylgvhyftd vlggwllgtg
      181 ivfliplivs
//
LOCUS       WP_010758636             403 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Enterococcus
            pallens].
ACCESSION   WP_010758636
VERSION     WP_010758636.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..403
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42929
     Region          1..403
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mahevlmpkl sstmdvgtit twlkdegdsv evgeaifevm tdkiaievea ydegillkky
       61 igddesapvn sviayigeag eevpdempgs teeaapaeek aaepekaeek tvaaapvaak
      121 niratpaarr iarekgidlq kvegsgpkgr iqaqdvanyq ekpaapaata eassgelipw
      181 sgmrkviadr mlnskttiph vtmnaevdmt klkelrgqll pmveeqtgnr isfleiiika
      241 amvalksype fnahgleegi qrfdevnmgv avavseglvv pvvknasrmg lseltksvke
      301 vtqkardgql spqemsggtf tvsslgrskv qtfnpiinap evailgvggm ydklaldatg
      361 evktisalnl slsfdhrvad gapaaaflsl ivemlenpms lll
//
LOCUS       WP_010758638             333 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Enterococcus pallens].
ACCESSION   WP_010758638
VERSION     WP_010758638.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..333
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36369
     Region          13..333
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 msetskmsvp nragltdedl kkvfrtmwei ryfdekvdql fakglihgtt hlavgqesss
       61 agsgavlrkt dwitathrgh gqtiakgcni nemmaelfgr ttgtnngkgg smhiadldtg
      121 nlgangivgg gfpiatgaal takmkgqdnv alayagdgst negsfheavn laaiwdlpvv
      181 yfiennqygm sgpfktmmrv dklsdrakay giegvtidgn dlievintty davekarrge
      241 gptlieamty rwkghsksda kkyrtkeeee dwrknrdpik lakdkfvaag lfteeeaeai
      301 rveskqaied avkfaeespm peiesmyedv ysd
//
LOCUS       WP_010758639             315 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010758639
VERSION     WP_010758639.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..315
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34338
     Region          14..315
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 msysddrrll temasmyyee gakqsevakr fnisrslvsk ylakaralgl veiiihddma
       61 hpyrvleeki aekfmlqevi ciaptgveml nkrigitaak ylarilqpnq kvgvsagtvv
      121 heaamnfspk sqmesvkfvp lvgglgqqhm alqanvvcel fakksdgiav elhapitvds
      181 aeakqvfmeq sfikqvfdea ksvdvalvgi gglpaystmt ktylladsdq lqvelsdrkv
      241 agdicynfid eegnlaactw ndrvlaidle dlkriptrig vsggkekvgg iraalkgglv
      301 nvlitdeeta kallk
//
LOCUS       WP_010758677             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010758677
VERSION     WP_010758677.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..290
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32825
     Region          1..267
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 miielleekk nftqtekqia dfilkkpfel seisadelgk rsftskasvf rfcktlgvsg
       61 ydelrrrveh esneksrlnm lleqepigke tslkdlisii psvydtaisk tkmlldysai
      121 srvvgymkra dkldiysggi tyscasaarf kflsigmdcn ahsgvnehyi manrernvva
      181 lvlsftgqnp tmiriaeylk kngilvigig gtespdlkni cdeyieifnr elvmsmeilt
      241 pftsltyald ilfaatlied yeknlkysvd viknkyidpp dksfyadfld
//
LOCUS       WP_010758679             320 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010758679
VERSION     WP_010758679.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..320
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35759
     Region          13..315
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mekgknnnrd lvkvatmyhk enmkqsdiak rlgisrslvs kylidaknqg iveiyikses
       61 aysielelql eqlfgltkav vldtstlren eiekiiiqta itaykrdiak aekiglswgk
      121 ilrrfvdeyp yenhpdacii pliggmgsdy vdihsnqlay dlarklrakc kflyspalvd
      181 npqikenlin naaikdvlea grsvdmaivg laspfsdsnt mteigyisqe diqmlaeaev
      241 vgdinskffd aegqevacti nenvigvsld sirkipkvat icyedtkket lyvamkskvf
      301 ncvtvtdvla eylinriqqk
//
LOCUS       WP_010758734              66 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Enterococcus pallens].
ACCESSION   WP_010758734
VERSION     WP_010758734.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6966
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mnngtvkwfn adkgfgfitg edgndvfahf saiqgdgfkt leegqavsfd veegqrgpqa
       61 tnivka
//
LOCUS       WP_010758793             395 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu [Enterococcus pallens].
ACCESSION   WP_010758793
VERSION     WP_010758793.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     gene            1..395
                     /gene="tuf"
     Protein         1..395
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43184
     Region          1..393
                     /region_name="TufA"
                     /note="Translation elongation factor EF-Tu, a GTPase
                     [Translation, ribosomal structure and biogenesis];
                     COG0050"
                     /db_xref="CDD:439820"
ORIGIN      
        1 mgkehydrsk phvnigtigh vdhgkttlta aittvlgkkg lanpqdyasi daapeererg
       61 itintahvey etekrhyahi dapghadyvk nmitgaaqmd gailvvsatd gpmpqtrehi
      121 llsrqvgvkh livflnkvdl vddeelidlv emevrellse ygfpgddipv lkgsalkale
      181 gdaeqeqvim dlmdtvdeyi ptperdtdkp lllpvedvfs itgrgtvasg ridrgkvnvg
      241 deieivgikp etqkavvtgl emfrktldyg eagdnvgvll rgitrdqier gqviakpasi
      301 tphtkfkaev yvltkeeggr htpffnnyrp qfyfrttdvt gnivlpadte mvmpgdnvti
      361 dvdlihpiav ekgttfsire ggrtvgsgiv teiaq
//
LOCUS       WP_010758962             302 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Enterococcus pallens].
ACCESSION   WP_010758962
VERSION     WP_010758962.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..302
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=32854
     Region          1..290
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mhkvidynrk dlvkkilvil ltgitgavgl nfflipanvf sagmtgiaqi vgaffqqlfg
       61 msidtgilif llnvpvfilg flklgksaml lsflnvlsis ffttlvpvge itdnvlmnai
      121 tggvllglgg gfslkygftt ggldivslll srttgrtvgn yimllngviv viagfffnwe
      181 salytiitif tmgsvvdmih tshqkmtafi ttnkskelrd alynslvrgm tvipakggfs
      241 stdrevlmiv ltryelyelk qivqtvdpma ftnivatesv vgsflnedeq kkikkssnqq
      301 im
//
LOCUS       WP_010758979             181 aa            linear   BCT 01-JAN-2025
DEFINITION  guanylate kinase [Enterococcus pallens].
ACCESSION   WP_010758979
VERSION     WP_010758979.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..181
                     /product="guanylate kinase"
                     /EC_number="2.7.4.8"
                     /GO_function="GO:0004385 - guanylate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006163 - purine nucleotide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20800
     Region          5..153
                     /region_name="Gmk"
                     /note="Guanylate kinase [Nucleotide transport and
                     metabolism]; COG0194"
                     /db_xref="CDD:439964"
ORIGIN      
        1 mnhcylfigp sgsgkttlaa ssfkpeqkii syttrpkrsg ekdnvdyhfv pravfeemiq
       61 qnafaeydyy dhqyygiama sikqalekgd cydpitmpgf wnlrktfgst vvpvlidvsk
      121 etihqrlkkr qasseeitrr lklfskeqeq ypeleklpdl ikidgeqplk amiqqlkanl
      181 r
//
LOCUS       WP_010758982             131 aa            linear   BCT 01-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Enterococcus
            pallens].
ACCESSION   WP_010758982
VERSION     WP_010758982.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..131
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=15334
     Region          3..127
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mkeeinites elkvmevvwg rdtisskein qqleqsegwn pntirtlltr leqkeiithi
       61 kcgrmyiysa qvprerfvkq eskkfiqkff dgrvsdlvmn fvkeeavdpk eierlqallm
      121 ernnqdgstd n
//
LOCUS       WP_010758993             700 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus pallens].
ACCESSION   WP_010758993
VERSION     WP_010758993.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..700
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80193
     Region          26..639
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mshikqykhf intrfgffsl lllllwiknm fgyvmdfhlt lqsplqffil linpisvsml
       61 lisiglfikr trvaytvlfg iyfllsiwlf snavyyreft dfitintllg agqvstglge
      121 savrlfriyd vfyiidlfil plllwkkkik mdnrvprlrq atalamvsll igsgnlflae
      181 idrsgllsrq fsrehlvkyl ginaftfydg yqtyqnnqvr aeasptdlke vedyvadhqa
      241 apndqmygia kgknvvyihl esfqqflidy qltdengeah tvtpflnslf hdqstysfdn
      301 ffhqvkagkt sdaetllens lfglnqgalf tqmgdkntfe aapnilqqta gytsavfhgh
      361 sasfwnrdat ykhlgydyff dssyydined nsfqygmhdk pflnqsvqyl ehlqqpfyak
      421 mitvsnhypy ssfnneedgf plantsdsti ngyfatanyl dtalqeffdy mkasglydns
      481 ifvlygdhyg isntrnsela pllgksseew gdfdnaqmqr vpfmihipgq tngginhtyg
      541 gqvdalptll hllgiptddy lmlgqdlfss ehqqvvafrd gdfvtpeytf yggkiydnqt
      601 glpvdepnle qqklftklnq avdeqlmtsd kinngdllrf yqgsglksin pqdfdyhnql
      661 erllqiesdk gknstslysq nneqttvply rtetyteyqk
//
LOCUS       WP_010759004             190 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Enterococcus pallens].
ACCESSION   WP_010759004
VERSION     WP_010759004.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..190
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22302
     Region          2..178
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtdeevktkl lagdeqffdq lidqyskllw avaatiltvk nsnqqmdiee visdvflrlw
       61 qqpekykpkk gslksylvim tkslalnklk gksrhqhedi gevnelylse taqkdediaw
      121 qdlydavmkl eeptrrilim rffyemkpse iqkqlglssk evdnrlyrgk kklhefleyq
      181 dfinevnsce
//
LOCUS       WP_010759163             248 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Enterococcus pallens].
ACCESSION   WP_010759163
VERSION     WP_010759163.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..248
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26439
     Region          1..245
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 maiknkvvvi tgassgigka tanllaekga klvlgarrea klkeladqik enggeavyqv
       61 tdvtipeenn alvklakdtf gkvdviflna glmpnsplsa lktdewdrmv dvnlkgvlng
      121 iasvlptfke qksghvitts svaglkaypg gavygatkwa vrdlmevlrm esaqegsnir
      181 tatiypaaiq telldtitdt etekgmsaty dkyqigpesi anivafaidq pedtnvneft
      241 vgptkqpw
//
LOCUS       WP_010759177             125 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010759177
VERSION     WP_010759177.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..125
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14478
     Region          1..112
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(49,52,56..57,66,84,88,94,98,101..102)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mniseaagkv qltpvalryy ervglippvk rknggvrefq ekdirwiefi kemresglci
       61 ealsefvqly qqgpetkgeq eqllkderdg llaryrelge tierlnkkid hytheekncl
      121 rcvav
//
LOCUS       WP_010759229             143 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010759229
VERSION     WP_010759229.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..143
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16252
     Region          4..140
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 maeqtvkhai eelkesnvri tpqryailef liehrshpta deifralesr fpnmsvatiy
       61 nnlrkfveig ivqemsygda asrfdfgvqk hyhaictdcg kiedffypgl edvemassel
      121 tgyeigehrl evyglcpncq tkg
//
LOCUS       WP_010759246             250 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Enterococcus pallens].
ACCESSION   WP_010759246
VERSION     WP_010759246.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..250
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=26716
     Region          60..247
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mqlrkillss slilsigvfa acnsggnann sssestasst qessvdlskv dlpqlsnevt
       61 ddeylvemdt tvgnikiklf pkeapktven fvthakdgyy ngttfhrvvn dfmiqggdpk
      121 gdgtggesiw gdpfedeisp slynirgals managentng sqffivqnkd dqsdglaiqy
      181 tpekiieayk nggtpsldgk havfgqvteg mdivdkiaga etkansqged stpvdpvkin
      241 eikilqepke
//
LOCUS       WP_010759304             142 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Enterococcus].
ACCESSION   WP_010759304
VERSION     WP_010759304.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..142
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=16292
     Region          <13..141
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mgdskethiq hmfdsfckkv vrneafniqk kdarfrqrqi smetleqknl gtefyysdtr
       61 lngngkfpvl gieilignev lanaieqlas vrqeiilmsf figlndreis eivgkslgsv
      121 wyqrqealed lnrilgesye en
//
LOCUS       WP_010759305             329 aa            linear   BCT 01-JAN-2025
DEFINITION  aromatic acid exporter family protein [Enterococcus pallens].
ACCESSION   WP_010759305
VERSION     WP_010759305.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10369318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..329
                     /product="aromatic acid exporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37675
     Region          1..198
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
     Region          159..318
                     /region_name="ArAE_1_C"
                     /note="Putative aromatic acid exporter C-terminal domain;
                     pfam11728"
                     /db_xref="CDD:432028"
ORIGIN      
        1 miqrlalwnh llyalkigig sgvsiyiaes lqleyassag iitlltiast rsetlriglh
       61 riitfigtvv lcglmnsvis aewvaygivm vvltfalslr dllktlsgna vvvshllrap
      121 dqiitienlv nefsllligl viaivvnnfq ncesqkkyle kavestdrem qkifyklsay
      181 lkdptlnnqv wediiqlekd ilgytaiafq yqqnrlprkd hyyvnyfemr lqqsgvlhnl
      241 hyemknirvf qsdsqivaef ldsmiddlsk mnspliqlrk vadlilyiqq nnlsttreef
      301 iskvrlyhiv mnieeflkfk erfvatldk
//
LOCUS       WP_010759324             380 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Enterococcus pallens].
ACCESSION   WP_010759324
VERSION     WP_010759324.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..380
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=41944
     Region          1..375
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mtfldlfagi ggfrlgmeqa ghqcigfcei defarrsyna ihdtrkevem hditsvsdef
       61 vqslepvdil cggfpcqafs iagkrqgfsd trgtlffeia rfatllqpkf lflenvrgll
      121 nheggatfet ilrtldglgy dvewqvlnsk ayvpqsrerv flighsrdac teqvfpiiga
      181 sptsdqnirn llninpsnrg mggqvygsdg vaptltgdeg ikialpvkdg isvagmlpgn
      241 feqgnrvyev tgtaptlstk qggtkimirk nkteyqevkp gdsvnlafpn stsrrgrlgk
      301 qsvhtlltgd qqavvtdqyq irkltprecw rlqgfpdwaf drasqvnsds qlykqagnsv
      361 tipvifdiar rlrevkahdl
//
LOCUS       WP_010759495             133 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010759495
VERSION     WP_010759495.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..133
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15442
     Region          32..124
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 msfwwtlnii llavillfvg yevfvrimvk rsakmltqee fqagmrkaqv idvrerdefn
       61 akhilgarsf pysmlketks slrkdqpiyi ydynksvsar aanllrksgy tdlyilkggi
      121 eewqgkvkkk kid
//
LOCUS       WP_010759498             223 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Enterococcus
            pallens].
ACCESSION   WP_010759498
VERSION     WP_010759498.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..223
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=24647
     Region          4..162
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mrrsqpyvty tflgintvff lleylipslr vnerlgmfip svilgheywr fltpmvihfg
       61 lmhfvlnsvv lyymgqqcea ifghwrfglv yilsglmgnm gsfafndlgv lsggastaif
      121 glfgaflvvg yhyqdnpavq gltrqfglfi llnlvfglfd ssidlwghlg gllggalsgl
      181 mlgvphgedr fsirgritgg lffaffvvva vllafrkigl pii
//
LOCUS       WP_010759541             295 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Enterococcus pallens].
ACCESSION   WP_010759541
VERSION     WP_010759541.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..295
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31811
     Region          1..284
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 melgfigtgv mgkaivghll naghnvhvyn rtksktdelv engatwqdtp akvteaaeii
       61 ftmvgypsdv eqiyykengi ftvpvknkif vdlttstptl akkiqetave kgsdaldapv
      121 sggdlgakna tltimvggnp styekvvplf eimgkayalh geagsgqhtk manqimiagt
      181 mtgmtemfvy aqkagldvpq vletlgggaa enwsmvnygp rilkedyspg ffvkhfikdl
      241 kialdeaekl slelpgtkla velyeqlaan gyendgtqal iklwwtegkp afdkn
//
LOCUS       WP_010759524             244 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Enterococcus
            pallens].
ACCESSION   WP_010759524
VERSION     WP_010759524.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..244
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26695
     Region          5..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mkealiqieh lnkkfgdnev lkdisaeiqp gevvviigps gsgkstllrc inllevptsg
       61 iikfegtdit dkkndifktr ekmgmvfqqf nlfpnmtvve nitlspikvk kmtkeaaeav
      121 ahellikvgl sdkadaypqs lsggqqqria iaralamqpd vmlfdeptsa ldpemvgdvl
      181 avmqqlakeg mtmvivthem gfakevgdri lfmdggvive egtptevfee tkntrtidfl
      241 skvl
//
LOCUS       WP_010759565             309 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus pallens].
ACCESSION   WP_010759565
VERSION     WP_010759565.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..309
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34784
     Region          4..187
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(7,9,94)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(40,93..94)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            92..94
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mlsiivpcfn eeeaiplffa emekiqsltg kkfeyifvdd gskdnslkai kklasikdsk
       61 vryisfsrnf gkeaalyagl qaangdlvtv mdvdlqdppe llpqmiqmie ssdidcvgtr
      121 radrkgeppi rsffakrfyh linkisdtym vdgardyrlm trqmvdavle vteynrfskg
      181 ifswvgfkte yisfdnrera agetswsfwk lfnysidgii nfsdaplnia sfvgalscvg
      241 sgialffiif ralifgdpts gwpsmvsill figglqllsl giigkyigki fletkkrpiy
      301 ivketeqse
//
LOCUS       WP_010759587             270 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus pallens].
ACCESSION   WP_010759587
VERSION     WP_010759587.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..270
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31537
     Region          7..270
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mikdlisffk eiysnrvllk qfsvndfkar yagsafgifw afanpivmvl tywfvfgvgf
       61 kaamtdgkyp fivflltglv pwlyfsevlg aatnvfreys ylvkkvvfni rilpsvklfs
      121 nlymhaffiv iafivaifnh ampslytiqi fyylfcmmmf ltgltwitss iqpffpdinq
      181 figvimqalm wgtpvlwsin qfqahptiqf ilklnpmfyv vqgyrdaffs eqwfwekpll
      241 siyfwvitli llvigsvvfk rlkphfsdvl
//
LOCUS       WP_010759694             203 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010759694
VERSION     WP_010759694.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23765
     Region          4..138
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          88..190
                     /region_name="TetR_C_8"
                     /note="Transcriptional regulator C-terminal region;
                     pfam14278"
                     /db_xref="CDD:464123"
ORIGIN      
        1 msnktdrtkq hivltffemm delgfdkitv aglskrakin rgtfyhyyvd kyalleeiee
       61 emyssfkqvm enhigvtvks kidqygrdni fqffkdacek lmvflydrke lakiligeng
      121 rpqfierler lyietvqlkl qnvspeites eklqqefiyy gviaivkrwl ltgakqspee
      181 iaeilakcmt tspltifeei esr
//
LOCUS       WP_010759733             794 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK [Enterococcus pallens].
ACCESSION   WP_010759733
VERSION     WP_010759733.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..794
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=87970
     Region          291..783
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 maqkkrtkkk rkttkkqkql qeqrlviiig lifilfavfs lfslgflgnl ianvlrmigg
       61 ntyqflafll gvyglllvvk ntklkfskgr rwagigvfyi gilvilharl fanvqsqnpn
      121 vlkttwellm idflgnqvtq nvgggmlgga iyslthflvs qvgsyiiagl llvlgvylfs
      181 mldfaqvtdf lnhsmdtlqq kltesdekka ertakreerq aarakqkaek eaaakerqae
      241 kernqvrplt pgeklakenl eplenepeqm tlvpieayqa naepkkpmpd pieeideead
      301 agdlefeisa epedhdyqlp psslldsipa adqsdeykki ennikilekt fdsfgveakv
      361 vkaslgpsvt kfeiqpavgv kvskivnltd dialalaakd vrmeapipgk sligievpns
      421 tistvsfrdi iesqpnhpdk llevplgrdi sgmvrtadlt kmphlliags tgsgksvain
      481 giitsilmra kpnevkmmmi dpkmvelnvy ngiphlltpv vtnprkasqa lhkvvqemee
      541 ryekfaatgv rnitgfnelv iqknledgqn rpilpfivvi vdeladlmmv asnevedait
      601 rlaqmaraag ihmilatqrp svdvitgiik anvpsriafa vssgtdsrti idsngaekll
      661 grgdmlflpm genkpirvqg afisdhevee ivtfvsdqqe ahyeekmmpt eettsspsev
      721 pqddlyeeak alvvemqtas isllqrrfri gynraarivd eleenkvigp svgskprevy
      781 lqkteeepee ttey
//
LOCUS       WP_010759751             125 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010759751
VERSION     WP_010759751.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..125
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13795
     Region          3..>86
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mileidphse epiylqlrqq iiigiakgev kpneqlptvr qiadelgmna mtvskgyqql
       61 keegylitdr rkgtlvaplp vekkgekaaa ltlllaelsl sgtseaeikq lideiltsfr
      121 kgreq
//
LOCUS       WP_010759762             391 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010759762
VERSION     WP_010759762.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12084760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..391
                     /product="PucR family transcriptional regulator"
                     /calculated_mol_wt=44717
     Region          7..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          <262..391
                     /region_name="PucR"
                     /note="DNA-binding transcriptional regulator, PucR/PutR
                     family [Transcription]; COG2508"
                     /db_xref="CDD:441998"
ORIGIN      
        1 msialrevls fdyfhfltla agksglenei ttvgileyey deglhpkrkf dvnslvitsl
       61 yfaknnpdll vdtirllyrd gvsglivkki ffqelpaevl ayadeinfpi ftyeqsatph
      121 fedilfqlkq visfdgqqki leglveella gdpipeariq tllfqqeslk kytlfyllpd
      181 rlnapivhwl slinnyqhss ffirgisyqq gffvllglkk hllkedhfpl iadlfqqigl
      241 sasdfivgks ldyrqtadlk nafsealvsa qfsrksqsrv nsyeelgvyq llipfyqedt
      301 frhysqqllt kiisndpskq qklletaraf vhcegnlsmm adtldihens vryrlhklke
      361 llsngtqsls dfalyeqlsl avktadllae e
//
LOCUS       WP_010759740             419 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus pallens].
ACCESSION   WP_010759740
VERSION     WP_010759740.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..419
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=44439
     Region          1..419
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdgfinfmer rfipiaskig aqrhlvaird sfmvtmplmi lgalavminn lsltipafgd
       61 fmngifgges wkgfggsvwn gtfgilsvfi aflvaynlan sygkdgvstg vvsvacfftl
      121 gaatsgmnss glfvalivai vvtelfrrll gnpklvvkmp dgvppavaks faalfpamit
      181 islfglvaav iasfgvedmf asfyamvqep fmglansygs alliafitpf lwffglhgan
      241 midpfmqain apaieanmaa lsagktapyi vnkpfidsfv nmggtgvtlg liiaiylvgr
      301 khkafmvvnn laaapgvfni neplmfglpl vlnpimfipf iltpmvcvtt ayfatkfglv
      361 ppatvmppwv tppilggfla tqsiagavls avnlaisivm yvpfvmlstk qelkreaaq
//
LOCUS       WP_010759761             502 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein/permease [Enterococcus
            pallens].
ACCESSION   WP_010759761
VERSION     WP_010759761.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 502)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11705690
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..502
                     /product="ABC transporter substrate-binding
                     protein/permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54630
     Region          39..249
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Region          279..499
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mkkrwlsklp illlglfill agtitgyaee ddslqkvldr gtlivgtsad nppkefirmn
       61 ngkeeivgfd idvakeiake lgveleitnm kfdglipsiq tnefdmalag fnptperrei
      121 vgfsnpyhtl pfvilttkdk aevftsvdsl tgkevaaqkg stqetilndy lgnaepvalg
      181 klpeviaein agtvdagvvg wltaqnyldv ypnltiadve ievpeektaq viafpkesna
      241 liarvneiia emeekgmmee lldknielak agdsqdsrsm lktygplflk gavttigvai
      301 icvlfgtllg iliallriss nkllkalatf yiqvlrgtpa llqvfifyfg lsmivnipsi
      361 hvwgvnlarl ipgcialsin ssayvaeiir sginavdkgq seagyslgln krmtmreiil
      421 pqairnilpa lgnefismik etsllsviav selmfvadtv kaatyrtmes lfiaaiiyfc
      481 mtcvvsllva rfekklahss kg
//
LOCUS       WP_010759560             155 aa            linear   BCT 01-JAN-2025
DEFINITION  GtrA family protein [Enterococcus pallens].
ACCESSION   WP_010759560
VERSION     WP_010759560.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..155
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17974
     Region          14..141
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 meyyrkfeny lkekklwelf iylffgglat vvnivtfaaa yqflhlswpi sntiswicsv
       61 lfafvtnklw vfqsktetfg alawefskfl fariisfgmd macmylfidl lstgnlvaki
      121 itqivvvvan yvfskvfifk kveiieetsp eskek
//
LOCUS       WP_010759870             247 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Enterococcus
            pallens].
ACCESSION   WP_010759870
VERSION     WP_010759870.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..247
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27291
     Region          1..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mievkdvykk fdrhevlkgv slkvetgdvi vilgvsgsgk ttllrcinfl dkadsgtlti
       61 agetvdlkha skkeilnvrk ktafvfqnhn lfnnktalen vmeglviark vpkaeaekra
      121 kealdkvgla ekydsypsql sggqqqrvgi araivlnpei imfdeptsal dpelvgetlk
      181 imkkiadegv tmivvthema fasevankvi fmdegvivee gppeeifsnp keertrrflk
      241 rilpesi
//
LOCUS       WP_010759879             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Enterococcus pallens].
ACCESSION   WP_010759879
VERSION     WP_010759879.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..238
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24425
     Region          5..238
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mtgdmaaifg efigtmiliv lgsgvcaavn lnkskaqgsg wiviafgwam gvamaayisg
       61 fmgpahlnpa vtvamamtgn levglvfpfi iaqmlgaivg avliwlaylp hwavtedqda
      121 ilgtfatapa irnypanvmt eilgtfilvl gllaftqnef aggvnvlavg glilaiglsl
      181 ggptgyainp ardlgpriah ailpiankgg sdwayswvpi vgpmlgavia vlvyqvmv
//
LOCUS       WP_010759874             302 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterococcus pallens].
ACCESSION   WP_010759874
VERSION     WP_010759874.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..302
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34844
     Region          1..297
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkkifignyk ggvgkttstl flgkclkdlg kkvllmdldp qsslseicik kddkersley
       61 lepkqtlnyv ydlsidnvrk gynlelqfdl nylisqyeek ldfiasslyy renvgldeln
      121 mamekdiryf silakliqni edklpdydyl lmdcppnssi itqsafmisd gyliptivds
      181 isakgimhyi gtiskihaky cndyedaylf rhyfgenpkl igifytlirg qvrydeviek
      241 lrnelgklni dqciyvfesf tnnyvaitra vaenklgnlh vskntypkit keflkrlsdl
      301 nl
//
LOCUS       WP_010759887             182 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010759887
VERSION     WP_010759887.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..182
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21186
     Region          8..>110
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvgiannrrt iytknsirea fltlltqkdl ekitvkeitq ladinrgtfy kyykdafdll
       61 qkieeetmed lladiqlnsq piekwlttll qkiqqrpevr ilvlgnhqsn flspllerik
      121 peafqhfsqy fpeastveke lylsyfvegs vglivrwlrd yesmsaaais klllnvfkte
      181 iy
//
LOCUS       WP_010759900             784 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus pallens].
ACCESSION   WP_010759900
VERSION     WP_010759900.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 784)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..784
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=85408
     Region          15..663
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(305..307,368,387..389,414,465..467,511,514,517,536,
                     539)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(596,600..601,603..604,629,632..633)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
ORIGIN      
        1 mrflrkagnv vkqtgltene vqqrkaqglq nnyeenatks tkailydniv tlfnflnlii
       61 giclflvgay tnmfylviil tnicigiyqe iharnlvqkl sivnqqkvkv irdgqeqain
      121 stdlvlddit ivhageqisa dmdvlsgfae vneamltges dlisktagse llsgsfltsg
      181 evvakvihvg adnyatklas eakvhkpfns elvrairkvs kftsfiiipf gillfleaff
      241 frtsgikasv vvsaaavlgm lpkglvllis ialttgvtkl akkrilvqdm ysietlahvd
      301 tlcldktgti tegnmrvtnv hsvasdvdvq allgsylaqs tdsnvtmqal rdyfpetdry
      361 rsldvlpfss drkwgamale dfgvvylgap ekllaanalp aqvasaqeeg lrvlllaagp
      421 gskvpeeken ltalavieie dvirrnaeet laylynegve lkvisgdnpi tvsniarrag
      481 lpnferyidl atcdtdqevi daaqqytvfg rvaphqkkll vqslknagrt vamtgdgvnd
      541 vlalreadvs iamadgddat rqianlvlld sdftslpevv fegrrvvnnv tkvsgiffik
      601 tiysfllsvi clltatafpf ipiqitlidl aiegypsffl sfegnkerik gkflptalra
      661 aapnallvva nvlivsllar nnhwtqidtt tlmyylligi sclavikacl plnplrifli
      721 vttvggiyva amlfhsilev gllhpgsfai figmmilnav gyiflskalp hpmpkkeaga
      781 kffh
//
LOCUS       WP_010759930             451 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus pallens].
ACCESSION   WP_010759930
VERSION     WP_010759930.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..451
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=49753
     Region          4..424
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mgfntlsekm dqyisplank lsqqrhlkat rdafmsmlpi tlfgsipiil naapvtentt
       61 ngfllawasf aeqnsmilnw isgitlsams lficigvtyf lcrhykedvl rplmfavagf
      121 lmlvltplkl gwdgkeveis fldgrgilla lfvsivtveg yhwmrkknig rismpdsvpa
      181 slsetfaalv pglilmtffs iifiifhafd ttavqflyni mapsfqaads lpftilsifl
      241 ihlfwffgih daalagilgp irdgnlsina aekmagtdls nifttpfwty fviiggsgsv
      301 lalaflmmrs kskqlstvgk vgflpsifgi sepmifgtpl mlnpiffvpf iftsvfngiv
      361 tylcmswgiv gktfavfswq mpapigafls tmdwraivlv avlialdgvl yypffkvyek
      421 nlvalekese aenaeaeqkt pvevsndttt a
//
LOCUS       WP_010759934             147 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010759934
VERSION     WP_010759934.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..147
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16346
     Region          1..147
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslltrlned mkqamrskdk eslqvirmlk aavqneqint gqelsedeel tvlsremkqr
       61 rdsltefeka drtdladkvk keivivekyl paqlsedeir sivsdaiakt gaaspkefgk
      121 vmgavmpkvk gkadgnqvna ivkellq
//
LOCUS       WP_010759951             791 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010759951
VERSION     WP_010759951.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..791
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=87206
     Region          30..682
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mahkkkekkk kprstkhlvg tsfyinvilr vvkslsiglv lvlflggmla lgigagyfay
       61 lvegtatptk eevkqtvgdi tesskllyad nkeiatisad pirqkvnsde ispwvkkaiv
      121 atedeyfyeh pgvvpkavvr alvsevtglg gssggstltq qlikqqvlts etsfkrkane
      181 ivlaldveky lskdeiltay lnispfgrnn kgqniagvee aatgifgvqa kdlnlpqaaf
      241 iaglpqspiv yspytntgdl kedysigmdr kdnvlfnmyr ekviskqeye daknydlakd
      301 fqprenvvee qrgflyytvy neavsilarq qaaqdgvsea dyskddvrtr yveqakvkiq
      361 nqglnvksti dkniydamql svaeygqyld ngsgtpietg nilmdnqtgr iygfvgsrdy
      421 ntnqnnhafd tirqpgssik pllvygpaid qgligsgtri adfpmkyqqg tnagkelkna
      481 tgegsrtfqt trealvestn ipayhvyqdl ltekgsdqyv yndylkkmnf pssdnwgves
      541 aplgtiettt lnqvngfqal anggvyqegy liesitdstg keiykhqenp vqvyskatas
      601 imndlmrsvi teqqttpfka llsgvnytls tadwvgktgt tdnytdnwli vstpsvtlgs
      661 wtgrddnqpm dsnagnrtat ymaylagriy gvnpdvfgvn eefklsddvk kekvstftgl
      721 kpgkvshdgt tyqvpsgese sfwakdgpgs ntykfgiggt danyedywnt rnrsnrsnvt
      781 nnnnneddde n
//
LOCUS       WP_010760008              91 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus pallens].
ACCESSION   WP_010760008
VERSION     WP_010760008.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 91)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..91
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10449
     Region          5..88
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 memkeeknrl vllndegqea gemtwsdage eimiidhtfv dpayrgqkla eglvregvei
       61 arrdhkeiip lcpfakrefe lkseysdvlr k
//
LOCUS       WP_010760025             247 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Enterococcus pallens].
ACCESSION   WP_010760025
VERSION     WP_010760025.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..247
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27540
     Region          1..211
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 milvtgaagg vgrqvvtelv kkglsirafd inpkveelkk lgvaetfvgd grlvndvkka
       61 lagcnkvlyi ppmfiydeae ianrfvdeav aagiqqfvmi tvthpnmstl pqhtqklkae
      121 ehlvykglsd klnytilqpm hymhnfsipm vwstnayqcf ytkttklsyv divdvaevaa
      181 kvlsepeqha natyelvgtd flspndmvek fnqltgrsae cqqipvetii nyfptakyds
      241 yfvktfq
//
LOCUS       WP_010760108              82 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus pallens].
ACCESSION   WP_010760108
VERSION     WP_010760108.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..82
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9189
     Region          1..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mrnnlkkimq vtnmnqtqla ektglsrqfi nklvneksgi npqqssmeai advtgfsvyd
       61 iffnndvqlv lqninieske vv
//
LOCUS       WP_010760130             119 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Enterococcus pallens].
ACCESSION   WP_010760130
VERSION     WP_010760130.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..119
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=12936
     Region          <6..118
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkkeikkkai vlsakqylgv syvwggttpn gfdcsgfiqw vfaqngiglp rtsqsqqiaa
       61 kevpltevqp gdlvfwgkpa yhvglyigdd cfiqalqpgd vvkvshvsyy pfesagrvl
//
LOCUS       WP_010760313             176 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010760313
VERSION     WP_010760313.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..176
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19105
     Region          <58..173
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
ORIGIN      
        1 mdeeysrrkq qrppstskft ivivillllv ntlalgglly lnvqasskqe arlnsiekqv
       61 skldlgvnvp vlatdntehn vpvresstqv skmeesssti essdqpaqtp psseaveqqt
      121 erstepsqva atsytvqsgd tlsviaeknk islqdlmlkn nltdstvyvg qvlslq
//
LOCUS       WP_010760400             202 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Enterococcus haemoperoxidus].
ACCESSION   WP_010760400
VERSION     WP_010760400.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..202
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22523
     Region          4..197
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mtytlpdlpy aydalepyid vetmhlhhdk hhntyvtnln aaidkhpelg tksvedliad
       61 mdsipedirt avrnngggha nhsffweima pnaggaptgd ikdaidatfg sfdklkeefk
      121 aaatgrfgsg wawlvlnngk leitstpnqd splmdgktpv lgldvwehay ylnyknvrpd
      181 yidafwnlvn wdevnkrfaa ak
//
LOCUS       WP_010760502             132 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Enterococcus].
ACCESSION   WP_010760502
VERSION     WP_010760502.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..132
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15014
     Region          32..123
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mnvlwiingv lltillamgi nelylrimak rsaktiteee fkegmrkaqi idvrekdsfd
       61 aghilgarsm pyttikttln sirkdqpvyi ydqkkslsir tanqlrkngy kdlyilkggy
      121 egwtgktkkk na
//
LOCUS       WP_010760610             287 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus haemoperoxidus].
ACCESSION   WP_010760610
VERSION     WP_010760610.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..287
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32216
     Region          19..285
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mikqefcysq lndldlsvtf yskqndssak atliylhggg llygsrddlp etycellvek
       61 gynlltvdyp lapevklpti inclreaidw flknyqsilg lersdyflfg rsaggflsyl
      121 lsaryalpeq kglisfygyy dlinpafsqp ssyynqfpki apltaqaliq pepiagvsin
      181 erfslylsgr qfgnwlsylt nspseketfs ltdtelaqlp ptflahssad qdvpveasri
      241 asnkisnvty eeveklphdf dgdltknegl nvyhaliewl dkvlatt
//
LOCUS       WP_010760621             427 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus haemoperoxidus].
ACCESSION   WP_010760621
VERSION     WP_010760621.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..427
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45704
     Region          12..423
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mdaksknsgm dywkkivill cagwvtiwvy rsalspaypq ineslggnit dtalgfistc
       61 yffgyvamqi pagflvdkig kkkvlipgfi vfgvaallis qatniqmiyv gsvlaglgcg
      121 sfygsayslt sqniprekrs fstaivnsgs avgsglglil ssflvvqlkf pwqtmmyisv
      181 alivvmlvaf vaiirnnked aeflaqseaa eaaeaaaaap eapvaekehv sikklfspkm
      241 lfayilyfat cyayymtvtw lpnflgterg fegaaigfsa slvafasipg alffsrladk
      301 fmhkkvqfiv ileflaaaml lltvqatnst llliglilyg flgklavepi iiswlgenap
      361 kvgigttlgv fnffgmmssv iaptltgsis datgskemgf yisvillvvg talfllanln
      421 kkkasae
//
LOCUS       WP_010760624             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus haemoperoxidus].
ACCESSION   WP_010760624
VERSION     WP_010760624.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45091
     Region          12..402
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mnekkrlngq mpywkqiiyi ltigwiviwi yrtiltpiyp iisdyfggat daelghissf
       61 yflgyvcmqi psgvlvdklg kkqilipgfl lfglgalvvg laqnigivfv gsvlaglgcg
      121 tyygvayslt aeyvpvskrs lstaivnsgt aigsglglis ssylvgtgvl pwqalifati
      181 vlillavtmf lyfirlekpn kaintksekk ktmsiralfk prmvsayily fstlytyyli
      241 dtwlpnflet ekgfsgtsvg lasslvffta ipgalifsri adripmkkvq miillellaa
      301 svlfitvttt sqtilvigim aygffgklav epiiiswlge saprgsiatm ygvfnffgms
      361 asvivpsltg kisditgskl yafylailii gigtflfyli nrfvrdtnen ty
//
LOCUS       WP_010760641             120 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010760641
VERSION     WP_010760641.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..120
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14471
     Region          3..113
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(4..6,20,36..38)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(50,53,57..58,67,85,89,95,99,102..103)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mgykinefsk mtgltpytlr fyekeglltv krdqnniriy ddrnkewidf fmhlkktgmt
       61 iddlkqyliw wyegdetnqd rldllkkqke nalnemkqiq egidmldyki dvytkrvlgn
//
LOCUS       WP_010760732             209 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010760732
VERSION     WP_010760732.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..209
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23586
     Region          3..205
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mklyftrhgk tewnqelrfq gmtgdspllp tsyeeikllg qtiknvpfek ifsstslrar
       61 ktaeginqel eqpveiiftd elkelglgkl egqsimemrk iysdemnhmr yrldrynpev
      121 fqgepieqai srissvvqaa vdtgdgpylf vghgasltaa iqslsgkelg elrsmgglkn
      181 nslsiletkn dekeqsytlk lwnddsflq
//
LOCUS       WP_010760829             348 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Enterococcus haemoperoxidus].
ACCESSION   WP_010760829
VERSION     WP_010760829.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..348
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39902
     Region          12..345
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 msiyekfvqn erlrrffvla vvifilflar smitmilltf iftflalhfv kfvqqylkvp
       61 slilvlatys livflvylav tkyvpvlihq svqmynsvir fyqtptddhn qllmvidnyl
      121 eksnlmsqiq ngasillryv qdigsiglsf ilsfilsfff miekkqmaef sklflksdfd
      181 wffqdiyffa dkfvntfgvv meaqffiavv ntgitticla ligfhqlpsl aimifilsli
      241 pvagviisci plsfiayseg gindviyilv viivvhlfes yvlnpkfmss ktdlpifytf
      301 villiserlf gvwglivgip iftffldilk vkpihsvtek lsdppnie
//
LOCUS       WP_010760880             225 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010760880
VERSION     WP_010760880.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..225
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=25720
     Region          75..172
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mteqideyls fsdrindyis almvannigy enydcsylwd fvkskgvsmr sfpfdgiard
       61 risgmivkds lettigynqn msekrknfti sheithylfh mtesdtiftd tdrslhysyn
      121 evlqefqani gasailvpdv vffrflkegw nlsqlsnhfg isesalyvrl ihtmqanfgv
      181 syiaaktnad airykfsgkg qhaavelgtn lesrlfrtnr fieal
//
LOCUS       WP_010760913             304 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010760913
VERSION     WP_010760913.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33844
     Region          7..219
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 menkqvlevk nisksvgkkt iikdasfnvk sgkvtgllgp ngagkttiir mlvglmshda
       61 gsiqidgqsl stnfkeamah vgaivenpef ynymtgmenl kqyvrmspkp itddeliqvi
      121 hsvhlennid qkvktyslgm rqrlgvaqai lhqpdlllld epmngldpkg mrefremiqa
      181 lknqgvgvli sshqlsdmel lcddlvivqk geityvgpmn nqedenklil lletdqqqaa
      241 lsflkeqeys vnvdgnylki elledtrtvl vkqlvdkgig ikelkvhvds leenflrwte
      301 dggl
//
LOCUS       WP_010760951             393 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Enterococcus haemoperoxidus].
ACCESSION   WP_010760951
VERSION     WP_010760951.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..393
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43748
     Region          45..367
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mekkqetrwi kflggknllf tlvallllga vififhqvgf ifgpigvvfk tiigptilal
       61 ilyylfnpvv nwlekhkvkr vygvsaifii litlivvgii lvvpilqkqv egliesfpqy
      121 mddlnkmvtd ffhnsalekp lanaldaiqr wfdnisdgig syfskavega stvfstltgf
      181 alvmvtapii tffllkddqk ffsfvlkiip prfrgdakei gatmssqvga ylkgqilvsi
      241 aigiltfigf wlikvpysgt lsiivgitav ipyigpviaf vpaaivalmv sfgmfikmsl
      301 vwmlvqmlng hliapqvmgk rlvvhpltiv ivllvmgdll gmfglifgip iyaiakvlvt
      361 yifrkfkqry nqfygdsgey edtefskeey lde
//
LOCUS       WP_010760961             189 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF1836 domain-containing protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010760961
VERSION     WP_010760961.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10556141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..189
                     /product="DUF1836 domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21120
     Region          21..121
                     /region_name="DUF1836"
                     /note="Domain of unknown function (DUF1836); pfam08876"
                     /db_xref="CDD:430279"
ORIGIN      
        1 mneiksslev wgkelvdvhl prwhelpele lymdqvitlv erylspvilk kkhtlltssm
       61 vnnyvklgli papnkkrynq khlafliait llkqvltipe ikqgivyqga avgireaynl
      121 fcdeqeaala vvvaqalgne pvaafdqpip veflivkgat lsfatklfte kvielaqknl
      181 eedgeqade
//
LOCUS       WP_010760985             394 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010760985
VERSION     WP_010760985.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..394
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=43832
     Region          26..390
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mrksltakse pvnyalllpv fllilvgfva qygafhadpm vesiapllkk qllwtilgig
       61 tmfgtmfipi kylwkltpal yglslilmgl likfhdpvma aatgtkrwlr lgpisfqpse
      121 fmklgyilml ayivtrrrqr attpstsked fhllgelviv slpvlalmfy qkdfgtslvf
      181 isiflgivlv sgcswkiltv gfsiigvlgv sgillvlteq gqkilsflhf kpyqfnriha
      241 wlnpfeyads isfqqarglt aigsgemlgk gltnlqvyvp vresdmiftv igeaygfvgt
      301 calillffyl iyqmlictln akrefyayit tgvimyflfh ilenigsnig llpltgiplp
      361 fisqggtayl anfigiglil smyyqkekve vdsv
//
LOCUS       WP_010760986             393 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010760986
VERSION     WP_010760986.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..393
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=43708
     Region          1..376
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mswpkrlskl hyvdfyilip ylilcvvgil mvyssssyql ldselgtask aikqsmyflf
       61 slfcmsfvyr vnlsvlrkpk mmyfllaltf lsivalpfig tsvggakrwi nlgvllfqps
      121 elvplvlvly lssnlskndt lvpftfknhk rsllvsiffm ffvalqpnia gasmifilvl
      181 vlflfsglsp lftslalvgf vaikrlgtvl llsiptdwmp qkfsylvtrf evmqnpfidp
      241 tgkgfqtsna yyamhnggfw glglgnsiqk kgflpaadtd fifaicieel glifslgilf
      301 avffivarlf llaikskyly ysylyigcgm llflqvsvnv gsllgyipmt gltfpfisyg
      361 gssllilsit lgvalnargt elretirrqg gvv
//
LOCUS       WP_010761035             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010761035
VERSION     WP_010761035.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..283
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32380
     Region          1..270
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnlilklknl drlttsekal vdyildspek vihfspkela nhsyvsisti yrlinkldld
       61 glndlklalv nylnehnseq iidmdypisa ednhyamtkk lktvyeqtvq stidvntvem
      121 maitsslidk safidiyass aniyfaqnfq fqmqeigkri nvpiddymqn lsaanstsdh
      181 laiiisyegr gssvkkivet lkknnskill itsknstlld ekvdgtlffs slenhynkis
      241 sfstrmslmf lldrlylsff nqnyeknlay klenyqkmnp nli
//
LOCUS       WP_010761047             475 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761047
VERSION     WP_010761047.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 475)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..475
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53698
     Region          1..466
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 midlhdvtfa yedqetiiqe velqvksgef ivlcgksgcg kstllrilng lipelytgel
       61 tgtgsvldqe lltkefnayv rdigvvfqnp ktqfftsdvy selafameny gipreemirr
      121 ideitslfsl eeflersmfh lsggqkqlia fasasmlkhr lflldepssn ldeatieqlk
      181 aylqvlknqg mtiivsehrl yyltdladry lvmdkghivk gytsqemrtk ssleikgmgl
      241 rsleqtslkk vvepdktegk ltltcvglef hyrkqssvlk ipsltlnssy itgiighnga
      301 gkstfsklls glikpkegvi klneqvmnpk elikesfvvm qdvnlqlffe tvekeislna
      361 kntnefdkiv amlnlepllc rhpqtlsgge kqrvaiasal lsgkkiiifd eptsgldlmh
      421 meevsntirw lhhenilvlv ithdkeflnq tcqrilhfek gnsiedyfie ptike
//
LOCUS       WP_010761051             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010761051
VERSION     WP_010761051.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..265
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29636
     Region          1..263
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mesyieliiq anqkkftdve rviaqyfldg nkelgiqela kklsvsnssi trfckkigla
       61 nykeliylyk ysskgaknqn dssisyvnln yslllndiie kldkeevkka almidagrii
      121 hywgtgynaf cgedfqfkfs rlgkivnvik dehsismmah gvqqgdlvvv ssisgdneai
      181 qeavktvsek nakvivitan ekspykefsn afcltssmgk kdmggispqi pvltvidily
      241 teilamyhed tikswiksev ilkgk
//
LOCUS       WP_010761064             410 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Enterococcus haemoperoxidus].
ACCESSION   WP_010761064
VERSION     WP_010761064.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..410
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=45806
     Region          5..406
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mkkevvvigl gyvglpsvin hvknghkvig fdideekvdm lnkgishldt vldetvrmik
       61 ergaeftcda qrikdkdvyi idvptpidky ktpdlsyiks avdliknkvk tgslivlest
      121 typgtteeyl vaefsklgyh igtdlfiays peridpgntq slsakipriv aghtdkclsk
      181 veeffgshvs tvpnlktael akiyentfrl vnialadelq kisdnldiev gevleaaatk
      241 pfgfmkftpn lgigghcipv dpyyltwlme srgietpliq tagkindsml dyylekiity
      301 ankksdknld emnvailgvt ykknvadtrm ssvitlikel eemnvtvvay ddiilsntns
      361 pvesitsleg dycqlkkfdm viyavdhely eknkeniidn sqlfydltlv
//
LOCUS       WP_010761058             690 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010761058
VERSION     WP_010761058.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 690)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..690
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75667
     Region          51..687
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     Archaeoglobus fulgidus CopB, a Cu(2+)-ATPase; cd07552"
                     /db_xref="CDD:319850"
     Site            order(338,340,644..645,672,676)
                     /site_type="other"
                     /note="putative HM ion binding site [ion binding]"
                     /db_xref="CDD:319850"
     Site            order(382..384,448,464..466,493,533..535,555,558,561,580,
                     583)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319850"
ORIGIN      
        1 mnsneethkn hhshkmenmd hssmnaddhe qmssmdhtmh mgnfkqkfwl slilaipiif
       61 lspmmgvdlp fqftfkgsdw lvlilasilf fyggepflsg akmelkqksp ammtliamgi
      121 svsyfysvya fvmnklmpqn hvmdffwela tlivimllgh wiemnaisna sdalkkmael
      181 lpdkvkrlnk dgseeevslq avkevdhlvv rsgdkipadg iiikgntsvd esmvtgeskt
      241 vtkkendkvi ggsvngsgti eisvtgtget sylskvmdmv kkaqtekskl eslsdrvakw
      301 lfyialgagv lafvvwlsid kdlsiaferm vtvfiiacph alglaiplvv arstsiaakh
      361 glllknrnal eqandmqyvm ldktgtltqg kftvtgiemi tneitkkeal kvigalenna
      421 nhplaigimn ylkekaispy kaenlqsisg vglsgkvnkq avkivnekev erltisfdrs
      481 lkqryqeqgn tlsyliiddq liamialgdv vkpeakqfiv dlktqgiipv mltgdnkvaa
      541 esvarylgid efqgellped kekiiqtyvt egkkvmmvgd gindapslvr atigvaigag
      601 tdvaidsadv vltdsdpkdi lrfldlakqt rrkmiqnlww gagyniiaip laagilapwg
      661 illnpavgav lmslstviva anamtlrihn
//
LOCUS       WP_010761078             159 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside 2-deoxyribosyltransferase [Enterococcus haemoperoxidus].
ACCESSION   WP_010761078
VERSION     WP_010761078.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..159
                     /product="nucleoside 2-deoxyribosyltransferase"
                     /calculated_mol_wt=17247
     Region          5..>109
                     /region_name="RCL"
                     /note="Nucleoside 2-deoxyribosyltransferase [Nucleotide
                     transport and metabolism]; COG3613"
                     /db_xref="CDD:442831"
ORIGIN      
        1 mniyfagpmf akadllyney lvkeiraldd sikvylpqen gaindktaya dskmialadt
       61 ekvlesdllv avldgitida gvaseigvay aknipmvgly tdtrqqgadn qkklaaigdi
      121 aenqfhylnl ytiglvklng avvsgeqafl dlikeklnk
//
LOCUS       WP_010761085             131 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761085
VERSION     WP_010761085.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..131
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14950
     Region          38..127
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(51,54)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkkislvili vlfligcspk eslteipkeh sidlvlpqhg raiiyfgrds cphcknffpk
       61 lkavmknqgk vlyyynidnh lqdsllskem enfkieqipa lviyknkeii atlvgdksek
      121 eienfikqse s
//
LOCUS       WP_010761095              66 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Enterococcus].
ACCESSION   WP_010761095
VERSION     WP_010761095.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7053
     Region          1..65
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mntgtvkwfn adkgfgfitq dngtdlfahf saiqgdgfks ldegqsvsfd ieegqrgpqa
       61 vnivkn
//
LOCUS       WP_010761114             317 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761114
VERSION     WP_010761114.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..317
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35264
     Region          1..249
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkqynwgiig lgdiatsfae sfqqensrit avasrtlaka ktfaeehgip eaygsfeell
       61 anetidiiyi avpnrqhleh ilkalkagkh vlcekaitmn seelgeamkl aeekglilae
      121 amtifnmply helrsqidsn rfgklkmiqa pfgsykdpdp tnrffnpdla ggalldigty
      181 avsfarwfft aqpkviasvm qpfstgvdeq satilqndaq ematvslsfq akmpkqgvva
      241 fenayivine ypradeakif fndgtietvv sgntsqalny eitnmvkmie gnlpnrslfl
      301 tkdvidlldq mqqqwnk
//
LOCUS       WP_010761140             468 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Enterococcus haemoperoxidus].
ACCESSION   WP_010761140
VERSION     WP_010761140.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..468
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49285
     Region          1..467
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mekffklken kttistemva gvttffamsy ilfvnpsils qtgmpfqavf latiiasiig
       61 tlimglfanv pyaqapgmgl nafftftvvf glgytwqqal amvficglin vlitvtkirk
      121 liikaipesm qhaigggigi fvayvgikna klldftvqae ptkgvvngns ivpalgnfnn
      181 peiilavigl vlttvlvvln vrgailigiv attiiaiplg vvdlsaidwq anslgnsise
      241 lgttfgaafg adgmqslfsd askipqvlmt iiafslsdtf dtigtfigtg rrtgifsked
      301 elaledskgf stkmdkalfa daiatsigav fgtsntttyv esaagigagg rtgltsvvva
      361 alfalsslfs pliaivpaqa tapalilvgv mmlasfkdie wtnleeaipa ffasifmglc
      421 ysisygiaag fifyaivkva kgkfreispi lwvvnalfil nfiilail
//
LOCUS       WP_010761166             212 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761166
VERSION     WP_010761166.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..212
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24472
     Region          6..198
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 mehqkmkaik dftqsimekd ksghgmdhin rvvrlankia etetcdhfiv taaaylhdti
       61 deklvsdser ayqqlndfln ginistfqid kiihiiknls fsqqlngtte rltsegqivq
      121 dadrldamga igitrtiyyg gykgnpiydp nikprtlqsk seyreestii nhfyekilll
      181 ndrlntkyak eigakrqkfl edfleeffee wd
//
LOCUS       WP_010761173             285 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010761173
VERSION     WP_010761173.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..285
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30941
     Region          1..278
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mqqniiltiq dhlkhlpgse qkvaeyilen tsavinlsak elakksgssp aaiirfcrsi
       61 evsgftdlkl llsanlgtvd tqmyteveng ettaaikekl qhrlihvler tnehledqai
      121 dqavkeleta eiifvyglga sslvaqdiyq kftrlglsvf ftmdhhlfas aigtnrlkgi
      181 figishsgtn qetnaladla iekgltvigl tansdsalaq kssillltpi ggeaplrsaa
      241 tvsltaqlyv vdvlffayaa knynetleki qdskeaveiv kkdln
//
LOCUS       WP_010761196             322 aa            linear   BCT 01-JAN-2025
DEFINITION  PhoH family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761196
VERSION     WP_010761196.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..322
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=35702
     Region          5..322
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 mtenqsisle lklndsddvs mllgthdkhi kyleentavt intrgemiql lgeeaevqlv
       61 asviktlqvl iqrgikvstp dvvsalkmak ngeldkfvtm yeeeilkdhh grairvknig
      121 qkkyidairk rdiifgvgpa gtgktflavv mavsalkkge vqkiiltrpa veageslgfl
      181 pgdlkekvdp ylrpvydaly qvfgmdhtnr lmergvieia playmrgrtl ddafvildea
      241 qnttvaqmkm fltrlgfnsr mivngdtsqi dlpkgvasgl ihaertlksi dkisfvhfda
      301 gdvvrhpvva qiirayekes qk
//
LOCUS       WP_010761260            1192 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761260
VERSION     WP_010761260.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1192)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1192)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1192)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1192
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..1192
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=138999
     Region          4..1169
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mslqfirgta emdleealiq asvqwlseed shevfylvpn hmkfeqeina lkrikyiqkn
       61 qndsiatmrf qvfsfyrlaw yflqhtqyyg seilseagaa mvfrkilsen eealkvfrge
      121 vnksgfiqql fdlyqemkeg nidldelfgh fsgqqtdske qdlqlkiqdi klvfskfeet
      181 msqygiksae iinylteyle tkdlrnvlfv ingyhnfsar elklietlmr rggevkislv
      241 ldkkypnelp slmnlfyetg ttyhklyqla rnanvailpd hveknkklia dnsiqtleky
      301 wieaqeshpk rgkqrinddh lqfwcaenpk eeinhiakei rrlvveenyr ykdiqlltre
      361 ldsyetmiep lfsmneipvy ldrdmameqh plvefiqslf aihayhyryr dvlrflrtel
      421 ffpiedqisv eewqvqrnew rrkidvaenv vlaygyegyh weknkdwhfi rydfeaeqqd
      481 dteliekdsn tvrkmiqqnv paffktiqka qtgveaadff yrflvnngve kqlmmwrnqa
      541 iemgqleqar nheqtwealm tlldeyvtiy gndsfdlaaf eeifssgleg lrynkvptai
      601 dqvqvrsidl arpgqakvvf aigltdqvlp qkfdnktlls deerqfvndq lddgqfllnd
      661 trksiakepf nayimfaaat erlyfsypsv kdtakdvkvs tyltniqndl glqmqqrnal
      721 tilddeqvsl ehigtyrtli sdltnlkrqk kemqegilaf wltlerqlmk hsqaalashv
      781 feslghrnlp enlqehlade lytkhiytsv srmesfyrcq yqyfsrfglg lkerdvfgls
      841 paatgdffhe aldqffklli mqnkqlselt drevsefteq ilntvfgeik fsildtssrm
      901 nyiryqlgqt ikkvswalkr qsersgmttv qtevlfgqia sqkgikglel plknggnisv
      961 rgkidrldql vtpdslylgv vdyksshkkf niteayygla mqmltyldva lmdavnlvgq
     1021 sakpagsfyl hvhnpilpye tedkkeqqll kkfqfdglll ndpvllenld kslqakqssl
     1081 ifpieesake iikpgrrqed kfvtepelga llthnrskfi eagnkvtsge ielnpayqgk
     1141 eriacrfcpf rsvcnfdvml kennynriet lskkdvmdrl ieneqeggtn de
//
LOCUS       WP_010761293             690 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010761293
VERSION     WP_010761293.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..690
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=80112
     Region          21..662
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mtdersrilm krliersihe vdeltdqtgl tkrqleysld kineyvttek gsklviennr
       61 iiltnqlreq fiailsdkty lkgylmnace rskylylllf yflddylsin hfieelgvgk
      121 ttiindlknl aielereniq lvytrkngyq lvgneeqiry hlmkmiiwds tenntvfvyd
      181 hfiekhqiet vdstkqlvek ytkrygisfv enrlteflyt fiflkkrlls ltanvnpkyq
      241 lsaliamkey qfsksilihf giedesarvy lcawilglsi grpndstkdy etiidlvkri
      301 ilrfeaisgi rfnnqelvvr qlythlrpay yrlyfklpiv nplhtkirde ynelfnivee
      361 tlkpiaslfe hpipedeiaf ltmhfaslcs sfdeytttqk valivcpngi gsssivytel
      421 kvlfpelsfl gpvetneier lsdsydlifs tvpnirlfyt kkpvyivspi mntrekyrli
      481 sdvytqigns nfklpsvgki meiiqryaai segaslekel ydyltnqeeq tenneegpsl
      541 leitapeliq ldmhaknwee airlsaasll kegritrnyi dtiietakne gpymviskhv
      601 alpharpvdg veklgmsisv lkhpivfgsq endpvkyifc laatennrhl namaelvrll
      661 ddpqfydlld tsndpneiyh ylsrkevllg
//
LOCUS       WP_010761300             313 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010761300
VERSION     WP_010761300.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..313
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34905
     Region          12..313
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mkisedrrkm lkivtmyyeq gltqtviakk mdisrpvisk ilqqakelgv vsisikdesa
       61 havelglqle kkyqlkdviv iptneqkqve slkkevsrsa sfylkerlka dmsiglswgt
      121 tladmidemp ycsfptinvy plvggisseh lyfdtnhlvf rlaeklnsrc qyfyapalae
      181 ssiladvlnq sqlvgnsmkq aknvdfaiig vgnpnesstw krlgyiekke lqiikktgvk
      241 gdavaslfdk ngqtvnneis krmlgikved lvnipdvmvi gcgeekaesi rpllrgkkct
      301 iliidqmiae all
//
LOCUS       WP_010761314             295 aa            linear   BCT 01-JAN-2025
DEFINITION  SPFH domain-containing protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761314
VERSION     WP_010761314.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..295
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32769
     Region          2..274
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mviivqqgev kivesfgkyv ktidpglhfl ipvlykvrgr vslkqtplei esqsvitrdn
       61 vivevdeaik yhvtdvrafv ydnedsvtsm iqdcqsnlrg iigkmdlnev lngteeinvs
      121 lfesvkdita gyglsidrin igeisvsdei vnsmnklita srdkestiti segrkqsiil
      181 dseanasqmq idaearakqt kidaearaer tkidadaeae riritteaer qrilalnqai
      241 kdsdlneqtl aylgieafkq vvrsdtntvi lpsnmtelgn ipvvkelwna qdtkd
//
LOCUS       WP_010761429             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [Enterococcus].
ACCESSION   WP_010761429
VERSION     WP_010761429.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26885
     Region          1..226
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 merlqkviah agiasrrkae eyivngrvkv ngkiirelgt qvgkndkvev ddvpiykeey
       61 gyylfykpkg visavsddkg rkvvtdffsh ikeriypvgr ldydtsglll ltndgefsqk
      121 lthpsheidk vyvakvkgla kkhdllpltk gmkiegykta paafeiisvd lktntsivel
      181 tihegrnhqv kkmlqavgyp vqklkrekyg dltlkglrpg eyrnlnkkei svlmnqsk
//
LOCUS       WP_010761485             390 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010761485
VERSION     WP_010761485.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..390
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=44363
     Region          3..390
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mnimvtkkse kkfkgrypli qkedlhdipk tfsnewvkfv dskgqfiatg ylgeqnkgig
       61 wlvnwqgsvd apflenlflk akshrmvyeq destsayrif ngegdglggl iidrydnfav
      121 fswynktlyq kkeeivqafk ksfpeivgay ekirfasksl pesqklfgnd apepllvyen
      181 gvlyatylnd glmtgifldq kevrgrlieg gaagktvlnm fsytgafsva samggssvtt
      241 svdlakrslp ktkeqfevnh laaedqkiiv mdvfdyfkya arkqlrydvi vldppsfarn
      301 kkkvfsvakn ygdlvkdsvd ilekegllia stnaanisle kykkmiieal eekqvryqfk
      361 etyqlpsdfk tnkhfeegny lkvffieilk
//
LOCUS       WP_010761518             327 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Enterococcus haemoperoxidus].
ACCESSION   WP_010761518
VERSION     WP_010761518.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..327
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36656
     Region          10..307
                     /region_name="AKR_AKR13C1_2"
                     /note="AKR13C family of aldo-keto reductase (AKR);
                     cd19078"
                     /db_xref="CDD:381304"
     Site            order(19..21,52,57,82,123..124,153..154,173,201..207,258,
                     275..280,283,286..287)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381304"
     Site            order(52,57,82,123)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381304"
ORIGIN      
        1 mkerqlgkng lvtseigfgc mglnyhrgpa kdknemievv rtaidagikm fdtaevygpy
       61 tneelvgeal agkrnqvqia tkggfkidgl knqpdssska iisavegslk rlktdyidly
      121 yihridpntp ieevaltiqk lkqegkilhw gvseagaeti rkahkvepla aveseysiww
      181 reveeevlpv leeleiglvs ysplgrgylt gklnkntrfn endnrgelpr ftqeamranq
      241 vlldfmqeia dtknittaql aiawildqep wivpipgttk kerilenvta tdttfspder
      301 viiskaleqi rivgdrypes ekkrtgr
//
LOCUS       WP_010761531             135 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761531
VERSION     WP_010761531.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..135
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14926
     Region          26..127
                     /region_name="cupin_HNL-like"
                     /note="Granulicella tundricola hydroxynitrile lyase
                     (GtHNL) and related proteins, cupin domain; cd02233"
                     /db_xref="CDD:380361"
     Site            order(35..36,67,69,90,92,94..95,114,116,118)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380361"
ORIGIN      
        1 makfeevkng vifpvgekne ayaqyfigqs ylnnliadpe vnvgvgnvtf epgcrnnwhi
       61 hhdgfqlllv tggegwyqee gkaaqfltag dvvvthdgvk hwhgaakdsw fehlaitagt
      121 pewlepvsde lynql
//
LOCUS       WP_010761537             130 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010761537
VERSION     WP_010761537.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..130
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14899
     Region          1..113
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(49,52,56..57,66,84,88,94,98,101..102)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mnikkvsels gvsadtiryy eriglippvk rnsngirnfd eedlrwivfs rqmrnaglsi
       61 eslveyltlf qvgnetvpar keiiadqise lkekaselnt aierlefkla nydehmipae
      121 nalrdfninr
//
LOCUS       WP_010761573             505 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus haemoperoxidus].
ACCESSION   WP_010761573
VERSION     WP_010761573.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 505)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..505
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53769
     Region          196..411
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mdfikramls mkskkgrtfl lcavfsaili fvlagltiqs aaltttenak ksvgatvtls
       61 anreaamkkn qegstgekpd pssfsltpvs ladaqkiadl anvksysfls sssagasdgi
      121 tpistesese tttgstasdg tqgepqavgr mgsgpmsdik qsdfqvsgvm elsmssdfsd
      181 gtaeitsgev inasdketnn vvieqtlada nelkvgdtfk vtdpeddtkt yeltikgiyk
      241 tsengnsmgm mfnflnpant lytsytfant lkgddakdti dsasytladp kqmdtfvkea
      301 eklidtenfs lqtndqayqq mlqplnnvas faknivilva iagviiltli vmmmirerry
      361 eigvllslge srfkvvlqff seiiicmfva lviatfsgni vgnvvgeqli tqqtesvsqa
      421 tnnqgqptek gdrgserqgv pgggsmnrlg assqgtakai eelnisvqpk eitivaglgl
      481 lisflsiils ssgilrlqpk kiltt
//
LOCUS       WP_010761655             212 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761655
VERSION     WP_010761655.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..212
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23731
     Region          4..203
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mttfyfvrhg ktelnlslrf qggdidspll pigveqaiqa grylcdtsfd iaavstqkra
       61 mdtanyilke nnfldgltvq yydslreikf gkregveidh tdeqtdhlrn rpdlydptaf
      121 dgetidslva rstetiekis esypdgkvli vahgvllitl inslvgkeka kwreggplan
      181 tsitileket nqqnytiksf ndisyqsqse ea
//
LOCUS       WP_010761756             422 aa            linear   BCT 01-JAN-2025
DEFINITION  RidA family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761756
VERSION     WP_010761756.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..422
                     /product="RidA family protein"
                     /calculated_mol_wt=45281
     Region          22..125
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
     Region          <171..273
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
     Region          300..412
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msnnnavlar ntknapqnpl asqtvafshy nnfsaqlpid pvtgqlvagg inkqaeqcfe
       61 nikaiaksid hvmndivrit ifvkhskdvd avdevytsff tsyqpsrtvv vvedlplgal
      121 vqiealvsng egtiphapqa gdlikltnnt snaptsslst qtvsfshynn lsaqlpidpk
      181 tgrvvagcik kqtgqclkni kailesidvp lddivkitif lkdlskmdav nkvyttffpd
      241 saiartvayv partvvavkd lpmgaavqie avvshgdgtp pqaiedrhgl iieanntela
      301 pkcpfstqtv afshynnisa qlpidsktne mvtggikeqt gqclenikai iesvehvmtd
      361 vvkvnifvkn iedmdavdev yarffpdgvp arrvvgvsel pkgalvqida ivgnaegtpp
      421 iv
//
LOCUS       WP_010761698             195 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761698
VERSION     WP_010761698.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..195
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21979
     Region          3..129
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,67..68,71)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(66,110..111,113..114,118)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(72,77..78,106,109..110,113..114,117,120)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95..97,106..107,110..111,114,118,121,125)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95,111,114,118,121,125)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(119,125..126)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mkiigyartt indndldaqi nilsdfgcde vyqesfditn dkhliselet vlngletgdt
       61 lvicrlnrlg rstrqltelt qtfkdtgihl vslheeidtr hpmgeiyfkl mnglatmecd
      121 litertligl snarkkgkig grpkidartv kkirhlyhek ketiqfissk cnvsvgtcyk
      181 yinlseadva klsqe
//
LOCUS       WP_010761803             312 aa            linear   BCT 01-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010761803
VERSION     WP_010761803.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..312
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35164
     Region          2..307
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mihlicpnpa idrtllvenf tserpnrpye vkefaggksf nvayaldfed stvpycihti
       61 lggrngaflk elasikdihl eitdvdvntr fctiivdtkt hriypiyens fvlnplllnk
      121 ftkqllntiq pkdtvvfsgs lmkgmpddyi aqiqnqlkgq nirffidtsg palveaykgk
      181 pdvikindee lndlvpdrtf keledyvnfl nsetaaaipy fivtlgekgv iaklnqqiyh
      241 lfvppvqakn piacgdfflg glvkyltlgs lkdidvlkka vsystanvln wfpemkqldi
      301 drieqkiiik kl
//
LOCUS       WP_010761824             230 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010761824
VERSION     WP_010761824.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..230
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25661
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mkaieflsvd kqfldgdtti ealkstdfsv ekgqfvavig psgsgkstfl tlagglqtpt
       61 ngevkinnea fseenektrs kirfseigfi lqasnlvpfl tvekqlrlvd kvkkektdvd
      121 kvnklltelg ieklkkkypd eisggerqrv aiaralyndp siiladepta sldsdrafev
      181 vkilaretke knkatimvth dqrliehcde vyvmkdgvlq kqktlkkqmr
//
LOCUS       WP_010761862             275 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus haemoperoxidus].
ACCESSION   WP_010761862
VERSION     WP_010761862.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..275
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30200
     Region          4..265
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,196,218..220,222..223)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 miklvaidld gtllnskkei sernkqalak akaagvkivi ctgrplaaig iyldalnlrd
       61 ngdysitfng glvqkndtge iiekasmple nvhdlfelaa alnvpldils dglvlqlptt
      121 qnyeslysql ntlltyesye ldqltadriy nkaviaveqt yldeqikkip spfydryeii
      181 ktrsnllefm pkgitkaygi sllardldin qeeimtvgde endlpmieya glgvamenav
      241 arvkdladvi tdtndndgva qavekfvlep lkggi
//
LOCUS       WP_010761922             143 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus haemoperoxidus].
ACCESSION   WP_010761922
VERSION     WP_010761922.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..143
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16497
     Region          13..142
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 meyhakeftt lttkefleiv klrisvfvve qncpyqevde adefawhtwl qegpdivgyt
       61 riidkgdtvt fgrviinpdy rgkklgnkll eetlkviedk ypnrpiiiga qahltdfyga
      121 fgfeaisdvy leddiphinm rrn
//
LOCUS       WP_010761929             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010761929
VERSION     WP_010761929.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..269
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31463
     Region          2..103
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(3..5,19,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            40
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(51,54,58..59,68,79,83,89,93,96..97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          119..258
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mfkisefsql tnisprmlrh ydklnllkpe iihqennyry ytaeqinqan rilslknvgi
       61 plkeiktlle nendqtdyli hhrtllerel aekklqlayl dwleekkksp eetgmnypie
      121 tkkmndllvl tyrqnvtsyy eeeqlwqqlf atirsedmst lgqsiavfhk ttsknidiev
      181 mvsipeslkh iypesktfsp gliasvvtng syasmptiht dmdnwlnvne ytlsgnifni
      241 yhsspaneer eecyitevcy piekpfnqh
//
LOCUS       WP_010762167             297 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010762167
VERSION     WP_010762167.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..297
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33793
     Region          27..291
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mskgkglgrg idalfqdfas ledvdvqkee vleiplnelr pnpyqprktf deaslqelan
       61 siqqsgvfqp iivrksavkg yeiiagerrf raskladket ipaivrefde eammqvavle
      121 nlqredlnpl eeaeaydmlm knlkltqvev aerlgksrpy ianylrlltl ptqvkemvqg
      181 eilsmgqart llglkdkdli ltlakrvvee nltvrqleqi vndfnenqgk kapkkekkai
      241 kdkpyyires edrlmdkfgt tvaiqekegk gkieieylsq sdlarildil eihfdea
//
LOCUS       WP_010762234             269 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010762234
VERSION     WP_010762234.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Stukey,J. and Carman,G.M.
  TITLE     Identification of a novel phosphatase sequence motif
  JOURNAL   Protein Sci 6 (2), 469-472 (1997)
   PUBMED   9041652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10107962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..269
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0042577 - lipid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0046839 - phospholipid dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=30322
     Region          128..252
                     /region_name="PAP2_like"
                     /note="PAP2_like proteins, a super-family of histidine
                     phosphatases and vanadium haloperoxidases, includes type 2
                     phosphatidic acid phosphatase or lipid phosphate
                     phosphatase (LPP), Glucose-6-phosphatase,
                     Phosphatidylglycerophosphatase B and bacterial acid...;
                     cd01610"
                     /db_xref="CDD:238813"
     Site            order(149,156,187..189,231,237,241)
                     /site_type="active"
                     /db_xref="CDD:238813"
ORIGIN      
        1 mkkqtkiffg fvaclllift ftdlqiseml ynpkstfgwf fesfgeviia ligcfstvgm
       61 irtsgkkwsv gtillgtlfl fdtfmasfli thylklptfa mgllgiccvi ifpligfniq
      121 padfevvrri akagvvisla pilivtlvkm lwgrqrfrsm ldpaaeftpw yvingftmnd
      181 dfmsfpsghs ansatiiwit wlplwlerlk gretllslis giwiicvmls rvimgahfas
      241 dvlmgaaivl flnmylkkkw ypsiefgth
//
LOCUS       WP_010762264             294 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010762264
VERSION     WP_010762264.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..294
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32853
     Region          2..217
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mitvtkltkm mnkatilnnv sftvnkgeii alvgpngagk ttlincltgl irptngeisl
       61 fgtnplnkkn kvkvgvmqqe sttlenvkvk elltlfrsfy pkplslddll ditgltehrn
      121 tyttklsggq krrltfglsi ignpellfld epttgmdvts rkifwkkinm lkeqgktiil
      181 tthyleeiek vatrillmkq geivhdgtle siqsemlqnk lsfqlldild eaklvdlpyv
      241 stiekvennv tlyssnsdet lielftteik fknllispgn letafntlve eedk
//
LOCUS       WP_010762361             302 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Enterococcus haemoperoxidus].
ACCESSION   WP_010762361
VERSION     WP_010762361.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..302
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33086
     Region          1..302
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mkeillqaig fcfviflgyl mkrigllska dggmlsviiv nitlpatviv slanvvvsgt
       61 lffllamgiv lnilviligg kvskkrsile qkfqmysmsg ynignfslpf iqgfyplavp
      121 fllmfdigns vmltggttll idkvvgtkee ttfkkivlal fksapftaym vmlllriiqf
      181 nlpvevlgvl emiakangfl smfmiglyfe lrlpkkalhl vkevlvwryl cgaifallfa
      241 fvipldpllr ivlvvlsvap mptfsvinsv kvgmpeetvg ftssasilis lvlmtlimmf
      301 mg
//
LOCUS       WP_010762371             505 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease/substrate-binding protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010762371
VERSION     WP_010762371.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..505
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56158
     Region          <45..208
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          235..498
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(241,243,291..292,295,338,340,418,442)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mgklietfia rkedfiqavv ehiqlsllsl liailiaipl ailltnykkv aefvlqitgi
       61 fqtipslall gllipvigig sppaivalvi yalfpilqnt ytglteidps leeaaeafgm
      121 nkreklikfe lqlalpyiis girtatvmii gtatlaalig agglgtfill gidrnnvyli
      181 ligaissavl avlfnfgihl lekatvkriv aafmvllall vgsfvythhe aeqkeitvag
      241 klgaepdili nmykeliean sdihvnlksn fgktsflfna lksgeidvyp eftgtvletf
      301 lkdnkntsnd prevyeyard qikkqenmdy lepmryqnty avavkrsfae englktiedl
      361 kkvesqlkag ftlefidred gykglqklyn lnldvksmep slryqainng dvnvvdayst
      421 dselkqydlv ilkdnkqlfp pyqgapllka etlekypelk ellqplvgki teeemsemny
      481 qvnveqkdpa tvahdylveh gmlee
//
LOCUS       WP_010762436             437 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Enterococcus haemoperoxidus].
ACCESSION   WP_010762436
VERSION     WP_010762436.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..437
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45855
     Region          1..434
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mkgkiisyfe idklnttmkr eflagfttfi smayilfvnp tvlgasgmde gavftatala
       61 salgcilmgi fakypiatap alginaffay svcvgmgvpw etalagvfva slifilitvf
      121 klreliidai padlkyaisg giglfiaflg lseggiivsn estlvalgpl nvgstwltif
      181 glvitaimmv rrvpggifig mtattilglv tglievpaki isaapslkpt flvalkhvgd
      241 inslqlwvvv ltfllvtffd tagtlvglan qagfmkdnkm prvgkalaad stamlagsll
      301 gtspvgayve ssagiavggr sgltavttgl ffivglffsp llsvvtsqvt apalivvgvl
      361 maqslsqikw kemeiaipsf lillgmplty sisdgialgf ifypitmiaa krgkevspim
      421 yalffvfvgf mwilnan
//
LOCUS       WP_010762462             558 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010762462
VERSION     WP_010762462.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..558
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=63940
     Region          8..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          264..556
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mltvknflql apfksfqlva gskglenkit gvnildnpda sdwlsagell itsgyffsen
       61 aeiqkrfiqr fkeincsaic ikphiylkgi pesmrnlade lslpiieipy giafskimnt
      121 vmaeisgrmn elnqasldih sqffeislhg ggmskialgl aemvnnpvvl vdtdwtvlav
      181 sdykqpliqg aikksddtcp fpiqiftdlp tnferiqkpi trgilldeqe ypcvimpvyf
      241 dtihygfilv yqierpltdl dyvalengsm afaleqmrif eiertenrir rdffdqlltg
      301 qiknlealaa ydttidpsln ytvlifsiqt fghesdslmk kkqsedrlmk sllsslttyt
      361 atrfpqlhlf srknqlvmll gtdpklstlk thneisdtae rirmyleqqg hsereifcti
      421 gstlpilels qsfdeakkvi qlleddlree kiyffndfyf dsflvdsisk eqgkkfythy
      481 ldtlltydre nntsftptlk aylahhlnia ttsrglfihr ntllyridki kgllpvdldq
      541 ekntfalqla lklyelyh
//
LOCUS       WP_010762468             156 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Enterococcus haemoperoxidus].
ACCESSION   WP_010762468
VERSION     WP_010762468.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..156
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17118
     Region          3..>109
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mnymkmaada tvvgmenkfg gpfgatlvrk gevivsvsnt mmrdtdpsah aemvavreac
       61 kkletmdlsd ceiyatcepc pmcvgailwa giktvyysnt redaakhgfs dmhlrnyldg
      121 tdksslamih tggcpecdsl wetfdkinln dveker
//
LOCUS       WP_010762475             346 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010762475
VERSION     WP_010762475.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..346
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38636
     Region          1..346
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtfvdlkeir vsydgkqdil kdlsismekg elvsllgpsg cgktttlrvi aglikpndgs
       61 ftldeddltk vpvhkrnfgm vfqsyalfph ltiaenvafg lklrkeskgn tkekvekmle
      121 vcglenlgdr ypkqlsggqr qrvalarali iepkllllde plsnldaklr vamrieikri
      181 qqqlgittvf vthdqeecfs isdkvaimnn gvieqydspe kiyrlprtkf vaqfigfenf
      241 favtknaegq yksengqlft ttnpqptate tvatirpedi eivqelthes vegmvairtf
      301 lgksyqyevt tplgkllvng tseqiyetgd kinlafpadk lvilek
//
LOCUS       WP_010762474             259 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus haemoperoxidus].
ACCESSION   WP_010762474
VERSION     WP_010762474.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..259
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28286
     Region          25..236
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrkqkgmtli ailvflflfl plclivvtsf gtaaaiqfpi kgftldwyak alqsdtfmss
       61 fklslmigvl atvlalvvgi pasyalarys vrgrnfiksf flsptvipgi vvgytlfqyi
      121 viklglpifq gllighflis lpyiirvvgs smeqldysme evawtlgctk trafiqivlp
      181 nvssgifaaf mlafvnsfnn vpvsmflsgp gvtmlptsll symeynydpt vsaisvmlml
      241 ltmglmflie ktlglasia
//
LOCUS       WP_010762508             160 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Enterococcus haemoperoxidus].
ACCESSION   WP_010762508
VERSION     WP_010762508.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Ko,T.P., Lin,J.J., Hu,C.Y., Hsu,Y.H., Wang,A.H. and Liaw,S.H.
  TITLE     Crystal structure of yeast cytosine deaminase. Insights into enzyme
            mechanism and evolution
  JOURNAL   J Biol Chem 278 (21), 19111-19117 (2003)
   PUBMED   12637534
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Carter,C.W. Jr.
  TITLE     The nucleoside deaminases for cytidine and adenosine: structure,
            transition state stabilization, mechanism, and evolution
  JOURNAL   Biochimie 77 (1-2), 92-98 (1995)
   PUBMED   7599282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..160
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0001882 - nucleoside binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17812
     Region          12..110
                     /region_name="nucleoside_deaminase"
                     /note="Nucleoside deaminases include adenosine, guanine
                     and cytosine deaminases. These enzymes are Zn dependent
                     and catalyze the deamination of nucleosides. The zinc ion
                     in the active site plays a central role in the proposed
                     catalytic mechanism, activating a...; cd01285"
                     /db_xref="CDD:238612"
     Site            order(28,45,56..58,86,89)
                     /site_type="active"
                     /note="nucleoside/Zn binding site [active]"
                     /db_xref="CDD:238612"
     Site            order(54,59,63,87..88,91..92,95..96)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238612"
     Site            order(56..58,85..86,89)
                     /site_type="active"
                     /note="catalytic motif [active]"
                     /db_xref="CDD:238612"
ORIGIN      
        1 mtknqhikll nrcieisqka rehgntpfga lladkegnil leqeniemte nictghaett
       61 laarasqkys keflwecsly ttaepcamct gtiywgnigt ivyamtekrl leltgdneqn
      121 ptfdlpskei lrhgqkniqv igpfpeieqa aaavhegywg
//
LOCUS       WP_010762533             216 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010762533
VERSION     WP_010762533.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..216
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=24673
     Region          25..202
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(105,112,128..130,173,179,183)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mknklyyqfa gscflvvfmf lgyvvrfysg wlkgfdqtit tivrtpypsa nqffiwytkf
       61 adpltigllt latafilfrg kyyaetlwll intaliagia nplikllfmr prpalnhlvt
      121 ehsysfpsgh stgsvllygt iilllpqfik qknlclflqs ilglgiflig isriyvgvhf
      181 psdvlggfcf glawllmtyp iylekrfvwr fkskqq
//
LOCUS       WP_010762542             878 aa            linear   BCT 01-JAN-2025
DEFINITION  fibronectin type III domain-containing protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010762542
VERSION     WP_010762542.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 878)
  AUTHORS   Bloom,L. and Calabro,V.
  TITLE     FN3: a new protein scaffold reaches the clinic
  JOURNAL   Drug Discov Today 14 (19-20), 949-955 (2009)
   PUBMED   19576999
REFERENCE   2  (residues 1 to 878)
  AUTHORS   Koide,A., Bailey,C.W., Huang,X. and Koide,S.
  TITLE     The fibronectin type III domain as a scaffold for novel binding
            proteins
  JOURNAL   J Mol Biol 284 (4), 1141-1151 (1998)
   PUBMED   9837732
REFERENCE   3  (residues 1 to 878)
  AUTHORS   Potts,J.R. and Campbell,I.D.
  TITLE     Structure and function of fibronectin modules
  JOURNAL   Matrix Biol 15 (5), 313-20 (1996)
   PUBMED   8981327
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10045852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..878
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..878
                     /product="fibronectin type III domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=95805
     Region          <557..611
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(600..601,603..604)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
ORIGIN      
        1 mkknihlift cfiiviifpi dwsyaieiek paietsstte vieedvtsds sempvsdsss
       61 sqestmeevi enekitdsnd inddiseins knmvkavatq dadgfwlvds aatlteylkd
      121 sqklkfrltn nidlgstgyq lkdgviidga nhiitynkga satsgfyanq anavieirnt
      181 qfgnldgsga vgyygflsgg aaanmtfifd gvdyystngq miyningsvi mrgqntidqr
      241 gtstysqewa einyveiqrg htsikhssnq tsafiwstsn ssanpyagks qiivrenaql
      301 diqtnsnmty gtlspnyive knavfnldkv tlatggarnq ffasaqtqpv tfdfqenaqv
      361 dfklpspinl ytakggmtva enadvsldvv sgtifstass stfalnmnka kkvslagtsl
      421 gtlglngang vknlsftsnf lqkietfssk tsstptqeif kkasdlsvqg tnftniqgss
      481 npfsaseila lknaqkmvfs efvdvpdqlg lfaydasdts islhgssvnn gsqatevkff
      541 ifsaeeeand lrnarqivtl rsfddqenta lnsyynvtvd glnpntvywv qmivvnrage
      601 sefsdtelfa tkpqlstlta nvtnttaiin gelasdtgkw tdysngeaaa ipdqqayfgg
      661 myrkvtieys knkdfpenet kaqvadlsgn knqkfstklk glegevtyyv rvrvagvyge
      721 evvlamnplt efqtvteiin vevpiemafq tqnkdlgtln egnvssaeyp vinkgntptk
      781 isitnltken taanqlllld slsgnpgkde lalqmlvnnk qeaplfltse lsknplsigv
      841 lnvneekkls lqgkyfnptk qavfpnykvt fkveknee
//
LOCUS       WP_010762566             446 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus haemoperoxidus].
ACCESSION   WP_010762566
VERSION     WP_010762566.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 446)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..446
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50331
     Region          160..425
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mfvfkhafln lrrhiwnyll vgvmlfllif gtmvtntiyt saklftknys kqfktivtil
       61 epdlsnlthe kkltkeqyik fgeskyvngm kmigttpisf dtlkaipssf pfqnvkgies
      121 eehydqatan wigaesadlv keltesgmei sagsnvlkhn eclvnsefaq lnqlkigdsi
      181 qvfltgnekt ekqtlviagm yqpnkqvqas gtsqltrakg ndiftnwetl damkefdysg
      241 ynsvsyelkn admldeflke mkanglpsey qvmtneanmk lflspinglg tlagtillgf
      301 lifgnfglal fsirkfkqrq teiyvfrsig itnqqiiksr aielvivtcv sfslafvavk
      361 efvqpiadwq lgnqrrltgn idqlfslvas ekkesitsip mvidansfit ifgitslfli
      421 timsidcykv fkfesiefll erklde
//
LOCUS       WP_010762606             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010762606
VERSION     WP_010762606.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 222)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..222
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23954
     Region          9..217
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mqnlqdmnll qqfiyyfeqn gsyvlsqfvr hflisiygvl faaivgipig ifiarrrkma
       61 gwvvsianli qtvpslamls ilmlglglgv ntvivtvfly sllpiiknty tgmiqvdrni
      121 ldvgkgmgmt kwqrlymvel plsvsvimag irnalvvaig itaigafvga gglgdiiirg
      181 tnatdgtaii lvgalptalm aiitdwvlgm ierrldpask hs
//
LOCUS       WP_010762626             878 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus haemoperoxidus].
ACCESSION   WP_010762626
VERSION     WP_010762626.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 878)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 878)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 878)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 878)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..878
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..878
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95403
     Region          2..869
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 meaykkpiet iikevntnke qglteqevkk rlaehgantf qeakkdsivk kflhslsdft
       61 tiillvaaai sfytaiatdh gdyfegilii aivvinavla ivqegnaeks laalqdmnkq
      121 sssvlrdgkv etidaenvvv gdilvlesgs mitadarliq asqlrveesa ltgesepvek
      181 dseyigedds sigdqinmvf kgctvsngrg raivtatgmq temgkiagll nddvtqqtpl
      241 qkrlnqlgkr islialgaaa lvfiigelqg epmlemfmta vslavaavpe tlmvivtltl
      301 aygvqkmakk haiirrlpav etlgtanvic sdktgtltqn kmrvrrvwsr gdevtdteda
      361 mtdeamevlk maslctdviv dkdgddlviq gnpteaaivr aveenyhtka eleekyprig
      421 eipfdserkm mttvhkmgkk yisvtkgafd vlltrfrfgd veqaavvndr fgkralrvia
      481 vgyaiydeep teitsealek nlrllgligm idpprpeskg aiarakkagi ktvmitgdhv
      541 vtagaiakel giltdkseal tgselqkmsd eeldsrvksl svyarvtped kirivkswqr
      601 tgavvamtgd gvndapalka sdvgcamgit gtdvaqgaad miltddnfat ivdavaqgra
      661 vyrnirkavn fllscnisei fivliamllg wgapftavql lfvnvvadgl pgfalgkepa
      721 ekgimdeapi prdegifarg lwqkiginaf vftvitlfgf ylganvdsvs yffeasheig
      781 qtvaflilay ssilhvfnvr stesifrvkl stnkslfema vlaviittvi allpftqelf
      841 glvpiginhw llvmglsiip ifvnemikfh yspeedte
//
LOCUS       WP_010762754             683 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010762754
VERSION     WP_010762754.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..683
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=78795
     Region          19..665
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 midyrmsyli dishsvgrsi qelseitglp tetvidqlgk ideqlqkfsy epiywekdkl
       61 yfpkqvadkw lelhfgklei eifyseyerq allylltfta dedlsvfhyq effqvsknti
      121 ladikklrkh laiqqisldy srkngfylsg neeqiriqah qmiakvvtsv sgkwglkkgl
      181 vkytrtfead vrtylfdtik aselvivpsr ieetiyfmay vlrrakshsi kldrqakerl
      241 kelnafhgsq lflakfsnil dseseefyft vifmtitqge irdtalefll ecgsqiihem
      301 erlaviefka yrkllldlfy hlvpaffrik yhfsltnvli eeikeqygel faltkialhp
      361 lerltgqaip deevgyftil fggeignqre lnrvirykal vlcpsgisss limqselkel
      421 fptidfsltt tvdqlesiae seydvifssv pldtpkktyl inpimtqlek nnlirhvqee
      481 llipgivvps ideiietllp yielkkgvtk ekiyrilnrk mikklkvked ekpmlsellt
      541 temiqltdkk ltweeaiaya aqplkeqgki tenyieamik kvndygafih igkgialpha
      601 rpedgvkqlg msllkveepv lllddpkhei tificlaavd nemhlkalas ltkilsnken
      661 lerllvakdq atiiqllkeg esl
//
LOCUS       WP_010762982             356 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010762982
VERSION     WP_010762982.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..356
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39961
     Region          1..342
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mielkninvt ffqkkqqida vknvsltiek edvfgivgys gagkstlvrv inllqrpssg
       61 eviinnknil sfspkelraq rknigmifqh fnlmkertif anvdfslkys glskeqrkek
      121 ierllelvgl sekkdaypsq lsggqkqrva iaralandpe illcdeatsa ldpkttiqil
      181 dllkklnkel gltivlithe mqvvkeicnk vavmedgqvi eendivsifs qpkealtkdf
      241 irtathidqa letiiqhpsl tnlsgnevlv efsyvgeqts epliaqlysk yhvvtnilyg
      301 nveilqqvpi gnlivilsge ehqrekaldf lqkqgvkikv lkkkepeeni iplhvi
//
LOCUS       WP_010763156             944 aa            linear   BCT 01-JAN-2025
DEFINITION  leucine-rich repeat domain-containing protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010763156
VERSION     WP_010763156.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 944)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 944)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 944)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..944
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..944
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=106491
     Region          <563..>658
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          573..596
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          597..620
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          621..644
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 mlrkkigyii fffllvsslf slpkicsaad fidvsgwshf gylsneyiln dqgiasnltt
       61 geqiditsnv inlnyfgqni qddvrlqnnv lkldtyyrvy kdqelrvkni giykgkalem
      121 ritflhddgv kigsigksdc lvnfidlnds kgtfapdisy ylvdqesgel indnvnvmvp
      181 vsskiayyey paalviqkdi glvvtdtgle knafrsrfng aytnialggv tgggggkrld
      241 vsmlhplnkk geigiyirpd fyssdfslfn yapriispqq ynkmsvtsid nelgnlnyii
      301 eqelpkqgfp vyypekleld ysketsnlkl sqptifsenk viaaseydfs nnkvtlpnsf
      361 lkkyagqkiq ikfssdidys dkktlsyydk dkqnfkfplg lkstsvknsv skteievtnn
      421 gvvkfplvlk adgrnktvdi esstdnynek dfitnvstnf pndtvittfk nkvefntvgn
      481 ltipitlese llgikneimv qvnviarpvt saffenqawl ideinrqfss kgkkidenly
      541 mpdlleitsi tnrtgadfld qyipkniaal enlevidlkd khlsgylpde lgnltklkkl
      601 sifgnsikge ipktlsklen leflalddnk ltgtippgle nistlrqvyl nknnlvgivp
      661 tfslgpfsnf hiwetqltyn ddkrpsfink vtqfkqsfvv gtdslsltgn iniaittkgt
      721 sikpfdpsdr gflnlhaqkn nktrvelysg htfkiinkks kqvlyngpan ksleikvdpa
      781 eiyqvimdga dknpnnitef ettlreykfs evpkslsldl klgdleyqpv kisskdnlil
      841 fdnrlnsqwq lriktselks ktrtmagsyf ykskdevpve ipvsdtfkti ekgnsepdmn
      901 tinlskewnd rrglfykqan tgnykdsysg kidwqlidvp mggk
//
LOCUS       WP_010763061             449 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus haemoperoxidus].
ACCESSION   WP_010763061
VERSION     WP_010763061.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..449
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=49490
     Region          1..442
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 metlekflnk figpiaqkmn gskffsalae afmrttpitl gvallmiign fpipqwiefl
       61 aktgmtahfn aalgatinll svyvtfnfay iyskkeghdp lpagllaigs ffilmpqmiq
      121 tytleqavtk fpaqtvvtas nnveafasqy tggtglfvai ivgyftavly gflirknlti
      181 kmpdtvpsnv seslspails gvilafffii rilfsftpfd nifafittli qaplqsltgs
      241 piaiiliftl anmlwffgih pnmvygvvmp vmtanmlanm tayqqhqelp ylamavvsyv
      301 cgnsfggqgs tyglvismft akserykslf klagppvifn vneplifgmp lmlnpfffvp
      361 mvaspllmgg iawgmlsild fskynplial pwttpapiam alkggfnyll ifivllivnv
      421 lvwypffkma dkkeylleqe nsktslkhn
//
LOCUS       WP_010763185             426 aa            linear   BCT 01-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010763185
VERSION     WP_010763185.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..426
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=45931
     Region          1..425
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mtnsnyqfet iqihgghtpd kdtnsravpi yqttsytfdd tqdaaekfal skagniytri
       61 tnpttavled rlneleggvg avavssgtaa vtyaiqnlas agdhivsast lyggtfnlfa
      121 htlpefgitt tfvdpdrltn feeaikentk aifvetignp itnvadleai aeishkhelp
      181 livdntfata ylnrpfdfga divvysatkf igghgvalgg viidsgkfnw angkfpklvd
      241 pdpsyhglsy tkdvgaaayi trlrvsllrd tgaaispfns fllilgletl slrlerhven
      301 alavaeflnk hpkvewvnyp glpdnkyyev akkylpkgag svftfgvkgg aeagqnlinh
      361 valfsllanv gdaksliihp astthsqlse eelkasgtsp elirlsigie niediirdle
      421 qaldkl
//
LOCUS       WP_010763176             344 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010763176
VERSION     WP_010763176.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..344
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38740
     Region          1..250
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtainfavig yggmgsyhvh nimpneneri hvvgtydisg erqkissqyn hkiyntledv
       61 ltdetieall iatpndshke laiqalqagk hvvcekpvam nveeldailk vaketgkifm
      121 vhqnrrwdpd flitrelykn hqigelfqie trvqgangip gdwrhelkhg ggmlldwgvh
      181 lldqllflvd sriekvsadl syilgdevdd gfityiifen gvraivevgt tnytklprwy
      241 lkgtkgtaii ydwdltgemv iesgkqniqa prpvqagvgl tktmappsee atetknlpqg
      301 saeydpfykn fynvvreqae pvvkneevrq vmvlieeifk aakr
//
LOCUS       WP_010763147             439 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus haemoperoxidus].
ACCESSION   WP_010763147
VERSION     WP_010763147.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 439)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..439
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51365
     Region          82..408
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 mldrpffisl lslnfiqllw lfaykkilsf retmilsail tvqfivgaft ddhfitllli
       61 pffllqfffq vrkvqnwvvp alflsfenai vllswlltld iwdilfinhl idaetysiyl
      121 klfiflqqfv fyllllfany lnkrfnittt ihllpkkyrl lsvllliflf vtitlqqfsv
      181 segysdsffy stfiiicfta flswnilliv krqneqqyin ilnkkyeqer ekinrsnefr
      241 hdykqlligl tsylelndtq qalhllhtii dysnslltpn lyktisvihn ppiqglltsf
      301 lkscsdkdiq lkititeklt didmnivdfi rcfsilldna yeavqetelk mieiaitgdq
      361 nfvkvvvknt ytadkdislq sllqnnfstk ekhqgkglyi laklidnykk asyqiakkds
      421 ffivsfsvpk lsepllisk
//
LOCUS       WP_010763233             361 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus haemoperoxidus].
ACCESSION   WP_010763233
VERSION     WP_010763233.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..361
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41206
     Region          1..344
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkkniitfdn vvkqyddekv lknvsfeieq gkfytllgps gcgkttilri lagfvdateg
       61 diyfdgqrin dipankrqvn tvfqdyalfp hmnvfdnvaf glkikkiqkk eiekkvkdal
      121 rmvqlpgyet reisemsggq rqrvaiarai vnepkvllld eplsaldlkl rtdmqyelre
      181 lqqrlgitfi fvthdqeeal amsdeifvmn kghivqsgtp vdiydepinh fvadfvgesn
      241 ivngtmiedn lvefvgkrfe cvdggmrqae pveimlrped ltittadkgk lvvtvdtqlf
      301 rgvhyeiich dedhnewmvh strkategak vglffepedi hvmrfnesee dfdarlesye
      361 e
//
LOCUS       WP_010763362             345 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010763362
VERSION     WP_010763362.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..345
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38082
     Region          4..341
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mplielqhvq kqfsgksgqv tavndvsltv dqgdiygivg ysgagkstlv rllnglelpt
       61 qgevviqgqn vaqmanrelr qfrkkigmif qhfnllwsrt ilenimlple lanvpknvrk
      121 eraqellnlv glqgrgdayp sqlsggqkqr vgiaralann peillcdeat saldpqttde
      181 vldllleink tlnltivlit hemhvirkic nkvavmelgq iveegdvlev frhpkqavtk
      241 rfvqqelepk edteellqel ikenpaglva tlqfsgdnan epvisqairk favdinvvqg
      301 qvqqakegaf gtltvmitgt pneieqalaf ftekevvmev ihrge
//
LOCUS       WP_010763390             222 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010763390
VERSION     WP_010763390.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24757
     Region          7..>91
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 makkytaeea kslildvstq lfiekgyekt sisdivkgld gltkgavyhh faskdeiida
       61 vvrrfipnea altaimekdk lnglekiqal lfegmfnsea sqsrilsftl ldnpkffsmy
      121 irttneimap lvetcliegn sdgsvtveqp kqmaelaili lstwfiqalf pntvetffek
      181 lmaaktmlen tgmpiisnaf lekldqqimi kaaelndqkt en
//
LOCUS       WP_010763442             306 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidase U32 family protein [Enterococcus moraviensis].
ACCESSION   WP_010763442
VERSION     WP_010763442.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..306
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=34574
     Region          1..298
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
ORIGIN      
        1 mieliataes ieqaeallav gidtlyigee mfglrlptsf sreeqqrite mahtvgkrvt
       61 valngimhpe kmkkvpeyla flqeikvdqv tvgdpgvvfv mqrdgidipy iydgetlvts
      121 srqinfwakr gsigavlare vpfeemkamk dnlmvpaevl vygatcihqs krpllqnyyn
      181 ftkndesaak erglfisepk keethysiye dshgthifad ndvnligele klheqnytkw
      241 kldgiyapge nfvkvaklfv eakekieagt wtsdqaqksi eqietlhpen rgldigffdl
      301 dpdeik
//
LOCUS       WP_010763441             829 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Enterococcus
            moraviensis].
ACCESSION   WP_010763441
VERSION     WP_010763441.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..829
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92446
     Region          1..814
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mdelftesak avlaiaqeea kyfrhqsvgs ehlllalvle pngiagkslr qlnadkndir
       61 eeiehltgyg tvkeypkgay lpysprakqi fayagdeakr lgapnigteh illgllrded
      121 ilasrillnl glslskmrql lmkkigitdp qmsgnvgrrr nnqaqkaapk gtptldslar
      181 dltklarend ldpvvgrsqe vrrliqilsr rtknnpvlvg epgvgktaia eglaqkiing
      241 evpedmlekr lmmldmgalv agtkyrgefe drlkkvidei yqdgqvilfi delhtligag
      301 gaegaidasn ilkpalarge lqtigattld eyqkyiekds alerrfarvq vdeptpeeae
      361 eilkglrsry eehhgveitd dalhaavqls vryinsrqlp dkaidlmdes sakvrldlad
      421 epseinnlrl eiarlvqeke eaiqsqsfes aarlrqkekr larklenill leqkeasgya
      481 nrvteqdvan vvsqwtgvpl qqlekkeser llelesilhh rvvgqneavq avsrairrar
      541 sglkdpdrpi gsfmflgptg vgktelakal aetmfgseda lvrvdmsefm ekystsrlig
      601 sppgyvgyee ggqltekirq kpysvillde vekahpdvfn illqvlddgh ltdskgrkvd
      661 frntilimts nigatairee knvgfnvkdi tkdydamqkr imeelkkafr peflnrvdet
      721 vvfrsldqee iheivkimsk sivkrlkeqd vnvkitaaai evigkvgfdp eygarpirra
      781 lqkevedrls eallsgqihl gdkvtigask gkitlnvksp kpeqvlqti
//
LOCUS       WP_010763447             140 aa            linear   BCT 01-JAN-2025
DEFINITION  NusG domain II-containing protein [Enterococcus moraviensis].
ACCESSION   WP_010763447
VERSION     WP_010763447.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009210
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..140
                     /product="NusG domain II-containing protein"
                     /calculated_mol_wt=15543
     Region          11..140
                     /region_name="COG5341"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444125"
ORIGIN      
        1 mdfkefiqks yirpwdivii llltissflp lvvfgiqnta qddatkqavl kvdgevikvf
       61 dlkedgptyt ykyedadgdy nlievsgdri rmvesncgdq vcvqrgwisk agetpiaclp
      121 hnlfitveas dgsedgsliy
//
LOCUS       WP_010763450             359 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Enterococcus moraviensis].
ACCESSION   WP_010763450
VERSION     WP_010763450.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..359
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=39743
     Region          45..338
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mknkksliiv iaalflvila gcntkdktee akinkepysd qqsllgtyvq vriyddgked
       61 vlekafarvk elgdkitvne kgseidkine qagikpvkvs ddiypllkra yeysedssgg
      121 fdmaigpitq lwhigfddar kpsqeeidqa lklvdyhkvk lndeektvyl eekgmqldlg
      181 aiakgfitde vvkvlkdngv ttaivdlggn vfvlghsprg kdmdwnvgiq dpnkarntvi
      241 gtiqesnktl vtsgiyerfl evdgekyhhl fdpktgypfd ndiagvtvit nesidgdgls
      301 tavfamgvkk gleyaeglkn vdvifvtked evfvskdiek vfelgkdsgy tmgdrkdlk
//
LOCUS       WP_010763498             207 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Enterococcus moraviensis].
ACCESSION   WP_010763498
VERSION     WP_010763498.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..207
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=22222
     Region          2..205
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mkvailgang kagseilkva kkrgldvtai vrdaakitdg tpvierdvya lttedvkdfd
       61 vlvsalgfwg dvseftgstq hlidiltnqk trlfvvggag slfvnpehtv rlsetpdfpe
      121 afkplatamg kgldlleask glnwtyispa aefdaegpat gkyviageel evdkdgksyi
      181 syadyasamv deieknthpn qrfsvhq
//
LOCUS       WP_010763534             225 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            moraviensis].
ACCESSION   WP_010763534
VERSION     WP_010763534.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..225
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24807
     Region          <147..213
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mqelfdrkvk lvpaivslvl lggafyslln tafilnfcii lvagligmyl mygvegikkl
       61 ysplkkgsvk iiliayvlsw vtallakfla evigqptadn pivnqfgqgl lpaltllvkt
      121 lfmlageeii ttiplillvh valrykverk taiigsvilt slmfgslhlt tydwnwfqcl
      181 vvigltripf twatlktnsi wagtiihiaf dwlifigvml stlah
//
LOCUS       WP_010763583             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010763583
VERSION     WP_010763583.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..255
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29106
     Region          1..247
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mvftsdiykd ihlnyerlsd terkvvdfil ksddvdklkl kdikdvlyvs natiirackk
       61 lnhptfnslk safvksekek styplevdfs yildgikket latlelidek nvdqicncli
      121 earrifcvgl dgssqvasef nrklksmdiw tnnysdqslv dcipyistdq dvviifslsg
      181 qiddinenml kvkrkgttii avtnvtankl klisthvlvt yndpddrrtl ysrlmlhals
      241 tviyeklrtk vpsfe
//
LOCUS       WP_010763536             191 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010763536
VERSION     WP_010763536.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22291
     Region          1..>87
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          74..175
                     /region_name="TetR_C_8"
                     /note="Transcriptional regulator C-terminal region;
                     pfam14278"
                     /db_xref="CDD:464123"
ORIGIN      
        1 msesqitkka isaalielcd rklfskisvq ditkevglnr qtfyyhftdk qdllrwiyth
       61 daliyldspd vsidnweeqa lkmlkaiqsk ndfyyntvss dsdilrtcfs titnklfinl
      121 fdqmdkenql lpedkvfyar ffsygcsgvl idwilggyke spleiatqlf rlakdteffs
      181 yrlyaqenel l
//
LOCUS       WP_010763609             295 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus moraviensis].
ACCESSION   WP_010763609
VERSION     WP_010763609.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..295
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33049
     Region          4..230
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnaielkglt klykkqpaid qvelsvekge iygfigpnga gksttiktml nfiypdhgta
       61 tllgldsike akeirkrtgy vssdvrfypn mttlevlkyv aafhqvkesk kqidyfielf
      121 didakkkmse lslgnkkkia itagilpnpe llildeptng ldplmqhrlf eelekynqqg
      181 mtiflsshdl nevqqhahra afiregeiit vqditkeksl gkvitligdh iplslfekmg
      241 aailkhqgne trllfegdlr eilplladas iqdftvtnpe ledqfmalye ggtvk
//
LOCUS       WP_010763597             759 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus moraviensis].
ACCESSION   WP_010763597
VERSION     WP_010763597.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 759)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 759)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 759)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..759
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87573
     Region          1..752
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mnhlfeidpw kiathqlerg errlqeslts mgngymgmrg nfeeqytgdh hrgtylagvw
       61 ypdktrvgww kngypdyfgk vinavnfiam difvngeaid lgmqepkdfy leldmrngll
      121 trtfvvnvde tsvkfrferf lsivqqelav irvtaevleg tadiqiiski dgdvrnedsn
      181 ydemfweaqq sgfeeaigfl ttktipnpfg ieqfsvtaam khltnaqvgv aeteplkvqq
      241 sfqatlqane sitlekqaiv ltsrdipeke qqekavqllk ettktfdall neqneawakr
      301 waladvvieg ddaaqqgirf nlfqlfttyy gederlnigp kgftgekygg atywdteaya
      361 vplylalakp evtknllkyr ynqleqakhn arqqglvgal ypmvtftgie chneweitfe
      421 eihrngaiay aiynyvnytg dneylknegl qvlteiarfw adrvhfskrt gkymihgvtg
      481 pneyenninn nwytntiaaw vlqytlenyt kyqaetpvei teeeqkqwqe ivenmyypfd
      541 eelgvfvqhd tfldkdlmpr taltpadlpl nqhwswdril rscfikqadv lqgiyffger
      601 fsraekernf lfyepmtvhe sslspsvhai laaelgmeek avemyqrtar ldldnynndt
      661 edglhitsmt gswlaivqgf aqmktadekl sfapflpstw tsyafhvnyr drllyvtvdk
      721 envrlqlvsg kelpltlydn kvvladelvi emkkvnehv
//
LOCUS       WP_010763614             505 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease/substrate-binding protein
            [Enterococcus].
ACCESSION   WP_010763614
VERSION     WP_010763614.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..505
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56148
     Region          <45..208
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          235..498
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(241,243,291..292,295,338,340,418,442)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mgklietfia rkedfiqavv ehiqlsllsl liailiaipl ailltnykkv aefvlqitgi
       61 fqtipslall gllipvigig sppaivalvi yalfpilqnt ytglteidps leeaaeafgm
      121 nkreklikfe lqlalpyiis girtatvmii gtatlaalig agglgtfill gidrnnvyli
      181 ligaissavl avlfnfgihl lekatvkriv aafmvllall vgsfvythqe aeqkeitvag
      241 klgaepdili nmykeliean sdihvnlksn fgktsflfna lksgeidvyp eftgtvletf
      301 lkdnkntsnd prevyeyard qikkqenmdy lepmryqnty avavkrsfae englktiedl
      361 kkvesqlkag ftlefidred gykglqklyn lnldvksmep slryqainng dvnvvdayst
      421 dselkqydlv ilkdnkqlfp pyqgapllka etlekypelk ellqplvgki teeemsemny
      481 qvnveqkdpa tvahdylveh gmlek
//
LOCUS       WP_010763627             381 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Enterococcus moraviensis].
ACCESSION   WP_010763627
VERSION     WP_010763627.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..381
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=42639
     Region          108..374
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mnkfafliig slfllsnyyi gkkflsilaq fsffkyplil wliigvlalt smltlllfda
       61 nvggligkig sywlsfwfls fvifglsdlv ltiakkiitv qakselivwl vstvlivvlf
      121 cygswqaqqi ktisyqvtid ksasnrpktv kavlisdlhl gyvndakkle kivtkinqlh
      181 pdivfisgdl fdgnykalqd tqqmekqfkr lsstygtylc wgnhdagetf ekmkalvkas
      241 nitlledemt vvgeellvvg rkdsspigsq dgsrksiqeq fnkvgnklpk iildhqpsni
      301 deykhaneli lsghthqgqi fpfnlvtkay ftvdygyyrk nenspqvivs sgvgtwgppm
      361 rigtqseivq iditvngdha k
//
LOCUS       WP_010763671             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010763671
VERSION     WP_010763671.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..251
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28869
     Region          1..245
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 maifdylkln dlssveqeiy rfvvnnldki pymrvrdiad gahvsstsvf rfvqkigfhs
       61 fpefrfyiks hldnvrqaen kkhigieerv nslnmeifhp dveyqikkma qelrdsdlil
      121 fmgmgasgai aqyiarklas lgylsisldd ltypirsflr kdqknvivfl svsgetkelv
      181 eviaglqdkn svkkycitln kkstlaqlcd ysieyeikee rkdifldlts qlpaiailet
      241 lisylkdfrn d
//
LOCUS       WP_010763705             783 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus moraviensis].
ACCESSION   WP_010763705
VERSION     WP_010763705.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..783
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91448
     Region          1..585
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 melrsfqkki ideielylkd ttihvvappg agktvlgvei ikkldkqtli lvpslvlknq
       61 wlnylrdnfg vehvsqrlsd hkkitittyq efhlqgesik rasyafiild eahhlkrtwa
      121 eeiisfreen qaiqslslta tppydattie wkrylalnga ididipapel ikedvlvpyq
      181 dyvylipesq eneeaffdfl qqqneivyam mndaevteyl lglafiqypl enesfiyenf
      241 dtylsvllyl ydqdfelsne hwevlgikny krkvrlpqqt keniktlyrf lyelnpnlsi
      301 feyltqnkwl fqnklslfpa ykdnkkyrsi plkkesiaki likeeaflge nlcsvvfmdr
      361 ikietlfgqe sylefgvapl flylkelinp ttnlavicgk fcllsnsval klfpelhfse
      421 lemdpnysfi sltdenrnqi ltgvtqalnq kkinlligtv sflgegwdcp alntvilant
      481 sgsyvqtqql rgrglrkspe ksfvniwhia tvyktialee qlefqyiakr lsfiegfnkl
      541 esvakistgi erfelplkit eesinsynan nfflaqrrda lkedwhkais kgthqsmpli
      601 mkplknkeyr indlkenhsp vkknfydsif nslffrnfri rrswkkyctq lerlingvfl
      661 llmedgvisk esrlriqked tlfsckldna sfnantlfnq yvlevmedid kpryllklnr
      721 iyfsvpsyfs knkkdvlrlv dslnglskkq siyytknsqg rkalieayiq qnsrevieek
      781 iwd
//
LOCUS       WP_010763727             437 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Enterococcus moraviensis].
ACCESSION   WP_010763727
VERSION     WP_010763727.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..437
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45941
     Region          1..434
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mkekiisyfe idqlnttvkr eflagfttfi smayilfvnp tvlgasgmde gavftatala
       61 salgcilmgi fakypiatap alginaffay svcvgmgipw etalagvfva slifilitvf
      121 klreliidai padlkfaisg giglfiaflg lseggiivsn estlvalgpl nvgttwltif
      181 gliitaimmv rrvpggifig mtattilglv tglidmptki vsaapslkpt flvalkhvgd
      241 inslqlwvvv ltfllvtffd tagtlvglan qagfmkdnkm prvgkalaad stamlagsll
      301 gtspvgayve ssagiavggr sgltavttgl ffvvglffsp llsvvtsqvt apalivvgvl
      361 maqslsqikw kemeiaipsf lillgmplty sisdgialgf ifypitmiaa krgkevspim
      421 yalffvfvgf mwilnan
//
LOCUS       WP_010763751             270 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010763751
VERSION     WP_010763751.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..270
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31152
     Region          1..68
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mtvemgkqlk kfrqeqgvsq qeladylsis rqtiskwelg kslpdvenii rlcdyfnisa
       61 dvligrkkps ffenlfrgke rrqmpmdqek ekknnavfys ayapdiepli lagqrvntfv
      121 kieenilpha tfsklmgyan clcnfngekv sidqigkfew vvntpiekpi vefslqdvle
      181 iklqfgkyfr nvggnfvtli divtkdqtys fwveslkiay viwhhekfkn vklnvdktfq
      241 kalnlsneee avaairndak niplfysnsk
//
LOCUS       WP_010763771             346 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus moraviensis].
ACCESSION   WP_010763771
VERSION     WP_010763771.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..346
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38604
     Region          1..346
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtfvdlkeir vsydgkqdil kdlsismekg elvsllgpsg cgktttlrvi aglikpndgt
       61 feldkddltk vpvhkrnfgm vfqsyalfph ltiaenvafg lklrkeskat tkekvekmle
      121 vcglenlgdr ypkqlsggqr qrvalarali iepkllllde plsnldaklr vamrieikri
      181 qqqlgittvf vthdqeecfs isdkvaimnn gvieqydspe kiyrlpktkf vaqfigfenf
      241 fevtktegnq yqsqsgqlft ttnpqpsvtg tvatirpedi eitkevtqet vegtvvvrtf
      301 lgksyqyevt tplgellvng tseqtyetgd kinlafpadk lvvlek
//
LOCUS       WP_010763844             105 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Enterococcus
            moraviensis].
ACCESSION   WP_010763844
VERSION     WP_010763844.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..105
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11719
     Region          1..95
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mkrvsvkelk klieltvnep vsiidvrevd efaaghivta knyplstlpe amaeidhdqp
       61 hyvicqhgvr sehacsflen ygynvvsvse gmsvwdgenk vtsyr
//
LOCUS       WP_010763847             211 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Enterococcus
            moraviensis].
ACCESSION   WP_010763847
VERSION     WP_010763847.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..211
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22889
     Region          1..202
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mlliknltks fdgrriidql nleikdgeil tivgpsgggk ttllrclagl etidsgeltm
       61 dgvpfnpvem dnadqvvgiv fqdfqlfphl svldnitlap ilslkqtkea seaeaidllt
      121 kfglsgkesl ypyqlsggqk qrvalarala mkpkvlgyde ptsaldpelr qqveeviltl
      181 kaqgmtqivv thdmnfaeni adnlltvtpv q
//
LOCUS       WP_010763889             126 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system PemK/MazF family toxin
            [Enterococcus].
ACCESSION   WP_010763889
VERSION     WP_010763889.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..126
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=13673
     Region          1..112
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mvkrgdiyfa dlspvvgseq ggvrpvlviq nnlgnhfspt iivaaitakm akpklpthig
       61 inseetgier dsvilleqir tidkirlkek vchlgieimd svdralgvsv gileaeleee
      121 nlgtyr
//
LOCUS       WP_010763892             131 aa            linear   BCT 01-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Enterococcus
            moraviensis].
ACCESSION   WP_010763892
VERSION     WP_010763892.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..131
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=13782
     Region          <53..130
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
ORIGIN      
        1 mkkqsnktyt illifsailf staiyfmsss lilgasaggs vsapvtties edvvpettps
       61 aavaepkeat tatsavvenn vreapkevyv vkegqtlwei aqdsglsiqt lmnqnqlsss
      121 vivegqelvi d
//
LOCUS       WP_010763863             449 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus moraviensis].
ACCESSION   WP_010763863
VERSION     WP_010763863.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 449)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..449
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50971
     Region          162..439
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mfvfkhafln lkrhtwryll vgiilfllil gtvvtstvyt sakvfaknys kqfmtlvtil
       61 epdlsslthe kkltkeqylk fgeskyvngt rmaanfpvsf dtlktnsess plqvqkmdgd
      121 evkenyypsi aswfgvdtqe lkteflqgdm eistgranlk mneclisael aklnqlkigd
      181 siqvtvignq vpekkvlvia giyqpkeqta skevnelmri qenniytnle tvqatksfee
      241 ygynnvayel knrsdfdafl kelqkkglpd eyhvmtnean mdmllspvng vgtlsgtill
      301 sflifgnfsl alfsirkfkq eqtdiyvlrn igitksqliq srlielgvst iisfslafmt
      361 arlvtqpiad wqlknqkqmm gnvaqlfsvm dngkvesitt ipmmltnysf vfmigitslf
      421 lmtiisieay kifkfepief llernides
//
LOCUS       WP_010763922             432 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Enterococcus moraviensis].
ACCESSION   WP_010763922
VERSION     WP_010763922.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..432
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48679
     Region          1..432
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mlainffilf lmiaitaffv asefalvkir msrleqlkke nvknaelaih vthhldayls
       61 asqlgitltg liigwvgegs vaallhplig nlpisvalsr tisvilgfai vtyvdvvvge
      121 llpksysiaq tekvvlaivk plhyfykvmy pfiwllnhsa arlgkmlgik lvsegeetlt
      181 qeellyvavd sykkgeltke eyhymenvfe fddtlakeiq vdrtsmevfe adetveqaiq
      241 hslkrghtry pvieeskdnv lgyvtlpali kesfinnqkk vselveepiv alttipiksl
      301 ltmmrkegkh iailkdeygg ttgmvtiedi leelvgdird etdlenalia kdsentyivs
      361 gkitlddfer yfkvkipife tsemstlagl vmeqknnqia vgdqikidhf mfevmdyeha
      421 hidyfkvtkt te
//
LOCUS       WP_010763936             487 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein/permease [Enterococcus
            moraviensis].
ACCESSION   WP_010763936
VERSION     WP_010763936.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 487)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
REFERENCE   7  (residues 1 to 487)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11705690
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..487
                     /product="ABC transporter substrate-binding
                     protein/permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52706
     Region          41..265
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Region          275..487
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mklckktlal iipvllvllt flpvttafad ekdpvydsim krgelivgls adyapyefha
       61 dvdgkdqvvg fdisiaqkia ddlgvklkie elgfdallga lktgkidlii sgmaptperl
      121 qevnfstpym tvqqkvvvrk ddtdkfqstk dfdgvkvgvq kqttqeelak telvgsipts
      181 lqkvpdiimn lknkkvdaav legpvaeayv drdkelafad vtfeqgekda avaipknasv
      241 leqkvnasik tindnnlleg ykkeagklmf tddesflgky gkfyisgagy tiflafmgvl
      301 fgailgglla lmklskskil rgiaicyiey vrgtpllvqi fivyfgtgvl gldlskiaag
      361 cialalnsga yvaeivragi navnkgqlea arslgmnqpq amrfiilpqa iknilpalgn
      421 efvtvikess vvsvigvsel ifqagnvqga sfkpflpylv vsliyfvltf tisrllgvae
      481 rrmstsd
//
LOCUS       WP_010763984             256 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Enterococcus moraviensis].
ACCESSION   WP_010763984
VERSION     WP_010763984.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..256
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29285
     Region          2..254
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mifdshthln aeqfnedipe tierakelgv temavvgfdt ptiekslels qqykeiqsii
       61 gwhpteagsy tpeiekklqq llttpkvval geigldyywm edpkevqdrv frrqiaiake
      121 mklpisihtr damedtykil keedirdigg imhsfsgdpe wmerfldmgm hislsgvvsf
      181 kkalevqeva kvvpldcllv etdapylapv pyrgkrnepg ytryvvekia elrdmpfeei
      241 atqttnnahr lfrlak
//
LOCUS       WP_010764042             349 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Enterococcus moraviensis].
ACCESSION   WP_010764042
VERSION     WP_010764042.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..349
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=39956
     Region          99..325
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mwkiskkkdd pegqggqqhe dtehlveqdl tpwqkenley mktkgnqpvw npsivseene
       61 epegeaaevd eadseeplld dseeekqkkt yesfadrlpk ikkvrnkllf rrltlivsvf
      121 liallivlyf vsplsklgsi svsgnksvds qkiieqskle kgeslweqfg drtiyeekie
      181 rqlprvkqat islnglnsfk ikieeykvva lesvnkvyhp ilengkilpe emkapvsgmp
      241 iflnfkdqsi iknlmnsynk lpenlkqnis eirytpsaan kelvnlhmkd tnevivnisq
      301 laekmayyek vasqmekpgi idmevgifsy pfnneedees ieessqlve
//
LOCUS       WP_010764063             266 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus moraviensis].
ACCESSION   WP_010764063
VERSION     WP_010764063.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..266
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30487
     Region          2..105
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(3..5,19,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            40
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(51,54,58..59,68,81,85,88,92,95..96)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          125..260
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mlsigdfskv sqvsaktlry ydeinllkpt ftdaasgyry ydvgqletil likrlkeytf
       61 sldeikvile seqdqellqv ainkkkkeit qkmqnyslll eriaddlatl ergnklmsyl
      121 nsievkltev pemnilylrk qmnvneygky igelfgrlta ekftptgppl tiyhspdfnp
      181 ensdmelavp ivekneqtrv fptclcatsi ytgpytelas vyskmlkwie eqgykmngap
      241 feiyqtdpnt tdpdknivev yfpval
//
LOCUS       WP_010764079             426 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus moraviensis].
ACCESSION   WP_010764079
VERSION     WP_010764079.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..426
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47554
     Region          1..421
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtfiknlpea wqehwqasgf sepsmiqeks fqplkerenv lgisptgsgk tlayvlplll
       61 nvekdqgsql lilapsqela vqisqvvrdw asllqlktqs ligganvgrq ieklkkkpei
      121 lvgtpgrvle liktkkiksh llqtvimdev dqlfhekeln ltkqilasap tefqlvfysa
      181 tadrvaeeaq klteqltiid vtdedrssgv vnhyfmalsp rkksdylrsl aytsdframv
      241 ffnqvadlgs veekliyegv svvglasdqn ktlrklaidq fakkravmll ttdiaargld
      301 feaipfvvna evplseesyi hrsgrvgrmg aagsvitfvn datkrdyqrl mkkierpske
      361 iflydgaihl trkekgaade kninptatpk kekaekiapn kqaakpkkrp knnknkgarr
      421 kpskte
//
LOCUS       WP_010764078             333 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus moraviensis].
ACCESSION   WP_010764078
VERSION     WP_010764078.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..333
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37499
     Region          1..254
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mihlgiigtn wishqfvkaa letnrydlta vysrkletaq kfgeeygdve yatdlktffg
       61 iahmdtvyia spnslhfeqa kqgilagkni ivekpafstp eemaeiitla nqqkvfffea
      121 arniheksfk kigdllplkn qilganftym kyssrydqvl dgqepnifsp hfsggamadl
      181 gvylvyaavg wfgmpneshy farklptdvd gigtailryd lfdvtlqtgk nadsfldsei
      241 yfdggtlild svntiskaef hdrnhqerdi lditteenpm ieeardfadi lenpndltmg
      301 aryeewvels rnvnkvlttl rksagivfda dke
//
LOCUS       WP_010764087             484 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus moraviensis].
ACCESSION   WP_010764087
VERSION     WP_010764087.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..484
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=51781
     Region          1..479
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdgltawmek yilpvagkig aqkhlvalrd afigtmpatm agsiavmina mirdlpqqff
       61 sdyaanlaad kgifavinvi igingfvwng tlaiaglifa fswgynlara ykvndlaggi
      121 vglatliqgi afaysntlet avpkelmnti nensatsgws ataegltagg wgwlkldhln
      181 gnayftvmim gaisviifck lmlanitikm pdsvppavsk afaailpati alyviaiinf
      241 vvgkltngql iidlvqkyia epflglsqgl gavlivtifv qifwffgihg pnvlapvleg
      301 iwgqaqlini difqkgykgl tgtpavlkai ddgkaymwvr gsfdafawfg gsggtivlii
      361 aillfskrad yltvgklslg pgifninepi mfglpivlna imfvpflvap vvatsigwla
      421 tyfglvapvs qqvtwvvppi llsflatgad wrapivtivc mvvtfliwtp fviaanrmep
      481 tdfe
//
LOCUS       WP_010764100             304 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Enterococcus
            moraviensis].
ACCESSION   WP_010764100
VERSION     WP_010764100.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..304
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33940
     Region          1..278
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mklvdkvkkn eklmrfiett qhrmidseig ntsvvvayyl llslfpllia vgnllpylhi
       61 dpnevlpyia eaipkaifdd lkpaiqsllt qrsggllsis alaalwsasq sinalqtamn
      121 kafgveqrkn fiivrimslv villfmiaiv gvvgvlglgk tildllqpil hfstdfidtf
      181 qalkwpitsf vllvimcliy rvvpnakltf rsiipgaifa tvgwmllsqa fgiyikyfss
      241 kiasyqiigs fiilmlwlnf aatiiilggi inavvkeyis nekiqhrygl inrlidkvke
      301 krkk
//
LOCUS       WP_010764155             296 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Enterococcus moraviensis].
ACCESSION   WP_010764155
VERSION     WP_010764155.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..296
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32222
     Region          83..286
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkknkyivkl figfvtlsag ftlseytfat seetmaqeki iatssqklaq lketkqnisk
       61 qllenekqhs tvgvniqkiq idldqlekie stttisevae lkdeqaltlt tslspvevqe
      121 dtmtkktkql telkqkqnrl tlekqnistq qadmqkqetq lskkiaqaqk qkdeqskqtn
      181 thleivaaak thlgkpyvyg aagpdafdcs glvqvafasa grsigrttvd qetagetipv
      241 seaqagdlvf wgshggthhv aislgdgsyi hapvpgdvvq iatvasyspd fairil
//
LOCUS       WP_010764170             285 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Enterococcus moraviensis].
ACCESSION   WP_010764170
VERSION     WP_010764170.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 285)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..285
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30528
     Region          12..270
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mianfidglv ryqflqnali tsiivglvsg iigsfivlrg mslmgdaish avlpgvaasy
       61 mfgvnyifga sifgilaall igfitqksql kndtaigvvf ssffalgiim isfaksstdl
      121 yhilfgnvla vrdsdilitv vvgiivlifv glfykelqit sfdptmaqay glnvqffhya
      181 lmflltlvav sslqtvgtil viamlitpaa taylltnhlp tmiglaslfg ilssiiglff
      241 sysynlasga tivltaaaff ilaflfspkk glffvnkqkt eestl
//
LOCUS       WP_010764171             251 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Enterococcus
            moraviensis].
ACCESSION   WP_010764171
VERSION     WP_010764171.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..251
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27280
     Region          8..240
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 msinnnniti qqltvsyqgq kaladislnv pagkitgiig pngagkstfl kgmlgllkad
       61 srtvligeqp ldtqkkriay veqrsaldls fpinvlevvl lgtypklgvl krpkkqekeq
      121 alaalktvql etfakrqige lsggqlqrvf iarvlaqkad iivldepfvg idmtsekvim
      181 dilkqlkeag ktilivhhdl hkvahyfddv iilkkeliac gpvsttftnk niqlaygetm
      241 gdiiikgvad a
//
LOCUS       WP_010764194             791 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK [Enterococcus moraviensis].
ACCESSION   WP_010764194
VERSION     WP_010764194.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..791
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=87072
     Region          201..>261
                     /region_name="Remorin_C"
                     /note="Remorin, C-terminal region; pfam03763"
                     /db_xref="CDD:427493"
     Region          286..783
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 maqkrksakk kktkkqqqqq ehlnfiflgi ffiffglfgl lklgflgtli anglrvvign
       61 tfsiaavllm lyglslvifg kdfpikkvrp migvlfiylg illflhaymf rnvgtqtpdi
      121 mgttweflrm dlkastvtqn vgggmigagl ysltfflvaq lgsyliavll mvigvflism
      181 ldfqqvmngl qvvreklgsl takseerqtq reakraekra akeakieqma qerlrndvre
      241 ltpgeklaqe araqvekneq epeqltlvpi dsfqsqteaq tlqqkvvaet etedeggeld
      301 feiseeaedr dyelppstll dsipsadqsg eyqkieknig vleqtfksfg vdakvvkasl
      361 gpavtkfeiq pavgvkvskv vsltddiala laakdvrmea pipgksligi evpnstvstv
      421 sfrdiieaap shpdkllevp lgrdisgmvq sadlakmphl liagstgsgk svaingiiss
      481 ilmrakphev klmmidpkmv elnvyngiph lltpvvtnpr kaaqalqkvv qemefryekf
      541 aatgvrnisg ynelviqknl edgenrpilp fivvivdela dlmmvasnev edaiirlaqm
      601 araagihmil atqrpsvdvi tgiikanvps rmafavssgt dsrtiidsng aekllgrgdm
      661 lflpmgenkp irvqgafisd heverivsfv teqqeadyqe nmmpteeett gnsneasqde
      721 lyeeakalvv emqtasisll qrrfrigynr aarlvdelee hgvigpsegs kprkvflepi
      781 pddapidhgt e
//
LOCUS       WP_010764195             233 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus moraviensis].
ACCESSION   WP_010764195
VERSION     WP_010764195.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..233
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26388
     Region          7..231
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mrrksvlyld vaeqiksdim ngtypvgsll pteaeleqlf dvskitvrra iellsseelv
       61 ekksgkgttv lsnrpynkls kagtfteyln nsgqkvakki lkletvtlvs gsavysclge
      121 kavkvsrlyi lddqpyiyfn yylpmtledv pladfeqesl yrlmdqhgie imkfedsfqt
      181 veltaeqqqi lttseknglk rirksvdlsg kivefseaiy ntslypyvie yea
//
LOCUS       WP_010764206             249 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus moraviensis].
ACCESSION   WP_010764206
VERSION     WP_010764206.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..249
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27649
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mlqvenltkt ygteikyeal kglnltvndg efigimgpsg sgkstflnll atidqptsgh
       61 vllngkdpnq lnqeevakfr rrelgfifqs fnlmptltve enivlpltld gekisvmkkq
      121 lnlladrlgi asllkkriae isggqaqrva varamihqpq llladeptgn ldtksskdvm
      181 qllqqlneee ratilmvthd plaasyckri vfikdgelvd eihhngnqkm fydeimvkls
      241 eiegvdnef
//
LOCUS       WP_010764254             345 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus moraviensis].
ACCESSION   WP_010764254
VERSION     WP_010764254.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..345
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38274
     Region          25..341
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mldelkmiea vapdlldvmq erfhilrniy wmqpigrrsl sdsmgiterv lrtetdflkn
       61 lqlietsksg mtltekglgv yqgletmmnq llgmhqveke isqyfgikrc ivvagnsdnq
      121 dkvlyefgdi ltdsldlllp egrniiavmg gttmamtaey mgslesekrh nlfvparggi
      181 geamtvqans vsavmasktg ghhralyvpe qlsletynsl lqepsiqevl tlieqsncvv
      241 hsigralhma arrkmsddem vmlkqnnava esfgyffdee gevvykipri glqlkdvqki
      301 pnvvaiaggk skakairaym knapkqtwli tdeaaaneil kgvtl
//
LOCUS       WP_010764246             434 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus moraviensis].
ACCESSION   WP_010764246
VERSION     WP_010764246.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..434
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=46383
     Region          1..433
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mnkessfnke algekiamya nkiatnrfia tirdafasti pitivaaffl lvnnvllaek
       61 tgllrnmpgh emiaeigvqa yngtlgilgl mvtfligfrl aksygsdgal eaiialacyv
      121 vlvpnsinit gfdgteiqts gtltqtytsa samllgiiaa iisvplvvkl stnnklkikm
      181 pdsvppaiak sfnslipaff titlfaifev vvrtfsghti pdvvvtilqa plvggfqtlp
      241 gilayvflst fvfifgihga fvfgaisgpi lltslqqnie aiqagsaapn ivtqpflday
      301 vymggggtmi clviavliws krddqrmiak lggvsslfni sepmmfglpi vfnpvyaipf
      361 civpmvstil aytatslnlv tptyilvpwv tppilsgyla tagdfravll qiviivigtl
      421 iympfvlfsn kvke
//
LOCUS       WP_010764306             170 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus moraviensis].
ACCESSION   WP_010764306
VERSION     WP_010764306.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20260227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..170
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19726
     Region          1..114
                     /region_name="Spm_actase_Thplmales"
                     /note="spermidine N(1)-acetyltransferase; NF041158"
                     /db_xref="CDD:469070"
     Region          71..170
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mieikpitln elaelkalsi ktftdtfakd ntpedlkeyl dqayteeklt selqnkqsef
       61 yfiysddlla gylklnvnda qtetieedtl eieriyidsg fkrlglgkml ynkaieraka
      121 lnktaiwlgv wernfsamkf yhkmgftqvg ehsfymgede qtdlimkmel
//
LOCUS       WP_010764510             280 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Enterococcus moraviensis].
ACCESSION   WP_010764510
VERSION     WP_010764510.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..280
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30691
     Region          43..269
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mklkkmlvgm allsmvlagc sngtakeekk adakekdnse vviylarhgk tmlntvdrsq
       61 gwidapltpa gvevaeqlgk glsdvtfdkv vtsdsgraie taelvlknng qekmmkemtk
      121 dkrlreynfg tyeglmnedm ltavakeqgk tyeeynewmk evgfykgiie fadvlsdldk
      181 knveegvnwp aedsktivtr lkaglddivk daekegannv lvvshgmsii tllgeldana
      241 elpdgglkna svskvtykdg kytidsvndl syvekgkesk
//
LOCUS       WP_010764427             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Enterococcus moraviensis].
ACCESSION   WP_010764427
VERSION     WP_010764427.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..228
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=27112
     Region          45..228
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mkcnycnrli srnltfkeif lpqkiiteql clqcvssfhl letknccqgc qrqtnkkycg
       61 dcikwqrhyp sydfhhealf syneamqewf eaykfkghyk lrysfapflq eyfkqkkdll
      121 vvpmpisskr metrgfnqve glleaanify qpylirfedg isqvqktrke rmeltqpfel
      181 tkegqrevqn revllvddiy ttgrtifhaa qvilekspsk lytfslar
//
LOCUS       WP_010764550             270 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus moraviensis].
ACCESSION   WP_010764550
VERSION     WP_010764550.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..270
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30054
     Region          1..195
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mgilirnewe klikkksswi mwivlvamtf gitllvrsta ksqsgevmmk andlfaslte
       61 mtsflnlfvv ivaasivaee fsrgtikfll irpytrsqil fskfivcliy saigtvilyv
      121 sslisanlll ksqspfavve gyhgwnaltv agayaganll llllyititl fisaairsqs
      181 lavgiglgvl fgsniinsfl nvvipkyewl kwnpfnmlni kntimddiga qnsypaylnf
      241 wqmtggiliy svmiyvvmql lfkkrdvsln
//
LOCUS       WP_010764622             285 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Enterococcus moraviensis].
ACCESSION   WP_010764622
VERSION     WP_010764622.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..285
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=31186
     Region          5..281
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mnkekiallv dsgtdvpqel veqygmymip lqiiykdriy tdkvditpee vyerlpieip
       61 stslpdgeti tkifekikad gyekvlavti ssglsgtfnv vrliseefeg letfvldtkn
      121 igigsglqai eaakmieagi swdeiklklt nnvtkakvyf nvatleylqk ggriglvasi
      181 lgnalklnpi iscngegvyh tvakargrkk sldktfelvk afvgehkkfv lavaqgqave
      241 eaeafyeklk tqfpqaekiy fgtispalvv htgpgllgig iqlld
//
LOCUS       WP_010764568             783 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Enterococcus moraviensis].
ACCESSION   WP_010764568
VERSION     WP_010764568.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..783
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=91263
     Region          181..783
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mqntqkiavr rlvefilrkg sidarhtseh talegakihr alqktagdny qkeiklaidi
       61 elnkqtyiie gradgifidd kkrtvideik tsepafsell deqidmfwyq vmcyghiycq
      121 qndletitlq ltyfqtttee itrqekeftk eelkiffddl tqkyeqwlif kanwrktrnr
      181 slqklsfpyg eyragqrela vavyktilsd qklfveaptg tgktistlfp tlkamgeeqa
      241 ervfyltakt itrqvaedav eamkqkemkl ksvtltakdk icflternct peacpfangy
      301 ydrlneglwd llnnesqftr eviesyaqkh tlcpfelsld vslwcdlvic dynylfdpvv
      361 ylrrffeeqt edkeniflvd evhnlvnrsr emysavlsks kltslketld kkqtkliral
      421 nkiekefdki kqicdeeeke fvhqnapids lvkvayslae kikewlpenq dyqeinqvls
      481 vyfdllnytk isegyddhyc tyvncqnhdi lvkqfcidps yllkqkldkg kasvlfsasl
      541 tpldyyqeil gggeaslryr ipspfpkenq llvieqyiqt tykeressye kiiasltnmi
      601 qqkkgnyfvf fpsyaymdsi yeqfkkqhph vktkiqasmm neaereafla dfisepeetl
      661 vgfcvlggif segidlkgsr ligtvivgvg lpqinheqel ikeyydrekn qgfqfayqip
      721 gmnkvlqaag rvirdtndrg vvllldqrfs tnavkrffpp hwnqaktsys sectqqflqq
      781 fwq
//
LOCUS       WP_010764647             393 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Enterococcus
            moraviensis].
ACCESSION   WP_010764647
VERSION     WP_010764647.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..393
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=44092
     Region          26..388
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mrraihskse linyalllpv fllilvgfia qygafhadps vesiapllkr qllwtllgil
       61 tmfatmfipi kylwkltpvi ygaslflmsl likfhdpvma vatgtkrwlr lgpisfqpse
      121 fmklgyilml ayivtkcrqn tsnpstlked frllgkmslv slpimalmfy qkdfgtslvf
      181 isiflgvvli sgcswkilav gfgsigvlgv ssillvlter gqkilsllhf qpyqfnriha
      241 wlnpfeyadt isfqqargli aigsgemlgk gltnmqiyvp vresdmiftv igeaygfvgt
      301 calillffyl iyqmlictln akrefyayit tgvimyflfh ilenigsnig llpltgiplp
      361 fisqggtayl anfigvglil smyyqkekdy pfr
//
LOCUS       WP_010764649             305 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Enterococcus moraviensis].
ACCESSION   WP_010764649
VERSION     WP_010764649.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..305
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=33936
     Region          76..301
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mkkvlicvfl ctlliitaig syavisfhng kkiaksqvnk tkntnfsgdq qtnmkeitim
       61 ligddgredd edggradtlm vahynsetkq pklisimrds yveipdhgle kinaayaygg
      121 adltrkvlnd sfglpinyyi svdfnhfirl inelypkgie idaekeidld nvvlkkglqi
      181 mdghtllqya rfrmdeegdf grirrqqqvm dalakqskka vsfiqlpkia geaigyldtn
      241 ipadllvdla kdfltgnvkd letlsvpvkg swsfndytda gsvleideqq nkkaiqdfla
      301 dgasq
//
LOCUS       WP_010764670             587 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CocE/NonD family hydrolase [Enterococcus].
ACCESSION   WP_010764670
VERSION     WP_010764670.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..587
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=65942
     Region          48..584
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mttkmtekmc fspsfdyidn gvehgvlspf etkeiilkkg dqiaegfkpl tndikmlkdv
       61 pvelrdgiti ytdiylpite kkvpvliaws pygksagtap ryknlfnmlg mgnhwnsglt
      121 kfeapdpdyw cahgyavcnp dmrgiahseg nttmigsqea qdgydliewl asqswsngkt
      181 altgtsylaf sqwyiaaeqp phltcinpte gladgyrdla figgipdenf ierlqvnhvs
      241 aknatredlv kemkayplan tavwqdkvad pnkitipafv iasysntlht mgtfrswrtl
      301 gskekwlrih drqewpyyyd eknieelrrf fdyylleken gwtetptvry slidfhggnk
      361 tdipsesfpp stsenkryyl nglsrtlqen petkdatvky tagnlpgrss fqltfakdtd
      421 fvgypkaklf mevegyedmd ifvwiqkldk lgnvlsefvv pnhgaalqdf tqegasalry
      481 kgawgrlras mrhldsgltt deipaytfdr vqklskgeiv aldivlsplg lsykagetlr
      541 mvistkdelg svmpgtpgct pdnqgthilh tggeyasylq lplivth
//
LOCUS       WP_010764728             270 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus moraviensis].
ACCESSION   WP_010764728
VERSION     WP_010764728.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..270
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30176
     Region          4..263
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,193,215..217,219..220)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mkkliaidld gttlnaqsli snttekalkn aiknghyvsi vtgrpyrmsg qfyrqlglnt
       61 pmvnfngalv hmpeqkwade ketgiqrdlv fdilaqkkal nldfvaaenk etffidsldy
      121 fdstffasea tpsnlltakn lvtdptsmmv rtskdqaahv sdslmkqygd yvdvrtwggp
      181 tpileivskg iqkargveqv aryldikrsd iiafgdehnd eemleyvgwg vamknatdqi
      241 ksvandvtek tndedglady leryldlknq
//
LOCUS       WP_010764731             468 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Enterococcus moraviensis].
ACCESSION   WP_010764731
VERSION     WP_010764731.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..468
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49391
     Region          1..467
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mdkffklken kttistemva gvttffamsy ilfvnpsils qtgmpfqavf latiiasiig
       61 tlimglfanv pyaqapgmgl nafftftvvf glgytwqqal amvficglin vlitvtkirk
      121 liinaipesm qhaigggigi fvayvgikna klldftvqae pvngavngds ivpalgnfnn
      181 peiilavigl vlttvlvvln vrgsiligiv vttiiaipmg vvdvsaidwk tnslgnsine
      241 lkttfgaafg adgmqslfsd askipqvlmt viafslsdtf dtigtfigtg rrtgifsked
      301 elaledskgf stkmdkalfa daiatsigai fgtsntttyv esaagigagg rtgltsvvva
      361 vlfalsslfs pliaivpaqa tapalilvgv mmlasfkdie wtnleeaipa ffasifmglc
      421 ysisygiaag fifyavvkva kgkfrevspi lwvvnalfil nfiilail
//
LOCUS       WP_010764756             213 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Enterococcus moraviensis].
ACCESSION   WP_010764756
VERSION     WP_010764756.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..213
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24488
     Region          17..212
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 mdnekviaie qftqsimkqd qtghgmdhin rvvrlaqkia etedcdffiv taaaylhdtv
       61 ddklvadsqe aykqleefll giavsseqmq qimhiiknls fsqqlngtae kltlegqivq
      121 dadrldamga vgitrtiyyg gykgnliydp nikprtlksk aeyreestvf nhfyekilll
      181 neylnteyak qignkrqrfl esfleeflde wdq
//
LOCUS       WP_010764784             149 aa            linear   BCT 01-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Enterococcus moraviensis].
ACCESSION   WP_010764784
VERSION     WP_010764784.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..149
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16535
     Region          1..147
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 msllttlndd iksamkskdk dtlsvlrmlk aaiqneqika grdldgeeel tvlsremkqr
       61 kdslsefeka grddladkvk ieiaivekym prqlseeeir qivqtaidqt gatspkefgk
      121 vmsavmpevk gkadgnqvna ivkellqen
//
LOCUS       WP_010764798             189 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010764798
VERSION     WP_010764798.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..189
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21862
     Region          6..>108
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdkemkntrd riiqvatrlf mdngyqstst rqiaqlaevt qpnlyhhfrn keevyigvie
       61 sllgdvneel lkivedqsld tinklqqfae clktkhpfdf dlmmhdfrtk ltketqfklf
      121 slwndsykkp llnlfeksdf sirkglspev atthflntls pyikteqsrs slsitqvvdl
      181 fvfgvsask
//
LOCUS       WP_010764821             107 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus moraviensis].
ACCESSION   WP_010764821
VERSION     WP_010764821.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..107
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12089
     Region          10..92
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 medtltdssy lillallkpq hgyaimkevn sltygqvnig pasmytilkk leknqlitle
       61 esnerkkiyl isdkglellk tdtkrrklly qagsrllaek gemnedv
//
LOCUS       WP_010764851             226 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus moraviensis].
ACCESSION   WP_010764851
VERSION     WP_010764851.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25283
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mikleqinkf ysleeeklhv lkdinfeike kefvavmgps gsgkstlinl igfidkkfdg
       61 qylfegkeit dfsdkelsai rnksvgfvfq nfslienntv fenvelplly ngsaytitka
      121 rvqevlgkvg ladkgnkypk qlsggqqqrv aiaraivnsp rfiiadeptg aldsktsedi
      181 mqlfqdlnkd egvtiilvth npemvsycdr lirvkdgaiv eeelik
//
LOCUS       WP_010764856             310 aa            linear   BCT 01-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Enterococcus
            moraviensis].
ACCESSION   WP_010764856
VERSION     WP_010764856.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..310
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34348
     Region          89..303
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mfilgqskss ttiestldst idiktvtenk vnalqrfwng inwdqiiatl iektiyllfl
       61 illfvilnri gktlidktyg nyskkqsfse srlktlhtli nnafqytlff ffvyslltvv
      121 gvpvgsllag agiagvaigl gaqgfmndii tgffiileqq mdvgdyvrlt algiegtvta
      181 vglrttqmka ldgtvhfipn rnittisnls rsnmqvlidv rimpdegydq itaiidqvnq
      241 elkekytesi qtgptifgmv dlgngnfavr ttmyvlngkq apireeflaq yvkklseanf
      301 tipntpitlk
//
LOCUS       WP_010764607             548 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha-keto acid decarboxylase family protein [Enterococcus
            moraviensis].
ACCESSION   WP_010764607
VERSION     WP_010764607.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..548
                     /product="alpha-keto acid decarboxylase family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60750
     Region          1..541
                     /region_name="PDC1"
                     /note="TPP-dependent 2-oxoacid decarboxylase, includes
                     indolepyruvate decarboxylase [Carbohydrate transport and
                     metabolism, Coenzyme transport and metabolism, General
                     function prediction only]; COG3961"
                     /db_xref="CDD:443161"
ORIGIN      
        1 mytvadylld rlkelgidev fgvpgdynlq fldhitarkd lewignanel naaymadgya
       61 rtkgisalvt tfgvgelsai nglagsyaes ipvieivgsp tttvqqnkkl vhhtlgdgdf
      121 lrferiheev saaiahlste napseidrvl tvamtekrpv yinlpidiae mkasapttpl
      181 nhttdqlttv etailtkved alkqsknpvv iagheilsyh ienqleqfiq kfnlpitvlp
      241 fgkgafneed ahylgtytgs ttdesmknrv dhadlvlllg akltdsatsg fsfgftekqm
      301 isigstevlf ygekqetvql drfvsalstl sfsrftdemp svkrlatpkv rdekltqkqf
      361 wqmvesfllq gdtvvgeqgt sffgltnvpl kkdmhfigqp lwgsigytfp salgsqiank
      421 esrhllfigd gslqltvqel gtairekltp ivfvinnngy tvereihgat eqyndipmwd
      481 yqklpfvfgg tdqtvatykv steieldnam trartdvdrl qwievvmdqn dapvllkkla
      541 kifakqns
//
LOCUS       WP_010764999             309 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus moraviensis].
ACCESSION   WP_010764999
VERSION     WP_010764999.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..309
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34564
     Region          66..307
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mnrivkilia ivvlvvvvlt gagmyfynya vvptekdfla gdtpgtnvek tpqekwfkde
       61 knrsywnlts kddlklkaiy lpatektdkn vimahgymgn aetmasfakm yhdwgynvlv
      121 pdarghgese gdyigfgwpe rkdylqwiek miaengqdaq itlygismgg atvmmtsgek
      181 lpknvkaive dcgystvnee lsyqlkdmfn lpsfplvpvt slitkvragy ffgeassiaq
      241 lkknkvpmlf ihgdadkfvp femldevyna tnapkekfvv kgaahaksys idpkaykakv
      301 esfltkyve
//
LOCUS       WP_010765006             176 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010765006
VERSION     WP_010765006.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..176
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20125
     Region          3..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvrkkvykkq hiltaaqdll tekgfsfita rnvaehmgis tqpiylefkn meelkltllk
       61 ttheflntef fskkqnsnil anfglnyidf aqsnsklyls lyidqhsygk elqqlsfesf
      121 qktaqendvy aevskeelek lhmnvwviat gmaslslsgi lnlskeqiis afktik
//
LOCUS       WP_010765049             298 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Enterococcus moraviensis].
ACCESSION   WP_010765049
VERSION     WP_010765049.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34205
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,117,122..128,220..225,231..232,
                     234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mnlrqleffr mladtqhmth aakllnttqp nlshsmsele keldaqlfek kgrniqltky
       61 gkffytyvst aleelakger alkelvspek glidfgfiyt agsflapmlm kefstypgne
      121 qirfnlfqgn ssdmtdlllk edvdiaitsk lkedeqlhye ilteqeivlv vpnnhplaih
      181 dtvslkhtse ypfvyfners glrpyldrlf ssasitpqiv ceveedhtll gfvahdygia
      241 lmpkipsisa ydvkaisled nffpryiyla tkkdhflspa alrfkefilp faqnmfyq
//
LOCUS       WP_010765014             126 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus moraviensis].
ACCESSION   WP_010765014
VERSION     WP_010765014.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..126
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14520
     Region          2..112
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mvsinktssk pyyeqlmlgi kedilsgllq sgdrlpsvre marqlmmnpn tvskayklle
       61 tqevivtvkg kgtyvnkidt tlrdeyqiqk ikkkfdelii danylnvqke emcqwldesy
      121 qhlkge
//
LOCUS       WP_010765134             593 aa            linear   BCT 01-JAN-2025
DEFINITION  V-type ATP synthase subunit A [Enterococcus moraviensis].
ACCESSION   WP_010765134
VERSION     WP_010765134.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF003220.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK04192
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..593
                     /product="V-type ATP synthase subunit A"
                     /EC_number="7.1.2.2"
                     /calculated_mol_wt=65465
     Region          1..584
                     /region_name="NtpA"
                     /note="Archaeal/vacuolar-type H+-ATPase catalytic subunit
                     A/Vma1 [Energy production and conversion]; COG1155"
                     /db_xref="CDD:440769"
ORIGIN      
        1 mqtgkiikvs gplvmaenms dasiqdicyv galgvigeii emrgdvasiq vyeettgigp
       61 gepvvttgea lsvelapgli semfdgiqrp ldtfaeitks nflsrgvqip aldrtkkwlf
      121 eptvsigdev sagdiigfvq etkviphkim vpfgnsgivk evkkgeftie etiyiietkt
      181 gekefsmmqk wpvrrsrpil eklnpavpll tgqrvidtff pvtkggaaav pgpfgagktv
      241 vqhqiakwad vdlvvyvgcg ergnemtdvl nefpelidps tgesvmertv liantsnmpv
      301 aareasiytg itiaeyfrdm gysvaimads tsrwaealre msgrleempg degypaylgs
      361 rlaeyyerag qvvalgkdhr egsitaisav spsggdisep vtqntlrvvk vfwgldatla
      421 qkrhfpsinw lqsyslydte vgkyldqqlq lewsdmvveg mrilqeesql eeivrlvgid
      481 slsdkdrltl evaksiredy lqqnafdevd tftsrekqyk mlhliltfyk egqmaldlga
      541 ylseimagtv eirdqiarsk yvpeeeitrl ddlvgemkqt ikqiiadggm tnd
//
LOCUS       WP_010765130             511 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus moraviensis].
ACCESSION   WP_010765130
VERSION     WP_010765130.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 511)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..511
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54203
     Region          201..416
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnfikralls mkskkgrtll lcavfsaili fvlagltiqs aalsatenak knvgatvtls
       61 anreaamkks qnddsgerpd pgsfsltpvs lsdaqkiael dnvksysfls sssagagdgi
      121 tpisnesesd tttssdvket qanggedaqt qgngrmgggp masmkqsdfq vsgvmnlsms
      181 sdfsegiaei tsgeaisesd kdtnnvvieq tladannlkv gdtfkvtnpe ddtktyelkv
      241 kgiyttseng dsmgmmfnfl npantlytsy tfantlkged akgtidsasy tlddpkemds
      301 fvkaaeklid tesfslqtnd qayqqmlqpl nnvasfakni vilvavagvi iltlivmmti
      361 rerryeigvl lslgesrfkv vlqffseiii cmfialviat fsgnivgnvv geqlinqqte
      421 atqqtgnnqg qpggmgdrgg eqrqggpggg smsrlgassq eaaeaikeln isvqpkeial
      481 laglgllisf fsillssvgi lrlqpkkilt t
//
LOCUS       WP_010765208             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010765208
VERSION     WP_010765208.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..265
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30981
     Region          1..257
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdffevvnph vseltknehl lfdyvvknln eiknksirev addcfvsttt flrfvrkigf
       61 sgysefttvi kytllnqkke ekvspfvvsq kdyreeylkn inesvrvidk nslrkvgeyl
      121 kkkpiiylfa kgmnkqlmqy vkylfvaagf lvvfpedqsm ravvqrqikp edmvfiltyq
      181 gkdeewvqlm qqlkkaahpl lvsitgadnn vvqnmsdvnf yvftdelfln kmeitshism
      241 lailelilyq yldnaeegey hlifk
//
LOCUS       WP_010765201             212 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Enterococcus moraviensis].
ACCESSION   WP_010765201
VERSION     WP_010765201.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..212
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=24806
     Region          76..176
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mdldydsyfe yhdqtyiiid kianyyglel kdlrwnhfkd yaidveniei ipyrfgevlt
       61 ehlsgniirf dnnygisfns lmnygrqrfs ilhelghfyf dmdqskasqs fsdllegngy
      121 seedfpkear anvfasltmi nnealkecfr knmsfeditv efgtskaaly vrifdfltkl
      181 ymlnpsiarq alnnyrysgd sskilrfisv sl
//
LOCUS       WP_010765218             419 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus moraviensis].
ACCESSION   WP_010765218
VERSION     WP_010765218.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..419
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=45222
     Region          16..416
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 msdvkkssfi nglnlfvnkf snnifvksia ngmmmtlpit ivgslttiig mipglpeivv
       61 kacslgtsis snlitvyvii gissamarek kgdviasiil slatffvltp itafdigqek
      121 pamafeltyl gskgifvgmi valfvtwlfa kmvekritfr mpesvptaia ktfeaivpaa
      181 iifivaimis tafaetqfgn ihdfiytnlq tplealggsi wsalfimfls ellwffgihg
      241 smvvgsviav lfttqayanm eavaagevat niinsfflda fkgpralala vilvwmsrse
      301 kfksigkisl ipsifgitep mkfgipmimn aiifipltls aavcvgiayl atiigflpvi
      361 svnvpknlpt flsgfmaagw qglvvqliqf vvvvllylpf mkkldkqgvv eeeatvkne
//
LOCUS       WP_010765222             401 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus moraviensis].
ACCESSION   WP_010765222
VERSION     WP_010765222.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..401
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43429
     Region          25..388
                     /region_name="MFS_YfmO_like"
                     /note="Bacillus subtilis multidrug efflux protein YfmO and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17474"
                     /db_xref="CDD:341027"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,151,
                     154..155,158,226,229..230,233..235,238,263,267,318..319,
                     323,327,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341027"
ORIGIN      
        1 meetdyleeq laevaiekgg lrsayavaft cmiafmgigl vdpilktiaq qldatpaqtt
       61 llftsymlvt gvmmlftgfi ssrigakktl ifgliiiimf sclagfseti kgliylragw
      121 glgnalfist alsaivgvla gqtekaiimy easmglgmsi gpllggvlgs aswrlpffgv
      181 aflmfiatla isflltpivk pkekvsifag ikalknhklr sigviallyn fgfftllaya
      241 pfllegftem qvgfvffgwg allavasvfi apilekrint yrtillalff flaslffigl
      301 naqnpqfvai gviiagffqg lintllttia meiptiersv asssysfirf fggaiapfva
      361 gklaetwnss vtfyfaalmv liglifvivh sqyfateeey e
//
LOCUS       WP_010765227             251 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus moraviensis].
ACCESSION   WP_010765227
VERSION     WP_010765227.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..251
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27704
     Region          5..212
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtnaivtenv sktidqkkiv ddisiqvaqg eilgilgrng agktslmkll lniispstgt
       61 iqlldktvtt qdnsvlgeig clietpvfyn qlsarenlei hclyidekhc enisetmalv
      121 glggkenelv ssfslgmkqr lgiaraivtk pkilildepi ngldpigmid vrnilsemnq
      181 tyqttiliss hiitelsqia sriiimeegk iirsldqiel ereersleev fieiiqnyqn
      241 paknfvnges q
//
LOCUS       WP_010765267             442 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            moraviensis].
ACCESSION   WP_010765267
VERSION     WP_010765267.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..442
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46485
     Region          25..431
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mdgkenqtkq ntqpetsngk savlglqhll amyagavavp lligtglnfn seqmtylisi
       61 difmcgiatl lqltvnkffg iglpvvlgca iqavaplimi gndkgvgaiy gsiiasgifv
      121 vlvsgifski kklfpplvtg tvitvigltl ipvavekmgg glasasnfgd stslllafvt
      181 igliivvqvw gkgfiksiav lvglvggtil aailgqvdla pvgdatwfhf pqpfyfgtpt
      241 fdvssivlmi iisivsmves tgvyfalgdi tgkrigeqel kkgyraegla vilggifntf
      301 pytgfsqnvg lvqlsgiktr rpiyysaffl ialgllpkvg avaqiipepv lgggmlvmfg
      361 mvavqgmrml skvdynndkn lliiaisigf glgfnmiptl fqqmpetvrm ftgngivmss
      421 ltaiilnllf nglkgeetae gl
//
LOCUS       WP_010765341             251 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Enterococcus moraviensis].
ACCESSION   WP_010765341
VERSION     WP_010765341.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..251
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29454
     Region          54..140
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 mkknelkkyw csieqmdfsg wdfsymrnrw eienlpwdys tlvrhyltne mdlldmgtgg
       61 gellrtfhhp ynktfvtegw pknyqllkes leplgvtvaf vdetdqlsyp ddsfdlvlns
      121 hesydpkevr rvlkpggifi tqqvgdqngq ilskklmtav qsnqewsldt akkgllkehf
      181 tslyaneyfp yqhfcdmegl iyyatqipwe yldfsvdthf aslvelqkel lskgfvynqq
      241 hrfilvgklk h
//
LOCUS       WP_010765345             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010765345
VERSION     WP_010765345.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..265
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29648
     Region          1..263
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mesyieliiq anqkkftdve rvianyfldg nkelgiqela kklsvsnssi trfckkigla
       61 nykeliylyk ysskgakkqt dssisyvnln yslllndiie kldkeevkka almidkgrii
      121 hywgtgynaf cgedfqfkfs rlgkivnvik dehsiammah gvqqgdlvvv ssisgdneav
      181 leavkivsek nakvivisan ekspykefse afcltssmgk kdmggispqi pvltvidily
      241 teilamyhed tikswiksev ilkgk
//
LOCUS       WP_010765346             440 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus moraviensis].
ACCESSION   WP_010765346
VERSION     WP_010765346.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..440
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=47977
     Region          1..429
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mkidiekiqd pllkiankvd nnsvlqaikn afissipftv vgsfsnlikm qidaffgeta
       61 igqtasaifg nvyqgtlgiv allivfstay nyakelmkkh peaninplla tllafaayfv
      121 mvpnnvnfad gsadiiqgya nnffsyegmf talivgllav flysilakhk iaiklpgnvp
      181 pnvfdsffal ipisivllic svmkvvieaf dfnsfmdlvs qlfvqpltsv gtglpaiivv
      241 illeqilwfl glhgfnivwg vvsalwlpif lenvakfaet ksfadisvap ntmtnvyami
      301 ggsgatfgli lailiftpkt ysgrevakls fipglfgine piifgfpivl nplmfilfvf
      361 vpvfnaivay ivtkigwvvp lvvlnsgnep ifistwilga fhlspvilta vlvvldvfiy
      421 apfvrmnmkf desqllnaqd
//
LOCUS       WP_010765357             216 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010765357
VERSION     WP_010765357.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24792
     Region          4..>66
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtkrydteat vqdildaatr lfvekgyekt tiqdivnald glsrgaiyhh frskeaiidg
       61 vvrrlipdta ylndisnrtd lnglekmqhl lletlfnkev gasfqlaysl fdnpkffmmy
      121 imntnevlap qierfinegn ndkslqieyp kqvseiivll lgtwfivalf pntietfwdk
      181 lyatkyvleg iklnllsdei mekiingike aenekk
//
LOCUS       WP_010765360             279 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus moraviensis].
ACCESSION   WP_010765360
VERSION     WP_010765360.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..279
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30633
     Region          6..277
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,208,230..232,234..235)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mdvkaivldi dgtllndekk lttltkeali naqkngikvi lasgrptpgm lkyveelema
       61 kyngmivsyn gahvldvstq kelfsqplsi essknilehl kqfdvkpmia kdeymyvndv
      121 fdgmldlgdp dglfniikye srggnfqlce kedlaafvdf plhkilvagq pdylqenwqa
      181 ilapfeqsvs gmfsapvyfe ftdkgidkan aleqtlkplg iheehiisfg dghndlslin
      241 yagmgvamgn avddlkkaad kitssnnedg iakalaell
//
LOCUS       WP_010765406             148 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Enterococcus moraviensis].
ACCESSION   WP_010765406
VERSION     WP_010765406.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..148
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16845
     Region          50..144
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(71,74)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkkktaflyl svvimfvamt icltdlllph eheanssevg mayfdelsfe siqkknenke
       61 vyfayfgfdd csgckeftpl liaaskdidy prifhtdtsi ksnkkvitef gievvptlll
      121 fedgkiskrf vfsgesekki kdfllknq
//
LOCUS       WP_010765402             364 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus moraviensis].
ACCESSION   WP_010765402
VERSION     WP_010765402.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 364)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..364
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41282
     Region          <161..>274
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mnkklfifel kkflkekknl fifslivffl gatffqtiir qnelrkkdir qtvsfynvat
       61 qniltlsdgq glgkeetkql nllsdiadnl nivvtlkknn qyiksypyqi ilfkqmlsle
      121 kehgialwen kaiitqlkrl kilqsqnide sfdekgttgf lflltflkns fsflgmgvii
      181 llfmdlwsge knsgisllyt lpikrkaiey sklylaisis cvilltssii aflvgtiysg
      241 mgsadfpivv vsnnqylvip lkvyltkgif lgilgiivfi ccikladtlf sqpsiilsvl
      301 llllgisfgi aqiipdnyfp lnlieswhyf sfhgkftkfi vaiiiqltti vcllklsdtl
      361 kkrt
//
LOCUS       WP_010765413             190 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010765413
VERSION     WP_010765413.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21799
     Region          2..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 martkefnes vvldkamltf weqgyektsm qdlvdnmgih rrsiydtfgd khalfmkald
       61 qyeteleqei sqrlkptmst kekleelfsi viqensdhpk gclivntate lalldsevte
      121 kvqgafskse nyiyrllkeg qknditlkkq nlhelasylh nawvgirvla kttndqkklr
      181 sivkvtlsil
//
LOCUS       WP_010765418             665 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF262 domain-containing protein [Enterococcus moraviensis].
ACCESSION   WP_010765418
VERSION     WP_010765418.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..665
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=78224
     Region          1..541
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 mkadtikffe fleqkktifn ipvyqrnyew sneqcvqlfn dvekiiqddf sakhflgtiv
       61 yvdergpkls kyfniidgqq ritsfmlfmk aiadlsddes lydeilddyl lnprseennk
      121 iklrsvekdr lvfrkiiekh eveetskvse nfnlfltrie eseyepkeff dalgmieivy
      181 ielngndese npqvifesin stglsltasd lirnfllmgi dhetqnrlyk dywtkieeri
      241 ptnqistfir fyltlkfgat vterrvyeey krffnnnhyt petaikelen yskyyfwlnn
      301 eiipkstvne rikrvnlmka tivypylmqi lklgddgiyt wdnvdeifgt vesylfrrsi
      361 tdkrtnvlnk mfaalsreis idnekdrlii eltnkkgtqi fprdaefvns fqtvalynrk
      421 nnlaklvlmm lelyrtkepi sfesiqvehi mpqtltndwk vsvknandvq ikygdtignl
      481 tltgynsels nklfsekskm yqqsnitltr elaneydkwd aytiedrakk lseealkiwk
      541 fpiqvqaeeq ssvsgehfld edvnitgskp kllsiedkdy kvdswkkvli sfldfvwefd
      601 sqtfanlkrr evlkrlfspa devrnpgkls ngeivetnfs setilsiiki iateynifdd
      661 isyti
//
LOCUS       WP_010765481             337 aa            linear   BCT 01-JAN-2025
DEFINITION  XdhC family protein [Enterococcus moraviensis].
ACCESSION   WP_010765481
VERSION     WP_010765481.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..337
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36857
     Region          2..336
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 mkelflqiik airqkedtvl vtviessgst prgagaqmlv gksgringti gggavefrge
       61 kiakeivksh lsrtekfila pndvadlgmi cggdvelffq ylswqdanvq eicgeiirhf
      121 ecnqqcwlim evnaegvndf glysqkngll gdipaelekm qfktglskav vdgkvysias
      181 llqtgkvfvf ggghvaqavi pilktldfyc vvlddrehfl tesifpdadq rmvidlgnid
      241 asiqiteady aivmtrghqf dfllakqlln tpahyigvmg skqkiatqir klkecsfsms
      301 diarinmpig lkikaetpae laisvageli ekratak
//
LOCUS       WP_010765479             257 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus moraviensis].
ACCESSION   WP_010765479
VERSION     WP_010765479.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28846
     Region          1..252
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mlevadltfa ykqqnilqni sfklgygqsv fvlgkngvgk stlfkcllrl lkprtgsiki
       61 ndqsiqmcsr nelsqlisyi pqnqrgtfhf tvfemvlmgt tarlknyqqp gkienelaes
      121 alkalnishl knrsyseisg geqqlviiar svaqqskiii mdepcanldy gnqimvlemi
      181 qklaeegyli iqathdpnha lqyadyvlil qegcllqgep kkiltsqqle aiyhvpitvh
      241 qlnsseqsic lpkkkvy
//
LOCUS       WP_010765484             439 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            moraviensis].
ACCESSION   WP_010765484
VERSION     WP_010765484.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..439
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46024
     Region          25..431
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 msekqekalf nydaklsike avpmglqhvv aavvgivtpg imiakvcnls sgdttimiqt
       61 slifsavatf vqlfpifgkv gsrlpvmmga sfayvpilma iggdfgiaai fgaqlvgsil
      121 vilvglsikk irvlfpplvt gtvilsigls lfpvaikyma ggagspdfgs vqnwlvallt
      181 fgvvfyfnyf skgflklssi lngmiigyvv slflgmvnft pvkeasvfqv itplyfgldf
      241 qivpiltlvv mfivdavqai gqftattvga mdreptdkel sggimgsgfs nfigsffgsv
      301 pvatfgqnvg lvtvtrvink yvmvfasvil lvagfvpkva silttipyav iggatvsvfa
      361 sismtgvrmi ssqaltprnt gvvgislafg igvtlsvgcl sgfppwvtti fgnseviltt
      421 ivavllnvvl keepqvale
//
LOCUS       WP_010765568             361 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus moraviensis].
ACCESSION   WP_010765568
VERSION     WP_010765568.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..361
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41093
     Region          1..344
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkkniitfen vvkqyddekv lknvsfeieq gkfytllgps gcgkttilri lagfadateg
       61 dvyfdgqrin dvpankrqvn tvfqdyalfp hmnvfdnvaf glkikkiskk eiekkvkdal
      121 rmvqlpgyet reisemsggq rqrvaiarai vnepkvllld eplsaldlkl rtdmqyelre
      181 lqqrlgitfi fvthdqeeal amsdeifvmn kghivqsgtp vdiydepinh fvadfvgesn
      241 ivngtmiedn lvefvgkrfe cvdggmrqae pveimlrped ltittadkgk lvvtvdtqlf
      301 rgvhyeiich dddhnewmvh stkkaiegak vglffepedi hvmrfnesee dfdarlesye
      361 e
//
LOCUS       WP_010765525              91 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus moraviensis].
ACCESSION   WP_010765525
VERSION     WP_010765525.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 91)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..91
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10599
     Region          1..88
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 meikeekdrf vllndenqei gemtwsnagd kmmiidhtfv dpayrgqkla eklvmngvek
       61 arreekkiip lcpfakkefd rkpeygdvlr k
//
LOCUS       WP_010765666             201 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus moraviensis].
ACCESSION   WP_010765666
VERSION     WP_010765666.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..201
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23135
     Region          2..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(7,9,65..66,69)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            9
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(64,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(70,75..76,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93..95,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..196
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(148..150,190..191,193..195)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mkvayarvss idqslerqiq efeklgaeki fiekksgatv eqrpifkeal dferesdifm
       61 veaidrlgrn ydeiiltvnq lknknvqlii tslpimaeai gnplldrfik dliiqilami
      121 aeqerteskr rqaqgikiak ergiykgrpk lysetardlq kraiyhqive klvmgisise
      181 iskelgitrq tvyrikkele n
//
LOCUS       WP_010765645             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Enterococcus].
ACCESSION   WP_010765645
VERSION     WP_010765645.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..245
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26898
     Region          5..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 maekilvehl vkkygdntvl ndinvsiqeg dvvcvigpsg sgkstflrcl nqleeatsgd
       61 iiidganltd kntninkvrq higmvfqhfn lfphlsimen itlaptdlgr lskkeaeeka
      121 iqlldtvgla dkkdsypesl sggqkqrvai aralamnpdi mlfdeptsal dpemvgdvln
      181 vmkklakqgm tmvivthemg fakevanrvm fidggnfled gspqqifenp qnertkdfld
      241 kvlni
//
LOCUS       WP_010765681             201 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010765681
VERSION     WP_010765681.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..201
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23466
     Region          13..200
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mieylkqnap hdciekkydk nsliideyek tttlyyvvdg visveilneg kryissfilq
       61 ndffgldsfs tfkqkehsir viseqatifs iskemllhsl nkvphyyell ltnfadifqr
      121 hysyfnflhl psterikqal iylsdhigil tvtdqlelpk fitqeilskf crtsqsrisi
      181 slnelqktgw llkkkvpitl n
//
LOCUS       WP_010765683             101 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Enterococcus
            moraviensis].
ACCESSION   WP_010765683
VERSION     WP_010765683.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..101
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11238
     Region          1..94
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 myksmmidef eqlekrnela ivdvrevdey vsghikgakn mplsmlqeta tslektkpyy
       61 iichsggrsq maseyfaslg ydvtnvmggm sawrgdvvdg m
//
LOCUS       WP_010765692             132 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus moraviensis].
ACCESSION   WP_010765692
VERSION     WP_010765692.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..132
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15123
     Region          1..113
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(49,52,56..57,66,84,88,94,98,101..102)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mtikemaelv gisadtlryy erisvipavt rtvhgvrdyd eihlewiqsi lklkasgmtl
       61 emiieyvrla nvgdstiear kqlleeeqer itakieelqd rlatinlkia dyyedllpkt
      121 taminkmkpk id
//
LOCUS       WP_010765717             427 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus moraviensis].
ACCESSION   WP_010765717
VERSION     WP_010765717.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..427
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45654
     Region          12..423
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mdakskgsgm dywkkivill cagwvtiwvy rsalspaypq inaslggnit dtalgfistc
       61 yffgyvamqi pagflvdkig kkkvlipgfi vfglaallis qatniqmiyv gsvlaglgcg
      121 sfygsayslt sqniprekrs fstaivnsgs avgsglglil ssflvvqlkf pwqtmmyisv
      181 aliavmlvaf vaiirnnked aeflaqteaa eaaeaaaaap eatvvekekv sikklfspkm
      241 lfayilyfat cyayymtvtw lpnflgterg fegaaigfsa slvafasipg alffsrladk
      301 fmhkkvqfiv ileflaaaml lltvqatnst llliglilyg flgklavepi iiswlgenap
      361 kvgigttlgv fnffgmmssv iaptltgsis datgskemgf yisvillvvg talfllanln
      421 kkktvae
//
LOCUS       WP_010765719             546 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus moraviensis].
ACCESSION   WP_010765719
VERSION     WP_010765719.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..546
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62903
     Region          6..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          256..538
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mttledllki prfsdlkllt hpskantive sieisetpdv anfvpkkifl lttamvykdn
       61 qeelirlids lkeqeaagig ikvgrfieti dpevvayank idfpvvqvps tqplgallhq
      121 llnylwdtkt eqlsyaldiq krfsnllihd vsiarfiadf gkmintpvil lspyrkviah
      181 skhftqtskp aeyyveqlvs kysnwnedsh asfmikdlnq eplqiagfsv tvnsyfphyl
      241 lilnpqqvpy pmsefaveqa clvlsfmlyk nqkvqesldf lksdflsqli eyqqtphqsr
      301 rdwldlgtny glkkstqyqv vyavcnqtit tatkikyqqe esdvafqwls etlpprikhi
      361 sifkvkntnh lailiqsrve dlekilsels lelseklpit ltfalgnlye tieqiassfi
      421 eaktayeeml tmtnvplthr yhpkgmkslf ekmsledihy fcettlkela ypvedsfiel
      481 rktlqcylsf qceisktake mylhrntiky ridhcakllg kniqdptnsl nlrlalelse
      541 rsnqhq
//
LOCUS       WP_010765753             421 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus moraviensis].
ACCESSION   WP_010765753
VERSION     WP_010765753.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..421
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45274
     Region          10..405
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(19..20,23..24,27,58,112..113,115..117,120,140,
                     143..144,147,225,228..229,233..235,238,262,266,329..330,
                     334,338,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 migkvnknil ylilgqvisv fggailrfal slyvldktgr adifatilai ssipvlfapi
       61 ggaiadrfdr rllmvlmdvt navlavvlff ilgltdsiam iglllfllsi vgsfdtpvvt
      121 asipllvkkd qleqinglvn avlsmsnvva piiggilysi lgaqklivgs avffilaaii
      181 esflripfek rpmesgvlst ltadlkdgfr evrnnriifn siliaalinf tlaaffivgv
      241 pvvlrvvlqa sdtiygigls vislstilga iftgvftkkl rinnlyklft lsglllilmn
      301 vglmfagspm gntigfiafi itgipigmim slisiylism vqritpkeni gkimatimav
      361 sqcavpvgqi iigflfkttt tnvffqvmiv avsvllvsgl cwylfknstd deigevgynk
      421 e
//
LOCUS       WP_010765758             381 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Enterococcus moraviensis].
ACCESSION   WP_010765758
VERSION     WP_010765758.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..381
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42026
     Region          40..366
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mfeklrqskl ffwsaellvi atlifvsski nfiftpigtf fstlfapvlv agflyyilnp
       61 ivnllmktnm krifailivf llliialvli lvsvipslvs qlsslasnmp dvfksveawv
      121 yqmaelpifk dfdlpkyidq ldisygniiq qfisglsssl gsivstvast tiiivtapfi
      181 lfymlkdgdr mipgvkrflp ekrqddivdl lgklnktlss yisgqaiecl fvatftvigy
      241 sligvryafl fgviagvtnl ipylgpyigl apavfvtvfd epfkallccl vvlivqqidg
      301 niiypnvigk slqihpltii lillvagnia gllgiflavp fyavcktivv hvfsmirkek
      361 vvkepeleia gelnspsske k
//
LOCUS       WP_010765760             144 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus moraviensis].
ACCESSION   WP_010765760
VERSION     WP_010765760.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..144
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16441
     Region          16..144
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mkivhtkdtm sdiyldavki rrqvfmleqg vpgeieidky eaacihfvly gekneviatc
       61 rllpledgli klqrmavqke frgkdygrli vegaelfske qgyntitlga qitalgfyer
      121 mgyikegelf ldaniehykm nktl
//
LOCUS       WP_010765782             148 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Enterococcus
            moraviensis].
ACCESSION   WP_010765782
VERSION     WP_010765782.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..148
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16650
     Region          14..141
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtktrfllpk enkdayqkia eldqigksgs iseqlqelik iyasqlngcv fcidmhskda
       61 lakgekmqri igltaweeaa fytvqeravl aftkevtlih qggvsdqtyq elqkyyseke
      121 igellvligt infynrigvt tllqpkvd
//
LOCUS       WP_010765792             304 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus moraviensis].
ACCESSION   WP_010765792
VERSION     WP_010765792.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..304
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34302
     Region          1..233
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkigiiglgn iaqkaylpvy sqlrdqatfl lstrneqtrk eisekygfne mvssteeliq
       61 agisacfvha atkvhgqlvk qlltagihvf vdkplseels evkeiqklaa eknlllmvgf
      121 nrrfapfvde lkavenknml liqknriase stvnfviydl flhvadtlvy lldddirhvq
      181 tkiieengvl krailqvete tttaiasmnl yagantetyq ltspegtlvl enltdltiqn
      241 qistqqksfg dwtttlekrg feqmvkkfiq avqtndgtql rqekiftshe lcaqmirkhq
      301 ehil
//
LOCUS       WP_010765856             236 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Enterococcus
            moraviensis].
ACCESSION   WP_010765856
VERSION     WP_010765856.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..236
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=26329
     Region          14..176
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mdyqtqmkik rlwkqplvty illgittlvf lglevsggst vqqvliewga msrkeivdyh
       61 eywrlftpmf lhigwlhfav nmvtlyyvgt qvesiyghwr ylliyllsgi sgnilsfalg
      121 sqgsisagas tslfglfgaf iilgrhfrnn paisfmvqry atfiginlif nlfsssvdim
      181 ghiggliggl lvatvlavpd rseefniher iisgiffifl lgvclvlgfk kfgllv
//
LOCUS       WP_010765864             304 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Enterococcus moraviensis].
ACCESSION   WP_010765864
VERSION     WP_010765864.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..304
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=33926
     Region          59..304
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mkksvkivii tvlsillvvv sagcyaaisf qtakeesesk lpkknqnftg deqtsdkelt
       61 vmvvgndsrd ddedqgrsdt lmvahydgkt kqpklisimr dsyvtfpdgs qdkinaayay
      121 ggaqmtkdvl ktnfdlpiny yvvmdfkefs diidelypkg vtidaekdin ldgvdilkrk
      181 qtlhgnsllq yarfrmdeeg dfgrirrqqq vmdalveqsk dlipvwelpq vagkmvgkid
      241 tnvptsllid lakdflsgkv kpleslsvpv egtwnfndyt esgsvielde pknaeaikaf
      301 mkdk
//
LOCUS       WP_010765935             275 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF92 domain-containing protein [Enterococcus moraviensis].
ACCESSION   WP_010765935
VERSION     WP_010765935.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487781
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..275
                     /product="DUF92 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=30139
     Region          13..262
                     /region_name="DUF92"
                     /note="Integral membrane protein DUF92; pfam01940"
                     /db_xref="CDD:460391"
ORIGIN      
        1 mtilfyklfl gfivgsligl fsyithlltk sgmiaivfva tivcgfgswf twgllilffc
       61 ssgcihlakk rinmtnldtv aekghtrdal qvlanslpai islvlfyytk nqlfligyas
      121 giagatadtw sseigilsks aprsiisfkp iqpglsggvs llgtiasslg sllisvvfwl
      181 lyrpddfstf pqifilivpf icgifnslvd sllgatlqak yrcsicgqlt enkqhhfhtt
      241 qqigglswlt ndwvnffsgc ltvlfswiil fyaqq
//
LOCUS       WP_010765953             202 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Enterococcus moraviensis].
ACCESSION   WP_010765953
VERSION     WP_010765953.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..202
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22555
     Region          4..197
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mtytlpdlpy aydalephid vetmhlhhdk hhntyvtnln aaidkhpelg tksveeliad
       61 mdsipedirt avrnngggha nhsffweima pnaggaptge ikeaidatfg sfdklkeefk
      121 taatgrfgsg wawlvlnngq levtstpnqd splmdgktpv lgldvwehay ylnyknvrpd
      181 yidafwnlvn wdevnkrfaa ak
//
LOCUS       WP_010765998             254 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus moraviensis].
ACCESSION   WP_010765998
VERSION     WP_010765998.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..254
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27894
     Region          2..240
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 miefinvskd ygtkqalktl slsikqgeif gflghngagk sttikslvsi iqpsngsitv
       61 dglalaehrq tikkkiayvp dtpdiflqlt ageywdliaa ayelddqqkq trlnelatlf
      121 dmlshqdetl asfshgmrqk tiiigallpd pdiwildepl qgldpqaafd lkemmkahaa
      181 kgktvifsth aldtaqqlcd rlailkkgel iyngsvddll aqspnetles iylkmagrqs
      241 dtqlverveg asye
//
LOCUS       WP_010765962             367 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus moraviensis].
ACCESSION   WP_010765962
VERSION     WP_010765962.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..367
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41833
     Region          149..353
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mmgkisrqml siyaacstfi vvlltlfsyf ysikqknwml ellqrkvfyi plifhmllis
       61 llvglstfll vsivqksqyg rieeklrlla rgsyespaiv kpvphasndq yieevdldil
      121 kvrtkllems kelqllnsrp qimdgetkee ileaerhrla relhdsvsqq lfaammmlsa
      181 lneqaqrsdt pemfrkqlvt vtdiinasqs emralllhlr pvslegkslr kgieqllkel
      241 qtkikieltw dvedvhlnns iedhlfrivq ellsntlrha kakelevylh qvdknvllrl
      301 vddgvgfdmn eqdnkagsyg lknirervag mggiikiisf kgqgtsveik vpvikeeits
      361 dqsnvsg
//
LOCUS       WP_010766022              66 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [Enterococcus].
ACCESSION   WP_010766022
VERSION     WP_010766022.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 66)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 66)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..66
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7035
     Region          1..66
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mektvtingm kcdgcvnivk enfekiagvq satvdlekks asvtsdreis nnelqnalse
       61 tkftva
//
LOCUS       WP_010766038             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010766038
VERSION     WP_010766038.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..251
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28295
     Region          9..249
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mfdlekvqsl nelemivyqy ilehmnsvpk ltirqlaadc hvststilrf cskmgfdgfs
       61 elkyflkked tekqqsfeqy ydatihvdsf lkqlnqqtyy dtlkpaitmi asarhivfsg
      121 igtsgilgsy gsryfanmgi naysigdpft pipqrgfent vaiilsvsge tsevikqasd
      181 fkrssakils itndehstis rladynisyy mpdersvyad pyinittqip vialiellah
      241 qaskelsekr v
//
LOCUS       WP_010766063             181 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Enterococcus moraviensis].
ACCESSION   WP_010766063
VERSION     WP_010766063.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..181
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19953
     Region          2..164
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtkygvivgs trknsyseai aksivkglpe nsevkfitig dlplynqdld enspkeytrf
       61 raevsqqdai ifvtpehnrs ipaalknald iasrpwgenv wdgkpalvas qsisgisgvl
      121 anhvlrqslt flnmptmqqp evyiansnnl fdenlqptnk gtedflksvg eqfssfvskf
      181 q
//
LOCUS       WP_010766099             226 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010766099
VERSION     WP_010766099.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24752
     Region          2..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msviearnik ksygrneskf dalkgvdlki eegesvaiig ksgsgkstfm hilalldkpt
       61 sgeillndqd vtsigkkeld ktrnkqfgfv fqqffmnskd tvlnnvmlpl kiggisnskr
      121 kemalealka velddkinnk annlsggqkq rvciaralvn npkiifadep tgnldsttgd
      181 kieqllfdln kekgitliiv thdpelaarc drqihvrdgl ivggne
//
LOCUS       WP_010766189             110 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Enterococcus moraviensis].
ACCESSION   WP_010766189
VERSION     WP_010766189.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..110
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12797
     Region          8..100
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(29,32)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkkiqtiqev itfiennpla flyvsqedcs vchalrpklm ellknyptie lreveadkvk
       61 eisaeylifs aptllffvdg keyiregkfv qfkklantid riysfeesri
//
LOCUS       WP_010766055             734 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus moraviensis].
ACCESSION   WP_010766055
VERSION     WP_010766055.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 734)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 734)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..734
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83303
     Region          21..722
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mnseyllaln dlnnqnpdyi etlfalcngh vgvrassilk gkttkgnpgt fingfydthp
       61 ivygewaygy aknhqtivkl pdirsliiei dgeksteadw rttqtdfqln mktgmleery
      121 eietlhgkif slslcsflsy sqaevsvfhy tiealnfsge llitkqiafq egntnedgti
      181 dprvassksk lgivplndew ievktefseq svllsqvmqt adgvdeiggl avskrvfvqk
      241 nqavtltnyv vlsnplttes rkierekdkl ttvkrhlefn qlakehiqhf sefwqasdie
      301 itgdpilqkg irfnlfhlyq nagrdgltnf aakgltgegy eghyfwdtem yilpffiytq
      361 pkiakqllty rvsilpkaqe rakemaqnsg alfawrting eeasayypag taqvhinadi
      421 ayafqlyerv tgdhqfiaes gaevifetar fwlnygswig nefcingvtg pdeytalvnn
      481 nyytnkmaqn nlsyavtlaq rlnsvkeaew stwqqaaegm klpydhekql ikqddtffek
      541 akwpfeetpk enyplllhyh pmiiykhqvc kqadallaem lfpqdysveq iqrdyqfyee
      601 vtthdsslsr sifsilasrt kqqdkaysyf mdtalmdltd lqgnakdgih aanmggswls
      661 iiygfaglss tgqtiqlenh lpkeieglaf klnihgtlvk vkmdkkelkv tllesneqls
      721 ikqlsenkam iain
//
LOCUS       WP_010766190             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus moraviensis].
ACCESSION   WP_010766190
VERSION     WP_010766190.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..255
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30291
     Region          7..99
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(8..10,24,41..43)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(55,58,62..63,72,84,88,94,98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mekeklltvg qvaeimnlpk skirywddmn lltssrnrqn gyrlfdmedi ltisdidfyr
       61 rldipinkmt nlyrkspeel wtildetetr vtaelaelkk kkqgikrrkd qllslielke
      121 kefidepldv eriipidlkd pdelqtyidn psslviysds nyekeltygf avtpkefmee
      181 etiwqqseqt npqykqfllt iksdsplenn fkfikeklek hgyqtgtmig rfimtaeded
      241 gfyrdyyktw vevsk
//
LOCUS       WP_010766435             292 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Enterococcus moraviensis].
ACCESSION   WP_010766435
VERSION     WP_010766435.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..292
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=31707
     Region          1..281
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mkfskrqiqd tlyvtigsfv lavsinsill pnkivaggan gisvvinylf ginpalvlya
       61 inlpllllcf lllgkevgik tiygsliypf fvgitthlpv lthniflati fgglltgigl
      121 glefrgnast ggtaiisqiv nkyfkislgv silfvdgivi lsalfvfntd tvlfslicly
      181 ligrvvdmvq vgfvrsknvl iispkyaeik ekilvdmdkg ltmipieggy qknpsmlmmt
      241 visekdfaki kenvmaidee afivsmnase vfgrgfslkk iaedygiesn nl
//
LOCUS       WP_010766238             198 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus moraviensis].
ACCESSION   WP_010766238
VERSION     WP_010766238.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..198
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22259
     Region          3..129
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,67..68,71)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(66,110..111,113..114,118)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(72,77..78,106,109..110,113..114,117,120)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95..97,106..107,110..111,114,118,121,125)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95,111,114,118,121,125)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(119,125..126)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mkiigyartt itdndldaqi kvlsdygcde iyheafdvtn dkhliselet vlgslaagdt
       61 lvicrlnrlg rstrqltelt qtfkgsgihl vsldeeidtr hpvgeiyfkl mnelakmecd
      121 likertlvgl nnarkkgkig grpkidgrtv kkirhlyhek ketiqfissk cnvsvgtcyk
      181 yinlseeevl aisqdnkn
//
LOCUS       WP_010766499             256 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            moraviensis].
ACCESSION   WP_010766499
VERSION     WP_010766499.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..256
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28968
     Region          1..254
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mkasqgdvfk rrenilerlk keqhltvtel anffnvsavt irrdllflek kkmierfygg
       61 vklihespls qplmheqkpf pvasfvekfs tfmpnraqlf vgsghfskei iyalsffeis
      121 iltndiraia idhpkkkavi slsggelere tqalvgdfai hsinkiqadl ciieaagfnt
      181 hevttktlne sfiyrtmiqh tkgpkivyts afnletvssf midktflfda lytdstispd
      241 ilthyqshgi pihvls
//
LOCUS       WP_010766444             398 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus moraviensis].
ACCESSION   WP_010766444
VERSION     WP_010766444.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..398
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43182
     Region          5..397
                     /region_name="ryptide_ex_MFS"
                     /note="ryptide export MFS transporter; NF041056"
                     /db_xref="CDD:468984"
ORIGIN      
        1 mnknkafnkl iigqmianig dtiytiaivs svftltnsal aasivpviit gsmvlsgllt
       61 plivvrvsls kilqisqlck tlilaglavy lqvaiehldl tilyvfivgi afldgcaepv
      121 stalipyyva eyyliransi fstmlqvvsi gswaigssll iifsvtnlvw ldvglfllsa
      181 iilwllpqva kgaesernew enfimgwqgi rkcslvrvvv gmdiletian tawvsaivlv
      241 yvkevlhvse swwgyinaty fagamvgsvi vmrnsdwinq hkskavimgs lfggvvtflv
      301 apgwnpvfil icsvfvgifs qiknipqata iqqtipkdml apiyaamnvl ytgtfalssv
      361 smglisesfg vqtvfgvsgt llfivamiak kkrtlfde
//
LOCUS       WP_010766473             562 aa            linear   BCT 01-JAN-2025
DEFINITION  molecular chaperone HscC [Enterococcus moraviensis].
ACCESSION   WP_010766473
VERSION     WP_010766473.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10178812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..562
                     /product="molecular chaperone HscC"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
                     /calculated_mol_wt=62327
     Region          4..344
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mgiigidlgt snslvsfwdg eavqliknqf gqtltpsvvg iddngdilig aiakerlish
       61 pqltaatfkr fmgtdkqydl gehtftpvel sslvlrslke daeaflkqpc tevvisvpay
      121 fnnvqreatv eaaklagltv qnliseptaa amaygfhkea dqsilvvdlg ggtfdvslle
      181 mfdgimqvea isgdnhlgge dfthvivrdc lsehkltgtv lsattqsvly qkaellkhal
      241 ttqeagsfef dweehtysyq lnqeqykvlc epllarmrqp igrvlndgqi tiqdidqvil
      301 iggatknsiv rnyfarllkt ipytqinpde avghgagiqa alkqdrsmvn emiltdvcah
      361 tlgvdsvsqt stgyiegvfs piiernttip vskmktfytl rdnqehvnfa iyqgenpmak
      421 dnlkigelei kiprapentp idcrftydsn gllevivtdq sghskqliie sapgkltseq
      481 meesfaklna lkvhprdrae nrlllarler lyaettglqr eqiqallfhf rsvlekqeei
      541 ltkrtaadvt qqlnelekdl wl
//
LOCUS       WP_010766372             235 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus moraviensis].
ACCESSION   WP_010766372
VERSION     WP_010766372.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..235
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27586
     Region          1..230
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mkipkyqqik ndllnkiksg efehgdrfys eneliklyna ssitviraiq elasegylvr
       61 yqgkgtyvsr srkrklveft dieifagkte tvevisivee sdprivkeln lqpdqtyrki
      121 trirkvdaia filhftfmpn qfinhdvtel syydsiyerf ktefgihmyd ehatetneil
      181 fptpkkvakl lsstesepvv fqmkkttlqd gtvaeyvesy kkwdyykief stykm
//
LOCUS       WP_010766575             175 aa            linear   BCT 01-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Enterococcus moraviensis].
ACCESSION   WP_010766575
VERSION     WP_010766575.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..175
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=19349
     Region          7..175
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mketsrrgid wgsmilgilf vltalvsfqd pagnliaivm vfalfailkg ifeifvrnrl
       61 keltgykaya piilgvidii igvyflfnln igvaalpfif avwfildsvf glfaldlaks
      121 vspgyfwftl vvdilgiilg vmllmnplss altlsflvgf yfmlfgithi vyafr
//
LOCUS       WP_010766585             221 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Enterococcus moraviensis].
ACCESSION   WP_010766585
VERSION     WP_010766585.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..221
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=25693
     Region          75..173
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mfkylkeyvd fsvrvndyis timldneisc esynysriwk lmqsqgavir gfqfndiase
       61 qiaglliqdp lettigfnre ldeksknfii sheithylfh mdkqnqlfyd tvrdirsceh
      121 kqlqefqani gasiilvpdr vlfyslkkgw dlsqisdsfg isedhlvmrl iqmmqanlgl
      181 sfrtakkhtd lfcgtgrvts vqlatkleyq ierpnyftei v
//
LOCUS       WP_010766678             321 aa            linear   BCT 01-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase [Enterococcus
            moraviensis].
ACCESSION   WP_010766678
VERSION     WP_010766678.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..321
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35074
     Region          2..310
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 miltvtlnps mdsiyftdtf vlgamnrcsn pikavggkgi nagrtaailg gkvttmgvla
       61 gkngelirhe leqepfktkf isifgesrna vtvmdreknq teivelgpei tadtekiild
      121 tildfadeqn egpiialcgs antkndylyq eyllqlrdkl gtkvkiltdi sgkqlknvln
      181 nsvkpyfikp niqefsdlid lpltskidvi nnlnhpmlke vpfvliscgg dgavakyhdq
      241 ifdviiptid iinptgsgda tvggvafald qnfsieetlr yamacgmsna leqavgyvsi
      301 envetlknqi ilkeieqmfh v
//
LOCUS       WP_010766720             411 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus phoeniculicola].
ACCESSION   WP_010766720
VERSION     WP_010766720.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..411
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=48068
     Region          <150..386
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mainetkngt yrvrkkypld valllelknp yfdkifktmk eakeaeldfe nkiqelrktk
       61 dktifelgge mlfrdfyesi wldaysngst sshptpptkv tinntkdvfr lhilpmfgry
      121 slnylnqnkq fvarkmtvka reyanfktlr syvnqifdla eeydyisynr lsktlkkika
      181 lkkiqlannk qkedkylsee elikwikaie edhgeglltt qdytlfwtty llsdrksesy
      241 alqwkhidfn nnqiyleqal dklgnvkstk gnkktiihlp vklkkilliw kseqkkelkt
      301 leieqtdqqf lftycdmhgn inkcvhtdfl nyrmksvrkr hpelkpasph klrhtsatla
      361 kkygmtvedi snglthsnie ttgtylnndk vvpltpadyt lnhlmqnagg e
//
LOCUS       WP_010766686             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Enterococcus].
ACCESSION   WP_010766686
VERSION     WP_010766686.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..253
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27809
     Region          2..251
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mariisvanq kggvgktttt vnlgaclayy gkkvllidid aqgnatsgig vrkpdvatdv
       61 ydvlvneepi knviqqtsre nldivpatiq lagaeielts mmaresrlka aieeindiyd
      121 fvlidcppsl ghltinafta sdsilipvqc eyyaleglsq llntirlvqk hfnpdlrieg
      181 vlltmydart nlgaevveev rkyfrekvyd tiiprnvrls eapshglsii dydprsrgae
      241 vyqalakevl dne
//
LOCUS       WP_010766753             491 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Enterococcus phoeniculicola].
ACCESSION   WP_010766753
VERSION     WP_010766753.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..491
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53049
     Region          14..407
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(21..22,25..26,29,60,110..111,113..115,118,138,
                     141..142,145,239,272..273,276..278,281,309,313,365..366,
                     370,374,390,393..394,397..398,401)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 merktnvtlv tisifvatfm taiegtivtt amptivgslh gieimnwvfs iylltnamlt
       61 piygkladki grkpvflfgv lvfmigsslc gfsqdmmtli iargiqgvga gaimpvalti
      121 igdlysiekr akllgltsaa wgiasvvgpl aggfivdtvg whwiffinip igivlmgliw
      181 yfliekkqvr etkktdilgs islmlvllml llafqflgdq gvsgtviglf igsilslvlf
      241 iwaeknaedp visltlftnr vfvvvnlvaa lvggflmgid vyipmwmqgv lgmsaaiggl
      301 vlaplsilwm agsfiagrwm gkmsihkllf igltiifagg lglvfmpiha hftwflviss
      361 itgvglgitf ttttvgaqss vpedqlgvat sfntlartig qtimvsvfgi linsvtkqel
      421 vekqltkdsd imnklvnpqt akelpidllk plreilyngl hrvyfvgill iiitlvltif
      481 mgkqgkgkvr n
//
LOCUS       WP_010766765             240 aa            linear   BCT 01-JAN-2025
DEFINITION  pseudouridine synthase [Enterococcus phoeniculicola].
ACCESSION   WP_010766765
VERSION     WP_010766765.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..240
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=27304
     Region          1..229
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrldkyladv glgsrkevkv fikkgnvqvn gevvksdkfq vkekvdiitf egekltyqky
       61 fyyllnkpqg visatqdnyd etvldlfsde ayredlfpvg rldkdtegfl litndgvlsh
      121 qllspkkhve keyyacvsgi mtqedvelfe kgliisgeeq tlpaqltivs vdkekqtsei
      181 qlilhegkfh qvkrmvaavg kevtylkrvr mgnlplpkdi elghyrqlse eeleklkgng
//
LOCUS       WP_010766769             252 aa            linear   BCT 01-JAN-2025
DEFINITION  WxL domain-containing protein [Enterococcus phoeniculicola].
ACCESSION   WP_010766769
VERSION     WP_010766769.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10617615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..252
                     /product="WxL domain-containing protein"
                     /calculated_mol_wt=26024
     Region          26..247
                     /region_name="WxL"
                     /note="WxL domain surface cell wall-binding; pfam13731"
                     /db_xref="CDD:433439"
ORIGIN      
        1 mkkttiltag iilfssllga tttfaadggs ydskgeitfk agtdktdpld psnpdpdkpv
       61 tpvdpvdptg pkpgtngpls ldyassfqfg eqsistvdkt yyaalqtfsd gtadgpnyvq
      121 vtdtrgtqkg welsviqgaq fetatsdvle gaklsfangk avsnlqegln etesqaitpv
      181 ataavtlvpg aksvimtagd kqgvatwlyd lgkdateaat avslkvpgks vklkdaystt
      241 ltwtlsdtpt ap
//
LOCUS       WP_010766850             557 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010766850
VERSION     WP_010766850.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19448763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..557
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=64911
     Region          9..124
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          232..545
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mattvtikdl lklkefqtad iistpvslkk svgvvtimdl ptidewlked ellimgfymd
       61 thfnrsfiek lgnrnaagii tkkkfkknit pdlvnalqqa nipvlivedr yswsditapi
      121 qsliirhqtt vlketerfhq amihslsnqh sfhdlcttlh hmtglslait deqfrildys
      181 ndfdwsdyvt dlishtprnw qtiavtpegr rkdgfieqrs twpntqlrlf llpvyqnqql
      241 vnylvvkqpa svdslpldll aklesfqsiy llkkafytef qkanshyqnl ileelirmdt
      301 pndeerkqls vtlgvhlekn yrvllvknln eddssltier ndryiafrnn lkqqsfmndn
      361 ilvfsrkdyl vfllaesfkq tdlflnqlvd yldsynekas walgisdlnp ywqlhtgwke
      421 aqqalhfirs ntssqriqyy qnlgilkmfa ndqgqlntly vqqmlsdyla pilandakqh
      481 sqlyktletf fetnfshist skilyihknt lrarlkriee llkidlkntd hlmnihialk
      541 lyqmmdgasc qkffdlv
//
LOCUS       WP_010766901             257 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus phoeniculicola].
ACCESSION   WP_010766901
VERSION     WP_010766901.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28852
     Region          13..255
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mfssnnknka lilskvnvra gkklilkdis ltlepqtiyt vigpsgtgks tlmnvlsgls
       61 svdsgqllyg eqayqpkdhv lglvpqnygl lpwetawktv tsnvkisqkk rkltkedeek
      121 ihdlframnl esvkdsypsq msggqqqrvs itrafgvdgd vllmdepfsa ldaftrekiq
      181 glfldtwknh pattffithd ieealllghk ivimkgqpge ihqimdspyn qietleekrq
      241 qsdfyervna lreeiqa
//
LOCUS       WP_010766910             277 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010766910
VERSION     WP_010766910.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 277)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..277
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29865
     Region          6..265
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 malfsyefmr laflaaifis giapmlgvfl virrqslmad tlshvslagv algfflnwnp
       61 dvttliivii aaiileylrm iyrtyseiai ailmsgglal alvlmqfssg nsatsiqsyl
      121 fgsiititkg qviflgslfv viaalfflfk rpmyvltfde daahvdglpt qwmsmlfnvv
      181 tgvaiavmip iagallisai mvlpaaiglr igksfnavia isvvvgfvgm lsgltgsfyw
      241 etppgatitl vfiglflvvn iskrliigiq rkkhlek
//
LOCUS       WP_010766959             206 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010766959
VERSION     WP_010766959.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..206
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23156
     Region          11..194
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mihysaemlt tkqhykfltg siiprpiawi ttknldtsvi naapfsyftv askevplvti
       61 sinrknhelk dtaanllknk qgvihivnde vlyamnataa slsseesels ltnvtladsy
      121 svdvpgikea pirmevrvhq ylpitdhqke visdlfvlev ldyyfsdsvf dkereyilpe
      181 klqpvsrlag nfyghlsevi everps
//
LOCUS       WP_010767080             683 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010767080
VERSION     WP_010767080.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 683)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..683
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77963
     Region          <30..169
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          <40..>360
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mlyrlasrsf mqqlriyfgy flsmsiavmi yysfsamtyd qpllrrasqd vrienflsmg
       61 simvilvilf fmvsanrffv nkrykevgly rlfgmsklri sllffwetmv lgsislvvgi
      121 ffgivfsklf smilvkamdl svgsdffisw psiwntivvf ffilllvsvr stlmifqyql
      181 gsffkqknsa lakkmrvrgw tflfgflgia mlltgyglal fignllpkiv latdhygwiv
      241 sfpllifflc vvgtylffgq tmkviyylig kwrdyvyrdl nilslgnakv hlakswrtms
      301 wvaiilgisl asiggtaflv svamktvqvd npasfqvree dvstlkevla endadilsev
      361 sltykvvgae iktaienetn tvmtlsnlis ekdyesfkki ypelpeisll dekhvvilds
      421 lqtimkgfdr yesdilfsgn iattfqkrlp dylgdsllry mglsgvtfvv sdevfketkg
      481 mdyrivsinv sakneealtq gvnevleqsw gneiissyhi tesgiegevr fstnedanan
      541 essylrlnls srypnvraar rqmgiliyva vfigmismia tgcilmlrqf seaesekeny
      601 kllkkmgipr kqlnrliyqk nagvffppmi lgmmhayfai yvfsefaaea sywlaylfcv
      661 llmvvygffy lltilmygki lek
//
LOCUS       WP_010767193             306 aa            linear   BCT 01-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010767193
VERSION     WP_010767193.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..306
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33670
     Region          1..278
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mgiidkvken kkllrfiett qkrildsemg vtsvvvayyl llsifpllia vgnilpylki
       61 dpntvlpyvk evmpsqiydf lgpaiqdllt qssggllsvs aiaalwsask sinalqtamn
      121 kaygveprkn filvrllslg vivlfmvaiv gvvvifglgq milsslqpif efpthiidtf
      181 qtlkwpvvsl alffimmlif livpnakvti rsvipgavfa tigwmllaqv fgiyanyfas
      241 kvsgyqiigs fivlmlwlnf satiiilggi inavvqeyls gteiearqsl isqgikkfka
      301 ifklkr
//
LOCUS       WP_010767211             200 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Enterococcus phoeniculicola].
ACCESSION   WP_010767211
VERSION     WP_010767211.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..200
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22428
     Region          4..196
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mtytlpdlpy aydalepyid vetmhlhhdk hhntyvtnln aaiekypelg ektveelisd
       61 msaipedirt avrnngggha nhsffweila pnaggaptga ikeaidttfg sfdklkeefk
      121 taatgrfgsg wawlvlnngk leitstpnqd splmdgqtpv lgldvwehay ylkyknvrpd
      181 yieafwnlvn wdqvnkhfsa
//
LOCUS       WP_010767236             458 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010767236
VERSION     WP_010767236.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..458
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51201
     Region          23..428
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mnadpdsqsl laqvlllvvl tlinaflaas eiavvsinkn rveqkagdgd vksqkllkil
       61 qdpnnflsti qvgitlvnil sgasladtls vklapylggg sagknianii vlailtyvsi
      121 vfgelypkri alnkseevak atsgfirgig ivakpfvwll sastnllsrl tpmefddeds
      181 kmtrdemrym letegvldnd elemlqgvfs ldtkvarevm vprtdafmid indtiqenin
      241 evlsenysri pvydedkdkv vgvlhtknll kaahingfdn ldlrqiiqep lfvpetifid
      301 dllyelkktq nqmailldey ggvvglatle dlleeivgei ddesdevekl yekvgenefl
      361 vqgrmlidef nevfetdlhm sdvdtmagyl italgtipde geklsfdvdn itliseemeg
      421 srvlvlrvff hdpedkevep eeerrlfrke fdedeprr
//
LOCUS       WP_010767218             225 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Enterococcus phoeniculicola].
ACCESSION   WP_010767218
VERSION     WP_010767218.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..225
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25994
     Region          <20..224
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mlreekkeyt nelinylqps pfflffkraf diiggflgml lfflaavilw miyffskknk
       61 gplifsqtri gkdgkkfdiy kfrsmvvnae dvlkqndely keyvncgykl degkdprvtr
      121 lgsfirktsi delpqfwnvl kgdmslvgpr pviqeelsey gekvelflsv kpgvtgvwtv
      181 sgrsdvpype rtdlelsylk dlslrndcki liqtfivvlk kegah
//
LOCUS       WP_010767312             503 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010767312
VERSION     WP_010767312.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 503)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..503
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56237
     Region          179..426
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnflqraiss vtrrkgksii lflvifvlgn viagaiaiqq stsnvekdvk aklganatve
       61 fdydtfqkdh kdedeatlvy pdnpkldvye kvgklsyvky fdyntysyfn srklksfdyq
      121 seengdegst ritgnrgley fnlkginypk ildieqkkis lvegtvfsdk dvkdgasvav
      181 vgkrfaeknn lslgdqllit atnedqlgfd segnevevkp ediksvdypv kiigffepvk
      241 sekepkknsd eyynqmnsst elentiylpn ktvseyskkq nelmfsgddt megdmgeyys
      301 payilknpgd teafkeeaep llpkyyvvra ssdqydeigg smkkmgqisk yvviisviat
      361 lliiglvvll fmrdrkhelg iylslgetrg kvmgqvliel liisalalvl slvtgnllgn
      421 mvskslmnsd llqttndnmm yyssvydsvs snltaddvtg aykvtfsvay iftyllvglg
      481 tvllsalipl myilrlnpkk imm
//
LOCUS       WP_010767356             116 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010767356
VERSION     WP_010767356.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..116
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13848
     Region          9..>94
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mahqttdlrv lrtkknihqa misllteksf dkitindisk kadisrgtfy lhyqdkyelv
       61 ekyqeellek aqllfeitsh enrqeffvvm lrffqqkgnc cpccypttvl rkykyr
//
LOCUS       WP_010767359             243 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010767359
VERSION     WP_010767359.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..243
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=27472
     Region          1..>221
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 miqlhhvskd yqqinalddl nfqieqgeiv giigksgsgk stllrilnli etptkgeiyf
       61 gekeiqtltk kqiqqtkqti gmifqhynll snltvhqnva lplkllgktn hekvdelldf
      121 vgmrmksqyy paelsggekq rvaiaralvr nptlllcdep tssldeente eiirllkrth
      181 kefsptilfv shelssvktl cervlvlesg ritdeffntp kdvsspvlsy aerikrgvkd
      241 vrn
//
LOCUS       WP_010767379             303 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus phoeniculicola].
ACCESSION   WP_010767379
VERSION     WP_010767379.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..303
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33608
     Region          6..223
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 maksvlqikn lskrvgkkti irninfevye gevfgllgpn gagkttiirs ivslisrtsg
       61 tvlikgmdvs vdfkktisev gaiienpefy mymsgmenlk qfarmsrkni sdeeinkiva
      121 kvkltnainq kvktyslgmr qrlglaqali hnpsililde ptngldpqgm aefreiirev
      181 skqgtavlis shllgeiqqi tdrfaiiekg elthietmsd vmedshgkfv fkvsdvnkai
      241 ellrmkeida vevgsqliev ttvetqipdm irllsaeldl yavsaktssl eerffelteg
      301 gel
//
LOCUS       WP_010767390             481 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Enterococcus phoeniculicola].
ACCESSION   WP_010767390
VERSION     WP_010767390.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..481
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=51773
     Region          5..479
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(62,64,68,71,75,108,111..112,121..128,133,136,139,
                     232,236,239,242,244,417,419..420,422..423,426,429..430,
                     432,434..437,446,450,452,466,473..478)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(148..151,159,174,177,207,224..227,230,248..250,282,
                     382,384,410)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(151,248,279,282)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mveilknyin gewvtatatq tedvpnpatg eimakvpisn svdfekavea adaafegwsn
       61 tpvprrarim fkyqqllidh wdelaeiitk engkslaeak gevqrgienv efaagvptlm
      121 mgeqlpdiat gvesgmyryp igviggitpf nfpmmvpcwm fpmaiatgnt filkpsertp
      181 llanrlaelv keagfpdgvf nivhgahdvv ngilthekvk avsfvgsqpv aeyvyrtaaa
      241 ngkrvqalag aknhsivmpd admdlavkni taaafgsage rcmaaavvva vgeiadelvd
      301 rlktaademv vgnglepgvf lgpvireghk ektigyiesg vsegaklvrd grldkevsdk
      361 gyfvggtifd evkpgmkiwn eeifapvlsi vrvesleegi aianqsdfan gaclytdsas
      421 avrtfrtkid agmlginlgv papmaffpfs gykksfygdl hangkdgvnf ytrkkmvtam
      481 y
//
LOCUS       WP_010767417             453 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010767417
VERSION     WP_010767417.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 453)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..453
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50261
     Region          166..445
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 msffkrslms iwqrkgrtsl flglffivfl lilagfaiqe saekskvdar kqlgaevrlk
       61 tdddkltqlv lsgkttmepl tkemveqmsd lpqvknssis gtvnmaksel esvtpenese
      121 mtlspppgye mpafeikgtn nmtkttdfmn hdakiiegep indksaknsa vveetfaknn
      181 hfkigdtftl rgvskeeqek eyrlkivgiy ksekvlaefe kmfaasqpen qifvdldtfl
      241 tmgkqarisd atfylndplk veafvkeaet klptednifk ldahtdqyeq migplekmsa
      301 fssimikiiv vaggliltfl sllsirdrkk evgillalge nkgkvilqlv teiiligiva
      361 fglsfavvgt sgqtisnvml sqqvekvest lqedeygqed ssiepvdkmn ltidknvvsk
      421 aaalgflliv lttlipsmmi aktdpkdlfa qke
//
LOCUS       WP_010767422             225 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus phoeniculicola].
ACCESSION   WP_010767422
VERSION     WP_010767422.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..225
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25192
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mirleninky ydvgeekitv leninfsies gefvaimgps gsgkstlinl lgfidrnfsg
       61 qyyfkekeia dfkdnelski rnqsvgfvfq nfslienltv fenvelplly nganhnktke
      121 evksalkrvg lankmsqlpk qlsggqqqrv aiaralinqp sfiiadeptg aldthttsdi
      181 mqlfkqlnte gvtiilvthd petvvycdrl lkirdgkmve evlqs
//
LOCUS       WP_010767423             401 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010767423
VERSION     WP_010767423.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..401
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44373
     Region          7..401
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkqyilwrta frsifknkrr sfltmfgiii giaavitiva lgngfkrnil anttsadetg
       61 qtkyvnikyn dmenlikdna gislsdkdmv anlpevkevn yyksnkneln qsiefydknt
      121 kltvtiqtpe qttlpiiegr qldladsdgm nkvvvldevv akqlygsskn alnkgfevkg
      181 qvftvvgvta ntsgeisvdn yeplvyfpkk thnhylekie dhstlsikfk eqekseeafe
      241 kvltqlnvng esrligeyrs ydpndeikql gsildqltif isavagislf iagvgvmnmm
      301 yisvsertke igirralgan aksikrqfly egiiltlsgg ligyifgmli ayvassalpf
      361 svrpdvttvf isvgtsalig ilfsylpasa askkelidil k
//
LOCUS       WP_010767427             105 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010767427
VERSION     WP_010767427.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..105
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12301
     Region          5..100
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mratsqfkkg alemcvldlv skrdrygyel tqivnsffsi tegalypvlr rlvkeeycyt
       61 ymkespdgps rkyysitksg ekylrtlqad wkefivevnk lmeee
//
LOCUS       WP_010767475             249 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010767475
VERSION     WP_010767475.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..249
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27573
     Region          1..240
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mltderkqri lqlleqhsiv ksqelmlsfd vsestirrdl qeledeglle rihggakksq
       61 klsyeqtmse ktfkniqekk qiatlavnei ddgdiiylda gsttlemipl lknksitvvt
      121 nsvqhasklv elqlptvilg gaiklateav lgstsiqqls qlrfnkvfmg mngahlefgy
      181 stpdleeaal kklaianaee afvlidhtkf nkvtftkvas lkeatiitdn cdaayledfq
      241 sittvkeal
//
LOCUS       WP_010767637             148 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Enterococcus phoeniculicola].
ACCESSION   WP_010767637
VERSION     WP_010767637.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..148
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16800
     Region          4..141
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 msntmvkdai sklkhaniri tpqryailey lienrthpta deiykslehq fpnmsvatvy
       61 nnlrlftkig fvkemsygda ssrfdfsstr hyhaicqscg kivdfhypgl edvemaasel
      121 tgfeinehrl elygicpdcq aaeseeak
//
LOCUS       WP_010767653             148 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus phoeniculicola].
ACCESSION   WP_010767653
VERSION     WP_010767653.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..148
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16765
     Region          3..132
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mdviirkaes tdwqdinrln tedlgyvvse tqtkkqleki laddtqiifv aaykstvqgy
       61 vhlsnyetly fstlknvmgl avssrfqgnk lgsklmkkae ewakaqgasg irvnsgetrv
      121 gahkfyeaig yeskkmqknf fkyfqqnd
//
LOCUS       WP_010767655             147 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus phoeniculicola].
ACCESSION   WP_010767655
VERSION     WP_010767655.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..147
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16999
     Region          13..144
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mnlvignekw iqaaafylry qvfvleqkis akeefdrldd dfatlylvyy nksqpvatlr
       61 yqkidektfn pdrfcvsecy rnqgigkqll leaekkaane gcttsvlsae vtaqafyekm
      121 gyrvisptym edgilcvkve krlnrye
//
LOCUS       WP_010767662             388 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Enterococcus
            phoeniculicola].
ACCESSION   WP_010767662
VERSION     WP_010767662.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..388
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43209
     Region          25..303
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 miqyllqkiq knspinstag rtkagvlagi lgllsnsilf gskltigfls gsvsimadai
       61 nslsdtassv ltlvgfhisa kpadrehpyg herfeyisgl fvsiivtyvg fqfldssfqk
      121 ilhpqnlsls piifivlils iaikiwqgam yrtigksiqs ntlnataqds lndvyttmav
      181 lisagvewgt gwridgyvgf iiavyilysg iqmikgfvdd llgsrptaee iekmkqrlss
      241 ntsilgyhdl lihsygpskr fasvhievde swdlnyahti idtiekefke tlgvdlvchl
      301 dpvalhdrny trlslilkei lakidgnlrm hdfriehate pkilqfdlav pakprysdee
      361 lkqliqsnlq qqvgkytldi tfdhnyll
//
LOCUS       WP_010767690             219 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Enterococcus phoeniculicola].
ACCESSION   WP_010767690
VERSION     WP_010767690.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..219
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24310
     Region          <105..169
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mpfegqwlvg ntpanqipsh gttlfgtsya fdfmavdrkt rtapskswrt ffgveqpelf
       61 ysfgksvfsp iegeivsihn geedhvarrs wftllpyvls qssrirkghq aiagnylvik
      121 akevdlfvai vhlqkdsilv kegqsvtegq hiancgnsgn stephihiqa mntldfsngs
      181 giplffrhft qrekeqikkr tnafpnsgsv vssekipae
//
LOCUS       WP_010767699             372 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010767699
VERSION     WP_010767699.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..372
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=41362
     Region          131..372
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 msrmdryknl hdesetvnnk ksfsprkerq qkepvesaae eqlsapqtkq rkkatffhts
       61 nspekekkpk qkksrkkhkg lrilgllill vflfsggmfa ygkysaehdt slpkeeletf
      121 ngvtsadksn nilllgsdsr ggetgradti mviqldgsgk kpkmisfmrd tfvtipgvgd
      181 nkinaayafg gadlvrqtll dnfgidckyy akvdfqsfek vidslfpngv qidaekdmss
      241 hlevpikkgp qkmngltllq ytrfrmdeeg dfgrvrrqqq amsaifsqmk npltlinlpl
      301 asgkaigyts tnipttfllk nsfsvlkgag gidrlsvpve nswsygnsdy agsilvvdke
      361 qnkqaiqtfl an
//
LOCUS       WP_010767738             319 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010767738
VERSION     WP_010767738.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..319
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33868
     Region          6..302
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mikqmigidi ggttiklali dvygeihkkw qiptniteng rniptdivrs iqqtmleqnd
       61 qqaeiigigi gvpgpispdg qivvravnlg wedmplksai ekeldipvvl lndanaaalg
      121 emwkgaargk snlvfvtlgt gvgggiilng kvingvhssg geighipiys qeqrtcgcgn
      181 tncletfasa nglvktmqnm meenqenlsa vdvftwieag dqkamtalti tvnylgqaia
      241 gimntvdaee vviggglsga gdalliplke kidqfifpai rgnynvskaq lgndagiyga
      301 vysylssnei ltmeetllr
//
LOCUS       WP_010767853             190 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010767853
VERSION     WP_010767853.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22033
     Region          8..140
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mafsevekkn irerlltnce eswstfgykk tsvdelcqka giskgsfylf fdskedlfcq
       61 vmirvqerli aitknslgek ptkydlantl klvfreyskv pfitetqspd fvmfinrlsp
      121 dklkeleehg nydiqdiire sglvyrveeq kglaslalif rpigasqqlp weyldvfdfv
      181 ldtliekife
//
LOCUS       WP_010767920             829 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Enterococcus
            phoeniculicola].
ACCESSION   WP_010767920
VERSION     WP_010767920.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..829
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92853
     Region          1..813
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mnelfterar mvltisqeea kyfkhqsvgs ehlllallle tegiagktlr qmglneqdvr
       61 eeiehligyg tiksypqgiy lpysprakqi fayaadeakr fgvpaigteh illgllrdee
      121 ilasrivmnl gmdlskmrql lkrkmgvtdt kgssgsrrkn gqaknqtvqg tptldslard
      181 ltklardgkl dpvvgrgsev krliqilsrr tknnpvlvge pgvgktaiae glaqrivnre
      241 vpeemqkkrl mmldmgslva gtkyrgefed rmkkvieeiy qdgeiilfid elhtligagg
      301 aegaidasni lkpalargel qtigattlde yqkyiekdsa lerrfarvqv deptpdeaee
      361 ilmglksrye ehhhveited alraavqlsv ryinsrqlpd kaidlmdesa akvrldkade
      421 ptelaklrnd laklsaekda airkqdfela aqirkkekrl dkkldaliyv eeknqtgyen
      481 rvteedvasv vsqwtgvplq qlekkeskrl leleetlhkr vvgqdeavka vsrairrars
      541 glkdpqrpig sfmflgptgv gktelakala eamfgsedsl irvdmsefme kystsrligs
      601 ppgyvgydeg gqltekirqk pysvilldev ekahpdvfni llqvlddghl tdakgrkvdf
      661 rntilimtsn igateireek nvgfnvkdvt kdhgamqkri leelkkafrp eflnridetv
      721 vfhslnkeei hsivkimsqs ivkrlaeqdi qvkitgaaid viskvgfdpe ygarpirral
      781 qkevedrlse allssqihfg dnvtigatkg kitvsvkskk evkeevqfv
//
LOCUS       WP_010768050             195 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768050
VERSION     WP_010768050.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..195
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22780
     Region          26..132
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 makrfseedi leikkklksa cemswrtkgy kqtnipsltk evgistgsfy liyktkeelf
       61 vevlqhvqst mlttwaryie eadsalegfk qgmnwlyhey rsypalydfn speydlflak
      121 lpkekirele easmsvfskm ivhsklrlkl seeetiniis tilflslier dtlkatektf
      181 tflmnhaldd lfeev
//
LOCUS       WP_010768052             240 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768052
VERSION     WP_010768052.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..240
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27423
     Region          1..232
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 maiakfypiy eelkqrihsr ryegmlpten eltkefeasr ntirraisll neegyvysvk
       61 grgvlilesl nssqwsfgag nfgglkaiqs snhleaktrv ltfekividd alarstpfkk
      121 nevvykierl rilnekatml dlsyfkaeli pelsetiveq siyayfsknn vkiaaakrrf
      181 svtaatdddl skldldtnnc vgmmenlvfn dmgrlieytr srfvpdqfsl syfvqnhean
//
LOCUS       WP_010768065             435 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus phoeniculicola].
ACCESSION   WP_010768065
VERSION     WP_010768065.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..435
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=46155
     Region          14..435
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mkkessfnke afgekvavma nkvavnryis airdafasti pititaaffl lvnnvllaek
       61 tgllrgipgr emiseicvqa yngtlgilgi mvtfligvrl arsyesdgal egivalaayv
      121 slvpniisit gvegteiqas galtqtytsa samllgilaa lisvplvvkl tandrlkikm
      181 pesvppaiak sfnslipaff tislfaigev vlrtvtgltv peivvnilqa plvggfqtlp
      241 gillyvflst fvfifgihga fvfgaisgpi lltslqqnve aigagaaapn ivtqpflday
      301 vymggggtmi clviavllfs krqdqrmiak lggvsslfni sepmmfglpi vfnpvyaipf
      361 civpmvstil aylatslhlv nptyilipwv tppvlsgyla tagdfraall qiviiiigtl
      421 iyipfvlfsn kieea
//
LOCUS       WP_010768101             402 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Enterococcus phoeniculicola].
ACCESSION   WP_010768101
VERSION     WP_010768101.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..402
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=46176
     Region          45..233
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(83,85,122,124,126,143,159..162)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(139..147,156..162)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mdqlwqadky kelepltaep dspilvrnnq sgefwvqkky preleanlrt lmtirnphia
       61 kieeihviee tiyvyeeyvh gknlntllqs sdglstkfiy emslqlldgl islhksglih
      121 rdikpsnimi snddriklid fdairqfngk kendttllgt vgfaspeqfg faetdsrsdl
      181 yslgvvmnvc avkeypqtkl pnnyalkaii lhatkmdpad ryqtaeemkr aikinlasyq
      241 svvqaqanrp yekaqtksqp teqtyqaspa gkkqnaskrl yqktqvekkv tksilftyfd
      301 dfrsmslpkk aviifgyvli amgaiggvke rftpnetffw ylgvfilifa pyffftslkt
      361 irlytpllqs nrkrdhvlay slfflawfia wfiyvaispn ls
//
LOCUS       WP_010768118             435 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus phoeniculicola].
ACCESSION   WP_010768118
VERSION     WP_010768118.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..435
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=47651
     Region          1..427
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mskvlswiel klmppmakfa eqrhmkairn gvistlslim igtlfltian lpipgyvdwi
       61 kpytadlaip fritmgllgi ygafsmgynl tksykldgit ggilslatfl mltipvnvde
      121 llpegqglgw vlpmnylggs gmfsailaml fasemyrlft thnitikmpe qvppavarsf
      181 ealipgafil tvvwvvrvil gldinkmlld lfaplvdimg nnligvllpm ffihllwaag
      241 vhgmsiigsl vrpmwlvmld gnaaafadgt pitqlpyiap eqfyqwtvti ggagvsisic
      301 illlfcrstf lkqvgrfsli pgifnineml ifgvpiimnp ilaipfitap lvtstisyfa
      361 vkfglvngfi snqawtlpap igaylssgnd wrmivlvvin vlvamaiyfp fvriydnkmv
      421 eeelaasnek qvvna
//
LOCUS       WP_010768123             287 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768123
VERSION     WP_010768123.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..287
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31769
     Region          1..282
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 megkhihrrv esifseltqs ekkiaqmvle tpeeviqmta nelakasqts pasvirfcrs
       61 igisgftelk lklsaevdtp nytsysdisp gepikdiksk llgnayqsmk dtvnlidenv
      121 idetnelirk apivyvyglg asylvaenia qkwnrigktv vclsdahlll viltsavkea
      181 vfigisnsge tkevihmlki aknsglktis itqfgsntis hltdvsihtv rsneaelrsa
      241 atssllaqfm aidvlfyayv sesyeenitr irqsrkaieq ykkdsfk
//
LOCUS       WP_010768125             275 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768125
VERSION     WP_010768125.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..275
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31632
     Region          12..101
                     /region_name="cupin_MmsR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MmsR, N-terminal cupin domain; cd06986"
                     /db_xref="CDD:380391"
     Region          <195..275
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mfleskdrse fffndclltd fltinfgher clpshsfgpq vreyfvlhyi lngkgtfsle
       61 nntyslnkgd ffmispndsa aiyqadnqtp weyvwfgfeg nlvddvlhdl gynaenrvgh
      121 lsnandinrq inqlltssff sesssltiqg rlielisrfs ldgsnlslns nmkiserhie
      181 qfvlyirqny wradltieki aadlslnssy lsrvikkafn qstlsyliny rllkakflle
      241 nsdhtvsmis kavgyqnpls fsraykrvyg hsprk
//
LOCUS       WP_010768179             148 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside deaminase [Enterococcus phoeniculicola].
ACCESSION   WP_010768179
VERSION     WP_010768179.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..148
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16314
     Region          1..>110
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mtdylklavd atlegmkrgd ggpfgativr ngevivavgn tmmrdtdpsa haemvavrea
       61 ckkldtmdls dcevyatcep cpmcvgammw anitqvyycs tredaakhgf sdmhlrnyld
      121 gsdksaltme kvanredcdh lweafker
//
LOCUS       WP_010768193             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010768193
VERSION     WP_010768193.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..238
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24373
     Region          2..236
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 msdmtqifse flgtamlvll gggvcaasnl kkskaeasgw iviamgwata vtiavyvsgf
       61 mgpahlnpav tvgmaiagkf swslvfpfvi aqvvggivga ivvwlaylpl wdetedqgai
      121 lgtfatgpav rnlpantmte aigtfvlvlg llafgensfa eglnpvvvgi lilaiglslg
      181 gptgyainpa rdlgpriahq ilpiknkgts dwsyalvpiv gpvigavlaa glylvlpl
//
LOCUS       WP_010768186             761 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768186
VERSION     WP_010768186.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..761
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88200
     Region          12..752
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 makiadiyyk ldpwviteqg fdkkrnevse sifslgneys girgyfeegf ggdtllgsyf
       61 ngiyenspqe nrvqykgiva rshfmvnavd wlytritldg etldlaqanv sdfvrtldmr
      121 tgvlsrsfvw qtknkkkvrl hferfldmth aqfgfqkiqa ealnftgevt felgadfnti
      181 hqsqeqnfwq evykqtntlt saiigktitt nqkiysgfkl kanqsletvs verdkfighk
      241 fnvkleerrl fevirfstnv akkkdidtee lleigetllt eqietyeeak mrqaaywadi
      301 wqnldiiieg delnqqgirf cifqlqqtyh gqnpsnniga kgltgesygg hafwdtetcc
      361 lpfyllnnid aaknllefry qtlpearnra keldckgacy piatlngnea sdlwqhaslq
      421 fqpstgvayg iwhymqvsed qdflmshgie mlieisrflr trgdwsptge fgffgvmgpd
      481 efqmmvnhna ytnymakktf eytlesleki ndqfperfte lvtefaltke eqmdwakcae
      541 qmliletkdg lieqhdgffk lphvdikkip veefplyhhw sydriyrndm ikqpdvlmfq
      601 flynqdfshe skrinyefye pktihessls psihsilaae lgrereayef fgfatrmdld
      661 nynrntregl httsiaaawm nivygfggir tdgkelvvap mipkqwtsys fkltyhqtli
      721 sihveqdtvt ltkvkgepit lklygefiei asepviktih l
//
LOCUS       WP_010768208             252 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus phoeniculicola].
ACCESSION   WP_010768208
VERSION     WP_010768208.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..252
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28045
     Region          4..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 maflqvnhiq kiyssrhqat qvealkdvtf sveegeyiai mgesgsgkst llnilatldk
       61 atkgevlles qelsqipegk laqyrrehlg fvfqdfnlld tfsvrdnifl plvlsrvkvq
      121 emekrlkpla islkitelld kypyeisggq kqrvavaral itnpdlvlad eptgaldsrs
      181 adsllelfed vnekgqtilm vthsalaash anrvlfikdg qvfhqiyrgq qnnqeflqsi
      241 ndtmtvlltk ga
//
LOCUS       WP_010768291             274 aa            linear   BCT 01-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768291
VERSION     WP_010768291.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..274
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=29829
     Region          84..274
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(115,119..120,123..125,127..128,132,135,144,180,182,
                     186..187,190..192,194..195,199,202,212,214,216,220..221,
                     224..226,233..234,238,241,250)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          115..144
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          146..173
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          180..212
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          214..250
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 myrgiflvlf illagcsqtt mstktptsss qsltsesais eantketdqt settlhstte
       61 sinqtsqtet aetsevwrak vgslipaves naieevrril ldptypinei nekqespllv
      121 athqnnveia kllidagadv nqqdeiqdsp ylyagaegrt eilayileha npdqsvrnrf
      181 ggnalipaae kghienvkll ladgrvnidl qnnpgytali eavalrdgsq vyqdivklli
      241 dagadktlkd ntgrtasdya kelgygniyr mlqe
//
LOCUS       WP_010768334             438 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus phoeniculicola].
ACCESSION   WP_010768334
VERSION     WP_010768334.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..438
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46777
     Region          1..438
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 menklkkein lfgalstvmg tvigagvffk tasvvshtqs psltlfawll ggilticagl
       61 tvaelataip etggavkyie vaygklpsfl lgwaqsliyf paniaalsii fgtqfvnlfh
      121 lsttyllpva iiaaisvtgl nllgtkvast vqsatlvikl ipiavivlmg lfttgevsfs
      181 lfpieagkev sffeglsgal latlfaydgw lgvgamagem krpekdlpka iilglsfvtl
      241 iytlvnfvfl kslpvevisg nlnaaseast vifgsgggki vtlgilisvy galngytltg
      301 irvpyamale nelpfskqfr kvskkyvapy vaaivqlvia lvmmqlgtfd lltdmlvfvm
      361 wlfsvlifva vfilrkrepd mirpykvply pfvplvgiag alfiliatil tqtllaligi
      421 gvtllgipvy yyqqktks
//
LOCUS       WP_010768286             238 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768286
VERSION     WP_010768286.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..238
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26904
     Region          3..237
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mqkyilisnd irnkilkgey tanqqipfek dlcvyydssk mtvkkaldml vtegliikrr
       61 gsgtfvkdig pdelermsva nqfrgttaln pdkevkstil nfsvipcpen vqkklnidad
      121 sfvydiyrar sidgqphvme kmympidlip glkkanvegs iyeyleeklh lviqsahrti
      181 svrkatayea eylalqegdp vavadqigyl dtgaafeyst svhrydeysv eivltrdn
//
LOCUS       WP_010768361             283 aa            linear   BCT 01-JAN-2025
DEFINITION  putative ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010768361
VERSION     WP_010768361.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..283
                     /product="putative ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32762
     Region          8..185
                     /region_name="COG4905"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443933"
ORIGIN      
        1 mqefikvvll fflysfvgwl wetvycslka khfvyrgflv gpitpiygfg ilgvlyfiep
       61 fqknlillyv lsiilvtvle yltsyvlekl fhatwwdyhd vplnlngrva lpvslfwgvg
      121 cvlivrvihp kmlgleqfls dkfsfylpvl llvitaidft ytvmnmtafk katqqlgeai
      181 elrkselqes fdetkgeftq kleaakenaa thfdnlasev tsrtekpttw lrsfqenpkl
      241 kanlpklnft qrrllksfpk lkltdvkste eirqlvellk krk
//
LOCUS       WP_010768395             197 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus phoeniculicola].
ACCESSION   WP_010768395
VERSION     WP_010768395.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..197
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22113
     Region          13..196
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 meylfekgtg khllllhgtg gdetslvdia rflddkstvl sfrgmiqeqg mnrffkrngl
       61 nqfdyeslee esdkllaeit rvseeqgial edwvivgysn ganiaahfil eretklnkgi
      121 ffhpmslgvv nkkvdlsekq fwlsfgagdp iveksvfdel ennlktqgae vtveltqtgh
      181 qltmpeltaa kkwldei
//
LOCUS       WP_010768367             437 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Enterococcus phoeniculicola].
ACCESSION   WP_010768367
VERSION     WP_010768367.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..437
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=48584
     Region          14..423
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mniyekivng deslaliglg yvgmpiaief akkvdvigfd idekkiglyk kgidptlevg
       61 deaiknttvk ftsdpvdlkk akfhivavpt pinqdktpnl kpvesasklv genllpgsiv
      121 vyestvypga tedicipile eysglkcgid fsvgysperi npgdkvhtld kivkivsgid
      181 nqtrdeiaev yklvinagvh lassikvaea akvvensqrd iniafmnela ivfdkmgids
      241 mdvveamntk wnslgfypgl vgghcigvdp yyfiseaekl gyhsqiissg rkindsmgef
      301 vaqavikeli kanknlkksr ivilgftfke ncpdirntkv tdiyktlney elnveitdpy
      361 adpeevfqey ginlipessi kdadclilav ghdkyknkef syfdqlfnde knnvmidvks
      421 ildktdflkn nykywsl
//
LOCUS       WP_010768399             505 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010768399
VERSION     WP_010768399.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 505)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..505
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53954
     Region          203..503
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnfikralks twskkgrtil llavfsaili fvfagltirs aalsatneak ksvgatvtls
       61 anreaafkqq knsseserpd pgsfsltpvs ledaqkiaal sgvktysfes sasamagsni
      121 tpissnsten tedtstsdep nskedspeev qgfpgggemm gggmtqsdfq isgvsataqe
      181 ssfsegtsti idgqgiteed letnnvviet slaqanelav gdsftltnpd dedtsynvtv
      241 kgiyqttdsg nsmgmrfnfl npsntiyaay tlantmngad sentidsavy tlndpqemds
      301 fvseaeklid tesftissnd qayqqmlqpl nnvadfskni vllvtvagvi iltlivmmti
      361 rerrfeigvl lslgeartkv ilqfftemai cmifalgiag vsgnlvanlv gqqlidqqti
      421 taqndtqpdq lnqgeggpss merggfggqq gnpfevsdei seldiqvhpk efgllavfaf
      481 lislfsvffa sigilkmnpk kilis
//
LOCUS       WP_010768419             363 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010768419
VERSION     WP_010768419.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..363
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40894
     Region          170..362
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mirfkaivvr vvkellrdkr tlalmlvapi liltmlyfvf dsntdthlti gvdetvpssi
       61 iesfpeksvk ikkytesrnk eeiikeegld afvtltdatf lvtyknedpg vtaqtrilfg
      121 naltgsklhe lveevqkfaq qtgttiqqes fkvkseyvyg tknstffdki lpilvgffvf
      181 ffvflisgia llrerttgtl erllatpvkr seivfgylvg ygifaviqtl iivfysiyll
      241 nlhiegsiww vlvtnisial valvmgifvs tfansefqmv qfiplvvlpq iffsgiiaid
      301 smagwvqklg ylfplsyggt iltdvmikgq gfeaiwknlg mlgifvilft flnikglkry
      361 rkv
//
LOCUS       WP_010768425             153 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Enterococcus phoeniculicola].
ACCESSION   WP_010768425
VERSION     WP_010768425.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..153
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16995
     Region          3..134
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mkirtpigdf wiaatekgic rasftpieie devltnphli qakqellayf nkerteftvp
       61 ldilngtpfq qavwhallti pygkthsyle vaemienpka vraigqanrk nplpifipch
      121 rvigingqlt gymgtsgiel kksllllegi slq
//
LOCUS       WP_010768451             511 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease/substrate-binding protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768451
VERSION     WP_010768451.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 511)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..511
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56447
     Region          4..204
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          235..501
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(241,243,292..293,296,341,343,421,445)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mslffqtlne rkeelvtaif qhlaislaal igaiviaipl aimlstrkka aevmlqvtsv
       61 lqtipslall gllipfvgig tlpalialiv yallpifqnt yiglseidps ieeaaiafgm
      121 srfrrlikve lpialpvivs girtalvmii gtatlaalig agglgtfill gidrnnptlt
      181 ligamsaall ailvsslirf lqkrkprvtl ftlaflligf agigisqstl fsketvviag
      241 klgaepdili hmykelieer npkievelks nfgktnflfs alqhdqitvy peftgtvles
      301 lvtlkdsekp snsseevyek akqlleqqya mtflepmtyq ntyalavkrt faeenqltki
      361 sdlakiqnki hagftlefid rsdgykgiqe lyqmsfdtqa mepalryqai nngevnvida
      421 ystdselkey dlvrleddqh lfppyqgapl mkqttaeemp elvealnqls gkiteqqmse
      481 lnylvnvenq spekvahdfl vkeglleeek k
//
LOCUS       WP_010768519             105 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768519
VERSION     WP_010768519.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..105
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=11949
     Region          2..103
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 missdgirgy ndtillsils egdsygyais krirevsnem yvikettlys aftrlekngy
       61 iksfpgavth gkkrtyyrit dagkeyltsk keewsltkdv vdrfi
//
LOCUS       WP_010768545             318 aa            linear   BCT 01-JAN-2025
DEFINITION  aromatic acid exporter family protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768545
VERSION     WP_010768545.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10532842
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..318
                     /product="aromatic acid exporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36173
     Region          1..141
                     /region_name="ArAE_1"
                     /note="Aromatic acid exporter family member 1; pfam06081"
                     /db_xref="CDD:428756"
     Region          147..307
                     /region_name="ArAE_1_C"
                     /note="Putative aromatic acid exporter C-terminal domain;
                     pfam11728"
                     /db_xref="CDD:432028"
ORIGIN      
        1 mriglrtvkt gvsaalamil analqllyap sagiiavlsv tnskksslqt giyrlfsltl
       61 atlisyicfs llgyqpiafg iflllfipia vslglsdgiv vssvlvthyl veesmswgii
      121 fneyllmtig vgfalianly mpnaenrlke dqqiietmfk klltemssyl kqeiteqkll
      181 encngllsfi rqgqlraqty qenqwvvrdv yyasyfamrr sqvsvlhdmi esldrievve
      241 iqvekivall eytsetfaee ndgneilari fdvyeeyrqm tlpisreefe nraelfqflq
      301 sfksfieika efsqrite
//
LOCUS       WP_010768579             280 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010768579
VERSION     WP_010768579.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..280
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29680
     Region          12..270
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 misafidgvf qyqflqnall tsvmvglisg vigsfiilrg mslmgdaish avlpgvalsy
       61 miggsyiiga slfglaasal igfiteksql kndtaigivf stffalgiil isfaksstdl
      121 yhilfgnvla vtdsdmfmta ivgvcvvlfv lifykellvs sfdptmakvy glnttlihya
      181 lmflltlvav tslqtvgtil viamlitpaa tayfltdrls imiilastig vvsavvglff
      241 sytynlasga aivltagvff tlaflfaksk gilrqkkgrn
//
LOCUS       WP_010768580             246 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768580
VERSION     WP_010768580.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..246
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27348
     Region          1..241
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mkttiiegen lnvsytgenv ltiknlqitk gklvgivgpn gagkstllka llklvpmdge
       61 vnfsgkslkq fqkkiayveq rsevdltfpi svtevvtlgt ypklglfhrp keadlknvek
      121 alkkvrlenf aqrqisqlsg gqlqrvflar aivqeaeiif ldepfvgidv tsekviiell
      181 kelaksgkti ivvhhdlhkv tdyfdeviil nkqviaigpv eevftqenll haygesigfi
      241 rrkeen
//
LOCUS       WP_010768668             245 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus phoeniculicola].
ACCESSION   WP_010768668
VERSION     WP_010768668.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..245
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26704
     Region          7..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mttnktivly dvtkdivlgk eqktlkilkd vsleaykgef lsivgpsgsg ktsllhcmsg
       61 lakptqgsve ilgsnpyqls sskiselrrt kigfifqsyn lvaalpafen ivlplrlakk
      121 kvdkkkvysl leqlnfkasa nsyvdslsgg eqqkiaiarv lvsdcqivfa deptgaldsa
      181 sgkmvydllk yltergvsvv mvthdiemas atdralimrd gqlvdtiiqp kdaqlfealn
      241 gnkrr
//
LOCUS       WP_010768723             242 aa            linear   BCT 01-JAN-2025
DEFINITION  pseudouridine synthase [Enterococcus phoeniculicola].
ACCESSION   WP_010768723
VERSION     WP_010768723.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..242
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=27013
     Region          1..226
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 merlqkviah agvtsrrkae eyilagrvrv ngkiikelgv kvgkgdkiev ddvpiyqeey
       61 gyyllykpkg visavsddke rkvvtdflps vteriypvgr ldydtsglll ltndgefsqk
      121 lthpshevdk vyvakvkgla tkqmlhpltr gikiegrkta pakvevisvd prtgtsivel
      181 tihegrnhqv knmlqavglp vqklkrekyg eltlkglrpg dyrelnkkev ssllnlatnk
      241 tk
//
LOCUS       WP_010768767             416 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus phoeniculicola].
ACCESSION   WP_010768767
VERSION     WP_010768767.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..416
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=45262
     Region          16..412
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 msemtkknft ghlnnfinkf snnvfvksia ngmmmtlpit iigsiatvis mipnlpeivi
       61 kacslgtsis sslitvyvii glsysmakek kgdtipaiil smacffvltp vskfdlgddk
      121 vasaydltyl gskgmfvgmi vallvtwifv kmvekritfr mpesvptaia kqfeaiipga
      181 iifmvaiiis itfeatrfgn vhdfiytnlq tpleslggsv wsalfimfls ellwffgihg
      241 smvtasviav lfttqayanm eavasggvae niinsfflda fkgpralala vvlvwlsrsk
      301 kfnsigkisi ipsifgitep mkfgipmimn vtifipltls aamcigiayi atiigflpii
      361 svnvpknlpt flsgfmaagw qglvvqiiqf favlllylpf mkkldkmnva eelstk
//
LOCUS       WP_010768829             202 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus phoeniculicola].
ACCESSION   WP_010768829
VERSION     WP_010768829.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..202
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22668
     Region          1..202
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mikldqitks fegkvlflrl cleieqgefv ifsgdsgsgk ttllnilggl etvdagkvyi
       61 ntmdiskkkn rsklfsteig flfqnfvlie nktvrqnltl ikkrnrsnit vekaleqvgl
      121 lskidtkvyk lsggeqqrva larllvkkct iiladeptgs ldkrngdrvl eilfemqrlg
      181 ktiilvthde sikqkvqriv el
//
LOCUS       WP_010768859             478 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Enterococcus phoeniculicola].
ACCESSION   WP_010768859
VERSION     WP_010768859.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..478
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50077
     Region          1..476
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mekffklken gtkvstevma gvttffamsy ilfvnptils asgmpfqavf latiiasvig
       61 tlvmglfanv pyaqapgmgl nafftftvvf vlgytwqqal amvficglin ilitvtkirk
      121 miikaipesl qhaigggigi fvayvgikna gllsfsadqs aitssivdgd qavnvttnsg
      181 ivpalanfdn apillavigl vlmtvlvvmn vrgailigiv attiigilmg vvdlgsiqwq
      241 qnslgnsike lgttfgaafg pdgmqslfsd sakipqvlmt iiafslsdtf dtigtfigtg
      301 rrtgifsked elaledskgf ttkmdkalfa daiatsvgav vgtsntttyv esaagigagg
      361 rtgltsvvva alfalsslfs pliaivpaqa tapalilvgv mmlasfkdie wtdleeavpa
      421 ffasifmglc ysisygiaag fifyavvkia kgkikeispi iwvvnilfiv nfiilatl
//
LOCUS       WP_010768860             268 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus phoeniculicola].
ACCESSION   WP_010768860
VERSION     WP_010768860.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..268
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29697
     Region          5..262
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(9..13,43..44,194,216..218,220..221)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mnqkliaidl dgttlnnesk istktaatlk kaidaghyvs iatgrpyrms hqfykelnlk
       61 tpmvnfngal vhlpeqkwag eretlikrei vfdilaqkqa lnldfvaaen ketffidsld
      121 fydskffaap atennllsak nlttdptsll vrtqtqyaqq vsdslmsqyg efvdvrtwgg
      181 ptaileivsk giqkakgvhq vadylniske nvvafgdehn dlemldyagw gvamsngtde
      241 lkqvandvtq ksnqedglad yladylsl
//
LOCUS       WP_010768901             461 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus phoeniculicola].
ACCESSION   WP_010768901
VERSION     WP_010768901.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..461
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=52124
     Region          19..377
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(22..23,26..27,67,70,128..129,184)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(126,129,213..219,248,274..279,306,335..339,341)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 myetnllfdy skeprrdilc idcrsfyasv ecaardldpl ktklvvmsyp sdspsergsg
       61 lilasspmak kayhitnvsr ardlpfpypn dlviaaprmk lymqknmein aiyksytdee
      121 nhhvysvdes fldvtnslrl fncasayela kkiqidvyrk tglytsigig dnpllaklal
      181 dteakhtkkm kaewryedvp eklwqiqelt dfwgigrrta ktlnrmgiqt indlahanyy
      241 dlksklgilg aqlyahawgi drsflgkkiq pkeksignsq vltkdytrkn eielvikema
      301 dqvgtrlrri haqtqvislw igfslgyvdl sgkkgfhhqm kvsatasskk iaetlllifr
      361 ryyknqdvrt isvgcskllf tdsiqldlfs dpnqqvkeit adravdiirs rygfkslvha
      421 nslldggrai arsslvggha ggmagiegek ndnksykkrv f
//
LOCUS       WP_010768915             231 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768915
VERSION     WP_010768915.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..231
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27062
     Region          10..229
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msniveavrk nldltqnktl nvliyeafrk tiilgdipad trinekvfae elnisrtpir
       61 lamkqlvnek lvehvpkvgi vvkgirmkda yeiydirksl dtlatikamn qmteqdfqel
      121 kellergeay nkadetelvl knfsdfnafi yeksqmlrlk sivlelqayl vyfrdiairs
      181 skrrdkalee hwliyrgmkt knveqitlit hehldrslqf ilaemerrqi d
//
LOCUS       WP_010768930             289 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Enterococcus phoeniculicola].
ACCESSION   WP_010768930
VERSION     WP_010768930.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..289
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32121
     Region          10..274
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mltevftlsn gvtipkigfg twmipdtqaa dsvkeaiqlg yrhidtaqay energvgegi
       61 rtsgvareel flttklaaei knyeeavsai disleklgve fidlmiihsp kpwiefqsde
      121 dhyfegnlaa wkaleeayea gkiraigvsn feqvdlenll ahaktppmvn qilahighip
      181 tkviefsqah eilveayspi ahgemmkspe itemakkyqv sipqlairyl lqldllplpk
      241 sskashmknn aevnftitde dmaqlnkvgt ldygvnseip vfkkvakkr
//
LOCUS       WP_010768969             341 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768969
VERSION     WP_010768969.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..341
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37766
     Region          10..325
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mknkikflli tlgfvfllas cgskeivvek ndkglakvai qidgaatpyy aplylakekg
       61 wfeeegldve fyyasaseiv knvaannvef gfpnsdpvvm grsnnvpvki ihttyqeglg
      121 siiyknesgi sepkdlkgkt igitsygspn fiqlqvileq aglslddvsi kiigtgaivn
      181 alvsdqvdai sfsmlrvydl eeqgisvgef rsenymptqg nvvitsdqll kehpelcqkf
      241 tqalnrsiay lvdnhldegi enaithyapa akgneekikk vmeneflpkl wqsdntvkng
      301 fgysdvdryn dyiallykyn lienkydaee lvvnldeggk k
//
LOCUS       WP_010768947             337 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010768947
VERSION     WP_010768947.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..337
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35004
     Region          7..336
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 measqtkept dnkvkklkqf lseylivlvl almiavltgl npnflsmnni lnlltqtaiy
       61 gilalgifiv lisrgidlsv gstlafagiv agtisqtqna idkifpglgm aplyvtilvt
      121 lligagigav nggliaytni ppfiatlgtq isvrgaalmv srgkpvsnin peinwfgsri
      181 fgvipvpvli yivlifiiwg imnytsfgks iyaiggntea aeisginvrk nlvwvyaisg
      241 ilasiaaliy igrtggsiqp aagtmfetta iaaatiggts hgggvgkvwg avvgalilgt
      301 ltngftllgv dayiqqiiqg aiivgavvid mrknkkg
//
LOCUS       WP_010769042             176 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769042
VERSION     WP_010769042.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..176
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20378
     Region          2..159
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkivfyggi sldgylades hslqwlfdad dgtpmnydsf ietidttvmg rktfeetlty
       61 tkgenpypgk tnfifsrkmq yttddfisis edpvaflnew rkkegkdiwi vgggkllkpl
      121 leadmideww iqftpillgk girlfeegny rnqlelievn kfgqfgelhl rkknlk
//
LOCUS       WP_010769073             218 aa            linear   BCT 01-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010769073
VERSION     WP_010769073.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..218
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=24995
     Region          14..214
                     /region_name="SGNH_hydrolase_like_2"
                     /note="SGNH_hydrolase subfamily. SGNH hydrolases are a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site...; cd01834"
                     /db_xref="CDD:238872"
     Site            order(21,65,94,195,198)
                     /site_type="active"
                     /db_xref="CDD:238872"
     Site            order(21,195,198)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238872"
     Site            order(21,65,94)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238872"
ORIGIN      
        1 mntpdfikqk krqrflfigd sitdvgrdre nfydlghgyp fliasilake lpdydiecln
       61 rgiggnkind lqerwqedcl slkpdvvtml igindtwhht asdefgskke aqrfessyrq
      121 lleqlkqstd ativlmepfv lpypedrrtw rkdldqkiqi irtlaeeyqt ifvpldgkln
      181 algiayghsh ytgedgvhpt laghaeiaes wlqathfk
//
LOCUS       WP_010769075             396 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769075
VERSION     WP_010769075.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..396
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43489
     Region          1..394
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,206,235,237..238,246)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,199,244..246,275,278)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            238
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mkisqraeql epsvtlvaaa kakalkaqgl dilsltvgep dfatpeniqe aaikaikngn
       61 asyytptagi pelrqaivsy lqenygltyk ttqtivtdga kfalytlfqa ildagdevii
      121 pvpywvsyge qvklaqgtpi fvnckesnhf kvtvdqleea yssrtkaiii nspsnptgmi
      181 ytkeelteig nwavekdili iaddiygrlv yngneftpia tiseairkqt iiingvskty
      241 amtgwrigya vgdetiiqtm vdiasqstsn ptavsqyaav eallgeqdtv eemrvafenr
      301 lnkfypliea lpgvriekpq gafylfpnvk etiaicgyen vtdwvddlle eaqvalitge
      361 gfgsdehvri syatnlgile eavdriaafi erkrka
//
LOCUS       WP_010769102             271 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769102
VERSION     WP_010769102.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746489
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..271
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31695
     Region          <44..82
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <69..271
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          189..268
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpvyynlayq enpfsvdsig shweqptvsr ptgypyyhwl qtesgvgeif legkkivlkq
       61 gqgiliapfv phqyfshrss iwitsfatfn gslaneigql vgkspyllae eqpyfsffqw
      121 vedqiqqqit npaidsiels iscyqflmql srfqdkhtnq khelyltyiq pvieeietny
      181 kealtverla eqvfvspqyl srlfqrflgi stytfilryr lnkakellin rqeleiqqia
      241 ylvgfkdash fvasfkkess ytplefrrlh r
//
LOCUS       WP_010769121             306 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769121
VERSION     WP_010769121.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..306
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34687
     Region          1..282
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mliqekmqqt hfssseqqvi dyllshtegw qdqtikeian qvythpstli riakklgysg
       61 wkelkeayie eityltshfa tvdanfpfdq sdgvmsiask igtlqkmtid dtlsllhhde
      121 lqkakqyllr adtvklfggn antlisqefa lkmsrlgkpt svsttfgegm yeaynlpess
      181 cailisytge nsyllelltv lqerkipvia ltsigtnqla eksnctlrmt trerlyskig
      241 sftintsicy lldvlyscvf gehyrknfnh ilnvsqrvdn rrstseiire knpqdvlnal
      301 dswipn
//
LOCUS       WP_010769165             325 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769165
VERSION     WP_010769165.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..325
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34424
     Region          37..307
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mkknlkfnlv wlaiaaglyg ilyalysagv isfftdfilv siginiilat glnliigfsg
       61 qfslghagfm aigaysaaim svknptmggf fsglvlgifl sglvalivgi ptlrlkgdyl
      121 aiatlgvaei irilivnlrd itngpsgifg ippfanwsmv fgfvvvttlv ivnflhsgpg
      181 ratmairede iaaesmgvnt tkykviafmi gamtasiags lsasyiqsia pkdfgfmksi
      241 diliivvfgg igsitgtfva aivlgvlnmf lqdfgalrmi iyalaliiim ifkpggllgt
      301 wefsvkrife kfgkkeddsd asigr
//
LOCUS       WP_010768758             268 aa            linear   BCT 01-JAN-2025
DEFINITION  triose-phosphate isomerase family protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768758
VERSION     WP_010768758.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..268
                     /product="triose-phosphate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0004807 - triose-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006094 - gluconeogenesis [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=30322
     Region          12..260
                     /region_name="TpiA"
                     /note="Triosephosphate isomerase [Carbohydrate transport
                     and metabolism]; COG0149"
                     /db_xref="CDD:439919"
ORIGIN      
        1 mkkissqfyk krtpivamsy knylnkpeev gllveeiilg lkesktefme cflfpsmgti
       61 etvarfckgs nlgfgaqnia pqkngaytge fsieslialg gryvelghfe rktlffetnq
      121 qikekihltl sesmipvlci getikcegqm leeilmeqlk ellseineek vvnvilayep
      181 gwaigqakpa siahihrsht cirrccerlf tkeiaehiri iyggsvslte vseivdhqev
      241 dgvfvgrfgh evnqfleiiq rvsqmkee
//
LOCUS       WP_010769186              91 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus phoeniculicola].
ACCESSION   WP_010769186
VERSION     WP_010769186.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 91)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..91
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10428
     Region          1..88
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 meikeeknrf vllndesaei gemtwsdage eimiidhtfv dptyrgqkla eklvlagvek
       61 arrenkkivp lcpfakkefd qkseyadvlr k
//
LOCUS       WP_010769193             345 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769193
VERSION     WP_010769193.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..345
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38167
     Region          25..341
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 minelkmiea iapevmdvlq erfqilrniy wmqpigrrsl aesmgmterv lrtetdllkt
       61 lqlidtsksg mtltkkgeni yqnlekimnq llgvnqiekq laeyfgikrc vvvagdsdeq
      121 pkvvdefgea lnealmqllp etqniiavmg gttmatvaeh ltnletdtrh nlfvparggi
      181 geavtvqans isammatkak gnyralyvpe qlslatynsl lqepsiqevl glisqancvi
      241 hsigralhma arrkmteeel lmlkqknava esfgyffdem gkvvykvpri glelkdiqdi
      301 piviaiaggh skakainaym knapeqtwli tdeaaanvil kgvtl
//
LOCUS       WP_010769198             456 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Enterococcus phoeniculicola].
ACCESSION   WP_010769198
VERSION     WP_010769198.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..456
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52870
     Region          13..425
                     /region_name="YdhJ"
                     /note="HD superfamily phosphohydrolase [General function
                     prediction only]; COG1078"
                     /db_xref="CDD:440696"
ORIGIN      
        1 mmipykqqtl piekvfrdpv hnyihvqhqv ildlinskev qrlrrikqlg tssftfhgae
       61 hsrfshslgv yeitrricdi fernysldkv giggwndqer lvalcaallh dvghgpysht
      121 fehifhtnhe aitveiitsp etevyqilnq vevgfpekva svitktypnp qvvqmissqi
      181 dadrmdyllr dayytgteyg tfdltrilrv irpyeggiaf amngmhaved yivsryqmyv
      241 qvyfhpvsrg mevilehlln rahelyqeds elfdsnaqll lpflkesftl deylklddgv
      301 lgtyftqwte endpvlsdla krflnrkplk satfsgkedq liikklqqlv ekvgynpryy
      361 tainssydlp ydfyrpeqgs hrtqieivkk dgtlielsqv sqlvsalagq qqgderfyfp
      421 kemvdptlrn hydlfeetyq efsqyirnga lvnaqs
//
LOCUS       WP_010769207             593 aa            linear   BCT 01-JAN-2025
DEFINITION  V-type ATP synthase subunit A [Enterococcus phoeniculicola].
ACCESSION   WP_010769207
VERSION     WP_010769207.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF003220.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK04192
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..593
                     /product="V-type ATP synthase subunit A"
                     /EC_number="7.1.2.2"
                     /calculated_mol_wt=65505
     Region          1..584
                     /region_name="NtpA"
                     /note="Archaeal/vacuolar-type H+-ATPase catalytic subunit
                     A/Vma1 [Energy production and conversion]; COG1155"
                     /db_xref="CDD:440769"
ORIGIN      
        1 mqegkiikvs gplvmaenms dasiqdmclv gdlgvigeii emrgdvasiq vyeetsgigp
       61 geavrttgea lsvelapgil sqmfdgiqrp ldtfmeitks nflargvqlp aldhekkwlf
      121 epvkavgesv sagdiigtvq etaiilhkim ipngvkgtik eiysgeytid epicvletee
      181 gdkvltmlqk wpvrrsrpik eklnpdapmi tgqrvidtff pvtkggaaav pgpfgagktv
      241 vqhqiakwad vdlvvyvgcg ergnemtdvl nefpelidpk tgeslmertv liantsnmpv
      301 aareasiytg itiaeyfrdm gysvaimads tsrwaealre msgrleempg degypaylgs
      361 rlaeyyerag rvialgsdhr egsitaisav spsggdisep vtqntlrvvk vfwgldslla
      421 qkrhfpsidw lqsyslysae vgkymdqalq adwsemvteg mrilqeeaql neivrlvgvd
      481 slsdkdrltl evaksiredy lqqnafdevd tftsrekqfk mldmiltfqk egqralelgs
      541 ylheimdgtv qlrdriarsk yipeselekl dsyllsirqt mqeiiaeggm shd
//
LOCUS       WP_010769214             239 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Enterococcus phoeniculicola].
ACCESSION   WP_010769214
VERSION     WP_010769214.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..239
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=26225
     Region          26..238
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mnqpiigiag nqlihatdvf ngnlvtytpq gfingvseag glpfvlpvsd pnnakeyigk
       61 vdklllaggq dvsprlyneq phpkleetny hrdlfeaali keaieqkkpi ftvcrgtqll
      121 nivmggslyq dlslyenwqv khgqqptapq fsthsvtvda tsklsmlvqd gsyvnsyhhq
      181 aikelapnlv atawatdgii eaveakdgsa ilgvqwhpel thtveqkdqa lfdyfvnem
//
LOCUS       WP_010769240             432 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus phoeniculicola].
ACCESSION   WP_010769240
VERSION     WP_010769240.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..432
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=46867
     Region          5..431
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mnesnvfidk mlvfankfss qrhitairdg fvtlipitii asfwvlinnl vlsptngllk
       61 nveaaakwsd lgnqiyngtl gvmalliamt igyklavsfg eegligsvvg lvsymivlpa
      121 qiiltdvngk tftatatmtq tqtsatgmfl aiiatlfsvt llckftkmdk lkikmpesvp
      181 psisksfnil iptflvtlll glievliiws lntdiptlis kffqaplvas fqsiggilly
      241 vllsnllwaf glhgtfilgs igepvmltai qqnmdalrdg qelpnivtkp fldsfgwmgg
      301 ggmiiclvia imigskredy rsitkvgiip slfnvseplm fgipvvfnpl lgiplilvpi
      361 vtvtiayyat afeliaktsv lipwttppvi sgylatngdw rasllqilli vvgvfiylpf
      421 vrlankslek ni
//
LOCUS       WP_010769266             310 aa            linear   BCT 01-JAN-2025
DEFINITION  permease [Enterococcus phoeniculicola].
ACCESSION   WP_010769266
VERSION     WP_010769266.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..310
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=34193
     Region          5..310
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mfellphsvl qmstiflsiv iealpfvllg clisgalyvf ltpervqkfl pknkllsiaa
       61 gcgmgfffps cecgivpivn qfvkkdvpiy tafafmltap iinpivifst fiafgnsfkf
      121 alwrilgsfl ialvvgiwla yfnktdvlkq kmnttleeep phehihvaha htkeeshprf
      181 ihqvahvfth gvdeffdtgr ylvigalias amqtylptgw mltlastkvl avlimlvlaf
      241 vlslcseada figssllslf gtgpvvgflv fgpmvdiknl lmmkryfsgr fitslvgiia
      301 vvvfvyamiv
//
LOCUS       WP_010769314             289 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus phoeniculicola].
ACCESSION   WP_010769314
VERSION     WP_010769314.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..289
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31370
     Region          4..281
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,214,236..238,240..241)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mikliasdmd gtlldahmgi skenaeairf aeskgiefmv stgrnyqear saldevgidc
       61 amitlngaqv fdkggtslft vpivpertat ildildahdi yyevstnkgl ysqsqsrrve
      121 sfasmiashl phltykmaia maaanlellh ieyvdsirel lvdnklevlk iicfhmegpq
      181 vlgpvateid algdlavtss gqnnieinhr daqkgiavah vasergidlt dvmtigdnfn
      241 dvsmlqvagv sfamgnaele vkeyakyetd tnlengvgka imraieeel
//
LOCUS       WP_010769288             639 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769288
VERSION     WP_010769288.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..639
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=73938
     Region          9..636
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mvsqrqkell ellesqtdfl tvqvlanqlg vskrtvhsel kllenhiqrl gkciekkrgv
       61 gillknckie qpftesldti dtystfsrri dimkillfde emisfnslse lylvsktsii
      121 kdlecikeil qagsditlks dvqgtrisgt esdiqkaylq fnryiishsn yyyddtirmk
      181 mnvlgpyyee tiisvctnil ynyvrdnsna ladyyvqnvl nifiilvhrn lnghhiqene
      241 ktkgsefslf feesavrllh kaalrlrfsy tnedvkffsq hlianrfesl pketidngvv
      301 ktlltrvska lsidfsndkk leqqlmdhip pmiyrlqsnn ktenpfteqi ktefsltfnv
      361 iwvvlseyek klnisfnede iafltiyfqs aieraklnrk ilvvcqmgia tsellmnrik
      421 nilpsldtie vasvaelehi dvyqfdliis tikieipekk vlfvspfltd idtqkiknsg
      481 ykpsnlspkn stltvqhlrk yiqpdlvyvn sefsskeelf rmvglqlikk glvsekfien
      541 lfqreklggt dlpsgtavph ghpsyvnktt ivfiknkkkf kwdkyyvdii fliciseedt
      601 nqtrqilsdi ynivdtenvl kqmrkpiskt eimeilrse
//
LOCUS       WP_010769376             288 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769376
VERSION     WP_010769376.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..288
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31632
     Region          1..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mgnflasqlk nyreqegltq kelakelyvt dkavskwetg rgypdldtle kisnlleitl
       61 ddlvnerkpy eyldfksekk ignlplyhfv ipnmsllfqn rlqnknrksf sqiptakgvl
      121 svgikakgil aigtfsigif sigaiglglf sigilsigli aagsagfggl amgnfalgit
      181 aignlaiama afgnfsigyf algnqslgvh afsagnevtr ekfseglqqf qlsqsytgls
      241 kiffdmlyti qknpfpvilg filivvffll iiwltvrify knnypsfq
//
LOCUS       WP_010769380             254 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010769380
VERSION     WP_010769380.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 254)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..254
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28652
     Region          8..196
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mrnyffflkk elkegiktyk lpillcifft fgvlspmtak flpkllpsll gegmnfeipe
       61 psstdswtqy fkninqlgfv vvilifsgil shefekgtli nlltkglsrt tvllskltym
      121 ivvwtvnlvl sflitwgytv yyfsdgksph lvsaifpiwl fgclllsvfl fsatlfekss
      181 gsllimvlft aaglflsiid riakfnpfsl vqknlpfiqg teflsdylpa mcisfllivl
      241 ltfgackvfk kkvl
//
LOCUS       WP_010769390             607 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus phoeniculicola].
ACCESSION   WP_010769390
VERSION     WP_010769390.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 607)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..607
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67832
     Region          <52..167
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnfnqfvvrn tvrnkhlyma yflstlfsvm vfftftvfaf hpdltsglnt kvqtgmlaaa
       61 viiygfafff vlysmdvflq srkkefgllm iqgmsptqlr kmvfienlvi gffatisgsi
      121 lgigfsqiil wlskqfmhvs ygfyfpvqaf vltiisflal fllisffiqf rlpkltlqel
      181 lkagdlgkgm iksskikgfl ailllatgyg iallapgltv plvmlpvifi vvvgtrfffn
      241 qlsvlviegl kkkqtifwkk tnmvvfsdla frmkdnarsf flvsiistva faaigtlfgf
      301 qnlimeqtna iayefqvegs psetaaaesl vtdtlakeni qatpvsavly gndkgeqfis
      361 qkeynqmake igeptistna avhlnsatav gepkkdttks vtvngetlsv dstetthvls
      421 ayqptfvvsd ktnlsgltet kltvwepksa nrqqlltagk afedvpqyif aktysqqsvi
      481 dmykpilfvg vfigivffvs agsflyfrly sdmdvdvekf kmiyklglsk selkkmiyqq
      541 vgilfftpiv vsvihgaval tamyhmfsmg mqltgwqvlg afvliqavyy liartfyfkk
      601 vyrlvha
//
LOCUS       WP_010769399             402 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Enterococcus phoeniculicola].
ACCESSION   WP_010769399
VERSION     WP_010769399.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..402
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=44164
     Region          1..378
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mkevvilgag yaglrtlkel qkskeafhit lvdqntyhfe atdlhevaag tqpkekityn
       61 iadvvkpekt tfiqakvvki drekeevfle sgqvltydyl vvglgfqses fgipgvteya
      121 lemvdvdsav kvnehihemm rqyvatkden flkiivcgag ftgiellgsl vegkkaladi
      181 agvtpdkiqi ycveavtrll pmfdeklady avkhltdwgi qwytgkpike ikpgvvvyqd
      241 daetketkel eaktiiwttg vsgshvmgds gfserrgrvm vsedltdpdh knvyvigdvs
      301 avmdaesqrp ypttaqialk mgttasknii hqlkgektea ftfksqgsva signthalgl
      361 vgkssvkgyp asfikkmimn kslletggvk ealakgrfdl yh
//
LOCUS       WP_010769440             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MIP/aquaporin family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010769440
VERSION     WP_010769440.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..240
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24408
     Region          4..238
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mdssvmtqfi gevlgtailv llgdgvvagv slkkskaega gwiaitlgwg aavsiaayss
       61 gylssahlnp avtlgmamag nigwdlvapy iaaqmvgaii gailvyvqym phwketkdpa
      121 tilgtfatgp airsyganli seiigtfilv fallsfgtgd fgaglnplav gvlimaigls
      181 lggttgyain pardlgpria haflpipnkg dsdwgyswvp vvgpmiggal aaglfmmlpi
//
LOCUS       WP_010769453             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus phoeniculicola].
ACCESSION   WP_010769453
VERSION     WP_010769453.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..277
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29974
     Region          1..268
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkrfiglits lgavflltac hssenekaiv vgsqgsdaqv wafiakseaa kkagikievq
       61 eidggpqlnt ataqgevdvn afqsisylns ynqdggdtla piaatymepl giyssiykti
      121 devkeksvva ladnpantar glklleaagl iklkedfdng tgtpsdiqen pkklefklid
      181 dttgprvlpd vdlvlisntv alegglnvlk daiyyekine dtkesinvla tkksrsdeee
      241 llalgelyhs kevqeyiket fdgtkvevke siekiie
//
LOCUS       WP_010769457             277 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769457
VERSION     WP_010769457.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..277
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31747
     Region          3..271
                     /region_name="RgfB-like"
                     /note="Streptococcus agalactiae RgfB, part of a putative
                     two component signal transduction system, and related
                     proteins; cd09079"
                     /db_xref="CDD:197313"
     Site            order(7,39,149,183,185,238,265..266)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197313"
     Site            order(39,265)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197313"
     Site            order(149,185,266)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197313"
ORIGIN      
        1 mklltlnths wmeeqplekl etlaqmiaar eidiiclqev nqrkdvgegh tdaffhhaln
       61 qmpikkdnfa yllvkrlkel emsyhwcwmp shigyevyee gsailsrntl qaesfiaset
      121 teftdyhtrr mlgattvvng kdvyvmschf swwegensgf yqewqttenv lssktvplfl
      181 mgdlnnpshi egqgytqlvn sslplvdsfs haknkmgeat vkkvidgwen nqeslridyv
      241 fvsnqlevst yevvfdgkrt pvvsdhfgvf vsgnwke
//
LOCUS       WP_010769490             614 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010769490
VERSION     WP_010769490.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..614
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=70437
     Region          20..599
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkkkiqallr dkrviypiit illlalvvgs nlylqwcqnn lswdlafkfa fswhaekffl
       61 gcfvlavlll ffislagsvg vgtllyslvi gilgyadymk mtlrqepiyp ddlkmitelg
      121 llkemagtgp filimalsla alslfgwgiy ksfkkprhfq virgttfils ialffyisnf
      181 nnpnnllrke ynktalwipy sqkmnyyntg figgflynlk vdpmdkpagy skekveeitk
      241 kykdlaknkn ktrtqrepni iyimsesfsd psrlngltis gdpladyyem anqtysgnml
      301 sqnygggtan iefealtsfs melmnpqmtt pytmlvpkmt efpslvsvlk drnyqttaih
      361 pyntsmykrk dvynvfgfdq fldedtmtyt dtiqknpyis daaaykevmd ilkddstpqf
      421 ihlvtmqthm pysgkytald yqasgegnmd slqnylqdvs yssqalktfl nelkkvdrqt
      481 lvvfwgdhlp giysdeiqaa ndestlhetq flmydnkgnl tnkdnhqait spfyfagdlm
      541 eqsnlpttgf yqlvnavqet lpafernlyf qngqwqkeik ltkdeseaye ayqmiqydiv
      601 agnqyslser ffke
//
LOCUS       WP_010769468             269 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769468
VERSION     WP_010769468.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..269
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31381
     Region          <32..98
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <75..269
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          186..268
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 meeliisflp eqfqfpdifr ielagitypf agycvkrehs qiysieyvls gsgeiqidgl
       61 syqseagdsy ilpknhhhfy wsdkrtpfhk iwinvsgtlc dqlfdvyhlh qryllksvdv
      121 kntlealikv cqeypltptq rtekssilfh klllgihqql rpkeelipea vqkaklildt
      181 hvqttltisd lasqvnlsss qltrlfkryf hqtpydyflt kkmemaevll setrlpiqei
      241 sdrlsfsdeh yfstlfkqkm nrtpgslrk
//
LOCUS       WP_010769459             764 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769459
VERSION     WP_010769459.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..764
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88381
     Region          5..756
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mkqvqrlfqv dpwkvsthtl dkenrrlqes ltslgngymg mrgnfeesys gdhhqgsyla
       61 gvwypdktrv gwwkngypey fgkvinsvny iamdiyvngv avdlysmepe dfyleldmkt
      121 gilsrqftit vndttirfsf erflsivqke mamirltaev lkgdatvtiv skldgdvqne
      181 dsnyeehfws preagrmegf sylsaktipn sfdieqfsvt samkhvsnkn ysheiskeal
      241 kieetfsfhv aendsfyldk qvlvvtsrdi pekkqietlg tlyqaltpdy sahkknqida
      301 wanrwaladv iidgdeeaqq girfnlfqlf atyygederl nigpkgftge kyggatywdt
      361 eayavplyla ladpsvtknl ltyrhnqlpq aqhnarqqgl kgalypmvtf tgvechnewe
      421 itfeeihrng aiayaiynyt nytgdtsyle nkglevlsei arfwadrvhf skraqkymih
      481 gvtgpneyen nvnnnwytnt iaawvlrytr esylqfkdkt sliieenela nwldivenmy
      541 yptdkelgif vqhdtfldkd lfaaselnle elplnqhwsw dkilrscfik qadvlqgiyf
      601 fsddytleek rknfefyepm tvhesslsps ihailaaelg leekalemyq rtarldldny
      661 nndtedglhi tsmtgswlai iqgfaqmktd hetlsfapfl pskwnayafh inyrgrlllv
      721 tvtkesvtld lvhgeplklk lynewllltd kttlplrkkd dkhv
//
LOCUS       WP_010769488             892 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus phoeniculicola].
ACCESSION   WP_010769488
VERSION     WP_010769488.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 892)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 892)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 892)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 892)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..892
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..892
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=96649
     Region          12..886
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mseekkqqlt hafygqteet vlseldtsre glsgaeakkr lseygeneld egkkksmlvk
       61 ffeqfkdlmi ivliaaaiis aivshevida siimlvviin avmgviqesk aeqaiealre
      121 mstpnanvlr dghtlsvksd elvpgdivll eagdvvpadm rlievqslki eeaaltgesv
      181 pvekeltvle gtdigigdri nmaysnsnvt ygrgkgvvvn tgmntevgki agmlaqadet
      241 etplknnlnq lgkfltlaii viavimffvg ifvnntspvd mlltsislav aaipeglpai
      301 vtiilalgtq vmakrnsvir klpavetlgs tdiiasdktg tltlnqmtve klytdnkqvs
      361 agsdisidnm alkimnfsnd tkfaqdgtli gdptetaliq fgldhgfnvt ekvaeeprva
      421 elpfdserkl mstvhqlkdg kflvavkgap dillqktnrv lldgkevamt qsekndilan
      481 ntdmakqalr vlgmaykvid tipnevtsdv letelvfagl vgmidperke aaeavrvake
      541 agirpimitg dhrdtaeaia arlgiikegd daavltgael nemsddefak rvheysvyar
      601 vspehkvriv kawqtegkvv amtgdgvnda palkqadigi gmgitgtevs kgasdmvlad
      661 dnfativvav eegrkvfsni qktvqyllaa nlgevltlfi atllawdtll pihllwinlv
      721 tdtfpaialg mepaekdlms hkprgrnsnl fsggvfgsii yqgileggit lfvywsaiqw
      781 pvhagydaih adaltmcfat lglmqlfhaf nvksihesif kvgpfrnktf nwaillsfal
      841 maviilvpgl ndifrvahld gyqwgivlaa sisiipivei vkffqrmglk ka
//
LOCUS       WP_010769494             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769494
VERSION     WP_010769494.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..251
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29102
     Region          3..105
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          135..248
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 meytikaiaq lsgvsartlr yydelkllkp krinssgyri ygeaevdrlq qilfyrsldm
       61 kleeikkild qpnfqittal eghyrqllkk rasidslist vektlryqkg espmtdsekf
      121 eafkaqkvqe neatygqelr eqygeeimkq snkkfsnlte eqyqkmnete knlisllrss
      181 lsadadvsev ktklvnlhke wlfytwpsys vdahkglaem ylvderftsy ydekagkgat
      241 kllaeaikes h
//
LOCUS       WP_010769600             607 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus phoeniculicola].
ACCESSION   WP_010769600
VERSION     WP_010769600.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..607
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=66737
     Region          16..448
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mdylkrllvg kplksaende qklsrfaala llssdalssi aygteqivvv lvalstaaiw
       61 yslpiaavvi vllvsltlsy rqiihayphg ggayvvssen lgknaglisg gsllidymlt
      121 vavsvsagae aitsaipaly nhqvgisvli vvlimmlnlr glresagflv fpvylfigii
      181 tilifiglfn iltgavplna tavpgtvvpg islalilraf ssgsssltgv eaisnavpff
      241 kkpraknaag tlammasilg fffvgitfin ywygivpete vtvlaqigka vfgsgfmyyv
      301 lqfstalila vaantgfsaf pvlaynlskd kfmphmyqdr gdrlgysngi itlaagsivl
      361 lfifngster liplysigvf ipfalsqtgm vihwrragek wlrksianiv gatisfsiil
      421 ilfifrlndi wpffiimpil lytfykihdh ykkvaeqlrl eekasahefe gntvlvlvgn
      481 vtranvgaln yarsigdyvv amhvsldedv kkekeieaef renfpdvrfs vvhssyrsie
      541 tpiiryvdlv sknaikhnyt ttvlipqfvp nhrwqnilhn qtslrlrlrl swrenivvgt
      601 ysyhlkk
//
LOCUS       WP_010769620             349 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010769620
VERSION     WP_010769620.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..349
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39134
     Region          1..249
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msvmnfavig yggmgsyhvh timpeelihv kgtydcsner qviseekghf iyttyeevln
       61 dqeieavlia tpndshkela ikalragkhv vcekpvtltt kefdeillva ketgktfmvh
      121 qnrrwdpdfl ivrelyknkq igdlfqiesr vqgangipgd wrhlkvhggg mlldwgvhll
      181 dqllfmidsp vktvaadfsy ilgdevddgv aayltfegge kvimevgttn fiklprwyik
      241 gtdgtavied wdlsgkmiqp tyapdvlapt piqagvgltk tmappseeat ktlelpkaea
      301 eytgfyqnfy dvvrhqaepi vkneevyrvl klietifeag ethqvlpfe
//
LOCUS       WP_010769669             454 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Enterococcus phoeniculicola].
ACCESSION   WP_010769669
VERSION     WP_010769669.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..454
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49319
     Region          11..434
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mreltkgnpa klififtipl lignifqqfy nmvdmiivgq tlgknalaav gstgsltfli
       61 igfaqgltsg lsiitaqrfg aqdfrgvkrs fatgiiisfi vtavltivsl vflrpmlllm
      121 qtpaeiidqa qafisvilag ifaamtfnll sniiralgds rtplfflvia vivnvlldli
      181 filyfgmgve gagyatviaq mvasllcliy ikkkipllql hrkdfvwdkk elrkhlnial
      241 pmafqasiia igaiilqsal nslgtdvvaa qaaagridqf atqpmmsfgv tmatftaqny
      301 gakeygrilk gvkqclimsc gfsiaagavv ilfghylvrl fvstsevkvf elsqiyfnvn
      361 gsmywilail filrytlqgl gqskiptiag imellmrsfa aifltqligy tgaaaaspla
      421 wigsvvvlly syikamkslk ilekeqqeks nlav
//
LOCUS       WP_010769661             316 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010769661
VERSION     WP_010769661.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..316
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35512
     Region          1..243
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtvrygiist aqivprfveg vrqskegevt aiasrsieka ekmagelsip kaygsyealc
       61 qdeavdviyi atynkghyea aklalsydkh vllekpftlt taeatelfel aqkktlflme
      121 aqkavflpit qevkaliaqk aigkiqfvns vtaypniehl twfhsldsgg gllhgsgsyp
      181 lhylsylfgd ieeysgsanv segvdeqvni tvkfdsdlla nlfltvkldl pskltlygek
      241 grieipdfwk akramiydnf gheeeiltaf eneftfevdh vntciknkqi tssimtkert
      301 iqtvnlvesf ykqwfr
//
LOCUS       WP_010769675             188 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Enterococcus phoeniculicola].
ACCESSION   WP_010769675
VERSION     WP_010769675.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..188
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21649
     Region          1..142
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mrivfisgsi igsktriate kayemmkery pneqvsfydl adfqlpfsdg rnyfdyeepi
       61 saflsdvmea dalvlgtptf qasipatlkn ifdmlpvnaf rdkivgilvt agspkhymmv
      121 eqqlkpilsy mkaiivpkyv fieekdflrk eivnddvlfr lerlvedvkn ttevynqlqe
      181 klneqygf
//
LOCUS       WP_010769688             302 aa            linear   BCT 01-JAN-2025
DEFINITION  class I mannose-6-phosphate isomerase [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769688
VERSION     WP_010769688.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Jensen,S.O. and Reeves,P.R.
  TITLE     Domain organisation in phosphomannose isomerases (types I and II)
  JOURNAL   Biochim Biophys Acta 1382 (1), 5-7 (1998)
   PUBMED   9507048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..302
                     /product="class I mannose-6-phosphate isomerase"
                     /EC_number="5.3.1.8"
                     /GO_function="GO:0004476 - mannose-6-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009298 - GDP-mannose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33988
     Region          1..295
                     /region_name="ManA"
                     /note="Mannose-6-phosphate isomerase, class I
                     [Carbohydrate transport and metabolism]; COG1482"
                     /db_xref="CDD:441091"
ORIGIN      
        1 myilksipkp rvwgtsrlqs ysteqmdgki gsvytasgia eidspialgk etlrkvvlqk
       61 pekfglvkge efpliismta adedlsiqvh ptdtyareve nklygkseaw fflsepksgs
      121 iiagqtaese vvfrqavadg ryqqilaret iaandmayip sgtihaltkg slvyeiqqst
      181 dityrfydyd rldvtgekre lhtkkaletv dyqqtisksp faleqtldvr efkvkrtvih
      241 gtytneesiv qvltllrgnt cinhkmlmkg qsvlvlpdeq itvehsaecm iatpktywrd
      301 kf
//
LOCUS       WP_010769695             134 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Enterococcus phoeniculicola].
ACCESSION   WP_010769695
VERSION     WP_010769695.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..134
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14998
     Region          25..126
                     /region_name="cupin_HNL-like"
                     /note="Granulicella tundricola hydroxynitrile lyase
                     (GtHNL) and related proteins, cupin domain; cd02233"
                     /db_xref="CDD:380361"
     Site            order(34..35,66,68,89,91,93..94,113,115,117)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380361"
ORIGIN      
        1 mtneevkegi ifpvgeknea yaqyfigqsy lntliadpei nvgvgnvtfe pgcrnnwhih
       61 hegfqlllvt ggegwyqeeg kparrlkagd vvithdgvkh whgaakdswf ehlaitagrp
      121 ewlepvsdel ynql
//
LOCUS       WP_010769700             205 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769700
VERSION     WP_010769700.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..205
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=23024
     Region          107..197
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mtkkrslylf fltliiglty qflpysglnq silnvvgsiw nvalaglaaf ylskteflqq
       61 fkhlkflail wgipltfavg iafstiynlv igqattnsig siitiqmvll qvpfmlmgee
      121 vlstnilial qkqgisffws siicgilfal whipaygfhp vqllatllpt rlalnyiwkk
      181 tgsiwnswic hfvydligfi gffvk
//
LOCUS       WP_010769717             328 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Enterococcus phoeniculicola].
ACCESSION   WP_010769717
VERSION     WP_010769717.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..328
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36609
     Region          2..327
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mktlkksgls keemiqayre vlrgrrlder lwqltrigkt sfnisgqgae vaqvamamaf
       61 dpkkdyflpy yrdmtaclvw gmtskdvllg sfgkeadpss hgrqmpnhyg skehnivsfs
      121 stvstqmpla tgvaysaqle ksdfvtlttt gegsanqgev qeamnfagvk klpvifvven
      181 ndyaisvpik eqyanekmsd rahgygfegi tvdgndftev yltfkkaved arsgkgpkli
      241 elmvsrltsh sadddqnvyr skeeieemkk hdpldtfekq lidegylske eiekmdeevr
      301 aevdkatdea eampdplass lleqvyak
//
LOCUS       WP_010769736             290 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus phoeniculicola].
ACCESSION   WP_010769736
VERSION     WP_010769736.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..290
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32527
     Region          48..290
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mmkidiptmr aqmaegdkkr dtglteptti taikelsygp hgientfdiy ypvgtttclp
       61 tivsihgggf fygdkelyrf ytmylasqgf tvvnfnyrla pvhqypaple dtnalmnwll
      121 ihgkehyvdt eqlflvgdsa ggqlaeqyat ltsnphyagl mdfaiadvqf kavglncgay
      181 figqtgainq dfpfyfgetl peqtaqqfpv esfittdfpp afittathdf lkdvaeplat
      241 ilrskgveae fhlyenpdgk elhhvfhldq rnpigkqcne etldffrkfl
//
LOCUS       WP_010769746             408 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus phoeniculicola].
ACCESSION   WP_010769746
VERSION     WP_010769746.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..408
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=46245
     Region          1..408
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mkkimkwlee tfqpkmnkfa nnrwvsslkd tinqimplif lgsifavltl pseikgfewf
       61 anfwtpfgwt mgvigmmiaf llpmilmekf rmrgsrfvaa iagmilyami ispqlvkdgv
      121 vgfshdsfgs sgmfismisg ffvafifktl rkisffkedt slpdfvrtwf dqmlpvgliv
      181 ifgwvlifif nfdlylaiqs ifvplksvms niwgftlvnf ivvflyslgi sgwilfpita
      241 pvylqnieln inegaqmfat qsfdyaylki gglactlglv ilmltmkskk ltslgrasiv
      301 psifninepi vfgaiafnpm lmipmwinsv vvpllawflt ivipfgkipd iqfnlwyipy
      361 piltwlatgg hlgsvalavi ifvvstliwy pflrvydnqc ireeaeea
//
LOCUS       WP_010769799             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus phoeniculicola].
ACCESSION   WP_010769799
VERSION     WP_010769799.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..283
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30406
     Region          3..281
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkkffglaa vllvavglaa cgngssdtka tgssekndek tvlkvgasps phaeileqvk
       61 pilakegvel eivnfddyvl pnkaladgei danyfqhlpf fnkavedngy dfanvggvhl
      121 epmglyskki kdikelkdga tiivsssesd wgrvisilqt aglvkvkdgv dletatfddi
      181 aenpknlkfe ntiapellat tynndegdlv ainsnfaygi glnpledavl legddspyvn
      241 ivatrtedkd sdavkkliaa lhepevqswi iekwggsvkp vdk
//
LOCUS       WP_010769857             158 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Enterococcus phoeniculicola].
ACCESSION   WP_010769857
VERSION     WP_010769857.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..158
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=18756
     Region          4..155
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkldayekql leiinelisy likmgannqd aqdiaqdtii kileieailp akmirpwifr
       61 vginlyfnlf nrkkkyqeil nlhmlpthfv tketdyeply halnqldqks anlllmkyeq
      121 nlrieemafv lkrpkeslkt elyrarkklq timeendk
//
LOCUS       WP_010769804             396 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769804
VERSION     WP_010769804.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..396
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=44101
     Region          49..392
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mnknktnsld nkidygvilp vfllcligll slyvalthdv lekeivkemf kqcmwyalgt
       61 iaiiiimhmr lkwiwkltpy iyglgiavml allkfydkdm dqltgsknwf rfgpltfqps
      121 elmkiafvlm lalivtqhna ktkektlktd gflilkmfav tlpvialvll qkdfgtmlvf
      181 laifggvflm sgiswrivvp iilfavivgg gtiylvttdt graflsdlgi fkayqfarid
      241 swldpfhdag gasyqpaqgl laigsggmfg kgynvsdiyv pvresdmift vigenfgfvg
      301 gafvillyfi liyrmirvcf dtnnefyayi atgiimmilf hvfenigani gllpltgipl
      361 pfisqggsai lgnmigvgli lsmryqsvre psetrr
//
LOCUS       WP_010769879             301 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Enterococcus phoeniculicola].
ACCESSION   WP_010769879
VERSION     WP_010769879.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..301
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33369
     Region          3..301
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mttivlneti illfymavga flnfkrkyhp svnvfigyll tnialpaail nsfqvektte
       61 vmtlmratfg ysfillsvtl lvgltiatlf kkkdsfkrlw incltfsnil figipivekl
      121 ygeqgliilv vyntvanlfl ftigmmifsn srkmairqml ttpallaavi gflffyfeih
      181 lpfpllsftk vmggmtapls mvingvlfsq nnfiqllldk dnlqftlars iivpllfipi
      241 lqlivpdkmi lgiltlivam ptgalnaila ekyggngnka sqyialttvi smitlpvvml
      301 l
//
LOCUS       WP_010769882             251 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769882
VERSION     WP_010769882.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28696
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mkakridlik eyilenehvs lkeledtfnv smntirrdia qlledprfek vyggisvkkn
       61 qlisfenrnt enqevkqaia etaaqfiqng dliyidsgtt tkyildyldk diqitiitns
      121 ldvilraekf knisvfvfgn ifkkttrsfv glpseqvvnr ynitksfmaa tavsienglm
      181 nsdimeyelk khivekaein yllvhadkfd kstlltyapl saidtiitdk qfddsytsyf
      241 ennnidvltv d
//
LOCUS       WP_010769889             335 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010769889
VERSION     WP_010769889.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..335
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37159
     Region          1..324
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mdlrigvigt gaigrdhiqr ingitsgakv saisdinsea gkllaseiga tffaegedli
       61 asdivdavlv tswdptheky vleaikhnky vfcekplave idgcrrivda eikagkklvq
      121 vgfmrrydrg yeelkamvds kelgevlmlh cahrnpsvde sydtpmaven tavheidvlr
      181 wllqedyvsa evklpkqtsy thenlhdpqf iiletesgiq idievfvncq fgydikcavv
      241 cekgevalsd psyttlktkg kdstkvssdw kdrfvtaydr efqlwvdsvr aenitgpsaw
      301 dgyvasvttt acskardtgt kveitleacp dfykk
//
LOCUS       WP_010769902             234 aa            linear   BCT 01-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Enterococcus phoeniculicola].
ACCESSION   WP_010769902
VERSION     WP_010769902.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..234
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26413
     Region          1..227
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mdkgiifvlh grkeklstkn qavvtsviee lsipseigll egeqatleea mhsliqqgvq
       61 tiyfvpvllf pathakedlp qrandflqgk aeyqiaetla ttqsikaflv rtiqeahied
      121 nrevlliahg tphyeapyeq lkqmaksveq kviipvhtan yigehrypef leahteplfi
      181 lplfltdgfl tkkiketvqe mrgtkdvflp tlqdseelkq ailervresv ciqs
//
LOCUS       WP_010769946             191 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Enterococcus phoeniculicola].
ACCESSION   WP_010769946
VERSION     WP_010769946.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..191
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19868
     Region          4..176
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mttvsifgkg nmgqaigknf eaagnnvsyi qsdspkselg divilavpyp airsiiegyk
       61 ealsgkiiid itnpvnfdtf delvvpadss aaaqiatllp dakvvkgfnt tfgatletkk
      121 vanqqqttvl lagdnqdaks tignalegsg lavidagslk rareleamgf lqislaaaek
      181 iswtggfgvf r
//
LOCUS       WP_010769980             352 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010769980
VERSION     WP_010769980.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..352
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39455
     Region          199..316
                     /region_name="FUSC_2"
                     /note="Fusaric acid resistance protein-like; pfam13515"
                     /db_xref="CDD:433273"
ORIGIN      
        1 mdqsfikelt tfhktkdnpf rlvgagicml silllgyalh dlaigsfgsl giftflyyqn
       61 ipikqlitrl slvgfflllg nflgmlsthl swtapilvgl vaflgrllfr lfkiakpgvf
      121 fivlvtgmgs stkiplesip kmsffflvgi lisiivaclv qkteklppvp vkkvtlqerl
      181 ytdpasivda lfyggilffa vylsqslhlv npywlvvsca ailqgdtlra mmhrnvqrif
      241 gttvgilias fllnlplstf qsiivitmly ltveffirrn yavanffttp mtlllsmlvr
      301 hqyvfslvqy rflgivlgsl lgllsawimi tgltfynraf qlheilhddi ek
//
LOCUS       WP_010769947             404 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769947
VERSION     WP_010769947.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..404
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43192
     Region          7..404
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mpkilksltn qillatilgi ilglifheqi vflkvvgdvf lrliqmsvvi limgavveav
       61 gsldpktlgg iglkvmlwfi gstilaagig vgmgllvkpg advvianldv eqitynssgs
      121 lseiileffp sniiesmana nmiqvivfal lfglalslta kkksqsvlef vvsfnhvilk
      181 mvtlvmklap igifclvapm igtvgvevll tltkflltlg iasilflmlw llltavycri
      241 pffslckkmw rmsvvafttt ssavtlpiql edseeklgis nrisklvlpl gmtlnsngla
      301 lflsiaiitf aqfyginlal pnliqvvils tlaclgtvvv pggglvalat vmpmiglpte
      361 siailagidw fsgmfrtlln vdadttvali iakdegeldy skyk
//
LOCUS       WP_010769985             508 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus phoeniculicola].
ACCESSION   WP_010769985
VERSION     WP_010769985.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..508
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57432
     Region          4..505
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mltltnitqq fgekilyegi dlqlnagehl gligqngagk stlikiitge ilpddgrilw
       61 qknarigyld qyvevdehls iraflrlafk dsyekeekia alyteygetl ddrllekagq
      121 lqtqldqgdf yqidtlvnem stglgidvlg mdtplknlsg gqrsklilak lllekpdvli
      181 ldeptnhldd ehiswltqfl qsfsgaflvv shdraflnqi tthiadiefg rlikytgnle
      241 qalkqkeqnr esylrqyhaq qkhiektesy irkykagsrs tmaksrqkql dkidrltppg
      301 stakpnfdfp yapivttlal ettsleigye rpllppiqlt irygekvair gfngigkstl
      361 lktligeiek ldgdfhfpen tkinyfsqdl vwsnpfetpl qylsdlypka tikelrkhls
      421 raglpnqlaq eplstlsgge qtkvklcqmt mqkgnflild eptnhidqet kvslqnslas
      481 fagtviivsh eqefyqdivd rvieiqad
//
LOCUS       WP_010770016             316 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010770016
VERSION     WP_010770016.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36158
     Region          6..306
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          <203..>253
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
ORIGIN      
        1 mtqtdsltml qfiemllkhg nytkaaksly isqpyltqvi kkkekelgve lidrqatplq
       61 ltdagriyyh ylttllaeqn qfkkrleayt spekiilkvg ilsslgtyll plflpefltl
      121 ypqvqielie dvphknekri lnsrldffig qnpetlppql tayergshgy yaiipesskl
      181 ykrnvrfvds sslslnqllq enliltlhgs airhqidyli qkfaiqpkii lesnniftig
      241 klaqenlgvt flpdsvqihe nggnynickl slqdvslnyf iahlnskpin diekafidlf
      301 lnaveksikk deetrk
//
LOCUS       WP_010770033             525 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus
            phoeniculicola].
ACCESSION   WP_010770033
VERSION     WP_010770033.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..525
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62019
     Region          5..123
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          247..518
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mllkqllelp ilknsktltg sigldnples vmvleaidie kwskqhqlil tsfyaltdas
       61 mdqvrlffkt mrkigvsglv ikvdrlitmi pewvielgve yciplikvhq dvsyeaimla
      121 vyepllnhqs hllrtyyevr qrfmkvernr ssfdqimqef fqliekpcfl siphldihin
      181 kgttfedyvv iqqypmknie ftknryeylh lfshknnqai tavkvdilnp fndlctllvy
      241 qkdaqipesk vmiienvvdv iyerlqmeyl qkkerytrln nladailqnt ptdlneltll
      301 leeanieqyd fyqaiafsst nfedkqrkdl vlqklhslra khiffehhny liflynfqha
      361 sqqitkqtls klfdfsilek ekaslilsev krkqaikeil pecldsirfn rhfylapiln
      421 ysdlgvfsmf ikghqldniq qiiptglyhl weneedlflt lytffisnrn ykktaetlfl
      481 hsktiryrln kieqlleidl tnpiqlvnye vgtyllelkk rsqsk
//
LOCUS       WP_010770034             267 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus phoeniculicola].
ACCESSION   WP_010770034
VERSION     WP_010770034.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..267
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30459
     Region          25..267
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mktaiqlssg akgtliskps dvgyllyfhg ggfiygsknd lpeslvtifq kqkfsilald
       61 yllapnssls eiiqstfdnf lelkdtvikd spfsfcgrsa ggylmlaltk klienkqalp
      121 eklinfygyt dlefiqtqre isnysvtpdm iqsinlkeqt wddplfqryl lyiygvqnqk
      181 ltdyyqisad qkealaispe ilaqfpptfs tasttdmevp fryskrlkni phsqfravyd
      241 lphdflkete neqvrtlmte leswlkk
//
LOCUS       WP_010770080             156 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus phoeniculicola].
ACCESSION   WP_010770080
VERSION     WP_010770080.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..156
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17304
     Region          6..146
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mstqeykhil vgidgseqan aafkkaveva rrnqgtvyva nvidqqyynf mgytpmnqtl
       61 vdqeteeakk liqeckdygk svnyekiegi vaygsakeam shqlpekyqi dlimvgqsgl
      121 naverfmigs vssyiireal cdvlvvsste dtevak
//
LOCUS       WP_010770081             105 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010770081
VERSION     WP_010770081.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..105
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12059
     Region          8..101
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(28,31)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 miipksleel atyvekgknv ffftagwcgd chfikpkmpe ieadfpewqf vevdrdafmd
       61 vavewnifgi psfvviedgk elgrlvnknr ktkeeieafi qsvqk
//
LOCUS       WP_010770101             329 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010770101
VERSION     WP_010770101.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..329
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36759
     Region          1..315
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkvgilgaah mhvhsyikel kkqgimitgv ydrtreqaee iahlyqlkvs esieellasd
       61 cntvficsen sfhkelaera flkkkhvive kpmalttkda rqmiesavka evklmvahpv
      121 rfsttaqelk qiideqalgn lvavnasnhg knpggwfiep tlsgggalid htvhisdliy
      181 yyfdltpksv rafirktket lkvedtgllq vtftngvims ldtswnrpat ypiwgdamve
      241 lifekgyltm dgfgrkmkiy sdslnqiedy yygndmdgam iqafiqaidh glpapvsgea
      301 glytvaitek aflaaiqere vnfeeeete
//
LOCUS       WP_010770109             244 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010770109
VERSION     WP_010770109.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..244
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27117
     Region          4..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mntiidvqhl kksfgknevl kdinltvdkg evvtiigssg sgkstllrci nllekptdgk
       61 ilykeenvle kgyslpnyrt hlgmvfqqfn lfnnmnvlen clsgqltvlk rskeeareia
      121 iknlenvgma ryidakpsql sggqkqrvai aralsmnpdv mlfdeptsal dpemvgevla
      181 tmknlahtgl tmivvthema fakevsdrvi fmdkgviaee gtpedifvhp keartkeflh
      241 rvld
//
LOCUS       WP_010770126             436 aa            linear   BCT 01-JAN-2025
DEFINITION  replication-associated recombination protein A [Enterococcus
            phoeniculicola].
ACCESSION   WP_010770126
VERSION     WP_010770126.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..436
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=48029
     Region          1..427
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mqqplayrmr prnldevvgq qhlvgegkii rrmveasmls smilygppgt gktsiasaia
       61 gstqyafrml naatdtkkdl qivaeeakms gtvillldev hrldktkqdf llphlesgri
      121 imigattenp yitinpairs rtqifevkpl teedikkave salhdkergl gtypvqleek
      181 allhlsratn gdlrsalngl elavkstpan degtilltls vieecvqrka lthdkdgdah
      241 ydvisafqks irgsdvdaal hylgrlveag dlaiicrrlm vigyedigla npaaaartvn
      301 avlaaerlgl pearipladt vvdlclspks naayvaldea isdirigkag dvpdhlrdsh
      361 ykgakelnrg vgylyphgye dawvnqqylp nklknahyyk pkstgkyeqa lgqqyqriqe
      421 wkkknrqtap ltesdn
//
LOCUS       WP_010770149             176 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Enterococcus phoeniculicola].
ACCESSION   WP_010770149
VERSION     WP_010770149.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..176
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21050
     Region          7..173
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mikdvsnehf feelyleyeq kiyflaysii nneqqaedit qdvfeqlfeq lstlktydsl
       61 trkkyilris knraidyyrk nkvelnyken lfpkneepvn nveiyfdsli seeqfnrvta
      121 nlkdsylnvf myriyyglsg ketaelmnir vdtvkkqler akkkvkeile gelkdg
//
LOCUS       WP_010770155             245 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus phoeniculicola].
ACCESSION   WP_010770155
VERSION     WP_010770155.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..245
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27384
     Region          3..242
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mslkieqvtg gyghipvlkd isfdvnngem vgliglngag ksttiknvig lltpqkgkit
       61 idglglktqp eeyrkkigyi petpslyeel tlkehievta maydipieva fqraekllkt
      121 frlenklewf panfskgmkq kvmvlcafli epslyiidep flgldplaih allelmdemr
      181 regaailmst hilataekyc nrfvvlhnge vraqgtmael rqefqlpdss ldeiyvaltk
      241 eqdde
//
LOCUS       WP_010770167             591 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Enterococcus phoeniculicola].
ACCESSION   WP_010770167
VERSION     WP_010770167.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..591
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=69706
     Region          25..>570
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mrktvvrrah prpqfiresw qlldgewgfs fddkkigiek rwfngfesth qikvpftyet
       61 klsgifdssh hqvvwyqkki qinekkaksi lfegvdyfsq vwlnghliga hqgayerfef
      121 elsdflvege nlivvrveds laceqprgkq rwlkdnfgcw yiqttgiwks vwiedhlhsq
      181 rlqqvkmtpd fendqiifep slhdrvaard atyeleidvs feevlvnqcr vtlshemqqi
      241 tldtrikeda cwgtkvwrpe qpnlydvtfr lwdhqgqlvd cvdsyfgmrk isiekgqvll
      301 nnqkiyqrli ldqgywaesg itppsieame kdidqilalg ynglrkhqkv ederflylcd
      361 ekgvlvwsem astyvfndla venftdewra ivqqnynhps iitwvpfnes wgikgvksdk
      421 kqqqftemiy hltktidpnr pvitndgwvh tisdiltlhd yeefgerftn rykdkekitg
      481 neyqfneewy afadgyeytg qpviisefgg iaftsneken wgygsqvntq ddflkrfdki
      541 hesiqkipyl vgycytqltd veqeinglld vnrtsklpvs rireinerrt r
//
LOCUS       WP_010770170             337 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus phoeniculicola].
ACCESSION   WP_010770170
VERSION     WP_010770170.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..337
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38169
     Region          1..337
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mitfgiigcg niaavhaeai reiaeaklva vcdsdrekgr lfgkmnqavv yddykellad
       61 qtievviiat phylhkemti esfshdkhvi cekpmaitvs eaneiyrake mfkkeyavcy
      121 qnrfnasfik lkellkqekf gqlkgircei awnrneayya easwkgtwek egggvlinqa
      181 ihtldviswf vkcpqkikgk imqtrlteii evedsamgta lidervpvvi fasnnfssdp
      241 spsvlfdfee amvelknkal fingqtiplg nekesnvske ywgnghqrli qtfinqliek
      301 edpyrsylac ndaidslklv cgiydsdktg ewinlte
//
LOCUS       WP_010770186             713 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Enterococcus phoeniculicola].
ACCESSION   WP_010770186
VERSION     WP_010770186.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..713
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=81477
     Region          3..713
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mktayidtrh gtenqysfsn gnclpytgvp fgmnyfapqt tsekgswwfh pkdrtfqgyr
       61 lthqpspwmg dyshllllpy sgalsepslf haqssyrpee stfspshlti telryqitst
      121 ivpsmyggll dihysdtdas lllslgenyq ieqtdahtlk ghvinfsgce dpnfsfyftl
      181 nfekpiqamt dtknkegiil iqfgnvsqqt vrfgtsfisl dqatlnlsre qeqtltdyle
      241 ksdqkwasyl nkitvthhde dqvktfyhnf yrtflfpqtf yeidgtgqki hydtlsktvr
      301 pgvlytnngf wdtyktlypl ysliakeeyg emlegfltsy ketgflpkwl spderglmpg
      361 tlidaviada avknirpdlm pefleamkka atiqsdnpny grqgtydylk ygyvpldyhe
      421 svnhtldycy sdfcihqvak tvkdseadfy ksqaanyknl fdptvgfmra kdkegnfren
      481 fldirwgkdy aegsawqssf avyhdfegli qsyggnevfe eklidlcnqa prynvegygf
      541 eihemsemaa tefgqlaisn qpsfhypflf syigkpemaq pllkqlmtqe fnasttgypg
      601 dedngstaaw yifnsmgfyp vcpgageyvl gmplfdnvtl hlsngrdlel sagpnypqqq
      661 fihevkrngq mhetlffthe dllsggtidf hlgtvprprt yrtdqlpfsl snk
//
LOCUS       WP_010770192             236 aa            linear   BCT 01-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010770192
VERSION     WP_010770192.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..236
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27111
     Region          1..230
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mmltlatfni asgripdter mnqlfnkhqi diiglqevdc qtkrnardlv kelageeyry
       61 qlfskampfe sgnygnalls kypvinykei gflssgeepr aaqfvqirlg nnqviticnt
      121 hlsfesieir qeqseeilqn mkviggenqv imgdfnmdqs eeewellkkd yqlangqrnl
      181 wlqtfrepde nmkrasidni lvsntielve ttmietqlsd hnllkvkiki degdtr
//
LOCUS       WP_010770240             252 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010770240
VERSION     WP_010770240.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..252
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28687
     Region          1..246
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlkrerhahi lellekntfm tvsdiaeeln vsemtirrdi nelsdsnqlv rlyggaqkid
       61 rknkelathe kinlhieqke yigkimnsli qdhqvvfvga gttilyalpf ikkqnlmivt
      121 nsllafnyvi ehtdyrillt ggdftpitee figehaektf etinidiafa atngiynnnv
      181 ttsnyleggv qraafknakk kivvadstkf nvsdvytfyk lsdldyvitd dqideqtlnf
      241 yqsygtllnk ks
//
LOCUS       WP_010770277             135 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Enterococcus caccae].
ACCESSION   WP_010770277
VERSION     WP_010770277.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Song,F., Zhuang,Z., Finci,L., Dunaway-Mariano,D., Kniewel,R.,
            Buglino,J.A., Solorzano,V., Wu,J. and Lima,C.D.
  TITLE     Structure, function, and mechanism of the phenylacetate pathway hot
            dog-fold thioesterase PaaI
  JOURNAL   J Biol Chem 281 (16), 11028-11038 (2006)
   PUBMED   16464851
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..135
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14649
     Region          7..115
                     /region_name="PaaI_thioesterase"
                     /note="PaaI_thioesterase is a tetrameric acyl-CoA
                     thioesterase with a hot dog fold and one of several
                     proteins responsible for phenylacetic acid (PA)
                     degradation in bacteria. Although orthologs of PaaI exist
                     in archaea and eukaryotes, their function has not...;
                     cd03443"
                     /db_xref="CDD:239527"
     Site            order(36,65,72..75)
                     /site_type="other"
                     /note="CoenzymeA binding site [chemical binding]"
                     /db_xref="CDD:239527"
     Site            order(37,39,42,66..70,72)
                     /site_type="other"
                     /note="subunit interaction site [polypeptide binding]"
                     /db_xref="CDD:239527"
     Site            order(38,46..47,50..51,65)
                     /site_type="active"
                     /note="PHB binding site [active]"
                     /db_xref="CDD:239527"
ORIGIN      
        1 mhlldylnie ttelskskvv ltmkiedfhk qpygilhggm ngilietacs lganeqldks
       61 syavgidlqi nhlkgvpngi lttvatpdri gqsiqvwegk ifneigemia vgrctlvsrk
      121 iknnegastp pfskq
//
LOCUS       WP_010770282             310 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus caccae].
ACCESSION   WP_010770282
VERSION     WP_010770282.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..310
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33596
     Region          1..310
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mnvekqtvkf dakglkvagi lnipdgldts kkypaivcvh pgsscknqta giyaeklaal
       61 gyvtlvfdas yqgesegepr fieepaarve dircavdylt tidyvdvdri gvlgvcaggg
      121 yavnaamter rikavgtvvg anigrvnres hgdtvgvika leaigqqrtv eargenplia
      181 nwipknqeer eaagitdidi ieavdyyttp rgqhpcspnk vrytsfgsvi gfdafhlvee
      241 lltqplqiiv gsvqgafgsn rdghelfara asekkdlyvi egashydlyd qeepvglave
      301 rleafyrenl
//
LOCUS       WP_010770317             225 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Enterococcus caccae].
ACCESSION   WP_010770317
VERSION     WP_010770317.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..225
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=25979
     Region          75..173
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mfkclneyid fsvkvndyit timtdngisc eqyhyshvwk liesqgvtir gfqfkdiase
       61 riaglfiqdq lettigfnqe ldepsknfai shelihylfh kdeqnqiffd ttknmqhsyh
      121 qellefqani gasvilipds vlcyvlkkgw nssriattfg lseemlavrl iqimqgnlgf
      181 sfqsakdytn vifyafhskg retaaqiata leyqmkrpkr fiqvr
//
LOCUS       WP_010770351             438 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus caccae].
ACCESSION   WP_010770351
VERSION     WP_010770351.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..438
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=47700
     Region          11..432
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mtksasakgs mvnrlndils pfankignqr hlkavstgmm fglpfivigs fflifanppi
       61 nidqydpaka gvfmkflaaw kefavanydm itapynltmg iiglisvfgi ayslsneykl
      121 naamngmvsm vtyllvctpv kegtislayl gtnglfvaii lgllvvevsr ffevknikis
      181 lpdtvppmvv tfintlipll tniilfygln lvflgmidkt fpdavmsvlt pavniagslg
      241 glllivtlgn vlwlfgings siifpivftl gvaqtglnae qaaageamth lmnlqmfris
      301 vlggagntlg lvvlmmfskv pqyrtigkls fvpgicsine pvifglpivf npilgipfli
      361 mpiislflty faqkiglisl gfivdpsftp ffaqaylatm dwrnivfyvf lvilsivvyy
      421 pffkvfeknq tklvdevl
//
LOCUS       WP_010770455             280 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Enterococcus caccae].
ACCESSION   WP_010770455
VERSION     WP_010770455.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..280
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31573
     Region          13..275
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 miesltdtvl lnnevrmpgf glgvfqvsne dtvlsvqkai eagyvsidta qiygneagvg
       61 egirrglast gkkreelfit tklwnhhldy dqtitefnds lvklgldyld lylihwpgnn
      121 eflepwtame dlylsgkika lgvsnfeihh lktllettri kpvinqvelh prmaqneira
      181 fgkeheilte awsplmqgkl leddtilnla skhnksaaqi ilrwhiqndi ivipksvkea
      241 riksnaaifd felskddlam idqlddgtrv gpnpdtfffe
//
LOCUS       WP_010770447             398 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus caccae].
ACCESSION   WP_010770447
VERSION     WP_010770447.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..398
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43591
     Region          5..397
                     /region_name="ryptide_ex_MFS"
                     /note="ryptide export MFS transporter; NF041056"
                     /db_xref="CDD:468984"
ORIGIN      
        1 mnknkafnkl ivgqmisnig dtiytiaivs svfsltnsal aastvpviit gsmvlsgllt
       61 plivvrvsls kilqvsqlfk tiilaglaty lqlnvehldl tilyvfiagi afldgcaepv
      121 staliphyvs ehyliransi fntmlqvvsi gswaigssll iifsvmnllw ldvgvfaisa
      181 iilwllpkvt krveseknew enfligwqgi rkqslvrvvv rmdilenian tawvsaivlv
      241 yvkevlhvse swwgyinaty fagamlgsii vmrhsnwinq nkskavitgs lfgaivtflv
      301 vpgwhpifil icsvfvgifs qiknipqata iqqkipkdkl asiyasmnvl ytgtfalasv
      361 smglvseylg vrtvfvlsgi llfvvamiak nkeslfde
//
LOCUS       WP_010770409             902 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus caccae].
ACCESSION   WP_010770409
VERSION     WP_010770409.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 902)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 902)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 902)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..902
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=103787
     Region          120..902
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mtvllftlep nclhiqekeq qtllseqilp fsdfefpkta qilttqikel yptvegaifn
       61 titpefylvn kqvsllnesl enftkqfsel lnipillase qsqetdlitv lkekadylaw
      121 nldyfgytpg keeysvesll tigngfmglr gttpemtlsn dhypatyiag lyneesseia
      181 gqivenedfv nspnnqsihi kvsgtdewln lknsilhylh rnldlktglf tshmiiedsy
      241 rhqlkitahk ivnmakmnny sikysiqpln fskeitvkat tdgsvynfnv eryrnltakh
      301 fhitqllaek nntvieiett qskikvqqis tmigdffdpa aikntiqkek ieqtltfsae
      361 knnlytlekh iqvtasiaeq swgnpslpat sfdlefaesk raweslwkks diqltgdmms
      421 qkllrihtyh llvsaspfnn neldvsvtar glhgeayrgh ifwdeifilp fyilhfpeta
      481 kqllmyrynr ldkakenare sgyegamypw qsgldgsedt qklhlnplng ewgedhsilq
      541 rhvslaiayn iwmywnnsgd dlfikeygae mlleianfwr saatfdettn ryyidkvmgp
      601 defheaypds tesglknnay tnlmvvwlfe eletilslln tqeqaklfnk teitaenlek
      661 mndirkhlsi evnedgiiaq yegyfdlkei dweqakeqyg niyrmdrilk aegqspddyk
      721 vskqadtlml fynlnkekid eileelgydl ptdyleknll yylnrtshgs tlsrivhaql
      781 aeevafhdls wklyqealys dyqdiqggtt aegihtgvma atiyvtltty agidikknyl
      841 tikpnlpknw sditfnfdhk gihysvtvsk nsvqicpskk ttvivkdqsy qltadentii
      901 ty
//
LOCUS       WP_010770554             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Enterococcus caccae].
ACCESSION   WP_010770554
VERSION     WP_010770554.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..255
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28645
     Region          1..219
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mkidlfhvgi atcilsinnq vkiaidpalf kkgtklkfks feserlenps fdsdtfedid
       61 iwlishfhed hidilgkeki sqdslvlsnk dsltfladkn vkkigwkekh vfskdnitve
      121 iqaipayhan sflmrklvgk vngylltvti dsvvqkiyft sdtvfhkdii kalpqsidil
      181 ianlgnvqan ktggpltmni smldkfvdil spsvivpvhi ndlshyetqe vsvteagykv
      241 letgkwhtli nqysm
//
LOCUS       WP_010770580             201 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Enterococcus caccae].
ACCESSION   WP_010770580
VERSION     WP_010770580.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..201
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22231
     Region          9..199
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mnnhyytenp dlahdleqws felrgkkfqf ltdsgvfsrn tvdfgsrvli dafdweelpe
       61 gklldvgcgy gpiglslasl sgrpvemidv nqravalaqe nakknhvenv dihtsniyad
      121 vhekeyaaii snppiragkk vvheilseay prllvggtlt vviqkkqgap saekkmaevf
      181 gnveivtkdk gyyilksvke a
//
LOCUS       WP_010770593             429 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 125 protein [Enterococcus caccae].
ACCESSION   WP_010770593
VERSION     WP_010770593.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..429
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48669
     Region          2..426
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 mtytkipnsv qqfmdkithl cgedhagwae nfnaafantl tttvkkqedg ttflltgdip
       61 amwlrdstaq vrpylviake deelremicg lvqrqffyit idpyanafne tpnsaghqtd
      121 htkmdpwiwe rkyeidslcy pvqlayllyk ntgytkqfdt nfiegvkkil tvftteqehq
      181 sslytferdt trledtlpne grgsvvgktg mtwsgfrpsd daccygylvp snmfavvilg
      241 yieelfteil sdpevvkqav slknqindgi qkygktdnqq gvtvyayevd glgnssimdd
      301 snipnllsap ylgyttidda vyqatrktvl skenpyfyeg kyakgigssh tpenyiwpia
      361 lamegmttqd kaekarilds lvandggthl mhegfdvddp snytrewfsw anmmfcelvm
      421 dyfdirvar
//
LOCUS       WP_010770617             395 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu [Enterococcus caccae].
ACCESSION   WP_010770617
VERSION     WP_010770617.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     gene            1..395
                     /gene="tuf"
     Protein         1..395
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43150
     Region          1..395
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makekfdrsk phvnigtigh vdhgkttlta aiatvlakhg ggeaqnyadi dnapeekerg
       61 itintshiey etdarhyahv dcpghadyvk nmitgaaqmd gailvvsaad gpmpqtrehi
      121 llsrnvgvpy ivvflnkmdm vddeellelv emevrdllse ydfpgddtpv iagsalkale
      181 gdasyeekim elmaavdeyi ptptrdtdkp fmmpvedvfs itgrgtvatg rvergevrvg
      241 deieivgike etskttvtgv emfrklldya eagdnigall rgvaredier gqvlakpasi
      301 tphtkfkaev yvlskeeggr htpfftnyrp qfyfrttdvt gvvelpegve mvmpgdnvam
      361 dvelihpiai edgtrfsire ggrtvgsgvv seivk
//
LOCUS       WP_010770619             108 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010770619
VERSION     WP_010770619.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..108
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12500
     Region          1..99
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 meeklrkiyv pmtetgfyil fslkeerhgy siiqyvknlt nqeiiisagt mygslskmek
       61 dgliqatkee nrrksylite lgneillhei nrinrlykns igakvnee
//
LOCUS       WP_010770663             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010770663
VERSION     WP_010770663.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..255
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30159
     Region          7..109
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(8..10,24,41..43)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(55,58,62..63,72,91,95,101,105,108..109)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mekeklltvg qvaeimklsk skirywddmn lltssrnrdn gyrmfdmedi ltisdidfyr
       61 kldipinkmt nlyrkspeel wsildetqtr vadelaelek kqqgikhrkd qllsliklke
      121 kefidepldv eriipidlkd pnelqtyidn psslvvyids knekeiiygf avttkefvee
      181 vsiwqrpeqt nysykqfllt iksddpldnn fqsvknklee qgyqtgtmvg ryimtaeeqd
      241 gfyrdyykaw ievnn
//
LOCUS       WP_010770697             263 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010770697
VERSION     WP_010770697.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..263
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29998
     Region          22..237
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mldlfdflhy lnttkrdaty sriiiylfnh lneiqtltit eiaercfvsp atltrfchhf
       61 glsnfaslre slivlgtmkk hsglrmkeqe lidlkddpks yltsygaeii tavndvltti
      121 dieqvdhlla dihqadevil igysstlela kdlqlsflln qklvfvgetv etqqafveel
      181 seksvvivis sygsllnrss elmrkisdsp aksilltqht qntltnqfdl smnvtttnyv
      241 rignypltff ldyfvrryts lyq
//
LOCUS       WP_010770703             243 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Enterococcus
            caccae].
ACCESSION   WP_010770703
VERSION     WP_010770703.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..243
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=27489
     Region          1..>219
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mitfeqvskf yshngvavta ldhidlkiqd heifgviges gsgkstllrm intlelpsqg
       61 kikiagtdlm qlndtqkrks rkkigmifqq fnllynqtvn enialplrln kaydqqkvre
      121 vlefvrlsdk gnhyprqlsg gekqrvgiar alitkpemll cdeptsaldg qnaydilell
      181 rrinqtfgtt mvivshelnl ikqlcnrtai lekgkvvetl eiqkgqqqpq fssyyervre
      241 slg
//
LOCUS       WP_010770722             250 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus caccae].
ACCESSION   WP_010770722
VERSION     WP_010770722.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..250
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29025
     Region          155..231
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mentigilhi geesdvneni alvikkafde eqscslitvt eksqiasldg lvinleqssd
       61 yvkafqwlih lqeecslfiw ilcseqnsel irlyphlskn svielvsydq gienlgtiik
      121 nainyknhll yqmgpkkeeh dhfldasklc lvvhetritl trkefkiiel lyqniedvvt
      181 yheineviyg nstgepieky rvanfifhir nklkeqtyfe ieivrtkgyi ltcpkkedif
      241 fkdinekvlq
//
LOCUS       WP_010770782             281 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Enterococcus caccae].
ACCESSION   WP_010770782
VERSION     WP_010770782.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11573834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..281
                     /product="VOC family protein"
                     /calculated_mol_wt=31456
     Region          9..132
                     /region_name="VOC_BsCatE_like_N"
                     /note="N-terminal of Bacillus subtilis CatE like protein;
                     cd07255"
                     /db_xref="CDD:319918"
     Region          170..279
                     /region_name="VOC_BsCatE_like_C"
                     /note="C-terminal of Bacillus subtilis CatE like protein,
                     a vicinal oxygen chelate subfamily; cd16359"
                     /db_xref="CDD:319966"
ORIGIN      
        1 mvytlpketi vkqvklkven ldvmtefytq miglvllnke qntaflgaqn sseaivilee
       61 lvdpilndkt tglyhtafll ptrkdlgnsl lwllqnniei gaadhgysea iylsdpegng
      121 ieiyrdkpmt ewdiradgei igvteeldgd avvaeadgqw lgmapgsrig hvhlqvadle
      181 etetfyeklg fslksnfgrr akffaageyh hhigtntwng ehvaligenq lglawytfql
      241 psreafelfv kqlgetsvey vkeneqvviq dpngmkikfg y
//
LOCUS       WP_010770832             177 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Enterococcus caccae].
ACCESSION   WP_010770832
VERSION     WP_010770832.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..177
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19696
     Region          3..174
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 msreiilyia asvdgyiaea dgsidflggg ielveedtsy qelmekidtv vmgrttydqv
       61 vnelspdeyp yeeqmsyiit shpdentekl mftsqnpvel vqklkkqegk aiwivggasi
      121 iaplveakli dtyilttipk ilgkgiplfn efngpvalkv eqvyvkndmv yttysnk
//
LOCUS       WP_010770836             204 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            caccae].
ACCESSION   WP_010770836
VERSION     WP_010770836.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..204
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=22035
     Region          101..199
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mktndtlhss tmrlvggall mligfwglma fswawwglfv ggalawmlaf gkdsksafhk
       61 prklwvipva vlsyfviglv igllskslgf nwaanpasgh lgaiilmlpf mlmgeellgi
      121 gileaaqskg lpliastlls alvfglmhip sywdgswfst vahvlllqgv arlilniayl
      181 kmgksiwgsw iahvlidlia lsvm
//
LOCUS       WP_010770888             254 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus caccae].
ACCESSION   WP_010770888
VERSION     WP_010770888.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..254
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27716
     Region          2..240
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mielvgvskn ygtkqalkgl nltikqgeif gflghngagk sttikslvsi iqpssgsikv
       61 dglelsenrq aikqkiayvp dtpdiflqlt ageywdliga ayeldetqkq trlselaslf
      121 dmlshqdetl asfshgmrqk tiiigallpd pdvwildepl qgldpqaafd lkqmmkahaa
      181 kgktvifsth aldtaqqlcd qlailkkgel iyngsvdnll aqspdeslea iylkmagrqs
      241 dtqllerieg etne
//
LOCUS       WP_010770903             309 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus caccae].
ACCESSION   WP_010770903
VERSION     WP_010770903.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..309
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=36195
     Region          7..302
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mlekmkleqy fdycryqkkl dsktlkayki dlrqffeyie qtdvdlinrs tiehyiqfla
       61 csykatsikr kyaslktyfs ylvymefisi npftnirlql kvetilprvf sldtleqllk
      121 taysqsynpv hkqssfqrfs tvrniavlel lfstgirvse lcnltmentd lanqkilikg
      181 kgskerilyl snqevitamk kyvalrdhsk sdcphffinr lgerlseqsv rtiiknigrk
      241 anlsvrltph mfrhtlattl ldegvdcryi qsilghssik tteryihvsl tmqknvllkk
      301 hprhhfsfg
//
LOCUS       WP_010770921             323 aa            linear   BCT 01-JAN-2025
DEFINITION  ring-cleaving dioxygenase [Enterococcus caccae].
ACCESSION   WP_010770921
VERSION     WP_010770921.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10327061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..323
                     /product="ring-cleaving dioxygenase"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36836
     Region          7..131
                     /region_name="VOC"
                     /note="vicinal oxygen chelate (VOC) family; cl14632"
                     /db_xref="CDD:472697"
     Region          158..314
                     /region_name="PcpA_C_like"
                     /note="C-terminal domain of Sphingobium chlorophenolicum
                     2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and
                     similar proteins; cd08347"
                     /db_xref="CDD:319935"
ORIGIN      
        1 mdthirgihh vtamtssaek iyrfftdilg lrlikktvnq ddietyhlff addlgsagtd
       61 mtffdfpgip kgtkgtntis rtsfrvknda aliywidrfn enqidhgeiq erfgkkylef
      121 edfdqqryql isdennqgvt sgtpwkksdv pteyaltglg pvfvtvadfd hmqrvlievl
      181 gfklidaegh fhlfevgdgg ngasiivehr ddlpeaqegf gnvhhlalrv adqealrfwi
      241 dkinrlqfpn sgfverfyfk sdyfraaphi lfelatdgpg flqdetyeta geklslppfl
      301 eskrteieef vrpfdtsdan ksr
//
LOCUS       WP_010770950             404 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-glycerol glycerophosphotransferase family protein [Enterococcus
            caccae].
ACCESSION   WP_010770950
VERSION     WP_010770950.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..404
                     /product="CDP-glycerol glycerophosphotransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=48740
     Region          22..396
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mnfaklrqqi fkmrkrdlfp likliltyip gklyrlfnsd vwviteyend ardngywlfk
       61 yiretypnkk vfypinfecn dfnkikslgn yikfggikhy ilfwgcskfi gttkyygfpy
      121 gricedlvqw dlhdfknifl nhgvargyss ivdakntnyd liismsekek eilikanfqs
      181 sekvkvvgfc rydslkniis dkkkivimpt wrnwldfrle idesnkekit kqfleskyyk
      241 sffslinnrs lldfldkndi elifylhgya qvysdyfyss ssrllvaske eyfvqdllki
      301 sdllitdyss vtydfcymkk pmiyyqfdkd efeekqyaes kyftydkdgf gpivdteenl
      361 vimikemyek nfeledeyrv rideffkydd ekncernyle ilnl
//
LOCUS       WP_010770958             372 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Enterococcus caccae].
ACCESSION   WP_010770958
VERSION     WP_010770958.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..372
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41204
     Region          37..365
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mgslfkqskl lfwtveivlt iigvffllkm pniftpifgm vsavfmplli agflyymfdp
       61 ivvflekrgl priggfllsf ailvvlialv vmnvvpqlvn qslelsqslp syaeemnqwl
      121 ndlgdleafk gfniqeqldk anitisniln faivgvtnsl skivgllmrf fillftvpfi
      181 lffmfkdghk fldamshffp ksirselrqt vrelnqtlsa yisstvldal iigilsfiam
      241 tifkqpyall lavfcgltni ipyvgpfiga vpailvglfi spwqalymal silviqqldg
      301 nlikpllmgk slnihpltii lvliasgsvg giigmlicip vyaviktlvl nigkiyrikk
      361 gstekvlkde iv
//
LOCUS       WP_010770972             169 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010770972
VERSION     WP_010770972.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..169
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19440
     Region          3..67
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mlksnlaeni kkyrkkkslt qvelaeklni skhsiisyek gatfpssdil enmmelfevt
       61 pnqlffpiyt dedeitdkea kikelesyre nilttvknie dnaslieykd pvydeqgnii
      121 eykdveisam dqaigvlvka idlenldmrl lievfnmkid geikkidik
//
LOCUS       WP_010771036             240 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Enterococcus caccae].
ACCESSION   WP_010771036
VERSION     WP_010771036.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..240
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=26317
     Region          24..239
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mgrsvigiaa neiedagakl yhlpisytpy gyvkavqnsg glplilpvgs pdlakeyitq
       61 idklilaggq nvspalygee iqveeaslsk erdqfelali keaikqkkpi favcrglqlv
      121 nvalggslyq dishlnqnai khmqapisre ipthlirtet gsilrkiyge etkvnsfhfq
      181 svkslakels vtalsedgvi egvesnnsgl vflgvqwhpd faydhleqem aifryvveel
//
LOCUS       WP_010770990             106 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Enterococcus caccae].
ACCESSION   WP_010770990
VERSION     WP_010770990.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..106
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11622
     Region          28..99
                     /region_name="Cupin_2"
                     /note="Cupin domain; pfam07883"
                     /db_xref="CDD:462300"
ORIGIN      
        1 mmikpslpqe mtiffdaenq pnenvqmgvv ilqpgekrpl egfarhgqde ysyvvsgeah
       61 tiledgqdlv gkpgdaqlie ageghinynd geqaavvvwm lverve
//
LOCUS       WP_010771013             216 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Enterococcus caccae].
ACCESSION   WP_010771013
VERSION     WP_010771013.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..216
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=24746
     Region          25..202
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(105,112,128..130,173,179,183)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mknklyyqfa gscflvvfmf lgyvvrfypd wlhgfdqait afvrtpypsa nqffiwytkf
       61 adpltvgilt laiafilfrg kyyaemlwll intgliagia npliklvfmr prptlnhlvt
      121 ehsysfpsgh stgsvllygt iilllpqfik qknlclllqv ilgfgillig isriyagvhf
      181 psdvlggfcf glawllmtyp iylekrfiwr frskqq
//
LOCUS       WP_010771049             324 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus caccae].
ACCESSION   WP_010771049
VERSION     WP_010771049.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..324
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36562
     Region          1..246
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkkiyygils taqivprfve gikksragqv aaiasrslak aeqmaselai pkaygsyeel
       61 ckdeeidiiy vatynkghye aakmalkhrk hvlvekpftl qaaqakelfe laeknncflm
      121 eaqksvflpi slqvkeaikk nkigqvywvq avttypsvdh iswfhsleag ggtlhgsgsy
      181 piqymqflld qpveessgcv trkagatddq vnlalkfqnq tlanvfisvk ldipskmtiy
      241 gekgrieipy fwktkeatiy yedgcceplt gefesefife vehvneclqk qlrespvmtk
      301 qltidtvslv erlygkwlek eeqa
//
LOCUS       WP_010771056             439 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010771056
VERSION     WP_010771056.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..439
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=48059
     Region          1..428
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mngfvqwmev klmpvankfg sqrhmtairk gliatmplti vgafftvfqn ipidaymkfi
       61 epyqavldip srytmgilal yatfgiassl atsykldslt cgilavmafl vtaapptrvf
      121 edvkdvigag ryinlanigs aslfgaivta lvsveiyrff iqkditikmp dgvppevsns
      181 fialipgavi lllfwvirhv igfdlngfls tllmplkdtl agnslfggll tvflicffwv
      241 lgihgpaimg pvirpfwdms iaentlafqe gasvhnlpni fteqflqwfi wiggagttla
      301 lvvlmmfsks tylkslgrls flpglfnine pvifgtpivm npilgipfiv aplitttfsy
      361 fltvtnvipm maarlpfaip apiaawmstn wsvpaallvc vnfaitlaiy ypffkvyekq
      421 qldkeaeela aeqkakaaa
//
LOCUS       WP_010771060             336 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Enterococcus caccae].
ACCESSION   WP_010771060
VERSION     WP_010771060.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..336
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37740
     Region          2..314
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(33..34,37,88,103,106,136,169,275,278,314)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(241,252,264,275..277,280,302,306)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mriaafgeim mrftppeylm leqtkdlrld ftgtgvnils nlahfgcqts lltnlpdnrl
       61 geaakatirq lgiqdrwigt lgdhigsyfa emgfgarptq vtyqnrrnss fgmsgtadyd
      121 fdtflaeidl vhicgislsl tketreaaft laekahtlgk kvcfdfnfrp slnevhgtsf
      181 mkeqyekmlp ycdlvfgsqr dltdllemtm deaiepskqf eelvhrfmti yqidcfagti
      241 rqgegdkryl tgyifdsehy vqaapreiih ldrigagdgy aagillgyse swsllesvef
      301 atangvlaht iqgdvplttr kqvrhimehp tvdlir
//
LOCUS       WP_010771077             387 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Enterococcus
            caccae].
ACCESSION   WP_010771077
VERSION     WP_010771077.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..387
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43510
     Region          24..303
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 minflighfe krqtknadtr tafgvfagvv gllsnlllfv gkfliglvsg svsimadamn
       61 nlsdtvssvl tlvgfyiagk padkehpygh erfeyisgml vsllitfvgf qffmtsiqri
      121 ktpqsihvtp vilvililsi likvwqsvfy krvaqkidsn tlvatakdsl ndvfttiavl
      181 vsatvegvtg lkidgivgli iacyiifsgl qlirefvnel mglrpdqaai dkmklylssv
      241 sdivgyhdll ihqygpnktf asvhieiddr wdltraheti deielvfkqk lgvdlvchid
      301 pvnlydqrqq fihqelkkii kgidnelkgh dirlvehgnk prilfdlvvp nhfkatdqel
      361 kiriqeqvyr nigdypvevt fdhnyll
//
LOCUS       WP_010771099             432 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Enterococcus caccae].
ACCESSION   WP_010771099
VERSION     WP_010771099.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..432
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48600
     Region          14..430
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mliinflill lmiaitaffv asefalvkir msrleqlknd gvknaelaih vthhldayls
       61 tsqlgitltg liigwvgegs vaallhpivg dlpisgalss tisivlgfvi vtyvvvvvge
      121 lfpksysiak pekvvlaivk plhyfykimy pfiwllnhsa aklgqlfgir lvsegeetlt
      181 qeellyvadd sykkgeltke eyhymenife fddtlakeiq vdrtsmevfe adetvaqaiq
      241 hslkrghtry pvieeskdnv lgyvtlpali kesfinnqrn vselveepii vlatipiksl
      301 ltmmrkegkh iailkdeygg ttgmvtiedi leelvgdird etdlenalia kesdnsyivs
      361 gkitlddfer yfkvkipife esemstlagf iveqqknqit vgdqikidkf ifevmdyeha
      421 hidyfkitln qv
//
LOCUS       WP_010771173             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus caccae].
ACCESSION   WP_010771173
VERSION     WP_010771173.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..397
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42792
     Region          11..393
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(23..24,27..28,31,63,114..115,117..119,122,142,
                     145..146,149,222,225..226,229..231,234,262,266,318..319,
                     323,327,343,346..347,350..351,354)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mennktrnvt wmlvaiflgy tciyvdktti gmslvtiand lgfdpqqkgl ilsafflgyt
       61 ifqipfgyls skigtrkmmi tsvflvgifl flfgfgfsll ylilirfmtg avahsgypss
      121 vstfisqelp iekrgpaqst miassgfaai vgplliapll lqigwhktyy flgaavllva
      181 vlmyfvipke fggvkeqlkn kkvisfrdvl kdrnvwilif aaffinaaiy glngwmatyl
      241 veahglvltq tayvaaiigf ftmiaamlgg vvvnkyfvgk eknvifiati gggifailvs
      301 vvgtfvmsmv altcavafas lafatlmsip lkifptdevs akyatinaig vsggfvapti
      361 igaliqlsng affssflfig isfivaggit llvkkse
//
LOCUS       WP_010771281             426 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus caccae].
ACCESSION   WP_010771281
VERSION     WP_010771281.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..426
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=45473
     Region          1..422
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdkfvqwmek yfmpkasvia aqrhlvaird afvvtmplmi lgalavlinn lpipgfpelm
       61 dklfpmiand apiwksfggn iwngtfaifs vliaflvayn lvksygkdgi aagtvsvasf
      121 favgglsgmd atglfialvi alisgelfqr lvgneklvik mpdgvppava ksfaallpam
      181 itislfslit sillglgidn ivvsfyeavq kpfmglansy psalllafit pflwffglhg
      241 anmvdplmqt invpaidani kaleagekip yivnkpffds fvnlggtgat lglliaiflv
      301 grknkpfkvi tnlslapgif ninepvmfgl pivlnpimfi pfiitpmvlv ttayiatstg
      361 lvpaatfmpp wvtppiiggf latksiaggv laavnlaisv liyipfvkva tdqflkqeaa
      421 aqenni
//
LOCUS       WP_010771183             369 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus caccae].
ACCESSION   WP_010771183
VERSION     WP_010771183.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41384
     Region          1..366
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mvemalkhiy kkydnaenys vtdfnleiad refivfvgps gcgksttlrm iaglediteg
       61 elsigdkvmn dvapkdrdia mvfqnyalyp hmtvfdnmaf glklrkydka eikkrvenag
      121 eilglteylh rkpaalsggq rqrvalgrai vrdakvflmd eplsnldakl rvamraeiak
      181 lhrrletttv yvthdqteam tmadrivimk dgfiqqigsp kevynmpnnv fvagfigspa
      241 mnffnvtlnn giirdghgle lkipegknkl lvekgyegks iifgirpedi hseqvaldtm
      301 ndavvrsevv vsellgaetm lytrlgdtef iskvdardfh epeemvdlaf niskahffdp
      361 kseqviklp
//
LOCUS       WP_010771292             190 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010771292
VERSION     WP_010771292.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21702
     Region          2..>120
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 markktitkd qilnaayevv ategfskfta rniatkmkcs tqpiylefkn mddlkeelfe
       61 kihqylakev fpithtgnti vdlalnyihf aknesklyra lyleeygggk rmqefsysyf
      121 snavkqdsdy eklsdteins lhmgtwivat giaalmtsgi ihpsdqqier lmieaidqil
      181 erdkpididn
//
LOCUS       WP_010771311             242 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus caccae].
ACCESSION   WP_010771311
VERSION     WP_010771311.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..242
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27020
     Region          8..193
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(11,13,95)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(44,94..95)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            93..95
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mktnkillii payneaagia dvirkveeyr qschydldyv vindgstdne eevlqennin
       61 hielvynlgi ggavqtgyky alnegydiav qfdgdgqhdi nslnklidpi ienqadftvg
      121 srfvsdsdst fkssgarqlg ikilsnliri ltgvnikdvt sgyragnrki iqqfvdryps
      181 qypepesymy lianksrike igvkmferet gkssislins isymvnvsls iliaslidke
      241 ef
//
LOCUS       WP_010771364              68 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010771364
VERSION     WP_010771364.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..68
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7909
     Region          1..58
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mnvhnkikei reskkitqiq matdlgvsrq tmnaiektky npslelslki akyfnmhvee
       61 ifqleeee
//
LOCUS       WP_010771381             249 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus caccae].
ACCESSION   WP_010771381
VERSION     WP_010771381.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..249
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27703
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mlqvenlskt ygteikyeal kelnltvndg efigimgpsg sgkstflnll atidqptsgh
       61 vllngkdpnq lnqeeiakfr rrelgfifqs fnlmptltve enivlpltld gekisimkeq
      121 lnrlaarlgi asllkkriae isggqaqrva varamihqpq llladeptgn ldtksskdvm
      181 qllqqlnqee katilmvthd plaasyckri vfikdgelid eihhngnqkn fydeimvkls
      241 eiegvdnef
//
LOCUS       WP_010771379             790 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK [Enterococcus caccae].
ACCESSION   WP_010771379
VERSION     WP_010771379.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..790
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=86949
     Region          <202..261
                     /region_name="CCDC47"
                     /note="PAT complex subunit CCDC47; cl46382"
                     /db_xref="CDD:480722"
     Region          287..782
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 maqkrksakk kktkkqqqqq ehlnfiflgi ffiffglfgl lklgflgtli anglrvvign
       61 tfpvaaillm lyglslvifg kdfpikksrp iiggvflylg vllllhafmf rnvgtqtpni
      121 igttweflrm dlkastvaqn vggglvgagl ynltfflvaq fgsyliagll iatgvflmsm
      181 ldfqqvmngl qiirerlssl tarsaerqae reakraekra akqeeikkea qkrlkndvre
      241 ltpgeklaqe aweqeekemq epeqltlvpi dsfqnqaevq piqqkvapes emdeggeldf
      301 eiseeaedrd yelppstlld sipsadqsge yqkieknigv leqtfksfgv dakvvkaslg
      361 pavtkfeiqp avgvkvskvv sltddialal aakdvrmeap ipgksligie vpnstvstvs
      421 frdiieaqps hpdkllevpl grdisgmvqs adlakmphll iagstgsgks vaingiissi
      481 lmrakphevk lmmidpkmve lnvyngiphl ltpvvtnprk aaqalqkvvq emefryekfa
      541 atgvrnisgy nelviqknle dgenrpilpf ivvivdelad lmmvasneve daiirlaqma
      601 raagihmila tqrpsvdvit giikanvpsr mafavssgtd srtiidsnga ekllgrgdml
      661 flpmgenkpi rvqgafisdh everivsfvt eqqeadyqes mmpteedtmg nsseasqdel
      721 yeeakalvve mqtasisllq rrfrigynra arlvdeleah gvigpsegsk prkvfleplp
      781 ddvtmdhgde
//
LOCUS       WP_010771385             255 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            caccae].
ACCESSION   WP_010771385
VERSION     WP_010771385.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..255
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27886
     Region          11..254
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mksshktika rrdkilellk tentlpvkev srelavseit vrrdlialek mglvqrahgk
       61 aqivqeigte dyneeievlk ntiakkaaef vkdgntlfin tgstalsslk nledkrvtiv
      121 tnnvkvanld hnpnstvils ggeirfpkea lvgdiaidsf skmssdisii gcsglsieng
      181 ittpvlheak insliiertn glvivvadyr kigfssnfts gtikdinyli tdtfaspevi
      241 reiekqgvqv iqvev
//
LOCUS       WP_010771428             447 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus caccae].
ACCESSION   WP_010771428
VERSION     WP_010771428.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..447
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=49118
     Region          1..442
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mealekflnk figpvaqkmn nskffsalae afmrttpitl gvallmivgn fpipqwiefl
       61 aktgmtahfn aalgatinll svyvtfnfay iyskkeghdp lpagllaigs ffilmpqmiq
      121 tytleksvte fpaqtvvtas nnveafasqy tggtglfvai ivgyftavly gflirknlti
      181 kmpdtvpsnv seslspails gvilavffiv riifsftpfd nifafittli qaplqsltgs
      241 piaiiliftl anmlwffgih pnmvygvvmp vmtanmlanm tayqqhqelp ylamavvsyv
      301 cgnafggqgs tyglvismft akserykslf klagppvlfn vneplifgmp lmlnpfffvp
      361 mvaspllmgg iawgmlsvld fskynplial pwttpapiam alkggfnyll ifivllivnv
      421 lvwypffkma dkkeylleqe naktaev
//
LOCUS       WP_010771430             291 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Enterococcus caccae].
ACCESSION   WP_010771430
VERSION     WP_010771430.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..291
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=31977
     Region          1..290
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mkkffeslpv hdyttklsva ivyailasva mnffyqpgni yssgitglaq ilttlstkiv
       61 gvkipvsitl yvlniplffv awlkigkkft vftfltvtlt sifmqivpqt tlsndpiica
      121 ifggavmgsg igfalkngls sggldifsit irkktgrsvg sismyfngli ifvagylfgw
      181 qymfysalsi fvsgkvtdav ytkqkkmqvm iitknpdavi dgiqqkmrrg itiiheaega
      241 yrhdkqtlll tvvtrfelpa leaamkesdp safvsisdnv kilgrfyeed l
//
LOCUS       WP_010771502             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010771502
VERSION     WP_010771502.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..247
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27614
     Region          5..246
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mekalsesek ylwdfidkhl vdipnysivk lsekanvsta tivramkkkg yegftsfkhy
       61 lkdqsnttin fsgvekidae ikrailkneq evirtinrld sgsiedaiqk ikaaqkivif
      121 argfseliaq emtvkfqllg kycelhadpn iitsmskkit kndivllisl ngetaelvta
      181 vknclknevs titltansss slaqlseivf tgfksegsyf peyevrsrlp lsvmarilld
      241 syairtn
//
LOCUS       WP_010771521             358 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus caccae].
ACCESSION   WP_010771521
VERSION     WP_010771521.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..358
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39375
     Region          1..357
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtlkvgiigc ggiangkhlp alaqvkevel vafcdliser aeeakmhygt ltaktftnyq
       61 emleemeldv vhvctpnsth aelsiaamea dchvmcekpm aktaaearsm ieaanktgkk
      121 ltigyqnrfr kdstylheic degelgeiyf akahairrra vptwgvflde eaqgggplid
      181 igthaldltl wmmnnykpky vvgkayhkla etenaanawg swdpkkftve dsafgfimme
      241 ngatifless walnsldvke akttlhgtkg gadmnnglti ngedhstlfe kkielepggv
      301 dfydgtgdkp evleaqswid ailndtepiv kpeqalvvte ileaiykase tnqpvyfn
//
LOCUS       WP_010771577             292 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Enterococcus
            caccae].
ACCESSION   WP_010771577
VERSION     WP_010771577.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..292
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31138
     Region          1..292
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mevviqqlvn glflgsiyal lalgytmvyg iiklinfahg eiymlggfmg yffinklslg
       61 ffpalilsma gaavigvvie flayrplrks triaalitai gvsfllqngm iywlgpekks
      121 fpqaiefkny qlgfiqisni qvlilvislv lmialqmivk ktkmgkamra vsvdadaaql
      181 mginvnrtis ftfalgsala aaagmligly ynsidpmmgv vpglksfvaa vlggigiipg
      241 aalggfvigl letvtialgf sdykdavvya lliiillirp agilgknike kv
//
LOCUS       WP_010771587             202 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010771587
VERSION     WP_010771587.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23436
     Region          8..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mskktdlrvm rthkmiieaf fhlvdekgyd citiqdiade aminratfya hfkdkqdlye
       61 qifdfaidaf tsvidteqii vsnrikvkqi eflltniyin iqknksfflt imdgssnell
      121 rkkladiiye kyadifsklk itendievpi dfiieymtsi figtlhwwit sdtdmspnhl
      181 arlviklvgn ghltvlglei dk
//
LOCUS       WP_010771694              84 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010771694
VERSION     WP_010771694.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..84
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9595
     Region          12..78
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mteqitettk ekskfestih vframkrmtq qeladkvgas rqtiiqlern rynpslllah
       61 kiaavfevpi eqifafkegd denv
//
LOCUS       WP_010771649             347 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Enterococcus caccae].
ACCESSION   WP_010771649
VERSION     WP_010771649.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..347
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39816
     Region          12..346
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 msmyekfiqn erlrrffvla vvifilflar smitmilltf iftflalhfv kfvqqylkip
       61 siilvfatys livflvylai tkyvpilihq svqmynsvih fyqtptddhn qllviidnyl
      121 eksnlmsqiq ngasillryv qdigsiglsf vlsfilsfff miekkqmaef sklflksdfd
      181 wffqdiyffa dkfvntfgvv meaqffiaiv ntgitticla ligfhqlpsl aimifilsli
      241 pvagviisci plsfiayseg gindviyila viiivhlfes yvlnpkfmss ktdlpifytf
      301 villiserlf gvwglivgip iftffldilk vkpihsvtek iadpptk
//
LOCUS       WP_010771772             279 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Enterococcus caccae].
ACCESSION   WP_010771772
VERSION     WP_010771772.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..279
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30620
     Region          42..268
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mklkkmvvga vlllmvlagc sngttkeeek kadtkensev viylarhgkt mlntvdrsqg
       61 widapltpag vevaeqlgkg lsdvkfdkvv tsdsgraiet aelvlknngq ekltkemtkd
      121 krlreynfgt yeglmneeml tavakeqgkt yeqynewmke vgfykgiief advlseldkk
      181 nveegvnwpa edsktivarl tdglddlvkd aekegahnvl vvshgmsiit llgeldadad
      241 lpdgglknas vskvtykdgk ytidsvndls yvekgkesk
//
LOCUS       WP_010771769             478 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus caccae].
ACCESSION   WP_010771769
VERSION     WP_010771769.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..478
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52491
     Region          24..471
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,280,283..284,287..289,292,320,324,376..377,
                     381,385,401,404..405,408..409,412)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mesvtsfqen pivqknrwwi lvsvamftfm stldasivni alptiskdmn vpmnqsewiv
       61 siylmivcac lllfgkigds fgkikvyrig tiiftvgsll cgfnqslgfl lfariiqgig
      121 ssmtmatnsg iitevfpfke rgralgsiga fvslgsiagp gigglilsqf swpyifwinv
      181 pvgiitilig ekflpkdrik sdkkvdmvgf slfavfimsf fgaifigqei gfnaflpfll
      241 filafasflt fikvekhvsq plitfsifkn nmftmslita vlifssnffv nvvipfylqn
      301 arglpaskag llmmvfpllm vigspisgfl tdkigtkllt fsglfllsvt almyiflnqg
      361 tplwyyilat gimglgnalf qspnnttvms svakedlgva gsmnsfarnl gmvlgislat
      421 tilynamsvl ygqrvttfis erpdififgm ritflgsfil citalsltlf rslktrrk
//
LOCUS       WP_010771778             146 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus caccae].
ACCESSION   WP_010771778
VERSION     WP_010771778.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..146
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16707
     Region          13..142
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mhthfgcepw hqaaafslry dvfvleqgis lqdefdfldt kdrkyfvvye qslaiatiry
       61 qkknehtiqp drfcvrkeyr nqgigkqlll lleqtavkdg ctlsilsaek talsfyealn
      121 yavnskeyve dgilcvemik kivagt
//
LOCUS       WP_010771836             562 aa            linear   BCT 01-JAN-2025
DEFINITION  ribonuclease J [Enterococcus caccae].
ACCESSION   WP_010771836
VERSION     WP_010771836.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..562
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=62609
     Region          1..552
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mstikivplg gvrengknmy iaevedeifv ldcglkypen ellgidvvip dftylvenid
       61 rvagiflthg hadaigalpy llskvhvpvf gtaltielak lnvgdhadsk dfndfhvvda
      121 hteidfehat isffrtthti pdsigvnlkt kegnivytgd fkfdqsaipm yetdfgrlae
      181 igkegvlall sdssnaenpa qvvselqiad evfdtirywe griivacvas nlqrvqqvld
      241 aahrsnrkiv ltgqdfqrii ntaikldklk lpseeliisv kdmkkyqadq lviletgtmg
      301 epikslqkma ngthrvvkik egdlvyittt pttametava ktedivyrag gvvkqisdnm
      361 rvsghanpnd lqlmlnlmkp kyfvpiqgey rqlaahadla helgipykni fitgrgdile
      421 yskqkmnvag sttaenimid gigvgdigni vlrdrrilse dgifvavvti nrrekrivsp
      481 akitsrgfvy vktskdlmke asvivteive khlesndfew sklkqdireq lsrylfeqtk
      541 rrpvilpvim eatqrkgrka an
//
LOCUS       WP_010771837             393 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Enterococcus caccae].
ACCESSION   WP_010771837
VERSION     WP_010771837.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..393
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43673
     Region          45..367
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mekkqetrwi kflggknllf tlvallllga vififhqvgf ifgpigvvfk tiigptilal
       61 ilyylfnpvv hwlekhkvkr vygvsaifvv litlivvgii lvvpilqkqv dglvrsfpqy
      121 mndlnkmvtd ffhnsalekp lanalagiqk wfdnvsdgig syfskavega stvfstltgf
      181 alvmvtapii tffllkddqk ffafvlkiip prfrsdakei gatmssqvga ylkgqilvsi
      241 sigiltfigf wlvkvpysgt lsiivgvtav ipyigpviaf ipaaivalmv sfgmfikmsi
      301 vwmivqmlng hlispqvmgk klvvhpltiv ivllvmgdll gmfglifgip iyaivkvlvt
      361 yifrkfkqry nqfygdsgey edtefskeey lde
//
LOCUS       WP_010771857             301 aa            linear   BCT 01-JAN-2025
DEFINITION  permease [Enterococcus caccae].
ACCESSION   WP_010771857
VERSION     WP_010771857.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..301
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=33042
     Region          5..301
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mfqflphsvl qmgtiflsiv iealpfvmlg cvisgalhvf ltpervkkll pknkflsivv
       61 gsllgfffps cecgivpivh qfvkkdvpty tafafmitap iinpivlfst yiafgnamkf
      121 viwrvvgsml valvvgiwla yinnepilkq agldtactit eeehhhekeg fwhkcwsvlt
      181 hgideffdtg ryliigslla aamqtylptg ailqlghtkl lailvmlvla atlslcsead
      241 afigssllsl fgngpvvgfl vfgpmvdikn llmmkryfkt sfmlkfvgiv tvvvslyala
      301 i
//
LOCUS       WP_010771873             393 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Enterococcus caccae].
ACCESSION   WP_010771873
VERSION     WP_010771873.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..393
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=43479
     Region          1..386
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mswpkrlskl hyidfyilip ylilciigil mvyssssyql ldsdlgtask aikqtmyflf
       61 slvcmsvayr inlsvlrnsk mmyclltftf lsivalpfig tsvggakrwi nlgvllfqps
      121 elvplvlvly lalnlakndt lvpftlknhk rsllvsmffm ffvalqpnia gasmifilvs
      181 vmflfsglsp lftsialvgf vvlkrlgtvl llsiptdwmp qkfgylvtrf evmqnpfidp
      241 tgkgfqtsna yyamhnggff glglgnsiqk kgflpaadtd fifaicieel glivalgilf
      301 avffivarlf llaikskhly ysylyigcgm llflqvavnv gsllgyipmt gltfpfisyg
      361 gssllilsit lgialnargt eqretfkkqg glv
//
LOCUS       WP_010771902             139 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Enterococcus
            caccae].
ACCESSION   WP_010771902
VERSION     WP_010771902.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..139
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15968
     Region          5..79
                     /region_name="Putative_PNPOx"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam01243"
                     /db_xref="CDD:426149"
ORIGIN      
        1 mktieafkki mneqteiala tsveeipnvr ivnffydetk kclffstfke nkkitefqkn
       61 pnvafttipn eqvnhvrvhd aqvkkselsv ydvaeqwiqk ipsyeenikl agamldlyei
      121 hfgeaivilg idsretiil
//
LOCUS       WP_010771924             319 aa            linear   BCT 01-JAN-2025
DEFINITION  aromatic acid exporter family protein [Enterococcus caccae].
ACCESSION   WP_010771924
VERSION     WP_010771924.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10532842
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..319
                     /product="aromatic acid exporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36449
     Region          1..141
                     /region_name="ArAE_1"
                     /note="Aromatic acid exporter family member 1; pfam06081"
                     /db_xref="CDD:428756"
     Region          148..293
                     /region_name="ArAE_1_C"
                     /note="Putative aromatic acid exporter C-terminal domain;
                     pfam11728"
                     /db_xref="CDD:432028"
ORIGIN      
        1 mkiglrtvkt avsatlsmiv agslgllypa sagiiavlsv tntkktsllt gfyrllslal
       61 ataiaylcfs ilgfnafafg vflllfipga vhfnlsdgiv vssvlvtqyl ieqdlswtii
      121 gnefllmtig vgfallmnly mpdteqhlke dqevietmfr kilnnmaayl nqpnkeknlf
      181 ekcnelkefi rtgenwaknh aenqlifsnh yyieyftmrr lqsnrlkdml rilenitvep
      241 eqveniqgll qytaetfaen nngqdildri dqvydvyrkk elpktreefe nraqlfqflq
      301 lfqsfieika efaknqnek
//
LOCUS       WP_010771938             306 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidase U32 family protein [Enterococcus caccae].
ACCESSION   WP_010771938
VERSION     WP_010771938.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..306
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=34624
     Region          1..298
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
ORIGIN      
        1 mieliataes ieqaeallav gvdtlyigee mfglrlptsf sreeqkfite kahgagkkvt
       61 valngimhpe kmkkipeyla flqeikvdqv tigdpgvvfv lqrdkieipy iydgetlvts
      121 srqinfwakr gaigavlare vpfeemiamk dnlmvpaeil vygatcihqs krpllqnyyn
      181 ftkndesask erglfisepk keethysiye dshgthifad ndvnliseld klhehnytkw
      241 kldgiyapge nfvkvaklfv eskeklesgv wssdqaqkvm eevetlhpeh rgldigffdl
      301 dpdeik
//
LOCUS       WP_010771944             635 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Enterococcus caccae].
ACCESSION   WP_010771944
VERSION     WP_010771944.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..635
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=71213
     Region          3..393
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
     Region          <519..612
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtkqkivvvg agyagvsatk flakklkkds dveitlidrh syhtmmtelh evaggrveps
       61 aiqydlqrlf srkknvtlvt dtvtgidkdk kvvqtklgsy efdqliigmg gepndfgtpg
      121 vkehgftlws fenslkireh iletvekaai epdpevrkam ltfvvcgsgf tgiemvgeli
      181 dwkdrlakef kldpneftlm vveamptiln mlsrndaaka erylekknvk lllnapivev
      241 aadhiklkdg stvpthtliw tagvkatsda adfglesarg nrlianefmq akgyedkniy
      301 ivgdlvyyee fpetptpqiv qaaeqtghta aanivadikg gekhkfkgny qgfmvsvgsk
      361 wgvanlfdki hlsgflaiim khivnlkyff dirsgyymfq yimheffhik ddrnvtrghs
      421 srygnvlwsv plrvfygmvw lvesmkkivg tgdylkpstw fgdgswftdk vafpfpwlqe
      481 qvttgasaag ggaeatetta kaaqfglsya ygeepmqvfd hmpkwfesvm kfmmpnqeva
      541 lfmqkfmtiv evlialalia glftwlssaa tigltiafcl sgmfywvniw fifvafalmn
      601 gsgralgldr wvipwlqrtl gkwwygtpks ryssk
//
LOCUS       WP_010772066             191 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010772066
VERSION     WP_010772066.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22328
     Region          1..>87
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          74..175
                     /region_name="TetR_C_8"
                     /note="Transcriptional regulator C-terminal region;
                     pfam14278"
                     /db_xref="CDD:464123"
ORIGIN      
        1 msesqitkka isaalielcd hklfskisvq ditkevglnr qtfyyhftdk qdllrwiyth
       61 daliyldspe vsidnweeqa lkmlkaiqsk sdfyyntvss dsdilrtcfs titnklfinl
      121 fdqvdkenql lpedkifyar ffsygcsgvl idwilnsyke spleiatqlf rlakdteffs
      181 yrlyaqenel l
//
LOCUS       WP_010772133             505 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease/substrate-binding protein [Enterococcus
            caccae].
ACCESSION   WP_010772133
VERSION     WP_010772133.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..505
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56325
     Region          <45..208
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          235..498
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(241,243,291..292,295,338,340,418,442)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mgklietfva rkedfiqavv ehiqlsllsl liaillaipl ailltnykka aefvlqitgi
       61 fqtipslall gllipiigig sppaivalvi yalfpilqnt ytglteidps leeaaeafgm
      121 tkreklvkfe lqlalpyiis girtatvmii gtatlaalig agglgtfill gidrnnvyli
      181 ligaissavl avlfnfgihl lekatvkriv aafmvllall vgsfvythqe aeqkeitvag
      241 klgaepdili nmykeliean sdihvnlksn fgktsflfna lksgeidvyp eftgtvletf
      301 lkdnkntsnd prevyeyare qikkqenmdy lepmryenty avavkrsfae englktiedl
      361 kkvesqlkag ftlefidred gykglqklyn lnfdvksmep slryqainnr dvnvvdayst
      421 dselkqydlv ilkdnkrlfp pyqgapllka etlekypelk ellqplvgki teeemsemny
      481 lvnveqkdpa tvahdylveh kmlek
//
LOCUS       WP_010772157             142 aa            linear   BCT 01-JAN-2025
DEFINITION  HIT family protein [Enterococcus caccae].
ACCESSION   WP_010772157
VERSION     WP_010772157.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..142
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16310
     Region          3..138
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mtdcifckiv dqeipsykvy eddkvyafld itqvtkghtl lvpkehvtdi feyeptlage
       61 vfarvpkvar aiekafpemq glniinnnke layqsvfhsh ihliprygks ddfsihfgnn
      121 qamysseemq eiakkikrqv ek
//
LOCUS       WP_010772171             431 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus caccae].
ACCESSION   WP_010772171
VERSION     WP_010772171.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 431)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..431
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49624
     Region          32..405
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 maeitalviq aliiyvsikl fikdksfflk eifvlllflv nnsivhinlg iytlifqlil
       61 lfiiirmheq dwkldliils tvliinilgd hiasllisff lklhlfdsls enivpflisy
      121 avitfgiili trnfsshfsd aiksnstknl fafgttstll lfylnvlfel isgnnrtiie
      181 lnllffiili lvssvsvhsy idslkrtyei ekketevram rkytsdleyq ylemrkfrhd
      241 yqniltsleg yfvnkdydal etyffnnikp tgrqieqynf eledisrlhl ddiksiltak
      301 iilaqekkmn vsveiqetid finiphvslv rilgilldna iealeelhdg llqvafikqk
      361 nsiliviqnt cktsipkiyq lkkqgfstkg ynrglgltnl qelieacpqc tsetlivdst
      421 fiqkiiihnk t
//
LOCUS       WP_010772199             290 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus caccae].
ACCESSION   WP_010772199
VERSION     WP_010772199.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..290
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32851
     Region          48..290
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mlnsdiptmr ihmqendqkr dagltepdtl emfknlsygp ygientfdiy ypkgtdkclp
       61 tiinihgggf fygdkelyrf ytmylatqgf avvnfnyrla pdhhypaple dtnalinwli
      121 ehgrsyyidl drlflvgdsa ggqlveqyat ltsnsayaqk fsfeiaavqf kaialncgay
      181 figknsainq dfpfyfgeti tsalksqfpv esyitanfpp afiatsthdf lkeiaspfad
      241 llqskgvetv frlyanpdyt elghvfhlnq kselakqcnn demaffnrfi
//
LOCUS       WP_010772225             475 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus caccae].
ACCESSION   WP_010772225
VERSION     WP_010772225.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..475
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56967
     Region          84..164
                     /region_name="Mga"
                     /note="Mga helix-turn-helix domain; pfam05043"
                     /db_xref="CDD:428276"
ORIGIN      
        1 mdflllddrt tlklaiirkl eqrysfserk dilcaelnis qyllersvle inedlkrfkl
       61 ieemelieqs neiilfqgaq iassiveeny lkfslefrll qtiffnqfts ikkygekhgm
      121 srtvvykivd rirkelaqyd iklsktfqlv gnemkirqyf nmlyyriykd sdelynqsdv
      181 lsvnellsaf rpyceevntf ylfkhylfim lqrvqrkskf flpsnitsvn fnkenqfyqi
      241 ldqwsartln gtkreieaev kgilsqlsvy rsefcdlkne evekyrlqlk qqflrypqle
      301 lmeselsnsv dmtiyqhqfs tpliditlrm mnleffhery pilfeichtf iyqlkedefr
      361 yskkslflnl llilsqqydq kneantinih vnftngekyn qfiknqiqif dsfsinfqpv
      421 vrpdtdlivs dylpqttfsa rsliwlappr asdwrnfgne ivqinralql nkkrm
//
LOCUS       WP_010772239             558 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010772239
VERSION     WP_010772239.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..558
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=63920
     Region          8..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          264..556
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mltvknflql apfksfrlva gskglenkit gvnildnpda sdwlsagell itsgyffsen
       61 atiqkrfiqr fkeincsaic ikphiylkgi pesmrnlade lalpiieipy giafskimni
      121 vmaeisgrmn elnqasldih sqffeislhg gglkkialgl aemvnnpvil vdtdwsvlav
      181 sdheqpliqe slkktgdtlt fpvqiftdlp kdferiqkpi trgilfdeqe ypcvimpvyf
      241 dtihygfilv yqierpltdl dyvalengsm aialeqmrll eiertenrir rdffdqllsg
      301 qikdldalaa ydttidpsln ytvlilsiqt lshksdslmk rkqsedrlmk nllsslttyt
      361 atrfpqlhlf srknqlvmll gtepklstlk thnevsdtae rirmyleqhg hsereifcti
      421 gstlpilels qsfeeakkvi qlleddskee kiyffndfyf dsflvdsisn eqgkkfythy
      481 lntllaydqk nntsftptlk aylahhlnia mtsralfihr ntllyrieki kgllpvdleq
      541 ekntfalqma lklyelhh
//
LOCUS       WP_010772249             489 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Enterococcus caccae].
ACCESSION   WP_010772249
VERSION     WP_010772249.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..489
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53476
     Region          7..489
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mddqqldksf lgqpkglstl fftemwerfs yygmrailly yiydtvangg lglpketala
       61 imsiygslvf mssivggwis drvlgarktv ffggvfimvg hivlatpfgi aalflsilli
      121 vigtgmlkpn vsgmvghlys ktdtrrdagf sifymginig allapfvvgt lgqtynyhvg
      181 fsvaafgmff gllqyylqgk ksldgiglkp tnpigteerk kfirslllal vfvivlfgga
      241 fileqltigf finsvsvlgi llpvyyfikm ltsknvtaee kpkvlgyipl flagiifwsl
      301 eeqgssilal fanertndtl fgfsiapswf qslnpifvvv ltpvfvtlwt rlgkkqpstv
      361 vkfslglvfa glsfvllmls gllygtdtrv splwlffsff imivgemcis pvglsittkl
      421 apkafesqtv aiwlladaas qainaqiarf ytpqtesayf givgfvavia giililsknp
      481 ikklmgsih
//
LOCUS       WP_010772252             259 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus caccae].
ACCESSION   WP_010772252
VERSION     WP_010772252.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..259
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28252
     Region          25..236
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrkqkgmtli ailvflflfl plclivvtsf gtaaaiqfpi kgftldwytk alqsdtfmss
       61 fklsliigvl atvlalvvgi pasyalarys vkgrnfiksf flsptvipgi vvgytlfqyi
      121 viklglpifq gllighflis lpyiirvvgs smeqldysme evawtlgctk trafiqivlp
      181 nvssgifaaf mlafvnsfnn vpvsiflsgp gvtmlptsll symeynydpt vsaisvmlml
      241 ltmglmflie ktlglasia
//
LOCUS       WP_010772283             175 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010772283
VERSION     WP_010772283.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..175
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20874
     Region          1..80
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          88..172
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mntlsyillc mlvrkpctgy elkqylalfw eahhsqiyts lakllkenyv siendekhlq
       61 kkiyhltekg ekvvnnwiqe etnepsqkde flakiyvasi lekdtvkgll ferkqhqlki
      121 lkqnqakqeq ieqlsdpieq krnfgrslvi qrririceee lrwcqwaeeq veqlk
//
LOCUS       WP_010772309             593 aa            linear   BCT 01-JAN-2025
DEFINITION  V-type ATP synthase subunit A [Enterococcus caccae].
ACCESSION   WP_010772309
VERSION     WP_010772309.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF003220.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK04192
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..593
                     /product="V-type ATP synthase subunit A"
                     /EC_number="7.1.2.2"
                     /calculated_mol_wt=65456
     Region          1..584
                     /region_name="NtpA"
                     /note="Archaeal/vacuolar-type H+-ATPase catalytic subunit
                     A/Vma1 [Energy production and conversion]; COG1155"
                     /db_xref="CDD:440769"
ORIGIN      
        1 mqtgriikvs gplvmaenms dasiqdicqv gelgvigeii emrgdvasiq vyeettgigp
       61 gepvvttgea lsvelapgli semfdgiqrp ldtfaevtds nflsrgvqip aldrtkkwlf
      121 epvvsvgdev lagdivglvq etkviphkim vpfgvrgtvk eikqgeftie eivyiietet
      181 gekeftmmqk wpvrrsrpil eklnpdvpll tgqrvidtff pvtkggaaav pgpfgagktv
      241 vqhqiakwad vdlvvyvgcg ergnemtdvl nefpelidps tgesvmertv liantsnmpv
      301 aareasiytg itiaeyfrdm gysvaimads tsrwaealre msgrleempg degypaylgs
      361 rlaeyyerag qvvalgkdhr kgsitaisav spsggdisep vtqntlrvvk vfwgldatla
      421 qkrhfpsinw lqsyslydse vgkyldqelq vdwsemvmeg mrilqeesql eeivrlvgid
      481 slsdkdrltl evaksiredy lqqnafddvd tftsrekqyk mlrliltffk egqtaltlga
      541 ylteimtgtv glrdqiarsk yipeeqidrl dglvddiklt lkqivadggi thd
//
LOCUS       WP_010772313             504 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus caccae].
ACCESSION   WP_010772313
VERSION     WP_010772313.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 504)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..504
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53815
     Region          198..502
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnfikrsrls mkakkgrtll lcavfsaili filagltiqs aalsaienak ksvgatvtls
       61 anratametd rgdrnegkpd pdsfsltpvs ladaqkiagl dnvkayslfs ssaagasdgi
      121 tpisnttese ttnndtnteq gtsgrsaqeg esmggapmqs mkqsdfqvsg vmnlsmlsdf
      181 sdgvaevveg eaiseadeet nhvvieqsla danelkigst fkltspeddt ktyelkvkgi
      241 yntsengdsm gmmfnllnpa ntlytsytfa ntlkggdtkg tidsafytle dpkqmnsfve
      301 aaeklinten lslqtndkay qqmlqpltnv ssfarnivil vaiagiiilt livmmtirer
      361 ryeigvllsl gesrfkvilq ffseimlcmf valmiatfsg niignivgeq ligqqtevaq
      421 qaennqdkig argnqgqegp srggingmgt sskeaaetik elniavqpke vatlgglgll
      481 isfcsivlss igilrlqpkk iltt
//
LOCUS       WP_010772388              66 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Enterococcus caccae].
ACCESSION   WP_010772388
VERSION     WP_010772388.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7545
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mekgfvkwfd nrkgygfigy nedeeifvhf taieedgfks ldenqavefe vmegtrglqa
       61 ahvkki
//
LOCUS       WP_010772420             183 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Enterococcus caccae].
ACCESSION   WP_010772420
VERSION     WP_010772420.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..183
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20394
     Region          3..161
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mkkkigffvg slrkdsyskk vavalsslfp eeyepifidl qdlpmynqdl ddegvppvaw
       61 tkfrdevkql sglvfvtpey nrsvpavlkn aldvgsrpyg qnvwdgkpgl vvsvspgals
      121 afganhhlrq slvflnvptl qqpeayigni anlinedeti aentmnffki iidsylvfle
      181 knr
//
LOCUS       WP_010772432             310 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus caccae].
ACCESSION   WP_010772432
VERSION     WP_010772432.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..310
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34322
     Region          60..308
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mnrimkvlia vvvfvviilt gaglyfynya vvpsqkdfla agtpgtdvev ktpqekwfkd
       61 knnrsyweit skdgltlkai ylpaeentnk nvimahgymg saetmasfak myhdwgynvl
      121 vpdarghges egdyigfgwp erkdylqwvd kviaqngknt qitlygismg gatvmmtsge
      181 klpenvkaiv edcgystvne elayqlkdmf nlpafplvpv tslitkirag yyfgeassva
      241 qlkknkvpml fihgdadkfv pfgmldevyd atdapkekfv vkgaahakay tvdpdgykak
      301 vasfltkyvd
//
LOCUS       WP_010772547             234 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Enterococcus caccae].
ACCESSION   WP_010772547
VERSION     WP_010772547.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 234)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..234
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25185
     Region          9..230
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mekkeyltfr egvnacipti lgylgigiaa gvvgknvgls iieialmsil vyaggaqfii
       61 cgmlaihspi saiifttflv nlrhflmsms vasyfknepl itsigigtll tdesygvlms
      121 slandhriss awthglnita yvawifstil ggllgtwipd pyllgldfal vamfaglfil
      181 qvdvpikkht ketlivlgtv clslyffmgf fspelsvlfa tllgctvgvv nhhe
//
LOCUS       WP_010772569             456 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Enterococcus caccae].
ACCESSION   WP_010772569
VERSION     WP_010772569.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..456
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53074
     Region          13..425
                     /region_name="YdhJ"
                     /note="HD superfamily phosphohydrolase [General function
                     prediction only]; COG1078"
                     /db_xref="CDD:440696"
ORIGIN      
        1 mptpykhqil piekvfrdpv hnyihvqhqv ildlinssev qrlrrikqlg tssftfhgae
       61 hsrfahslgv yeitrricdi fqrnysserl gedgwndser lvtlcaallh dvghgpysht
      121 fehifntdhe aitveiitsp etevfqilnr vsadfpdkva svitktypnp qvvqmissqi
      181 dadrmdyllr dayftgteyg tfdltrilrv irpykdglaf amngmhaved yivsryqmyv
      241 qvyfhpvsrg mevildhllh rakelyeqqs edyqlhsqll vpffkghfsl qeylklddgv
      301 lntyftqwts lpdpilndla nrflnrkplk satfsgdrds vtirhlkali ekigynpkyy
      361 tainssydlp ydfyrpekns hrtqieimqk dgtlielski shlvaalagq tqiderfyfp
      421 kemvdpkrqq hydlfddtyr efatyihnga lvegkn
//
LOCUS       WP_010772571             692 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus caccae].
ACCESSION   WP_010772571
VERSION     WP_010772571.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..692
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=80597
     Region          21..662
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mmdersrklm krliersvhe vdelavqnsl tkrqleysle kingysvfds naklviennr
       61 iiltnqlreq fmtilsdkty rkgysmnafe rskylyllmf yfsdeylsin yfidelgvgk
      121 ttvmndlknl tieleieniq lvytrkdgyq lsgneeqiry hlmkmiiwds tenntafiyd
      181 qfiekhqvet idsmkdlvek ytvkygisfv enrlsefiyt fiflkkrlfn qsvsfcdkyq
      241 lsaliamkey qfsksllahf ciedqsacmy lcawilglsi grpddstkdy etiielvkri
      301 iqrfeaisgi rfnnqelvvr qlythfrpay yrlyfklpiv nplhnkikde yselfnivee
      361 tlkpiaslfe hpipedeiaf ltmhfaslcs nfdeytttqk valivcpngi gsssivytel
      421 ktlfpelsfl gpvetkeier lsdsydlifs tvpnirlfyt kkpvyivspi mntrekyrli
      481 sdvyaqignf nfklpsvdki meiiqkhaav nggsalekel yeylinqeep vekngegpgl
      541 qeitapeliq lnieaknwee airlsaapll kygritrnyi dtivdtakke gpymvisknv
      601 alpharpidg vkrlgisisv lkeplvfgsk endpvkyifc laatennrhl namvelvkll
      661 ddpqfyylmd nandshelyr ylfqqdilia rn
//
LOCUS       WP_010772593             242 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Enterococcus
            caccae].
ACCESSION   WP_010772593
VERSION     WP_010772593.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..242
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26856
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mislehvnky fgdhhvlkdv sldvnegeki viigpsgsgk stlircinrl ekvtdghilv
       61 dgiditepka pvqkvrqkva mvfqsfnlya hktiiqnltl apikvkgvsk eeatktgmey
      121 lervgladka haypaqlsgg qqqrvaiara lnmhpeiilf deptsaldpe miqevldvmv
      181 dlskqnitmi cvthemgfar qvadkvifmd dgqiietgtp ehfftstqne rakeflskii
      241 hn
//
LOCUS       WP_010772601            1192 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Enterococcus caccae].
ACCESSION   WP_010772601
VERSION     WP_010772601.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1192)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1192)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1192)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1192
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..1192
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=139130
     Region          4..1176
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mslqfirgta emdleeallq asvkwldedd ahevfylvpn hmkfeqeina lkriktiqgn
       61 qsesiatmrf qvfsfyrlaw yflqhtqfys seilseagaa mvfrkilsen eeelkvfrge
      121 vnkagfiqql fdlyqevkeg nvdlddlfgh lsgansdske qdlqlkiqdi klvfskfedt
      181 msqygiksae iihyltdyle tkdlshvlfv vngyhnfsar elklmetlmr rsgevkislv
      241 ldkkypnelp slmnlfyetg ttyhklyqla rnsnvailpd yiekkkmlie nsslhtledy
      301 widaqeshpk kekqiltddh lqfwcaenpk eeinhiakei rrliveenyr ykdiqlltre
      361 ldsyetmiep lfsmldipvy ldrdmameqh plvefiqslf aihsyhyryr dvlrflrtel
      421 ffpindqitt eewqtqrnew rrkidvtenv vlaygyegyh weknkdwhfi rydfeteqqd
      481 dtewiekesn vvrsmvqqti ptfykqlqka htgieaadsf yrfmvnngve kqlmmwrnqa
      541 iergeleear nheqtwaalm tlldeyvtiy gnesfdltvf eeifssgleg lrynkvptai
      601 dqvqvrsidl arpgqakivf aigltdqvlp qkfdnktlls deerqfvngy leegqfllnd
      661 trksiakepf nayimfsaat erlyfsypsv kdttkdvkvs tylaniqkdl glqlqqrnal
      721 tiidreqvsl ehvgtyrtli sdltnlkrqk ketqegilaf wltleealmk qsqgklashv
      781 feslrhqnlp enleehlane lytkhiytsv srmesfyrcq yqyftrfglg lkerdvfalt
      841 paatgeffhe aldqffklli iqnkqlselt drevgefteq ilnavfgeik fsildsssrm
      901 nyiryqlgqt ikkvswalkr qsersgmttv qtevlfgqia sqkgikgldl plknggnisv
      961 rgkidrldql vtpesiylgv vdyksshkkf niteayygla mqmltyldva lmdavnlvgr
     1021 takpagsfyl hvhnpilpye tedkkeqqll kkfqfdglll ndptllenld kglqpkqssl
     1081 ifpieesake iikpgrrqed kfvtepelda llshnrskfi eagnkvisge idlnpayqgk
     1141 eriacrfcpf rsvcnfdvml kennynriet lskkevmerl leneqeggsf de
//
LOCUS       WP_010772695             212 aa            linear   BCT 01-JAN-2025
DEFINITION  HD domain-containing protein [Enterococcus caccae].
ACCESSION   WP_010772695
VERSION     WP_010772695.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..212
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24470
     Region          6..198
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 mdnlkmeaik kytqsimekd qtghgmdhin rvvrlankia esencnrfiv iaaaylhdtv
       61 ddkivskpeq ayqqlreflq tidlsikeid qifhiiknls fsqelagtae eltiegqivq
      121 dadrldamga igvtrtiyyg ghkgnkiydp kikprllrsk teyreestvi nhfyekiill
      181 ngklntehak eigikrqkfl eeflneflee wn
//
LOCUS       WP_010772605             253 aa            linear   BCT 01-JAN-2025
DEFINITION  (Fe-S)-binding protein [Enterococcus caccae].
ACCESSION   WP_010772605
VERSION     WP_010772605.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..253
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28082
     Region          <2..235
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mkvsifstcv vdllfpnvgq amvevlerlg cetsfpdnqt ccgqptynsg yveesyatlk
       61 nqidcfeeae yvvgpagscv gmlreyqhfl kndpvygpka ealaaksfef sqflyrvlgv
      121 tdvgatlkak atyhrschmt rilkereapf illdhvagle miplnhienc cgfggtfsvk
      181 mpeiseqmvt ekmndvldte aevlisadmg clmniggkfn regkpikimh iaevlnqqvd
      241 kkrmdqpkim tvi
//
LOCUS       WP_010772647             488 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus caccae].
ACCESSION   WP_010772647
VERSION     WP_010772647.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 488)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..488
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54515
     Region          <273..487
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mgfvkralcs vtrkkgksli lflvifvlgn viagsiaiqq stqnveknvk kqlggtatiq
       61 ldyennqeef akedfkidql kvdlmkkigk spyvkyydyn avsgtqtkel ksasieseqs
      121 gvmmegftlk gsnyhkildv eekniklvdg kvftqedidn gknvglissk iaeenglsvg
      181 dqmvmdsrgy dyaengeeke lfkidipiqi igifepttve mkdkenkkne eqnmnkqyms
      241 lqqlntvylp nkavveinkd yteklkkvap dsafipeddq eeyytpvyvl kspddveafk
      301 eetqpllpkl yavkastdqy eqiggsmkkm sqisgyvvvi avlatlliis lvvllfmrdr
      361 kyelgiylsl gdkrshvmgq iiiemlvisg ialilslitg nflgkmvses llnsdllsns
      421 sdqmnmfmgf dglssnelta ddimnayevk fslgyivtyl vvglgtvlla ailpllyivr
      481 lnpkkimm
//
LOCUS       WP_010772803             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010772803
VERSION     WP_010772803.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..265
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29666
     Region          1..263
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mesyieliiq anqkkftdve riiaqyfldg ntelgiqela kklsvsnssi trfckkigla
       61 nykeliylyk ysskgtkkqs dssisyvnln yslllndiie kldkeevkka almidsgrii
      121 hywgtgynaf cgedfqfkfs rlgkivnvit dehsivmmah gvqqgdlvvi ssisgdneav
      181 ekaikivsek nakvivitan ekspykefak afcltssmgk kdmggispqi pvltvidily
      241 teilamyhed tikswiksev ilkgk
//
LOCUS       WP_010772807             476 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus caccae].
ACCESSION   WP_010772807
VERSION     WP_010772807.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 476)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..476
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53543
     Region          1..466
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 midlhdvtfa yedqetiiqh idlnvkagef ivlcgksgcg kstllrilng lipelytgel
       61 sgtgsileqe lvtkdfneyv rdigvvfqnp ktqfftsdvy selafameny gvprgemlsr
      121 ieeitslfsl epflersmfh lsggqkqlia fasasmlkhr lflldepssn ldeatieqlk
      181 aylrvlknqg mtiivsehrl yyltdladry lvmekgeite nytsqemkak slteiqalgl
      241 rslnqtrvmk sdekakgkdk lvlscdglaf hyrkqpsvlk ipsltltsaa itgiigpnga
      301 gkstfsklvs glikpkdgvi tlnnrvmrpk elieesfvvm qdvnlqlffe tvekeislna
      361 knsaefdkti emlnlapllm rhpqtlsgge kqrvviasal lsgkkiiifd eptsgldleh
      421 mkevsdtirw lhqenilvlv ithdkeflsq tcervlhfeq gkiiedyfie tttkee
//
LOCUS       WP_010772817             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010772817
VERSION     WP_010772817.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..283
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32289
     Region          1..283
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnlilklknl dklttsekal vdyildfpek viyfspkela ehsfvsisti yrlinkldld
       61 glnalklalv nylnednaek iididfpisa ednqyaltkk lktvydqtiq stidanhvem
      121 maatitllnk asfvdvyass aniyfaqnfq fqmqeigkri nvpiddymqn lsaanstpdh
      181 laivvsyegr gssakkilki lkknnskill itsknspllt eevdstllfa smenhynkis
      241 sfstrmslmy lfdclylaff nhdyeknlay klehyqkmnp dlr
//
LOCUS       WP_010772893             345 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Enterococcus
            caccae].
ACCESSION   WP_010772893
VERSION     WP_010772893.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..345
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38030
     Region          4..341
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mplielehvq kqfsgktgqv tavsdvsltv dqgdiygivg ysgagkstlv rllnglelpt
       61 egeviiqgqn vakmanrelr qfrkkigmif qhfnllwsrt ilenimlple lanvpknvrk
      121 eraqellslv glegrgdayp sqlsggqkqr vgiaralann peillcdeat saldpqttde
      181 vldllleink tlnltivlit hemhvirkic nkvavmelgq iveegdvlev frhpkqavtk
      241 rfvqqelepk edteellqel ikenpaglva tlqfsgdnan epvisqairk favdinvvqg
      301 qvqqakegaf gsltvmiigs anevektltf fkekevglev ihrge
//
LOCUS       WP_010772896             394 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Enterococcus caccae].
ACCESSION   WP_010772896
VERSION     WP_010772896.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..394
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=44040
     Region          1..388
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mnknklmrnl dnridygvil pvfllsiigi lslyvalsnd pnrpeignml mkqglwylvg
       61 gvsivivmnf sskllwrltp vfyviglimm glllkfydpy lesqtgsknw isiggttfqp
      121 selmkvafil mlayvvtmhn vknvnrtiks dfwligkmll vtmpviilil lqddfgtmlv
      181 flaifggvfl msgitwkiil ptflaalllg agtiylvttt tgreflysvg fkpyqfdrid
      241 lwmnpfhhdp drsfqpalai taigsggllg kgfnvsdvyv pvresdmift vvgenfgfig
      301 gcfiillyfi liyrmirvcf dtnnefyayi atgiimmilf hvfenigani gllpltgipl
      361 pfisqggssi lgnmlgvgli msmkyqkeat ieey
//
LOCUS       WP_010772944             236 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus caccae].
ACCESSION   WP_010772944
VERSION     WP_010772944.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26569
     Region          10..234
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 miqqeqsprp liqmqainky fpvgkeklqv lksldltine gefimimgks gsgkttlmni
       61 igfldrvsdg tylfkgedvs klsenkksef rneylgfifq qfflinslnv sqnvqlpcvy
      121 agkknndekr riaekylelv glgtktkakv nelsggqqqr vaiarslvnd pllimadept
      181 galdsetgte imelltelnr qgktivmvth dadmkkyatr vihmkdgrfl eeevir
//
LOCUS       WP_010772976             136 aa            linear   BCT 01-JAN-2025
DEFINITION  GtrA family protein [Enterococcus caccae].
ACCESSION   WP_010772976
VERSION     WP_010772976.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..136
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15953
     Region          2..123
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mkelfhkyke visylvfgva ttivnlviff lckdilgvdy kisnaiswfl svlfafftnk
       61 yfvfasnhed igsfiremll fywyrvlsfv vdmalmvlmv evmqissfwa kmvtqvavvv
      121 lnyffskffi fkkkts
//
LOCUS       WP_010773074             268 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus caccae].
ACCESSION   WP_010773074
VERSION     WP_010773074.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..268
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30759
     Region          64..227
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mikssiimci gevkkqyrny hnslstfmsl liwpiitffh tyftyqsfdv sslknfnihs
       61 nkefiiflit galvfncfws mvqsafflil erqngtiett flapvnrtvl mygralggll
      121 tnvwmfgsfs lllillsssi sikvlllsfl sffvilisst iwggfmnslf lisrdanylf
      181 sifdepmnlf sgtkmpvqaf plwgrfissf fpatyclyiv raifldqkiq itmillfils
      241 lvvlvlltql ilyfaeknnk kngslqly
//
LOCUS       WP_010772978             363 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus caccae].
ACCESSION   WP_010772978
VERSION     WP_010772978.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..363
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41535
     Region          115..362
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnkclmrhlf dkafllglcl sillkqvyqs emvifvlvtv vlsmlvwvik dpkfstltil
       61 illiasvwwq eyayflpvlf ydglmetgkk gmilnsslvl lfflssgnys tslklyiill
      121 calasylalf tlrdkrlyqd yllleeekce hrfilesqna elirqqeitv nlelsnernr
      181 iardihdnvg hllssallqt aalktinqeq hlveplnqlq etinegmssi rdsvhdlhde
      241 sislslacqn ilksftfcnv evrgsfteri skeyklacim likealanvm khsqadtvim
      301 dfqehpgfyk laiedngqqn rkknpneigi gligmqerie klggrlswqq kevgflllvi
      361 lpk
//
LOCUS       WP_010773170             121 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010773170
VERSION     WP_010773170.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..121
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14032
     Region          1..107
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mnydgnrpiy qqiieqvehw iasnqwqpne kvpsvrqlae dldvnpttvq raysvleqee
       61 ilisqrgigk fvtdktdkia dlrlrlieah ieafitqlqk lnltqnekeh iierivrsan
      121 e
//
LOCUS       WP_010773175             104 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Enterococcus caccae].
ACCESSION   WP_010773175
VERSION     WP_010773175.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..104
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11311
     Region          9..96
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mfsflkgnsi nttdlqqmld skpimidvre kseftaghip naknvplski styqskesqp
       61 vyvicqsgmr srqavkklka kgidainvkg gmsawrgvvr ggkl
//
LOCUS       WP_010773186             120 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010773186
VERSION     WP_010773186.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..120
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14406
     Region          3..113
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(4..6,20,36..38)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(50,53,57..58,67,85,89,95,99,102..103)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 maykihefsk mtgltpytlr fyekeglisv krdqnniriy ddrnkewidf fmhlkktgmt
       61 ivdlkqylvw whegdstnqn rldllkkqkk ialnemkqiq eginmldyki nvytkrvqgn
//
LOCUS       WP_010773209             546 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus caccae].
ACCESSION   WP_010773209
VERSION     WP_010773209.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..546
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62800
     Region          6..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          256..538
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mttledllki prfsdlkllt nprnadtive sieisetpdv anfipkkifl lttamvyknn
       61 qkelitlids lkeqeaagig ikvgrfieti dpaiidyanq idfpivlvps tqplgallhq
      121 llnylwdtkt eqlsyaldiq krfsdllihd vsiarfiadf gkmintpvil lspyrkviah
      181 skhftqtskp aeyyveqlvn kydnwnedsh asfmikdlnq eslqiagfsv tvnsyfphyl
      241 lilnpqqvpy pmsefaveqa clvlsfmlyk nqkvqesldf lksdflaqli eyqqtphqsr
      301 rdwldlgtny glkkstqyqv vyavcsqttt tatkikyqqe esdvafqwll etlpprikhi
      361 sifkvkntnh lailiqskvd dleniltels lelskklpit ltfalgnlye sveqiansfi
      421 eaktayeeml tmtngslthr yhpkgmkslf ekmsledihy fcettlkela ypvedsfiel
      481 rktlqcylsf qceisktake mylhrntiky ridhcakllg ksiqdptnsl nlrlalelse
      541 rsnqhq
//
LOCUS       WP_010773203             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus caccae].
ACCESSION   WP_010773203
VERSION     WP_010773203.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44915
     Region          11..404
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mdelkgrnrq tpywkqiiyi ltigwiviwi yrtvltpiyp iiseyfggas daqlghissf
       61 yflgyvcmqi psgilvdkvg kkqilipgfl lfgfgalivg laqnigivfi gsviaglgcg
      121 tyygvayslt aqyvpiskrs lstaivnsgt aigsglglis ssylvgtgkv pwqalifati
      181 lliiiavglf lryirfektg rvvnvnknfe gkkqvslssl fkprmisayi lyfstlytyy
      241 lidtwlpnfl etekgfsgts vglasslvff taipgalifs rladripkkk iqliillell
      301 aasvlfvtvv ttnqtilvig imsygffgkl avepiiiswl gesapkgsva tmygvfnffg
      361 msasvivpsl tgkisdltgs klyafylaim iigigtllfy vinrivdsks ke
//
LOCUS       WP_010773247             417 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus caccae].
ACCESSION   WP_010773247
VERSION     WP_010773247.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..417
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=46507
     Region          1..414
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mnklifwlen sfspkmnkvn nnpwivsikd simqtlpfif lgsifsmlai lneyfpalps
       61 fwvpfgwtmg kislfvafli pfnlmekkrl rkqrivagms glvlflmiis pqiekdgvig
      121 fghdalgagg mfvaivagli agfvlvtlgk ftffkeesvi pdfvrawfds mlpigiiiif
      181 gwvvvlimkv dlynivlsif mplssfmesp ggfvgmmfli cflysmgist wvltpvvqpv
      241 llkaiaenia lvqngtasve tlnlvtsstl ysaylwiggi gctmplvlmm mrarskkisa
      301 lgkaciapsi fninepvifg avawnpllmi pmwlqgiilp iviyiftkvi pfapipkvqf
      361 elwycpfpfa twfttgtitg iilmlvifai staiwypffk ayddqetkae nqtmkea
//
LOCUS       WP_010773257             149 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Enterococcus
            caccae].
ACCESSION   WP_010773257
VERSION     WP_010773257.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..149
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16860
     Region          15..145
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtstrfllpk enktayqkia eldqigksgs ineklqelik iyasqlnscv fcidmhskda
       61 lakgeklqri igltsweeas fytaeeravl aftkevtliq qggvrdetyh elqkyyseke
      121 igellilvgt iniynrigvt trlqpkidq
//
LOCUS       WP_010773278             226 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Enterococcus caccae].
ACCESSION   WP_010773278
VERSION     WP_010773278.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..226
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25496
     Region          47..222
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mrnemmhrpv vkqelvdfmr nkqkkiqgel gvieeeahea gvpiiphetv vflqffldqi
       61 kpknileigt aigfssslma qyvgeeghvt tidrfdvmir kakvtyerlg ltdkvtlleg
      121 qaaevlptlt gpydfifmds akskyieflp eclrllrvgg vlmvddvfqa gtildpieei
      181 prsqrtihrk lnqfldtvmt hpdltstllp lgdgvimitk ekelte
//
LOCUS       WP_010773237             459 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Enterococcus caccae].
ACCESSION   WP_010773237
VERSION     WP_010773237.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..459
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51036
     Region          25..429
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mnnadpesqs liaqilllvi ltlinaflaa seiavvsvnk nrveqkaeeg dakakkllkv
       61 lqdptsflst iqvgitlvni lsgasladsl saklapvlgg gtaakniani iilalltyvs
      121 ivfgelypkr iamnkseeva qatsgfvrvi gvvakpfvwl lsastdllsk itpmkfddad
      181 skmtrdemry mlesegvldn delemlqgvf sldtkvarev mvprtdafmi dieddiqkni
      241 davlsenysr ipvynadkdk ivgvlhtknl lkaahkfgfd niqlnsiiqe plfvpetifi
      301 ddllyelkrt qnqmaillde yggvvglatl edlleeivge iddetdeven lytkinehey
      361 liqgrmlide fneafgtdlh msdvdtmagy litalgtipd egeklsfdvg nltltseeme
      421 gtrvlalkvv fhdeeivdee peeyrrffrk emeddeprr
//
LOCUS       WP_010773724             143 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus faecalis].
ACCESSION   WP_010773724
VERSION     WP_010773724.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15659
     Region          4..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msvyqhilva ldgsdqseka fheavriake ekatlylati indaefttsp fsfeelydle
       61 khkseemltg kakqaseigv ktvkkivelg spkrylanti senyaidliv lgatgrgaiq
      121 rtligsttdy vvnhalcnvl vvr
//
LOCUS       WP_010773780              61 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010773780
VERSION     WP_010773780.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 61)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..61
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7240
     Region          1..60
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mrewlvdsrl knkltqeqva eradiersyy nmiergkrrp sveiakkian vlsidwtiff
       61 k
//
LOCUS       WP_010773748             686 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus faecalis].
ACCESSION   WP_010773748
VERSION     WP_010773748.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..686
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=79098
     Region          19..629
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkkinnrlgl flffvllfwa ktilayyldf slgvkgslqr eilwfnpvat tlllfgfsly
       61 fkkhktfmls ltllnvlntl ilylniifyr eftdfitiqs vfgfskvseg isgdllalmr
      121 vhdvfywldt lvllvlvfys fkqrrnhqvf vtkpinrrla isisclsvll fsvnlflset
      181 drpqllqrif drnyivkylg ldaftaidgv ktamsnevra eassnelpei mkftkqnnlp
      241 lnpqyagiak gknvfvihle sfqqflinmk vqgqevtpfl nqlyqnkati sfdnffhevg
      301 qgktsdaenm letgtfglpq gslftqlgsd ntfeaapavl gqkgyttavf hgnvgsfwnr
      361 dhvyknlgyq yffdrsyfsk ddkmlgygil dkqllresas elehlqqpfy akfltvtnht
      421 pyytddqnfp fpklntgnsi vddyvrtahy ldqsleqffh ylqttslynh sifviygdhf
      481 gisdannkdl ckafnrdpkt wtnydnaqlq rvplmfympg ytqgkimhey ggeidvlptl
      541 yhllgvddkn yihfgtdlls pqykqvvpfr ngdfvtpqfs ylggeiynnq gkkldqvpad
      601 lkaevtkdnd wvkkslslsd klnrenllrf ykpqgfqevq pkdynydvaf eknkvlevek
      661 qknaqstslf sqngnqttvq nypttp
//
LOCUS       WP_010773832             402 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010773832
VERSION     WP_010773832.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..402
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43824
     Region          6..402
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkrsiiwkta frsilknkrr slltmlgivi giasvitiva igngfkedmv dklsaekqke
       61 nvkkisfsay ntsdmfsdqa mftdndlgvv rmvpgvekid fdqrevdgaq kgtlnfqagp
      121 knlsvtyela nkttkellag rqlndgdnak ldktvvvdel vakelyqdst aavnrtfpyk
      181 eqlftivgvt tntsgaigpg nddsllyfpk ntyehyfgkl kdtstlkltv apgyqpdqvl
      241 ketiktlsqq gtmknsgtyq eynvkdtike mgsllnnltl fisaiaaisl viagvgvmnm
      301 myisvserik eigirralgg tasdikkqfl tegialtlig gitgyllgmi iaylasmalp
      361 fsvrpdlmtv slaigisvfi gvvfsyfpas aaskkdlidi mk
//
LOCUS       WP_010773792             443 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            faecalis].
ACCESSION   WP_010773792
VERSION     WP_010773792.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..443
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46404
     Region          28..438
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 msekkqnnlh ltvgpedsvs fgqatmlgiq hvlamdvyvv pviiasiigi staqtssliq
       61 atfiaaglat iiqshfcmrl pvaqgpsfip igaiagiyfa nnqqgngwga vlgaslvgai
      121 vviilgftgi fnrlitkfvp pivggtiifv vglslmpval sdniyhakge lgqnillafi
      181 aagtliffal lgsalkkgri frvssvilal lfgsiaaqll gvldlsavsk aawfilpqlp
      241 lvnfsfqfdw saiatmlviy lvlmaettgt wfavshvvae plteekinrg vigeglgclv
      301 ssfiggtpvt systnagiis itgvasrkvf vaagawfvlf glsgklstli saipapvigg
      361 vfvvvcgiis vsgmkvmsdv tihekemyvi avpiimtlal tllpkeflet lpqflqylfs
      421 spvatasiva illqailpnv qeg
//
LOCUS       WP_010774008             698 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010774008
VERSION     WP_010774008.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 698)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 698)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 698)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..698
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80286
     Region          <53..187
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          <57..>344
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
     Region          583..696
                     /region_name="FtsX"
                     /note="FtsX-like permease family; pfam02687"
                     /db_xref="CDD:460652"
ORIGIN      
        1 mifklslknl kahvpnylvy yismtfaavv yycfraiayn qplvagagrd ieikrslglg
       61 stlvtiiilg fmlaanrffi gkrsqeigly rliglrksqv sliflvenlv lgfvslingi
      121 ilgviftklf smilakvmfl evpsffyisw rsvietgvaf afmilivclr siwmiyrypl
      181 sqlmhqekig qinysrltkr rqflgilgpi cllagyfiaf dfrnlatgiv ykqlndsldi
      241 sipmiitltp fiilglcvvg tylffrytmy fiirlfnhrk kwyyqdlrmi tlgnakrylf
      301 kssktltglt lliatalsgi gvmvfvytis mhtvnsdgpv dflvsqesyp klkkvldeak
      361 dtkiknevil sykitgiers lrigqaqeeq etieavnvls fsnyrnyqki npylndlhlk
      421 ndqsviymds ftnilsgmsr yesklqfveg ekaqlqqvlp nylgnfllqy slptivvsda
      481 lyqkvtknsi qyqinavnvd tksreklyea vnkqiatewq apilykyekn nqqlsgfakq
      541 mpneeakntq ddvtetwrln mndryaslry erkingltly vsmfvailal fitgsilmlr
      601 qlfsavserq dyvtlkrmgv sskaitkqiy rqnsliffpp mvigilhttf aiyllsqfik
      661 spgyllvyls cviliivyli fyiltsaiya rmirhihf
//
LOCUS       WP_010774048             530 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010774048
VERSION     WP_010774048.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..530
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62253
     Region          5..123
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          273..519
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mklrellsig dlkkgkiltk eigldnevds amvleaidie nwsrknqlil tsfyalhdlp
       61 ekeleiffvk mrrigisgli lktdrfikmi pewfielcfn yeiplikitq disyekilft
      121 iyepllnyqs hvlrtyydvr qrftklerhy ptvetimqef ydiiklpfal kmldkhleis
      181 dgdlphdaiv lsreklknse ftkndysllt lyshanpkkq lalevsifns ystnclllvy
      241 lqdekvketd lviienaidv lqekfntenl lkkerytrln nladailqnt pqnpdelnsl
      301 lrevqmqeld syqaiafstk dtntqlmker iiallrtlrv ksiffdqlny savlfnfnes
      361 dgkitklqls rllaelleen dtltvavssl ksregikell iecldilrfn etfyngpivt
      421 ladigvfknf iredqlenld elipralyql aennydlfet lysffqnnrn ykqtseamfl
      481 hsktiryrln kveqlldidl anplqllnye iatyiikmrr ralekqsntr
//
LOCUS       WP_010774143             345 aa            linear   BCT 01-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Enterococcus
            faecalis].
ACCESSION   WP_010774143
VERSION     WP_010774143.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..345
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38528
     Region          4..343
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 malielrhvk kefsgkagkv talkdidltv esgdiygiig ysgagkstlv rllngletpt
       61 egeveiqgqd iallpnkelr nfrkkigmif qhfnllwsrt vlenimlple iagvpkqnrk
      121 sraeeliklv glegrenayq sqlsggqkqr vgiaralann pdillcdeat saldpqttde
      181 vlelllkinq elnltvvlit hemhvirkic nrvavmeyge iveegkvidi fkkpqteiak
      241 rfiqqeadkn ieetelvvee mleqypngki vrllfhgeqa klpiishivq eyqvevsiiq
      301 gniqqtkqga vgslyiqllg eeqnilaaie glrklrvete vigne
//
LOCUS       WP_010774368             220 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease, partial [Enterococcus faecalis].
ACCESSION   WP_010774368
VERSION     WP_010774368.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15349074
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         <1..220
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          1..216
                     /region_name="ABC-2_lan_permease-like"
                     /note="lantibiotic immunity ABC transporter permease (also
                     called ABC-2 transporter permease) subunit and similar
                     proteins; cd21809"
                     /db_xref="CDD:409634"
     Region          26..42
                     /region_name="putative TM segment"
                     /note="putative TM segment [structural motif]"
                     /db_xref="CDD:409634"
     Region          83..103
                     /region_name="putative TM segment"
                     /note="putative TM segment [structural motif]"
                     /db_xref="CDD:409634"
     Region          117..142
                     /region_name="putative TM segment"
                     /note="putative TM segment [structural motif]"
                     /db_xref="CDD:409634"
     Region          154..176
                     /region_name="putative TM segment"
                     /note="putative TM segment [structural motif]"
                     /db_xref="CDD:409634"
     Region          189..209
                     /region_name="putative TM segment"
                     /note="putative TM segment [structural motif]"
                     /db_xref="CDD:409634"
ORIGIN      
        1 llmliealqt hfdkpeiift lsdiysdsvl yimllvnimi yvaiaaylfs reytestlkt
       61 ilpipisrtk lligkfctll lwivmltlvt wagifiacgl yhavftlegy sllvaivwlp
      121 kflfgsilmf ltvspfvfva mktkgfvapm igsavivmgs aalsnqewga lypwtatyfl
      181 vqgklqstgy ptllsvsiii lvsavgflmt fhhfkkedlk
//
LOCUS       WP_010774450             254 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Enterococcus faecalis].
ACCESSION   WP_010774450
VERSION     WP_010774450.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..254
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=30058
     Region          104..213
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mynkkmleyr dvdsedynny senalfllkv isdwaaipis eityhevidy fvnnfnieiv
       61 ffddndriin pdykfindti ykiyptfker vsgftvtdgy nykiflnfdm mrhrliftil
      121 helvhiyfhc sskkymkifa slniedhypk eilpfedean iiasilylnd tklinyileg
      181 nsfhsimslc kiskaalhcr imnylihnig lnkntalfky lnpykeevfg qtalknlqsi
      241 isypsfikrl nqea
//
LOCUS       WP_010773916             746 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Enterococcus
            faecalis].
ACCESSION   WP_010773916
VERSION     WP_010773916.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 746)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..746
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82360
     Region          1..>81
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          106..705
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 micqncqqne atihlyanvn gqrkqldycq scyqklknqa nnspqnmgqd pfgfgslddl
       61 yrslsrqmqq gnpyeqqtpp tqfgdggngg qpprggagag qgllgeygin iteaarqgdi
      121 dpvvgrdqei krvieilnrr tknnpvlige pgvgktavve glaqkivdgd vpqklldkev
      181 irldvvslvq gtgirgqfee rmqklieeit eaenvilfid evheivgaga agdgnmdagn
      241 ilkpalarge lqlvgattln eyriiekdaa lerrmqpvqv deptvaetit ilhglqkrye
      301 dyhhvkytde ainaaanlsn ryiqdrflpd kaidlldesg skmnltiqlv dpktidkkla
      361 eaeqqkqqas aeedfekaay yrdqinklqa ikekqisdee tpvitekdie aiveqktgip
      421 vgdlkekeqt qlknlavdlk ahvvgqddav dkvakairrn rvglgkqnrp igsflfvgpt
      481 gvgktelakq lafelfgsed smvrfdmsey mekhsvskli gsppgyvgyd eagqltekvr
      541 rnpyslilld eiekahpdvl hmflqilddg rltdaqgrtv sfkdtiiimt snagtgavea
      601 nvgfgaareg vtksvlgqln nfftpeflnr fdgiiefkal skenlmnivs lmleevnsll
      661 akqklhievp tevkeklvdl gydpamgarp lrrtiqeqie dgiaeyyldh penhqlvaal
      721 dnegkiivtg aqevtktets tsdqae
//
LOCUS       WP_010774494             505 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease/substrate-binding protein [Enterococcus
            faecalis].
ACCESSION   WP_010774494
VERSION     WP_010774494.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..505
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55955
     Region          2..208
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          236..499
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(242,244,292..293,296,339,341,419,443)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mqalietffa rkeeylqali ehmqlsfisl lfaaliaipl aiyltshrkl aesllqvtgi
       61 fqtipslall gllipligig rppaivalvi yalfpilqnt ytglteidps leeaaeafgm
      121 skkeklfkfe lqmalpfiis girtatvlii gtatlaalig agglgtfill gidrnnlsli
      181 figalssaal avlfnygihw lekangrrli iggtilglll ggsffwnqqt sskekqltia
      241 gklgaepdii inmykaliee nsdiqvklkp nfgkttflyn alksdeidly peftgtviet
      301 flknppqldn qpqvvyeaar aglkkqenlt llkpmryent yavavkrsfa kahqlktisd
      361 lqkisnqlka gftlefidrq dgykglqeky hlnlnvqsme palryqainn gevnvidays
      421 tdselrqydl vtleddqalf ppyqgaplik tatlekypel aeilnklagk iseeemsemn
      481 yqvnvegqdp sivakdylke knllk
//
LOCUS       WP_010774501             903 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010774501
VERSION     WP_010774501.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 903)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 903)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 903)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 903)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 903)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..903
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=105050
     Region          1..898
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
ORIGIN      
        1 mkllaveivg fgkwqqqkit fesgnqllyg anevgkstly qfiqamlfgf ptkgkrkrdy
       61 apknggsygg rlwlahpvfg evqverfkek nkgqaiiyyq qqmgdektlq qmlhpltkkl
      121 fqevftfqqe qlitsdklte eelqtsllai gvsgsqqllt yrnayfkeaq kifkgkgqqp
      181 llnqklaayq elkeqiqeke aqqqtfqqle etireteqqr vtlqqqlket qqdllqvaeq
      241 qrhfplyeew qslpeetenv vlvkedqvql eetfqeymyl dkerqrltke lslqsealdv
      301 pegyafyleq ealiqqllnq rydmqqlmte sewmtqtfdq nrqemvllen ewswsperpp
      361 qlfydnetvq kwrqqqvayt qalqkgqeqk aflasqienl edqltdfeke haaffgeatr
      421 aqkaqktsqp lwlllgsila llgfflpspl kwglvlvgvs liakevigya trkeassdev
      481 keewqtklsq ldylneqfqq alnqereaql qveqleqava eqaqvhqlgk mnqidtlmnq
      541 relitrylll vqtneelmsq lkenqqkrqv feeqifplmt hlplqgksls eklhflegfa
      601 eemekvrfaq eyqadgylkq qlrelktkqq ealtriqpll iryrilsiad vpsriqqltt
      661 qqaqvgrgqe latqlgnlfp eavteatlkd rslqlalqqa leesqldkiq eqyqaliyek
      721 qqlmtdgtld elyqrqailk aeikelaqrw sgyqlagqll mdlltelseq qlpsllqyas
      781 syfalltnqr yqsiqvaegq lvavtkgqem fylhelstgt kdqlmmavrf aflavqgeql
      841 icpiiiddgw lhydhqrkaq laelftkfgq kqqvicfssd qemvsyyqdl qqrvialegg
      901 svk
//
LOCUS       WP_010774529             205 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010774529
VERSION     WP_010774529.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 205)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..205
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23556
     Region          2..202
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 medinwkiek gqcwgilghn gagkttlsyl vlgllkpskg vvhnyikkve ylpemggfye
       61 rltvrenilf klelsgekqk skklkqvlke fglidyefkr vdklsqglkk rvalamlflr
      121 eseayyfdep tnaldpemkk klrqliihlk eagkiilins hdlafveeic tnflilnngk
      181 vcfnepnigv nleeiylekv gerhk
//
LOCUS       WP_010774588             349 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Enterococcus faecalis].
ACCESSION   WP_010774588
VERSION     WP_010774588.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..349
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=39590
     Region          1..346
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mkfldlfagi ggfrlgmesa ghecigfcei dkfartsyka ihdttgevem hdittisdef
       61 irgigsvdvi cggfpcqafs iagkrkgfed trgtlffeia rfasilrpry lflenvkgll
      121 nheggatfet ilraldelgy dvewqvlnsk dyvpqnrerv fiighlrger trkvfpfkkn
      181 drtftklqgq qiyantlttr ieaqgtgtyv iereqhedki aipvltpdrl ekrqngrrfk
      241 ddgeemftlt aqdkhgvaii qksrgyndgg iykvaptvts nswhennflk dnirirkltp
      301 recwrlqgfp dwafdkakev nsdsqlykqa gnsvtvpvia diasrlese
//
LOCUS       WP_010774629             106 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010774629
VERSION     WP_010774629.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..106
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11648
     Region          28..99
                     /region_name="Cupin_2"
                     /note="Cupin domain; pfam07883"
                     /db_xref="CDD:462300"
ORIGIN      
        1 mliksaesee mtiffdkenq pnaqvqmgii tlqsgekrpl agyarheqde ysyvisgeah
       61 tiledgqdlv gkagqaqlie ageghinynd glepavvvwm lverte
//
LOCUS       WP_010774678             240 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Enterococcus faecalis].
ACCESSION   WP_010774678
VERSION     WP_010774678.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28080
     Region          1..227
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mrtivfdvdd tlydqqqpfr namtkifpnv atedmhelyl rfrhhsdetf pkvlanewsl
       61 dfmrffrmne tlkdlnypgi sqeegkifqq vyeeeldnit mhpevtklld tlqekeipmg
      121 iitngptdhq fkkvkqlnle kwvpsqniii sqstgfqkpe keifdlacnq fcmepehtly
      181 vgdsydndiv garnggwhsl wfnhrsrelp scqpashlae vtcftelcpt veklfnlrel
//
LOCUS       WP_010774711              66 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Enterococcus faecalis].
ACCESSION   WP_010774711
VERSION     WP_010774711.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7141
     Region          1..63
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mnngtvkwfn adkdfgfitg edgndvfahf saiqtegfkt ldegqivtfd teeglrgpqa
       61 dniakd
//
LOCUS       WP_010774714             363 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010774714
VERSION     WP_010774714.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..363
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40570
     Region          170..362
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mirfkaivsr vvkelirdkr tlalmllapv iiltmmnfvf vsnsethvki gydssvptev
       61 mkafpsdkvk tkeydgnndi kktlsdnsld afitlkdstf evtyenedps staqikalft
      121 gvltsnklke ltvevqkmai qtgqtpqlee fsvkdayvyg sknstffdki fpiligffvf
      181 ffvflisgia llkerttgtl erllatpvkr seiifgylag ygifailqtm iivfysmfil
      241 nleiagnlgw vlatnilial valvigifvs tfansefqmv qfiplvvipq iffsgiipln
      301 tmadwvqkvg yifplsyagn altavmikgq gfdhiwldll ilglfvlvft ilnviglkky
      361 rkv
//
LOCUS       WP_010774729             298 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Enterococcus faecalis].
ACCESSION   WP_010774729
VERSION     WP_010774729.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..298
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=32001
     Region          2..283
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mnkfftaqrl kdtayvtvga filaisinav llpnklvagg angisiviny vfgispaivl
       61 yainipllvl cflllgkevg vktiygsliy pffvgitsem pvlthnifla alfggiitga
      121 glglvfrgna stggtaiisq ivnkyfkvsl giailfvdgl vilsamyafn adivlfslic
      181 lftigrvvdm iqvglvrskn vmiispkyva iqerllreld kgvtlvpieg gyrsakgmll
      241 mtvirekdfp rlkeaileid eeaflismsa sevygkgfsl kkvadsygve atnannlq
//
LOCUS       WP_010774791             487 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus faecalis].
ACCESSION   WP_010774791
VERSION     WP_010774791.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..487
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=51631
     Region          1..478
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mnglmawmek yilptaakig aqkhlvalrd afigtlpatm agsvavmina iirdlpqefv
       61 styaaslead kgifavlnvi igingfvwng tlaiaglifa fswgynlaka ynvnelaggi
      121 vslatlisgv afapnntael avkvpekian aingaeigas iannqltvnp wgwlnlnhln
      181 gnafftvmim galstiifck lmqadltikm pdsvppavsk afaailpati alyvvaiinf
      241 tvsklsggql lidliqkyia epflglsqgl gavlivtvfv qifwffgihg anvlapvleg
      301 iwgqaqlini difqkgyegk tgtaavlaai ddgkaymwvr gsfdafawfg gsggtivlii
      361 aillfskrad yltvgklslg pgifninepi mfglpvvlnp imfipfviap lvattigwva
      421 tylglvapvs qqvawvtppl llsflatgad wrapivalvc mvvtfliwtp fviaankmdp
      481 algeseq
//
LOCUS       WP_010774859             752 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Enterococcus faecalis].
ACCESSION   WP_010774859
VERSION     WP_010774859.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..752
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85910
     Region          235..723
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mqgnnlfnng llqpkkppig qeqqkmtryh qlrlvfglvg vllypfailg siplliglav
       61 dkrdkaanvf dmdyesflkr nsivflsfsa vlfvinvfaf ilwiprgyls ayllfplnll
      121 htalrfnwet iaalligssg mgaiflafss fvakrkvisk ederkkites kaykdreknk
      181 feesqrftde qeeayeeave tvdidaykql tnqlllgtse fglsyimnfs efnqhalipa
      241 ttgsgkttll qllvqhavkf nfpvilidgk gardtlesmr eiakfydkev haftddgdmr
      301 ynpvehgndi sirdklvsla etesvfysga akallqvtiq lldefkgakv tlsgdtrtte
      361 tverslpfvq rfllprnvlh lfadailqnn pklfeievek kiqqpkkksa kerseilpds
      421 dldkeekeed sqirnskfrn isqlgiaqke tetvvlnpet ldldsyylll krnlrylptd
      481 ketgenikqk lferlfvrye hkdspfylya tsealqtnin mlldselgkl fdtknaknvl
      541 dvqeivnqrk lvyvsfngli ykeyirtlaq mlvgdvnyfa semyrknvkr evlvifdepa
      601 sylnetfidm vnkgrgagvy giftpqtmad iaklgdklme qlvgnvntlf igktnekgea
      661 eywsetmgty qdidvtsvte qedgysdvgk sdwsgdrgtk rnvdrfkisp nkikelrtge
      721 fiiyrtaenv nlppqkvyvr nalewlqksn sk
//
LOCUS       WP_010775037             154 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Enterococcus faecalis].
ACCESSION   WP_010775037
VERSION     WP_010775037.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..154
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=17660
     Region          35..119
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mvtseelmar fsdltykfep nmpekqkgly innvvylnpq qhpreltstv aeeighhlts
       61 vgdiidqdtn ekrkqeqkar digatmvvtp qdlidcyher ftyvwecadf lgitkqalec
      121 alsayskqfp eglvygdyrl ffkpngtlgi vkwf
//
LOCUS       WP_010775162             752 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Enterococcus faecalis].
ACCESSION   WP_010775162
VERSION     WP_010775162.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..752
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85910
     Region          235..723
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mqgnnffnng llqpkkppig qeqqkmtryh qlrlvfglvg vllypfailg siplliglav
       61 dkrdkaanvf dmdyesflkr nsivflsfsa vlfvinvfaf ilwiprgyls ayllfplnll
      121 htalrfnwet ivalligssg mgaiflafss fvakrkvisk ederkkites kaykdreknk
      181 feesqrftde qeeayeeave tvdidkykel snqlllgtse fglpyiinfs efnqhvlvpa
      241 ttgsgkttll qllvqhavkf nfpvilidgk gardtlesmr eiakfydkev haftddgdmr
      301 ynpvehgndi sirdklvsla etesvfysga akallqvtiq lldefkgakv tlsgdtrtte
      361 tverslpfvq rfllprnvlh lfadailpnn pklfeievek kiqkpkkksv kegseilpds
      421 dldkeekeed sqiknskfrn isqlgiaqke tetivlnpet ldldsyylll krnlrylptd
      481 ketgenikqk lferlfirye hkdssfylya tsealqtnin mlldselgkl fdtknaknvl
      541 dvqeivnqrk lvyvsfngli ykeyirtlaq mlvgdvnyfa semyrknvkr evlvifdepa
      601 sylnetfidm vnkgrgagvy giftpqtmad iaklgdklme qlvgnvntlf igktnekgea
      661 eywsetmgty qdidvtsvte qedgysdvgk sdwsgdrgtk rnvdrfkisp nkikelrtge
      721 fiiyrtaenv nlppqkvyvr nalewlqksn sk
//
LOCUS       WP_010775174             630 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF262 domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010775174
VERSION     WP_010775174.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..630
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=74375
     Region          5..590
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 mkkkfeakqc sveellkknk qlykvsnfqr tyawkykqqe dlmndlfnhl kitdeglyen
       61 sdffmgsfif ykgsrekyiv dgqqrlitls ivfsimrrkc ieiknnsrik fkkietheia
      121 gdiindlygy iytkigseia ptvwphskne qgylfgeiln tdsnqkintp ectscnsyye
      181 aynsieeiid sklerkrnnf ekvkllkalf dqikfaetvv lnlddentay eiysninskg
      241 vtltdidlik ndyiyktkdy ysvpgqtnia selwdkinln itlsstitfh dffkycwyml
      301 heedvdeyyd sesnlfemfq nkyrdgssar kldklfhdle llskllhnle ttdnlpkndn
      361 wpitikkitf lnkisndsis nlyklwvlpl yykaisadkp nnmkyfsvfk kcipfisdtl
      421 ftyklllryq etqyevlrdl eslyssifrn llkfkanesp aiiveelkre rsgilnnsqe
      481 iiqkaiqels yskktnspmd tdlvrylier lnendfntqs vvggiehiie dekgtkcssn
      541 ignlvflegn yndmankfkq dllkkhndde nkverlllek kfteiytrse ypqvkelcrt
      601 ypdgdfteve vkerakymak yfideylein
//
LOCUS       WP_010775182             764 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus faecalis].
ACCESSION   WP_010775182
VERSION     WP_010775182.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..764
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87990
     Region          4..757
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mkqikrlfqi dpwkirtthl dkenlrlqes ltsigngymg mrgnfeehys gdhhqgtyla
       61 gvwypdktrv gwwkngypdy fgkvinainf iamdlqidgq tidlattpye dfsleldmqn
      121 gvlsrqftiq tpknkvrfsf erflslekke aayihltiem legtgtitlh skldgdvqne
      181 dsnyeehfwe eraietqetl gfvttktipn nfeierftvt agmrhfidga svvptytqqp
      241 laltaeltvs lnegettait kevlvvtsrd vpetqqitrv nelfaemttl ypeakagqaa
      301 awakrwqlad vviegddeaq qgirfnlfql fstyygeddr lnigpkgftg ekyggatywd
      361 teayavplyl alakpevtkn llkyrhnqlp qaihnaqqqg lkgalypmvt ftgvechnew
      421 eitfeeihrn gaiayaiyny vnytgdedyl kdaglevlva iarfwadrvh fsqrhkqymi
      481 hgvtgpneye nninnnwytn tiaawvlryt resylkfqee ttlkiaddel akwadivenm
      541 yfpvdnelgi fvqhdtfldk dlmpvsdlpl selplnqhws wdkilrscfi kqadvlqgiy
      601 ffndafslee krrnfnfyep mtvhesslsp sihavlaael gmeekavemy qrtarldldn
      661 ynndtedglh itsmtgswla ivqgfaqmkt dhqqlkfapf lpatwtaysf hinyrnrllf
      721 vevaadqvaf tlldgpaipl tvydqkytlk drlvlpirke evhv
//
LOCUS       WP_010775251             138 aa            linear   BCT 01-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Enterococcus faecalis].
ACCESSION   WP_010775251
VERSION     WP_010775251.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..138
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=15309
     Region          1..106
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 miktsavgrl tksselrvts tgkavanfal ackrerldkd gnaqttfiqc viwgkpaevl
       61 akytqkgsli avngelqsrs yddqqgqthy vtelvvsgfe flesketvqn reqkqqmpem
      121 anaepfygmd dmeppayh
//
LOCUS       WP_010775204             686 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus faecalis].
ACCESSION   WP_010775204
VERSION     WP_010775204.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..686
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=79112
     Region          19..629
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkkinnrlgl flffvllfwa ktilayyldf slgvkgslqr eilwfnpvat tlllfgfsly
       61 fkkhktfmls ltllnvlntl ilylniifyr eftdfitiqs vfvfskvseg isgdllalmr
      121 vhdvfywldt lvllvlvfys fkqrrnhqvf vtkpinrrla isisclsvll fsvnlflset
      181 drpqllqrif drnyivkylg ldaftaidgv ktamsnevra eassnelpei mkftkqnnlp
      241 lnpqyagiak gknvfvihle sfqqflinmk vqgqevtpfl nqlyqnkati sfdnffhevg
      301 qgktsdaenm letgtfglpq gslftqlgsd ntfeaapavl gqkgyttavf hgnvgsfwnr
      361 dhvyknlgyq yffdrsyfsk ddkmlgygil dkqllresas elehlqqpfy akfltvtnht
      421 pyytddqnfp fpklntgnsi vddyvrtahy ldqsleqffh ylqttslynh sifviygdhf
      481 gisdannkdl ckafnrdpkt wtnydnaqlq rvplmfympg ytqgkimhey ggeidvlptl
      541 yhllgvddkn yihfgtdlls pqykqvvpfr ngdfvtpqfs ylggeiynnq gkkldqvpad
      601 lkaevtkdnd wvkkslslsd klnqenllrf ykpqgfqevq pkdynydvaf eknkvlevek
      661 qknaqstslf sqngnqttvq nypttp
//
LOCUS       WP_010775257             212 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010775257
VERSION     WP_010775257.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25523
     Region          5..>82
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msinkkdikk eeiiftamkh fskfgyektk lldianeakt stttvysffk tkhdlyeavi
       61 vynldiinse lekiadksst ideyimniie rvrlksdkeq lllnfymlis tnsvqiknle
      121 iiekferkrf syylkfienp kikdrytllf idniitiyiy syfnvfyrkk iflylslyqq
      181 dresiefeed lmkylkllvk kdflklnkii al
//
LOCUS       WP_010775702             315 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: 1-phosphofructokinase family hexose kinase
            [Bacillota].
ACCESSION   WP_010775702
VERSION     WP_010775702.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..315
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34972
     Region          2..309
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 miytitlnpa idhvfhiqde ltrgknnria erymdvggkg thvsvglnil gkennctgit
       61 gennwnelkn llikhqtkss fytvskedvr nnivltddgg kgsfmiteyg fkinkqiida
      121 fftqelnqls skdtvvvagn pslqtpvevf aylldkleek kvqliadvsg kfldevlkra
      181 vflikpnnye fseiigeeil slehcievyq kkksvltnmk cisvsmgekg svlltndeqy
      241 ifnsprvktv ndtgsgdayv sglvygfsek lplkdigila tavgaakaee tlstgfsker
      301 vlelkklvqy rkige
//
LOCUS       WP_010775748             562 aa            linear   BCT 01-JAN-2025
DEFINITION  ribonuclease J [Enterococcus faecalis].
ACCESSION   WP_010775748
VERSION     WP_010775748.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..562
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=62721
     Region          1..552
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mstikivplg gvrengknmy vaevedeifv ldcglqypen ellgidvvip dftyleense
       61 riagvflthg hadaigalpy llskiqvpvf gteltielak lsvnshaetk kfkdfhvidp
      121 hteidfgqat vsffktthti pdsigvsikt kegnivytgd fkfdqsaiem yqtdygrlae
      181 igkegvlall sdssnaenpv qvaseaqiad evfdtirywe griivacvas nlqrvqqvln
      241 aadrsgrkvv ltgqdferii rtamkleklq lpsedllvkp kemkkyapeq lliletgrmg
      301 epikslqkma nnthgvvrie egdlvyittt pttamettva ktedivyrag atvkqisdnl
      361 rvsghanpnd lqlmlnlmkp kyfipvqgey rqlaahadla heigmpykdi fitgrgdile
      421 ytkgrmsvag sttaenimid gigvggigni vlrdrrilse dgifvavvti nrrekrivsp
      481 akitsrgfvy vktskdlmke ssnivteive khlesddfew sklkqeiren lsrylfeqtk
      541 rrpvilpvim eatqrkrpkn na
//
LOCUS       WP_010776140             104 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Enterococcus].
ACCESSION   WP_010776140
VERSION     WP_010776140.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..104
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11523
     Region          10..100
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mlfqlfkktp sistkelqsr lskeitlldv rtpseyragh ipqainvpln kipaynkpan
       61 evyvicqsgm rsknaakila rknyhvinvr ggmsqwsgqi kggk
//
LOCUS       WP_010776138             402 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010776138
VERSION     WP_010776138.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..402
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43861
     Region          6..402
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkrsiiwkta frsilknkrr slltmlgivi giasvitiva igngfkedmv dklsaekqke
       61 nvkkisfsay ntsdmfsdqa mftdndlgvv rmvpgvekid fdqrevdgaq kgtlnfqagp
      121 knlsvtyela nkttkellag rqlndgdnak ldktvvvdel vakelyqdpt aavnrtfpyk
      181 dqlftivgvt tntngaigpg nddsllyfpk ktyehyfgkl kdtstlkltv apgyqpdqvl
      241 ketiktlsqq gtmknsgtyq eynvkdtike mgsllnnltl fisaiaaisl viagvgvmnm
      301 myisvserik eigirralgg tasdikkqfl tegialtlig gitgyllgmi iaylasmalp
      361 fsvrpdlmtv slaigisvfi gvvfsyfpas aaskkdlidi mk
//
LOCUS       WP_010776141             419 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus faecalis].
ACCESSION   WP_010776141
VERSION     WP_010776141.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45383
     Region          5..412
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtdktkssla ywkkivillc mgwvtiwiyr salspvypqi raslngnasd talgsissfy
       61 flgyvvmqip agflvdkigk krvlipgfil falaalliaq aqtigtiylg sllaglgcgs
      121 fygsayslts qnipqakksf ataivnsgsa vgsclgmils sylvaqkglp wqvmmyisaf
      181 miicmlvafq viirnhkedm aliqptvvde kdngavkekv pfkklfaphm lfayilyfgt
      241 cyayymivtw lpnflsterg fqgaaiglss slvafasipg alffsrladk ymhkkvqfiv
      301 vleflataml lltvqvsnat lllialimyg flgklavepi iiswlgenap kigigttlgv
      361 fnffgmmssv iapaltgkis dttgskvmgf yiavvillig tilfmlvnlk krgadssnk
//
LOCUS       WP_010776158             154 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Enterococcus faecalis].
ACCESSION   WP_010776158
VERSION     WP_010776158.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..154
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=18145
     Region          4..154
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkkeanfdev lfslgqgviq vlihrgasle daqdavsqty ttifsilpei tsenlrpwff
       61 rvtfnyyitm yrkkkrertf vanshpvqsi ekmegqelll lidslkdeeq ellllkyyyq
      121 lsyaeialil elsvenvrkk lyrtrqklkk elee
//
LOCUS       WP_010776231             659 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Enterococcus].
ACCESSION   WP_010776231
VERSION     WP_010776231.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..659
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76142
     Region          <459..648
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdkrkkvgig lkwlvtisyi viysafmeke msflsllcsi yiiflgsfvy iklpqklysl
       61 sffsltfylg wtvllvysdi wvlklvglfl lcchpltlyl flysfihidd kkklnknril
      121 lccvslysyl allldfyvgp tlillmissi tvnsltiike kkfffsalky kvlitsllls
      181 fvllilfyfi cllfpelsfy dwdkttilvt ilptgvvyil vkereiilse kfllvfcilv
      241 ysaffflile vigivlwksf iltilfalvc ylthlsinai rsnkvkqlkn nfrnlnnekl
      301 evldqvtysq flnnvselll dkleeltasq rlavfveske gcyllcqkge tvfnslkkei
      361 hslkkqkqki kfrkkeynci piiisgytvw iffenndndi dlksihktve qhgtliitvr
      421 llhlnsksyv kdpievcqll riklfnsmei ekknyanylh dnilqsvigl htlisnlsgd
      481 vmvmdlinee fsklvssirs eifntypstl yhltfkenlq iliddfnkky pktefildys
      541 ieeiipqhvi aplyrivkel nenigkhada eigkvtveid naeiqlived dgvgvgnile
      601 feksliqtnd higllsiknd inwlngsfkm lslpgpnsgt kvwvtipcmk geqyenits
//
LOCUS       WP_010776286            1196 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Enterococcus faecalis].
ACCESSION   WP_010776286
VERSION     WP_010776286.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..1196
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=138856
     Region          4..1173
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 msvqfirgta vadleapliq atkqwleeda qhevfylvpn hikfeqeiqv lqklrqlqtt
       61 tsdsitstrl qvfsfyrlaw yylqhtpfys advlsdagaa mifrkilvea eeelqifrgk
      121 inkpgfiqql fqlyqemreg nieiaelypf lekqtenpkg qdlqlkfqdl tliftrfqlq
      181 msqygyesae iiqhlseylq tvdlsnvqfv isgyqqftar elklievlma qagsvkvall
      241 ldkqyphdlp dprslfyeag qtyhqlyqla rqkqipilsd yvekkevlit npdlqglndy
      301 wiqsqehlpp lsaadwrgdg lflwraenvk eelthvatei rrlvveegyr ykeiqvltrd
      361 ldcyenllep ifaeheipvy vdrdmamdrh plvewieslf aihsynyryr dvlrflrtel
      421 fmpmnqlats eesltdwlnq rnawrrkvdi tenvvlaygy egyywsqekd wefirydfea
      481 eeqedvatme eesnairqsl qrllpsyfqa misaktglea atvfyhfllq sgvatqlkmw
      541 rlqaieagql etarnheqtw dalmslldey vtvygessfd fttfqeifvs gleglhyskv
      601 ptaidqvqvr amdltrpgaa kvtfaigmte eifpqkienk tllsdeerqt indtltenqy
      661 lrgttgrkia qepyvaylvf ssarerlylt ypsvkdtaqe vkpspyfkni qkdlnlpvfe
      721 knettifdde ttslahisty rtligeltrl krqrketqeg llpfwlnmek almnqsiapl
      781 akqvfeslth qnipekidev laeplygkdi ytsvsrmesf yrcqyqyfsr yglrlkerdv
      841 fglspaatge ffhealdqff kllimnqrnl seltdqevnl laeevlnsil gdarfsvltt
      901 ssrmnyiryq lsqtikkvsw alkrqsqrsg mttvqtevlf gqiaakkgis glelplknqg
      961 kihvrgkidr idqlvtpest ylgvidykss hrkfnmteay yglamqmlty ldvalmdavq
     1021 lvgqeakpag slylhvhnpt lsyegkddie qqmlkkyqfd gllmkdpdll dhldtslqak
     1081 qssllfpiee sakeqikpgr rqedkfvtep elgallshnr nkfieagnqi iggevqlnpa
     1141 yqgkeriacr ycpfrsvcdf dvmlkennyh rienlskeei marllnkdee gatede
//
LOCUS       WP_010776295             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endonuclease/exonuclease/phosphatase family protein
            [Enterococcus].
ACCESSION   WP_010776295
VERSION     WP_010776295.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..254
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29165
     Region          2..249
                     /region_name="EEP-1"
                     /note="Exonuclease-Endonuclease-Phosphatase domain;
                     uncharacterized family 1; cd09083"
                     /db_xref="CDD:197317"
     Site            order(7,43,132,166,168,215,241..242)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197317"
     Site            order(43,241)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197317"
     Site            order(132,168,242)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197317"
ORIGIN      
        1 mkiatynvrv dteydqdwqw sfrkeavcql infhdwslcc iqevrpnqvr dlkayttftc
       61 lsaeregdgq geglailyne qkiqaidtgy fwlsetpqqp sihpeagcpr ialwglfket
      121 tqntpflvin vhldhisaha rlagmtvile elhdkiaeyp tllmgdfnae sgeevhqlvq
      181 kkfqdsknla thygprgtfq nftytkpwae leeidyiyvk gwqvqqtasl tdsidgrfps
      241 dhfpleaevc ieer
//
LOCUS       WP_010776396             119 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010776396
VERSION     WP_010776396.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..119
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=13716
     Region          4..>90
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mssrqiqvtn selevlkfiw ksepvpsgsi themklcnnw hpstsktlik rllnkqticy
       61 stvnrrryys aiiseqefll feiqrimsgm nseciaeiss ylaeldnsnk mevihdnkt
//
LOCUS       WP_010776564             325 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus faecium].
ACCESSION   WP_010776564
VERSION     WP_010776564.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..325
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=38948
     Region          17..318
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mqnfrleell eemlfneksr gisqktikkh qkflklffef lkkeqiyfie dvtpksirqf
       61 mlmkleegca etyvnshlrs irayfkycvd edyirydrnp cmrvkwvker kviiqtfndm
      121 eikemlkvak kltffkpqkm dkqhtgyqtk ftnqrdylll lilidtglri sevmnlkdvh
      181 itnkelfven gkgkkdrivh cspliykeyi kykrvansff eyneienidn yvfltregkq
      241 ynyilaerai ikignqceir ksirvsphsf rhyfaqklvr ngtdiyriqk llghasiktt
      301 evylrslnie deiskavnfs plqtl
//
LOCUS       WP_010776599            1104 aa            linear   BCT 01-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Enterococcus faecium].
ACCESSION   WP_010776599
VERSION     WP_010776599.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Burnim,A.A., Dufault-Thompson,K. and Jiang,X.
  TITLE     The three-sided right-handed beta-helix is a versatile fold for
            glycan interactions
  JOURNAL   Glycobiology 34 (7) (2024)
   PUBMED   38767844
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12131601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..1104
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=121596
     Region          491..>662
                     /region_name="NosD"
                     /note="Nitrous oxide reductase accessory protein NosD,
                     contains tandem CASH domains [Inorganic ion transport and
                     metabolism]; COG3420"
                     /db_xref="CDD:442646"
     Region          600..766
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
ORIGIN      
        1 mlkkrikysa lmmnllmlst pvlisvveva aneqqsvnee nahvniegms tmeevprtse
       61 dmdteegndp mmkesenekt kkqseeanee wkgvvfgest sasryaiepl edgvrlsstn
      121 nggkfqssgs dgmtyyyqai pkdinfrmra tieieswtyt naqegfalmv rdavpkdhlf
      181 gqafysnsfa ilgsrieyvw dsdrqevvnt sgskytmrlg lgtraitgis sedpqaapap
      241 gsvsvettpl etsagfleke tgsynifgng hgnlfpatns itkldvemkk tntgleayyy
      301 dpetgeemas dimydwekly asdesviyag faaarnmtik vegievaysd patdppgqer
      361 ptrlidpiyt vtssnhsgnq dhtmsfrana dglltiknqa tgevlenakd lvitanrefd
      421 yqtklmegtn eftfsftpdk nyppeeyvem asyetkeilh tvdyrkpnys tvyvtpegsd
      481 tgngsrqnpl sltqalryay agqtivlapg tysferglti pkgvngtren piqliaeknp
      541 enkrpvldfk gtgngmtlfs hywvlrgfdv tnsaamqkgl qisgnhnlie eihayrngnt
      601 giqisgssnd pfeawpahnl vknctsfena dpgfedadgf aakltigegn vfdgciayhn
      661 addgwdlfak netgsigkvv iknsvayrng wvpgvegegn gngfkmggss lsgphelins
      721 lsfenlakgi dsnsgtdiiv nsstsfnngs ynvalytssa gntdfhasgi lsfrtenlem
      781 reqirplnqn edqiyhslny ywnerekqse ntlghtvskd wieslnthsq egqqpvtrya
      841 ngsihvhglm qikpenrqte kgrvdglpls vgatfdrets psseypeyai vqepnqtkpn
      901 eqnnpiiiqe angvaenaeg niielkpftv fvstftpnqg tpvfedmryf pekiqivetq
      961 ssaqfsnhta ifsapskgey tlevtyrsei fdgekwsaht esvtqqkait vretadvppg
     1021 ndkperenpg nespngkpng kpngkpngkp ngkpshpdrt akesekngtq glpktgefnn
     1081 pllalaggil ligvvvyvmk qrkk
//
LOCUS       WP_010776676             303 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Bacillota].
ACCESSION   WP_010776676
VERSION     WP_010776676.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..303
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32814
     Region          33..294
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mekgrllqnk nmnkaiqvsk itliinlsls llkfaagyig kssamlsdav hsasdvvsti
       61 vvmvgikise kqpdrehpyg hermecvasi ilsvalaitg agigysgikk ifsgqyntls
      121 vpsgialtaa vlsivikewm ywftrsaakh tnsdalmada whhrsdalss vgsligilga
      181 rlgyaildpi asvvicgcil kaalnifkes inkmvdhscd natetrirev vlqqqgvdgi
      241 delktrmfga kmyvdieila dgnlalydah riaegvhqti ennfpqckhc mvhvntnell
      301 ysa
//
LOCUS       WP_010776680             317 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus faecium].
ACCESSION   WP_010776680
VERSION     WP_010776680.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..317
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36440
     Region          9..184
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(12,14,88)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(41,87..88)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            86..88
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mesrekiavl ipcyneeati stviedfkre lpeadiyvyd nnstdrtyel avqggaivkk
       61 eprqgkgnvi rqmffdidad yylmvdgddt ypaeaahgll eklrsgeadm vigdrlsngt
      121 yfdenkrpfh dfgnnlvknt itylyktkir dvmtgyrgfn qifvksfpim ssgfqietel
      181 tihaldkkfk fveipidyrd rpegseskln tfsdgfkvim miikmckdyk pllffgiwti
      241 ffflfglvmg ipvireymlt sfitripsai lstglmtlal lslvtglild tvvtnakkey
      301 elnlyhvyhe yqnkemk
//
LOCUS       WP_010776724             315 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Enterococcus].
ACCESSION   WP_010776724
VERSION     WP_010776724.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..315
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35475
     Region          5..185
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(8,10,92)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(39,91..92)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            90..92
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mkvsivvpcf neektvplff devekfkgvh efeylfiddg skdgtlaaik klasaypyvr
       61 fvsfsrnfgk eaalyaglqa stgdlvtvmd vdlqdppell peminritts didcvgtrrs
      121 tregepairs ffakkfyqli nkisdtemvd gardfrlmtr qmvdavlelt eynrfskglf
      181 swvgfkteyi syenrervag etswsfwklf nysidgivnf sdapltiasf igalscvgsg
      241 iailfiilra llfgdptsgw psmvsiflfi ggiqllclgi igkyigkifl etkqrpvyii
      301 retekvkpne lkphq
//
LOCUS       WP_010776749             146 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleoside 2-deoxyribosyltransferase [Enterococcus faecium].
ACCESSION   WP_010776749
VERSION     WP_010776749.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..146
                     /product="nucleoside 2-deoxyribosyltransferase"
                     /calculated_mol_wt=16797
     Region          6..141
                     /region_name="RCL"
                     /note="Nucleoside 2-deoxyribosyltransferase [Nucleotide
                     transport and metabolism]; COG3613"
                     /db_xref="CDD:442831"
ORIGIN      
        1 msqiylagpf fseeqidrvs riekaleenk tvtsfysprh hqesnyelfs agwaqevyek
       61 dmeeltnaef vvaildfehq tidpgtayel gvatmlkkpm iivqeetvpt nlmitqslht
      121 ylksdqaire ydfetlpvet yvgeyl
//
LOCUS       WP_010776847             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Bacillati].
ACCESSION   WP_010776847
VERSION     WP_010776847.1
KEYWORDS    RefSeq.
SOURCE      Bacillati
  ORGANISM  Bacillati
            Bacteria.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Bacillati"
                     /db_xref="taxon:1783272"
     Protein         1..201
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23742
     Region          3..139
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,67..68,71)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(66,120..121,123..124,128)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(72,77..78,116,119..120,123..124,127,130)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(97..99,116..117,120..121,124,128,131,135)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(97,121,124,128,131,135)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(129,135..136)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 makyayirvs skdqniarqv eamqevgltk kqmyidkqsg kdfirknyqr lirklkagde
       61 lyiksidrlg rdydeileqw ryltrvkdid mivldfplld trnqvngvtg kfiadlvlqi
      121 lsyvaqiere ntkqrqaegi riakekgvqf grpkhdfpeq feeiyqlwvi geismreggr
      181 rlnthhttfa rwivryqqqk a
//
LOCUS       WP_010776951             147 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010776951
VERSION     WP_010776951.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..147
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=17166
     Region          46..141
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mqiledikiy wkriigytlv llvvnlflsm ialvfvnqrk dnvtelvtfi sffisgifap
       61 ffeetlmrgi iqnqlelktn lstrsiyiiv ailfslfhln lyfipyfmts lilsfvydns
      121 dkrlivpvti hcfynlivil lsivfyt
//
LOCUS       WP_010777023             428 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Enterococcus faecium].
ACCESSION   WP_010777023
VERSION     WP_010777023.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..428
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44625
     Region          124..414
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mdrknvtpkm kknknnslwr klglglvggi vgglltagif yaamgtgnns sttsgnqnsa
       61 getvvenvkv nvdsditkav dkvqdavvsv inlqsqnqss gfgglfgqqe essssddsnl
      121 gaysegsgvi ykkdgntayv vtnnhvvdgq qglevlmkdg tkvkaelvgt daysdlavlk
      181 insdkvetva sfgdssalkv gepaiaigsp lgseyansvt sgiisslnrq vtstnesnet
      241 vninaiqtda ainpgnsggp lvniegqvig insskiasts estsnvsveg mgfaipsndv
      301 vniinqlekd gkvtrpalgi tmvdlsavst qqqeqilkip ssvtngvivt nvqtatpaek
      361 aglkqydvit kiddkevssg velqsalykk kvgdsvkity yegskekttt veltidqsal
      421 kqnqnsen
//
LOCUS       WP_010777053             245 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Enterococcus faecium].
ACCESSION   WP_010777053
VERSION     WP_010777053.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..245
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26697
     Region          1..242
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mndlsekviv imgassgige attkllaekg aklviaarre drlkaikesl peaelyiqta
       61 dvrdfaqvqa vidlamekfg ridvlynnag imptaplveg hrdewqnmld inimgvlngi
      121 savlpimekq ksghimstds vaghvvypds avycgtkfav raimeglrqe qrqnniksti
      181 ispgavqtel yqtisdkkaa lelheaqkew gltsediasa vafaietpdr msvsnmiirp
      241 ttqev
//
LOCUS       WP_010777072             246 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Enterococcus faecium].
ACCESSION   WP_010777072
VERSION     WP_010777072.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..246
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27448
     Region          2..177
                     /region_name="RNaseZ_short-form-like_MBL-fold"
                     /note="uncharacterized bacterial subgroup of Ribonuclease
                     Z, short form; MBL-fold metallo-hydrolase domain; cd07716"
                     /db_xref="CDD:293802"
     Site            order(34,58..59,61,63..64,133..134,156,176)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293802"
     Region          <130..230
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cl23716"
                     /db_xref="CDD:451500"
ORIGIN      
        1 mkltvlgclg aypyknqgtt gyllqsdgfn llidagsatl iklqehldpl dldavilshy
       61 hhdhiadlgv lqyywqlhpk rnpetllsiy ghtkdsihfe eltmenvskg hpyfeaeelk
      121 igpflitfme tihpvvcyam riveettgkv fvftgdsgyl esfadfakda dlfladtylf
      181 egnehhhahf tskeagelak sanvkklvlt hlpqfgdleq lkneaqkaag kgidvelavv
      241 dkvfni
//
LOCUS       WP_010777075             425 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus faecium].
ACCESSION   WP_010777075
VERSION     WP_010777075.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..425
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47934
     Region          8..425
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnefvqvfpe nwqkkyedkg fispsliqra vfqplsnkqs ivavsptgsg ktlaylwpll
       61 lnvepgeasa lvifassqel aiqvadvare wgkdkelkvq slvgganvkr qieglkkkpe
      121 iligtpgril elmkakkika hqvktmvfde adqlfdtgns qiidqilhqa pteyqlaffs
      181 atadrslesi ekitgktfet idvtaeddsr kglrhyflrv pirkkddylr rlthiedfhg
      241 liffnqltel gvmeekllyr gvpvgslasd qnkllrkaal eqfkkkmvra llttdvaarg
      301 lditglpyvv naevplseea ylhrsgrtgr mgnegivitl vqdnnlrdlk rllrpsnitl
      361 eeiflyggkl qteqptkeda apavnkkyak tfsgkeqnpe ynkekirkkv knkskkernk
      421 garrk
//
LOCUS       WP_010777413             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_010777413
VERSION     WP_010777413.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..143
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16177
     Region          11..143
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mhvaqtkdtm sdlyldavrl rqrvfvaeqg vpeemeidey eahcihfvly tnhvavatcr
       61 llplengvmk lqrmavekay rgadygrvim eaaenfakeq gyhkitlgaq vtavgfyerl
      121 gyqktgapfm dagiehyemn kdl
//
LOCUS       WP_010777300             105 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein, partial [Enterococcus faecium].
ACCESSION   WP_010777300
VERSION     WP_010777300.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..>105
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          3..>92
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,63..64,67)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 makigyarvs skeqnldrql qalqgvskvf sdklsgqsve rpqlqamlny iregdivivt
       61 eldrlgrnnk eltelmnqiq ikgatlevln lpsmngiede nlrrl
//
LOCUS       WP_010777442             457 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
            ligase [Enterococcus].
ACCESSION   WP_010777442
VERSION     WP_010777442.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..457
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50144
     Region          1..457
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mkltfwevaq aveasndwqq wpdfpltgie fdsrkivkgn lfvplqgend ghrfiesama
       61 ngcqaafwgq dlvdapqqlp vlhvtdplva mqklatyyln kmqpnviavt gsngktttkd
      121 liaavlsekf vtyktqgnyn nqiglpytil hmpdetekli lemgmdhaqe isflsnlaqp
      181 evaaitmige ahvenlgsra giaqakmeiv dglakdgslf vpsdepllep lvekvtqqvi
      241 tfgfsqesql qgivtneake qtsfkisdtq mtftipvpgt ynvtnaliai gigryfqltd
      301 seiqkglata eltknrtewl kaangaeils dvynanptam glvldsfskm skvgkriavl
      361 gdmlelgpds aamhqemaqh lapdaieevf lygsemayla dklqetyapt nihsfkkeek
      421 nelieavkkv lqpedmvvlk gsngmglrev idallek
//
LOCUS       WP_010777472             240 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010777472
VERSION     WP_010777472.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..240
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27063
     Region          3..222
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mniiadqitk nygeiialqs vsfdfpknsi vgvvghngsg kttlleilcg lrkedagrmn
       61 vkinkeyksk lgvilqnnaf yddakviell klfssfyket vdidelidit qireyshkfy
      121 kdlsggmkqk vnialallnn peimildept tgldpiarke lwgivhrfak nnivflsshy
      181 mdevesncth llflkkgkvv ecgklsdils kydtnmnefy leknkgginy dskystttks
//
LOCUS       WP_010777473             272 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010777473
VERSION     WP_010777473.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..272
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30693
     Region          51..248
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 miasilqqlk vefkiylrqp fyllfslvmp vasflffgsl yssqdygaad ffsmyipgfc
       61 mlvlfstsvf nvgnqvisdk ekgiynrilt tpislmrfig vilskafmla flgfvlilfv
      121 ahfsfsipig lerlgfvamy tvfilyslsl gvsiaflvnk lntysitmma affpmfmlsd
      181 asiplmslpk waqsvaefnp lyhsnlvlrt fwdssmqemy ganiwksylv lglilsilya
      241 lvvykwkkgk islkqksenk gslpladtse ii
//
LOCUS       WP_010777488             434 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus faecalis].
ACCESSION   WP_010777488
VERSION     WP_010777488.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 434)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..434
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49251
     Region          6..405
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mgealfvlvs mqfmtsyist gliigktnks ffriamvlfl svigalsyqf tgvygalfil
       61 cfnfllyyid ikklipvlgg lgiamisnll fdhvasvlds lfeipsrfpp iiyilihqgv
      121 vivssiitcm lvrklllrfl pqglkskegh visllsffty ivylvciflg vglgntieli
      181 qlnllffaiy igfvlfsfsf ysrslkkeyq vkekevehqa lhrytaeiea qyiqmrkfrh
      241 dyqnilasld syikeedlsg lteyyqatlq hssknisdnn fklddlskie vkavksllal
      301 kliyaqekkl dasfeaselv teiwldplil vrvlgifldn aieeleilgy gslrtaviky
      361 pnsiqiiien tcrkkvghsr qlrqegystk gqdrgmglsn vdellsgvrn vtletvvene
      421 rftqilyite vgfk
//
LOCUS       WP_010777567             201 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Enterococcus
            faecalis].
ACCESSION   WP_010777567
VERSION     WP_010777567.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 201)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..>201
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          2..199
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mqleniskti dkkeiltnis itvepgeivg ligpngagkt ttmkimsgli vnfqgkvvgq
       61 erigvlidgp kyfpnrtare nlnyfralsk esysvdyves lfdmknygkk kvkdfslgmk
      121 qrlgmalali nknellilde pmngldpdgv qatiqtlkhl akelhigivi sshilgdldk
      181 lcdrayfikn gaiiqtvtlg k
//
LOCUS       WP_010777573             346 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010777573
VERSION     WP_010777573.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..346
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38747
     Region          1..346
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtfvdlkdir vsydgkqdil kdlnismekg elvsllgpsg cgktttlrvi aglikpndgq
       61 ffvdqeeltk vpvykrnfgm vfqsyalfph ltiaenvafg lklrkenkqt mdqkvtemlk
      121 vcgleslgdr ypkqlsggqr qrvalarali iepkllllde plsnldaklr vamrieikri
      181 qqqlgittvf vthdqeecfs isdkvaimnn gvieqydspe tiyrlprtkf vaefigfenf
      241 fsvekmeagh yrtqtnqivk ttnpepnvtt tvatirpedi eivseaatnt vagtvavrtf
      301 lgksyqyeve talgtllvng tseqlyetne tihlafpaek lvilek
//
LOCUS       WP_010777599             401 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YdcF family protein [Enterococcus].
ACCESSION   WP_010777599
VERSION     WP_010777599.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..401
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45695
     Region          219..369
                     /region_name="DUF218"
                     /note="DUF218 domain; pfam02698"
                     /db_xref="CDD:460654"
ORIGIN      
        1 mqfygdltfl gvyllglffi pswrkkkkeh dwlpwmfgwt vfmffsyvly leiirgtaff
       61 lipiaffglf alfyfkekrr llngtlfnif lvvlatylgi tairtnnyfl itlaiialla
      121 ifialalgly aliiflywna vvvmrkegrs lgnlltllla igltllliyn fffqsllptw
      181 lslpltiapf iltyfafvfy nfltvstlyq fnqpkytqdy ivvlgsglin geivppllqa
      241 rinkaiqfyk aqnratlnpp kivmsggqgp dellpesvam kmyaltqgip dddilveahs
      301 kntlenmrfs ketmiedfgn anfqaifttn nyhlfraglf armaglkadg igaktafyfl
      361 pnafirefia ivvmykrrhi ivcglaaigm vmlfliglii q
//
LOCUS       WP_010777665             184 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [Enterococcus].
ACCESSION   WP_010777665
VERSION     WP_010777665.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..184
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20085
     Region          3..162
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtkkigifvg slrkdsfnkl vaktmadlfp adfepifini gdlelynqdl ddegtpteaw
       61 ttfreevkqv dgvmfvtpey nrsvpavlkn aldvgsrpyg esvwdkkpgl vvsvspgais
      121 gfganhhlrq slvflnvptl qqpeayiggi tnligedgki idgtvgflqs ivdayvdffn
      181 rlta
//
LOCUS       WP_010777871             648 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Enterococcus].
ACCESSION   WP_010777871
VERSION     WP_010777871.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..648
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73804
     Region          6..534
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          571..643
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 millqanqva rhfgsetlfe nihleiatks rialvgrnga gkstflkiia gidapdsgti
       61 aknktatlgy laqntglesd ktvweemtka fadilemeqr mreletkise mepitsvyeg
      121 ilkeydqlqh tfsekngygy eneirsvlhg fgfdesfykk diqtlsggqk trlalarmll
      181 qkpdililde ptnhldietl swlesylpsy agallivshd ryfldkvvne vyelsrkkmt
      241 hykgnyskyl elkaeqlase wkayekqqee inkledfvak nlvrasttkr aqsrrkvlek
      301 mdrldrpqgd eksahflfds ekvsgnvvlq vedaaigydq ehilsepihl dirrkeaial
      361 vgpngigkst llksiidrip fikgsktfgt nvsvgyydqe qanlhgnktv laelwdehpt
      421 tpekeirsil ggflfsgddv ektipllsgg ekarvalakl amdrdnflil deptnhldid
      481 nkevlenali dyegtilfvs hdryfinria tkvvelsekg sklylgdydy ylekkqeeee
      541 iaallaneea akkpepvtak ntfyqnkeqq kllrtlqrki tqveenlaql dttiaqleaq
      601 msqpdilenh vellalnqql ddarqqqdel leqwenfsle leemennn
//
LOCUS       WP_010777992             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Enterococcus].
ACCESSION   WP_010777992
VERSION     WP_010777992.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..161
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18047
     Region          1..142
                     /region_name="CFF1"
                     /note="Predicted sugar epimerase, cupin superfamily
                     [General function prediction only]; COG3542"
                     /db_xref="CDD:442763"
ORIGIN      
        1 mteqmwiekl gleahpeggy fkqtnkseql iptkrgeral htailfllnt espshfhrlk
       61 adelwffhdg qpltvhcifp dgtyqavqlg kdlvqgqqls fsvpagtifg stvaagfalv
      121 scvvtpgfef edfelftqae llndypqhse iiqhlayrel p
//
LOCUS       WP_010778085             142 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ImmA/IrrE family metallo-endopeptidase
            [Enterococcus].
ACCESSION   WP_010778085
VERSION     WP_010778085.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..142
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=16351
     Region          54..141
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 memdvislvg klkqkynsan pfticekmdi qiryvpflnn pkgqfqellg rsvillnhel
       61 kyseerfyic ahelghaifh qglssyyvst rssrsksese ancfaanliv slykednaqy
      121 prkieeltnl yglpesvyrf li
//
LOCUS       WP_010778140             364 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide pyruvyl transferase family protein
            [Enterococcus].
ACCESSION   WP_010778140
VERSION     WP_010778140.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10514996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..364
                     /product="polysaccharide pyruvyl transferase family
                     protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42876
     Region          14..302
                     /region_name="PS_pyruv_trans"
                     /note="Polysaccharide pyruvyl transferase; pfam04230"
                     /db_xref="CDD:427804"
ORIGIN      
        1 mkkigiltfh raenygavlq tyalqeyisk mssnyevevi dyrspfieky ykllsfkaft
       61 nikslkrivy vllyngtlks krkifdnfid kfirvslsey ddktirgldd kydlficgsd
      121 qiwspysagf dpiyfldfvk krnkknayaa sfgveivpee tikeysrrlk nfnvisvree
      181 igkkiiknli eedvpvsldp tlllsktewd liiekkrkis ekylliylit etreiielak
      241 kvarekklkl vyindniykt kgiynynncs psdwlnlfyn adyivtnsfh giafsinfek
      301 efsvqylpep akvnsrinni ldnyslkwri nydgnekiny skvnkilved rvasqqilkd
      361 imey
//
LOCUS       WP_010778241             115 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Enterococcus
            faecium].
ACCESSION   WP_010778241
VERSION     WP_010778241.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..115
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=13341
     Region          8..111
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mseeriyipk kgdivwidfd psvgkeiqkr rpglvvsrye fnrktmfsvi cpitstiknl
       61 ptryslpeel dikgqviisq lksldfkerk lkkienlplq dmakidqiiq ydlsn
//
LOCUS       WP_010778279             376 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerate kinase [Enterococcus faecium].
ACCESSION   WP_010778279
VERSION     WP_010778279.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..376
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39506
     Region          2..367
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mriliapdsf kesltaveaa qaiqsgfqev fvqaeydllp igdggegtvs sladslrlkr
       61 qtavvtnsfg knkeiqyasd gqtaifemae ivglkdvpln qrqplrlstr gvgelirqll
      121 qqgvrhiiig vggsstndgg igmaeglgya fydqdnqkve algenlgkia tvdktnvpie
      181 likakitvit ditnllcgke gasfvfgpqk glkenelava dqamhdfymr fapqvieasg
      241 sgagggmgag llafasgkiv sgidyvldll efdkrvqqad lvivgegrld gqslkgkapv
      301 giarrvpegv pviaicgsvg kgsekaadvg isavfpilpa avplqealqq atdnlhrtak
      361 niasllqvvh fqggnr
//
LOCUS       WP_010778520              71 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010778520
VERSION     WP_010778520.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..71
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7836
     Region          10..70
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 meiandahlk mrsirkekgv tqayiakrlg fsssqayani eygntnlkld vavrvadiln
       61 vsiydflsek s
//
LOCUS       WP_010778547             380 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Enterococcus gilvus].
ACCESSION   WP_010778547
VERSION     WP_010778547.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..380
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=41458
     Region          3..372
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mmkrkkidwl lllpylgvsl igllmvfsas syrlmaegqn plslfskqai fmglswllia
       61 fiyrvksnvl vkgtlakgll aaglvslilv kisgvninga qrwvsvmgiq fqpsevtnva
      121 lilylayyfr vkrtqrellv pcglvllsgl lillqpkvtg aiiiwgvalv iittaelpyq
      181 lsvmvfatif agivliggii lflgshhllp elfahtydri rlvrdpfldp ygkgfqmsns
      241 yyalyngglf grglgnsitk kgylpvaetd fvysilveel gmivgllvla llflialrlf
      301 vlaskevsqq vsliyfgvga lillqtsini asilglipmt gvplpfisyg gtsylilsaa
      361 lgvclkfsse vrvndqtikq
//
LOCUS       WP_010778552             235 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative ABC transporter permease [Enterococcus].
ACCESSION   WP_010778552
VERSION     WP_010778552.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..235
                     /product="putative ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26703
     Region          5..178
                     /region_name="COG4905"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443933"
ORIGIN      
        1 mdhlfmtflv ysvigwlwes fycslkarhy vyrgfllgpy cpvygfgvas vlilvpenag
       61 tllnlyfniv vivtiiefit swmlekffgm klwdytkvpl niegrvavpv slfwgvgcli
      121 lmkvinpviq dgiqefidat nhlgpvilaa lfaadvastl iftlttkkev ssvidtsdpe
      181 naavkefrlk hlisnhhsst sreqvlkmik erpknltrrn lnrlaknypn mhfkk
//
LOCUS       WP_010778625             374 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Enterococcus gilvus].
ACCESSION   WP_010778625
VERSION     WP_010778625.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..374
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=42004
     Region          58..301
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mkrsqkivll cltallmcai svsayslfvn qhlrntldng yhpikneyqt ttkkdtesfl
       61 vmgldntier klgttrtdam mvitvnhktk kitfcslprd sfvpisskny qgnqrieaay
      121 tingptasvn tvenllkipi dhycvfnfls fiqfidaidg idinvqhafd gvtkdgpgai
      181 hfdagkqhvd gtkalsyare rhsdndimrg frqqeiiqav gkkltsktav knltkiidsf
      241 dnniqtdits dqlmdlmksg llynsyekqr vdfdwrtfsn qgrsmvelyp dsieyvshel
      301 rvslgidkkd ardkktnpfh tngeylyqsd ysvqdadaed kettslngnt yigtagntet
      361 gplptvktkn gfvq
//
LOCUS       WP_010778632             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010778632
VERSION     WP_010778632.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..259
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28841
     Region          1..234
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mentellnvr avskefeieg rkeqlkvlen idltvqtnef lsiigqsgtg kstllrsiag
       61 llqptrgvit fenktltepd anismvfqhf alfpwltvek nisfglesle glsreqislr
      121 vsnliemigl kgfekaypre lsggmkqrvg faralaieps lllldepfsa ldivtasqls
      181 ndlleiwlgn qiatksivmi thdvqqavql sdrvvlmdan pgrvakiypi tiprnqrspk
      241 tilpiveqit kemirrmqa
//
LOCUS       WP_010778640              69 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010778640
VERSION     WP_010778640.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..69
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7585
     Region          8..69
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mseeklvlkn rlkearknkk lsqaalaklv gvsrttissi etgqfsptak lalilciald
       61 vkfedlfyf
//
LOCUS       WP_010778637             179 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus gilvus].
ACCESSION   WP_010778637
VERSION     WP_010778637.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..179
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20350
     Region          3..175
                     /region_name="COG3981"
                     /note="Predicted acetyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443180"
ORIGIN      
        1 mekitlvlpq ahhqnavtey ieehfnsgee flhgssrlte mesygewlrh lsnqadqdtv
       61 spdwvasttl lairesdqkl lgtinirhel neflrefggh igygvrpter gkgyateilr
      121 lglahcrmlg lekvmvachk envasartiq rnggvlekef iytdgkmvqi ywidllkek
//
LOCUS       WP_010778678             539 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010778678
VERSION     WP_010778678.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..539
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62875
     Region          6..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          237..532
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtslkeilqt prfselslln qkadlerpld tieifetpdi lyyipknall vttgmafced
       61 pdglctlvks laelpsagla iklgrylphv daqvlaladd lnfpilqipv smplgdishk
      121 llsflwhdqt eqvffaleiq qkfvnlmvhg asfkilikel ssmiqqsvll idpfgkivss
      181 hlqfsnsavl kdrkeaflek irecqlkkqr etllfdfahe kmlisifpln sdrylpymlv
      241 ifepdklpyp fsqfviqqsl tvltlalyke qtllnekrae rrnlltylls rktsseedtd
      301 wlhykrhfpk lnstyyrvif ihsfikkdqh yyvkeidali ydylfqevek ksenillfpt
      361 enlnqmvlvl qkkaeilpil eklhkellgl fdiyaqfgig dpvnnidllh fsykeskqal
      421 eesedrttfv synkiqgikr itenvsnedm ryfcisilkn laypeneqdq emrktlmtyl
      481 dqqceitkta emlfihrntv kyrikkceel lnnnidhpef slqlrvalfl sdpeakdie
//
LOCUS       WP_010778679             417 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus gilvus].
ACCESSION   WP_010778679
VERSION     WP_010778679.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..417
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45167
     Region          7..401
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 meeqtrttra pywkqiifil tagwvviwiy rmvltpiypi isayfggatd sslgnissfy
       61 flgyvsmqip sgllvdrfgk kkilipgfll fglgtlivas asalsavflg svlaglgcgt
      121 yygvaysltt eyvpankksl ataivnsgta igsglglvss sflvgegvlp wqslllmtal
      181 livvmlgvfk kmireekptp apqvqtaakp kgtlkdlfkl pmiasyvlyf stlytyylid
      241 twlpnflete rgfqgtgigi asslvfftai pgalffsria dkiphkktmi iilleilaas
      301 vlfmtittnn qvlliigima ygffgklave piiiswlgqf apkksiatty gvfnffgmsa
      361 svivpsvtgm isdatgtkvy afylaigiiv agtlvfygin kyyqekeaaa evmetty
//
LOCUS       WP_010778683             411 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Enterococcus].
ACCESSION   WP_010778683
VERSION     WP_010778683.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..411
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44446
     Region          12..404
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 memnnerigm eywkkiivll csgwvsiwiy rsalspvypq inaslggnvs dtalgsissf
       61 yflgyvimqi pagflvdkig kkkvlipgfi ffalaafiis qastismiyi gsfmagigcg
      121 sfygsayslt sqnipaekks fstaivnsgs avgsgigmil ssylvvqlgl pwqvmmyism
      181 alilvmlaaf slvirsnkdd vafnqpkevv eekpkeavsm ktllspamlf tyilyfatcy
      241 ayymtvtwlp nflgtergfq gaaigfsssl vafasipgal ffskladkym dkkirfivil
      301 ellaavmlli tvrsststfl mialimygfl gklavepiii swlgenapqv gigttlgvfn
      361 ffgmmssvia ptltgsisda tgskvmgfyi aivllvvgsi lfllsnlkka k
//
LOCUS       WP_010778702             859 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus gilvus].
ACCESSION   WP_010778702
VERSION     WP_010778702.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..859
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=93010
     Region          14..846
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mqkklietek qqgkgltqqe aaerlerygp ntieqgkkng fwtyllsalk ditiiilvia
       61 tvlsiyvalk nhpdnfsepi vifgivllnl flsirqqkka eksmdelkrf sipktkvyrd
      121 gqltviqste vvpgdrllle lgdrvsadat litsknllid esfltgesep sekeadyqpd
      181 aadtigdlkn svfsgalvvs grgeaiveat glateigkis dllteeqpvq aplqvkmqkl
      241 gkvlggvaig aavlailigl irgysleiai mtaismavaa ipevlpvvvt islsfgirnm
      301 akkntiirtp aavetignvs vicsdktgti tenqmtvkkv vpvlteqtsg akealllhfy
      361 lasnlseeqg shgnpteqai kqaaethfgg eklntllrqy eridelpfds krkkmtvlyk
      421 kgdsylsitk gafdrlpiqe aradfqechd dlaaqayrvl gvavkeyeel ptqitseele
      481 telhflgfig iidparkesy qavqiakkag irpvmitgdh lltakkiaad vgilepgkka
      541 mtgaelgkls egdlaevige yrvfartspe dkirivkalq angetvamtg dgvndapalk
      601 asdvgiamgg gtevakeasd mvllddnfat iveavkegrr vyanirksly amlgcnisal
      661 tivlislimg lgapvtaiql liikvvadgi pgfslsvepa ekdvmrqqtv drnasifdng
      721 llnkiieisi vftavtllti fvghtaafnh elpngeqatt mtflvmgltt ivhmyncrsh
      781 esifkldlag nkllvgttll ggavlilaat lpqtanilgl talqptqwlf vlglsfiplv
      841 yvelkktlnl fdyrvkrra
//
LOCUS       WP_010778723             586 aa            linear   BCT 01-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Enterococcus gilvus].
ACCESSION   WP_010778723
VERSION     WP_010778723.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..586
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=67191
     Region          1..583
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mrasiwkrfi ngekavldel pekiatswgt cyqqgidpyv ykpqkilslq elkgqqrknq
       61 dmirhverei rkvkkklqlk kplfiltdek grilwrdgnh eakdfanlmf fregsrwtei
      121 dvgtnaigla leskstesis leehysiasr dwscaaapif dgedklvgil distyknesa
      181 keylllltai aqkvsnylmr dylegerell hyvtnyseqe ilcntqhrim yappahqqlf
      241 evgkdirayl tsallynenp ilmdqrvigy rymiysstat kpyysegvls rsarynaflk
      301 kalllaessl pihiygesgs gkevvarmih ynsdvqdgpl isvncgavse nlleselfgy
      361 apgaftgana qgyqgkieqa dggslfldei dsmpakmqta llrvledhqv tpisgvakqv
      421 sfrlitasnk klqqqvsqhe fredlfyriy vgqlflpplr erledivpli ekfcqennws
      481 itwqqkieta artfswpgni refnnflqrl yvfyfdqept ldqlnelils gsllnvtnla
      541 eevpeekrei qlalektnyh atntaknlgi sratlyrkmk qyniek
//
LOCUS       WP_010778799             180 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Enterococcus].
ACCESSION   WP_010778799
VERSION     WP_010778799.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..180
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20171
     Region          6..154
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mteartcres rviqthrifp fdlnpfgylf ggklmtlidd aasiaisrhc rrgavtasld
       61 nlnflkplha nhsvcvkcyv sgshnksmev fvkvigedla tgerylaatc fttfvavpsh
      121 mneekqftvp hvvpeteeek mvcggyekrr nhrlkertey qnfaallstd lpwsdegtgd
//
LOCUS       WP_010778741             240 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            gilvus].
ACCESSION   WP_010778741
VERSION     WP_010778741.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..240
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=26584
     Region          140..237
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mkkgcasens lplwkgssgd tggsrhplhh qkeenmtiqk ranaaiglti lvavlflvlp
       61 mtplagamkg igflfnalfa gligffflkd dfiqqfkhfk fktllygipl tiltgvafgl
      121 lfhmiagkpt tnsidssisl vfiltqipfm lmgeelistn lliafekkgl sftvssvlva
      181 llfafwhvta ygfhplqlll tlaplrlvln flwkrsssvw vswichflyd misllpmafk
//
LOCUS       WP_010778884             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ImmA/IrrE family metallo-endopeptidase
            [Enterococcus].
ACCESSION   WP_010778884
VERSION     WP_010778884.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..155
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=17654
     Region          35..135
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mdkaeklmad fqgidytfep ampdglkglc iddqvylnpr qspeeltetv aeeiahylts
       61 vgditsqdtn ekrkqeqkar dvgatlvvtp qdiidchkeh fsavwecady lgitkrafeh
      121 avrvyarmye eglsyknyri lfradgtigv feffe
//
LOCUS       WP_010778817             345 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Enterococcus gilvus].
ACCESSION   WP_010778817
VERSION     WP_010778817.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..345
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39078
     Region          204..329
                     /region_name="FUSC_2"
                     /note="Fusaric acid resistance protein-like; pfam13515"
                     /db_xref="CDD:433273"
ORIGIN      
        1 mshfqslflf nkskdtffrp lgsglsiaip illsfflkdi qvaslgvmgs faylsfqrrs
       61 vlynvqaicv hgillflsfs lglyaasisw aipliisvis ftafiltkmy qipkpsysfi
      121 imlfatgitl pethhvvqts yyllfgivga iisgllvcfi erlplktsvn pherlsfkdk
      181 yyvtiyefpd lfikainfst ilfltayisy llrdysgqwi lisassvlag eytqkikers
      241 lhriigtilg lmvgfllial dfpnfvnlil liplnigvey fmsrnyavan vfinpqvlll
      301 vslvsttdky nfvyyrfisl iigvsltivl vlifdyslki frrdy
//
LOCUS       WP_010778897             141 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Enterococcus].
ACCESSION   WP_010778897
VERSION     WP_010778897.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..141
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15233
     Region          5..140
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mkesykrilv avdsseqarr afqeaievtr rndahlyili vsdtnhlgae pyavdqvvkq
       61 ahkaagavve sleelipedi ahttivddgn pkakivayae eekidlilmg atgtgtfsrl
      121 llgsttafvv nnapcnvmvv r
//
LOCUS       WP_010778905             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Enterococcus].
ACCESSION   WP_010778905
VERSION     WP_010778905.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..145
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15515
     Region          5..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mvdeyknilv avdgseqskk afdeainiak rnkgkltlat vidtasfsgt tggnsiplmq
       61 evhekaqkii tdlehhrvae eqevhltsqi iagnpkreiv elaekletdl ivmgatglga
      121 lslifvgstt ayvvnqapcn vmvvk
//
LOCUS       WP_010778908             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pyridoxamine 5'-phosphate oxidase family protein
            [Enterococcus].
ACCESSION   WP_010778908
VERSION     WP_010778908.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..135
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15646
     Region          1..80
                     /region_name="Putative_PNPOx"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam01243"
                     /db_xref="CDD:426149"
ORIGIN      
        1 mdknmeklla sadtftmitm dnrgfphaia ispplerngf yyfkfyingd grtaenirqn
       61 rigslfcfnk ekhesialkg ylfveelvey kklaaqlnef qkeldyehpv iavfetlsvk
      121 hyenmhgefl dvpek
//
LOCUS       WP_010778915             205 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus gilvus].
ACCESSION   WP_010778915
VERSION     WP_010778915.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 205)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..205
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21881
     Region          1..203
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mldnlmqyls enssyliaqf gihvyisvig vvltfligfp lgillserpk lsdvvigiin
       61 viqtvpsiam ltvllilmgl gqntvvatvv lysllpivkn tyvglvnvdp myidsakgig
      121 mnryqilymi kiplampvil agirnalvis vgittigsfv gaggvgdvil rgiaitdgap
      181 iiivgavlca fiaimmdwlf dwimk
//
LOCUS       WP_010778916             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010778916
VERSION     WP_010778916.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..238
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27649
     Region          1..235
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mkiqldrmne lertiharll eesrektnlt iteaakfadv spskiskmvk kmgfsgykey
       61 frfltgkelv kqkrlnsefa rikefmenfd easvdylael iqqsgkillf gygptnfcme
      121 yfeyklnftl nknvirvsqp slipdllted slllvfsvag kfanfdplfe eakkhhaksl
      181 lvmeelntdl sldsseiifl tkshqneqlk shektrtill myieevirkl tqedprne
//
LOCUS       WP_010778921             481 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FGGY-family carbohydrate kinase [Enterococcus].
ACCESSION   WP_010778921
VERSION     WP_010778921.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167356
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..481
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=53304
     Region          5..451
                     /region_name="ASKHA_NBD_FGGY_YgcE-like"
                     /note="nucleotide-binding domain (NBD) of Escherichia coli
                     sugar kinase YgcE and similar proteins; cd07779"
                     /db_xref="CDD:466798"
ORIGIN      
        1 mekkyivgid ggsqsakivi fdlegnivge gkeatrpmil gedvlvehpg ddlwdalcsa
       61 snkamdefgv rkenivgigl gfirccrvll kkdgslaqpv iswmdkrtst pyvhenpevq
      121 yvtstsgyit hrltgefkdn ignnfgqwpv dyetwdwskd edvlkqynlp eemlfeavkp
      181 gdqlgtvtke asektglpeg lpvfattsdk avealgagli qdtsavvslg tyicsmmmgk
      241 tmppsdavny wgilssmpgr yiyegygirr gmwtvswfkd llgekisirs nyqgiseeey
      301 lneqasnipa gsdglmtkld wlanpwepfk rgvmigfnah hdyrylyrsi legiaytmkn
      361 nvtnmtdemn hpidevivtg ggsnsdllmq ifadvfnlpv krnvvngsas vgaainaavg
      421 lgiyesyeea vekmvkvkdv ftpkpenvav ykrlneevyq gltdytdevl kktysvlhpe
      481 g
//
LOCUS       WP_010778929             641 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus gilvus].
ACCESSION   WP_010778929
VERSION     WP_010778929.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..641
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74316
     Region          6..639
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mrqekiveyl yakkhaiapk alaaefqise rtlandikwl kdigaaegft ierirsagyq
       61 lnildsgrfr sylsqskqqe rvdnsspqer ikniellllf nedyitmqqi aewldislst
      121 vkadikqveq fceqyelslf skahyglkil gtetrkrrai lylirntiht pvltekykef
      181 nfvfdetdlr qflqeqlqrn qlkisdivfe nivqhirlls frimqnntls heeieepaiv
      241 dgydrlteel vsylettyhl afskeekryl eeqlrgkfav lddvvsnqsl rssiekaldf
      301 vdrqyhtqfr ndqelanall mhvapllqrl ytghqlenpl iediytqyan vfnvamvfin
      361 elnkdldadi skdeigyvai yfaaslekqs nqviedyqki avicstggga ayllkvnler
      421 lfsnaevstf alnerdqids sfdlvistvp lnqavfeipi iytktilsha eitkiekdln
      481 llresqnklf dvhhvilslf dpewfqiqeg gnaylqllen egarleeagw veagfkesvl
      541 rrekmidtiy qhgvagphpm eqaaikevid vvllkkplty rdkqvriifl itikkdhlnl
      601 hkeisrlmik mmddpslelq lakitnfqdf vsymkslmke g
//
LOCUS       WP_010778932             449 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus gilvus].
ACCESSION   WP_010778932
VERSION     WP_010778932.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..449
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=49026
     Region          11..425
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 menpkkqgtf ekvegfirkt lvpiankvds npyltaikkg mvvmtpvlll gsiaaifpsi
       61 pefiktqava nwfenygyif giiskvslgl vglyavlais yflsehykly tvgsmmlsai
      121 aflivamdvd dngnivaayl dskglftaif vaiisvklyq fftkhklvik mpegvpdfvs
      181 ssfelitpta aigvlfivir aitdslsggv llpqvimdvl apaigsldsl wiiyivlvlr
      241 lvfwffgihs avlspilspi avqylsenia aheagqplqh vitngtlsaf anfsgsgvti
      301 glvlamlisk slrykkvgav allpslfgin epvlfgvpii lnpvlmipfi fggalvgmfp
      361 micmklglln yplfdppyvp vfmegfltgf dwraiviqvi qvamsfglyl sffkvlekqe
      421 lerealleae ksssvisddd eqyltdidf
//
LOCUS       WP_010778961             487 aa            linear   BCT 01-JAN-2025
DEFINITION  BCCT family transporter [Enterococcus gilvus].
ACCESSION   WP_010778961
VERSION     WP_010778961.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..487
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53094
     Region          3..482
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mkknivfyvs llitglivli gliapdpfaq amnstkaflv dtfgwfylia mfvfvifsll
       61 iafsrfgkik lgpddsvpey snrswfamlf gagmgiglvf wgvaeplnhf ttfggtekaa
      121 dmamqksflh wgfhpwaays iigmalayfq frkntsglis siflpilgek gvrgpigkli
      181 dicavfatva giatslgqgt lqinsglnyl fdipttrlvq iviivaltiv ytwtavsgid
      241 kgikllsdin lflaiaillg aflvgpkima lniftnsfgg yintivsesf sinpfgdnaw
      301 lgswtifyws wwiawgpfvg tfiariskgr tikefvlgvi iapsmvsfiw fsifgslglh
      361 ldieiinkak evtetalfvv faeyplgmlf siiaicllct ffitsansgi fvlsmfsseg
      421 dlnpgndkki lwgviqamla lvllmtggld alqtcsivaa lpltvimllc avclfkalll
      481 ekpesie
//
LOCUS       WP_010778988             473 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus gilvus].
ACCESSION   WP_010778988
VERSION     WP_010778988.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..473
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51856
     Region          1..418
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 meekkkkfsl msailsvicv vfvaeaaapv aaignsqffw wiflliafll pyglisselg
       61 ttyigdggiy dwvtqafghr wgsrvswyyw inyplwlasl avvcpdlltt itgiefptia
      121 ailielvfiw vivwisfypv adsvwilnga avikmllail igalglytfv tkgaaneftl
      181 ssmlpsfdln slsfisviif nllgfevict faddmenpkk qipqsiiagg lviaaiyifs
      241 afgigvaipt dqistgsglm dsfklltgst ggwfiiamaf lflltlfgnm iswslgvnnt
      301 acyaaengdm pkifakrggk dempigaaim ngivatvvvv iapilpnqdl fwaffslnlv
      361 mflmsyvpvf pafyklrqid pdtprpfrvg gsdgvlkllv alpmimivis liftalplqf
      421 dpetlsqqlp itigaiafti fgeaiiwvkk ikkegviyhg eenrkdntea rrv
//
LOCUS       WP_010779078             127 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF805 domain-containing protein [Enterococcus gilvus].
ACCESSION   WP_010779078
VERSION     WP_010779078.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..127
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=14529
     Region          2..114
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mksllefwtd mfkwqytasr kqywlptivy svlfdslfyr tgialtgfsy ltlenanmfv
       61 lslgvvlfia qlsltirrlh dtnhsgawil mglipivgwl lliymlcqpt neaaganyst
      121 ylnqstr
//
LOCUS       WP_010779124             247 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Enterococcus gilvus].
ACCESSION   WP_010779124
VERSION     WP_010779124.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..247
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26810
     Region          5..244
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mreskvivit gassgigeas akllaahgnr vvlgarresk lreivedirn nagkaiyqet
       61 dvtdnrqvea lvqlavdtfg rvdvlinsag imphsplkdk rikdwdqmid snikgtlygi
      121 gavlpfmnaq ksgqiiniss vaghyahagg avysatkwav raiseflree vaqdesnvrv
      181 tivspgaint nllssvtdpt lkknyetfyd hfgisvdrva ttiqqaidlp ddaawneiii
      241 rptkqvq
//
LOCUS       WP_010779128             192 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Enterococcus gilvus].
ACCESSION   WP_010779128
VERSION     WP_010779128.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..192
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22256
     Region          4..185
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mktiylmrhg etlfnqqkki qgwcdsplte lgkkqaliar dyfvrnkiel dsayastser
       61 acdtlelvtd mpykrvkglk ewyfgdleae heylnpplpy gdfftkfgge gekdfrarva
      121 qtvlelared qgktilmvsh gascrqfmre wehktkidlq grianccilk fafeedqfel
      181 leiinhdfsl iv
//
LOCUS       WP_010779139             136 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Enterococcus gilvus].
ACCESSION   WP_010779139
VERSION     WP_010779139.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..136
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15263
     Region          26..127
                     /region_name="cupin_HNL-like"
                     /note="Granulicella tundricola hydroxynitrile lyase
                     (GtHNL) and related proteins, cupin domain; cd02233"
                     /db_xref="CDD:380361"
     Site            order(35..36,67,69,90,92,94..95,114,116,118)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380361"
ORIGIN      
        1 mvkhkeveng vifpvgekne ayaeffvgqs ylhpliadpt vdvgvanvtf epgcrnnwhi
       61 hhegyqlllv tggegwyqee vkearrlsag dvvithdgvk hwhgaakdsw fehiaitagt
      121 pewlepvsdd wydqlk
//
LOCUS       WP_010779167             193 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Enterococcus gilvus].
ACCESSION   WP_010779167
VERSION     WP_010779167.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..193
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22667
     Region          41..188
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 masevlsreh pivgffkelf aflnpakekq eseketdfyy ldrygdhllr lamsyvhnqs
       61 daedivqetm iqlirkapef eneehekawl yrvtinlskn rlkangrrrf eplpetltee
      121 tpedfgylwe avaqlpeiqr salhffyyeg fstkeiaqll emkestlrsh lhrgrnqleq
      181 llkgeapdet nls
//
LOCUS       WP_010779170             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010779170
VERSION     WP_010779170.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..259
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29920
     Region          1..248
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mtetknfysa anqhltqlne sekrifnyvl knfdeakhhs irqlakkcyv ssatifrftk
       61 klgfegysdf idsllhapqa pqtiphsvkq kdykeeylkn imesirvvdq ermetfnqll
      121 dndpviylmg eeldlqalry vdwlftaqgf hsvllsdqas irhalhhird qdilfvfayn
      181 gdspavieti elvkqasqat vvsftravtn vvqnlcdldf yiftdeiiyd sldmtsrvsm
      241 iaivelilyk rlkksltte
//
LOCUS       WP_010779174             324 aa            linear   BCT 01-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase [Enterococcus gilvus].
ACCESSION   WP_010779174
VERSION     WP_010779174.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..324
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35570
     Region          2..312
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 miltitlnps mdynylvssl ildqvnrven phtsiggkgi nagrviaqsg esvvltgilg
       61 gpvgkmildt lnaenryhle flsvegnsrn aitimhdgnt htelvekgly lskenealff
      121 qhvahllkky kidticisgs vnsddakfhl hlldfirsiv gksfpilmdi sgeqlenvlv
      181 qqsvrptfik pntheleelv grkiqtpeei vvllheplfd nietimisqg gdgaivkhes
      241 tvydvripkv divnttgcgd stvggmafai sngysiedai ryamacgisn slfetngtis
      301 teqvnqffke iklveieell lkns
//
LOCUS       WP_010779247             187 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010779247
VERSION     WP_010779247.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..187
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21600
     Region          3..82
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mydllllgsl itgdktgykl qkivgsalqp mrkvssgvly pslerlekeg lvtstvheeg
       61 rkmklwhita sgvdrfielm kekipsdakr ndrihfklrs ldsvslteql aileefqsfi
      121 ekdldfyqha qkdmtehqar fpenkerfri laeayeldiq laktkltwin kqladrknsa
      181 qqldtyn
//
LOCUS       WP_010779292             471 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cytochrome ubiquinol oxidase subunit I
            [Enterococcus].
ACCESSION   WP_010779292
VERSION     WP_010779292.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..471
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53210
     Region          1..448
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdivtlarfq famttvfhff fvpfsigmvl vvaimetlfv ktknekyrel akfwgnifll
       61 sfavgvvtgi iqefqfgmnw sdysrfvgdi fgaplaveal lafflestfl glwiftwdrv
      121 kplmhvtfiw lvtlasmlsa fwilaansfm qhpvgyalrn graemidfga vignpkvwye
      181 fghviaaait mggmiaagla afqllkrkdq kmreffmksm riglvitlfg svlvlgagda
      241 qmkaliegqp mkfaamegty edtgdpaawt liawdnereh kqvfgvqipy mlsilsynkp
      301 sgsikgmdti nkelvkkygd rnyyppvnvl fwnfrimagf gmlmllvsim glfftrkknp
      361 ilyekrwmlw vmglctfapf lantagwlvt elgrypwtvy glftiedsvs pnvsvtslli
      421 sniiyfllfs glavtmiylv rrelnkgpgl dqmnedtgsv dpfdkgafth e
//
LOCUS       WP_010779355             252 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010779355
VERSION     WP_010779355.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..252
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28034
     Region          2..238
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mieltgitkv ygekkalnql sltiregeif gflghngagk sttikslvsi ieptsgeilf
       61 dgknlkehrl aikkkiayvp dspdmflqlt aneywdlisa ayelkgqekr hqelielfdl
      121 vghedetles fshgmrqkti iigallpdpd iwildeplqg ldpqaafdlk emikrhaekg
      181 ktvifsthvl dtaqqlcddl ailkkgeliy ngsvddllae hpneslesiy lkmagrqang
      241 dlvaeieeda he
//
LOCUS       WP_010779369             304 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidase U32 family protein [Enterococcus gilvus].
ACCESSION   WP_010779369
VERSION     WP_010779369.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..304
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=33959
     Region          1..299
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
ORIGIN      
        1 mieliataes maqaeellaa gvdtlyigee afglrlphsf sreeqralie mahaqgkkvn
       61 vaitgimhpd kmkkipeyla flsevgpdhv vvgdtgviyl lqeydlpyiy daetlvtnar
      121 qinfwqkkga vgailarevp feemqrlsqh vevpvevlvy gatcihqskr pllenyfnyt
      181 nqtevssker glfisepkkt ethysiyedq hgthifadnd lnlikelael nqagyqtwkl
      241 dglftpgadf vaiaktfaha kkaiesdswd eaaataaqqd iqkyhpvgrg mdtgfyhldp
      301 taik
//
LOCUS       WP_010779521             255 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus gilvus].
ACCESSION   WP_010779521
VERSION     WP_010779521.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..255
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27881
     Region          5..255
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
     Region          16..>127
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mikdyvyddk nqltldiyep etieaaiili hgggwfrgdk skeatlaerl vsdgflvvap
       61 syrlapdhif paamddlltv ydwlaasdyq vkgkitalgs saggnlslel alqrgipaas
      121 wsgiidlydw vqqhpevvaa mnqkpdfdkq asgkidqdga ndafykwfvl nyvnqdeall
      181 kqadplsrvs dksgplflan slhelvpltg vyklqsqlae ngvpsevkli tgtvhgegya
      241 diaysstiqf lkdnl
//
LOCUS       WP_010779544             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MIP/aquaporin family protein [Enterococcus].
ACCESSION   WP_010779544
VERSION     WP_010779544.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..243
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25712
     Region          4..242
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mdyslttrla aeflgtallv mlgngavanv dlrgtkgygs dwmliavgyg cgvmipamif
       61 ggisgnhinp aftiglavsg mfpwaevlpy ivvqilgamv gqlvvvasyk pyydqtedkl
      121 hvlgtfstin svgskfngfv neffgsfilf fgalgitkap ffqnnlgtah lalgflvwtl
      181 vasfggptgp glnpardlgp rimhailplk hkgdsqwgys wvpvlapiva siaaialykg
      241 lfm
//
LOCUS       WP_010779556             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus gilvus].
ACCESSION   WP_010779556
VERSION     WP_010779556.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..228
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25395
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mivmekinkf ytadqerihv lkdisltiee hefvavmgps gsgkstlint isfldgdfeg
       61 tyrfegqday rfndeklsgl rnqsvgfvfq sfqlidnntv menvalplly ggmkqkqtks
      121 lvmealrkvg iadkynklpk qlsggqqqrv aiaraivgnp kfivadeptg aldshtseei
      181 mhlfkrlnee ekvtilmvth dpeaaaycqr iitvkdgevl eegvvhad
//
LOCUS       WP_010779557             404 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus gilvus].
ACCESSION   WP_010779557
VERSION     WP_010779557.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..404
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44254
     Region          5..404
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mrisevwkts fkaigknkrr sfltmiglii gvsavitvfs igrafenyas efigldqfdg
       61 svgytfsakd etfhenglsg fteedisqie sipgvqsvny ydnsrngvky adqtfddvgn
      121 dgrwncfkli knkgskvlyg rgiqasdyyn enpvvvidqt aakaiqkeep aslvgqsvki
      181 gghlfevvgi medrnggtiv stqedyvvae lpenvfesyf nsedhsmiqv emnqsanikd
      241 vskeaentlk kygtwkelgn yktedlagqv dqlrmlltsi tllisviggi slfisgigvm
      301 nmiyisvser tkeigvrram ggtkgnimmq fllegisltl vggtigylia mllgfaislf
      361 tplsvrpdlf tvtlafglsv vigivfswlp aksaakkdiv sllr
//
LOCUS       WP_010779634             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphatase PAP2 family protein [Enterococcus].
ACCESSION   WP_010779634
VERSION     WP_010779634.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..219
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=25043
     Region          25..204
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(105,112,129..131,174,180,184)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mknkpiyqli gsftllffaa lcyivrfype tlsgfdrgii hgvhqlypqm ngyflwvtkf
       61 anpitiills fvfvglfyfn kqkitalwla lsmvlisgig nhllklffhr arptilphmv
      121 sehsfsfpsg hstastllyg tlifvmplff kektprliaq ilvgllifsi vvsriylgvh
      181 ypsdvlagtl fgsswllfty pmykekklay dlksirrkk
//
LOCUS       WP_010779645             196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010779645
VERSION     WP_010779645.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23199
     Region          10..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpreltpdek arnkqmlvdk gralvyqygi kkvsvddvva sagiakgsfy hyfsskdefl
       61 yaivyqihre lfgrlkiiae rikplssher rqtikafsdq ffssndmiff vkeqqeiqrf
      121 llryskekma eletyekqny rdffaileie dkhpeivqny vhllgfgmfh revmidtylt
      181 etvhimldgl mdylel
//
LOCUS       WP_010779660             191 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Enterococcus gilvus].
ACCESSION   WP_010779660
VERSION     WP_010779660.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 191)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..191
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22129
     Region          45..181
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mleykdfeek tierkelfkg kiidvylddv ylpmggtakr elvfhhggvg iipitkenkm
       61 imvkqfrkpl ekvvleipag kidpgegqhp ektavrelee etgyrtenlm yinemylspg
      121 fsneklyiyt atdlvkvenp kpqdedevle lyeltmeeak qaihdglicd aktifavnyw
      181 elmhyrkedh a
//
LOCUS       WP_010779663             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cysteine hydrolase family protein [Enterococcus].
ACCESSION   WP_010779663
VERSION     WP_010779663.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..181
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19963
     Region          3..181
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mrallsidyt ndfvatdgkl ttgeagqaie qalvdrtkdy fqqgdfivfa idghdpndhy
       61 hpenslfpph nvigtsgrdl ygslaafyqa nqaekniywi nkrhysafsg tdldirlrer
      121 gitelcltgv ctdicvlhta vdaynlgyql vipenavasf datghawaln hfkhtlgatl
      181 i
//
LOCUS       WP_010779689             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010779689
VERSION     WP_010779689.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..305
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34383
     Region          1..282
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mllsekmkqt dfsnaesalv ayildkgtai epmtikeiae anyvhpstli rvakklgyqg
       61 wlelrtefla eqtylqtyfd dvdanfpfqs neglmtiank iaslerttid dtlsllnhdd
      121 lqkakqllln asqikifgsn anllisqdfa lkmrriqrnv vtsqtmgeda yeafnsqpdt
      181 cailisytge nnfilqiari lrkqqvpfia ltsigentla slshatlrmt trerlyskia
      241 nftinssicy lldvlyscif aedyqknlnh lieigeladk rktssaimae spesmvrfte
      301 sfrpn
//
LOCUS       WP_010779716             258 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Enterococcus].
ACCESSION   WP_010779716
VERSION     WP_010779716.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..258
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29215
     Region          2..254
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mifdshthln aeqfeneipe tveraralgv temavvgfdt ptieksleln qqyegiysii
       61 gwhpteagsy tkaieedlik kltlpkvval geigldyhwm edpkevqdkv frrqiaiake
      121 mnlpisihtr ealedtykil keedirdigg imhsfsgsge waerfldlgm hvsfsgvvsf
      181 kkaldvqeaa tvvpmdkllv etdapylapm pyrgkrnepg ytryvvekia elrnlpmeev
      241 ahlttqnahr lfritadd
//
LOCUS       WP_010779733             261 aa            linear   BCT 01-JAN-2025
DEFINITION  putative ABC transporter permease [Enterococcus gilvus].
ACCESSION   WP_010779733
VERSION     WP_010779733.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..261
                     /product="putative ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30586
     Region          9..178
                     /region_name="COG4905"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443933"
ORIGIN      
        1 meqiftivvl lffcysfigw lwetvycsik akhfmyrgfl lgpitpiygf gvvgvlylie
       61 pyqknivllf ffalvlvtal eyltsfllek ifhltlwdyk evplningrv avpvsifwgl
      121 acvfivriln pylmqvvfgw qqrfgmflpm lllmltsfdl gftlanlasl rqamtkmsvt
      181 iqdkkeqlrt digdlkvaae grlqnrqwls eikeqpewrr qlpklnfqer rflnsfpnmk
      241 skelksplte irqlskelrk k
//
LOCUS       WP_010779812             889 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus gilvus].
ACCESSION   WP_010779812
VERSION     WP_010779812.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 889)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 889)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..889
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95959
     Region          2..842
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mtkhayqqet eelltdfhss teglspaeaq qrlqengpnq lkeakkkssl tlfletfkda
       61 mvivllivav vqmimgahve sivifavlll nsfvsviqtk kaegsldalk klsapdasvl
      121 rggqeqsipa kdivtgdivi leagdyvpad grlleegslk vdegmltges tpaekeltll
      181 tsdvpigdri nmvfsgtivt ygrgkflvta tggdteigqv agllestteq ktplqrgldr
      241 fskklslail vlsvvilgvq lmrvfldgst dmtqdivnaf mfavavavaa ipealqsivt
      301 ivlslgtkkm akqhaiirkl pavetlgsts iictdktgtl tqnkmtvvdh fladgqsgef
      361 skdpkqwead eqrlieisvl andatisedg tklgdpteia lidysekqnq syrelrkkyp
      421 reaelpfdsd rklmstlhti dqkktmvtkg gpdivferss kvlldgqvva ftpevkarfq
      481 kqneafsera lrvlafayke latddlsled eeelvlvgll amidppreev fqavadansa
      541 giqtvmitgd hkttavaiak eigifqqgdl altgaeldql seaelterle qvtvyarvsp
      601 enkirivraw qdkgkisamt gdgvndapal kqadigiamg tgtdvakdaa amvltddnfa
      661 siikavevgr nvfdnikkav aylfagnlga iiaiifalvi gwanpftalq llfinlvnds
      721 lpaialgmek aeptimkrqp rdpdsgiftg ktlisvtyrg ilialaviia qwlgnqqspe
      781 mgvamafstl ilsrtlqtfa arsntqtafq vgflsnkmvl laivvcaalf sltllpglre
      841 vfaiptafal keigialala asavllmeit klilvkvqep kgeaqvhkq
//
LOCUS       WP_010779869             404 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ammonium transporter [Enterococcus].
ACCESSION   WP_010779869
VERSION     WP_010779869.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..404
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43029
     Region          2..397
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 maaniafili csglvflmtp alaffyggle rrknilntmm mvictmglas liwvvvgysl
       61 sfsgggefig nldklffngv smtkgdsipe glfaffqmmf alittailtg svagrmrfsa
      121 iflfiaiwli vvyfpmahmv wgggfldkig sidfaggnvv hissgisglv laivlgrrre
      181 yhlgdyrphn vpfvvlgtgl lwfgwfgfng gsalaadgla ihamittnta aacamlswml
      241 iekvlngkpt vvgactgavv glvaitpgag fvsiwsslli galvspfcyf fisvikqklg
      301 fddaldafgc hgvggifggi vtgifadpsv ggrtgliyge thlfiaqies viftlifagv
      361 asyliislir vfmpirvsqq eealgldqie hdenayptfm gmds
//
LOCUS       WP_010779875             395 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent aminotransferase
            [Enterococcus].
ACCESSION   WP_010779875
VERSION     WP_010779875.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..395
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43033
     Region          1..392
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,206,235,237..238,246)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,199,244..246,275,278)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            238
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mklsqrvtnl epsvtlaata kakelkaqgl dvisltvgep dfttpenieq aaikgieggk
       61 vsfytasggt pelksaivdf tkknydlsia pknvivtsga kfalytlfqa vldagdevii
      121 pvpywvsyge qvklaqgnpv fvagaqnndy kitidqleev rtektkalii nspsnptgmi
      181 ytedelreig ewavrhdlli vsddiydhlv yngnkaahla slsedifhht viingvskty
      241 smtgwrigya igneeiigam tsiasqatsn ptavsqvaaa ealsgeqeta ekmrqafeer
      301 lntiypkvad lpgfelkkpq gafylfpnik gameiggydn vttwvndlle qervalvtge
      361 gfgssdsvrm sysssmenle eavvrirrfi enskk
//
LOCUS       WP_010779877             685 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Enterococcus gilvus].
ACCESSION   WP_010779877
VERSION     WP_010779877.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 685)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 685)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 685)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 685)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457627
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..685
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73662
     Region          1..65
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          98..683
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Site            order(393..397,533..534,561,579..580,583..584)
                     /site_type="active"
                     /db_xref="CDD:319763"
ORIGIN      
        1 mekvyrldgl dcancaakie rsvqqikgve qaqvdfmstk ltivapekdi ervseeakei
       61 vnklepdvev nsvqtqreee sskgkiiqiv vaiialggla iftpamplkl iaylilylwi
      121 gydvlktais nifhgeifde nflmaiatvg aiaigeypea vavmlfyqvg effqdyavak
      181 srksisslla irpdsanliq ngevkkvape aikvgdrili kpgekvpldg ivkegnsmld
      241 tsaltgesvp rsihpeeqil sgfinqsgql tvevtttfge stvskildlv enasskkapa
      301 enfitsfary ytpivvglav llavvpplvt gepfydwvyr altflviscp calvisvpls
      361 ffggiggask agvlikgsny ietlanvetl vfdktgtltk gvfevqtvet tmnkkeflqy
      421 vssaeqssth piaqsivnyv dqpllavsql eeiagfglsv eidghhflvg neklmankni
      481 pfqavqeigt ivyvamdgrf vghlviadei kdnvsealae akslgvkrtv mltgdnrgia
      541 daigkkigid qvysellped kvthleeelq retktafvgd gmndapvlar adigiamggl
      601 gsdaaieaad vvimddqpek iptaigiark tmgivkqniv faigvkvvvl vlgalgfatm
      661 yaavfadvgv tviavlnamr clrik
//
LOCUS       WP_010779905             235 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010779905
VERSION     WP_010779905.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..235
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27344
     Region          7..223
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mkkrefivqd llskiyqeef kegklpnqrk ladiygvsrf tiqqavknle eigivrvvqg
       61 sgifvhekwv knplifnslt rtpydrigsk midlkkgpat ldeqkifqlp dgeeiwtfer
      121 irivnykieq leisklpvam fpdlskevve hsiqnyveqk gfrishyits ydpittskeq
      181 srlllckrgt pamqitnrai ledgqvfeys sivaidysvt yirpfdreih rsrid
//
LOCUS       WP_010779936             182 aa            linear   BCT 01-JAN-2025
DEFINITION  LemA family protein [Enterococcus gilvus].
ACCESSION   WP_010779936
VERSION     WP_010779936.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..182
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20971
     Region          1..178
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mknhklilii agticavffa tflycksven kaivleesis esksaiskee qrrvdlfsil
       61 vdaiqnynsy esntlekivd arktaesgdv ekaseklsvv vekypdlksq knyqttmkef
      121 sitenrlady rdnyndfvkq ykryirkfpv kqflsisgyd iqsynyleft vdnkvatnlf
      181 gk
//
LOCUS       WP_010779977             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: O-methyltransferase [Enterococcus].
ACCESSION   WP_010779977
VERSION     WP_010779977.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..222
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24534
     Region          47..220
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mrnemmyrpi inedilhylr teqkqltgsl gdlealahen gvpviphetv vflqfllkqk
       61 qpksvleigt aigfsaslma eslgkeakit tidrfpvmie kakanfeklg ladqvtlleg
      121 daadilstle gpydfifmds akskyiaflp eclrllsddg vlmvddifqa gtvlqpiedi
      181 prknraihrh lneflevvtt speltstllp lgdgvalisk nn
//
LOCUS       WP_010779990             683 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Enterococcus].
ACCESSION   WP_010779990
VERSION     WP_010779990.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..683
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=78274
     Region          10..661
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 myfsirekki lsllldypng itpeelqdil qvskrtvyre issiektiks qdiqiikprg
       61 egyrivgesv nlerlqqqlt ekqeelftdn vqrqsaivcs lllmdeeeti eglaidfkvs
      121 patitsdlsa iekslidyrl elkrlkgrgi riegrekqrr qllsnliyng vsefdffqyi
      181 dsledetvtt dsfflnllsr snlllsrtil eqvsqqafeq vtdnqlqrvl illalsidrm
      241 meerfveveq enkakpesmq iasqimikva ttikqsippq evrffafqle gvnykrpqni
      301 fidsfdvels ykikelirlv setteidfrk deqlftdlsa hmsaalkrnl tviqgannpl
      361 lqkirdkyqa lttaiikela vvfpdhqfta delgyvvihf atslerhpsg ralsalvlcs
      421 sgigtarile srihkylnei qkvqvakise mnqldyksyd lilatvflpg fhlpykvisp
      481 lllddeikei keyiqtlhpe kaneradepe qepseafdei yetmriansl lqnfdvkqvs
      541 aretieltld eiieqlqgti vsdaklvtdk vikrylvapi gvpktnfalf hcadahvkep
      601 lftiydldqk fliqgmdkks ieltrvllll apdpmpesqq sllgkisssv iesdlnteiy
      661 kfgnkeiiyq llsslfvkei ren
//
LOCUS       WP_010780014             348 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010780014
VERSION     WP_010780014.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..348
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38637
     Region          4..324
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mekilevnnl nisfdtyagk vkairgvdfd lnkgetlaiv gesgsgksvt trtimrllsg
       61 nanidegqil fkgqnivdks ekemqkirgr eiamifqdpm tsldptmtig kqvaeslrkh
      121 kkiskkeglk aaldllnlvg ipdaekrlkn yphqfsggqr qriviaiali cnpeiliade
      181 pttaldvtiq aqilellkei qekietsiif ithdlgvvan vadrvavmya gkivevgtae
      241 eifynpqhpy twgllgsmpt lesendrlya ipgsppdlld ppkgdafypr nefalkidae
      301 meppffeise thkaatwlla pqaptvtppa eiqrrwdifr kkqnqysa
//
LOCUS       WP_010780065             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF1836 domain-containing protein [Enterococcus].
ACCESSION   WP_010780065
VERSION     WP_010780065.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10556141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..182
                     /product="DUF1836 domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21235
     Region          19..119
                     /region_name="DUF1836"
                     /note="Domain of unknown function (DUF1836); pfam08876"
                     /db_xref="CDD:430279"
ORIGIN      
        1 medtklrtwa eglkdlrlpr weelpelely mdqvitlvdr ylsplieddk hqllssamvn
       61 nyvkhklvpp pvkkrynrnh layliaitll kqvfaipdin elirmqlain epkdaynsfc
      121 tvqeeallql akivlgeeie fnsykkdfyy lamesaiasf tqkmltekii qlekekeget
      181 de
//
LOCUS       WP_010780071             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Enterococcus].
ACCESSION   WP_010780071
VERSION     WP_010780071.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..269
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30198
     Region          11..198
                     /region_name="YycJ-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Bacillus
                     subtilis YycJ and related proteins; MBL-fold metallo
                     hydrolase domain; cd07733"
                     /db_xref="CDD:293819"
     Site            order(63,65,67..68,128..129,150,198)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293819"
ORIGIN      
        1 mlemnnafni silasgstgn slylespqkr ilvdaglsgk kitsllaevd rkpedldail
       61 vthehrdhih gvgvlarkyk lpvyanektw eamspligkv dveqqhifem gkvltfgdld
      121 iesfgvshda aapqfyrfyk dghsfvmltd tgyasehvrg tirdadaylv esnhdlemlr
      181 mgaypwslkq rilgdrghls nddgalvmtd ilgdrtkriy lghlsrennm kelahmtmee
      241 tltrydlgvn hqfqifdtdp dsatelfai
//
LOCUS       WP_010780091             529 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus gilvus].
ACCESSION   WP_010780091
VERSION     WP_010780091.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..529
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59909
     Region          1..488
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mqlrpyqqea reaiqqewkn ekkrtllvlp tgcgktivfs kviedrvkkg ervlvlahrg
       61 elldqasdkl qkstglktat ekadqtsigs ffrvvvgsvq tlmrekrlsq fppnffdtiv
      121 vdeahhcisd gyqrvlqhfe danvlgvtat pdrgdmrnlg syfeslayey slpqaikegy
      181 lspikaltlp lkldlsavkq qagdfstkdl gtaldpylyq iademakhck drksviflpl
      241 vktskkfrdi lndrgfraae vngeskdrae iledfdndky nvlcnsmllt egwdcpsvdc
      301 ivvlrptkvr slysqmvgrg trlyegkeel llldflwhte rhelchpahl iantdevakk
      361 mtenieesse tgfaidleea evqaekdvvs ereealakql aemrkrkrkl vdplqfemsi
      421 qaedlssyvp sfgwemapps dkqiktlekl gilpdqidna gkatkmlerl ekrrveglat
      481 pkqirqleqr gflnvgtwsf esaskmigri aangwrlpqg itpstytee
//
LOCUS       WP_010780073             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010780073
VERSION     WP_010780073.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..214
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=23935
     Region          114..206
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mnekkysfit iftyglvlfs plifqrvlqa nssqliqltt layflgaalm vvyrfksnif
       61 glegtrksvl isiligilgv paslllqmvi lqieqrflgq siasqntqni vqlimnnmif
      121 ilattiagpi meefvfrrai fgslekrfgf flpallssvl fafahndghy llyaglgflf
      181 cgmyrysgri wtsmithvgm nllviltqla lhan
//
LOCUS       WP_010780126              66 aa            linear   BCT 01-JAN-2025
DEFINITION  cold-shock protein [Enterococcus gilvus].
ACCESSION   WP_010780126
VERSION     WP_010780126.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7039
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mnngtvkwfn adkgfgfitg edgndvfahf saiqsdgfkt leegqavtfd veegqrgpqa
       61 tniqka
//
LOCUS       WP_010780149             465 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TrkH family potassium uptake protein [Enterococcus].
ACCESSION   WP_010780149
VERSION     WP_010780149.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..465
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52511
     Region          23..448
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 msfdrrvnfl kknwqkinnr fssiqiivfy ylamtilslv lfylpifrep gshvpfldmv
       61 fmaistisvt glttfninsv fndngvlmle vlfhigglgi mmittfffiv skrritlkqr
      121 qlimtdmnqp rlsgivnlir vtftmllvie vlfgtifsiy fylagyyrtf skaiffgfyq
      181 aisavtnsgf dvtgdsiipf shdvffivti mvlifiggig fpvlmdfhgw iyhkksksrl
      241 pfrfslfski allaffvlfi ggtiaiwlle kdhsfasmnl fdqwlnssfy smttrnaglq
      301 ihdltifqnt tliifsllmf igcspssvgg girtttiaii glylysflkn endinifgrk
      361 iaqedvrksv vvfmlsagmc lfsilfltat edhslisiiv evtsafgttg lslgitddls
      421 stgkimiail mfigrvgmly tlmlfvpket qdlgyefpee kiiig
//
LOCUS       WP_010780166             280 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Enterococcus].
ACCESSION   WP_010780166
VERSION     WP_010780166.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..280
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30623
     Region          3..278
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkkilgfaa vglltiglaa cgnnnsassd ssskeksdtl vvgasptpha eilehvkpll
       61 ekegiklevk kfddyvlpnk aladkdidan yfqhkpffek avkendykft dagaihiepm
      121 glyskkikdi kdlkegatvi tsssesdwgr iitilqdagl vkvkdgvdle tatfddiaen
      181 pkklkfdhsi dpallattys ndegdlvain anfaygagln pvkdavllek dtspyanila
      241 vrtedkddpr iqklvkvlhe kdvqdwilek wdgsvkpvdk
//
LOCUS       WP_010780167             140 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Enterococcus].
ACCESSION   WP_010780167
VERSION     WP_010780167.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..140
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15806
     Region          1..129
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mnaagsclcg evnivipeia eeitvchchm cqkffggpfl slsgilpeaf vmrgetkirr
       61 fmssewaerg sckvcgsslf yhsladdtyy fptglfdald hamlkeeify dqkpaffhyq
      121 esteklteaa fmerlfddle
//
LOCUS       WP_010780174             965 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus gilvus].
ACCESSION   WP_010780174
VERSION     WP_010780174.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 965)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 965)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..965
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=109633
     Region          24..514
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 msyfssnyil mkyplslysc egqglrnaqi gavhalgayf ttkkepvlls mptgtgktav
       61 immspyllgv skvlvitptv lvrsqiaqnf svlkdlkkig vfeqeveppe tyelkhkytd
      121 dlkeniekad vvvstpgcal plsenqeink tfdlviidea hhepaktwre vlanisdakh
      181 vlftatpfrr dkkeikanhi ynyplsqayk dgvfgsinfi pveikanedk ditlakkgee
      241 iffrdkasgl ehammvrcks kkeairlfkl yedntvlnlk ivnssksrqe vlkiidqlen
      301 qeingvicvd mmaegfdfpn lkiavihdph kslattlqfi grfartnqek ligeasfiav
      361 ndeqfalenk rlfstdsiwq eiiidlseer inqdiesqey fksydnqlis tnnqefslhs
      421 lytnfrariy yaksfnlnae fpdlrmkien invseddqtv vvvasnkqlp rwstadgiyf
      481 nleyntvlih yqkknkllfi nshlksesiy daiaiaycge enyekitlsn ihkvlsgvkn
      541 heifnsglan rlsegetyki sagsdvskai dvdsgkmysp ghvfckaeea daqitigyss
      601 gskiwssryg siqemvkwfn lngdkisnkh akvktntnyd nlpmptemtv fpkdifmwdf
      661 nvhsyrkphn lliseedist stildvdisi esvepveiwl kvslngrsyn ivrningkyk
      721 cfveeeffim vgreamplsi yfnqfplsfy tsslslisgk eisiydynlp afdknkivsi
      781 dwkkyntdit mefktnkykg nknsiqdaig ekldeneayd yvifdhgsge iadyisievl
      841 ekeiivslyh akskssvnfn ssvgdvyevl gqsiksliwl ksksillakl kdrqrsghsv
      901 fikgeikhle ktlkdnkpmr gkiiacqpgl tghkklpdki gevlsatnmk iknsatakdf
      961 yvwgs
//
LOCUS       WP_010780189             174 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010780189
VERSION     WP_010780189.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..174
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=19622
     Region          1..85
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrtidlivlg ilkkdslsay diqklidyrn isqwvkvstp tiykkmlqle kqgyvkstlk
       61 kngkmpekav ysltqkgkte feklmlgiaa rpitifldfn avilnldsls sadqkacisi
      121 ieanvkkmkr rlkddladsn dsadihdagk avmqqqylla eaiekwieei kksl
//
LOCUS       WP_010780202             175 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010780202
VERSION     WP_010780202.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..175
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20730
     Region          1..77
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          87..170
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mntisyvvla mlirspltgy elkrflnlfw eahhsqiypt lkelrkqeli eiidipdgkr
       61 kiyditpagk elvkewvftk shapsqkdef lakvftisal drdtskflim erkqyfheqv
      121 ndyskvlasl ddldeeerrk nfgreliler kirlskeela wcdwaeekie ayfak
//
LOCUS       WP_010780239             333 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Enterococcus].
ACCESSION   WP_010780239
VERSION     WP_010780239.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..333
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37327
     Region          1..254
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 minlgiigtn witdqfvqga letgdyqlta vysrkletaq kfgekygdve yatdlktffg
       61 iahmstvyia spnslhfeqa kqailagknv ivekpafstp demdeiiela nqksvfffea
      121 arnihekafk tvsdflplkd hvigadfsfm kyssrydqvl dgeepnifsp hfsggaladl
      181 gvypiyaala wfgmpqdsfy fgqkistgvd gmgtgilryd hfdvtirtgk igdsfqqsei
      241 yltngtlvln avnsideavf hdrghqrrek ltvhqlenpm veeakefaqv imnptdrklg
      301 tdyeawvels rnvnqviydm rksagivfda dek
//
LOCUS       WP_010780240             392 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Enterococcus].
ACCESSION   WP_010780240
VERSION     WP_010780240.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..392
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43200
     Region          8..378
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mdkqefvpfl qknwedagfe kpaliqssvf tpitegknlv giaptgsgkt layllpllnk
       61 mtpgkasqvl iltssqelam qvvevarkwl sgsgmkvqpl igganvkrqq ealkkkpell
      121 igtpgrvmel itakkiktpn iqtlvfdevd qlvqgqslql iqkilkasdn gaqhlyfsat
      181 adtvleelnt fesellvvdv seeddsqgev shfyletsdr kkveqlrrll nlptfwgmif
      241 fnqlgdmgsa eekllfhqlp vaslasdqsk lsrkgaieqf kkhqalgllt tdlasrgldi
      301 eslpfvinad vplseesylh ragrvgrmgk tgvvislvtp qekadltkig kklalnlapi
      361 ylfggellte epvkqsdpkk kknkkskgkr rk
//
LOCUS       WP_010780244             307 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YihY/virulence factor BrkB family protein
            [Enterococcus].
ACCESSION   WP_010780244
VERSION     WP_010780244.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..307
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33865
     Region          1..286
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mgpidkiken kklmdfiqsi qkhlaeteig drsvvvayyl llsffpilii vgnllpyfni
       61 tpetvlpyls eaippnvysf lkpaiiglle ntsggmlsis vlaalwsssr ginalqtaln
      121 raygvedrgn fvisrivsvg ivgilmmaii avalffsagq vildalqqll rfspdiietf
      181 lalrwpvtli gllvilggly ivipnahvri kyalpgtifa tvgwivlaqg fsiyaqtfaq
      241 rvsgyqiigs fivlmfwlnf aatiiilggv lnvtieeyht gqevtegsnr vnkwfnqlkd
      301 rfikkkk
//
LOCUS       WP_010780280             310 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Enterococcus].
ACCESSION   WP_010780280
VERSION     WP_010780280.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..310
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35226
     Region          4..186
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(7,9,93)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(40,92..93)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            91..93
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 misvivpcfn eeeaiplffv emeevkkkvs ydfeyifind gsedqtldvl rklareysfv
       61 rylsfsrnfg keaalyaglq aakgklvavm dvdlqdppel lpqmiemiet tdvdcvgtrr
      121 adrkgepair sffakkfyql inrisetemv dgardyrlmt rqmvdavlel tehnrfskgl
      181 fswvgfktey isfenqerva getswsfwnl fnysidgivn fsdaplnias fvgafscvvs
      241 giamlfiivr allfgdptag wpslvtiilf iggvqllcig iigkyigkif metkkrpvyi
      301 iketekkleq
//
LOCUS       WP_010780326             137 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Enterococcus].
ACCESSION   WP_010780326
VERSION     WP_010780326.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..137
                     /product="VOC family protein"
                     /calculated_mol_wt=15191
     Region          3..134
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(3..6,22,60..61,64,82..87,89,93,122,132)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mdiylhfddq aadaiafyee vfhtepanim tfgqmphdee hpvdeaikel vlnanlking
       61 tnvmisdspk gmappiaign nvalvydaet aeeaseifmk lsengaillp lektfwaely
      121 gmvkdsygvn whinlys
//
LOCUS       WP_010780420             258 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010780420
VERSION     WP_010780420.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..258
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29005
     Region          1..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlkterqqsi lamcdrygtv tvkfiqetlg vsdmtirrdl eelaqrkqll rvhggaqkmn
       61 nqenatthie tnelshkekk klhtkekeyi aknaaayitk eddtiflgsg ttielmtqyi
      121 natslrivtn slpvfnllsd tksfelylig glyrektgaf vgsianeavq kigikkafvg
      181 vnglkgtevs nfsieegtlq kivldnaaek clvsdankfd hsdfytfydl rkidalftdt
      241 tlsaelksyy qqytkiiq
//
LOCUS       WP_010780449             449 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010780449
VERSION     WP_010780449.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..449
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=49036
     Region          1..424
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdrlvnsieq klmpfankig tqrhmmairk givatmplti vgsfftifln fpipsvaami
       61 epylaildip frytvgilal yatfgiasql aksykvdslt agilsvmafl vtaappirvf
      121 dnvegvidag rylnianlga aslfgaivta lisveiyrif ieknitikmp dgvppevtns
      181 fmalipggai lvlfwvirhm igfdingfls nllmpfkdvl agnslfggll tvflicffwv
      241 lgihgpaimg pvirpfwels iaenmeafad gasatampni fteqflqwfi wiggagttla
      301 lvvffmfsks kylkslgrls flpglfnine pmifgapivm npllgipfiv aplvtttlsy
      361 fltisgvipm mvarygftip apiaawmstd wsiaaailvi vnflismaiy ypffkvfekq
      421 qlareaaele aeekakkeka anlqgatsn
//
LOCUS       WP_010780455             331 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Enterococcus gilvus].
ACCESSION   WP_010780455
VERSION     WP_010780455.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..331
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36929
     Region          2..309
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(33..34,37,88,103,106,136,169,270,273,309)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(236,247,261,270..272,275,297,301)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mkfaafgevm lrlsppeyll ldqtnelrmd ytgtgvnima nlaqfgydss lvtvlpenrl
       61 gqvaksalak ygiktellsf ahhhigsyfa engygqrpth vtyqnrhhss fgvsdhtayn
      121 fekvaaendl ihicgislsl tdatrdaaht laqeaakagk kvcfdfnfrp slntepnkla
      181 fmkeqyekil pycaivfgst rdlldllqvp ktgsedemiw qfmekyaidw fagtrrttad
      241 srkqmqgfly nrkeravsav rdlvaldrig agdayaagil tgyaenwplv etvefatmna
      301 vlahtihgdv plttkeqvft vlknpeidli r
//
LOCUS       WP_010780467             271 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010780467
VERSION     WP_010780467.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..271
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30780
     Region          2..110
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(3..5,19,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            40
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(51,54,58..59,68,81,85,91,95,101..102)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          120..263
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mfkigefskl snttvrtldh yaalglltpe kideqtnyry ysagqlsrln qikllqqtgl
       61 plktikeiie mndlefleqh yklqevrvqe elselvkkqr miallqqqmk egkkmlnypv
      121 vvkeiperti lsvreviady slegdlwqkl qhkmeaakak mtqppmnltv fhdveyvekn
      181 advevqttiv deagnvgrvd ykkepaftla svtfsgsfdq mpkvtqtige wleangysiv
      241 gpminishvs paedpnpdnw vtesgfvvak d
//
LOCUS       WP_010780506             320 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar kinase [Enterococcus].
ACCESSION   WP_010780506
VERSION     WP_010780506.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..320
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34954
     Region          3..300
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(35..36,39,91,105,107,136,169,260,263,299)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(229,234,250,260..262,265,287,291)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 msefltigep ialfgseevd kslkdachfq kflagaevnv avgvsrlghs seyitqvgkd
       61 pfgefiidrl heneigtdyi sesadfwtaf qlkdrvsegd psifyfrkgs aaahfdqsvl
      121 dtidfsdvkm ahlsgifpai skeareafry lirlleknhi rttfdpnlrp qlwvsteemv
      181 etinelaaha eivlpgineg eilmgsrdpe aiadfylnng eatqtvivkl gtegayvkqk
      241 dgtqftvpgf kvakvvdtvg agdgfavgli talieektlk eavvranaig amavqspgdn
      301 dgyptqqele aflqqqevna
//
LOCUS       WP_010780526              68 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF378 domain-containing protein [Enterococcus].
ACCESSION   WP_010780526
VERSION     WP_010780526.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..68
                     /product="DUF378 domain-containing protein"
                     /calculated_mol_wt=7197
     Region          14..68
                     /region_name="YuzA"
                     /note="Uncharacterized membrane protein YuzA, DUF378
                     family [Function unknown]; COG2155"
                     /db_xref="CDD:441758"
ORIGIN      
        1 mkyldiiali llivgginwl lvglfeydlv aaisggstai lakiiyivvg lcalyclkfi
       61 pgianrte
//
LOCUS       WP_010780560             564 aa            linear   BCT 01-JAN-2025
DEFINITION  terminase large subunit [Enterococcus gilvus].
ACCESSION   WP_010780560
VERSION     WP_010780560.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..564
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63840
     Region          1..564
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mneyiekvls gkliapkkii qacerhisdl ersksdsfpy vfdeeqanka irfiellpst
       61 dgkgikmlgf qmfiigslyg wrtkegnyrr fnrafisksr kngktyiasg maanaliveq
      121 epaearqvlf vsnalkqakl gydmlsnslr nvvksskflr pqlkimnski qhlpsnsfam
      181 alasetstld gfapttaild ewheaktrkt ynviksgmtq qkngllcvis tagldlnvpm
      241 yeeyvlldrv ltgeeqadry fiaiwelddp eeihdqekwi kanpifesee ikkvmiptiq
      301 ddvnlalkqn nlnsvlvknf nlwrqaseds ymatedwqat evepqditgk pvyigvdlsk
      361 tddltsvswi vpldngelyc dshsfvatky glqdkekrdg lpyrelekvg ecsitqlesg
      421 ivdydqvfef iqsliemndl ecmgicydpy nansliskae kanypmlevr qgtitlnvpt
      481 rtlreqvyeg nvihnkntil thavnnailk tdnngiqink sknsnkidpi aalinayvfa
      541 mdyftttega kadnvfytse efsf
//
LOCUS       WP_010780596             395 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu [Enterococcus gilvus].
ACCESSION   WP_010780596
VERSION     WP_010780596.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     gene            1..395
                     /gene="tuf"
     Protein         1..395
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43359
     Region          1..395
                     /region_name="TufA"
                     /note="Translation elongation factor EF-Tu, a GTPase
                     [Translation, ribosomal structure and biogenesis];
                     COG0050"
                     /db_xref="CDD:439820"
ORIGIN      
        1 makehydrsk phvnigtigh vdhgkttlta aittvlgkkg lanpqdyasi daapeererg
       61 itintahvey etekrhyahi dapghadyvk nmitgaaqmd gailvvsatd gpmpqtrehi
      121 llsrqvgvky livflnkvdl vdddelidlv emevrellte ygfpgddipv lkgsalktle
      181 gdpeqeqvil dlmdtvdeyi ptperdtdkp fllpvedvfs itgrgtvasg ridrgevkvg
      241 deieiigikp evqkaivtgl emfrktldyg eagdnvgvll rgitrdeier gqvlakpgsi
      301 tphtkfsaev yvlskeeggr htpffnnyrp qfyfrttdvt gnimlpegte mvmpgdnvti
      361 dvdlihpiav ekgttfsire ggrtvgsgiv teiek
//
LOCUS       WP_010780617             179 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RDD family protein [Enterococcus].
ACCESSION   WP_010780617
VERSION     WP_010780617.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..179
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20322
     Region          31..167
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mteetpqrpa vgpvtqllek krqspqfhdy pnyfyagfwi rffaylvdli cisaitgivt
       61 ripiavfglt ksnellsayg ltavilylay filltklnhg qtigkmifgi rvicfieeql
      121 swktvlvreg acrfilrgsf fmlgylvtif tptkqhigdy fsdtsvvtln lltaredfk
//
LOCUS       WP_010780666             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Fur family transcriptional regulator [Enterococcus].
ACCESSION   WP_010780666
VERSION     WP_010780666.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..145
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16553
     Region          4..140
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mvneavdqav relktggvri tpqryailey liqyrnhpta deifrslesr fpnmsvatvy
       61 nnlrkfveig ivqemnygda asrfdftnkq hyhaictecg kivdffypgl edvemasskl
      121 tgyqinkhrl evyglcpdcq ttaee
//
LOCUS       WP_010780744             699 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus gilvus].
ACCESSION   WP_010780744
VERSION     WP_010780744.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..699
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80059
     Region          33..639
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mshlkkysqf iktrigffsl llgllwlknm fayvidfhlg iqslmqfiil ivnplsvsml
       61 llsiglfikr skvaygtlfv iyalltiwlf snavyyreft dfitintmlg agqvstglge
      121 savrlfrwyd vfyildlivi plllfkkkip itddyprfrq aaalsalsll igsgniflae
      181 idrsgllsrq fsreylvkyl gvnaftlyds yqtyqnnqir aeaspndlke vqsyvkdhya
      241 kpndsmfgva kgknvvyihl esfqqflldy qltdengvnh tvtpflnsly hgestysfdn
      301 ffhqvkagkt sdaetlmens lfglnqgalf tqmgdkntfe aapnilkqka dytsavfhgh
      361 sasfwnrdkt ykhlgfdyff dssyydindd nsfqygmhdk pflnqsvqyl ehlqqpfyak
      421 fitvsnhypy srfkneedgf plantkdeti ngyfatanyl dtalkeffdy mkasglydds
      481 ifvlygdhyg isntrnkdla pllgkdsdtw tdydnaqlqr vpfmihvpgv tngginhtyg
      541 gqvdalptll hllgldskny lqlgqdlfsa dhkqvvafrd gdfvtpeytf yggkvydnqt
      601 aqviseptpe qeklfvelnq dvdqqlitsd kitngdllry yqdsgltsin pndfdyrdqk
      661 arleeierqk ganssslyse nnqkstdgly ktktyqqye
//
LOCUS       WP_010780746             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Enterococcus].
ACCESSION   WP_010780746
VERSION     WP_010780746.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..265
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28300
     Region          72..262
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          72..99
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(101,103,107..108,111..113,115..116,120,123,132,168,
                     170,174..175,178..180,182..183,187,190,200,202,204,
                     208..209,212..214,221..222,226,229,238)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          101..132
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          168..200
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          202..238
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mkkilaital lfvlsgcqqa sqnnnaanss ssaekavsks tttkdstssl vsstnttqsk
       61 eeqsmtnvpg sliqsvsand takvteilks spnmidevna ngetplliav hnnqidlakl
      121 lidagadvnk qdakkdsayl yagaegrtei lsymlshsqp nqqitnrfgg nalipaaekg
      181 hlenvkllla dgnvninhqn nygytaliea valrdgsqvy qdivsellkh ganpdikdny
      241 gksakdyahe lgygnmskml qeskr
//
LOCUS       WP_010780765             293 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Enterococcus].
ACCESSION   WP_010780765
VERSION     WP_010780765.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..293
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31215
     Region          1..292
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 miisaigqgf lwgilglgif mtyrilnfpd mttegsfplg gavcvtaitn gvspvfatml
       61 giiagmcagf itgmlytkgk ipvilagilv msglnsvmlf imqtpnlsll kqpkiqdfft
      121 nlnlpnhfdi vllgliaili iislllffff tdfgqayiat gdnenmarsi gintdrmkvi
      181 gltlsngvia lsgaliaqnd gyadigkgvg viviglasii igevlygevt fverlvaivl
      241 gsiiyqllil iiikagldtt ylkifssiil alclmiprlk etlnlktgle kge
//
LOCUS       WP_010780800             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HD domain-containing protein [Enterococcus].
ACCESSION   WP_010780800
VERSION     WP_010780800.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..214
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24489
     Region          5..211
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 mqnkiekirq yakeklgkdr sghdfyhver vakiaqelae qegiadkmii eaasylhdvi
       61 ddkvaedvek eredlekflk dldltslein eivdiienis fskelehgka kltfagkivq
      121 dadridalga igilrtayyg ghtqsplydp niqpqnfqsk keyrknstvi nhfyeklfkl
      181 patmntaagk aeadrrvvfm kdflktfyee wgls
//
LOCUS       WP_010780795             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_010780795
VERSION     WP_010780795.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..146
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16663
     Region          9..142
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mkeyfgalpe tqaaafylry qvfvleqkis pdlefdlldt pdrkylvffk enipvgtiry
       61 qkidaltlnp drlcvgrdyr kqglgkkllk rieeqaiseg cihsilsaev saqsfyekls
      121 yrvvsdvfee dgipcvkmqk dlvsan
//
LOCUS       WP_010780855             175 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HdeD family acid-resistance protein [Enterococcus].
ACCESSION   WP_010780855
VERSION     WP_010780855.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..175
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=19866
     Region          14..175
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mlnfidsikk dgylrsafyl ilgiailisp rsvfrgivyi iffyllifgi mqiirgvkak
       61 kytgnvgfet tsgitriiia fvilwfskgi isilpmflgf iilifaigqf lqswsakrng
      121 fpvmaqviys almivagffl lfnpfsslmf lfqifgflli tmaisefint rrfsr
//
LOCUS       WP_010780857             143 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus gilvus].
ACCESSION   WP_010780857
VERSION     WP_010780857.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15351
     Region          5..141
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mkesykkilv avdgstastd afnealniae rngaklfilt vvdykfslgd pafindalkf
       61 hlnnaeiele qliansdisk ldyetkidsg npkrkivdya vetqvdliiv gstgkgaveq
      121 aivgsttayv vnhascnvmv vkp
//
LOCUS       WP_010780885             224 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010780885
VERSION     WP_010780885.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..224
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25296
     Region          23..213
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtyplqehhf kllkkyglsd hhalceirhy esgdivfsqg feykyillvv sgkakvctts
       61 psgkslvlay ylssgiigdv elmsktnyat asvvalsafe clvvpfqddd dtmfknltfm
      121 telakglsnn lmssshdyss nalysgeqrl ctyilkgayk nyfydnlsdv aatigisyrh
      181 llrllkklce snilkkekra fllldkekli qyssevsyfe netl
//
LOCUS       WP_010780901             163 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Enterococcus
            gilvus].
ACCESSION   WP_010780901
VERSION     WP_010780901.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Leiros,H.K., Tedesco,C. and McSweeney,S.M.
  TITLE     High-resolution structure of the antibiotic resistance protein NimA
            from Deinococcus radiodurans
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 64 (Pt 6), 442-447
            (2008)
   PUBMED   18540048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..163
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18577
     Region          1..159
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 mrrkkrqvtd lelikkfvek tqvvrialng ekypyvvpvn fgyewneeel mlfihgaaeg
       61 kkvnmikndp hvaiemdghh rliegtsnaa tysyayqsfi gfghasfled leekrkalhv
      121 lmdhaakgas fdeipeamlk rtgiikitla sytmkenihp dek
//
LOCUS       WP_010780910             239 aa            linear   BCT 01-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Enterococcus gilvus].
ACCESSION   WP_010780910
VERSION     WP_010780910.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..239
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=26827
     Region          12..236
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mkpiigvlpl ydevsesvwm lpgylnlvee nggiplilpl tanketwqpf lslcdgfift
       61 ggqdiapary nekttdacge vnqlrdemef qlmeevivrd kpflaicrga qllnvflggt
      121 lyqdlmsdnp qtmnldhhme apynrtqhqv eliensllhk ilerhylgvn syhhqaikkl
      181 gkelkvtals pdglaegvfi pkasfalgvq whpeffsatt svnqaiikaf feacerkhs
//
LOCUS       WP_010780955             296 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YitT family protein [Enterococcus].
ACCESSION   WP_010780955
VERSION     WP_010780955.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..296
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=32635
     Region          4..284
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mettlstrik eitfivvgta iyafglvyln ianhlaeggv tgitliiral fgidpayttl
       61 iiniplilig gkilgkrsfy ytilgtvcls vflwiwqrip lqinldhdlf ivsilaglfa
      121 gfgsglvyrn ggttggadvi arileqkigf tmgksllvfd iivlicslty ldlkrmmytl
      181 ivsfvfskvv dmlssggyaa kgvmiisnes nviaellmah lergvtylhg eggfsselkr
      241 ivyivvsqqe inevkklvhs vdekafilis nvhdvegegf tylkpqrrrf tlkrtn
//
LOCUS       WP_010780957             415 aa            linear   BCT 01-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Enterococcus gilvus].
ACCESSION   WP_010780957
VERSION     WP_010780957.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18641232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..415
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47154
     Region          <4..127
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(9..10,12,34,37..38,41..42,44..45,68,71..72,75..76,
                     79)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          32..62
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          67..92
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          70..333
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          102..129
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(139..140,143..144,146,173,176..177,180..181,
                     183..184,207,209..210,213..214,217)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          139..163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          171..201
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          206..232
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          238..268
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          272..406
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          273..301
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(274,277..278,281..282,284,308,311..312,315..316,
                     318..319,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          306..334
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          339..367
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          373..396
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mssysekmlt alkneeltea nlmfeealkk depevlasls eelqtlgfle eakrileklv
       61 adfpeedvfy lslaeiaied ddidgafeyl ekiqpdseny lesllvtadl yqvlgipevs
      121 eakllqaktl apeeplitfa laelhfsanq lgeaiddygq lqkqgideva nisiderigs
      181 aysmmggfee aipflekale kehtsdrlfq lgftfyqlhd hqkainylqe litldpeyqs
      241 gyyyladslk eeelleeals aaeegikenp yqvellhlas eiayrlrdsk kseellkqal
      301 etgektdetl ltlsnlylne dqpdkviemi sqmdeegnpy aawnlaqayn eledfgaart
      361 yykqayedla hepdflkayg iflredgqld lartvlvdyl qmepgdlevq sllee
//
LOCUS       WP_010781001             494 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus gilvus].
ACCESSION   WP_010781001
VERSION     WP_010781001.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..494
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54296
     Region          10..463
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 maktvivdda pkfgmkdkig yalgdfgcnl sfvmvstyfm vfyvtvmgis pvhfgfiala
       61 srvwdglndi fvgsmvdrlr pkpgkskfkt wmfygsilli fatiimftpi ealsyggrla
      121 mcmgsyalwt lvytavnvpy gsmasvittd gveraelsky ralgsllgnv pagvvlplvl
      181 ynaqsgdpif srfiptaivm glmgtvciqa cakmcteriv rveeptdtnq srgnffktff
      241 samssrpmig liiatcallm llqsnnatnq yvfmlhyqrt dllsltmmls yipqilmmif
      301 ltplvkkigk knlitypfig vvavaafmmi tpmdnpyvwi acqffigllq gafvmlmwal
      361 isdiidymea rtgrreegtv yssvtlfrkf asgfgqvvig tglsavgyne tvnvaqqaag
      421 vgsgvktfaa lllliggaii fcsmkfiynl ddekmkevea klnhepevet eaamimesia
      481 esnqsneimk epna
//
LOCUS       WP_010781024             393 aa            linear   BCT 01-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Enterococcus gilvus].
ACCESSION   WP_010781024
VERSION     WP_010781024.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41945
     Region          3..393
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mnrkvvitsa vrtpigsmgg slsdtpvtdl gshvirgaid ksnitpdlvd evfmgcvfqa
       61 gqgqnvarqa amkagvpfhk pattinvlcg sglqtvnmaa kfiaaghsei ivaggmenms
      121 aspyllpkar ygyrlgsgei vdsmikdgle dafndyhmgv taeniaekwe lsreeldqfv
      181 ftsqsnavra ieekkfveei lpfeiktkra nhlfsedesi rkdttleklg klrpvfmkdg
      241 kvtagnssgi sdgaaavllm seekaiemdi pilayweage lagvepsimg igpvdstrkv
      301 lsktgltidd ielvelneaf aaqsiavire lglrqelvnv nggaialghp lgasgcrilv
      361 slihemirrd triglaalcv gggmgcstii rrd
//
LOCUS       WP_010781075             177 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010781075
VERSION     WP_010781075.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..177
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21182
     Region          1..84
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mipllilgll qempesygye llaemkanyf qyfvrftkgs fyyniqqlee krmiekvqst
       61 erpeekeknr yvltelgkne fkrlfykygs ksepitfpfy tsmlfanqrr pdeiqqllqt
      121 qiqqtkekir liddalsssk qlhsnfakmm enskrhhevn lewfqeqlvd slkkpse
//
LOCUS       WP_010781078             241 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010781078
VERSION     WP_010781078.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..241
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27132
     Region          11..234
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdlelvtkgk qlsdndrail tylanhvhel dgvslrkiaa tlytspativ rlaqkldfsg
       61 ylelffflkn qyrpqnqfve atvdisiptd klapsiqdmk qiyrknqekf itiyatgfss
      121 iiaeylykkl lvngiktlfv naadssgiin nnaeninmli visksgetqk viekmhfsse
      181 hniptilftg nshsrgteaa siifevader pmdsqnikyn sffgkllllm eyivqeftat
      241 d
//
LOCUS       WP_010781082             362 aa            linear   BCT 01-JAN-2025
DEFINITION  YncE family protein [Enterococcus gilvus].
ACCESSION   WP_010781082
VERSION     WP_010781082.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..362
                     /product="YncE family protein"
                     /calculated_mol_wt=41091
     Region          <87..152
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mqkkkygvll wfllmvlfpv rvdasyhglt vdqqkekles ynefyqaafs gkeettdfgm
       61 ykipglysak tlsletndls esrtmtpqgi altekyilis ayshdhknhs viymldrqth
      121 eylktvvlpg kphlggityd pkhqrvwvtt gglfaglssi dlkeledyrm qagqvvsyhq
      181 qislkevsha savtytsgvl vvgyftldey grmatyrldn qgeltidshe kvssfdqgnq
      241 krsgvtpvps sefarslgsw ktldmiqgmt fykdylvmsq swgpdrpgki yffnldkvdn
      301 ffsikdaase mdtppyieqi tankdqlfav feggawpyrt rnpvlvdhvi qldipqllsk
      361 ke
//
LOCUS       WP_010781121             347 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar-binding transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010781121
VERSION     WP_010781121.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..347
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38315
     Region          29..341
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mlselrvlea iapdvlevvk kryrimqnif wmqpigrrnl adslglterv lrseteylrd
       61 qrlidatksg mlltekgegl lqhlellmeq ftgmdqlekq laslfsierc livsgnsdeq
      121 gkvigefgel vdealqrqlp dgrniiavmg gttmaevarh vspletakrh nlfvparggi
      181 geavsiqans vsalmaanah gehralyvpe qlseeayhtl lkepsirsvl amikeancvv
      241 hsigralhma arrkmsedei irlkqknava esfgyffden gaivhkvpri glslediqkm
      301 ptvlavaggk skvkaitaym knapkqtwli tdeaaaneil kgisplk
//
LOCUS       WP_010781116             311 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus gilvus].
ACCESSION   WP_010781116
VERSION     WP_010781116.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..311
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=36546
     Region          1..306
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdfetlfkey lldlklknfs krtiesynfh knkfirfykr eintevdilk itsydyklfi
       61 sdmldseyka tyintilktq rafwnylvne dvvkvspmak iknlketkvv lttfndaeik
      121 rmlnfwkfdg fmnarnkcii avladtgirv sellnikdsd lssqhiricg kgdkwrvvpi
      181 sdeldyfitk yrrirdnhfk nirnrnnrer kiaenlflnk tgseiktvan lqimiketai
      241 kanvresvra sphtfrhywt vknlnlgqdi ftisrilghs kldttkiyis sitdeqlitk
      301 akqtspladi l
//
LOCUS       WP_010781132             593 aa            linear   BCT 01-JAN-2025
DEFINITION  V-type ATP synthase subunit A [Enterococcus gilvus].
ACCESSION   WP_010781132
VERSION     WP_010781132.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF003220.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK04192
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..593
                     /product="V-type ATP synthase subunit A"
                     /EC_number="7.1.2.2"
                     /calculated_mol_wt=65247
     Region          1..584
                     /region_name="NtpA"
                     /note="Archaeal/vacuolar-type H+-ATPase catalytic subunit
                     A/Vma1 [Energy production and conversion]; COG1155"
                     /db_xref="CDD:440769"
ORIGIN      
        1 mqegriikvs gplvlaekme qaaiqdicyv gdlgvigeii emrgdvasiq vyeetagigp
       61 gepvkttgea lsvelgpgiv sqmfdgiqrp ldtfkeqtks nflsrgiqip aldhskkwlf
      121 epiveegval sagdivgivk etkiithkim vpngisgtlk rissgeftid ervyaietsn
      181 glqefsmlqk wpvrrgrpva eklnpeapmi tgqrvidtff pvvkggaaav pgpfgagktv
      241 vqhqiakwad vdivvyvgcg ergnemtdvl nefpelidpm tgeslmerti liantsnmpv
      301 aareasiytg itiaeyfrdm gynvaimads tsrwaealre msgrleempg degypaylgs
      361 rlaeyyersg rvialgsegr egsitaisav spsggdtsep vtqntlrvvk vfwglsatla
      421 qqrhfpsidw lqsyslysse vgkyldndlq gnwsqlvaeg mrmlqkesel neivrlvgid
      481 slsekdrltl evakslredy lqqnayddvd tftsrekqfk miqnilafnk egqralelgt
      541 ylkeimegti vlrdriarsk yiaetelekl dqikldivse iqaivaeggm tsd
//
LOCUS       WP_010781164              76 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010781164
VERSION     WP_010781164.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..76
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8601
     Region          6..65
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mkkegrlady rkragltqvq lakqlgvsqq tlssyeravt tpkpyqmqrl eeilgiskei
       61 lfhdefhkeg gnknvl
//
LOCUS       WP_010781188             229 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010781188
VERSION     WP_010781188.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..229
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=26243
     Region          116..214
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 meatkkqwwg lliiplelli gdylfpllhl dkdpkislls stglflagfl imiylfhdfl
       61 keqwqlyrhr lflklllsiv lvaiaffils fvrrmipsel lqlrssents gqtlsagwav
      121 laavspfiap faeeltfryl llgkfsngfl rivmlfvqgi lfglvhwnnf ngnvyamipy
      181 mvlgvylgli ylftkniwgs imvhwmlntm nsmfpalllf vlsffgitt
//
LOCUS       WP_010781232             333 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus gilvus].
ACCESSION   WP_010781232
VERSION     WP_010781232.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..333
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=38349
     Region          58..331
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 memkeqfins virnmepele vnqlkklkiv ltinlnhirv ekentdlviy desgdiaayk
       61 qyfvsmklrn lsngtielam rtidafqrsv kkqykdvstq dirlyiayrd mkdhlssatl
      121 nrergcicrf ytwlfeeeyi pknpakrvep ikvekrlkka ftpievelmr nacrkpkeka
      181 vfelllstgc rvteltmlam enydqqrgti tvigkgnker tvfvnarakv aidnylmikp
      241 hfegsiicgl hgvgtqmtsn giqkmvkeia krahvahahp hkfrrtaatf alkrgmslnd
      301 vrrflghtdv dttlqyidts gsdlklehek yva
//
LOCUS       WP_010781304             261 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010781304
VERSION     WP_010781304.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..261
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29942
     Region          1..255
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mtleqlihqh leelseldkd ilqfilanpe qvqssgimel atmvhaskss vlrttkklgf
       61 sgyselkyfl rhseaneqte tnekdifekq fddikktley mhsvnlepin emfdksqiiy
      121 cyatgfsqkn aidefykmml hvdkrvlvlp nkteldmvmp iitkndcviv aslsgetdei
      181 kenltafevr kipvlsvtai gdnyfarhst fhlnyycdyf vvgrrhtqaq sliglnclmd
      241 ylsrsysvyt ldkgetvatd n
//
LOCUS       WP_010781321             186 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Enterococcus gilvus].
ACCESSION   WP_010781321
VERSION     WP_010781321.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..186
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21114
     Region          2..178
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mlyvarhget ewnkqgiisg rsdialsgvg yrqaaklaee vaqldkpitr iihspleray
       61 etarivgekn qlslnvdnrl ieldygdydg tsdeqegylk trtqfalryp ngeslmdvya
      121 rivplleele qdqenvyllv chnsviraik nyfeplendk vfdyrtpnak lisfdwknaa
      181 vvsksa
//
LOCUS       WP_010781331             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010781331
VERSION     WP_010781331.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..283
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31537
     Region          1..279
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 msvlshmksm qkdmsaaekk iycfirdnse kaasmtanei aeasgssapt vvrfskkmgf
       61 nsltdfkiel saetmqkrsk ntysdvdhde sfhslkskla snarftidet talfseeefi
      121 sacklleeka fcyvlgigas nlaatdivqk wsrlgknvis epdyntilpq lvlhqkeavi
      181 wlisnsglts elialaetak dlgipiitlt qfgqnplakl sdvslrtsrp teatyrsaat
      241 dsilaqfiti dllfyvyisr nqenaekiyt traivqeyrk kyf
//
LOCUS       WP_010781415             141 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HIT family protein [Enterococcus].
ACCESSION   WP_010781415
VERSION     WP_010781415.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..141
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16190
     Region          2..138
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mencifckii nqeipsykiy eddkvyafld isqatkghtl vvpkkhvtdi fdydedlaad
       61 vfaripkiar aiehafpemd glnilnnnke layqsvfhsh ihlvpryskk ddfsihfgnh
      121 adqqtaeemq liadqikeqv k
//
LOCUS       WP_010781337             444 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Enterococcus gilvus].
ACCESSION   WP_010781337
VERSION     WP_010781337.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..444
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48696
     Region          2..430
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 menklqkqmt srhimmlalg gaigaglfkg sgeaigiagp svilafllgg lvlfivmngl
       61 grlvlssdnv qglsgiikpf lgdrtadfid wlywslwmvn iiaeavaaas fmqlwfphvp
      121 swifvlilal lttlinlysv rlfaeteywl afikiaviil livfgvylvg hevwniglvd
      181 tvsrmnshgg faphglkglv nsllvviysy ggseliaitv setedpktai pkaikgvmgr
      241 iisfyivpmi llliiyrwdt laattaspfv mvfqkmhipf atdivnfviv lalfssinsg
      301 vyassrtlyf rvkdhsgfts klavlnkhqv pqrtvlfctg tlylgvilsy flgdklfnyl
      361 vgslsysvll twmlisvaaf vlalkkgtrt erffsglvil vlglifvgil innpvgvtlf
      421 taciylaill syrkkqvdta tdqi
//
LOCUS       WP_010781435             421 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010781435
VERSION     WP_010781435.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..421
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=44603
     Region          1..420
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdkfvnfmek hfipvaskig nqrhlvaird sfmvtmplmi lgalavminn lslsipafgn
       61 fmngifgges wkgfggavwn gtfgvlsvfi aflvaynlar hygkdpiatg vvsvasfftl
      121 gaatsgmnss glfvalivgm vvaelftrlv gspklvikmp dgvppavars faslfpamiv
      181 isifgliaai iagfgvedmf aafyaavqep fmslansygs alliafitpf lwffglhgan
      241 midpfmqain apaieanana laagkaapyi vnkpfidsfv nmggtgvtig liiaiylvgr
      301 knkpfmvvnn laaapgifni neplmfglpl vlnpimfipf iltpmvcvtt ayfatkfglv
      361 ppatvmppwv tppiiggfla tqsfsgaila avnlvisiam yvpfvslatr qelkkvkeae
      421 a
//
LOCUS       WP_010781429             802 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA translocase FtsK [Enterococcus].
ACCESSION   WP_010781429
VERSION     WP_010781429.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..802
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=88732
     Region          309..795
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 maqkkrtkkk rktkkqkqlq eqrliigigl lfilftvfal fklgflgnli anvlrliggn
       61 tyqflalllg lygtllvvkn tklrltkprr wvgigffylg illilharlf anveskdpni
      121 lkttwdllmt dflgnqitqn vgggmlgaal ynlthflvsq vgsyliagll lllgiflfsl
      181 lefnqvtdyl gnfvemmqek fsesdekkel kaakreerqa qkaqakaekq aaakakleae
      241 laereknkvr smtpgeqlak esqeplvkep eqmtlvpieg fqenlepert taapvpkkap
      301 ledeeiddpg dlefeisaep edhdyqlpps tlldsipaad qsdeykkieq nikvlektfn
      361 sfgveakvvk aslgpsvtkf evqpavgvkv skivnltddi alalaakdvr meapipgksl
      421 igievpnsti stvsfrdiie sqpnhpdkil evplgrdisg lvrvadltkm phlliagstg
      481 sgksvaingi itsilmrakp nevklmmidp kmvelnvyng iphlltpvvt nprkaaqalq
      541 kvvqemeery ekfaatgvrn isgfnelviq knledgqnrp ilpfivvivd eladlmmvas
      601 nevedaitrl aqmaraagih milatqrpsv dvitgiikan vpsriafavs sgtdsrtiid
      661 gngaekllgr gdmlflpmge nkpirvqgaf isdheveqiv efvsdqqeah yeekmmptee
      721 tssspsetpq delyeeakal vvdmqtasis llqrrfrigy nraarivdel eehgvigpst
      781 gskprevfmq kaeeepenpl de
//
LOCUS       WP_010781485             399 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus gilvus].
ACCESSION   WP_010781485
VERSION     WP_010781485.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..399
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43110
     Region          6..399
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkfyvnwrss lgsifknkkr saltmfgivi giaaviails igrgferdti esltasdsdk
       61 levtidfaps ndalyssnid miqdsdfsil rtidgvesvn ypkndlsyiy kdvqvkdkkk
      121 nyrvgvvskk gkavshgrsi smydnqtqsk vvtidsslak dlfgtaksav grgftldnqv
      181 ftivgvfpsg meetmfsmgs tkiqisrqty vhffgneryt ssvvltladg sqlnkvadka
      241 ikklqdagam rqqgeyqvsn mammtdgise vlssitlfis avagislfia gvgvmnmmyi
      301 svsertkeig irralgatrg airlqflleg mtltlvggii gyllgmivay aignvmdisv
      361 svdlftvcla vgvssgiglv fsvmpaseaa kkdlidilr
//
LOCUS       WP_010781493             313 aa            linear   BCT 01-JAN-2025
DEFINITION  AEC family transporter [Enterococcus gilvus].
ACCESSION   WP_010781493
VERSION     WP_010781493.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..313
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34854
     Region          1..313
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mvsayiniff ifvlmfigyv ltykqwfsnq igdafsklvl qialpcnmfl titknfsrse
       61 flhlvsgmvi pllsmlltfv lsfayrrlfk issarkgifs tmftcsntif iglpinlaif
      121 gekavpyvll yyivnttifw tlgiyfiard npqieqatvn fhlvpilkki fspallgfli
      181 glaavlintt vpaslatflg ylanlttpls mfvigiivyn vgiknltlnk dilgvligry
      241 visplvvwil gqwiivpplm lsvfiiqsam pvqnsvpila rsydadqpfa asslgysvll
      301 ylayiplllk lil
//
LOCUS       WP_010781486             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus gilvus].
ACCESSION   WP_010781486
VERSION     WP_010781486.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..228
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25830
     Region          1..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mielkdinky yrndeeslhv lkdinlkada gemiaimgps gsgkstlinl lgfidtkfeg
       61 qylfedenli tttddrlskt rnqivgfvfq nfslienytv yenvelplly ngygfhqtkk
      121 kvmtvlekvg lsdkaekrpr qlsggqqqrv aiaralinqp kfiiadeptg aldthtsnei
      181 melfqelnrq dkvtiflvth dpevvpyctr lvkirdgait edravnde
//
LOCUS       WP_010781514             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Fur family transcriptional regulator [Enterococcus].
ACCESSION   WP_010781514
VERSION     WP_010781514.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..145
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17164
     Region          5..142
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mtqttlleka lskvkengfk ytkkretlld yliksnryva arevydylnd qfpglsydtv
       61 yrnlrefcei gliedtelqg emkfrfscse nfehhhhfic tvcgmtkeih mcpmnffkeq
      121 ldgceieghr felygrcekc qkvne
//
LOCUS       WP_010781542             186 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010781542
VERSION     WP_010781542.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..186
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21119
     Region          7..>127
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mktsrlnrei vidcamglvc esgidglrln kiadrlevks pslythtgsv telrqavver
       61 amedfrellv dslmgrsnlc afvelgktwa cyakdqnafy tvfyekgyid sykksisafl
      121 raafnriffe celsdqeviq vervmtnyfr ghaegfadns isekdlvsdl eiiyngvlkn
      181 fmkvsq
//
LOCUS       WP_010781561             145 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus gilvus].
ACCESSION   WP_010781561
VERSION     WP_010781561.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..145
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16649
     Region          10..140
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mikttneltp qelltilear tavfvveqqc pyqevdeadr savhvcieke gelqayaril
       61 aegerihfgr vlvvkkfrrq qlgrklvakt mkeiekrypd qpvsisaqah lsdfygsfgf
      121 ketseeyled giphvemlwq ksenh
//
LOCUS       WP_010781573             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010781573
VERSION     WP_010781573.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23307
     Region          8..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 makkidlrvk rtnkmimeaf ihlvelkgfd nitiqeiade aminratfya hfkdkqdlyd
       61 fifkqavdaf asvldpdqiv qgnrlkvrkv emvlkniyeq iqdnrkfflt imdasgneil
      121 rkkiaeildv kyahifnrlk itendievpl dfiieymtsi fvgtlhwwit sdttmsadsl
      181 sklvvklvgn ghltilgiei dh
//
LOCUS       WP_010781579             324 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Enterococcus
            gilvus].
ACCESSION   WP_010781579
VERSION     WP_010781579.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..324
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34215
     Region          34..307
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mkknltynli wlalivlgyv alyvaysagm vnlfldnilv qiginvilav glnliigfsg
       61 qfslghagfm aigaygaalv smsmptyggf flgmavgvil agivavavgi ptlrlsgdyl
      121 aiatlgvaei irillinfkd itngpsglfg iepfvdwqmv ygfmaittll ivnyirsgag
      181 ratmairede iaaeamgvnt tkykvmafaf gamtasiags lyagylqsia pkdfaftksv
      241 dililvvlgg igsvtgtfia aillgiinmy lqdfgtlrmi iyalaliilm ifkpggllgt
      301 kelsvkkiid kfkkgddqna svgn
//
LOCUS       WP_010781580             292 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Enterococcus].
ACCESSION   WP_010781580
VERSION     WP_010781580.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..292
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31367
     Region          1..292
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mevfiqqivn glflgsvyal malgytmvyg iiklinfahg eiymigsfig yflinqfnmg
       61 ffpalvlsma gsailgvaie flayrplrns triaalitai gvsyllqntm iyffssttrp
      121 fpqviklqvy nlgflrvsni qllilglslf lmialnlivq rtkmgkamra vsvdtdaaql
      181 mgidvnrtis ftfalgsala aaggmmigly ynsidpmmgy ipglksfiaa vlggigiipg
      241 aaiggfvigl ietlttalgf sdfkdavvya vlilillvrp agilgkhvke kv
//
LOCUS       WP_010781646             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Enterococcus].
ACCESSION   WP_010781646
VERSION     WP_010781646.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..206
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22899
     Region          11..169
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 myfysakdlt tkqnykfltg sviprpiawi ttiddttnvv naapfsyfnv vakdlplvsl
       61 sinrkehqmk dtarnllqqk egvihmvnds vlsemnhssa slpaeesela esgltlvdsk
      121 evavpaiqea pirfevrlhq yvpvsdhegt visdlfilev lnysfeeavf daekeyidpi
      181 sldpaarlag ttyshianti dlerpn
//
LOCUS       WP_010781740             479 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Enterococcus].
ACCESSION   WP_010781740
VERSION     WP_010781740.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..479
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52797
     Region          21..469
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,146,
                     149..150,153,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mhtyqedavv qknrwwilvs vamftfmstl dssivnialp tisrdlsvpm nkaewvvsiy
       61 lmvvcaclll fgkvgdsfgk ikvyrigtvv ftlgsllcgf nhsltmllfg rviqgigasm
      121 tmatntgitt evfpmrergr algaigafvs lgsiagpgig glilahfsws yifwinvpvg
      181 lltiligeky lpkditmskk kidwlgfvtf aitimsffga vfigqevgyi htvplllfva
      241 aivffvifir vekqkenpll vfhilrnklf tmslvtalli fsanffvnvv mpfylqnarg
      301 ltasyagllm mvfpflmvig splsgyltdq igpqklvlmg lallsvtqlm yvfmnqtspi
      361 wyyilataim gmgnalfqsp nntivmssve kenlgvagsl nsfarnlgmv vgialsttil
      421 ysgmstaygq rvttyiegrp dififgmrvt fmasfaicvi awvlslirfr kkttdqtih
//
LOCUS       WP_010781742             559 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease J [Enterococcus].
ACCESSION   WP_010781742
VERSION     WP_010781742.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..559
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=62217
     Region          1..551
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mstvkiipfs gvrengknmy avevdndifv ldcglkypen ellgidvvip dftylienad
       61 rvagvflthg hadaigalpy lvsevavpvf gteltvelak ltvsqneesk nfkdfhvide
      121 hteidfgtav isffrtthti pdsvgislkt segsvvytgd fkfdptaipm yatnyrrlae
      181 iggegvlall ssssnaenpi qvasereias evydtinewd griivacvas nlqrvqqiln
      241 aakkagrkvv ltgqdldrii ktgmrlkkle vpedslitik emknyspeel iiletgrmge
      301 pikslqkman rshrnlkied gdlvyitttp tiamettvak tedmiyragg ivksisenlr
      361 vsghanprdl qlmmdimspq yfipvqgeyr qlsaharlan elgmpfknif itgrgdvley
      421 knkhmsaags vpadnimidg igvgdigniv lrdrkvlsdd gifvvvvtid rklkkivsap
      481 qitsrgfvyi kasrdlikes aditseivek hlhsddfews klkqdirdhl srhlfeqtkr
      541 rpvilpvime anqrrgrrk
//
LOCUS       WP_010781760             103 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Enterococcus gilvus].
ACCESSION   WP_010781760
VERSION     WP_010781760.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..103
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11692
     Region          7..98
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mfqlfkript istqelaerm dqslslldvr taeeyrrghi akaknyplnk idryqgkeke
       61 vyvicqsgmr skqaakvllk kgynvtnvqg gmnrwqgatr ggk
//
LOCUS       WP_010781793              70 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tautomerase family protein [Enterococcus].
ACCESSION   WP_010781793
VERSION     WP_010781793.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..70
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=7815
     Region          2..51
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mphvsvklyp grskevkqaf aeklqdfvvq elgcepnvvs vsfkeidaek wkdvivdeia
       61 geetyidadf
//
LOCUS       WP_010781796             291 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Enterococcus].
ACCESSION   WP_010781796
VERSION     WP_010781796.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..291
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=31158
     Region          <3..150
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; cl46157"
                     /db_xref="CDD:480497"
     Region          <100..285
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; cl46157"
                     /db_xref="CDD:480497"
ORIGIN      
        1 maqiifyili glmifqaiml ihdiithrdd lgpgnwlisg iigfitdfad tigigsfait
       61 tmllnatkqi dddrklpgil nvghaipvlt eaiifvtvik vdaltlvsli vaamvgswfg
      121 skyvtklsek avqkwigwal litailmllr qteviallgk gntataltgv kllagifgnf
      181 lfgalmtvgv glfapcmamv ymlgmtplaa fpimmcscag lqpvaninfi rekaysrkia
      241 laitiggvpg viiasqfllg lditmvtylv iviifytgiq yilksrktaa a
//
LOCUS       WP_010781812             291 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Enterococcus gilvus].
ACCESSION   WP_010781812
VERSION     WP_010781812.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..291
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=31352
     Region          4..284
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mtqkllaidi ggssvkagiw eqeqltelps fatpktweem kaylkslved yeisegvais
       61 apgavdadeg viygvsavay lhrfpikkel aaflgmpvsf qndancaala eiwqgngkgl
      121 esvalmiigt gigggialng klrtgahlfg gefgyqilny dtletlselg spvmmakrys
      181 kikadgkkyt skdvfefaaa gealaqeqie rfyqaismgi ynvlisldpd rvlvgggist
      241 rddllpnlee rvqhlltkng akelsadimp ckfldqanli gaiyqflteq a
//
LOCUS       WP_010781821             250 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010781821
VERSION     WP_010781821.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..250
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28486
     Region          1..243
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 miihlnrnmy tslsqsekqv idfinqnekl ipslsitqla ektftspptv srtiqkcgfs
       61 giselrhkis qqmsdekrnd spfivnsile ksfrecketi dlipttsilk tieylkeaqr
      121 ififargfsa iiaeefqmyl qllgynaiiv kdvmwmkkth rivkstdmai ifsvrnstpe
      181 llesaktihr igaklvtccc lsptqledys disiighseq imeihdlkvy skiplfiiar
      241 tiidyisaes
//
LOCUS       WP_010781883             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010781883
VERSION     WP_010781883.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..283
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31869
     Region          1..273
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mqsavllkik slessftsse heiskfvien peyvisntit nlakktdtse asinrfskki
       61 gfkgfnkfki alaqsmthle dqeksfdesn lieyvtldyk kmltntcaml daqniedaas
      121 mitlnrkvfi lsiyntsfvs kefafklrql gmevttlken letqlaienm ssdsvliavv
      181 psvitkdiip fltkikrkdv ktilissndn pkvsdmidik fiipdhmsan nslvltnsvm
      241 islvfdiifa tilrdnrglr qrklssdtii nsyesadsai yew
//
LOCUS       WP_010781881             270 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus gilvus].
ACCESSION   WP_010781881
VERSION     WP_010781881.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..270
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30942
     Region          14..>131
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkksthstpn gtidlyespe nnrfvlylhg gglvygsksd lptdlktrfl tkgysviald
       61 yplapnhslk eilealektv sylldtiikd rpfgvcgrsa gsflmlhltk nlqkahvsph
      121 flvnfygytd lqfiddprel ipqkieakqi egidlkspiq ddpslsryll yhyavqqhll
      181 peyygietla efaltkeald hfprtfstas tsdkeipfry skslarsipn srfvplyyld
      241 hdflkniekp evqrlldtle ewleeqkkqv
//
LOCUS       WP_010781897             718 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Enterococcus gilvus].
ACCESSION   WP_010781897
VERSION     WP_010781897.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..718
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83074
     Region          41..712
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mftkfskdir sdlfktksde lqdketlrrl teanggnafs deqltairfp mqthlriiag
       61 agsgktqtic akaaylvleq gidpkaimmc tfsrkaklem earvnhylgg narinvqtfh
      121 gwfngeynal trrdprlnqw giegtidedq yyqtltqlik kyklynfdkf dertiasris
      181 ywrnmgysdd emvgfvekyf ddedlilnhs lstvfqqfla elamlkksqr fitfddmlfn
      241 lkqmlendad arqilqekyr yifidefqdi nplqkqiial icppdkhlkq taagkliivg
      301 dddqsiyyfr gaepryikef eqeyqqtslq lmtnyrseap iveagnrliq ynghdrlekt
      361 miankktseh ecygigfkdd deeaawigmk iqeltrqtag kdgrpnyret mvlyptrvql
      421 rsllkqlkkq kvpfvtpsnd dllgifglpp fktlfqqlel lasassiqqk nealkkiiqq
      481 yaflhfikfg asaafseklf sknkfkvkdl vaflvsernl sqasqeqakq ffkqiylfyq
      541 qqqlelaela eallatpkfk kelsdeecdw lrkeliaakd wpglleayqq aseqnqsmkk
      601 rlqdydqekl navyllsiha skglgkktvf ikgvyqdalp nhhtvekaec dlqrakeeaa
      661 ppttmeeqrr lmyvaltrak enlyvtypkt vnnktvtasp flkeaglplk eyqknsil
//
LOCUS       WP_010781950             105 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thioredoxin family protein [Enterococcus].
ACCESSION   WP_010781950
VERSION     WP_010781950.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..105
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11913
     Region          8..101
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(28,31)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 miipksieel agyaekgknv ffftadwcgd cnfikpqmpe iesmfpqfqf iqvdrdeyid
       61 vaaewsifgi psfvvvndge elgrlvnknr ktkdeiagfl qrveg
//
LOCUS       WP_010781957             449 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus gilvus].
ACCESSION   WP_010781957
VERSION     WP_010781957.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..449
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48033
     Region          11..447
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mavdqtevvg spkgelkrtm tffpalstvm gtvigagvff kaasvaavtg stslhmlswf
       61 lgglisvcag ltgaelaaai petggmlryi eraygefwsf llgwaqviiy fpanvaalai
      121 ifstqfinlf gmspsllvpi aivaatsiml inflgskagg mfqsitlvck lvplalivif
      181 glmrrgdvtv slfpvtagpa vggfapalga gllatmfayd gwihvgniag elkkpardlp
      241 raiaggilgi mvvyllvqfa flrtmnisdl agndnaamqv antifggmgg klvtigilis
      301 vygtingytm tgmrlpytmg lekqlpfsdk lvklnknqvp yiagilelvi aigmmmiggf
      361 dmltdmlvfv iwifytlvfi aviklrktep dlvrpykvpl ypiipivaii gglfilvmtl
      421 inqfqlamig ilitalgipf ymylkkkyk
//
LOCUS       WP_010781986             311 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus gilvus].
ACCESSION   WP_010781986
VERSION     WP_010781986.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..311
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34295
     Region          10..310
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mandistllk vaelyyldkm nqndiakiig vsrpsisrml eearekqivk isieapfern
       61 ntlmmqlkek ydllevivvk glgdyefdld nvgkasadyi snvlandrll giswgatvek
      121 mvknfldhel envhvvqltg slgpnrtvmd gnelvfrlaq klngrheffn apafvnsrkl
      181 qeellaqpqi dlnislgrki dvafsgigni ettrntlvss gildnrdlnd lvaegavgtm
      241 igrafdiegk eiqyrnqfpi ssgldslrla pisigavcsk kratatlgai ngklinvlic
      301 deevgyelln n
//
LOCUS       WP_010782002             607 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Enterococcus].
ACCESSION   WP_010782002
VERSION     WP_010782002.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..607
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=66942
     Region          16..445
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mdylkrllvg rplkssendd qnlsrfaala mlssdalssv aygteqivvv lvtlsaaaiw
       61 yslpiafvvl illaslilsy rqiihayphg ggayvvssen lgknagliag gsllvdymlt
      121 vavsvsagae aiasaipaly hhrvlisvii vlllmlmnlr glresagllm tpvysfiavi
      181 tiliivgvfk ivtgaaplhs taqvgavvpg ismalllraf ssgsssltgv eaisnavpff
      241 kkpraknaag tlammglilg ffftgitfln ywfgivptae vtvlsqvgea vfgkgimyyv
      301 lqfvtalila vaantgfsaf pvlaynlakd kflphryqdr gdrlgysngi itlalgsivl
      361 llifqgster liplysvgvf ipftlsqtgm vlkwhkeghh wirksianii gacisfaivv
      421 ilfvyrlpdi wpffiimpil ifgfykihgh yknvaeqlrl addvelheyd gntvivlvgn
      481 vtqvnigain yarsigdyvi amhvsleene ekekeirref rekfpdvrfs vvrspyrsiv
      541 npvsryvdrv cknakqhnyt ttvlipefvp nrtwkrslhn qtalrlrfrl syrddiiist
      601 ynyhlkk
//
LOCUS       WP_010782086             239 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus gilvus].
ACCESSION   WP_010782086
VERSION     WP_010782086.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..239
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26629
     Region          1..220
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mepiieavai kknygqqnvl rgidltilpg dflcimgrsg cgkttllkii glmhpptrge
       61 vafesrwtqs lfpdelsdir rrkigfvfqe fnlmesisvk enillpaild kqditkaeer
      121 mapffqllri eqlldklpqe lsvgekqlaa icralinepq iiladeptgn ldsnagaevi
      181 nifkrinqel gitivmithd skvaqaakev lflkdgkiyd rlvngvgset qisekmlev
//
LOCUS       WP_010782205             691 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus gilvus].
ACCESSION   WP_010782205
VERSION     WP_010782205.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 691)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..691
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=79610
     Region          14..669
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnleertnqi fvelvnnpqi tskalcekfd ltrgqlnyal kkindslvde klseikrtkn
       61 ghflitndil stykggdeql gepaesyvfs skerasiiel mllskedyls lnhfidelkv
      121 srntvlrdlk evdqelqkne lalkytrqkg yfiqgdewnk rnilsnllnn lavmyngvnf
      181 iiqfanidpq qidifrkrve lveeelevqf tderlktlpl liilmirraq kgklisysfk
      241 vnyreladtk eylaadrviw dvdglsener vyvtmllltt nlsrgdilsv keinkmkdal
      301 ekvianferi asvsleekek llerllvhmr payyrikyhl nlqtrfyqen kdanlfslfy
      361 lvkeasgple tyfgqpvpda elffislfig shivesseiv hpenrkraii vcpngisiav
      421 llentlknll peidfvtsms arefyrteyd vdfifsavpl ktekkvfvvn nflsdqekrq
      481 lrervlrsta iiqteivtpe kiltvvkkha nvtdeaslye ellslfapke skilekkrph
      541 lidllkgeti qifeeaisws evletlarpl eqqqvitkay vkalkkempi lpaytvlrhk
      601 ialphtvtea gaigvgislg lvkkgvlted grkihtvill gsndkeehld lifemmslag
      661 aeelaqleka ttkeeireal irfndeywra n
//
LOCUS       WP_010782228             246 aa            linear   BCT 01-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Enterococcus
            gilvus].
ACCESSION   WP_010782228
VERSION     WP_010782228.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..246
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=26847
     Region          102..205
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mdksykkylk ligaavaltg vislfsaagi vfnlndngii vcqimafsic gvasvlymkk
       61 keptlrafgf qkpplnkrml lfmtlivliq pglfgvnhql plstmalimv qmllvgfvee
      121 tvfrgiflyv lrnqspkvfl lfsslvfgvl hmasslnpet agilvglqii nalllglvfs
      181 liyytqrsiy tvilfhgafn vlatlsnags ieknitavll lslcygvfll yfsrgiapia
      241 nlkssh
//
LOCUS       WP_010782250             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Enterococcus].
ACCESSION   WP_010782250
VERSION     WP_010782250.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..321
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34760
     Region          3..321
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 miffqsiqsv lsiilmialg yilkrqgwfd esfgksissl itrvalpasi fvsvlknltk
       61 eslfqlsgsl iypvgaviis yilayalvki lkirpgrrgi fmnavvnant ifiglplnia
      121 lfgekalpyf lvyyvtntvs twafgvflis nddptkvkge nkaklnwkkl lpppllgfiv
      181 aivflligip vpgfinatlg yvgsivtpls llyigivlyd aglksirfdr dtvvallgrf
      241 vlapavlial iaigsnffga nlapllkqtl vvqsatpmla vlpilaneah gdvkyatnlv
      301 ttstilfvvv vpilmelvqf i
//
LOCUS       WP_010782294             430 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus gilvus].
ACCESSION   WP_010782294
VERSION     WP_010782294.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46105
     Region          1..422
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mkmknvtfke ktglflvfag napmmgllss ffliyyttvv glnpaalgtl fliskvvdgi
       61 sdpmmgffld klpitkygkf rpmlvlgtii cvinyillwf gavwfpgaky vvvyvtylll
      121 gwtfdcmdit knslipvmsa danernglal tgslgglfcg avlgiaapli vaeatlenyy
      181 ilifgsmffv licsilgall vkervafegs aeerysfkdm lkffryrpvw sffvmslvig
      241 vassigggvg tffftyiigd mtklsfvtvi slitslvgmi iapaianrlg kkkvfliaia
      301 iavstslirl ldvesmllly istffggvag gatgpllism qadntsyvqk ktgaraeaai
      361 asltsfigkm aqgiggaipg yilalfgfvg gagiqpdsvk tgiilcaiia pavintigai
      421 lfhinyrfed
//
LOCUS       WP_010782297             364 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus gilvus].
ACCESSION   WP_010782297
VERSION     WP_010782297.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..364
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40903
     Region          154..362
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkilamimlv llilavgfvg yvykknamfl palfgiggfp nikkkdyyqa dgtfrkaekd
       61 dkmaffmqhp vfggykhmff nvednvlkai apakytdflk aqgrsdqmen aleafnyltr
      121 lvesgeaqli sdinskemie qnpyqshltg mfykgkqgkp lavvvpgggf isnvtdcegy
      181 pvamklhklg ysvlvisypi gkqlgetehe kqgqaavrel vqvirylkeh eqelsvdmdd
      241 yaifgfsagg mmttaysfan yedcchkvkl prpkvifpmy gldwnvkale qdkglavfsi
      301 agredeygfg nvekrlpqlk svlgednvsv riydnlghgf gigsntivph wfeeavefwe
      361 ahrk
//
LOCUS       WP_010782332             341 aa            linear   BCT 01-JAN-2025
DEFINITION  conjugal transfer protein [Enterococcus gilvus].
ACCESSION   WP_010782332
VERSION     WP_010782332.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10576919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..341
                     /product="conjugal transfer protein"
                     /calculated_mol_wt=39059
     Region          117..336
                     /region_name="TpcC"
                     /note="Conjugative transposon protein TcpC; pfam12642"
                     /db_xref="CDD:463652"
ORIGIN      
        1 msekkskfnp qamssqpism gkketgikgk kgfslskkem kevntrairf aprtaqnvys
       61 ilfmclfvam svaillvfar vdtlariads kainkeelvs eiqtslsdns qlqfegsqlv
      121 eklftyekdk dddqawnnql apylasglsv dqlgfsttkq drktkevqfi klqtvnekrk
      181 qyrlyynvaf tegehwkkve lilpisyakk dlkiidrpqf vnvdksnsdn hvaysdrtfl
      241 pkgeevngak qteieeftkr ffelyvvnde klgliskvqg ldqaklksve psiiikeang
      301 nyfvkgtynf yyeeesifts gftleirptk dsyfvekmne k
//
LOCUS       WP_010782298             345 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus gilvus].
ACCESSION   WP_010782298
VERSION     WP_010782298.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..345
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38149
     Region          135..342
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mgkykglfwp ailgvkhmpk vkesefynva ggfrratind kiafflqhpv wegrpelfmk
       61 tgspkeiyam sgmsvhglcn ligqpaqaqs ivdgfnyvve qkglkkvhfi sglyaedevr
      121 rdpdkgkvqg ilfqgepgkp vavliagggf dgvasylesi paamelhrrg ysafvlvyrv
      181 nvelhetepq akggeaskdv lpavryligh qaeygytmdg fgmfgfsagg lmttayafsd
      241 ykdcchkhnl prpaaifpiy glhwelkvhe edkelaifsr vgrddptgfa avekiipdir
      301 kalgqenvdi vmydklghgf glgidtaaeg wlrdavafwe ehrkc
//
LOCUS       WP_010782449             321 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterococcus gilvus].
ACCESSION   WP_010782449
VERSION     WP_010782449.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..321
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35938
     Region          5..294
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 malklsvsan kggvgktlis inligairks fpsarilavd tdaqgnltks frvkvgkeqn
       61 tiydvfmgqa kveetivpty dtqidvlpan sdnnflefdk meefrdnile wfvslvkksk
      121 dnlkaissva glkkilnksi dpssnyfnal egyfdsvedn ydfiifdtpp elkqvtssvl
      181 tisdvviipy epdmngvdgv vhlisrvntl kekfnpslri ggvlgnkvyn tnvhakmina
      241 mmkytnrngy hyfdtelprs ikfadklirs gmpitmsfpd npfaqhfykl ldemnrigll
      301 sakgetldip hnlfkeseve e
//
LOCUS       WP_010782697             397 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase, partial [Enterococcus faecium].
ACCESSION   WP_010782697
VERSION     WP_010782697.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         <1..397
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
     Region          1..325
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(72,75,164..170,199,226..231,258,283..287,289)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 dntgsglila sspeakkryg itnvsrprdl pqpfpktlhv vpprmnlyik rnmqvnnifr
       61 ryvadedlli ysidesilkv tkslnlftte etrsqrrkkl aqmiqerike elgliatvgv
      121 gdnpllakla ldneakhneg fiaewtyenv pekvwnipem tdfwgigsrm kkrlnqmgil
      181 sirdlanwnp ytiknrlgvi glqlyfhang idrtdiaipp eptkeksygn sqvlprdytr
      241 rneielvvke maeqvairir qhncktgcvh lhigtsilet rpgfshqmki pitdntkelq
      301 nyclflfdky yegqevrhvg itysklvytd slqldlfsdp qkqideenld kiidkirqky
      361 gftsivhass mlegarsitr stlvgghagg nggiknd
//
LOCUS       WP_010782817             458 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_010782817
VERSION     WP_010782817.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..458
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50596
     Region          158..454
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 miknafayvt rkslksliii lvilsmstls lislsikdat drasketfan itnsfsmein
       61 rqvnpgtprg ggnvkgedik kisqtdsids yvkrinsvad lvdydiietq etlanqsper
      121 aknfkrtvml tgvndstket kfvseayklv egkrlenedk nkilmhkdla eknnlkvgdk
      181 ikiksnlfda dnekgadetv eveikglfdg hnsgvvsaaq elyentlitd ihtaakvygn
      241 tedtavyqda tffvkgdknl dsvikdlgkl dinwreynli ksssnypalq qsisgiysis
      301 nklffgslif agvvvslllf lwmnarkkei avllslgisk leifgqflie mvfisipafv
      361 gsyflaqyta dklgnnilnk vtgdiakqia kqsassqlgg gaeaegfnkt lssldinvlp
      421 kfmiyvvifm slvllvslii ssfnilrrnp kellidnn
//
LOCUS       WP_010782821             204 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecium].
ACCESSION   WP_010782821
VERSION     WP_010782821.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..204
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23381
     Region          2..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(7,9,65..66,69)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            9
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(64,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(70,75..76,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93..95,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..199
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
ORIGIN      
        1 mrvayirvss idqneqrqie emkkfgaeri fiekqsgati thrpvfqeal dfvrdqdifi
       61 veaidrlgrn ydeiiasvny lkkknvqlii tslpimaeai gnplldkfik dliiqilami
      121 aeqerteskr rqaqgikiak angvykgrpk lysanakdpq rrlvyknive dlkkgvaiak
      181 iakdynvtrq tvyrikkdsm vndk
//
LOCUS       WP_010782949             271 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Enterococcus faecalis].
ACCESSION   WP_010782949
VERSION     WP_010782949.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..271
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=30253
     Region          5..270
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mnvylflalf fiiigilsys ffiepkclvi hknqikvtes gktlrivqls dihlkknysv
       61 kalkqivekt ntlqpdivvf tgdlfddyar fgieiqdevs qlfrkinapy gkfaiygnhe
      121 ysgldtnfye tileaadftv lkntgkllpv shrislyvag ledslygqtd laaalvnrpt
      181 gtptlllthe pdvadsavnk nidlilaghs hggqirlpff tyknqlakky thglyhlede
      241 tpliihpgig ttkisarfgv lptielielt i
//
LOCUS       WP_010783009             752 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Enterococcus faecalis].
ACCESSION   WP_010783009
VERSION     WP_010783009.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..752
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85993
     Region          235..723
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mqgnnlfnng llqpkkppig qeqqkmtryh qlrlvfglvg vllypfailg siplliglav
       61 dkrdkaanvf dmdyesflkr nsivflsfsa vlfvinvfaf ilwiprgyls ayllfplnll
      121 htalrfnwet ivalligssg mgaiflafss fvakrkvisk ederkkvtes keyknrqknk
      181 feesqrftde qekeyqeave svdidkykel snqlllgmse fglsyimnfs efnqhvlvpa
      241 ttgsgkttll qllvqhavkf nfpvilidgk gardtlesmr eiakfydkev haftddgdmr
      301 ynpvehgndi sirdklvsla etesvfysga akallqvtiq lldefkgakv tlsgdtrtte
      361 tverslpfvq rfllprnvlh lfadailpnn pklfeievek kiqqpkkksa kegskilpds
      421 dldkeekeed sqiknskfrn isqlgiaqke tetivlnpet ldldsyylll krnlrylptd
      481 ketgenikqk lferlfirye hkdspfylya tsealqtnin mlldselgkl fdtknaknvl
      541 dvqeivnqrk lvyvsfngli ykeyirtlaq mligdvnyfa semyrknvkr evlvifdepa
      601 sylnetfidm vnkgrgagvy giftpqtmad iaklgdklme qlvgnvntlf igktnekgea
      661 eywsetmgty qdidvtsvte qedgysdvgk sdwsgdrgtk rnvdrfkisp nkikelrtge
      721 fiiyrtaenv nlppqkvyvr nalewlqksn sk
//
LOCUS       WP_010783097             455 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecalis].
ACCESSION   WP_010783097
VERSION     WP_010783097.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..455
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=53437
     Region          5..386
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 maneikrval yirvsteqqa khgdsldeqq htlneyvrqq gnmkvfktyi ddgisgqkly
       61 rdefqklldd vkkgridtil ftkldrwfrn lrhylniqei ldknnvtwla vtqpffntet
      121 amgrsfvnqs mgfaeleaql tseriravfd nkirkgevvs gkvplgyeik dkhlvpneka
      181 eivkeifqyy letgsmratv rhlenhfnmt rdyqsvrqml tnrkyigelr dnknfcepii
      241 drdvfervql qlsknirmnk krdymftgll vcsecgcnys atavisryvr kdgttnpner
      301 hlyrctknrn nakkcsnkkg iyettlekfl leniekqaee lsvkmqqepd vkktkntndk
      361 ikkkidrlkk aylnevisle eykkdreele allipepnnk iakidlnllh nystaefrdg
      421 ykqltiseks slwrqvikni vvypdgnlki nflgy
//
LOCUS       WP_010783149            1045 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus faecalis].
ACCESSION   WP_010783149
VERSION     WP_010783149.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..1045
                     /product="DEAD/DEAH box helicase"
                     /calculated_mol_wt=120277
     Region          237..>698
                     /region_name="BRR2"
                     /note="Replicative superfamily II helicase [Replication,
                     recombination and repair]; COG1204"
                     /db_xref="CDD:440817"
ORIGIN      
        1 mliennskyy lkkvqakskm feynvpleeh iqveymaqel ivlaiatigd asnfiwdnry
       61 tefssklnne lfenlnftsi yfdslltsei geasyndyfg llgaisfyls dalgstkvmi
      121 nkidwamdle ineidtflly lladrldelk gyefssqygn lfyyliydls qfyldgtpid
      181 feklndlkqe iylsqnprei lfgdsllavf ikkyknsaln llpnysdtti qdwedlllnn
      241 htikelwpsq illgeknifk gksgviqmpt ssgkttsigl iirsafithr tklavvvapf
      301 kalckeitln lieffsndev iinelsdiae kddiaffdnd iatntliilt pekllflirn
      361 nseileelnl iifdeahlfd dssrgtnyel lvstiryyln essqkilisa viansevine
      421 wlngtdgevi snnniissqr siaigdwmgq tgqlyflnqd npdiddfyvp rivdireinr
      481 ldrerakryf pdvdfrkrkl nkpydmqiyy alkmvhngat aifsgtkkta dktierllel
      541 eergldisaf snevsqnent kiaslinmnl gsdteyyisa lkgifihhgn iplgirlsve
      601 yamsqnlinf vvctstlaqg vnlpikylii sslyqgksqm kvrdfhnllg rvgragkhie
      661 gtvilsepfi hsnksnwkwn ryknmldidn sedsesnllk lvrpiiidkf ppinlwnvlp
      721 qkytnqeqfn dvinkiktvi snsnfpnkis dfnfelkiil dilkdvenyv myfvkyfkds
      781 npnftnmvtq qtlgyhlasd sekeklvelf eviktyslsf teaelslysi sslgfdnskv
      841 lsqwisekie nitqarsefe lidiifpqli lfsenniinr iddtsiftqi celwtqgqny
      901 sdilnycqsn qfqiskrnql vplilqdiie icdnilayst ilplngvatf mensendstl
      961 hlikslqkki ryglpsnlsi nifelgfsdr viaqilarii ensssftits iskritkell
     1021 rqnkreieea lkvfpqyfld ilrki
//
LOCUS       WP_010783104             275 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein, partial [Enterococcus faecalis].
ACCESSION   WP_010783104
VERSION     WP_010783104.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         <1..275
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          21..267
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 eelrrilnnk neaiiilnny fkggvgkskl stmfayltdk lnlkvlmidk dlqatltkdl
       61 aktfevelpr vnfyeglkng nlassiihlt dnldlipgtf dlmllpkltr swtfenesrl
      121 latllaplks dydliiidtv ptpsvytnna ivasdyvmip lqaeeestnn iqnyisylid
      181 lqeqfnpgld migfvpylvd tdsatiksnl eelykehked nlvfrniikr snkvstwskn
      241 gitehkgydk kvlsmyenvf femieriiql eneke
//
LOCUS       WP_010783197             361 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010783197
VERSION     WP_010783197.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..361
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40858
     Region          1..344
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mrnhvisfen vvkqfddepv lknvsfeiee gkfytllgps gcgkttilri iagfndvtsg
       61 dvyfdgkrin dvpankrqvn tvfqdyalfp hmnvfdnvaf glkikklska eiekkvkeal
      121 rlvqlpgyet reisemsggq rqrvaiarai vnepkvllld eplsaldlkl rtamqyelrd
      181 lqqrlgitfi fvthdqeeal amsdeifvmn kghivqsgtp vdiydepinh fvadfvgesn
      241 ivdgvmledn lvsfvgkkfe cvdggmrkne pvevvlrped ltittlekgk ltvtvdtqlf
      301 rgvhyeiicf deqgnewivh strkakegaq vglsfepedi hvmrfnesee dfdarlesyd
      361 e
//
LOCUS       WP_010783223             337 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus faecalis].
ACCESSION   WP_010783223
VERSION     WP_010783223.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..337
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37750
     Region          79..336
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkrkivrfil wllgiivvic lgvflafqls pkpgawvinq lfageveikd sasydkalpn
       61 vqfqenqtyp ssrkkntfdl yypqtskqav pvvlwvhggg yvggdksgmk efatrlvads
      121 svafismnye lapdapypsq lqqvnelvqf llekkqaypm ldlsklfigg dsagaqialq
      181 yatvqtnany akelgmtaal pashlkgtls ycgpvdlkqm anqqsdnrfm kffvktvaws
      241 llgtkdwqts velqevslvd kvtkefppty ltdgnsfsfq eqglalvqrl ktlnvpvsal
      301 ffkdkkatit heyqfdyqtk eakqcyqetv qfvntyk
//
LOCUS       WP_010783326             154 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus faecalis].
ACCESSION   WP_010783326
VERSION     WP_010783326.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10084616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..154
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=16696
     Region          7..143
                     /region_name="USP-like"
                     /note="universal stress protein (USP) and similar
                     proteins; cd00293"
                     /db_xref="CDD:467483"
ORIGIN      
        1 mlqqyqkimi aidgsdeadl afkkavnvak rndaelllah vvdtrsfqsv ssfdgalaee
       61 amsmaketld tyqqqavdmg qtkvssvlay gspkniiake lpkeynidli mlgatglnav
      121 erlfigsvse svirnascdv lvvrtdldnk lpkk
//
LOCUS       WP_010783390             204 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecalis].
ACCESSION   WP_010783390
VERSION     WP_010783390.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..204
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23776
     Region          3..132
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,63..64,67)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(62,113..114,116..117,121)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(68,73..74,109,112..113,116..117,120,123)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,96..97,109..110,113..114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(91,114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(122,128..129)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 makigyarvs svdqnldrql ellsqcdkif tdkasgkdtn rdgfqemmkf iregdiivvt
       61 elkrlgrnnk eltetmnliq lkkatlevln lpaltgitdd nlrrllnnli ielykyqaee
      121 erryiretqq qgitlakakg kyrggkpkyr endprlqlaf klflagstdk eveeqtginr
      181 rtfrryrmky gitdenrkkh knek
//
LOCUS       WP_010783392             438 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus faecalis].
ACCESSION   WP_010783392
VERSION     WP_010783392.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..438
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=48923
     Region          14..364
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(17..18,21..22,57,60,116..117,172)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(114,117,201..207,236,263..268,295,324..328,330)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mkfdyskepr rdvlcidvks fyasvecver gldplktmli vmsgadnagg lvlaasplak
       61 kvlgisnvtr kdevpdhpel livpprmnly mkrnseinnl lkrfvadedh svfsvdesfi
      121 ditaslkyfn cdtayrlaki iqrviynhmg lyvtigigdn pllaklaldn eakntpgfva
      181 ewryenveek vwtispitef cgigkrmaar lkmsgiesiy dlahadpyil kqrfgvmglq
      241 lyahswgidr sflgekrqva keksfgnsqv lprdyarrdq ielvlkelsd qvatrlrnsn
      301 cqtecvsifv gyskgqvdgl grsgwrkqlk iarsnntkvl tehvlklfrd nyvpgmdirn
      361 lgvsfgklvw dttlqldifs ppeeqiinnq ldflidkirq kfgfkaliha ssllegatav
      421 nrsglvggha ggnvglgg
//
LOCUS       WP_010783467             345 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010783467
VERSION     WP_010783467.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..345
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38328
     Region          25..341
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mlkefkmiea vapdmldvlq erfqilrniy wmqpigrrsl setmgiterv lrtetdvlkq
       61 lnliepsksg mtlterglev yqglelvmnq llgmhqieke mtqyfgiqrc ivvagdsdiq
      121 kkvlsdfgdv ltntlnlllp ngentiavmg gttmamvaen mgsletekrh nlfvparggi
      181 geavsvqans isavmanktg gnyralyvpe qlsretynsl lqepsiqevl tlishancvv
      241 hsigralhma arrkmsddem vmlkqknava esfgyffdee gkvvykipri glqlknlqei
      301 pyvvaiaggk tkakairaym enapkqtwli tdeaaaneil kgvtl
//
LOCUS       WP_010783753              66 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Enterococcus].
ACCESSION   WP_010783753
VERSION     WP_010783753.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7118
     Region          1..63
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mnngtvkwfn sdkgfgfitg edgndvfvhf saiqadgfks leegqavtfd ieegqrgmqa
       61 vnifka
//
LOCUS       WP_010783638             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Lactobacillales].
ACCESSION   WP_010783638
VERSION     WP_010783638.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillales
  ORGANISM  Lactobacillales
            Bacteria; Bacillati; Bacillota; Bacilli.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Lactobacillales"
                     /db_xref="taxon:186826"
     Protein         1..255
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28565
     Region          2..253
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 makiiafynn kggvakttta tnvagvlslq kkkvllidgd pqghtsltfg vdsddlqttl
       61 gaylssnwta seasqyfiki ndfldvipsn qslsdfiilt ssedpkirnk hlknfinpir
      121 keydyiifdm apavdiilen iveivddlvv vatpetyavk naettlkitd dkqvtvrhiv
      181 ptktqmntkt hkfmlenlqe vadshhinmt ktyipnliaf seavsiyelp lalvndkryl
      241 kaqeyyqnlv eelgy
//
LOCUS       WP_010783877             108 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Enterococcus faecalis].
ACCESSION   WP_010783877
VERSION     WP_010783877.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..108
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=12380
     Region          13..>61
                     /region_name="T4P_ComGE"
                     /note="competence type IV pilus minor pilin ComGE;
                     NF041013"
                     /db_xref="CDD:468942"
ORIGIN      
        1 manirrklti ysgfillesl vgfsivcvia gifsltitql iqqnyqreqe ltrtrlgyea
       61 ilfleqtgdl rfkeriyqge tyrfslmend grrilkvtds rgailigq
//
LOCUS       WP_010783963             233 aa            linear   BCT 01-JAN-2025
DEFINITION  XRE family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010783963
VERSION     WP_010783963.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..233
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26444
     Region          4..>69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          116..232
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 meseklskyi gqkiklyrsk knltqeelar kvgtkkatis nyetgyrspq qdmlfelanv
       61 ldisindlfp pssnsknnhs sietiyekle pyrkekvytf aeeqlheqet vnnkviplvg
      121 ksaanpavle ygdtdieqqs fahvpdnadc aiyiqgdsme plikngsivf ykkqcdveng
      181 eiaiveidgd gvtckklikd yeneriilrs inkkyddrvl kceeiriigk vvv
//
LOCUS       WP_010784149             304 aa            linear   BCT 01-JAN-2025
DEFINITION  permease [Enterococcus faecalis].
ACCESSION   WP_010784149
VERSION     WP_010784149.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..304
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=33703
     Region          5..304
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mfqflpnsvl qmstiflsii iealpfvmlg clisgalhvf ltpervkkvl pknkflsicv
       61 gsflgfffps cecgivpivh qfvkkdvpth tafafmltap iinpivlfst yvafsgatkf
      121 viwrvlgsmi vawiigiwla yfrkesilte kelaqikeeq vahthehvde arsfwkngws
      181 althsideff dtgrylifgs llaaimqtyi ptgalmqlgh skilailvml viaatlslcs
      241 eadafigssl lslfgtgpiv aflvfgpmvd iknllmmkry fkmsfivqfv livalvvtiy
      301 aavv
//
LOCUS       WP_010784257             344 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Enterococcus faecalis].
ACCESSION   WP_010784257
VERSION     WP_010784257.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..344
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39027
     Region          199..325
                     /region_name="FUSC_2"
                     /note="Fusaric acid resistance protein-like; pfam13515"
                     /db_xref="CDD:433273"
ORIGIN      
        1 meqsffrell hyqrpkdnpf rlvfaglvmf silflgyinh qllissfgsl giftflyyqp
       61 lplkqlmtrl svvgsylflg nllgmlsthi awlipivval vgfggrfffe vydiskpgaf
      121 fgvmvtamga stsiplakip fmsgcmllgi gfsilfalvl hftekeisap lakrslreri
      181 yrhreaplds iyysfvlffa vyiseslhlq npywlvvsca silqgdnlra ikqrniqrif
      241 gttiglvisa fllnlalttf esivvitilf vtveyfirrn yglaqffttp malmlsllvr
      301 qqyvitliqf rflgivlgsl lglaaawlft vvvtfyerky hlne
//
LOCUS       WP_010784274              78 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010784274
VERSION     WP_010784274.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..78
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9001
     Region          19..78
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 msvkqidkka lkvqyllpkt klkevrrlkk vttaeiakvi gvsrehyekk eagkypfqdy
       61 emilisqelg eevsnlff
//
LOCUS       WP_010784380             142 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ImmA/IrrE family metallo-endopeptidase
            [Enterococcus].
ACCESSION   WP_010784380
VERSION     WP_010784380.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..142
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=16609
     Region          54..141
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mnyyveetfn kiidlyhpys vyqlikeanc kllyadldde tggctqtnnr chtiivnanw
       61 peyyqqfvil hefshiklhs gsstpfyrsl gldsfiskme ceanslamkl liymqdqdvl
      121 enltefqimd ylglppelrr yl
//
LOCUS       WP_010784550             377 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010784550
VERSION     WP_010784550.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..377
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39502
     Region          1..356
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mnnrsekirn ilvpvlsvim gfllgaiimv ifgydpvagy qamfetafqg nksigeifvt
       61 aapliftalg fsvansagff niglsgqalc gwvasiwval smpdaprmia lpvaiivgav
      121 agalaaaipg flrayfgtse vivtimlnyi llytgnhian nvmkpsiman kgitkmigan
      181 aslrspflts isdgsrlnig iflafiflil vwflmkkttl gfeirsvgln pfaseyagms
      241 skrtiilsmm isgtlaglgg avqglgtfqn ffiqntslsi gfdgmavsll gagssigill
      301 sallfgmlkl ggqgmpliag vptelvdvvi aaiiffvgis ylirfllaka sgskkevaiv
      361 etieaapdkn nqeggdi
//
LOCUS       WP_010784686             455 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Enterococcus faecalis].
ACCESSION   WP_010784686
VERSION     WP_010784686.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..455
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50663
     Region          13..437
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mkhqikrrly ispvqtivlg ffllivvgti llmmpfsaqa gqktqwidaf fvatsavcvt
       61 glsplntaeh wspigqviim ilielgglgf ltvatiffsl lrkkaslsvr mlyqealnvs
      121 evsgvfrlmk yimkfaaiiq llgafllsfq fvptfgwkkg mffslfhavs afcnagfdll
      181 gdsmvpyqns pylllvisfl iiagglgfiv wrdifamikg yknkikhrvs ihtrlaltvt
      241 atflvlgtvi fyiseyrhfp admsfwqrlv nswflsvtpr tagfysvdys kmsnpglivt
      301 ilwmfiggts gstagglktt tfgvlflqfr aifkgkqrve fhertiperv vlqaftlffl
      361 atflcvtasv ilsftetlpl kngieyivfe visafgtvgl tmgltpdltv fgklviiflm
      421 fvgrvgvytv llslikkgle sqskvqypke svmig
//
LOCUS       WP_010784741             556 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010784741
VERSION     WP_010784741.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..556
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=63956
     Region          6..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          238..552
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mmtvndllha eelpgltllt hetnldapil qanilenpda fdwltpgeil lttgyifkdq
       61 pclqkrliqe lanmncaalg fkvqryfnev pqemiqland vglpilsipy nynfsqiisl
      121 vnrrvnqpde tisqhsvhmh nkfytiikag gkstqllevl saaiqapvml lderfqimnh
      181 fdlpdaptri tsilnsatlk kqfetalkaq nnelllfyke pltvefslan hqlslrilpi
      241 kkknlslsyl viwqttkklq tidllsvevc ahyllpqlql essenlttrq kigalfqdli
      301 qekntnpqaw qefskylqln ekdtfslllv aieqleqlfn ptiqmnsigh qlnhilegyr
      361 qkitafptqt gfilllenpa qeeatylaqt thlaknlleq lmklnpklsf klaigptvkk
      421 itnlcdsykl aqetfhlaqa sqelqqrtil nyddlffyrl mietltkqak qkiyqrliep
      481 lekedqkhes slletintyf qsnknislta tnmyvhrnti iyrlkkieei lhltlefpds
      541 slqlslavyl ykqkll
//
LOCUS       WP_010784759             249 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Enterococcus faecalis].
ACCESSION   WP_010784759
VERSION     WP_010784759.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..249
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=27089
     Region          64..246
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mkhkkmlava svaaftllla gcnttnnkgt tatsdsvaks sesktkdsvd lnsldlpqld
       61 dkvaedqdlv qmvtsmgnie iklfpkqapk tvenfmkhak dgyydgltfh rvinnfmiqg
      121 gdpsgdgtgg nsiwnkpfed efsnqlynir galsmanagp ntngsqffiv qniddqsdgl
      181 lyddypkaii daykkggyps ldkkhtvfgq vtkgmdivdk iakvevgand kpktdvkiek
      241 inilqeakk
//
LOCUS       WP_010784814             435 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus faecalis].
ACCESSION   WP_010784814
VERSION     WP_010784814.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..435
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=47162
     Region          1..431
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdkltnwveq tvvpkvsrit slryfqalrn gffaimplti igsifmlitd fpvagygdfm
       61 agifgagwad mispayratf nmmgiifagt msyklaesye mdrltslilg ivayvvvlpk
      121 tvttesgevv tkvlsfdwlg tqgvitaiim silsveltrf cikkklvikm pdsvpsmvsq
      181 afsalipgif vvavalling iglsfadsfp qliyaviqap lqgligtpfa iiivaglngl
      241 fwwfgihptv insmlypily anadknqsla elgqltaqng nfgtvqmldq fatiggagct
      301 iglaiamviv ghssrmkams kisfvpaffn ineplifglp vifnplllip iavapivsvl
      361 iaflsmkigf mpmftniqap watpflfsgf lvgkwqgavt qvlavaasvv iyypfvkald
      421 rqyqkeeahe vpetl
//
LOCUS       WP_010784782             236 aa            linear   BCT 01-JAN-2025
DEFINITION  ion transporter [Enterococcus faecalis].
ACCESSION   WP_010784782
VERSION     WP_010784782.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..236
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=26728
     Region          6..188
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mkinqkiyny svvilalisi alvifdfsnv inisdppfni idnfilitft idyivrfiis
       61 knkikffken ifdliaiipf daifsffria rlfriakiar lakltraigv vgkltrntks
      121 flnviylssv livisamiys yaenvpyida fwwalvtttt vgygdispat plgrvaaiil
      181 milgigfigm ltstiteyfn ksnnedeesn dkieilinki dqlettieql keeikk
//
LOCUS       WP_010784918             326 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus faecalis].
ACCESSION   WP_010784918
VERSION     WP_010784918.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..326
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37199
     Region          7..190
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(10,12,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(45,97..98)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            96..98
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mkkkilisip ayneannirp lykklnetle ekrdevdfei lfindgskdn tvsevlslie
       61 qtdnvslidl srnygkeiam sagfdysthd avitmdadlq hppatiidmi dlwqqgyedv
      121 yakrnqlkge swfkktsskw fykvlgklan tpvlpdagdy rlldrkvvea lkqmresqry
      181 tkglynwvgf kkvaiefdad erlhgetkws fgallklaie gitsyttapl kismyfgflv
      241 sfvafvymiy vliktlifga dtsgfpslmi milflggcql isvgilgeyv grvfletkkr
      301 plyfveniys lpkknetkes elkeid
//
LOCUS       WP_010784940             575 aa            linear   BCT 01-JAN-2025
DEFINITION  terminase large subunit [Enterococcus faecalis].
ACCESSION   WP_010784940
VERSION     WP_010784940.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..575
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66098
     Region          1..573
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 miepgvnyad lfakevrkhp kkypktvrla idrwyrwkkr kdiwfdvdra nemmdwvesf
       61 ivhtkgdmvg kpfllepwek fiyswiygwv kenekgqvvr vtreayvqip kkngktliav
      121 galgyamyge galsvdcyac asdfaqaqya akpfaatiln npvlldgtki fkgpkgtvss
      181 itydylhgdm aytnkfivqt knidniegsn pyfvlndelh kqekmeqydn fksaqislpq
      241 plmfnistag kgsssvgirv ykeakevlkr ddndsnfvli yepnkgydwt dkkvwemcnp
      301 nlgisvdlsa lesafktaqr sahskaeflt khldvfvnga dnffeqdqve pclvptnelg
      361 nlsgepcwig ldlsksrdlt cvslnfptwd aegkailkvk qlyfipseni dfrekednvp
      421 yselaeqgfv efcdgklidq eqifhfiedc mdfydvqqvn ydpamsdrlv eklenlglec
      481 vqvdqyarvl nspledaerl fyeqrimfdn plflycalnv vvkmdfqgrk vpsknqskrk
      541 idgfvaflca hketmdqmid vneddmdeyl dsiyr
//
LOCUS       WP_010785054             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Enterococcus].
ACCESSION   WP_010785054
VERSION     WP_010785054.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 264)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10586710
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..264
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29998
     Region          <1..39
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Region          28..227
                     /region_name="AAA_12"
                     /note="AAA domain; pfam13087"
                     /db_xref="CDD:463780"
ORIGIN      
        1 mvgdhkqlpp iinefdanii kntsseklse slfedlflla kdsdiaitls kqfrmhpais
       61 kminkvfyld dgvvittdit peerrlnyri akpvvwlste rlqnnqqkkt tsksftntce
      121 aniilmeleh ledsnstnek ikvgvisays gqksllekli kpsntrwenl eivienvdaf
      181 qgsevdvviy svvrsnankd igflseqrrl nvalsraksq viivgnahfm keaskkehny
      241 fedvliyinr yktdcelevi qsgi
//
LOCUS       WP_010785112             113 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Enterococcus
            faecalis].
ACCESSION   WP_010785112
VERSION     WP_010785112.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..113
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=12972
     Region          8..113
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mnvekkyipk kgdivwidfd paagkeiqkr cpglvvsrye fnrktmfavi cpitstikni
       61 ptrytlpddi etqgqvvisq lksldfterk lsqiehlplk dmakidqiie yif
//
LOCUS       WP_010785081             590 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Lactobacillales].
ACCESSION   WP_010785081
VERSION     WP_010785081.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillales
  ORGANISM  Lactobacillales
            Bacteria; Bacillati; Bacillota; Bacilli.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449397
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Lactobacillales"
                     /db_xref="taxon:186826"
     Protein         1..590
                     /product="recombinase family protein"
                     /calculated_mol_wt=68093
     Region          17..394
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
     Region          448..509
                     /region_name="Zn_ribbon_recom"
                     /note="Recombinase zinc beta ribbon domain; pfam13408"
                     /db_xref="CDD:433183"
ORIGIN      
        1 mkviqkiept kpkiakrkrv aayarvsvdk grtmhslsaq vsyyskliqk npdweyvgvy
       61 sdggisgrtt esrnefkrli kdckdgkvdi iltksisrfa rntvdlletv rdlrainvev
      121 rfekenihsl sgdgelmlsi lasfaqeesr sisnnikwsi qkrfkegkhn grfniygyrw
      181 vgqeliveps eaeniklmya nymnglsaef takqltkmgv tamkggpfka tsvrqilkni
      241 tytgnlllqk eytpdpitgk srynngempq yfvenhheai ipmeewqavq derlkrrklg
      301 aranksintt cftskikcgn cgknfrrsgk rqgknkelyh iwtcrnksek gvkvcnarni
      361 pepalkkyat evlglevfde qifidsieei vasegnmlqf kfyggrevev kwtstarkdy
      421 wtpevrraws ernkrkesrt wngrtteftg fvvcgrcgan yrrqavtskt dgtvrrkwhc
      481 snsavacneg ksrnciyeed lkvmvaeilg iptfneptmd eklsrisiid tevtfhfkdg
      541 hdevrtfeip kkkartfsee erarrrlvmk krweekkrde esnndtsdnh
//
LOCUS       WP_010785116             260 aa            linear   BCT 01-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Enterococcus
            faecalis].
ACCESSION   WP_010785116
VERSION     WP_010785116.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10053807
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..260
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31296
     Region          16..83
                     /region_name="HTH_ARSR"
                     /note="Arsenical Resistance Operon Repressor and similar
                     prokaryotic, metal regulated homodimeric repressors. ARSR
                     subfamily of helix-turn-helix bacterial transcription
                     regulatory proteins (winged helix topology). Includes
                     several proteins that appear to...; cd00090"
                     /db_xref="CDD:238042"
     Site            order(17..19,33..35,44..45,50..51,53..54,57..58,60..61,
                     67..69,74..76)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(33,36,83)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mkpllynyyi dytkkdktrl iilcllhelr visvqqlidf fqierlsaes tvykhlnllk
       61 tdgliarskn gmhtfyyltk eghnyiggyy tlpkvpeynl qhhlqindyl ikmlelcnnh
      121 phlkavvser rkvyevkdek knqkgvkyfv pdfifmflds igrevewqfe ieltlktkrr
      181 ysqgvfpkyi khlknyedar liyvtpssii keeldmfkey fidkegdeyk evfdrlhvfs
      241 aeefepnmkk lieedtfinw
//
LOCUS       WP_010785171             438 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus faecalis].
ACCESSION   WP_010785171
VERSION     WP_010785171.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..438
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=48965
     Region          14..364
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(17..18,21..22,57,60,116..117,172)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(114,117,201..207,236,263..268,295,324..328,330)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mkfdyskepr rdvlcidvks fyasvecver gldplktmli vmsgadnagg lvlaaspmak
       61 kvlgisnvtr kdevpdhtdl livpprmnly mkrnseinnl lkrfvadedh svfsvdesfi
      121 ditaslryfy cdtayrlari iqrviynhmg lyvtigigdn pllaklaldn eakntpgfva
      181 ewryedvqek vwaispitef cgigkrmaar lkmsgiesiy dlahadpyll khrfgvmglq
      241 lfahawgidr sflgekrqva keksfgnsqv lprdyarkdq ielvlkelsd qvatrlrnsn
      301 cqtecvsifv gyskgqvdgl grsgwrkqlk iarsnntkvl tehvlklfre nfilgidirn
      361 lgvsfgklvw dttlqidlfs ppeeqiinnq ldflidkirq kfgfkaliha ssllegatav
      421 nrsglvggha ggnvglgg
//
LOCUS       WP_010785188             166 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Enterococcus faecalis].
ACCESSION   WP_010785188
VERSION     WP_010785188.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..166
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19529
     Region          3..>152
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtyknivfdl ddtlydqqlp fkrsvekcfp tidiqqidni ykrfrywsnv afpkytkkli
       61 sieklrifrc qktmeefgid sisrtealdf qadyeldqit mipeihqlll alhknripig
      121 iltngpvdlq srklqnigay qyfekqniii ssplteelqk iamkvm
//
LOCUS       WP_010784904             348 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010784904
VERSION     WP_010784904.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Hoskisson,P.A. and Rigali,S.
  TITLE     Chapter 1: Variation in form and function the helix-turn-helix
            regulators of the GntR superfamily
  JOURNAL   Adv Appl Microbiol 69, 1-22 (2009)
   PUBMED   19729089
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..348
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=38536
     Region          1..>92
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
     Region          97..338
                     /region_name="PBP1_LacI_sugar_binding-like"
                     /note="ligand binding domain of the LacI transcriptional
                     regulator family belonging to the type 1
                     periplasmic-binding fold protein superfamily; cd06267"
                     /db_xref="CDD:380491"
     Site            order(97..98,101,138,163,176,213,237,287,304)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380491"
ORIGIN      
        1 mkqplyqqii dylqneidsg rlpvgaqvpt ekelsaqfnv sritskralt eletqgviqr
       61 hqgkgsfvqa pkhplhtsln kvlfllpfad dlsvgnfysg laptiqaagl evfmtspnfl
      121 reknaadivn efaglvyyaa tsndyldllf elalmnfpvv vldkkihdlp fvtiqsdnfa
      181 ggktaterli glghtkigyi lsgspalqsv rqrylgylqa lkeanlafht aitetnllde
      241 hnfkqyfeah qltavvcdnd fsalhclrnc knlgihvpee lsiigfddiq aaafvepplt
      301 tmaqdfkemg klagevllqt mqqdiqiied iqvpvtlier etistvsk
//
LOCUS       WP_010785362             220 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010785362
VERSION     WP_010785362.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25115
     Region          7..146
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mepklskdti iaaafsllek sptleqlsmr kvakqlgvqa paiywyfknk qallqsmaea
       61 ieehfqepal cgewysdlla fmenyydlyq qfpcavaiei qtvpaypqrl rhlnqmmgil
      121 reagfspemt hlavtslqhl lfgmimdate ekqlvlqvln gddylkeqal hmkqyvsdng
      181 ltymeesiqf rrsihqksaf iqavktyldg lqayntsssk
//
LOCUS       WP_010785828             437 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Glaesserella parasuis].
ACCESSION   WP_010785828
VERSION     WP_010785828.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..437
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44950
     Region          5..434
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 msllsrfqle ergsnvrqev iaglttflam vysvivvpnm lsaagfpads vfiatclvag
       61 lgsiliglwa napmaigcai sltaftafsl vlgqgisipv algaiflmgv lftivsvtgi
      121 rawilrnlps siahgagigi glfllliaas gvglvvsnqa glpvkmgeft sfpvmmslig
      181 laaiiglerl qikgsilwvi iaitiiglif dpnvkfggev fklptfgens qflnldivga
      241 lnaailpvvf alvmtaifda tgtiravagq anlldkdgqi ingdkaltsd slssvlsglf
      301 gtapaavyie saagtavggk tgltavvvgv lfllmlffqp laflvpgyat apalmyvgll
      361 mlsnvskldf ddfigamsgl vcavfivlta nivtgimlgf atlvigrtis gefnklnvgt
      421 vaiaialvaf yafgfai
//
LOCUS       WP_010785862             350 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Glaesserella parasuis].
ACCESSION   WP_010785862
VERSION     WP_010785862.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..350
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=38744
     Region          36..343
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mkiktllmwa isaffavmls acnkepqqia fegktmgtty hikyiddgsl tnlpkpeevq
       61 rqmdtllkmv nnemstyqkd sqisqfnqmk eadkpfeias dfakvvkeav rlnkvtegal
      121 dvtvgplvnl wgfgpdkrln kapteeqiae ratwvgiekl vlddnatkat ltkkvpelyl
      181 dlsaiakgfg vdkladyleq lgvqhylvei ggelrgkgln lkgqpwriav ekpefaqgts
      241 sqivvplhnl gmatsgnyrn yfedeqgnrl shiidpkalr pishnlasit vfapttmtad
      301 glstglyvlg aekalevaer enlaifliik kgdgyetkms safeklinqk
//
LOCUS       WP_010785999             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Glaesserella
            parasuis].
ACCESSION   WP_010785999
VERSION     WP_010785999.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..222
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=24765
     Region          2..211
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mnliqllqqq divlsisfgi lvvmsilswt iilirlikmi gvrknnqqsf qlvksaenlt
       61 qaeqyiqnkr seiadilqlt fkqcelyqak eknhlshqlp fkdfltlhlr naitqslrky
      121 dgglvalasi gavapfiglf gtvwgifnal mdisqqgqvs iatvsapige alvatamglf
      181 vaipavlayn litrlnrnls qdldhyanel fiyllhhyge nk
//
LOCUS       WP_010786019             398 aa            linear   BCT 01-JAN-2025
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme [Glaesserella
            parasuis].
ACCESSION   WP_010786019
VERSION     WP_010786019.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 398)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..398
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=44487
     Region          5..395
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 minhtfrsyf pffqdnpdav yldtaattlk pkvlidatln fyrssgsvhr sqydfpqtqr
       61 yelardlvak rfnvatrdav iwtsgtthsl nlvanglads ieasdeivis vaehhanfip
      121 wqqlaerkqa rlivlplnsn yqiapemlqt alsertkiva fnlvsnvtgv rqpaeqlipl
      181 irqqcsakiv ldvaqavcce qidvqaldad fyafsahkmy gptgvgvltg klssleqlrp
      241 llfggkmlqe iteqkltmat lpyrleagtp niagiiafge vlewlekwdf salnsplyql
      301 akearqrlat ypnirilpeg clsptisfvf hhqhhadiaa ilaeqqialr sgehcakpyl
      361 rylaqngtlr islahynvqa dldrfftald faldilen
//
LOCUS       WP_010786084             355 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Glaesserella parasuis].
ACCESSION   WP_010786084
VERSION     WP_010786084.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..355
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40730
     Region          16..344
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mnyvipdlfa lgdlesksvf kacthahral gelkgvvhtm pnpnilfgtl plqeakesse
       61 ienivttqdd lyqsnyatqq fasgaakevh yyvqamslgf hevqksglit lnlikeiqre
      121 legnnagfrk qagtglvnqt tqevvymspq tydeienlma glerfindse qmdydplvkm
      181 alihhqfesi hpfydgngrt griinilyli qqglldtpvl ylsryinrnk seyyqllqav
      241 retqqwepwl ifmlngiaet aiqsvkline ikalmmkqkq mirenlpkvy shellnnlfk
      301 ypytkidfvm edcqihrnta vkrldelval gvlaktkigk enfyinvelf hllmq
//
LOCUS       WP_010786188             538 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA recombination protein RmuC [Glaesserella parasuis].
ACCESSION   WP_010786188
VERSION     WP_010786188.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19771199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..538
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=61463
     Region          <50..>298
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          184..513
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mnldpiwlya tiallllisl wlffsysrsq rdsqerqqal eqlqqqfstl sqkyeqisle
       61 knqveqfavq qqtkaestle rlnerdlaiq klqqqleqae lqedqleryi nelkerigsa
      121 qtkaesleeq lqqtqlqlqh qqaesgqlqa kfsqsqqelt elrttlsekq anfetqqknf
      181 levrqqlnve fqhlaqqile eksksfsesn qsaldvllkp fkeqiesfqk rvnevhseai
      241 kgnadlgaei krvleiglsm sqeaqnltta lkgnnkiagn wgeiqlesal qtagllageh
      301 yvaqesyrde egkrfapdfv vklpddkhli ldskvsliay dqavrsednf aiqqaldehc
      361 rslrthidgl skknysqlig ikspdfvlmf vpiepayiea mkhdpqlfny gyernvilvs
      421 httlmpilrt vanlwrierg naeareisek agdiynqvcv iaerlaklgn tlntasnqyn
      481 qsvtalvgkq gllgkverfq qlsakahqtt pqvelletdw dttrlhllve kpitqdnv
//
LOCUS       WP_010786237             253 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Glaesserella parasuis].
ACCESSION   WP_010786237
VERSION     WP_010786237.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..253
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27598
     Region          8..243
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mnillsslsv sdvtvrysng htaihdvtfr ldggticall gvngsgkstl fksimglvqp
       61 kgnielcglp vnqalkrnlv ayvpqseevd wqfpvsvydv vmmgrygymn flripsavdk
      121 qkvaeamerv niahladrqi gelsggqkkr vflarslaqe skiilldepf tgvdvntena
      181 iidllkqlrd sghlilvsth nlaavpsfcd qavminrtvl atgsiettft penlgrvfgg
      241 vlryqqllgd hke
//
LOCUS       WP_010786292             260 aa            linear   BCT 01-JAN-2025
DEFINITION  TatD family hydrolase [Glaesserella parasuis].
ACCESSION   WP_010786292
VERSION     WP_010786292.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..260
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29418
     Region          6..260
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mnnlfiidsh chldsldyet rhknvdevid nakargvqqm isicttlgrf eamkrltahr
       61 sevalscgvh plnvedepfd ydklvalvqd prvvavgetg ldyhytpetk alqqslfeqh
      121 ievakqvqkp lvihtrsare dtmqfleqgn aeqcggvlhc ftedwamakr aldigfyisi
      181 sgiitfrnae elrdvvrkvp ldrllvetds pylapipyrg kpnqpayvre vceyvatlkg
      241 vsleefanit tqnvrklfki
//
LOCUS       WP_010786439             230 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Glaesserella parasuis].
ACCESSION   WP_010786439
VERSION     WP_010786439.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 230)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 230)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..230
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25485
     Region          11..196
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 msfntenswe rafkltipif mgylaagiay gmlatnagmp awftivmcft vfsgtaqyaa
       61 ipffvsgagv vsvflstllm slrfifytln mhsslpkekl nrffvlsylt denfgvlttl
      121 pqetrqammf kisilgmsyw tfativgill gdsvsqyipn ldfalpclfa ilayeqyssq
      181 kqwkpifial igfllagqit qtsvllvaii iaiiivaflp qsftekkgqv
//
LOCUS       WP_010786415             219 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF799 domain-containing protein [Glaesserella parasuis].
ACCESSION   WP_010786415
VERSION     WP_010786415.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..219
                     /product="DUF799 domain-containing protein"
                     /calculated_mol_wt=23489
     Region          3..214
                     /region_name="COG4380"
                     /note="Uncharacterized conserved protein, DUF799 domain
                     [Function unknown]"
                     /db_xref="CDD:443506"
ORIGIN      
        1 mkklfvllts lillagcakq kvdsydytel knskpksilv vmptnssvda kadtsvlart
       61 syplgelgyy vfpvalvdei fkqngltdgn airsaktnki reifgadaif yvnieeygts
      121 yklidsvtnv slegklvdlk tgktlwegag sfaqgssnsn dgllvmlvka avsqimdtsk
      181 dkgyqiaapa tsnlvhlgkn gglligpkhp dynktqvsk
//
LOCUS       WP_010786445             150 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Glaesserella parasuis].
ACCESSION   WP_010786445
VERSION     WP_010786445.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..150
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=16581
     Region          41..148
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 meqltfaeqf qqfaanhtim vvawvalfva viinlykgat skfkivdnaq atqlinkeda
       61 vlvdvrsdde frhghiiesv hlipsdikgk ktqaiekykd rpvivvdang lsasglanel
      121 vkqgfnkvyv lkegiagwrt anlplvkkhk
//
LOCUS       WP_010786498             408 aa            linear   BCT 01-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Glaesserella parasuis].
ACCESSION   WP_010786498
VERSION     WP_010786498.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..408
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42697
     Region          4..408
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mttenistpk qafvglqmlf vafgalvlmp litgldpnta lltagigtli fqictkgqvp
       61 iflassfafi apiqygvqqw gipvtmggiv fsgliyfvls alvkfkgvai ldklfppvvv
      121 gpviiiiglg lapvgvdmai gkgtdipyat avtvsmitli ttlivavftk gmmklvpimf
      181 aivvgyivsl ffglvnfqpv ydaawfslpk lttpefklea ilyllpiala pavehvggim
      241 aissvtgknf lskpglhrtl lgdgvatsaa amlggppntt yaevtgavml tknfnpkvmt
      301 waacwaiais fcgkvgallq tipgvvmggi mmlvfgsiaa vgmstlirak vdmsearnlc
      361 ivsvvmtfgi ggmlinvgef slkgislcav vaiilnlvlp kektekte
//
LOCUS       WP_010786225             651 aa            linear   BCT 01-JAN-2025
DEFINITION  dipeptide/oligopeptide/nickel ABC transporter permease/ATP-binding
            protein [Glaesserella parasuis].
ACCESSION   WP_010786225
VERSION     WP_010786225.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 651)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Monnet,V.
  TITLE     Bacterial oligopeptide-binding proteins
  JOURNAL   Cell Mol Life Sci 60 (10), 2100-2114 (2003)
   PUBMED   14618258
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..651
                     /product="dipeptide/oligopeptide/nickel ABC transporter
                     permease/ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70633
     Region          26..279
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
     Region          340..620
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mfrqgladrl asggarfkal stasklalgf ivlvallail apwvspydpl qtlrpvqapn
       61 adywfgtdrl grdilsrliy gaqtslfigl gavglaivlg silgataata dklgnevimr
      121 fmdilmafpg ialaavllat lgnavpiiil aiaivytpql arvvranvvs qweedyvrae
      181 rviggsrtyi lvkhvvrnsa apvlvfatvm vadaivleas lsflgagvql pqpswgnils
      241 egrnivlsgf wwattfagla illtvlslni lsegltdalv npklkrsptt skedvskpls
      301 tdvqeamaes lalkryllkl hekeatrtdr mqlnpnakpi lqvknlsirf pnrygdiplv
      361 dnisftvneg etmglvgesg cgksisafsi mgllpptaki tgeilftdra gnqhdllktd
      421 klnelrghei smiyqdalsa lnpsmrikdq maqlisrggk qsaetllkwv kldpektlnr
      481 yphelsggqr qrvliamala repklliade pttaldvtvq aevikllnel reklgfamvf
      541 vshdlalvaq mahhiivmya gqvvemapts allsnpthey trgllgsvls tecraerlyq
      601 ipgsvpspfd fakgdrfasr slrpdanpnq rlklvpasdn pkhlwashle g
//
LOCUS       WP_010786504             427 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Glaesserella parasuis].
ACCESSION   WP_010786504
VERSION     WP_010786504.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..427
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=46585
     Region          32..409
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 metivivggg agglelatyl gnklgkkkka niilvdknis hlwkpllhev aagslddgtd
       61 alsyrahakn hhfefrqgtl tqvkpaekii vlapiydeag ellvaertiv ydklvlaigs
      121 rsndfntpgv aehcifldss eqakvfhkrm melflkfsnn nekevhiavv gggatgiels
      181 aelynavkhl nsygygkldn tslkvtllea gerllpalpe rvsasaikel ralgvdvltn
      241 tpvirataeg lvtkydenfk adlmvwaagv kapeitktfg fetnrinqia ikdtlqtltd
      301 envyvigdca fllqadgkpv ppraqsahqm atvcgknila qlenkplkaf ifddkgslis
      361 fsrfgtvgsl mgnltkgsmf iegkiarmay lslyrmhqva lhgcvktgli mlvgrinrfl
      421 rptmklh
//
LOCUS       WP_010786522             243 aa            linear   BCT 01-JAN-2025
DEFINITION  copper homeostasis protein CutC [Glaesserella parasuis].
ACCESSION   WP_010786522
VERSION     WP_010786522.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..243
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26116
     Region          1..241
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mkveicvdnl esvitanqfp idrielcsal avggltpnlg fiqqaqhist iplalmirpr
       61 agdflysede iqimlndiat akqlgiqavv fgalsangei dlattellvk asqgmeitfh
      121 rafdlckdpi taleqlidlg chriltsgqa atafdgipvi qqlvkqangr iqvmagcgvn
      181 adnvkqiieq tkvpeihfsa kgqrqslmds issarmgtss qdnvldiads qkikgilkyi
      241 sll
//
LOCUS       WP_010786537             138 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Glaesserella parasuis].
ACCESSION   WP_010786537
VERSION     WP_010786537.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..138
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14605
     Region          7..138
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mnnffeklaq tfspyillit rvlvgymfll hgtakffelp ismtggngav plfslfgvag
       61 vleivggill ilglftrata filagqmavv yfifhaasga ifdpisnkge aaalfsmafl
      121 llwhsgagkl sldaklgk
//
LOCUS       WP_010786611             268 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Glaesserella parasuis].
ACCESSION   WP_010786611
VERSION     WP_010786611.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..268
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28762
     Region          12..262
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mtittilili tcgiltnlms alfgigggvl mvpilhtlfp efslqmvaat slmtvmgtaa
       61 inlvyfykqr vpvkmkslll wsigmiigvq lgfeisffip nwaivavfvt tlvvlalcli
      121 lakksensta csslkenikg isvclfggsv agitgigggs imaplisllp svkphqiaay
      181 snymmiiggl gnlygylski ppvylenswq vgyvnftvvs ivvlcsflts ffsmklrgil
      241 kpltmqrlls gillviagym lilqgvry
//
LOCUS       WP_010786703             251 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Glaesserella parasuis].
ACCESSION   WP_010786703
VERSION     WP_010786703.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..251
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28229
     Region          42..139
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mkkeevghhf larlgktrlr pggkmatdwl iangdfrkdk kvlevacnmg rtaieiaqqf
       61 gcqvigidld eealekaqqn ikehkveelv qvqranatkl pfednsfdii ineamltmlp
      121 qeakekaire ylrvlkpngl llthdlllng dnreeviakl rdainitvap lnkqdwketf
      181 lhcgfrnvet fsgemsllsp kgliqdegvl gamkvvgnal kpenrdtfkk mfqtfndpen
      241 qlgfiavcsq k
//
LOCUS       WP_010786767             401 aa            linear   BCT 01-JAN-2025
DEFINITION  ROK family protein [Glaesserella parasuis].
ACCESSION   WP_010786767
VERSION     WP_010786767.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..401
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=45657
     Region          79..395
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mkitssdyky qhlgtvyrlv eqfelisrtd laklsgfapa smtvltkili dhklilerts
       61 qnlpsrgrpa vglsvspfhw rylcltlapq klsialcdls gkliyqqhys ltsdeylsld
      121 qhilnciqtf slntpltnea llaisisvvg kidrtktiit qlgqqpltcp lvetlhshfn
      181 qpillnehfq lwllaeatlg sliandnvif lqlddqvnls vllkgallhq dehkrmnvdk
      241 mimpkfspls deiaeqqtei eryqltnqvt fpalanlidr yfdhqhtcle dkinyfceqv
      301 eaenpqamqi lshltdnlay mlmnlinifs tekimfnspl lrikkplfeq lqtklqqnll
      361 lnelridivt sqydwdspli psiaiklgiy egcllkgive v
//
LOCUS       WP_010786796             801 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Glaesserella parasuis].
ACCESSION   WP_010786796
VERSION     WP_010786796.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..801
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90891
     Region          29..782
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 minnsttafs lafslllccl ginaeqleld eisvmgkvpe gnsisflkvs daiidgekfk
       61 nrsatlgnal sselgvhstp fgggasapii rgqegvrvki lqnnadvvdm snispdhait
      121 adtllanqve ilrgastlly assspagivn ivdqripnkm pkkgyevtls srfdtaskek
      181 vyalgttigi gkhlalrleg ldrqsqnykv pqiklgetln yvpdtyhqsk vgtiglsfig
      241 ekgylgasyn qrkdryglpg hnhkfdtcia hiydmrlqgk hsytnlyphl msdemvtenp
      301 hfhcgtdydl dpshshdhpy ghdhdhthig pwvdlhskri dikgeikqpl pmldkiqlsy
      361 aqtdyyhdek dagksgdtin pnrvdkskdf gkpvnifknq gknarleffh tpiggltgmf
      421 gvqyqtlqss antpsnrevq wplvdnrnkq islfaleqya wdnfaielgl rtekqnihid
      481 ydlakiqkqq kfnertygkq vdpdlsdyde kavsytgtfn wffhpdyqls ltashnerlp
      541 tpmelyyhgq hlatnsfeyg nkdlkkeisn nfelglgyht etldyklsty ynnfdnyiyn
      601 etlyrsnnlf mrrynqakat fyglegiiny rftpdyqfsv fgdmvkgklk qlpdikglnd
      661 vygepildpd ydpeydeped qyyrpylgke mikqadrvsp rlppirlgar fnaqltdyls
      721 gsvewmkvft qnkvskless tkgyqllnas lnyrrqikgv eytvsltgnn llnqavyihn
      781 syhpyvpqmg rnfilgldls f
//
LOCUS       WP_010786824             867 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA translocase FtsK [Glaesserella parasuis].
ACCESSION   WP_010786824
VERSION     WP_010786824.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12144184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..867
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..867
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=95353
     Region          9..>143
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <379..867
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 midrlkgken lirlvlllsa cfgiylitaw asyspldnaw stassithet lnktgalgay
       61 lvdllfamfg kvavfvpfgl aftsiyvlil rladdlnwak iglwlgsffl flvglaglss
      121 vlfenspyyl sggfiggmla swlnsqmvll lvamlltavg fyfcsgqill qlfnrlyhwi
      181 vegktedkps tlntdeavqt ekneekveae seseetvdnp qytdvsqftr phitglktvq
      241 eeevaadvel tdvtkfkven psslpsitvp efdvsvpsvs tsvelpeatv ivpnvtepvm
      301 pkvrlnpvve vaakptvepf eeaqstvqfl qenlplfepk aataeaqpek kgvtypkgyg
      361 dslihpllqt krkvekpttp lptidllttv kseeqqiteq eirdtsarie relanfgvra
      421 tvedvlvgpv vtryeikpaa gvkaakitnl asdlarslif eairitdvvp gkpymgietp
      481 nrqretvwlr dvldsnefrh tkatlpmalg kdisgkpivv dmakmphllv agqtgggksv
      541 gvntmilsll fklspeqvrf imidpkvvel siyndiphll tpvvtdmkka enalrwavee
      601 merryllvss lnvrniegfn akidqaaamd lpipnplwrp gdtmdslppp leklsyivli
      661 vdefadlmms agkqvedhim riaqkaravg ihlilatqrp stdvitgvik anipsriaft
      721 vasqidsrti ldkggaesll grgdmlysga gspemirvhg afmtdedvqr vadnwrargk
      781 peyiesivat pegdengens ertsgeldpl fdeiaqfmid ggatsisgvq rrfslgfnra
      841 ariidqleeq giisapdsrg krevlar
//
LOCUS       WP_010786801            1054 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Glaesserella parasuis].
ACCESSION   WP_010786801
VERSION     WP_010786801.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1054)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1054)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1054)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1054)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..1054
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=119451
     Region          3..1044
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mlinentieq aclqhlqelg wdythgstin adgenpwrlr tdevvfrsvl reaverlnpq
       61 lpsatvdevv alvcktditd lternqqayr ylregvrvey rendeqkvef arlidfqqps
      121 rnrfdvvnql tiagrkgnrr pdvicyingl pvvvlelknp lkenadlpqa fnqlqtykqe
      181 igdlfvynqa lvisdgilak vgsltadler ftpwrvvdek nkqrisfehe leglvrglln
      241 paslldyiqn fivfeqtssg rlvkkiaayh qfygvneavd ctlwaaseqg ngkigvmwht
      301 qgsgkslsml fyagkllsqa elrnptivvv tdrndldgql yatfsggqal irqqpvqadg
      361 realreelak retggviftt iqkfglqege qahpvlnarh niivisdeah rsqygfsqsm
      421 klnelnrtgi yrvgyakhlr dalpnasfig ftgtpisled kdtqevfgky vsiyditdav
      481 edgatvpiiy earqipiaqs aefenvvrea qtlldeddes synfrlrekl mgtegrlsrl
      541 aedfvkhfeq rtalidgkam vvamsrqicv klyekitalr pewhsddvne gaikivmtgs
      601 asdpadiqkh iyssqdkkll errfkdpddp leivivrdmw ltgfdapccn tmyidkpmkg
      661 hnlmqaiarv nrvfrnksrd ngglivdyvg ltselreate qytrshgkgq mthniaeikv
      721 kmleyidvvr gqfatpvngq sfklfdalki edelalfqqv mlganyilal dhqmvadkte
      781 ktprrnaflk avrlakkgfs lcgadgdvqq yqkelafyda vrailakrep nstasneerq
      841 lqlvallnka vdasgainlf dllnqeqpni nilsdeflek iknsqtkelw llaverylrs
      901 qinekgagnl avqkdfaerl kqalnqyhnq nltimqvlee llnmskefte rlqrgeklgl
      961 spaeiafyda larnesavre lgddalknla kaitdklrks atidwqykea vrakmrnlvr
     1021 vtlrlfkypp dkcdeaiqfv leqaeviade lttv
//
LOCUS       WP_010786841             210 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF1919 domain-containing protein [Glaesserella parasuis].
ACCESSION   WP_010786841
VERSION     WP_010786841.1
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008161
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..210
                     /product="DUF1919 domain-containing protein"
                     /calculated_mol_wt=24956
     Region          2..210
                     /region_name="COG3955"
                     /note="Uncharacterized conserved protein, DUF1919 family
                     [Cell wall/membrane/envelope biogenesis]"
                     /db_xref="CDD:443155"
ORIGIN      
        1 mplikkitnk indffrksln aknhqrlntn tlavissnct gafmlhdlgl rfnspfvnlf
       61 ltptdfikyv kniahyqtqe itfpkeiqrk ypvgllgdih lyfmhyhseq eavkkwqert
      121 armdlnhlfi mmaerdgcrd edllefeqlp fknkvvfthk pyleltsavy iqgfeqqqki
      181 gdlfeycgln rkrfydqfdy vgwfnqhkqn
//
LOCUS       WP_010787006             461 aa            linear   BCT 01-JAN-2025
DEFINITION  GspE/PulE family protein [Glaesserella parasuis].
ACCESSION   WP_010787006
VERSION     WP_010787006.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..461
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=52678
     Region          29..459
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 msqyticeqq terifdisps rwqknceekq lllrylavpv qetehklwla vddennltac
       61 eifafmthkq iepvviasde lkyllnalsp eqqpiyeese lafveqeqeq lnlndpiiql
      121 ldnlfkfcla qnasdihiep rkqkliirlr idgvlhlyks lsiqlasrli srikllakld
      181 iselrqpqdg qfsfttalad tldfrvsslp tiygeklvlr lqknkptsfd flqlgfnpqq
      241 qttllnalkq pqglilvtgp tgsgksitly salnylnqmd khiltaedpv eieidgliqt
      301 qvnrsiqldf sqllrtflrq dpdiimlgei rdeesakmal rasqtghlvl stlhtndals
      361 averllqlgi qeyeiqnsll lviaqrlvrk lckkcrgvgc decyqgyrgr igvyqclsrt
      421 akkfdkqtay ldfsslresa kqkieqqltn etevdrvlgy e
//
LOCUS       WP_010787033             675 aa            linear   BCT 01-JAN-2025
DEFINITION  M13 family metallopeptidase [Glaesserella parasuis].
ACCESSION   WP_010787033
VERSION     WP_010787033.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..675
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76962
     Region          1..675
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mkktlsfsli alalgltact tktyqstlte gvdnsvapqq dfyryvngkw ldtaqipsdr
       61 tswgtlaeln elnekrsvel lqavisdpnf andekaqrlk alyqsytdlt areklglspi
      121 qadlsrieri ktfaeleqyl inetkqgnem lfgwsvfahl knsrqnaiyf sndslglsnd
      181 yyqkdtpenr ktlqlyqdyv aqmlhfaqvk nskqkakaiv eyekaiaktl ftneqrrdiq
      241 krynplsine lakaskhinl anylnavgvn teevivwepn flkqfdqlin pqnlalikdy
      301 lrfktvsnas tylnkaldda nfafyskqlv gqkqqrpldk ralrlinnqi gqefaqfyve
      361 kffpatakkd llemagylvk ayhqridnls wmsaetkaka kvkldkfive vgypnkwkdy
      421 sqlhlktveq ggslyanlre iakwnyqeal skigkpvdln ewgmlpqvvn asysplmnri
      481 vfpagilqap lydmnadpav nfgaigaiig heithgfdds gskfdgdgnl kewwtaedrq
      541 kfealadqlv aqfdkfevap kifvngrftl geniadlggl siaydalkry eqdhgvtptl
      601 enltpdqrff mswtrswrnk atvqalthqv ksdphapgqy rafapvlnis gfhnafntkq
      661 gdamyrpine ririw
//
LOCUS       WP_010787363             389 aa            linear   BCT 01-JAN-2025
DEFINITION  AAA family ATPase [Glaesserella parasuis].
ACCESSION   WP_010787363
VERSION     WP_010787363.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 389)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..389
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44593
     Region          6..323
                     /region_name="COG3950"
                     /note="Predicted ATP-binding protein involved in virulence
                     [General function prediction only]"
                     /db_xref="CDD:443150"
ORIGIN      
        1 mnntlhlkkf hfeqvkgvgt ievelfpnqr vytfigengi gktkfleslf amllftnkqa
       61 mktdfyiqhs lipfksatid disfsfnend gfslgnhsya filamhsypv vylsaqhrga
      121 inekayeyer gnvsklgnks krqkgyleyl ltsfngnpqn lknlnmdsni eewivqrals
      181 snpyqskedn reieiktlls llhkidhrid kdfleisgdn rvflkienqk reiselssgf
      241 tsilkiiqsi iagysyftne lqianvpgiv lideieshlh nkwqaniipl lkdlfpktif
      301 fitthssivi sqlnhgeayr lkrceddgvv yaelidypsk vsfidllnda fdvnlnrlki
      361 nraqeegqqe akqtllklvq qelanleak
//
LOCUS       WP_010786723             301 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Glaesserella parasuis].
ACCESSION   WP_010786723
VERSION     WP_010786723.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..301
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=34452
     Region          <13..297
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mvgieknevd tgrlkvvtyn diekrlnrhl lkllghypia disapiaiek lkplererkl
       61 dtlhrmigyl nqimiyavnr gvikynptad igkvflkpvv ennptirpel lgklfedlqn
      121 stleietrca lelllltagr agaitqlews evnfeemild ipkekmkgrq gkvqdfvlpl
      181 stqaikilql lqklnryhsr fvfpsrknph qpisketpnk alqrmgyrnv ltahglrsvf
      241 stamneaefn seiievclah feyssvraty nkakyltqra eymqwwgnfv eqaaegrglc
      301 s
//
LOCUS       WP_010787475             171 aa            linear   BCT 01-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Bacillus atrophaeus].
ACCESSION   WP_010787475
VERSION     WP_010787475.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..171
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18509
     Site            order(14..15,18,21..22,53..54,57,60..61,64,86..87,90,
                     93..94,97,116..117,120,123..124,152..153,156,159..160)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          24..161
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          37..64
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          98..124
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          135..161
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mksngdelsl svqnlantne itivqaigel kksgkdaipv lvealkdegs lrniaaavlg
       61 efgedaseaa eelsrllksh aedtrmaaai slmrigkpsl pfvikiaqds egqscfwasw
      121 ciawidpsri epkmyeclkh eqehpsgmva pfaaeealgk liafqlkdke d
//
LOCUS       WP_010787585             336 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Bacillus atrophaeus].
ACCESSION   WP_010787585
VERSION     WP_010787585.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..336
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37040
     Region          8..318
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maenqeiydv tiigggpvgl ftafysgmre lktkvieflp rlggkvsfff pekiirdigg
       61 ipgiagqqli eqlkeqaatf epeivlnqrv egfermndgt ivltasngek hytrtvilat
      121 gmgtlevnel dskdaskyag knlhykaekl gdfkdrhvvi sgggdsavdw anelepiaas
      181 vtiihrrnef gclessmtkm kqssvrvltp ytleqihgne erihsvtarh setgrtelie
      241 ldelminhgf kidlgpmldw gldieegrik adrhmrtnlp gvfvagdaas yesklrliag
      301 gltegptavn sakayldpea enmamysthh kklihk
//
LOCUS       WP_010787598             378 aa            linear   BCT 01-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Bacillus atrophaeus].
ACCESSION   WP_010787598
VERSION     WP_010787598.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..378
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41445
     Region          1..378
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,85,163,167,186..187,189..191,210..212,216,
                     231,255..257,280,297..299,322..324,364)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,59,163)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(89..90,92,95,103)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mkaltyqgke hmevkevadp riqhaqdviv kitatgicgs dlhlykngip aqpdyivghe
       61 pmgiveevgs evkklkkgdr vvipfnigcg ecfyckhqme sqcdesnpnp htdagglfgf
      121 sefngnfpgg qaeylrvpya dfssfivpad seledeqvlf lsdvmptafw svehsgvkkg
      181 dtvvilgagp iglmaqkfaw mkgakrviav dqvphrleha krtngaetfn ftehdeigql
      241 lhqethggah vvidcvgmdg tplpkekane kpnqfgtisp iltaseavrk fgtvhltgay
      301 isqadgfpig dfftrnvslk mgqapvihlm pmlyqmvekk eidptdiith kmslaeapla
      361 ydifdkkedg nikvilkp
//
LOCUS       WP_010787606             567 aa            linear   BCT 01-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Bacillus atrophaeus].
ACCESSION   WP_010787606
VERSION     WP_010787606.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..567
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=61358
     Region          21..566
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mlkknmkfkl gtkilcmvlt iillfsvsvg tviikditns lkkmatekak gdlalssryi
       61 ddvitgdwni khnelykgdt pinnnekivd mlgektgdti tifkedtrva tnvikdgera
      121 vgtqaspevt davlkggref ygeanvagsv yqtayqplkd kdgaiigmly tganqnilts
      181 ltqslfiqfa ivlaaaiils iilvllftrr inkrlnalkg afegaengdf tieitdrssd
      241 eladlsvcyn nmrktlskti qtvqqsavql asssqqlaag aeetnqasek iteavqhian
      301 tsdfqmtkvv nseksleqav ediqyiteka lsiaeqgqya qekaevggke iadtqnqmdt
      361 ihhsiqksge miqrlddhsk qigqilsvit qiadqtnlla lnaaieaara gehgkgfavv
      421 adevrklaee sqrstgqise liteiqsdmn qsslsietvk teaiegvsmi qrtgevfkei
      481 vyatkeisvg isglssatqn isastqeiaa sftentaaik estensqqaa alteeqfaam
      541 qeitaasdtl sdlagelnai inefkid
//
LOCUS       WP_010787623             191 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010787623
VERSION     WP_010787623.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21839
     Region          2..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marskefdek avlrkamelf weqgyektsm qdlvnhmgih rrsiydtfgd krslflasln
       61 hyeelivnem esiisstssi kqairdvfif vlnsieqypk gclsvnaaie lslldkeigr
      121 ivtkmfnrte dmfnnlikrg qtsgeiskei dsdnisrflh nnlvgirvli ktnynkkele
      181 giitlalsvl d
//
LOCUS       WP_010787634             175 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Bacillus atrophaeus].
ACCESSION   WP_010787634
VERSION     WP_010787634.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..175
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=20495
     Region          2..175
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mktlviithp sletsvvnkr wveelkkype kytvhelykv ypdgnldvek eqklveahgn
       61 lvfqfpvywf ncppllkkwl ddvflygway glkgdklknr kvalgvsagi knvdyseagr
      121 yhytfeqvlr pfemtaiyck adyrsyfafy gaefepsvne iekstqdyln fidnm
//
LOCUS       WP_010787644             400 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bacillus atrophaeus].
ACCESSION   WP_010787644
VERSION     WP_010787644.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..400
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43277
     Region          15..390
                     /region_name="MFS_MdtG_SLC18_like"
                     /note="bacterial MdtG-like and eukaryotic solute carrier
                     18 (SLC18) family of the Major Facilitator Superfamily of
                     transporters; cd17325"
                     /db_xref="CDD:340883"
     Site            order(22..23,26..27,30,62,112..113,115..117,120,140,
                     143..144,147,224,227..228,231..233,236,264,268,318..319,
                     323,327,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340883"
ORIGIN      
        1 mkksikeqkt vliillsnif ivflgiglii pvmpsfmnim nlsgstmgyl vavfavsqli
       61 tspfagrwvd rfgrkkmivi gllvfsisel ifglgthvsi fylsrilggi saafimpavt
      121 ayvadittmq erskamgyvs aaistgfiig pgaggfiady girmpfffaa aiaclaaiss
      181 vfilkeslpk kereqllana kesnffkdlk ksihpvylia fiivfvlafg lsayetvfsl
      241 fsdhkfgftp kdiaiiitis sivaviiqvl lfgklvnklg ekrviqlcli igavlafvst
      301 vmsgflavll vtcfiflafd llrpalttfl skvagnqqgf vagmnstyts lgtifgpalg
      361 gilfdlnihy pflfagvvmi iglsltmlwk eksnevspln
//
LOCUS       WP_010787671             199 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010787671
VERSION     WP_010787671.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..199
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22397
     Region          7..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mksrkgrkge esrkrllkaa ahefsirgfh etkvsaivkr agltqpsfyl yfqskeaife
       61 elindfhsrl rkltesllle tglhandvtn kvlsavetvf qflaedkdlt rigfflnpea
      121 kqlkqdvamv lkdnleaeqr lgyfrselem etvaecligm iehltdsyll tgvkdpasla
      181 aqvvnlliyg mltkgsdar
//
LOCUS       WP_010787672             114 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Bacillus atrophaeus].
ACCESSION   WP_010787672
VERSION     WP_010787672.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..114
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=12610
     Region          5..104
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 mismimkvsl aafmlaggii kvfrvpfqve hwrhyqyplw fltvtgilei agalamtagi
       61 wnryaafgag ilfvvlmaga vhahivrahq sflmtipami clivsimvmi reft
//
LOCUS       WP_010787703             241 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Bacillus atrophaeus].
ACCESSION   WP_010787703
VERSION     WP_010787703.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 241)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..241
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25865
     Region          17..241
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 meaqlkkves vqredtflqg vkdciptllg ymsigfafgi vgissnlsil eitllsllvy
       61 agaaqfifca llasnspasa iilttfivnl rhlllcltla phftryslmk nigigslvtd
      121 esfgvainkl athgklsdrw mnglnitayi cwiisctlgg flgqwisdpe algldfalta
      181 mfvalmvlql qstaseklkh slslvvymii amvslsffvp shvavitatv ivatigvvtd
      241 k
//
LOCUS       WP_010787717              80 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010787717
VERSION     WP_010787717.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..80
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8747
     Region          1..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mpvkardwlk nkrlskgltq kgvadkagia rttyasieqg ernagvptak aisqvldfhw
       61 aiffdetlrv ssneresnta
//
LOCUS       WP_010787743             122 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease [Bacillus atrophaeus].
ACCESSION   WP_010787743
VERSION     WP_010787743.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..122
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14088
     Region          51..114
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mplkpmrica apgcpsltrs rycdahktqq qeetkhynkh srnktitsfy ksrdwkrtrq
       61 lalirdnylc qhclkehcft padmvhhive vkddwskrld ldnlvslcna chnkvhgggk
      121 gk
//
LOCUS       WP_010787440             352 aa            linear   BCT 01-JAN-2025
DEFINITION  Mrp/NBP35 family ATP-binding protein [Bacillus atrophaeus].
ACCESSION   WP_010787440
VERSION     WP_010787440.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Vitale,G., Fabre,E. and Hurt,E.C.
  TITLE     NBP35 encodes an essential and evolutionary conserved protein in
            Saccharomyces cerevisiae with homology to a superfamily of
            bacterial ATPases
  JOURNAL   Gene 178 (1-2), 97-106 (1996)
   PUBMED   8921898
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..352
                     /product="Mrp/NBP35 family ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0140663 - ATP-dependent FeS chaperone
                     activity [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=38316
     Region          109..345
                     /region_name="ParA"
                     /note="NUBPL iron-transfer P-loop NTPase; pfam10609"
                     /db_xref="CDD:431392"
     Site            order(115..117,146..147,149,152..153,193..194,224,226,229,
                     253,256,312,314)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349757"
     Site            order(115..122,247,249,274..275,311..313)
                     /site_type="active"
                     /db_xref="CDD:349757"
ORIGIN      
        1 miredevrki vgemrepflq rplgeldavk evkikpekqh vsvkvalakt gtaeqmqiqq
       61 eivnvlkgag aetvglrfee lpeetvakfr apsaenetll nrdqppvfla vasgkggvgk
      121 stvsvnlais larlgkkvgl idadiygfsv pdmmgitvrp tvegekllpv erfgvkvmsm
      181 gffveenapv vwrgpmlgkm lnnffnevew gevdyivldl ppgtgdvald vhtmlpscke
      241 iivstphpta afvaaragsm aiktdhevvg vienmayyes aatgekeyvf gkgggdklae
      301 elkvpllgri plkqpdwnkd qfapsvydrs hpigeiyyei akevaekasv na
//
LOCUS       WP_010787849             285 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010787849
VERSION     WP_010787849.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..285
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32782
     Region          3..144
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnekkekiik tgihlfakkg fssttiqeia secgiskgaf ylhfkskeal llsaceyyis
       61 msmdnmqkik ekhhhlppke ifkkqithql qeflehrdfi vlllsenvip enqklkqyfh
      121 naniefnkqy rmalvssygd riapflsdis imaqgivnsy inllifneqi kldfehlsqf
      181 imdrlddliy gliqsgkkpi lpeeifrvip agteqvlkei rkvkengels ddlmislevl
      241 eeefskeepr kpiikgmlsn ltasndeeia qlhsiisgyi secrs
//
LOCUS       WP_010787778             136 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bacillus atrophaeus].
ACCESSION   WP_010787778
VERSION     WP_010787778.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Munoz-Lopez,M. and Garcia-Perez,J.L.
  TITLE     DNA transposons: nature and applications in genomics
  JOURNAL   Curr Genomics 11 (2), 115-128 (2010)
   PUBMED   20885819
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..136
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15768
     Region          7..>37
                     /region_name="HTH_28"
                     /note="Helix-turn-helix domain; pfam13518"
                     /db_xref="CDD:463908"
ORIGIN      
        1 mkdnetkqkf ielrakgvsf rkiaeelnia kttimawskv hlteienlka iemeslqeqf
       61 ymtkkariel lgrkvermkk elenrdfsdv psdklldals ktlnqlkkde iettfkgegd
      121 tfedllvtmn tvtwkp
//
LOCUS       WP_010787850            1054 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Bacillus atrophaeus].
ACCESSION   WP_010787850
VERSION     WP_010787850.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..1054
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113410
     Region          1..1048
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnhiinfilk nkfavwlmti ivtvaglyag lnmkqesipd vnmpyltist typgatpsqv
       61 adevtkpieq avqnvdgvsv vtstsyenas svmieydyek dmdkakteaa ealenaslpd
      121 dakdpeisry smnsfpiltl svssdkdsle dltkkvengl vpklegtegv asvqvsgqqv
      181 eevefsfked klkdyglded tvkqviqgsd vttplglytf gkqeksvvvs gdiesikdlk
      241 nmriptasan sgsassaaas sssassaaaa qsaqaasqaq qsastdvptv klsdiadikd
      301 vrkaesisrt ngkdsigini ikandantve vadqikdelk qykkdnkgfq ysstldmaep
      361 itesvdtmls kavfgaifai viillflrdi kstlisvvsi plsllialla lnqlditlni
      421 mtlgamtvai grvvddsivv ieniyrrmrl kdeplrgaal vreatkemfk pimsstivti
      481 avflplalvg gqigelfmpf altivfalaa sllisitlvp mlahslfkks lsgapvkake
      541 hkpgrlanfy kkvlnwalsh kwitsiiavl mllgslflvp ligasylpsd sektmqitys
      601 pepgetksea edeaekaeki lldrkhvdtv qyslgsenpl gggnsngalf yvkyeddtpd
      661 fdkekdnvlk eikkqsdrge wksqdfsssg nnneltyyvy gdsesdikgt vkdiekimkd
      721 qkdlknvnsg lsstydeytf vadqeklskl gltasqisqa lmsetsqapl tsvkkdgkel
      781 dvniktekde yksvkdlenk kitsatgkev kigdvakvke gttsdtvskr dgkvyadvtg
      841 evtsdnvtsi saavqkkvdk lelpdnvtvd tggvsadiad sftklglaml aaiaivylvl
      901 vitfggalap failfslpft vigalvglyv sgetislnam igmlmligiv vtnaivlidr
      961 vihkeaegls trealleags trlrpilmta iatigalipl algfeggsqv iskglgvtvi
     1021 gglisstllt llivpivyev lakfrrkkpg meee
//
LOCUS       WP_010787886             663 aa            linear   BCT 01-JAN-2025
DEFINITION  beta-galactosidase [Bacillus atrophaeus].
ACCESSION   WP_010787886
VERSION     WP_010787886.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..663
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73779
     Region          4..610
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
     Region          602..660
                     /region_name="Glyco_hydro_42C"
                     /note="Beta-galactosidase C-terminal domain; pfam08533"
                     /db_xref="CDD:400716"
ORIGIN      
        1 makklyhgac yypelwdeet iqqditimre tginvvrige fawsvmepee gninvnffke
       61 iigrlyengi etimctptpt ppiwlshgrp ermyvnesga imghgsrqha ctnhpyfrkk
      121 aalittslak elgrlpgvig wqldnefkch vgecmcetcl glwhewlknr ygmidrlnea
      181 wgtdvwsety qsfeqvpqpg papflhhasl rtmyqlfsme kiaafadeqa riiriysdap
      241 ishnstvmfs vdnerlfqgl dvasfdtyat qenasaflfn cdlwrhfkkd rpfwiletsp
      301 syaaslesya lphadgylka eavssyalgg eafcywlwrq qrsgseiphg svlsawgekt
      361 igyknvldve rarkeiepfi istvpaqaea amtysdraka ffrtephrel nhrslvtsfy
      421 erilkagihr dvipehhpld gykllftpyv pylssdyikk asafaeaggi wiagpmtggr
      481 tkehtihtdc algelektag iktlftfpmd edtdsgrafg vcaplglwsa vfdaksgetv
      541 giiekgpasg kaflteqkhg agkivllgst psgkdgeaml ealiahyake agltfrtnvt
      601 pgtivaprig dsgliwvivn mdgkggsvtl peagtdmlsa laveagslsv geyeyriiqf
      661 drp
//
LOCUS       WP_010787973             603 aa            linear   BCT 01-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator [Bacillus
            atrophaeus].
ACCESSION   WP_010787973
VERSION     WP_010787973.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..603
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=66993
     Region          13..600
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mnsipndlqi wkrfvkegvl dearlskria eswhrckkae vnpyqnkgpa vlekkklsdq
       61 aekhslflkt aipyleklrp flkdmemmgl lidadgvvls leghrrtlhe arqinfskga
      121 cwteqavgtn aigtalqise pvaiqgsehy slashnwscs aapiryedgr lagiidfscp
      181 apraqpfmlg iataiayaae relaaqnrla elellshfsg messhvpavl cneqnkiiaa
      241 svpvrhaite wcgmalaeie dqgfkiekav tvqkgyicfy lserkkkraf lfkgaagisg
      301 kfqsmlkdle rvaavdasvc ltgetgtgke vaaralhens srkngpfiav ncgaipadlv
      361 eselfgyaeg aftgakrngy kgafqradkg tifldeigei shamqvallr vlqerkimpv
      421 ggtkeipidi rvvtathcdl rklvesgklr edlfyrlhvf pirlpplrer pedipalfdc
      481 fkeknkwnae lpqefletlk vmewpgnire lfnvferlsi ifpdgrlksr slpsllqaag
      541 lptnheqaek dsaasltlre hiqkniiisa lestkgnvsk aaemtgiprs tfykrlkkfk
      601 vsp
//
LOCUS       WP_010787988             400 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Bacillus atrophaeus].
ACCESSION   WP_010787988
VERSION     WP_010787988.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..400
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45042
     Region          166..384
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msallftrlf tllvicsvyl fvaadnlyhy ificggacif lsnhfllikt kpplifclid
       61 iivgfsfafv fpgtglyitl lspvavtffl kgfkrrtvws vlcfciilwl ivlfrtyqlf
      121 gnehvmdhci smtfvvfcgv vgklirklme aqettkqqyq eltdshqals aahqelhlya
      181 kqveeltaih ernrmardih dtvghkmtal lvqlqllrew qkrdsqkaeq tvgvcealsr
      241 ealeeirlsv rtlqaensqp sfvetlkqlt edfyqnarva seialngdps liplslqpai
      301 trtvqealtn akrhggatrc siqltcepek isviieddgk gnpeteagfg llnmkkrvae
      361 hggtvrfese rskgfkviae fslaikkwsf gpvqqkesls
//
LOCUS       WP_010788046             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Bacillus atrophaeus].
ACCESSION   WP_010788046
VERSION     WP_010788046.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..279
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31243
     Region          1..264
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkwlayclf lilaislsac stsaenetik igindsdrai wdfiagkaee egqqiemief
       61 sdygesnmal angeidanaf qtisyfqaft kkykdklapl gttyiagmgi ysktykrikd
      121 ipngavvavp degidlgral mllqeagllk lkkgfngngs mdmikdnskh lkiktvsked
      181 ayrrlddvdv tvltmedaek adlhpekdal qraeqtaevy mnmiavraed rdrenlqnil
      241 elyhsddtaa fiekeyhgnl ipaflplksl sdwkneftq
//
LOCUS       WP_010788112             420 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Bacillus atrophaeus].
ACCESSION   WP_010788112
VERSION     WP_010788112.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 420)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..420
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46045
     Region          1..414
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
ORIGIN      
        1 mnkffimlfh tyknkitaks fiistvisvl lvlfvtnles iismfqsddd akqeiavide
       61 tnelypifsk qlkavdadse ldmkqtkkse kevsqqvkde kldgmfiikr dkngeisgty
      121 kaltisdeta ynylkqaltq tktavgtadl gvsqekissl yapvsvdnva lqtgakseee
      181 lgqvmglvyi llfmiyfavi myasmiamev atekssrvme ilissmppiq qmfaklfgia
      241 lvgvtqlaii lsigfaslkl getgettssv sqfinvtdvp vstiiyavif fllgyflyat
      301 maaflgsvvs riedvqqtit pmtllvvagf miamfgirap dagfitatsf ipfftpmimf
      361 lrvgmldipf wqaalgigit lltiiilavi gariykggvl fygnssafka ikqalrlskn
//
LOCUS       WP_010788123             247 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus atrophaeus].
ACCESSION   WP_010788123
VERSION     WP_010788123.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..247
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27601
     Region          4..243
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msllsvnnvt ggytrnpvlk nisftlepnq ivgliglnga gksttirhii glmdphkgai
       61 elngktfadd ptgyrsqfty ipetpvlyee ltlmehlelt amayglsket lekrlppllk
      121 efrmekrlkw fpahfskgmk qkvmimcafl aepelyiide pflgldplai nallermnev
      181 krggasvlms thilataery cdsfiilhng evrasgtlad lreqfgmrda alddlyielt
      241 keedghe
//
LOCUS       WP_010788130             713 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Bacillus atrophaeus].
ACCESSION   WP_010788130
VERSION     WP_010788130.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..713
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=78770
     Region          3..615
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mfkkkkriii plfilavtaf laligyisii flghyvidek klilhasski vdqngdevas
       61 lytenrepvt fadipkhvsk afvavedkrf yehhgidlqs vgravyrdil aggkveggst
      121 itqqlaknif ltndktflrk tkeviiainl erdyskdkll emylnqlyfg hgvygiqaas
      181 hyyfnkevkd ltvsegavla aipkapstys pilhpdknke rrdtilsmmn eqgiisakea
      241 vraqgqtlgl hikkksetpw fdsyidlvmk eaetkysisg eqllqggyti kvpldsklqk
      301 taytlmkess yypgsdenae gsavfinnkt ggvkaaiggr eytsrgynrv tavrqpgstf
      361 kplavygpam qekkfkpysl lqdemktygd ytpknydgqy rgevtmsdai tysknapavw
      421 tlnevgieta ksylkangid ipddglalal gglekgvspl qlagafhtfa aggaytepff
      481 itkitdedge tvaghkasak rvfskqtawn mtrmlqqvvk kgtatsgvyh gdlagktgtt
      541 sfteipgatk dawfagytpd tagtvwmgyd ktdknhylkg gssyptrlfk diltqageng
      601 safskpdkvk elespivlep vktvtadytf kaaglftvvl kwdaqedkrv vyriyvkkdg
      661 eetlldsteg kdsydipyan lfsgasykiv pyntqtkkeg egtdyvqpkl fss
//
LOCUS       WP_010788204             284 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Bacillus atrophaeus].
ACCESSION   WP_010788204
VERSION     WP_010788204.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18662707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..284
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30546
     Region          11..123
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          159..275
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mpmsdaalsv ltekdvpgls alcrhagwpg yderelglll qngrlfgykn segtllscsg
       61 ifsygafasl glvivqkefr gaglgkkmve acigelnnti pimlvateqg lplyqkagfq
      121 qissiykyvc drflphtads didiapfqpk dfqaltktdr aafgtgrerl lqqlisgcle
      181 cavaknkdgs ivgyglsrqt pdslrigpli apsrecaall inelangkqg riridisgdy
      241 rcidpdlaam gfvrdtespl mvlqkssfpe rnghlvavts qglg
//
LOCUS       WP_010788213             280 aa            linear   BCT 01-JAN-2025
DEFINITION  YitT family protein [Bacillus atrophaeus].
ACCESSION   WP_010788213
VERSION     WP_010788213.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..280
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30388
     Region          4..280
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mvleltkkii ivvigallna aglnlflipa dvyasgftgv aqllssvvdq yapfyistgi
       61 llfllnipvg ilgwlkvgrs ftvysilsva mttvfmgvlp etslshdill navfggvisa
      121 vgigitlkyg gstggldiia mvlakwkdkp igtyffilng iiiltagllq gwekalytlv
      181 tlyvttrvid aihtrhmklt amivtkkade ikeaiygkmv rgittvpakg aftnepkemm
      241 vivitryely dlekivkevd pkaftnivqt tgifgffrkd
//
LOCUS       WP_010788267             761 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent helicase [Bacillus atrophaeus].
ACCESSION   WP_010788267
VERSION     WP_010788267.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..761
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=87440
     Region          136..750
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mkcarlndrt ihlhtysreh yqflyeeavk ghlfcahcgr pvimrldilq epeflhrekg
       61 dfsaceeach stprkqeakk edyeesgvfr lpkgkaisad kspvltewqp prkinpgtpf
      121 lkkpeaqhls lfptiglntd qlqavteteg pllvlagags gktrvltara ahmiehlgvs
      181 penmllvtft tkavaemker maneyglapq hvgrlvtgtf hslfykilyh ydsskwngdh
      241 llkmewqkeq yikkalyeeg adekefpvdq aiqqisywkn sylpgeripl kdewekqvyr
      301 lyehyerqkk ehgqfdfddm asacyelfqs rpdilehyqt rftyilidef qdinpvqyki
      361 mqmlaspeqn lccvgdddqs iyafrgssps fildfqkdyp gaktvyltan yrsthpivss
      421 adlvvkknkk ryvktleatr ddvqhpvlfy pydeeeeatm vvsdikekiq ngarpedfav
      481 lyrtnsggra iyerlhqssv pyttdrgvqs fysrrivrqi laylyvsqne ddteaikhll
      541 palflkqsal ntlkalsite dcsmvkaltk lpdlkpfqln kikkivpffa slrtmkpvea
      601 itfaegkmgf seylkkrgne gnklekgsdd lrdvkvvakk fktipdflah vdhmraaekn
      661 ktaengvqlm tvhrskglef ktvyvlgavd gsiphdfsle tarkgdetal eeerrllyva
      721 mtraeqhlyi scpanrrgkt ahrsrflqpl mllnkrsslh k
//
LOCUS       WP_010788322             125 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Bacillus atrophaeus].
ACCESSION   WP_010788322
VERSION     WP_010788322.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10547098
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..125
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13657
     Region          2..122
                     /region_name="bPH_1"
                     /note="Bacterial PH domain; pfam08000"
                     /db_xref="CDD:462337"
ORIGIN      
        1 mgfingmfgn astvskasve aelasilieg esvdaafklv rdlivftekr lilvdkqglt
       61 gkkteyqsip yksisrfsie tagrfdldse lniwisgtel pavskqfkkd dsiydiqkvl
      121 aavcm
//
LOCUS       WP_010788407             271 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Bacillus atrophaeus].
ACCESSION   WP_010788407
VERSION     WP_010788407.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..271
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=31061
     Region          1..270
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mfifllslai ilsipfiyra thntkdvkvn titvnqnnag askkqltilh lsdlhlenis
       61 vspeqlldlt kknsidiial tgdfldrkrn ipklanylda lqelkpkygm yavfgnhdyv
      121 lkendfqrlk qvleehgcrt lqnehvqiqt eegflniigi ddystkrsni pdsykglkdg
      181 yhlvlthdpn ivldmekfrf dyllsghfhg gqihwpkpyh mvkmgklvrm nmikglhyhh
      241 dkpfyisegl gqtgvnirvg srpevtfhqi s
//
LOCUS       WP_010788394             277 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Bacillus atrophaeus].
ACCESSION   WP_010788394
VERSION     WP_010788394.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..277
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31869
     Region          165..273
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 mklneklftf fsdhveqmat ewidtmeetd pdsiyalkdp vvveelteqd kefyrnlnqm
       61 yikpekeflq vfqewvielt ndqkhldtpv qyvirefmrn rtlykkyfdt fvasnssefa
      121 egeskkwadl ivkvfdftiy tfvdhaekna kkqlnaqrem ildlsspvit lsqrtallpl
      181 vgdidterak filentldac akrrvehlli dlsgvvvvdt mvahqifkli ealtligvss
      241 tlsgirpeia qtavqlgvdf tnikikanla qalnydk
//
LOCUS       WP_010788438             282 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Bacillus atrophaeus].
ACCESSION   WP_010788438
VERSION     WP_010788438.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..282
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31736
     Region          161..269
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 mkdelkyige kivqyeeala rnvadieins lgrrleeerq alsgityreq litylgqaly
       61 qdmqevteri sewskqagem firlnvslse slraisfyrt viwnvfteel eqrkfaaitm
      121 ldvskmldpl fdkvssiige vyeqhnnrlm kiaytaleel svtvvpvaet iaviplvgai
      181 dthraklimd islnegarlk lkhiildvsg vplidtmvad qifhivnalr ltgikamitg
      241 ihpeiaqtiv slgldfgdik tratlqqalk elgftqdkmq kg
//
LOCUS       WP_010788476             229 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus atrophaeus].
ACCESSION   WP_010788476
VERSION     WP_010788476.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..229
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25363
     Region          1..219
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 miqlskvkks yqigketfdv lhsidllieg geyvsimgps gsgkstimni igcldrptsg
       61 iyrldgedis sykdkelaav rnksigfvfq qfqllprlna kknvelpmiy sgfnkkerqe
      121 raekalekvg lkdrmlhmpn elsggqkqrv aiaraivnnp kliladeptg aldtktsaai
      181 meqftelnae gttivlvthe seiadytnrv itvrdgeivp lqeqrrvge
//
LOCUS       WP_010788505             403 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Bacillus atrophaeus].
ACCESSION   WP_010788505
VERSION     WP_010788505.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..403
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=43780
     Region          1..352
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mlkrmlksyd yslifaiill cgfglvmvys asmitavsry gvnsdfffnr qvlffiagsi
       61 lfiimalfpy kalanqkfqk imlltslial ialfgfghva gnaqswfkif gisiqpgefv
      121 kltvilylaa vyakkqsyid qlltgvappv vvtviicsli aiqpdlgtam iigmialcmi
      181 lcsgfsgktl lklvvmggiv lllvsplvyf nldsiltegr larfesfenp fnyanssglq
      241 vvnsyyaigs ggifglglge siqkygylpe shtdfimavi aeelgvfgvl fvifllsfiv
      301 lkgfyiarkc edpfgsllai gissmiaiqs finlggvsgl ipitgvtlpf vsyggsslll
      361 llgstgilvn ismfvdyfek kkkkedlspk glkkkqvkks vyl
//
LOCUS       WP_010788535             261 aa            linear   BCT 01-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Bacillus atrophaeus].
ACCESSION   WP_010788535
VERSION     WP_010788535.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..261
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30041
     Region          18..247
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mrpdhereki vnieeripki keqrkqkanr rlisfillff vmtliivylq tpiskissva
       61 isgnenvtkq eilslsdikn gdtefwsldk kktekkiqqn klvkkaqisk slpnkinisi
      121 eeykaiaylq kdnvyyevle ngsvlpnevt pddagpilvn wkntkkriqm akqldalses
      181 lkqsiseiyy tptkmdnnri kmfmndgyvv taslktfadr mktypsiisq lkgdkkgiih
      241 levatyfeef gknnsddkke d
//
LOCUS       WP_010788709             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010788709
VERSION     WP_010788709.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18916717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..277
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32411
     Region          6..112
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(7..9,23,41..43)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            44
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(55,58,62..63,72,84,88,94,98,101..102)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          126..272
                     /region_name="SOUL"
                     /note="SOUL heme-binding protein; cl46436"
                     /db_xref="CDD:480776"
ORIGIN      
        1 mvkkflsigd msklnnvsiq tlryydkigl fkpeyvnpdn hyryysirqi fyldiikylk
       61 higtsleeir siialppesi yeflkkqelt ieeqmkklen ihqslkhhks qlheqillnn
      121 qehgvvytrk iderlvlkvd ckdtvtpldq pdiyfrelad alekegtvvd lqygciyplk
      181 hyestekihy sslytniskt dlnstgvsvd sipkgtymci afkwskadyy dhfnklkkay
      241 fssgfpiend vyevslpnny assneedfit elqiqid
//
LOCUS       WP_010788731             174 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Bacillus].
ACCESSION   WP_010788731
VERSION     WP_010788731.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..174
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=18644
     Region          34..167
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 maklngvdms iieglveqyk knpaegtgsw sssvkwdngf hveakvgdha pihvdepkwl
       61 agsnkganpv eyllsalgsc lsvgfianas gmgikinsle vevsgqldln vflglkegnp
      121 gfdeinahfn vdsdadehqi eelvaqamkl spvkntiqrn vhvqaslshn kkke
//
LOCUS       WP_010788733             242 aa            linear   BCT 01-JAN-2025
DEFINITION  DsbA family oxidoreductase [Bacillus atrophaeus].
ACCESSION   WP_010788733
VERSION     WP_010788733.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..242
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26996
     Region          3..205
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(11,14)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mkievwsdva cpfcyigkqn lqkalaqfpf kdevkveyks feldpsasvy ngqsyyekll
       61 pkfgdsgqtk qflenltqna kkvgltfnle glkptntfds hrltkwaktk gkeadisetl
      121 lyahftdskd vgdhetladl aeasgldrqe alkvlndksl yadevrsdqi eakrygisgv
      181 pfliinhkya vsgaqpaeaf lealnkvwee enpllklknl svnseddtlc tdgscgiptr
      241 kk
//
LOCUS       WP_010788734             111 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Bacillus atrophaeus].
ACCESSION   WP_010788734
VERSION     WP_010788734.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..111
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12857
     Region          11..103
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(32,35)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mvetveltsl dsidnfihhn kfsflyisrp dcgvchavlp qlrdlldkfp hiklgyinay
       61 nveeiasrfs iltvpalllf iegteylrea rfvhferlek rlekvskiyt t
//
LOCUS       WP_010788735             144 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Bacillus atrophaeus].
ACCESSION   WP_010788735
VERSION     WP_010788735.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..144
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=15201
     Region          10..138
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 msnlnvklna vwkggvkgng tiksqyidtp iaigteyggn gegaspkeil vssvqacyva
       61 tlvsmvesrk lpvvsievds emvasdssfd iihyprvvls adatekevqs mqrvneaadr
      121 acivgnmvkk agveievkgr vstl
//
LOCUS       WP_010788781             224 aa            linear   BCT 01-JAN-2025
DEFINITION  SOS response-associated peptidase [Bacillus atrophaeus].
ACCESSION   WP_010788781
VERSION     WP_010788781.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..224
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=25661
     Region          1..222
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgrftlfse fddileqfdi dqflpedeyd psynvapsqn iltiindgss nrlgklrwgl
       61 ippwakdeki gykminarae tladkssfrk plisnrciip adsfyewkrl dpktkipmri
      121 klkstnlfaf aglyekwnsp qgnpiyscti ittkpnelme dihdrmpvil phdnqkawln
      181 pqntdaaylr slllpydadd meayqvsslv nspknnspel iesh
//
LOCUS       WP_010788912             378 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Bacillus atrophaeus].
ACCESSION   WP_010788912
VERSION     WP_010788912.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..378
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43291
     Region          129..370
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvkkylkfqk lsgispyiwt iffilpfyfi fkssstlvii igivltllff svyrfafvsk
       61 gwaiymwafi ligistasit lfsyiyfaff iayfignire rvpfhilyyv hltsaavaan
      121 fsfvlkrelf ltqipfvvit lisaillpfs irirkdrerl eeklefaner iselvkmeer
      181 qriardlhdt lgqklsligl ksdlarkliy kdpeqarael ksvqqtarts lnevrkivss
      241 mkgirlkdel vnikqileaa gieliyeekq tpasisllne nilsmclkea vtnvvkhsga
      301 ttcridvhqq wkeviitvtd dgcfkgteqy fskghgllgm kerlefangs lqidtengtq
      361 ltmkmpnesk ikekegsk
//
LOCUS       WP_010788918             163 aa            linear   BCT 01-JAN-2025
DEFINITION  TraR/DksA family transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010788918
VERSION     WP_010788918.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..163
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18285
     Region          3..118
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 maltkeqtqh lyhklldlqk elsgpkkate smteeagels ngvdnhmadh gslytdrmtd
       61 qtvkevdrel ldevnnalqk ikdgtygice atgeeipyer ldavpyarmt veaqtdreea
      121 lepdapavek efhaqvkdls nketidqkss atyevldreq dsk
//
LOCUS       WP_010788921             495 aa            linear   BCT 01-JAN-2025
DEFINITION  aldehyde dehydrogenase family protein [Bacillus atrophaeus].
ACCESSION   WP_010788921
VERSION     WP_010788921.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..495
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=53931
     Region          21..489
                     /region_name="ALDH_F1-2_Ald2-like"
                     /note="ALDH subfamily: ALDH families 1and 2, including
                     10-formyltetrahydrofolate dehydrogenase, NAD+-dependent
                     retinal dehydrogenase 1 and related proteins; cd07091"
                     /db_xref="CDD:143410"
     Site            order(164..165,167..168,191,194,223..224,228..229,
                     242..245,248,251..252,266..268,300,397,399,425,463)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143410"
     Site            order(168,266,297,300)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143410"
ORIGIN      
        1 mssltmqisk rletflqgtk klyidgkfvp sasgatfvtp npatgetlmt lfeaqaedvd
       61 kavkaarkaf dqgewrtmpa asrsrlmykl adlmeehqte laqletldng kpisettngd
      121 iplaiehmry yagwstkitg qtipvagsyf nytkhdpvgv vgqiipwnfp llmamwkmga
      181 alatgctiil kpaeqtplta lylaelidea gfpdgvinii pgfgetagea lsnheevdki
      241 aftgsteigk kimetaaksi krvtlelggk spniilpdan lkkaipgaln gvmfnqgqvc
      301 cagsrvfiqk drydevvsem vtyaeslrqg aglhkdtqig plvskeqher vlsyiqkgkd
      361 egakavtggs cpyeegyfvs ptvftevedg mtiakeeifg pvltaipydt vdevierann
      421 teyglaaglw tenlkhahyi adrlqagtvw vncynvfdaa spfggykqsg lgremgsyal
      481 nnytevksvw inled
//
LOCUS       WP_010788948             200 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Bacillus atrophaeus].
ACCESSION   WP_010788948
VERSION     WP_010788948.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..200
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22035
     Region          8..199
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mkyiyekgts dnvllllhgt ggnehdllsl grfidpgahl lgvrgsvleh gmprffkrls
       61 egvfdeedlv ertkelkdfi deaaetlefn rnnviaagys nganiaasll fhfggavkga
      121 ilhhpmvpir glelpdmkgl pvfigagkhd plctraetee lqqylneaga stavywqegg
      181 hqltqqeaeq armwyqdafl
//
LOCUS       WP_010788976             263 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF817 domain-containing protein [Bacillus atrophaeus].
ACCESSION   WP_010788976
VERSION     WP_010788976.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..263
                     /product="DUF817 domain-containing protein"
                     /calculated_mol_wt=30567
     Region          1..251
                     /region_name="YoaT"
                     /note="Uncharacterized membrane protein YoaT, DUF817
                     family [Function unknown]; COG3739"
                     /db_xref="CDD:442953"
ORIGIN      
        1 mrplkqlvrf gweqalsclf pvvifaslai tqimplpflp rydwlliicl lmqwqmvrsg
       61 letrdelkvi tlfhliglal elfkvhmgsw sypeegyskv fgvplysgfm yasvasylcq
      121 awrrlkvelv kwppfwavvp laaaiysnff ihhywidvrf wlsglvmivf wrswvtyevg
      181 gtryrmplal sfvligffiw iaeniatffg awkypnqtda wslvhlgkvs swlllvivsf
      241 livatlkqvk gknstwkdts qfl
//
LOCUS       WP_010788987             168 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase [Bacillus atrophaeus].
ACCESSION   WP_010788987
VERSION     WP_010788987.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..168
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19145
     Region          1..159
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(5,22,27,57,95,101,114)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(7,14,44..46,96..99)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 misfifamde nrligknndl pwrlpndlay fkkvttghai vmgrktfesi grplpnrkni
       61 vvtsadkaef pgctvvrtie dvlttasdae ecfviggaql yqalfpyadr lymtkihhtf
      121 dgdryfpefn edewelisee qgikdeknpy nyeflvyekk nsseaggl
//
LOCUS       WP_010789017             644 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Bacillus atrophaeus].
ACCESSION   WP_010789017
VERSION     WP_010789017.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..644
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=74212
     Region          35..618
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mttsrlpfsl tktknfyeel nnwigdvfyd ilpekgfdlr deqifmafql erafkeknvm
       61 faeagvgtgk tlvyllfais yaryvgkpav iacadetlie qlvkkegdis klsehldlki
      121 dtrlsksheq ylclkklekt mqrsdddkwl dlyealpsfv hesqamqrfh pygdrkqyan
      181 lsneewsqvn ydsfqdcltc dmrhrcgltl srdhyrkstd liicshdfym ehvwteesrk
      241 regqlpllpd hsavvfdegh llefaaqkal tyrvkqstle mflerllqnd ireefaelie
      301 dslaandeff yvlteeskev agshrleikn dkrvkqaade lcrlldkige alvfesemyt
      361 idqyalsvve eyieqmahsl slyqknaisw leqkeadstf vvmprtvsev lgekvfskki
      421 pfifssatls eggsfdyiag slgirdylsl tvdspydyee qmavnlygee kgneltaeqk
      481 taqtietikh yngrtlvlfp sfaeldlfke qssawdlpyp myfegdeeis nlvekfqqde
      541 esvlcsvhlw egldipgdsl knvtiwslpy ppydpvftak rngakkdpfq evdlpymllr
      601 lrqgigrlir snqdsgsini yvsgeketvl nevknilpvd pish
//
LOCUS       WP_010789022             749 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Bacillus atrophaeus].
ACCESSION   WP_010789022
VERSION     WP_010789022.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..749
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84341
     Region          5..729
                     /region_name="YprA"
                     /note="ATP-dependent helicase YprA, contains C-terminal
                     metal-binding DUF1998 domain [Replication, recombination
                     and repair]; COG1205"
                     /db_xref="CDD:440818"
ORIGIN      
        1 mkkkslaeli selkgsehvv nwheieprka rtkpmpdsid sriktalgkr gidelfthqf
       61 safqsvqkee sivtvtptas gktlcynlpv lqsiaedpsn ralylfptka laqdqkseln
      121 eiieemgvdi ksftydgdts pairqkvrka ghivitnpdm lhsailphht kwvslfenlk
      181 yividelhty rgvfgshvan virrlkricq fygsspific tsatianpke laeqltgspm
      241 rliddngaps grkhfvfynp pivnkplnir ksatievnel akeflknkvq tivfarsrvr
      301 veiilshiqe lvkkeigtks irgyrggylp kerreiergl rdgeilgvvs tnalelgvdi
      361 gqlqvcimtg ypgsvasawq qagragrrhg ealivmvans tpidqyivrn pdyffdrspe
      421 sarinpenli ilvdhlkcaa yelpfkadee fgpldvtdil eylqeegvlh hnsgryhwan
      481 esfpatnisl rsasqenvvi vdqsdianvr iigemdrfsa mtllhdeaiy lhegiqyqve
      541 kldwdhkkay vrkvdveyyt danlavqlkv leidktidrk qtslhygdvt vnalptifkk
      601 ikmttfenig sgpiylpeee lhtsaawmei keidphlgek tleqlllgia nvfqhivpvy
      661 vmcdrndihv vsqikaahtg rptiflydhy pggiglaedv ykrfaeineg akrlitncpc
      721 qdgcpscigt eiegikakdn ilrilnqfn
//
LOCUS       WP_010789034             393 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Bacillus
            atrophaeus].
ACCESSION   WP_010789034
VERSION     WP_010789034.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..393
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42945
     Region          1..392
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(98..100,124,174,205,234,236..237,245)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(101,134,198,243..245,274,277)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            237
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mklakrvsal tpsttlaita kakelkeagh dviglgagep dfntpqhiid aavrsmnegh
       61 tkytpsggla slkesivekf krdqqieyks seiivctgak halytlfqvi ldeedeviip
      121 tpywvsypeq vklaggrpvy vdgleenqfk ispeqlksai tdktkaivin spsnptgvmy
      181 tedelsalge vclehdiliv sdeiyeklty ggrkhvsiaq lsdklkeqti iingvskshs
      241 mtgwrigyaa gaqdiikamt nlashstsnp tsiaqygaia ayngpseple emrvafehrl
      301 ntiyakliei pgftcvkpeg afylfpnake aahscgfkdv defvkallee ekvaivpgsg
      361 fgspdnvrls yatsldllek averinrfve khn
//
LOCUS       WP_010789157             330 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Bacillus atrophaeus].
ACCESSION   WP_010789157
VERSION     WP_010789157.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..330
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36320
     Region          4..330
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 msknrhtalg lsdneaidiy rtmllarkid ermwllnrsg kipfviscqg qeaaqvgaaf
       61 aldrdndyil pyyrdlgvvl tfgmtatdlm msgfakeadp nsagrqmpgh fgqkknrivt
      121 gsspvttqvp havgialagr mekkditafv tfgegssnqg dfheganfaa vhklpvifmc
      181 ennkyaisvp ynkqvaceki sdraigygmp gvtvdgndpl tvyqavkear erarrgegpt
      241 lietvsdrlt phssddddms yrtkeevtea rkndpllnyq aylqetgllt eetetkmlee
      301 imtivnqatd eaekapyaap estldnvyae
//
LOCUS       WP_010789277             445 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Bacillus atrophaeus].
ACCESSION   WP_010789277
VERSION     WP_010789277.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..445
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48549
     Region          16..440
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mtfqketvik wvrfsppqvl aigffltimi gslmlklpia sngpltwida lftsasattv
       61 tglavvdtgt eftvfgqivi maliqigglg fmtfavlivi mlgkkiglke rmlvqealnq
      121 stiggvirlv kvlfmfsisi eltaffllsf rfvpeygwgy glftslfhav safnnagfsl
      181 wpdnlmgfag dpavniiitf lfitggigft vlydiwtyrr fkafslhtkl mlsgtlllnv
      241 lamlviltle ysnpgtlgsm hftdklwasy fqavtprtag fnsvdfgsmr ectlvfilll
      301 mfigagsgst asgiklttfi vimmsviafl kgnkdtvifr rtvkhaviik slavsvislf
      361 ivfigifalt itehapflqi vfetfsafgt vglsmgltpe lstagkciii vimfigrigp
      421 ltlvfsfakt eksnirypdg evftg
//
LOCUS       WP_010789239             319 aa            linear   BCT 01-JAN-2025
DEFINITION  PhoH family protein [Bacillus atrophaeus].
ACCESSION   WP_010789239
VERSION     WP_010789239.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..319
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=35318
     Region          12..317
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 maehllainq rlkstdeals lfgnqdaylk lmekdlnvni vtrgetvyvs gdeetfqiad
       61 rllgsllali rkgieiserd viyaikmakk deldyfesiy eeeitknakg kpirvktigq
      121 reyvaamkhn dlvfgigpag tgktylavvk avhalknghi kkiiltrpav eageslgflp
      181 gdlkekvdpy lrplydalhd vlgtdhterl lergvieiap laymrgrtld dayvildeaq
      241 nttpaqmkmf ltrlgfgskm vitgdvsqid lpkgvksgla vardmlnris gisvieldqt
      301 dvvrhplvak iieaydkqn
//
LOCUS       WP_010789294             286 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus atrophaeus].
ACCESSION   WP_010789294
VERSION     WP_010789294.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..286
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32775
     Region          5..221
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 menvielkhv yksfgdfqlk dismtvkkgf itgfiggngv gksttiklim nllqpdsgsi
       61 sifgldhkeh ekeikrrigf vfdenifyah ltlaemkemi rpcymnwdds lfnhyveife
      121 lplnkkiksf skgmmmkasl sialshhael iimdeptsgl dpifrrefld ilhnimqdgk
      181 ktiffsthit tdldriadyi tfihngehif tkksyqiqee yaivkggvel ldrdteqefi
      241 sirksnagfe altankarie dvfgdlvlie kptieelmfy tkkgak
//
LOCUS       WP_010789295             125 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010789295
VERSION     WP_010789295.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..125
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14266
     Region          3..116
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mqiiisnhsk epiyeqiyaq ikkhilsnel hagqslpsmr qlakdldisv ittkrayeel
       61 ekngfiysvv gkgsfvseqd semikerkmk vieeqlltai qnskeigisl telkdiltll
      121 yreee
//
LOCUS       WP_010789299             342 aa            linear   BCT 01-JAN-2025
DEFINITION  ketopantoate reductase family protein [Bacillus atrophaeus].
ACCESSION   WP_010789299
VERSION     WP_010789299.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..342
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37089
     Region          1..322
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mriavlgags lgtivgayla aggmdvelid tyqahvdaln hkgakvigtt dfqakvkait
       61 penksgkydl vllltkqlyn dsvlqellpf lgadsivcsl qngipeekva sivgrertia
      121 gsvefgatfi epgvsrltte ythfkkyafq igelngeite riqriksmld lvggthisdn
      181 lvgtkwskll innafsglsa alngkygdil dneigivsav hiadetikvg hangvtfakm
      241 ggldieslel tsendlpdri qtfraamess rllkasmlqd iekkrkteid yingvvprlt
      301 egkgistpyn dmvvklvkta eqyqtvpnfd vnikfikdli ra
//
LOCUS       WP_010789317             309 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidase U32 family protein [Bacillus atrophaeus].
ACCESSION   WP_010789317
VERSION     WP_010789317.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..309
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=34801
     Region          1..306
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
ORIGIN      
        1 mktpellvtp tntadilpli qagataflvg eqryglrlag eftrediqta vniahkegak
       61 vyaavnglfh ndkvtelgdy laflseagvd aavfgdpavl maaresapel klhwstettg
      121 tnyytcnywg rkgavravla kelnmdsive ikenaeveie iqvhgmtcmf qskrslvgny
      181 feyqgkvmdi egkkketglf lhdkerhnky pifedength imspndvcii deleelidag
      241 vdsfkidgvl ksseylievt rmyreaidlc iekrdeyedk kegwieries iqpvnrsidt
      301 gfffketvy
//
LOCUS       WP_010789318             217 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Bacillus atrophaeus].
ACCESSION   WP_010789318
VERSION     WP_010789318.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..217
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24987
     Region          38..217
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mndryeqind yieallkpqp dkvrkletya dehhvpimeq agmevllqil svkqakkile
       61 igtaigysai rmalelpeae iytierhekr hgealnnvrd fqledrihlf ygdalelade
      121 vrpaapydvi fidaakgqyk nffhlyepml apdgviitdn vlfkglvaed yskiepkrrr
      181 qliskidhyn qwlmdhpdyq taiipvgdgl aiskkkr
//
LOCUS       WP_010789414             325 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Bacillus atrophaeus].
ACCESSION   WP_010789414
VERSION     WP_010789414.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..325
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34486
     Region          4..321
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mgkkvivlge irdgelrnvt feaisagrtv sdngevigvl igdnvsnhap qlihygadkv
       61 ltaedpqlan ytsdgysqal rtiieqekpd avimghtamg kdlspklaar fetglisdat
      121 dvsvtggnvv ftrpiysgka fervistdaf mfatirpnni ealekdesrs gdiesvqvsi
      181 adlrtiiedv vkktaegvdl seakiivagg rgvkseegfq plqeladvlg aavgasrgac
      241 dadycdyslq igqtgkvvtp dlyiacgisg aiqhlagmsn skvivavnkd peaeifkiad
      301 ygivgdlfev vpllteefkn inihs
//
LOCUS       WP_010789451             261 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Bacillus atrophaeus].
ACCESSION   WP_010789451
VERSION     WP_010789451.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..261
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29328
     Region          1..258
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mkavffdldd tllwdeksvs ttfaetclqa ekeygldpke feaavreaar elymsyetyp
       61 ytvmiginpf eglwanfsep isdgfkqlnk iapeyrrnaw tnglkafgie daaygeylae
      121 ffaaerrkrp fvydetfdvl dklkgkyell lltngdpslq keklagvpel apyfneivis
      181 gafgkgkpda sifehclgll hiskddaimv gdnvntdilg agragmktvw vnrtgkknet
      241 dvkpdyvisd lhelfailen k
//
LOCUS       WP_010789509             132 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Bacillus atrophaeus].
ACCESSION   WP_010789509
VERSION     WP_010789509.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..132
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13631
     Region          17..132
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mlsvglliir liigllfvgh gaqklfgwfg ghdlkgtggw fesigmkpgv tvallaglse
       61 lfggimfalg lltplagiii agtmvmaivk vhganglwvt nngyeynltl lavtigialt
      121 gpgqyavdtf lf
//
LOCUS       WP_010789538             435 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Bacillus atrophaeus].
ACCESSION   WP_010789538
VERSION     WP_010789538.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..435
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45782
     Region          2..432
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mfhlkehqts vkkeimagmt tfftmvyivv vnpiilsdag ipfdqvftat iiasivgtlw
       61 malaanfpia iapgmgmnay layhvvgssg gsityatafs avfiagvlfi ilsltplrkq
      121 lieaipdnlk ygittgiglf iafiglrqag iiaadksnlv tlgnlhspgv iltliglfis
      181 iilmvlnvng alfigmiata liafftgqlh ftegfisfph lpeglvisnp faafgdvihh
      241 glyavvfsfl lvtifdttgt migvaeqagl mkngqlpnar ralladstat tvgaafgtsp
      301 ttafiessag vavggrtglt sltvavlfaa smffsplvsv lsgisaitsp aliivgslmm
      361 gavsnirwge ldeafpaflv ilampltssi stgialgfis yplvkaakrk wkdihplvii
      421 failffiqlf ilesh
//
LOCUS       WP_010789513             293 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010789513
VERSION     WP_010789513.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..293
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33289
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..279
                     /region_name="PBP2_YofA_SoxR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators, YofA and SoxR,
                     contains the type 2 periplasmic binding fold; cd08442"
                     /db_xref="CDD:176133"
     Site            order(104..105,107..108,111,115,117..123,208..213,
                     219..220,222..223)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176133"
ORIGIN      
        1 melrdlqifq cvakkgsisk aavelnyvqs nvtarikqle qelrtplfnr hkrgmsltse
       61 grkmleyask illdlqelkr vfldsetptg ilnigtvetv sslpkilasy hkqfsnvdls
      121 iqagltedlv kdviefrldg afvtgpikhp qiqqydvcfe elvlvtrnqt fnleefsiep
      181 flvfsqgcgy rskleqwlke eeimpkrime fsvletilss valglgitlv prsvvkhlav
      241 dekvylhkip ekhsiistvf ihrkdtyitn slqsflqtia ayevnrchsg qdk
//
LOCUS       WP_010789557             299 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Bacillus atrophaeus].
ACCESSION   WP_010789557
VERSION     WP_010789557.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..299
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33981
     Region          38..261
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mkdmkreqll qllgdlpekr kmsistltae erendiletl lldlngiekv payfvkpknr
       61 tdkmpavlfq hshggcyerg kreltegaey liapsfsgef tsrgyavlal dhwgfgdrrg
      121 ktesgifkem lltgrvmwgm miydsmraid ylqtrsdilp drigtigmsm gglmawwtaa
      181 lddrikvcvd icsqvdhetl ietqdldrhg iyyyvpslak hfsasdiqsm iaprphlslv
      241 gehdrltpvk gmnkietalt alyqeqgasd ryrmvrsasg hfetavmrhe alrflekwl
//
LOCUS       WP_010789595             443 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Bacillus atrophaeus].
ACCESSION   WP_010789595
VERSION     WP_010789595.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..443
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48890
     Region          1..443
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mddlvlarsl fgttmgfhii fatlgvglpl milmaeliyq ktkddhyaim akrwtkaqav
       61 llgvaiptgt iagtqlallw pgfmevigrv mslpfqieiy affiealfms iyvyaadrlt
      121 pamritavvf vligaaasav litnvhafeg tpagfkivng qitdvdpwaa ffnpsffvta
      181 thvvltafmt gafivasiaa ykmirtrkne kvyrfhrkal llaliiggif svvtslnghe
      241 saqmlykyqp eklagaeglf etrshaplai ggftdaneek vkwaievpwa lsflaansfd
      301 tvvkglnafp kdewpplfih tlfngmvgia mvlilysivg llwrkvlkkd rfptwllvif
      361 vtagplslig iefgwifact grqpwviyhl lktsdvvttt gsigvlfmlf tfvyavlgaa
      421 vvyvllyyfr khpveedlka aes
//
LOCUS       WP_010789631             199 aa            linear   BCT 01-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Bacillus
            atrophaeus].
ACCESSION   WP_010789631
VERSION     WP_010789631.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..199
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22300
     Region          13..198
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mfirtenfqt firlypavac ilaiqsvlwi ffklpihsvi lwgdavtgyn lgvangewwr
       61 litpiflhag fahllfnsms iflfapaler llgkarfllv yvgsgiignv gtyftesldy
      121 vhvgasgaif glfgvylymv lyrkelidqe nskmiitllv vavlmtfins ninvmahlfg
      181 lgggfvlsfi cvqkkerrf
//
LOCUS       WP_010789657             606 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Bacillus atrophaeus].
ACCESSION   WP_010789657
VERSION     WP_010789657.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..606
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=66095
     Region          28..453
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mlhsikrfli gkplksqsag eqkltklkal amlssdalss vaygteqili ilaavsaaaf
       61 wysvpiaagv lilllalils yrqiiyaypq gggaymvske nlgekpglia ggsllvdyil
      121 tvavsisagt daitsafpgl hdyhlpiavl lvivimilnl rglsesasil aypvylfvva
      181 liiliavgty klatgqidta hhtpigtpva gitlflllka fssgcsaltg veaisnaipa
      241 fknpsaknaa ktlammgill avlftgitll afgygtapkp netvisqiaa etfgrnsfyy
      301 viqgvtslil ilaantgfsa fpqlafnlar dqymprmftv rgdrlgfsng iiflgvasil
      361 lillfggqte hliplyavgv fipftlsqtg mcvkwirqkp kgwagkmmin aagaaisfmv
      421 lsilfvtkfh lvwpvlifmp pvvllffaik nhytsvgeql rivnkpaeei kgtvvivpia
      481 gvttvveksi qyakslsdqv iavhvsfdke hekkverrwe elnngvrlvt lhssyrslvh
      541 pfdkfletve akarkrqfsv mvlfpqfitk krwhtilhnq safllrvrlf wkkdiivatl
      601 pyhfkk
//
LOCUS       WP_010789686             191 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Bacillus atrophaeus].
ACCESSION   WP_010789686
VERSION     WP_010789686.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..191
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21486
     Region          5..177
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mlqkplvili heiygvnshi kkmarlikma gydvvtpnll gdqevyslke ekaayeqfsm
       61 hnrltageki irklivrnkn agriiyvigf sagatiawkc ssmpelsgav cyygsrirdh
      121 ldihpacpvl lffpayepsf dvsdvitrik kkenrfisly lfdaphgfan pdsayfdrsv
      181 flkslsiiad l
//
LOCUS       WP_010789712             249 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Bacillus
            atrophaeus].
ACCESSION   WP_010789712
VERSION     WP_010789712.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..249
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27581
     Region          1..242
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 miqvknirka fkdlvvldgi dlevkrgevv aiigpsgsgk stllrclnll erpdqgliei
       61 geaklnaeky trkeahqlrq qtamvfqnyn lfknktalqn itealivsqk ksreeanrig
      121 mdilkqvgle hkansypitm sggqqqrigi aralavnpha illdeptsal dpelvagvlq
      181 viqsiaekqt tmiivthema farevadkvi fmadghiieq gtpeelfdhp ksertkkfik
      241 qvgepteli
//
LOCUS       WP_010789735            1276 aa            linear   BCT 01-JAN-2025
DEFINITION  non-ribosomal peptide synthetase [Bacillus atrophaeus].
ACCESSION   WP_010789735
VERSION     WP_010789735.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 1276)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1276)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1276)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1276)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   5  (residues 1 to 1276)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1276
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..1276
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=144091
     Region          7..1110
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
     Region          1060..1269
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 msqfskdqvq dmyylspmqe gmlfhtllnp gqsfyieqit mkvkgsfevk lleqsmnvmm
       61 drydifrtvf ihekvkrpvq vvlkkrpfqi eeidlshlse keqeqkiney keqdkrqgfd
      121 ltrdipmrta vfkkgeasfe wvwsyhhill dgwcfgvvvq dlfqvynalr ekkpyslkpv
      181 kpykeyikwl ekqnkqaslq ywtdylsgfe gqttfaeqrk kekadykpne llfslpeaet
      241 kaftelaksq rttlstalqa vwsillgryq rtddlvfgtv vsgrpaeisg vehmvglfin
      301 vvpkrvrlte disfngllqt lqeqslqsea hqyvplydiq sqadqpklid hiivfenypl
      361 qdansngnsq ngfemedvhv feksnydlnl maspademli klaynenvfd eafilrlksq
      421 llaaikqivq qpdtpvahin iieekerqhl lmglnpsaek peikrltewf tqsaertpda
      481 paltaggvtl tyhelntean rlahrlrksg agkgsvtalf tkrspemvig ilgilkagga
      541 ylpidpeype driaymleds gancllthlp lqneagqlpy kgevvyiddt srfeesgadp
      601 deagepddpa yimytsgttg kpkgnittha niqrvvkqtn yialserdti lslsnyafdg
      661 ftfdlyaall nggrlviaeq etilntdrlm tlirgenisv mfvttalfnl lvdagqewmk
      721 glrhvlfgge rasaahvrka lqtmgphkli hvygptevtv fatahqvqev pesmsaipig
      781 kplneteayi ltetsqlqpf gavgelclsg mgvskgylnr eeltkqkfiq hpfkpgerly
      841 rtgdlarwlp dgtiefagri ddqvkirghr ieleeiekql qeheevkdav vvvdrtetgd
      901 asinaylvce tqasskeiqa fiskqlpaym vpqsftfldq lpltpngkvn rrllpkaead
      961 lsagdewigp rnqtedmisr iwcdvlgktk igihddfftl gghslkamta asrikkelgi
     1021 elpvkllfea ptiagisdyl kngnstglqd vtvmnadqdq tifafppvlg yglmyqnlak
     1081 hlqaykicaf dfiededrld ryaamihelq pegpvtlfgy sagcslafet akkleeqgrs
     1141 verlvmvdsy kkqgvsdldg rtvendveal mnvnrdneal hneavkqglk kkthafysyf
     1201 vnlistgqik adidlltsdt dfempewlqs weeatkgsyr vkrgagthae mlqgksldrn
     1261 aeilleflse etikls
//
LOCUS       WP_010789810             286 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Bacillus atrophaeus].
ACCESSION   WP_010789810
VERSION     WP_010789810.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..286
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31575
     Region          17..278
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mdgkkteqaa alaaraftip gtesrlmcsr tgnreyqifv skpsedpppa gypviyllda
       61 nsvfgtmaea irvqsrrpek tgvipavivg igyqteapfs parhcdftlp lpdselpsrp
      121 ggtpwpeqgg aedfltfiee evkpeierdy qidtsrqtif ghslgglfvl qvlftkpdaf
      181 qtyiagspsi hwnkrfihke srqfgdrvsr eklnvnvmla agelekshks rindhakels
      241 eqlsslaghg vrtqfhefeg eghisvlpvl isralrfalh pdgpnl
//
LOCUS       WP_010789836             273 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Bacillus atrophaeus].
ACCESSION   WP_010789836
VERSION     WP_010789836.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..273
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28945
     Region          1..272
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 msymilivlg liagtvgsli glgggivivp allflssatp ffqdvtpqva igtsllviif
       61 tglsstlayi kyktvdyksg liffigsgpg siigayvskl fnsdsfsvwf gifmilisvs
      121 lmlkkkarpl nkehqgiirt frddsgepyt ysynaaagia iafavgflgg lfgigggslm
      181 vpammllflf ppkvavatsm fiiflssvtg svshvlsghv dwlyalalip gawfggklga
      241 ainkrmqtkt ivatmrivli ligcqliyeg ifr
//
LOCUS       WP_010789891             291 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010789891
VERSION     WP_010789891.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..291
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33294
     Region          2..>104
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkekekliie aaiklfaqkg ykstsvqeia deckmskgaf yiyfpskeal llsmlnyyyd
       61 kmftrihhiq tksgnprsay keqlavffen ilehkdfitm qmregslpyt eeveqcakki
      121 rqavlqfhid sllnmygaka epytaelcfl iegisqiyle liivtgqtlk peqlaetvik
      181 riddmvngma ernedpfisl deasslfgpl yhgrpdplse siikeiriki gkmntisape
      241 ltesldilea emkkktpkqa iikgmilnlk eseaiskeae qlryllkqqf i
//
LOCUS       WP_010789898             423 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bacillus atrophaeus].
ACCESSION   WP_010789898
VERSION     WP_010789898.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..423
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45955
     Region          15..402
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(25..26,29..30,33,65,120..121,123..125,128,148,
                     151..152,155,237,240..241,244..246,249,273,277,329..330,
                     334,338,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mvkfidgesv wkrnfnylfy srlvkisads fafnsilwll iydgegaigt alliavtflp
       61 eaflapitgp fmkkntlkfw myfsditraa vvliipicyf ngfsplwfvm almilhsatg
      121 aaynpasvai ipqivneqgi qkanallqss aqivrlgaft lcgailtfig paytmlfali
      181 lylisgflvl fikyktvqtk tmdlpaatqr gtyfgrlkrg fvlvrkhqil yplaiycifm
      241 nlaaapweal savyvaeeln slpitfsllk avtsggaflm gfllakvkvn kygllfvtag
      301 iiegiaffit gmntflplvf laafafgaav sainvpeyti iqtsvdeedq pqvyavihmi
      361 snlslpagai acgyaanafg sgkviavgga ieilagigil lftklakaqr sdlirereas
      421 vhi
//
LOCUS       WP_010789912             408 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Bacillus atrophaeus].
ACCESSION   WP_010789912
VERSION     WP_010789912.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..408
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44207
     Region          3..408
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mlenirisfq silshklrsi ltmlgviigi aaiiaivsmi kgqseqlkqs migmgnnsin
       61 vvyqqnggee egfhelsytt appisdetie sitsdpmvkg vslyhlaegv tafhltnsay
      121 pqvygvdqdy fnmfpirite gkaltdkelg skhqvvmine dardelfpdg dainkkvein
      181 gmpfrvaaif tekkqdesmy ygeygnpify lpkgvwplie gfdaptqiav qadssdhiqe
      241 agmmaadlln aslpeaelek aeysvtdlqe iaeemesfnq afalllggia sisllvggig
      301 vmnimlvsvt ertreigikk algakrrvil fqflteavvl tslggilgvl agcgiaklit
      361 vfypmpfivs vpavagalif smavgiifgl lpsikasklq pvdalrye
//
LOCUS       WP_010789914             269 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus atrophaeus].
ACCESSION   WP_010789914
VERSION     WP_010789914.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..269
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29904
     Region          4..255
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mdslsteqlg igygdrlive dlnisipkgk ittligpngc gkstilktms rilrsktgav
       61 ylngngihqm stkdiakdma ilpqtpeaps gltvyelvsy grfphqsgfg riqaedrrii
      121 kqaleetgma eyherpieal sggqrqrvwi amalaqgtel llldepttyl dlahqleilq
      181 lleklnkqqg rtilmvihdl nhaarfshym ialkkgkvvk egtaeevmtp dvlkqvfqid
      241 aeivndprtn kpicltydli qhdkliehv
//
LOCUS       WP_010789927             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: trimeric intracellular cation channel family protein
            [Bacillus].
ACCESSION   WP_010789927
VERSION     WP_010789927.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..202
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21493
     Region          1..195
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mawellsvig iiafavsgai vameeeydil gvyilgivta fgggairnvl igvpvsalwe
       61 qgaffqiala sitivflfpk lllkhwnkwg nlsdaiglaa ftiqgalyav kmghplsavi
      121 vaavltgsgg givrdllagr kpmvlkaeiy avwaalggli vglgwmgnsv glyvlfimlv
      181 acrvcsymfk wklpnrsfyv nn
//
LOCUS       WP_010789979             447 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Bacillus atrophaeus].
ACCESSION   WP_010789979
VERSION     WP_010789979.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..447
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49282
     Region          2..446
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mekdkqtlkr tmtsrhimmm alggaigagl fkgsstaidv agpsviiayl iggiillfim
       61 qglaemavrn snartfrdlv qsvlgnyaay fldwiywkmw vlniaaeavv aaiflqywlp
      121 dcpiwalalg isllvtvvnl lsvkifaete ywlalikiav ivifiilgll llfftfgnhs
      181 avglsnlteh ggffphgpsg litamlvviy syggteiigv tlaetknpek vvpkavrstl
      241 trivafyllp ffiivslipw nqvnsvpesp fvmvfkmvgv pgadhimnav illaiissmn
      301 sglygssril ytqamdgrvp kmfsklskkk vpvyailmct sflyvgvlis lfagsqtfty
      361 lmgslgytvl fiwliigfah lksrknqtem psyyvkwfpy ttwfailsli ailigviltt
      421 sivitcitaa iyllitaayv wkgrrhq
//
LOCUS       WP_010789988             202 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar transferase [Bacillus atrophaeus].
ACCESSION   WP_010789988
VERSION     WP_010789988.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..202
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23029
     Region          <1..183
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 miakrvfdlt aailllccas liivfamcii rlkigspvff tqvrpglngk pftlykfrtm
       61 tderdkegnl lpdevrltkt gklirklsid elpqlwnvik gdlslvgprp llmeylplyt
      121 nkqsrrhevk pgitgwaqvn grnaiswekk feldvwyvdh rsffldlkil fltvrkvlis
      181 egihqsdhat serfrgsgdv sl
//
LOCUS       WP_010789999             490 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Bacillus atrophaeus].
ACCESSION   WP_010789999
VERSION     WP_010789999.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..490
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=53687
     Region          2..485
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 madltvqtry galkgtaqns vrtwkgvpfa qpptgefrfk epqapkpwsg vrnaaefgpv
       61 cpqpsdllsm sfagaempvq sedclylnvy apdtpekdlp vmvwihggaf ylgagseply
      121 dgsalaaagd vivvtlnyrl gpfgflhlss idnsytnnlg lldqiaalqw vkdnisafgg
      181 npenvtifge saggmsiaal ltmpkakglf qkaimesgas qtmpsekaad iaaafletld
      241 iepdqsellh sktsedilna adkirntnne nifsllfqpt adpdtlpvep keaiaqgaae
      301 gipfligtnk degylfftpd sevmsqaein qaleqfggqe farraaglyp pslesqihmm
      361 tdllfwrpsi tyasaqsnia pvwmyrfdwh lgrppldkai haleipfvfg nfesleaalq
      421 tkisedtkql sthiqtawit fartgdpnhs tvewpnynee trktlifnss isieqdpdad
      481 krkqlerkki
//
LOCUS       WP_010790013             161 aa            linear   BCT 01-JAN-2025
DEFINITION  DinB family protein [Bacillus atrophaeus].
ACCESSION   WP_010790013
VERSION     WP_010790013.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..161
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18688
     Region          24..152
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 mtdktifidq laacydqntw fvslkhaieg lseeqaqwks vsgtnsiqei mnhlnfyner
       61 yllrfkgeev lsskgdnntt fhagktswhd tvenmesifl swrkelhhce dekftsvayi
      121 nddepwssvl thlflhntyh igqilhirke qgswdsargv h
//
LOCUS       WP_010790009             521 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 32 protein [Bacillus atrophaeus].
ACCESSION   WP_010790009
VERSION     WP_010790009.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..521
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59043
     Region          47..517
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mikrvfnkkv ykrlsvfivc clglfigigl avhhkeekkk ttdppsyraa yhfttpdkwk
       61 ndpqkpiyfd gkyhyyylyn gdypsgngte wrhaisedlv hwtdkgvaip kytnkngdiw
      121 sgsvvvdted tagfgknaiv aimtqpsang gkqeqylwys tdkgqtftsy sedpvmanpg
      181 tkdcrdpkvi wddqagkwvm vmaegtkigf yeshnlkdwh ytggfltqht gliecpdlfk
      241 mraddgtykw vlgasangks egnpntyayw igdyngkeft aedkepqwld ygfdwyggvt
      301 fedgtssdky qkryalawmn nwdypdntpt lrdgfngtds ivrqiklahe gdngytlkse
      361 piealnslis stdtiehlev tgektlnitg dtyqldtdil wsdikntgir lresadkkrh
      421 idvgvfaegs ysyvsrasvr qpdkkktyle skapfdahnk kvhlkvlidk tsievfiddg
      481 ktvfssevfp rahdkgitlf aeggtsvfkn veikhlesiy k
//
LOCUS       WP_010790101             275 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Bacillus].
ACCESSION   WP_010790101
VERSION     WP_010790101.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 275)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..275
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32267
     Region          6..275
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mnalvkilke qfnsfplimr lavyetksky qmnylgvlwq flnpmiqmla ywfvfglgir
       61 gghdmklgng dsvsfiiwml aglipwffis ptildasnsv fkrinlvskm nfpisslpsv
      121 vivsnlfsyf vmmaiylivl lsnglfptlh wlqyiyylfc miafmfafgl fnstisvlir
      181 dyqfllqavt rllffllpif wdiaekfgdk kevltllkln plfyiiegfr dsfmegqwff
      241 qdmkytlyfw litlllltvg sllhmkfrdk fvdfl
//
LOCUS       WP_010790128             178 aa            linear   BCT 01-JAN-2025
DEFINITION  SH3 domain-containing protein [Bacillus atrophaeus].
ACCESSION   WP_010790128
VERSION     WP_010790128.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..178
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18864
     Region          50..169
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 mkrtaktlsv ftlaagvtaa salgasplqa kqpmkavsid dlysypidsy lvsaealnvr
       61 tkasassaka dtlhlgdslk misfsnadwa kvhykngktg fvsthyivke attvktttkt
      121 nvyasaagks taslpantsv sflgwnktkn ggfdydwvlv dyggktgyik tkdlqmsk
//
LOCUS       WP_010790134             695 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Bacillus atrophaeus].
ACCESSION   WP_010790134
VERSION     WP_010790134.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..695
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=78653
     Region          10..678
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mpldqrssai lylvmntnsy vtgseltehl kisrrtlyyd iekingwlke tglspikrmr
       61 smgfylednt kksllsemkt lthnsyefsp serqarvivr llirssrhll qdfiilnrvs
      121 rntaiqdmkh ireklktfgi vlsftkekgy fmsgleqqkr kllaeytnkl mqkngsksit
      181 adlcpggtay eplirkmrsi llncegllqi kyadhvlnsl svhftlflir ikagkeield
      241 qaeqyairqt keyqaavqaf etahlpveaf ipdqelcyft thllgakisq fpsscltage
      301 ldihdiadkm vvdfqryacv lfqdpeslrk hltlhlrsay yrikydisnn esdvaasiqt
      361 kysdiynltk kvvhhlekev rhtisseeta fiamhfggwm kregvvpssr kttvivcpgg
      421 igtskilqsq iedllpnvdi lstvssrvye tmavdadfli staplpdrgv pvfivnpiln
      481 sqekisllkk vdalsgaasr fhpcardlmt iiekhadvfh knellqevae ylgqpykhkk
      541 eandkpmlae lmthqnitmt hsarnweeav rlaakplldd gsitpqyiea mintikklgp
      601 yivitpkvai pharpedgvn kigmsflrlk egvsfsdqpe htaqliivla aidnethlka
      661 lsqltnmlgd peniqylina esaeqvltli kkysi
//
LOCUS       WP_010790242             458 aa            linear   BCT 01-JAN-2025
DEFINITION  YncE family protein [Bacillus atrophaeus].
ACCESSION   WP_010790242
VERSION     WP_010790242.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12830793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..458
                     /product="YncE family protein"
                     /calculated_mol_wt=49359
     Region          101..317
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          154..450
                     /region_name="PQQ_ABC_repeats"
                     /note="PQQ-dependent catabolism-associated beta-propeller
                     protein; TIGR03866"
                     /db_xref="CDD:274824"
ORIGIN      
        1 mkkndlsafq encfcfcdee isrealfqvp idipegftid saeaaaavtw stdnlscise
       61 pcliqtgpep edigvqyavr lqgtvtllvs vspvrnqygq gdgavsvihn aeidqvvyys
      121 dnpddcpdfs ditienlvvv ppfygsplsv tgtivlvpap dqrsyvftan tgdstvsvid
      181 tdvntlvsti slsdiptdlg vtldkaytyv lhrnanlvsi innetltvtq tiplagaprk
      241 iqfetgggfa yilaggssiy einissqtit ntftvspaad dfaldpngqf fyttnsvfwv
      301 vnkydintgq lidslsnfet pnlietplig dfaylengel rpnvvsvidl ttfsessqin
      361 rlfdglitiv fsadgtraff lepyydsfpe nltvvdttlh tfittaslpg aidltvtpdn
      421 qyiyvaqpaa ntvtvyrtsd ytavavipvg agpsaisi
//
LOCUS       WP_010790307             214 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010790307
VERSION     WP_010790307.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..214
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24707
     Region          9..176
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkknkfqikr eetferflda gltllidkay davsieeisk aagfskgafy vhfegkedfl
       61 khlldrrkir kriitdylne ierisarplt lqdaagraae llfchlnskp swdiasfaln
      121 mptykvlqey kayymlyelw idenifyiqw lkernlieds idteytaklm caaidgivkq
      181 snvlgtsvtf rslfdalsvf lkadknsddk tplc
//
LOCUS       WP_010790430             312 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010790430
VERSION     WP_010790430.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..312
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34996
     Region          11..309
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mdrdkqqlsi eaarlyyqsd ysqqqiaeql nisrptvsrl lqyakekgyv qirvldpfed
       61 ldalgtmlee kyglleahvv fsptadyrti thylshygae ymhdvikdgd ivgvswgttm
      121 yqiaqnmqpk hvkgvevvql kggishsrvn tyssetiqlf aealqtmpry lplpvvfdna
      181 evkkmvekdr hieriiemgk qanvalftvg tvrdeallfr lgyfneeeka llkklgvgdi
      241 csrffdangd icsnaindrt igvqladlrl kersilvagg nrkiaaihga ltgkyanvli
      301 idqhtakala dq
//
LOCUS       WP_010790477             382 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerate kinase [Bacillus atrophaeus].
ACCESSION   WP_010790477
VERSION     WP_010790477.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..382
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39479
     Region          2..374
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mkiviapdsf keslsaleaa haiergfktv fpdaeyrklp madggegtvq slvdatngcm
       61 keqfvtgplg etvkafygll gggktaviem aaasglhlvp eenrnplvts trgtgelila
      121 aldsgvkhli igvggsatnd ggagmvqalg grlldqsgnn igpgggalsq lvsidvtgld
      181 arlkdvkiev acdvdnpltg prgasaifgp qkgatpemvh lldqnlsrfa diaeralgks
      241 crdiegagaa gglgasllaf ldadlkrgid ivlefvgfed avkdadlvit gegridsqti
      301 ygktpigvak aakkydvpvi glagslslds dvvyehgida lfsivpgvit lpdafehaah
      361 ymertarnia asmktvrnay ri
//
LOCUS       WP_010790506             541 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Bacillus atrophaeus].
ACCESSION   WP_010790506
VERSION     WP_010790506.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..541
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61148
     Region          4..531
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mlnvhnltvn lagdcifqnv sffinegeki liagpngsgk stlfnvlagh lepeegniai
       61 nkgatvgllk qiaepkedmt lyqyletsfe slmeiqnemk aievklseal sdreltnlle
      121 kysklteife rnngyqmhti iddvcnglsi shlkdqpfss lsggektkag laeilirndd
      181 iilldeptnh ldvhaiewle sfikksdkti lftthdktfa nqaamkvlel ddkelriwpy
      241 gfneflkkke efivaqfeky eeqqkkiqkm kesiaqlrdw anrsnppsvg lhrrannmek
      301 alkrieiink pvkteqklkn afqeagigsk divfiengtv aqgsamlyen lnlnikhkdr
      361 vgivgrngvg kttlirciig ekqladgtik igenlkigyi dqkshvgdsn qtivqffken
      421 lmseegmarn ilakygfygs svfkklsvls ggerirlkls ilmekklnvl ildeptnhld
      481 iesqeilens lqqfqgtvic vshdrhllen fnkilwledk kvtvfvgpys yaknkrrcaa
      541 e
//
LOCUS       WP_010788549             124 aa            linear   BCT 01-JAN-2025
DEFINITION  TraR/DksA family transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010788549
VERSION     WP_010788549.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 124)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..124
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13862
     Region          1..93
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mndqltaiyt elllmkeelq srlfeyscfq vsaaaespin dnqkatliyh ikeelqdvll
       61 alskfesgtf gcceatgapi plsklavlpt artaddflys vqfekktlpl wkasdieydq
      121 alye
//
LOCUS       WP_010790545             177 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase [Bacillus
            atrophaeus].
ACCESSION   WP_010790545
VERSION     WP_010790545.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..177
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19920
     Region          9..168
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mqakrhtiiy wtlfvcnqwn vyiaatskgl cfvgskdfde lvlwaerkfp qhtlvqddkv
       61 lhpyvaelee yikgdrkeft mpidvqgtpf qlavwnalce ipygetysys diaeriqkpd
      121 svravgtaig anpvlitipc hrvigkngkl tgfrgglemk kqllslekes schsgkq
//
LOCUS       WP_010790542             448 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Bacillus atrophaeus].
ACCESSION   WP_010790542
VERSION     WP_010790542.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49183
     Region          31..438
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(41..42,45..46,49,81,131..132,134..136,139,159,
                     162..163,166,274,277..278,281..283,286,313,317,366..367,
                     371,375,391,394..395,398..399,402)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnsgqnhtqp fsnvanrldr lpisrvhyqv ltalgivyff dladlftlsn vapaliehwg
       61 iklstianvt aasflgmflg aslggrlsdr igrkkalnwf vfifsvssll nalawdipsl
      121 iafrfltglg vaaamivtns ylaeffpsnv rgkyisfcam igligvpvtn vvsafviplg
      181 pwgwrlvfvw gaagliyfls trrleesprw henrgeygka daimkrietr veqekgplpv
      241 pkeaapvqtv qkagylglfk grnlkitivl savwifetfg fygfaswvps llksngitme
      301 ktlwynvlhs vgaplgalig smisetfqrk wilaasaflt aiagllygmt fiplmiiifg
      361 fvvnitervf tsnlyaytse pyptefrssg sglayglgrf snifgsllvg fiavqlgyvs
      421 vflfiggcwl acsvlliffg pktnsqqv
//
LOCUS       WP_010790537             270 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Bacillus atrophaeus].
ACCESSION   WP_010790537
VERSION     WP_010790537.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..270
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31805
     Region          5..112
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(6..8,22,40..42)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            43
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(54,57,61..62,71,84,88,94,98,101..102)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          122..269
                     /region_name="GyrI-like"
                     /note="GyrI-like small molecule binding domain; pfam06445"
                     /db_xref="CDD:428947"
ORIGIN      
        1 mkeffsigev sklfnvnipt lryydeigll kpeftdehnn yryystqqfe rlstikylrt
       61 lglpinklld fydslevdtl ihllkdqqte idrkkrelah ierkisrrik qmedavnmpl
      121 eeiskiklpe lrvaylqhey ilgqdieypv telrtkfkvh kdiflgkvgl sisatniksn
      181 kfdryssifm vlededeits seitfpsrey lqirfkgshs eaaqyyemll tymkkhnyel
      241 agdsieitli dygvtnnpdn yvteillpik
//
LOCUS       WP_010790582             328 aa            linear   BCT 01-JAN-2025
DEFINITION  c-type cytochrome [Campylobacter jejuni].
ACCESSION   WP_010790582
VERSION     WP_010790582.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     Protein         1..328
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36128
     Region          95..297
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 mnkfsivltl llygscalal dpnlektksa tgidlptakw nlpkalnedg tidetkipkn
       61 seyskmvilg nkilnetsky vgpqakdpkk rfagnnlscs schanggsvq nqsgfvgiwa
      121 rfpqynargd kvitladrin gcfersmngk rmpsdapemk amltymqwls qgvpvgakie
      181 gqglkkidfi sraadpkkgk aiymdkcavc hqenglglkn edsagayyly pplwgddsyn
      241 tgagmyrlik aasyikenmp qgapdlsled aydvaaymns qarpikanrd kdfpdrkvkp
      301 ldmdvgpydd sfsttqhryg pytnmikk
//
LOCUS       WP_010790633             200 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Campylobacter jejuni].
ACCESSION   WP_010790633
VERSION     WP_010790633.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     Protein         1..200
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22571
     Region          4..174
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mqeiisfive tasawgylgi iilmtlescf ipfpsevvmi pagylahkge lditlcilsg
       61 tlgsvlgali nyyicffwgk nfvlkwgkyf ginetkftkf eeffnkhgef stftcrllpg
      121 irqyismpag lvkmklvnfi lftalgsaiw vailvflgyy igqneelikt yltqiliiii
      181 vfvilasliy ikikkpfkka
//
LOCUS       WP_010790657             171 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system protein [Campylobacter jejuni].
ACCESSION   WP_010790657
VERSION     WP_010790657.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     Protein         1..171
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=18620
     Region          1..>61
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mrkaftilel vfvivilgil aaialpkmss skdeaevsks lnnlktlind isiytlkndh
       61 lssiktmsnv sgvenvdlgn fndtkevnfr vgddkeclkl vfidradfil mgissneask
      121 naiinaanqs hedlenidft ssssnkacvi lsknenfknl asktylligg m
//
LOCUS       WP_010790747             129 aa            linear   BCT 01-JAN-2025
DEFINITION  ExbD/TolR family protein [Campylobacter jejuni].
ACCESSION   WP_010790747
VERSION     WP_010790747.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10021508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     Protein         1..129
                     /product="ExbD/TolR family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=14486
     Region          7..129
                     /region_name="tolR"
                     /note="TolR protein; TIGR02801"
                     /db_xref="CDD:274306"
ORIGIN      
        1 mpfddekpel nitplvdiml vllailmvta psityeekin lpqgsqknts vptvksliis
       61 inakkeifln qekydfisfa dnlaqrkaqf ntedpvfira dknlkyddvi svlrsvknlg
      121 fnkvalqte
//
LOCUS       WP_010790751             267 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Campylobacter jejuni].
ACCESSION   WP_010790751
VERSION     WP_010790751.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     Protein         1..267
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29244
     Region          7..266
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mleilnftff qnallgailv siacgiigtl vminrlfsma ggithgafgg igiafyfslp
       61 illstgiftl flaflvafla khyehrsdsi iaviwafgma vgiilidlsp syntdlmayl
      121 fgsilavgtq dlwlmalvds vvvlliflfy rqfealsfda efakvrgint sffhyllial
      181 mafcivisir lvglilvmal lsipsfiaen ftkrlgfimi lasflsmifc vlglilsyyl
      241 nlssgaciit vacfgflvhl igkflkr
//
LOCUS       WP_010790782             453 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Campylobacter jejuni].
ACCESSION   WP_010790782
VERSION     WP_010790782.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     Protein         1..453
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49895
     Region          24..437
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(37..38,41..42,45,84,142..143,145..147,150,170,
                     173..174,177,266,269..270,273..275,278,306,310,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtnqqidgia dknfntpegr kvfkkavfsc wlgtameyad falyglaaat ifsevffpeq
       61 tpvialllsf vtygigfiar pigalffgyl gdkhgrknvm matialmgis ttligfipsy
      121 avigvwapic lvalrfmqgf gagaelsggt vmlgeyapsk rrglvssvia lgsnsgtlla
      181 sfvwllmvqm deasfkewgw rvpfmgsnli alfavyirfh vketpvfekq knemmklrln
      241 nekhmkkder sfwqrsrafw tmvglrigen gpsylaqgfi vgyvtkilll dksvattavm
      301 iaslvgflvi plagylsdrf grrityrmfc lllmiyafpa fmlldsknei iviltiivgm
      361 slaslgifgv qaawgvelfg vknrytkmaf akelgsilsg gtapmvasal layygtwwpi
      421 atyfvltagi gfvttffape trgrdlnkie dai
//
LOCUS       WP_010790797             348 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Campylobacter jejuni].
ACCESSION   WP_010790797
VERSION     WP_010790797.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     Protein         1..348
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=38410
     Region          51..343
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 mskkfflslg lvvllfsnsq aidenlikaa qaegrvnsla mpdtwanwkd twadlknlyg
       61 iehsdtdmss aqeiakfkae kknasgdigd vgasfgeiav kqgvaqpfkt sywdqiptwa
      121 kdkdgnwlla ytgtiafivn kdvvkdipkt wqdllkgnyk itvgdvsvaa qavsavlaan
      181 yalsgdekdl spalaffntl akqrrlvnnd vsianlekge vevglvwdfn glgyrdkvgk
      241 dryevlipad gsvisgytti inkyakhpna aklarefils dkgqinlakg yarpiridhi
      301 tlpddikakl lpseqyknar aikdqkawek sakelpqlwq ekvivdmk
//
LOCUS       WP_010790832             517 aa            linear   BCT 01-JAN-2025
DEFINITION  peptide MFS transporter [Campylobacter jejuni].
ACCESSION   WP_010790832
VERSION     WP_010790832.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     Protein         1..517
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57409
     Region          9..517
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 msknvknldt sffghpkpll slsltelwer fsfygirpll ylfmiasfek sgmnlkpeea
       61 saimgifasc lylaalpggw ladnylgqkr aillgaliia fghlciafsy fnnkiifvgm
      121 vflvigtglf ktcasvmvgm lykkddarrd sgftlfymcf nfgafiapli cgflqkeygw
      181 hfgfgaggig mllaviifyl ktmpdlkefd ekigidstwd kpskknknav yiiivssivl
      241 lgaiflilgg fikldaqvin kniiltilac agiyflylfa ftslkieekr nliifivlfl
      301 aaalfwsvye qqytsfnffa ekltdktmln yefptiwfqs lgglfvilfa pfsvfiwtic
      361 aknnkeissi ikfalgllga alaflimala snhaislngd antlrenlen ssqiilvspw
      421 wlvssfllmv lgelclspvg lsimtkiapn liksqvmglw fvasalgnal agfiggkase
      481 eniaylpnlf yqcmwillga viillilkkp inkilkn
//
LOCUS       WP_010791392             248 aa            linear   BCT 01-JAN-2025
DEFINITION  AAA family ATPase, partial [Escherichia coli].
ACCESSION   WP_010791392
VERSION     WP_010791392.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 248)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..248
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          <111..246
                     /region_name="COG3950"
                     /note="Predicted ATP-binding protein involved in virulence
                     [General function prediction only]"
                     /db_xref="CDD:443150"
ORIGIN      
        1 nlnndlvryf svlsqqfsdh tiefqkqsfl alinnegana ifqfsssidi enerkqliev
       61 fevlgvenka yakklndhfa rlekvrkknn ltgiavddfs viynswraht lvadyevlqa
      121 kkakifkprd nfinllnsmf ggrksfsvsd knelivmtkd grpigleels sgekqlliil
      181 getllqhsks viyiadepel slhviwqeql tgaisklnpn aqiifathsp divginqdai
      241 idmekiil
//
LOCUS       WP_010791418             162 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein, partial [Escherichia coli].
ACCESSION   WP_010791418
VERSION     WP_010791418.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 162)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 162)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 162)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 162)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 162)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604589
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>162
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          15..>73
                     /region_name="COG3950"
                     /note="Predicted ATP-binding protein involved in virulence
                     [General function prediction only]"
                     /db_xref="CDD:443150"
     Region          16..>151
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mniitnvnii glwgnqdini avndktnfii gvngtgkttl inllaaalti dieklirief
       61 ssievklkev ggsrrpsirv tkdsnfgddt ltyeikkavk enpiisifds rfdrivfetk
      121 dgmrtykrkt hgydapnihe isstledlik vswlsvnrvd nl
//
LOCUS       WP_010791684             401 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [Pseudomonas].
ACCESSION   WP_010791684
VERSION     WP_010791684.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..401
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=43791
     Region          82..365
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 midrvkplma awvlvfasss fasetagklp rkpalgpeta gatlvipget drlaslyara
       61 rgeggkvvlw aggdapnqmd wlktafesrf pgvildvtvd lskfhdlrid qelaagtltp
      121 dvamlqttfd fdkwkardvl lrykpvgfar qkkgyadpdg ayvtaynnaf vptyasvrlp
      181 aeryptrfad ylkpafkgkl vltyphddda vlyvydkler rygsgflral aaqkpnflrg
      241 taapaasvgt dsigslgnlt gyatdsdtpa gyfiptdepf ivwnqraaif kaarhpatak
      301 lllsylgsae fqssyggwra radvgeapgl ppleslknvd vhdftrwmad rqrvaslrrh
      361 maqifgpvrg esplrdpalm sllgltandi valpepdlpi y
//
LOCUS       WP_010792102             240 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Pseudomonas aeruginosa].
ACCESSION   WP_010792102
VERSION     WP_010792102.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..240
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27148
     Region          16..231
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtqnppplei ahddgetlse hvfrkiqsai vsgeiapgsk isepelarty gisrgplrea
       61 ihrleglrll vrvphvgarv vslshaelie lyeiresqeg macrlaaerm sqaeidelrr
      121 vldtherdea fqagrgyyqq egdydfhyri iqgsgnatlt rmlcgelyql vrmyriqyst
      181 tpnrprqafa ehhrildaia drdgelaell mrrhisasrr nierqlepqp aklasasstv
//
LOCUS       WP_010792142             602 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF262 domain-containing protein [Pseudomonas aeruginosa].
ACCESSION   WP_010792142
VERSION     WP_010792142.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..602
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=68552
     Region          4..579
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 miqdvkalpv sfyfspdgtt sffipkyqre yvwggknwda lfndleesps ghflgsiicv
       61 ntqqdgmagg rlelidgqqr fttisllfca fydklnaipn qdrrllveld nlesrifvrt
      121 sgqwrlepse qaqnktdfqk vlsdlfpkqv kapkglsnfg nrriarayry fcerleglsq
      181 dsalallekl kaamlvkiev rshsdafmlf esinnrgipl saidiiknnl laeldkrpdy
      241 gidrafdewk dlidllpdpa vqerflrqly nmfkylkrve vkgctratrs nlitiydtll
      301 rkrpvwlfga lqakgktysa llnpavarae wgdaaaaalq dlqrlgaapa yafllwasqv
      361 aqsqkwnegd alsrlaallt kwffwrnltd mpptreldpm fmelvshllt qirsgeital
      421 dgfiqqssnw llgraapqdv cesrlkgdvy lenydatrfm lckleethqt renkrdlwvh
      481 dandrpvftv ehilpktenl gpgwvtmleg nqkgaaaair ercahqlgnl tlsgynsklg
      541 tmeflkkrdr kndqgdfigy rnglylnadl asrddwneaa itartdkmlk evmsilslrg
      601 eq
//
LOCUS       WP_010792180             288 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Pseudomonas aeruginosa].
ACCESSION   WP_010792180
VERSION     WP_010792180.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..288
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31400
     Region          1..267
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mqvvsiistk ggvgktttaa nlggfiadag lrvllldldv qptlssyftl dvrapggiye
       61 mlafnerrie qlvsrtaiag ldlvlsnddr gelntlllha pdgrlrlrhl lpvfrthydl
      121 llidtqgars vllemavlas dlalspvtpe ilaarelrrg tlqliediap yrhlgieppp
      181 lrllinrvhp vssnarlvqq alrqvfqeqa gvqvldtdvp aieaypraat rglpvhrvey
      241 rrpagrtapa aldtmrklag elfpawrerf alvtgradtg gashgert
//
LOCUS       WP_010792375             536 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010792375
VERSION     WP_010792375.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..536
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59070
     Region          1..524
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mnrellrven lsvaygdtqv vkgidfslra getlalvges gsgksqtaha llrllpgaar
       61 lggsvrldge ellalspqal lairgqrigm vfqepmtsln plqrigrqvg eglrlhrrlr
      121 gaalrgrvle llelagleqp rrlleayphq lsggqrqrvm lamalacepq lliadeptta
      181 ldvtvqkrll ellqslqrrl gmaillishd lnlvrrvadr vcvmrdgqiv eenacetlfr
      241 sprhpytrll ieaepgglae pvacretcle vralsldypa pggwlrrrag lravhevslr
      301 lrrgstlgiv gesgsgkssl gqallrllpa egqilfqger ldrlhgkrll plrrqfqavf
      361 qdpygslnpr lsveqivgeg lrihgigdag errarvleal revgldepcl eryphefsgg
      421 qrqriaiara lvlkpalill deptsaldrs vqcqvvellr rlqrrhglsy lfishdlavv
      481 ralahdilvl kdgrvveqgs aaalfsqprh pytrellgai palrleehlr vaglgi
//
LOCUS       WP_010792478             134 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator [Pseudomonas].
ACCESSION   WP_010792478
VERSION     WP_010792478.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..134
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14702
     Region          3..123
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mskalivdds rtdayvsqkc adqlfdevkv vgtlqellqv vpsfnpdvif mdlylgewhn
       61 glshirelrs ghgelsitpi ivlsskaaee dkrlaveaga agyivkpatl dkmmeslrry
      121 vpgfipkgwe svia
//
LOCUS       WP_010792488             381 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycerate kinase [Pseudomonas].
ACCESSION   WP_010792488
VERSION     WP_010792488.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..381
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38826
     Region          2..374
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mkvviapdsf keslsaelva eaialgvrds apdaeivcvp madggegtvd avlaatrger
       61 rfsrvrgplg aevqatwgwl sesrtaviem aaasgihlva paardvtras tfgtgqlvlq
      121 alnagaqrii mgfggsatnd ggtgmlralg akfldsagde leegglalna lrridlssld
      181 erlhkvridv acdvdnpltg pkgashvfgp qkgaspdqvl aldeslaaya divaeqlqed
      241 vrdfpgagaa ggigfaakaf lqaefrpgvq liadlsglrl avqgadlvit gegkldeqtl
      301 ygktpagvaa iaaaagvptv aiagtlgagy qrlrnigiva afsitsgpmn lesacadaam
      361 llrhraadvv qlwkvarvgg a
//
LOCUS       WP_010792531             122 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudomonas].
ACCESSION   WP_010792531
VERSION     WP_010792531.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..122
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13510
     Region          6..108
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mtaanrrytr yaipenslqk qqiktrgvlg flagwgdcrv rdisyagalv ltdkkigigd
       61 qvllrltekd ggvmdfegtv ancskdpith qfrvgvalse peadrrekgf llqlqdryrp
      121 va
//
LOCUS       WP_010792535             236 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010792535
VERSION     WP_010792535.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..236
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26132
     Region          42..220
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpnstakrqv tvsvlstpep swfkssslta gswaswlmma hqygrvvdhp agieidanhg
       61 dfyillngtm vvstvppdpn lkplfidtlr rgdiivpsrh tdlkftyvvr gsasllkvsk
      121 dkfnafmndm knsevvlmaa elnlltkhat aastvqmkdq dkiwrvvvnl ashpdvahrp
      181 ggvevkatre eirrlagver rsasrafhlf qekglvvfsg ykrfffahgk eglnad
//
LOCUS       WP_010792598             128 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator [Pseudomonas].
ACCESSION   WP_010792598
VERSION     WP_010792598.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..128
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=13848
     Region          9..118
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 msnirsvciv ddspgmrkmg agflqkadie vhlakdgyea lrvirearpd acfidiempn
       61 ldglklasil rastqfkhlp iamlssassp fdiqkgllag adlyltkpft gdkiakalid
      121 meaiideq
//
LOCUS       WP_010792915             140 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TraR/DksA family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010792915
VERSION     WP_010792915.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..140
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15738
     Region          19..136
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mstlltqqql lsapesdyms dqqlaffkel llnrklhlqg llaqraeafr ddsearlpda
       61 adtasaeeqr amemrmlkrd qaelldveaa lkrieegdyg ycaefgqpig lkrllvapta
      121 slcidaqeiq erraqrqrva
//
LOCUS       WP_010792997             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HEAT repeat domain-containing protein [Pseudomonas].
ACCESSION   WP_010792997
VERSION     WP_010792997.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..321
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33907
     Region          <9..315
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Region          73..101
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          122..161
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          167..192
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(184..185,188,191..192,215..216,219,222..223,
                     246..247,250,253..254,277..278,281,284..285,308..309,312,
                     315..316)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          198..225
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          228..255
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          259..285
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          289..317
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtcknatlpe ilelsprled adpgvrrlal ieladlelpe alplliaalr gdpdpgvrge
       61 aarlleawee davvdalcaa ladpvpavad aaaqslgelk epavgrrllp wlghadafvr
      121 asvlralrel rleesavpal aalgdpqaav rreavavlgw lrhqpalael arlasadvdp
      181 evrraatgal glsreatvlp alcaaladaq wqvreeaatt lgklgreeag epllkaladd
      241 ywqvrlraar algrlrhrpa realeallgh pignlrkeaa lalgeladpa saqalrvaeg
      301 dgdpevrkav rialaqlrvp a
//
LOCUS       WP_010793029             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_010793029
VERSION     WP_010793029.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..251
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26934
     Region          14..239
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mtvaerlcat pcgpaiefag idlslggsri ldgvrlrvea gsvhalvgpn gggksslvkt
       61 llgqmphrge lrlewpgapg cigyvpqale fdrglpltvd dfmaamcqrr paflglsrsr
      121 rpaidaaler vgmlakrgrr mgalsggerq rvllaqglvp ppqllvldep msaldeggiq
      181 vferllldwr qagvtvlwie hdleavgrla drvsglnrhl lfdgpaassl tperlltlfs
      241 tqprknveas r
//
LOCUS       WP_010793031             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thioesterase II family protein [Pseudomonas].
ACCESSION   WP_010793031
VERSION     WP_010793031.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..254
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27759
     Region          2..238
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mggtpvrlfc lpysgasamt ysrwrrklpa wlavrpvelp grgarmaepl qtdlaslaqq
       61 larelhdevr qgpyamlghs lgallacevl yalrelgcpt plgffacgta apsrraeydr
      121 gfaepksdae liadlrdlqg tpeevlgnre lmsltlpilr adfllcgsyr hqrrpqlacp
      181 irtlggredk aseeqllawa eetrsgfgle lfdgghffih qreaevlavv erqveawrag
      241 qgaaalaves aaic
//
LOCUS       WP_010793190             377 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aminotransferase class V-fold PLP-dependent enzyme
            [Pseudomonas].
ACCESSION   WP_010793190
VERSION     WP_010793190.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 377)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..377
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=42024
     Region          16..375
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mncyqdefdq tnglrylnha avapwprraa davsafaren vahgandype wlkiehrlre
       61 rlarllnara gsdlalvknt sealsfvafg ldwregdqvv igneefpsnr vvwealrprg
      121 vevvevglag ddpesallaa cgprtrllsi savqyasglr ldlerigagc rrrgvlfcid
      181 aiqqlgalpf dvqtydcafa madghkwmlg peglgvfych peqrerlalh eygwhmleha
      241 ldyerrdwrp arsarrfecg spnmlgamal easlglleev gmervgrdia ervqwlqdgl
      301 sgipgvrlhs prnpsrragi ltfsldgqdn rtlfetlrqe rvicaqrggg irfsphfyts
      361 stviddtlai lrqiagt
//
LOCUS       WP_010793233             629 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Pseudomonas].
ACCESSION   WP_010793233
VERSION     WP_010793233.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..629
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=69853
     Region          16..348
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          399..605
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 msssssklln gmvavssgrn irldvqglra vavlavlayh ansawlragf vgvdvffvis
       61 gfiitallve rgvkvdlvef yagrikrifp ayfvmlaivc ivstilflpd dyvffekslq
      121 ssvffssnhy fanfgsyfap raeelpllht wslaiemqfy lfypvlfmcl pcrwrlpvfi
      181 llaillfiws gycvfsgsqd aqyfallarv pefmsgavva lslrdrelpa rlailagllg
      241 aallvcsfii idkqhfpgfw sllpclgaal liaarrgpas lllasrpmvw iggisyslyl
      301 whwpilafir yytgqyelsf vallafltgs fllawfsyry ietparkavg lrqqalkwml
      361 aasvvaivvt ggaqfnvlvv apapiqltry aapesichgv qvgeckrgsv navprvlvig
      421 dshaaqlnyf fdvvgnesgv ayrvltgssc vpipafdler lprwarkpcq aqidavaqsm
      481 lnfdkiivag mwqyqmqspa faqamraflv dtsyagkqvv llgqipmfes nvqrvrrfre
      541 lglsaplvss swqganqllr alaegipnvr fmdfstsaff adapyqdgel iyqdshhlne
      601 vgarrygyfa srqlqrlfeq pqssvslkp
//
LOCUS       WP_010793235             386 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010793235
VERSION     WP_010793235.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..386
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42140
     Region          1..363
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matlelrnlh ksygsgladt lrdirlkids geflilvgps gcgkstlmnc iaglesitgg
       61 ailvdgqdis gmspkdrdia mvfqsyalyp tmsvreniaf glkirkmpqa aideevarva
      121 rllqiehlle rkpsqlsggq qqrvamgral arrpkvylfd eplsnldakl rvemrtelkl
      181 mhqrlktttv yvthdqieam tlgdkvavmk dgviqqfgtp qqiyndpanl fvasfigspp
      241 mnfiplrlqr rdgrwtglld sgqdrielpl slepsleegr elilgvrpeq ialgdgsaah
      301 dlrtevevle ptgpdtlvfv tvnqvkvccr lapdvapaag sgmslrfdpa rvllfdaqsg
      361 ervavrtagv aaekvtalng nrqkns
//
LOCUS       WP_010793263             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010793263
VERSION     WP_010793263.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32799
     Region          4..219
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mslveidgat lrygaltals gldlrlepge vlgllghnga gktttiklvl gllapsegrv
       61 rvlghdarsl garrqlgylp envtfypqls gaetlrhfar lkgvapaeaa rlleqvglgh
      121 aarrrlktys kgmrqrlgla qallgeprll lldeptvgld platvelyql ldrlrgqgtg
      181 ivlcshvlpg vethidraai laggrlqvag slaelrrkaa lptrvrlasp hnpqwlerwr
      241 raglaarrld gqrievlldd aerdgvleal laarefdlei lppsledlyr hhmspapaga
      301 tpcp
//
LOCUS       WP_010793341             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Pseudomonas].
ACCESSION   WP_010793341
VERSION     WP_010793341.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..259
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29201
     Region          3..258
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mrlvdthnhl dfpdfdadra allqrsralg verqvvlgvy renwqrvwdl aqaedglyaa
       61 lglhpvylar hrpqhlddlr qwlqrlrget klcavgeigl dyylehldrd aqqalfeaql
      121 rlaaefrlpa lihvrrahat tiatlkrirl errgiihafa gsreeareyl klgfrlglgg
      181 aptwpqanrl rkvaaelpae aivletdapd mapsmhpgqr nspehlpdic ralaelrgvd
      241 aeelaasssr naaelfgwd
//
LOCUS       WP_010793272             328 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Pseudomonas].
ACCESSION   WP_010793272
VERSION     WP_010793272.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..328
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35358
     Region          17..54
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          70..317
                     /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"
ORIGIN      
        1 mnspqeqqqi rqqaaewair ldggdldrsr realdgwlaa dprhpaalal aqrtwkqlgs
       61 laeprtmvqt pvasaprrag grrkgwrgwa aaaavllalg sawnerdagv swladhatgk
      121 gevrilrlvd gseveldaqs aidvaydsre rrvrllegsa ifraapragr etrpfvvesa
      181 ggstralgtr flvsrnddgs vqvgvlehrv avalahprtg tvgrrelgeg eslrysaegg
      241 veaplggrld dltswrrgll vfdeqplgev varlnryrpg hllvapgala qrrvsgvfrl
      301 adleaslqsi sdelgvrslg lagvtlly
//
LOCUS       WP_010793353             440 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Pseudomonas].
ACCESSION   WP_010793353
VERSION     WP_010793353.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..440
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47220
     Region          1..422
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 marlkrtlsl gsvvlfgiay mtpiivlgtf gilaettqgh vpaayiaasl amfftalsyg
       61 rmaaafpvag saytyvrkai dsrlgfiagw avlldylflp maiwligaay lhsafpavpn
      121 avwvlafigv tttinivglr laknvngllm lvqflvlgaf valcvhyvlg dpgkplwslq
      181 pllggdlqvp lvmsgaaiac ysflgfdavs tlteetrdpr rniprailli tllgglifiv
      241 tsyfvqlahp sfafdsadsa ayeiarnigg dlfvtfflvg livgqftsgl saqasasrll
      301 famgrdgvlp rpffgrlgkr fetpansiil cgvvallalq mdvttstsfi nfgaflafsl
      361 vnlsvvfhyy lgaerrgpre tllflvfpgi glvadlwlma sldhlaiilg lcwlalgavy
      421 laaithgfre pppemrfeeg
//
LOCUS       WP_010793355             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010793355
VERSION     WP_010793355.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..256
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27575
     Region          1..256
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrrpyllwsa talvylflyv plvivvlysf ndsrlnaewv gftldwyrkl fgnrdmlqaa
       61 anslvialvs asvatllgtl agvalhrfkl rvlpllvltp iaipellmgv slviffigln
      121 mslgmlsvtl ahitfsvgfv alvvqarmsg mdeslteaar dlgatpwqsf rlvtlplimp
      181 givagalmaf tlsiddfvit ffaagggfat lptqiytmik iavtpevnav stllmlltlv
      241 liviasklsp saikgh
//
LOCUS       WP_010793412             215 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010793412
VERSION     WP_010793412.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23169
     Region          11..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvyrvterrl qrdsalrehi lqlglrrvae ggfaaltmqa laddagiatg slyrhfrgkg
       61 elaaeifrra sqrevdalav vlrgpgapaw rlaeglrrfa arawssqrla faliaepvdp
      121 evdeqrlryr eayaalfvel leegrrsgaf qlslvplaaa clvgaiaeal vgplsppara
      181 ardsgqpeps lepvstalvn fclravgapv ceeps
//
LOCUS       WP_010793395             191 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Pseudomonas].
ACCESSION   WP_010793395
VERSION     WP_010793395.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..191
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21287
     Region          2..121
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(7,9,64..65,68)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            9
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(63,107..108,110..111,115)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(69,74..75,103,106..107,110..111,114,117)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(92..94,103..104,107..108,111,115,118)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(92,108,111,115,118)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Region          138..180
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(139..141,174..175,177..179)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mligyvrist ddqlldlqrd amakagcerv fedtasgaka driglaalla nlrrgdtvvv
       61 wrldrlgrsi kdliylveql edagvglksl qenidttstg grlvfhlfaa laefernlis
      121 ectharlsaa rargrlggrk krldpakrkv alklyherqy tvveicrmmg igrstlynyi
      181 teaernahqq a
//
LOCUS       WP_010793567             270 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Pseudomonas].
ACCESSION   WP_010793567
VERSION     WP_010793567.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..270
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28680
     Region          191..269
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 matpqpvdar tqpwretpgg dlvalgrpvr qalhlvrhnp aqgrvlsrre tillvlfalt
       61 lhgavihwls qqrtpalpev ppqvppmtie ftasappvve ppppeplppv veeppppvvd
      121 enavkppppk pvpkpkpkpk pqprpkpapk avepappapp qpaappappa paaapapltp
      181 psanagylhn papeypalam rrgwegtvll rvhvlasgsp seiqvqkssg realdqaavk
      241 avkrwsfvpa krgdkaedgw vsvpidfkln
//
LOCUS       WP_010793644             387 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010793644
VERSION     WP_010793644.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..387
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40351
     Region          9..368
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(16..17,20..21,24,56,106..107,109..111,114,134,
                     137..138,141,209,212..213,216..218,221,245,249,298..299,
                     303,307,323,326..327,330..331,334)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mrwgsyfavc savisiglal gltmplvslr leswgygsfa igvmastpav gvllgamiag
       61 rlaarvgtpr lmqlclltga asvgllallq sypvwlllrl ligvqltvvf ilgeswinql
      121 avekwrgrlv alygtgyals qlsgpvlltf igtaddrgfw fgvclliags llllgrggap
      181 rvdphsasgr glwafcrglp aiawavvlfa afeamiltll pvyglrqgfp qavalamvst
      241 vvvgdallql pigwladrvs rsglfggcgl vlllsslaip lllqtsliwp llvlfgasag
      301 glftlalili geryrddalv ranahvaqlw gigcllgpla tgaasqwisg halplmmalg
      361 aagfvvlvrl rgaipaddea tglease
//
LOCUS       WP_010793656             662 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Pseudomonas].
ACCESSION   WP_010793656
VERSION     WP_010793656.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..662
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=73473
     Region          1..353
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          397..648
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 msslpyrrdi dglralailp vvfyhlglgg ftggyvgvdv flvisgylit siirrdrqag
       61 rfsfvdfwar rarrilpalf vmmavslaag wflmeprdye qlgravryqt mfasnilfwk
      121 qdgyfdaase fkpllhtwsl sveeqfyilf plllaaisgr llrwrlaill avlalslaas
      181 vwavsqrpgs affllpmraw ellagaalal lpgasrghsq wslqlaatlg iaaillpvff
      241 ydsdtpfpgl aalpavlgta lliwangagd twarrllgwq plvwfglisy slylwhwply
      301 vfvqyhalet lglparlgll aasiglaals lycveapfre rklfagrrqm lgaalcslll
      361 lgvigqlvrh ydgvpsrlse ealryakask wrdgqtdcmf dkkalsqesi crfpaelaae
      421 rpllvswgds hsaalspllr elatsrrlpi wqaslagcpp llgmlekdtc lrfnqqmlef
      481 veqqrpggvi lagrwdmyiy gdsqdgtrni lrepddtpds siaeallrqr lsgmierlna
      541 advhvwlvkd vpllpfkapa rlvrlslsge dvgrarfpfa ehaarvayvn alfdalaegn
      601 prvsvldpss vlcdgldcfa erdgwslymd nnhlstqgah elgplfepml qslddsrias
      661 qq
//
LOCUS       WP_010793727             324 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Pseudomonas].
ACCESSION   WP_010793727
VERSION     WP_010793727.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..324
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35590
     Region          19..200
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(22,24,108)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(55,107..108)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            106..108
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mmiepslask leapcllsvv vpvfneeavl pafhqrlgav lgdlgddcev lyvddgstdr
       61 savilaqlqa adrrvgvarf trnfgkeqam saglklsrga avividadlq dppelipqml
      121 dawiggaemv nmrrrsrage swlkrasasa fyrlinrlse vpiprdvgdf rlldrrvvda
      181 lcelpegnrf mkglfawvgf rqvdiaysra arvaghskwr ywrlwnfale gitgfstapl
      241 kvagylglls llaalatlla gifgqqeihe hwpviaalfl igglqllaig vcseylgrmt
      301 mearrrplyl idrylpaqvg ganp
//
LOCUS       WP_010793760            1050 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type I restriction endonuclease subunit R
            [Pseudomonas].
ACCESSION   WP_010793760
VERSION     WP_010793760.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1050)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1050)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1050)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1050)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..1050
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=116987
     Region          1..1041
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 msvneqqled aaigwfgelg wqyvngpdia pdgdspartd yrqtvlrerl laalsrinph
       61 vpaaaleqaa helltvsepl liarnrrvhr lllsgipvef segeekrtdl vnlihfanpr
      121 nndfllvsqf tvagtkqprr pdlvafvngl plavielknp aneqtdiwda fnqiqtykee
      181 igdlfntnva vvvsdgftar lgsltanqer mqpwraiane ddrpllefel etlvrgffep
      241 alfldyvrhf vlfeqdadei ikkiagyhqf havreavkat viaasnpnkg rlevqeprat
      301 ygkevqpgsr kagvvwhtqg sgksitmacy agkllqqpem knptlvvvtd rndldgqlyg
      361 tfcaaedllr qtpvqagsre elremlasre aggiifttvq kfalledeeq hpllsgrsni
      421 vvisdeahrs qygmkgrldt ktgkyvfgya khmrdalana tfigftgtpi aledkdtrav
      481 fgdyvsiydi qdavddgatv piyyesrlak ldvnqaeida lnaqvdevie deeditarek
      541 tksdwaaltk lvgarprleq vaadlvqhfe trtatlegka mivcmsrdic aelynaival
      601 rpdwhdadpe kgaikvvmtg saadkpllqp hlysqqvkkr lekrfkdpad plklvivrdm
      661 wltgfdapcc htmyvdkpmk ghnlmqaiar vnrvfrnkpg glvvdyigia nelkaalkty
      721 teskgkgdpa hnaaealavl lekldivrgl mhgfdysgfe tdamkllvpv anhilglkdg
      781 kqrfldamla vskafslcst ldeaaalrte iaffaavkaa ivkfttvdrk rsdadknsal
      841 kqildnaiva dgvadifala gldkpnigll seefledvrq mksrnlavel lekllrdeik
      901 ararnnvvqe kkygdrllet lrkyhnrave taqvieeliq makdfqaale reaalglnpd
      961 eiafydalan nesavrelgd dtlkkiavei teklrnsttv dwqvresvra klrilvrrtl
     1021 kkwkyppvge daaielvlkq aeslsnawsk
//
LOCUS       WP_010793780             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010793780
VERSION     WP_010793780.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..397
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41396
     Region          9..397
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 msaspsprql lhealaslrg lgrrsllall givmgcssvi amlnigsnat deamsifkdm
       61 gtdtlvvqfp fapqapmpmp asldtepllr dvaglehlaa lglysapvtf hgrtsnasiv
      121 gasaglaaaa rlrlregrfl srfddhdtyv vvgatiaeal gapgdplrlg eqltvndylf
      181 rvvgilqpqa saallpfaan dslfvpapgm prlqpaaevs hvvarvspga dvysvgaalg
      241 aaltarlpgh eaqvqvsqqv ldglkrqtrt ftyllaglgi isllgggvgv mnvmlmsvae
      301 rrreigvrma lgarqrdirn lflieavtlt aagalsgavl gvaaaylyar fsgwtfslay
      361 aalplgmgst llvglffgly pavsaarlqp vealrde
//
LOCUS       WP_010793790             435 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Pseudomonas].
ACCESSION   WP_010793790
VERSION     WP_010793790.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..435
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47342
     Region          3..418
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mshrivivgg gagglelatr lgrtlgkrgk aqvtlvdanl thiwkpllhe vaagslnsse
       61 delnyvaqak wnhfefqlgr mqgldrackr vrlaalvden gvelvperdi aydtlviavg
      121 sttndfgteg aaehcifldt raqaerfhrq llgqylraht ghdannnavs iaiigagatg
      181 velaaelhha aqmlaaygld rirpedlhis lveagprvlp alperisqpv hqtlsklgvr
      241 vmtgsavskv dadglwtgdg efvpatlkvw aagirapafl keldglesnr inqlvvrptl
      301 qttrdddifa fgdcaacpqp aqpgeqprnv ppraqaahqq asllvkslra rlegkplgey
      361 hyrdygslis lsrfsavgnl mgnlmgsvml egwlarmfyv slyrmhqmal ygplrtamlm
      421 lsgrlrstep rlklh
//
LOCUS       WP_010793770             790 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fimbria/pilus outer membrane usher protein
            [Pseudomonas].
ACCESSION   WP_010793770
VERSION     WP_010793770.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 790)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..790
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=85971
     Region          49..782
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mprpcqrrsr rhrslligla llspvhaady laglpppqpa psgggnalyy lelvingrds
       61 gqvvpvnaad ghylldaaal reagvrlpgn pagqvavdal pevradydsa sqqlhlqvpp
      121 dwlpeqrfdd pglvarapar sslgalfnyd lyysdpadga tpwlsalleq rlfdgfgvis
      181 ntgvytryfg dadnldsryl rydtywlynd ernmhsyqlg dyvngalnwt tpvrmggfrf
      241 arnfgvrpdl vtypllrfdg qaavpstvdl fingykassa dlqpgpfais nvpyingage
      301 atvvttdaqg rqvvtslpfy vsntllargl sdfdlsvgrl rddyglrnfs yadnaasgiy
      361 rygvsdrltl sthaeaasdl rllgiggdia vatfgtlsla asgsdgqgds gqqyllgysy
      421 ysrrlglslq hiersagygd lgtldgeyql srrtdqatas ltfdeqgtig tgyfdirard
      481 gsrtrlanls ysrpigsrss fylalnkdld gdgysalmql vipfdingll nigvtrdsdr
      541 ryserviwsr stpsqgglgw nlgygggasr yqqadltwrm qnvqlqggly getgnytrwa
      601 dlsgslvwmd navfasnrin dafvlvstkg ypqvpiryen qlmgstddng hllvpwvaay
      661 ypakfqiepl dlpanvsape veqrvavrqg sgllldfpir avvaasinlv dergeplplg
      721 sqaeetgsgq rasvgwdgqv yfeglqsdnq lrvvrpdgra cqarfrldtr kptvsqvgpl
      781 tcsapigdtp
//
LOCUS       WP_010793851             502 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [Pseudomonas].
ACCESSION   WP_010793851
VERSION     WP_010793851.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..502
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54385
     Region          5..481
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(62,64,68,71,75,108,111..112,121..128,133,136,139,
                     232,236,239,242,244,417,419..420,422..423,426,429..430,
                     432,434..437,446,450,452,466,473..478,480..481)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(148..151,159,174,177,207,224..227,230,248..250,282,
                     382,384,410)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(151,248,279,282)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 makaipqlid gewrgsrsre lievtdpatq dvlalapkat adeieqaias aqrafetwre
       61 vpaperarlm lryqhllkeh hdelgellar etgknladak gdvwrgievv ehaanvaslm
      121 mgetvenvar eidtaswiqp lgvcagitpf nfpamiplwm fplaiacgnt fvlkpseqdp
      181 ltpnrlaelf leagapkgvl qvihggreqv dallthpdir aisfvgsvav gqhvyrtgta
      241 hlkrvqafag aknhmvilpd ankaqvlgnl vgascgaagq rcmaisaavf vgaarewipe
      301 laermaalrp ghwqdpdaay gplispqarq rvlrliaegk aegaeclldg sqcqvegypn
      361 gnwlgptlfr avtpkmglyr eeifgpvlac levesleeai alvnanpygn gtslftrsgg
      421 aarryqhavq vgqvginvpi pvplpffsft gwkgsfygdl haygkqavrf ytetktvtsr
      481 wlddepttde ssagpnmtih lk
//
LOCUS       WP_010793914             303 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010793914
VERSION     WP_010793914.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33347
     Region          9..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(107,111,150,164,167,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(108..109,113..114,116..117,120,124,126..132,194,
                     224..228,235..236,239)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mpaftrsela dlnvfmtivr rrsfrhsaqe lgvstsalsh smrnlearlg vkllnrtsrs
       61 vvptdagsal aakledgfqv igealgelda yrtspvgrlr lnvprdasrl llgpvlrrft
      121 eaypdlqlel svedrmvdiv adgydagiry ggtvpqdmva vpltgelrwv vaaspdylar
      181 hgvpqrpddl lrhacirmrl gdnsfykwel gdgermvevd vpgpfsvnes ntavaaaldg
      241 vglayclevg iaeelrsgrl qlvlpdwtsm gapfclyyps rrqpqpglrq lmeiirgdwl
      301 gra
//
LOCUS       WP_010793926             177 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Pseudomonas].
ACCESSION   WP_010793926
VERSION     WP_010793926.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..177
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=18931
     Region          <41..166
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mhalarfsil afaalltaca skapppapak qvvfrparnf spaaddvlfr alglvgtpyr
       61 wggntpdsgf dcsglinfvy rdmtgiklpr stremismra psvpvqalqt gdlvffatsg
      121 grtvshagiy vgegrfvhap rtggtvrlds lqnsywqray ldakrvlvap splarvp
//
LOCUS       WP_010793990             412 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Pseudomonas].
ACCESSION   WP_010793990
VERSION     WP_010793990.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..412
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44066
     Region          8..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msiteqvdva ivgsgpagla aaielrrqgv arvcvlerdg eaggiprhca hppfglrehg
       61 rlltgpayal rnveqaerag vdirlrhsvv alaaagllql atpegprslr atrvllatga
      121 retprsarll ggdrplgvin tgalqaylyl qglkpferpl ivgtelvsls avmscrragi
      181 rpvamlerna ratarwplsl fprlcgvpmh fsselleieg rgrveaarvr lgdgrveria
      241 cdgillsgrf vpesslvrls hleldpasgg pridqfgrcs dpayfaagnl lrpietagws
      301 fregrriagl laadlraelp saapgiaidc sgplklcvpq rlladptpgl ahlqlrvsea
      361 asgrlrilad grpvwerals clperrllvp laalrlppdt rrlevaflts gh
//
LOCUS       WP_010793993             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ion transporter [Pseudomonas].
ACCESSION   WP_010793993
VERSION     WP_010793993.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..283
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31704
     Region          42..240
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 msapdswrer lyivifqtdt rdgrrfdsal llvilasllv vmidsideih qdygdllayi
       61 ewgftgiflv eyllrlycsp kplryafsfy glvdllailp gflallypda qyllivrvir
      121 mlrifrvlkl rqylsqanfl ltalrgskqk iivffltvmt lvtvfgalmy vvegpehgft
      181 siprgiywai vtlttvgfgd itpktplgqa iaslvmltgy siiavptgif taelatamrq
      241 dpanllqrdc lvcrkathev qaafccrcgn plfpreegsh gks
//
LOCUS       WP_010794008             288 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010794008
VERSION     WP_010794008.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..288
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32168
     Region          40..286
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mrgnderrsp aegasteaev safeavlidp mqekdeelkd rqfvtalarg lellrcftpr
       61 esllgnqela kktglpkptv srlthtltrl gylrhlphsg kyqlevgvms fgyamlsnls
      121 iralarplme emagyakaav amaardrlsm vyldvvhgea nltmrrqvgs hlslhrsaig
      181 raclaamped erefilghir krhpedwpev rkglerafrd cadygfclsl gewqrdvnav
      241 gvalhheshg llafncggps fhlkrekled digprllhmv hnieaatr
//
LOCUS       WP_010794083             170 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [Pseudomonas].
ACCESSION   WP_010794083
VERSION     WP_010794083.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..170
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=18157
     Region          10..156
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mtnpepadlp isllingqrr elrvppwltl ldllrerldl vgskkgcdhg qcgactvlcn
       61 grrinacltl avmcdgdalt tieglaegdr lhplqqafir hdafqcgyct pgqicsalgl
      121 asegrarsra eiregmsgnl crcgaygnil davedalpll drdgqggqra
//
LOCUS       WP_010794207             276 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Pseudomonas].
ACCESSION   WP_010794207
VERSION     WP_010794207.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..276
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30116
     Region          18..260
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 maatvikkkr kepadvhvft nqkggvgktt idfhwlvyla eqgykvlgid ldgqgnfssr
       61 lapqgreggl rsahlfqdtl pdlmpiktef gadliyslng dtdlysveqm glqvirtfas
      121 hiqrlgeeyd yividtpptn gvkmtaasvi adhiyvpvel aafavdgvis liesfdkltp
      181 ilgtrieptg iicnklntrv kahqeslael revvgkkilr tslsirgaid tavrqckpvw
      241 alrtsgaerd aakemitlme elahmsgvkv kkagak
//
LOCUS       WP_010794345             331 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParB/RepB/Spo0J family partition protein
            [Pseudomonas].
ACCESSION   WP_010794345
VERSION     WP_010794345.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..331
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34962
     Region          69..>215
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mttktiaanl itesaqaala gcnslrsihd takklitgkq lgldfdpkrq nafemptall
       61 vcnveeairs efdqdairgf adsykagepv eplgvvaeng klrvvtgftr haglmlaiae
      121 gadikrvwvs qveggravei vrqcvsnqqv pvspldlaea yreliddhkf tvagvaaavh
      181 rkvshvrkml alvnvapevk emvekgqasv stalaadkqc kangedtvvh mqeqlakaqr
      241 ngsakitaks vgapsalygr kdldvaapvl vqladqleka lpfmatpesv kveltlsgad
      301 lnlqdlakal aniraavksa qsgtepaanv g
//
LOCUS       WP_010793357             335 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolB family protein [Pseudomonas].
ACCESSION   WP_010793357
VERSION     WP_010793357.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..335
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=35754
     Region          53..201
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mniaplkvsl lslalllspv aslpahaact anlalqpass lpalggrlvy hsymeygdgs
       61 snlylhdfks kstrqlnqpg wniedpmnah fspdgryltf mgrqngawhv fawaiggtqa
      121 psnltaaigg rnedpkfsfd grqvvlkheg dirlatlvfn gdgsvgvsaw kavtgdgwst
      181 eesmpfltps gkyvvyatga gdslrvvhrn lengqvcala tpaaggrdyy pvvrdytayf
      241 lsrtqpagnd qlamvvpnsp pgtpailpln hcqgdnsdaa pvnedylifs stsfdptysl
      301 llgdiaaarv wrldpaqinl pdgrqklgas ytaar
//
LOCUS       WP_010794384             501 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Pseudomonas sp. P179].
ACCESSION   WP_010794384
VERSION     WP_010794384.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. P179
  ORGANISM  Pseudomonas sp. P179
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Pseudomonas sp. P179"
                     /db_xref="taxon:1125698"
     Protein         1..501
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=56304
     Region          159..>367
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mqaagyallh erlalsavpl rlpaivqpvt rlerigqtla vppaiapakd dllgnvlfal
       61 kheginlsil aqtlplipve eferalqaap ngiyirkasf lreaftgeql aqhapvrgpf
      121 vplfdperyi trpgnrnskw rvefnglgdl tycatvertp aitellehdi lgrakafmes
      181 lppgmmdrai nwaylsetkd sfaiereapt edksrrfiql lrqaherqpl teeylvglqn
      241 atvanpydla aafrheqnhl agalqgaagv tyvppppelc relmeslmgf aneapmqidp
      301 lvaagiisfg fvflhpfmdg ngrlsrflih qalcragale nglllpvsva mkreermyle
      361 alqtfsrpvr dfwdvqwidy ghlafqfrgh pavyrfwdat pcvtftmvma rhalevelre
      421 etaflecfda vyravderfd vrgselaqlv mmcltnqgiv sknrrkqfqy tvpeevfefi
      481 eqvaqqvlgd qrnegnvgeg e
//
LOCUS       WP_010794448             134 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator [Pseudomonas].
ACCESSION   WP_010794448
VERSION     WP_010794448.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..134
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14741
     Region          3..123
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mskalivdds rtdayvsrkc adqlfdevkv vgtlqellqv vpsfnpdvif mdlylgewhn
       61 glshirelrs ghgelsitpi ivlsskaaee dkrlaveaga agyivkpatl dnmreslrry
      121 vpgfipkgwe svia
//
LOCUS       WP_010794499             381 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerate kinase [Pseudomonas sp. P179].
ACCESSION   WP_010794499
VERSION     WP_010794499.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. P179
  ORGANISM  Pseudomonas sp. P179
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Pseudomonas sp. P179"
                     /db_xref="taxon:1125698"
     Protein         1..381
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38766
     Region          2..374
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mkvviapdsf keslsaelva eaialgvrds apdaeivcvp madggegtvd avlaatgger
       61 rfsrvrgplg aevqaawgwl sesrtaviem aaasgihlva paardvtras tfgtgqlvlq
      121 alnagaqrii mgfggsatnd ggtgmlralr akfldsagde leegglalna lrridlssld
      181 erlhkvridv acdvdnpltg pkgashvfgp qkgaspdqvl aldealaaya divaeqlqed
      241 vrdfpgagaa ggigfaakaf lqaefrpgvq liadlsglsl avqgadlvit gegkldeqtl
      301 ygktpagvaa iaaaagvptv aiagtlgagy qrlrnigiva afsitpgpmt lesacadaam
      361 llrhraadvv qlwkvarvgv s
//
LOCUS       WP_010794696             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nuclear transport factor 2 family protein
            [Pseudomonas].
ACCESSION   WP_010794696
VERSION     WP_010794696.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..143
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=15740
     Region          29..135
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 mrniklivgf lclfsgyama atssdetava eavdkltqam whkdiaslna ltaenltygh
       61 ssgniqdkka fiadietgks afkelkmlnq kitmsgdval vrnhfsaqai nsgkltptei
      121 enfqiwqkqn gkwlligrqa frf
//
LOCUS       WP_010794704             298 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: bestrophin family protein [Pseudomonas].
ACCESSION   WP_010794704
VERSION     WP_010794704.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..298
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33531
     Region          2..290
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mptlirrkyr flhktlsytg wslfwlliwd ivvtvdfmlf vddrmslpsm pltllgsala
       61 mlvsirntsa ynrwweartl wggmvnssrn farqvlilvd dpgdalnpik evlfrrhvay
      121 vnalaahlkk apiperlael lpaeevarsg dtnnfpndil sgsaaliaqe ykagrldsir
      181 larlestmvd isnwqggmer iantplpypy vyfprlfisl fclivpvglv eslgwftpla
      241 stvvgfmlla lekigtdlqs pfsesqhqiq mtdlcaniek nlssmfrese nasvrste
//
LOCUS       WP_010794842             156 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Pseudomonas].
ACCESSION   WP_010794842
VERSION     WP_010794842.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 156)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..156
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17730
     Region          11..142
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04688"
                     /db_xref="CDD:467570"
ORIGIN      
        1 misvdidgyr fqvraaavve hdnhillhrg vndsfwalpg grvepgenaq atlvremmee
       61 ldepivcgel lylvenffdy lnqpnheigl yfraqlrshs tlldksrthn gteagtslef
      121 rwfpraslhd vdlrpaflre slslstlnfl hvvqrg
//
LOCUS       WP_010794854             103 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SCP2 sterol-binding domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010794854
VERSION     WP_010794854.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Burgardt,N.I., Gianotti,A.R., Ferreyra,R.G. and Ermacora,M.R.
  TITLE     A structural appraisal of sterol carrier protein 2
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (5), 565-577 (2017)
   PUBMED   28284963
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Dyer,D.H., Wessely,V., Forest,K.T. and Lan,Q.
  TITLE     Three-dimensional structure/function analysis of SCP-2-like2
            reveals differences among SCP-2 family members
  JOURNAL   J Lipid Res 49 (3), 644-653 (2008)
   PUBMED   18084051
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Bun-ya,M., Muro,Y., Niki,T., Kondo,J. and Kamiryo,T.
  TITLE     New aspects of sterol carrier protein 2 (nonspecific lipid-transfer
            protein) in fusion proteins and in peroxisomes
  JOURNAL   Cell Biochem Biophys 32 Spring, 107-116 (2000)
   PUBMED   11330036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007129
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..103
                     /product="SCP2 sterol-binding domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11050
     Region          4..102
                     /region_name="SCP2"
                     /note="Putative sterol carrier protein, contains SCP2
                     domain [Lipid transport and metabolism]; COG3255"
                     /db_xref="CDD:442486"
ORIGIN      
        1 mssadiienl kskfnpdaaa gldltyqfdi edgenyhlvv kdqtcdvkag nadepdctli
       61 mntdtlkgiv sgetdgmqaf magkvraegn mmlamklsel fpn
//
LOCUS       WP_010794868             549 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010794868
VERSION     WP_010794868.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 549)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..549
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60606
     Region          16..542
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mhstpennva ssaqqttrll evrdlcvefr ngqevvrave qvsfdiypge tlalvgesgs
       61 gksvtahsll rllpastahy pagrilyggq dllklperkl ygirgnriam ifqepmtsln
      121 plhtldkqlg evlalhkgmk gpparkrmie lldlvgipdp asrlsayphe lsggqrqrvm
      181 iamalacepd lliadeptta ldvtvqqkvl hllkdlqkrl gmsillishd lnlvrqiadr
      241 icvmqrgriv eqetcktlfq hpqhpytqll laaepsgdpi pshpapvela tehlsvwfpi
      301 rkglfrrtvd hvkavddvsl avprgqtlgi vgesgsgktt lglailrlle srgrirfgnq
      361 aldqlssaqi rplrrqmqvv fqdpygslsp rmsvsdivge glrihrigtp eeqetaiiga
      421 lrevgldpev rhryphefsg gqrqriaiar alivkpslil ldeptsaldr tvqrqvvdll
      481 rdlqakhnlt ylfishdlav vralshqllv mkagqvveqg saedvfqrpq hpytrqllda
      541 alassapay
//
LOCUS       WP_010794975             213 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Pseudomonas].
ACCESSION   WP_010794975
VERSION     WP_010794975.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..213
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22029
     Region          103..210
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(110..111,145..146,149,153..154,157,200,204)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mtiirtalpl ilvgsvltgc agvkktdwpa caaiggatga avgaiesssy agwgglvaga
       61 tagaycyvhg qgeeqvaave pvtpapaptp apeplprqet ivvrdlhfaf dsaeispadr
      121 aqldtvasrl rneasttrlt inghtdskgt ekynqrlser raaavrnylv qsgvpaasiv
      181 svqglgesqp vatnetaegr atnrrveilv erq
//
LOCUS       WP_010795008             246 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010795008
VERSION     WP_010795008.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..246
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27136
     Region          10..245
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mpqtsfdtfl enlglgafal hgygpllleg twmtmklavl slvvsvilgl lgataklspi
       61 kafrlpaaly ttlirgvpdl vlmllifysl qswlgeftdy mdwdyieidp lsagvltlgf
      121 iygayftetf rgailavprg qieaataygm trtqtffrit fpqmmrfalp gignnwqvll
      181 katalvsiig lsdivtatqe agkttykmfy flilggviyl litaltnqvl nwlerrysag
      241 vreavr
//
LOCUS       WP_010795085             380 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010795085
VERSION     WP_010795085.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..380
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39025
     Region          11..377
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(21..22,25..26,29,61,111..112,114..116,119,138,
                     141..142,212,215..216,219..221,224,252,256,305..306,310,
                     314,330,333..334,337..338,341)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 maektlagsa rwacayffai nglvhgslma ripalkmqag ldegtlgqal lclglgalta
       61 fpltgilqrw lgsrrivigg gllllfafpl vglahqwlsf alamyligla sgamdvavnt
      121 qsveveralr rptlsllhgm yslgglvgal gaaalvalsp vwhflllavi alifllpggk
      181 rllpdehmpa rthkgsglrl ppmavvglgl malcsfvseg aiadwsalll hdvksasegl
      241 salgyaafsa tmvfgrlfgd rlrvrfqdhs lvralgglat lgmvvallap daiisiigfa
      301 laglglsiiv pilfsaagnr pgidpgvgva avatlgyggl lmgppligll aqavglklal
      361 lsivalcaal clragivrrg
//
LOCUS       WP_010795089             344 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010795089
VERSION     WP_010795089.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..344
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37169
     Region          1..343
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msiltlshla cgyggstivs dlslslesge igcllgpsgc gktttlraia gfepvmqgei
       61 rladqvisra gftlaperre igmvfqdyal fphlnvgdni afgirkhper erivgelmal
      121 vkleqlakry phelsggqqq rvalaralap sprlllmdep fsnldvelrr slssevrdil
      181 kargtsailv thdqeeafav sdkvgvfqhg hleqwdtpgh lyqtpatpfv atfvgqgffi
      241 pgraadsesi qtelgvvkar nkafkegdel rvllrpddil yspastltaq vvsqvflgas
      301 tryqlalasg arleasfpgf iehsigerig ialkktaltt fsat
//
LOCUS       WP_010795113             195 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Pseudomonas].
ACCESSION   WP_010795113
VERSION     WP_010795113.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..195
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21123
     Region          1..193
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdvlfsmagf alassispgp vnlvalssga cygfrkslrh vtgattgfta lllliglgly
       61 evlaripeli kliqwsgvaf lfymayqlam ddgvldikee gsgpsmmrga lmqwlnpkaw
      121 laslagmglf vadgntvmvw tfailyfvvc ygsvacwaft gsflrryvqk psrvrflnrm
      181 magllvasaf yllqg
//
LOCUS       WP_010795124             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Pseudomonas].
ACCESSION   WP_010795124
VERSION     WP_010795124.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..283
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31537
     Region          12..276
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 myrnvlelht gqpasdgagv rmtrvfagqg verfdpflml dqfdtanadd yiggfpahph
       61 rgfetvtyml egrmrhedhl gnqgllkpgg lqwmtaargi ihsempeqqe glmrgfqlwl
      121 nlpgktkmgp asyrdyepae vprlttsqgv evvvlaghfd dgehqqlgav qrpdtdpyyf
      181 dfimpaqsai sprlpeghra llyvyegqie vegdtvapvt tnrlvrlsde gqlrirsaqg
      241 arvlliagap lnepivqygp fvmntreqie qalrdyqrge fgq
//
LOCUS       WP_010795135             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkaline phosphatase family protein [Pseudomonas].
ACCESSION   WP_010795135
VERSION     WP_010795135.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..265
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29423
     Region          2..254
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mktilvvldg laygvardcm gylqgicqag rgrlytmqce lpslsrplye ciltgvrpvd
       61 sgithnqivr lssqrsvfhy aceaylttaa aayhwisely nrspfdaard rhicapdlpi
      121 qyghfyyadh ypdshlfdda eslrrrhsld fllahsmnid daghkyglss sqyrnaarva
      181 diclsghlpv wleagyqvmv tadhgmnddr shggllpeer evplfvfgtg fslqeaspvq
      241 tdlcgtlcel lgvahdkpvc rella
//
LOCUS       WP_010795137             264 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010795137
VERSION     WP_010795137.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29011
     Region          33..263
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 msnanrsvsl yhrlvvwllf lilllplaat llyslatqws atllpsgltl kwyvalwsds
       61 rfliafghsl ivcvgallla vflvlplmfv iayhfprlda lmnvfillpf avppvvssvg
      121 llqlyaggpl pligtpwili gcyftialpf myraisnnlq alnihdlmda ahllgastfr
      181 aallvvlpnl rkglmvalfl sfsfligefv fanilvgary etlqvylynm rngsghftsa
      241 lvisyflvvl tvtwaasgls rdks
//
LOCUS       WP_010795253             230 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RDD family protein [Pseudomonas].
ACCESSION   WP_010795253
VERSION     WP_010795253.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..230
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25021
     Region          11..151
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mplpldtllr vetpeaidlm lrpasvipra layaidlair gaimalaylv lgflghvgvg
       61 lialltflis wwymvlfevl nqgrspgkql mklrvlnddg tpvgwsgsll rnllrvvdll
      121 pfgyamgils sllhpsfkrl gdlvagtlvv hqeqpherft lqgviplspp falglieqqa
      181 ilsfaerqng lslsrrdela allaeplgvd rseaterlnr iaqallgahv
//
LOCUS       WP_010795263             369 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Pseudomonas].
ACCESSION   WP_010795263
VERSION     WP_010795263.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..369
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41268
     Region          210..363
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(245,288)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(250,253..254,258,262,284,286..289)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(280,308)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mrdltvtrsi nasaighqvl plavvvlall plllstavgf ysssiasffa dtlgflagva
       61 vmtgviawgg gkhlkalple pyiivsilfl tyslthivhl rgtflvsyvl vlmlgifqir
      121 laafvrcall aygayvglcl winlepqdsr tvrmmivqsi ilaivlvsmv lfaryhhrir
      181 yqlnarradl erhqdnlrhv mrqleaqvit deltglrnrr yflqiaseal hrlghgrmhg
      241 lalidmdffk qindqfghgi gdlvlktfae vgeaclreqd vlaryggeef vlllpfsdpq
      301 qlvvccerlr eafsrtvfeh adlgtltvsi gmslimtgrt leesllladq alyrakrngr
      361 nrcevswes
//
LOCUS       WP_010795320             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
            ligase [Pseudomonas].
ACCESSION   WP_010795320
VERSION     WP_010795320.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..455
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=47759
     Region          3..450
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mlkpmflqdl teplsaslkg gnvsftavst dsrtleagql fvaltgprfd ghaylssvaa
       61 kgavaalvek aqpdlnipql ivkdtrvalg qlgelnrlsf sgpvvavtgs sgkttvkeml
      121 aailntlgst latqgnlnnd lgapltllrl eqshqyavie lgasrlgeia ytvglthphv
      181 siitnagrah vgefggveki ieakgeileg laangtailn rddqafeiwr krakgrnvis
      241 fglndmamfr aanivrdarg cpsftllspa gsadiqlnll gehnvvnala aaaaahvlgv
      301 elahivqgle alqpvkgrtv sklgindsrv iddsynanpg smkaavdvlt gfsgrtvlvl
      361 gdmgelgewa esahrevgey akgkvsafya vgplmkhaae afgadarhfd draalieall
      421 leaapestfl ikgsrsaamd nvvfalcnkd veekh
//
LOCUS       WP_010795352             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_010795352
VERSION     WP_010795352.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..255
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28805
     Region          15..253
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 msenaktlgi gdkimiqmqd vnkwygqfhv lkdinltvrq gerivlcgps gsgksttirc
       61 inrleehqkg nivvddveln gdlknieair revgmvfqhf nlfphltvle nctlapiwvr
      121 klpkkeaeev amhylkrvri pdqahkypgq lsggqqqrva iaralcmkpk imlfdeptsa
      181 ldpemvkevl dtmiglaqdg mtmlcvthem gfartvanrv ifmdkgeive qappdqffdn
      241 pqnertklfl gqilh
//
LOCUS       WP_010795354             391 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter permease [Pseudomonas].
ACCESSION   WP_010795354
VERSION     WP_010795354.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..391
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42474
     Region          9..391
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 msksigtsgs lindpraraw afqilaivav aalgwylfnn tqtnlehrgi tsgfaflehs
       61 agfgvsqsli dykesdsygr lflvglantl lvsilgiila tvlgfiigia rlspnwlvrk
      121 laaiyietfr nippllqiff wyfavlrlvp gprqslsffd tlflnnrgly vpapvsaegv
      181 vpflvaiala vvasialarw vkvrrdrtgr gfpllisiia llivlpglaa lifgapfhwt
      241 vpqlkgfnfq ggwvvipelf allvalsvyt aafiaetvrs giqsvshgqt eaanslglkp
      301 srtlrlviip qsmrviippl tsqylnltkn sslaagigyp dmvslfagtv lnqtgqaiet
      361 iaitmsvylv islsisllmn vynkrmalre r
//
LOCUS       WP_010795356             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Pseudomonas].
ACCESSION   WP_010795356
VERSION     WP_010795356.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..219
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23995
     Region          12..219
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mpeitpliie spqpanscvi wlhglgadry dfqpvaeivq rvltttrfvl pqapsrpvsi
       61 nggwampswy dilamspara idhsqldesa ryvdelitqq mdigidarri vlagfsqgga
      121 vvfhtafaia hkplggvlal styapgfqet laseaqrdip vlcihgtldd vvplglgrea
      181 ydflakeqvp vqwqdypmgh evtqeeiali aqwlqdrla
//
LOCUS       WP_010795448             336 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Pseudomonas].
ACCESSION   WP_010795448
VERSION     WP_010795448.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..336
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36415
     Region          <95..328
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mpvftprqil lvswfvilas lmlvfplglv pslfagllvf elanmleprl qglisgdrar
       61 ivavallvtl vvcvlavffa gaisfvlhev rnpgslidkf malterargq lpmaldkylp
      121 asaedfrhsv newlgahlge lqtigkdaih tfvtlvigli lgaavalqrk rsraqerpls
      181 talldrvall seafrnvvfa qvkisfinti ltavflagvl plcgihlpli ktmivatfil
      241 gllpvignll sntlilivgl svslwvavsv gcylvaihkl eyflnarivg gqikarswel
      301 llamlvfesa fglpglvaap iyyaylksel tradlv
//
LOCUS       WP_010795391             297 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Pseudomonas].
ACCESSION   WP_010795391
VERSION     WP_010795391.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..297
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32875
     Region          211..289
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mnaaipntlp aasavrpadr lgftlfiaal vhvvlilglg fsmpepsevs ksleitlasf
       61 ksdkapekad flaqenqqgs gtldkalaps tteevpfkds eikpavkpts prqttepkts
      121 kaavttksar qdkaptrkek pepeavaret phfdnsqiss eiasleaqls qerqqyakrp
      181 kiyrinaast mkdkgawyke dwrkkiervg nlnypeqarr erlygslrll vsinrdgsly
      241 evqilessgq tvldqaalri vrlaapfapf sgdlsdidrl eiirtwrfer gdrlasq
//
LOCUS       WP_010795514              65 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010795514
VERSION     WP_010795514.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 65)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..65
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6770
     Region          1..65
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mhtfnvqgms cghcvkavtq aitaldasar vdvdlptgkv tvdsreapep lleaireegy
       61 saeia
//
LOCUS       WP_010795550             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent rRNA methyltransferase
            [Pseudomonas].
ACCESSION   WP_010795550
VERSION     WP_010795550.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..397
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=43715
     Region          5..396
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mslpslrlka naerrlragh lwvysneidv aatpltafqa geqavleaag gkpigivals
       61 phnlicarli srdtkhvldk sllvhrlkva lslrerlfdk pfyrlvygds dllpglvvdr
      121 fgdvivaqla satmerhkdd vlaallqvlk paavlwknds sareaeglpr yvesaygdvp
      181 ewaaleengv kfeapivegq ktgwfydhrm nrarlapyvq gkrvldlfsy iggwgvqaav
      241 fgasevmcvd asgfaldgve rnaalngvae kmacvegdvf ealkelkaad erfdvivadp
      301 pafikrkkdv kngeaayrrl neqamrllnk dgilvsascs mhlveenlqe illssarhld
      361 rhiqlierga qgpdhpvhla ipetryiksl tcrilps
//
LOCUS       WP_010795551             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Pseudomonas].
ACCESSION   WP_010795551
VERSION     WP_010795551.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..301
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32385
     Region          1..299
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mvvvlaimpv fglivlgyvl gwrqwltpes mggltqlafk vfmpavlftg iakadlrhgl
       61 spllllgyfg pvllvfllvn lfvhwrwrep tafgltasys nnvligiplv vnlmgeenlv
      121 yvfailalhs ltlfamqsfy tafggtekvs ipellmslan plivglllga avnvsgltlp
      181 gpiwqiatwl aqaglpcali vlgvnlsryr lrpslsvvgl taikllvfpf vvwtvclwlp
      241 glsgaarsvl mlmaacpsgv nvlafartle enrvvsstvf lstvlavvtv plwmalvgln
      301 r
//
LOCUS       WP_010795573             134 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Pseudomonas].
ACCESSION   WP_010795573
VERSION     WP_010795573.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..134
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15056
     Region          3..131
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mnfhtrkwvk pedlnanntl fggsllkwid eeaaiyaivq lgnqrvvtky iseinfvsas
       61 rigdiielgi tatefgrssi tlrcevrnki trksiltidk ivfvnldeeg nptphgktki
      121 tyiedqfkde ekga
//
LOCUS       WP_010795594             194 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TMEM165/GDT1 family protein [Pseudomonas].
ACCESSION   WP_010795594
VERSION     WP_010795594.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..194
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20647
     Region          1..178
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 mesllvptlv valaeigdkt qllalllaar frkpwpiimg mvastlanhf vagavgswvs
       61 rffsetalsw ilaisfvava lwtlipdkld edeasglkks ygpflttlva fflaemgdkt
      121 qvatvmlaaq yphfilvvmg ttlgmlvanv pvvlagnfaa drlplvlirr laatafgila
      181 laaayhalql sgmf
//
LOCUS       WP_010795595             273 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M48 family metallopeptidase [Pseudomonas].
ACCESSION   WP_010795595
VERSION     WP_010795595.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..273
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29399
     Region          78..263
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(144..145,148,202,206,246)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(144,148,202,246)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mrrvlpivgl slsvllsacq avnttsgnav gverkqymfs mlsadqvnqm ysqsyqktvt
       61 eaknagklan dtaqgkrvqa iakqliahts alradaanwd wqvnvlqnde vnancgpggk
      121 ifvytglldq lkptddelaa vigheiahal rehsreqmsr ayaiemgqni ggallgigqg
      181 gmqvadqvtq vsltlpfsrs neneadligl elaarsgynp naavtlwqkm aklsngnqsp
      241 eilsthpsdd krmsnleaai pkvmpfyeas rks
//
LOCUS       WP_010795648             317 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010795648
VERSION     WP_010795648.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35341
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,146,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..220,222..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdnlfnmraf mcvveagsft aaaqrleltt ayvskavtnl ethlqtrllh rttrrialte
       61 agerylqrcq qifayiqeae aeashahahp vgklkvhtmt glgqhylikt iaryceqype
      121 vnfdlrltnt ftdiledgyd vsvilasqlk dsgyfskrlg sthsilcasp aylekygtpq
      181 ttaalrqhrc lrlvnkamsl dkwlfqgpkg eelvtidqtl fqvntadalm eaiasgmgig
      241 alpiyaavkg lkdgtlqqvl phhslyplnv yalypsrqyl dakirtlvdf lrdtlpgllk
      301 adeqavkrly eegpvsa
//
LOCUS       WP_010795634             340 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Pseudomonas].
ACCESSION   WP_010795634
VERSION     WP_010795634.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..340
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37390
     Region          1..339
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrvglvgygk ggrffhapli tsvspialvg vvirsserra elqqdypgvp ayetlaelid
       61 agvdavvist ppeiregmil eavsrgvpvv sdkpfalges raqllisaar eagvpltvym
      121 nrrwdsdirt arrmitsgkl gevltfesrv etfvsgtrgn asgggllrdl gshlvdqalw
      181 lfgsvrsvya evrfmdeqqq ldedfflslt hqngvisrlw gstiqhnpgp rlkvngtegc
      241 yriecldgqd qallagrspk terdrwgved hlrwgwmqhg eerelvpser grwdlfyehl
      301 aaalsgkgel pvsledalet trildaarrs aqqgqvitlg
//
LOCUS       WP_010795667             220 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010795667
VERSION     WP_010795667.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24633
     Region          11..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 martpsprka rsssrqrieq iltaarhmli dqgparlsiy giaeradlpp ssvyhffpsv
       61 tallealtqe ahaafraclq asvdhdslnd wrdlsrivea rmlevyeqda aarqlilanh
      121 gltevvqadr qhdtrlgeql qalfathfhl pplpddidvf tlamelgdri yarsvqqhgg
      181 itprwaaegh rvfdaylsly lppylpkrnt plpndltvaq
//
LOCUS       WP_010795734             681 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M13 family metallopeptidase [Pseudomonas].
ACCESSION   WP_010795734
VERSION     WP_010795734.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..681
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76295
     Region          1..681
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mrhifagavc vlalsacgks efvqpqtpan tlqsgikken fdpgvrpqdd ffnaingqwl
       61 kntpipadkt sygafhaiad ttekqlhaii ealaakpdka tgsdeqkigd lyasfmneaa
      121 ieaqglkplq gafdaidsih drrsllitma rlqrlgidvp lepyvtqdak dskryvaeia
      181 qsglslpdrd yyliddtsfa eirsgfvshv qrmldlanlp dpagsarkva alekqialaq
      241 wdkvdnrdpi ktynayeptq lrtltraidw psylketgfv dqhpiiveqp syitglgkll
      301 tstplstwkt ylkwhvlhay aqalphayaq edfaffqqtl ngakeqrprw krgvsavegs
      361 lgealgkeyv arhfppenka rmealvrnli aaygqamdkl dwmsedtrqa akaklakfty
      421 kigypnqwrd ysslhiapdd lignlqraqt feyqrslakl gkpvdpdewa mtpqtvnayy
      481 nplrneivfp aailqppffn mqaedavnyg gigavighei shgfddqgsq fdgdgnlrew
      541 wtktdrerfa kratalaeqy sayepvpgyh ingrftlgen iadlggvtis ysayhlslng
      601 kpapvidgmt aeqrfftgwa qvwctkytqq nllnrlktdp hspaqyrtng vlsnvpgfye
      661 aydvkpddqm ylppdkriki w
//
LOCUS       WP_010795758             108 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thioredoxin family protein [Pseudomonas].
ACCESSION   WP_010795758
VERSION     WP_010795758.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..108
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11926
     Region          21..101
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(33,36)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mamnttyaaq epsrnevdal egatliefga pwcgfcraaq plieqafqdh pairhlkied
       61 gsgrrlgrsf kvklwptlif frngqevsrl vrpastddir qglagidq
//
LOCUS       WP_010795777             209 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Pseudomonas].
ACCESSION   WP_010795777
VERSION     WP_010795777.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22356
     Region          1..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtlhvwfvfc vaylvttlsp gpnvllvirn tlrygargtl atlagnltaq lfviilvalg
       61 igalvaampm aflamkliga ayliylgfvq llkrqpgsst vtpaialsvs sskvfgeall
      121 vsisnpktli ffsaflpqfi epgrslvvqf ttmyltiali vvtvhcvycf svsrlsrrls
      181 asrwvtaikr asgalfvglg vkllmarqa
//
LOCUS       WP_010795790             302 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Pseudomonas].
ACCESSION   WP_010795790
VERSION     WP_010795790.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..302
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32083
     Region          <131..275
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrylcsallt swllasptwa maeqsketsl iskadqtslt ekprakrkgg vrlltlntka
       61 gkalevrndm dvpvtvtvrl srtvnvggvg ngvirqtvpa nsqlrvatlq krqqgfpmhy
      121 dqafsfsphf apgsggglgn pnslasitag yayslpwqgg pffisqgang dfshhtpkgr
      181 yavdvampeg tpvvaarsgt vieiqnrqfg hgpspsgnfv riqhddgtqs aylhlkrgsv
      241 vvregqkvtt gtplaqsgnt grstgphlhf vvqqgegdal vsipfrfarp vgelpnfalg
      301 gq
//
LOCUS       WP_010795833              69 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Pseudomonas].
ACCESSION   WP_010795833
VERSION     WP_010795833.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..69
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7368
     Region          4..69
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 msgrqngtvk wfndekgfgf itpesgpdlf vhyrsiessg fkslsegqav sfvavkgqkg
       61 mqadqvqva
//
LOCUS       WP_010795816             707 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_010795816
VERSION     WP_010795816.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..707
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77914
     Region          4..706
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mrrlivpvls lhaftcyaqe tpsdsepasl sqmeitanvt esaqgpvegy ratrsasatr
       61 tdtaihetpq sisvvprqvv edigatrled aldyaggver gnnfggqglt eflvrgfstq
      121 efyrngfavn rgypnmpdas tierlevlrg pasmlygrgd pggtfnivsk qpqadrktvl
      181 gsqfntqglr rgtldttgal denaeftyrl nlvaegsdsf rdhveseryn vapvlrwqls
      241 drtavilegd ylhnrhpmdr gvtryatqag qlqrdrflge edagklrnen attqlrlehq
      301 lnddwairgg vqyldgsldg gavennglaa dgrtigrnys ertlewddia fqtnveghfk
      361 tagfahtlla gveyddfnyt sfirrssgsv safpldlyap vygqplpalt rttthddenl
      421 ksyalylqdq veltdrlkaq vgarlerfeq qytnylstsg sweqahnavs prfglvydlt
      481 dslavyanta rsfkpnrgad rssqafdpek giayetgiky dvpehdlsit aalfhitken
      541 vltsdpldsn yqiaagevrs rgfdlslagn itpqwrvigg yayvdaevtk sttstmpags
      601 rlanvpkhsv nllntyefds gllsglgvgv glkyvsdrkg stsstafdms sytvvdllay
      661 ypltdrirln lnldnvfnee yderawgsiw aypgaprtlq agvsitl
//
LOCUS       WP_010795836              72 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Pseudomonas].
ACCESSION   WP_010795836
VERSION     WP_010795836.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..72
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7674
     Region          4..72
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 msdrqtgtvk wfdrvkgygf ivqaqgpelf vhhksvnggh avkqliagqp vsyiaaegkl
       61 gkgmqaehve al
//
LOCUS       WP_010795868             760 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Pseudomonas].
ACCESSION   WP_010795868
VERSION     WP_010795868.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 760)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..760
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84494
     Region          46..734
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkytriylal vasglchgva maqetderdv gtigvegkat lgsgymtpee spksrstltr
       61 eamnkqtata navdrlkytp glnissedat glsgfrftlr glnsdqvgms vdgmpindsg
      121 nyalysnllg dpenldqisv vqgasdadgp higssggnit lttirptket gafvkqtags
      181 ngtyktfarl ntgewnglsn wlsashtegq mwrghgavra dkvewnsffd agdgntanli
      241 lkyheqdnns ysqltkseft qygrkydpnp nppalgsngk iskyyelaqn pfktftgvln
      301 tqfrlrddms lsvipyyywg dgsgvgstay slnrgtssng vydlgnlpta ssyandglsy
      361 tgvyyrpsrt qtwrpgittk lnwdlgdhsl qfgywyerar qrqtqpfial kssgkpesvw
      421 sdsdetrdan gniiqgrdry tvtpahkvwv qdtwymnpdw tlnagvaymd vdrkgtnhgs
      481 ltelpekrhq nyskvlptfg igyrfdeqnq ffynltrnmr ipynyvlydq gegsinlnpe
      541 tswsnelgwr ytqedmalsa tlfylkfkdr qvssrdengd yadinagdvd nmglelewsg
      601 llphnfnyyt sytytrakqk ddvtaynngv avelptsgkq fanvpknmla anigyddgry
      661 ygtfgakyts klygdltnde sipgrtifnl gagvylpvdk hivkgatlrl nvdnlfdkky
      721 ldgvytyktn aasysgyrdg dpayivgver tvtvsleasf
//
LOCUS       WP_010795922             177 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010795922
VERSION     WP_010795922.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..177
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18702
     Region          <26..175
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          51..81
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(52,56..57,60..62,64..65,69,72,81,83,85,89..90,
                     93..95,97..98,102,105,114,116,118,122..123,126..128,
                     130..131,135,138,147)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          83..114
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          116..147
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mteenrdaql sedqaiefah qvldlarsgd avtlgklldk glppnlrtsk gdtllmlasy
       61 hgqldavrtl ldhgadpnic ndngqspiag aafkgnlpmv kllveqgadv egvspdgkta
      121 lmmaamfnra eiaeyliekg aninaqdang vtplaaaqrm gapetvalle riqelqk
//
LOCUS       WP_010795936             441 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Pseudomonas].
ACCESSION   WP_010795936
VERSION     WP_010795936.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..441
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45981
     Region          5..438
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mstsspepdt klrraitgpl lllfilgdvl gagvyalagk iagevggaiw vplvvamgfa
       61 mltaasyael vtkypkagga avfaarafkh plvsflvgfs mlaagvtsaa glslafagdy
      121 lgafihvspt mtalvfltlv allnargike slnanlvmtl ielsglllvv ilavlyvshg
      181 qgeparvlqf aegtspplav lgaallafys fvgfevsani aeevkdvrri yprtlfgall
      241 iagviyvlvg laasivlspa qlvessapll dvvratgygi ppqlfavaal lavsngallt
      301 mimasrlayg maeegllppv lgrvlprrrt pwvaiiattl vamaltvtgt lsalaetvvl
      361 lllfvfmstn vavlvlrrdk vdqphfrtpt lvpllaivsc lvllsqqsae twlragillg
      421 vgvvlyfvtr ahttreaadv v
//
LOCUS       WP_010796008             386 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: lipase family protein [Pseudomonas].
ACCESSION   WP_010796008
VERSION     WP_010796008.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wong,H. and Schotz,M.C.
  TITLE     The lipase gene family
  JOURNAL   J Lipid Res 43 (7), 993-999 (2002)
   PUBMED   12091482
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Cygler,M. and Schrag,J.D.
  TITLE     Structure as basis for understanding interfacial properties of
            lipases
  JOURNAL   Methods Enzymol 284, 3-27 (1997)
   PUBMED   9379943
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..386
                     /product="lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43439
     Region          <2..135
                     /region_name="Lipase_3"
                     /note="Lipase (class 3). Lipases are esterases that can
                     hydrolyze long-chain acyl-triglycerides into di- and
                     monoglycerides, glycerol, and free fatty acids at a
                     water/lipid interface. A typical feature of lipases is
                     'interfacial activation,' the process of...; cd00519"
                     /db_xref="CDD:238287"
     Site            order(9..10,13..21)
                     /site_type="active"
                     /note="active site flap/lid [active]"
                     /db_xref="CDD:238287"
     Site            66..70
                     /site_type="active"
                     /note="nucleophilic elbow [active]"
                     /db_xref="CDD:238287"
ORIGIN      
        1 mvlisirgtq enppdllrdi dakqvpykeg vgqahrgfye aflavknfvt pylrnfyteq
       61 kivvtghslg gaiallvaew lrrdaqgydv llytygapra gdrnfvegas elihhrlvnh
      121 ndpipslpat wmdtdqrifi pgiaalitga tgiggaafla givnlkgdny qhhgtlhhfl
      181 plpigrgett svlwqpecsg ieeaactyya anikndmpdr alfiaqlasm sqhftvagyv
      241 pachatllrw kasaaqegqs ltkreqewle keiysyqknl elwekqawqk ydalhrhqev
      301 slslrrqqfe qaisfaaaer rrlprtlgri relaqkpisl envygsqinn pmllslisrw
      361 qqhdenlpsk tpqlasiprt ykpsyv
//
LOCUS       WP_010796057             542 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Pseudomonas].
ACCESSION   WP_010796057
VERSION     WP_010796057.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..542
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=57462
     Region          16..542
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mgfrslniap rsaicfalfa llilfqgvys lkqsasmnea ekmvelnvlp tlkvlgqidt
       61 tlmrirldns rlrvesdpas kkadalkdiq iartellgyv dqlgkvivtk aghdtfnals
      121 kglsdylsih qryldlltng klteavalss gemfaaaeav knaittlkqe advkasnagl
      181 haddvysstr mmtaiivvaa llatvllawr lthslvapih qslqvaqria nrdfsvaies
      241 hgndeparll kalavmqsnl retlghisds saqlastsee msavteettr gvmrqndeie
      301 qaatavnqms aavdevarna asaseaalss sqaaatgqlk vsqtleaine lydsveatag
      361 evqglavmtq diskvldvir gvaeqtnlla lnaaieaara gdagrgfavv adevrglahr
      421 tqestreies migsiqagtd kavqsmaqss srahgtldia raagealtti nssiaeiner
      481 nlliatasee qaqvarevdr slvsirdlsm qtgsgahqta aasndlsqla vslnglaqqf
      541 rl
//
LOCUS       WP_010796050             387 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Pseudomonas].
ACCESSION   WP_010796050
VERSION     WP_010796050.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..387
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41014
     Region          1..385
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdyhlssklt alkstveevv dqaiaplasq vdqnclwpah sidalseagl mglqvpvaqg
       61 ghgqgllals vitetigkac pssalcfgmh cvgtaviaak atsyqkehyl eaiaagrhlt
      121 tlalsesgsg ahfylpatqi atvgdefvvn gikqfvtngg hadsyvvstv aseedneegd
      181 fsclivdsta qglewqapwn gfgmrgnssr alglnnvrvp aknllgepgd qvwyvfevva
      241 pfflmamagt ylgiaqsald aagehlrtrs yahsgetlrd ietlqsrygs mwialektrs
      301 lvreaarlgd lgdpnalpfi lackadagdt avmlaneamt icggaayren srvsqmlrda
      361 rashvmsptt dllklwtgrs llglpll
//
LOCUS       WP_010796059             198 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Pseudomonas].
ACCESSION   WP_010796059
VERSION     WP_010796059.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..198
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21793
     Region          93..197
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(99..100,133..134,137,141..142,145,189,191)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mskafrqavw lllavwlagc ssksyvvlvd spygltrdvt vttptgttqi drtqqaisld
       61 keapgrtftl ppkqilmdft palaaqptlp vyytlyfega snrltdesqd tlqrivdtlr
      121 krtpaavsii ghtdtlgsas inekvglqra qliarqlqar hldlldltva shgeenlliq
      181 tppntaelrn rrveviir
//
LOCUS       WP_010796193             234 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AzlC family ABC transporter permease [Pseudomonas].
ACCESSION   WP_010796193
VERSION     WP_010796193.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 234)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..234
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25501
     Region          13..233
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mntrvltrka pelrtfseas pvvagyftvs fvfglmavsa gyplwlpvam clfvyagasq
       61 faalalmtan asivtivmtt flinarhmlm smymsralrt tglsrlerwv yaaeltdesf
      121 afhssklqkg vavnarylis fnlfchsawv lgallgalss tytahliqyk ldyaltamml
      181 yvlvslcdsk gklvaalaav acmgvlnllf esalnvfiat ffgcwigvcl kkrs
//
LOCUS       WP_010796256             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [Pseudomonas].
ACCESSION   WP_010796256
VERSION     WP_010796256.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..455
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51003
     Region          29..451
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mdpspsfdts vlfadfglvl falllvllng ffvaaefamv klratrvegl aeshgwrgri
       61 lrtvhsqlda ylsacqlgit laslglgwvg epafaellep llrmagvdtp elvhgiafft
      121 affiisylhi vvgelapksw airkpdllsl wtavplylfy wlmypaiwll nasanailri
      181 agqgssngdh ehhysrdelk lilhssrald ptdqgmrvla saveleelev vdwansredl
      241 iyldhtasle eiltiirrhk ysrypvynee envfigvlhi kdlllaiagl dsqaesfeld
      301 elihplervs khmplsrlle qfrqggahfv lveeadhkvv gfltmedvle vlvgdiqdeh
      361 rkaergvlay qpgkllvrgd tplfkierll hidldhvead tmaglvydsl krvpeedevl
      421 eaeglriiik kmkgpkiila kviklggeed alrhh
//
LOCUS       WP_010796361             341 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010796361
VERSION     WP_010796361.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..341
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37900
     Region          <11..77
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 mrkslfalll vaasswvqad vqlrqghpds ytvvrgdtlw disgkflskp wqwpeiwhan
       61 pqvenphliy pgdrlslvyv dgqprlmlnr gesrgtikls ptirstpiae aiptipleai
      121 nsfllsnrvi ddanqfrnap yivagnaerv vsgagdrvya rghftedqpa ysiyrqgkay
      181 kdpqteeflg inadyigsgd kvtsegdmtt lvlsrsneev rlgdrlfpte qrvvnstfmp
      241 sapdrdingi ildvprgvtq igqfdvviin kgmrdglveg nvlavyktge tvrdrvtgdn
      301 vkvpdersgl lmifrtydkl syglvlnatr qlsvldkvrn p
//
LOCUS       WP_010796404             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Pseudomonas].
ACCESSION   WP_010796404
VERSION     WP_010796404.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..207
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22831
     Region          1..204
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 milydlersg ncykirllls vlelnyqrvk vdlnagenrq peflainprg qipvlvddsv
       61 tlwdstsilv ylarqygrgl wlptdpvtma kvmqwlafeq negryglgra rsislnntsv
      121 fartgnltdc qalglaglev lekqltgeew lvpeaggpti adiacypyta mapeggidla
      181 pfvavqkwlr rvqalkgyve mptatpa
//
LOCUS       WP_010796427             887 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [Pseudomonas].
ACCESSION   WP_010796427
VERSION     WP_010796427.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 887)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 887)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 887)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..887
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=94753
     Region          577..864
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mpkqisrvcl afllilslgh alaadqsata detispgdar ravsvlqdeq qraeavralk
       61 aiadtapakd adaaksddql addtaadtaa paeapaavai eangliartl rqvsrwgdgl
      121 edqlhqikqa alafpvwlrt hsasgqgkhi lsealvdlti vfgvglalew glryllgrpr
      181 raliqhaeea derarreqae rderqrlaqa qararaereq aeqaaavnaa evggirpase
      241 evalvqttrd gveqieavpv gatnaakggp astasdsaaq sqqqatadaa thdtaasprh
      301 tampgehwst lrhlpyalgs lifdllplal ffgaaalimr alsgdeqsvm tvvqgfvgay
      361 vtvrvcmavv rllispighg mriirvrtdi aqtletwirf tvvlaafgia laeavealga
      421 graghlaivk lfsllvhlcl vvlifkvrkp vgalieapae atgpvaalrn wlalvwaffa
      481 aafviglwvv walgvengfp klinfialsg avviaarlla ilvlgavgra fqpktdapsd
      541 esntpassvr srladryypl arrlitaait vctvivlfql wgldalswfa sgtigrslls
      601 avltilvaal vaivvwesan asvqrrltqw tnegdlvraa rlrtllpmlr sflliiivlv
      661 vgltalsqig inttpllaga siigvavgfg sqklvqdfit gifllmenam qvgdwvtvag
      721 vsgtveylsi rtvriragdg slhivpfssv stvnninrgi gnasirinvg yntdidqvfd
      781 elkaigaemr qdpafkdlii ndlevwgvda vdgsmvtvlg qmrcidkgrw gvqretnrri
      841 lkrfrelgit iadprtylvm psetaatdrs plphgnylps nqpspda
//
LOCUS       WP_010796428             183 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: gamma carbonic anhydrase family protein
            [Pseudomonas].
ACCESSION   WP_010796428
VERSION     WP_010796428.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..183
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19469
     Region          1..176
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mtirtyqnkt pvlgerafvd atavvigdve lgadssvwpl tvirgdmhrv rigartsiqd
       61 gsvlhithag pynpdgypli vgddvtvghk vtlhgctign qvlvgmgsiv mdgavvesqv
      121 iigagslvpp gktlesgfly vgspvkqarp ltekersffe ysaanyvklk dqhlaegydq
      181 hda
//
LOCUS       WP_010796434             141 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Pseudomonas].
ACCESSION   WP_010796434
VERSION     WP_010796434.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..141
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15814
     Region          1..141
                     /region_name="COG3565"
                     /note="Predicted dioxygenase of extradiol dioxygenase
                     family [General function prediction only]"
                     /db_xref="CDD:442786"
ORIGIN      
        1 malspfhlai pvydlaaarh fygdvfgcpe grsseqwvdf dffghqlvih ehpptaaqeh
       61 ahtnpvdghd vpvphfgvvl rweewealad rlkaretafv iepyvrfkgq vgeqatmfll
      121 dpcgnalefk afkdigqlfa k
//
LOCUS       WP_010796437             368 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Pseudomonas].
ACCESSION   WP_010796437
VERSION     WP_010796437.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..368
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40215
     Region          7..337
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mpsaegkiry avvaggwisq gafmpgvgqt snsvmtalvt gdpvkadela krynlksyry
       61 edfpallssg eidaiylatp nfrhrefavp aleagihvll ekpmatseed ckaiieaskk
      121 sgaklmiayr lhcepgtvem verirngdig dpriftstfa qpldpqnhra lngywagpvp
      181 dmgpyplnav rnlfgdepie vhavgvntpg rdittydavs vtlrfpqerl aqftvsysap
      241 nterfqvvgs kgeieaspcf gfgegvaity ratiegetqe hkhpvvdqfg geteyfsdci
      301 lndrapemdg degwrdirvl aaieraletg qtqtleplpp rqgptqaqvr tlplakvpdy
      361 intteptt
//
LOCUS       WP_010796512             445 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ammonium transporter [Pseudomonas].
ACCESSION   WP_010796512
VERSION     WP_010796512.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..445
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46239
     Region          27..444
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mtlrkyaglg allslampsl amaqeaaaep tlnsgdtawm lvstalvlfm tipglalfyg
       61 gmvraknils vmmqcfaitg lisilwmiyg yslafdttgm ekgvtnfnsf iggfgkafls
      121 sithdgltga aalfpesifv tfqmtfaiit palivgafae rmkfsamlvf tgvwftlvya
      181 piahmvwsgd gglmwdwgvl dfaggtvvhi nagiaglvaa lvlgkrkgyp ttpmaphnlg
      241 ytlvgaamlw vgwfgfnags avaangtagm amlvtqiata saalawmfae withgkpsal
      301 giasgvvagl vaitpaagtv gpmgaliiga vagvicffca tslkrkigyd dsldafgvhg
      361 vggivgallt gifaapalgg fgtvtdiggq lwiqlkgvlf tlvytgiltf vilkvidmvm
      421 glrvsdeeet vgldltlhne rgynm
//
LOCUS       WP_010796542             275 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aldo/keto reductase [Pseudomonas].
ACCESSION   WP_010796542
VERSION     WP_010796542.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..275
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31091
     Region          11..272
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mssipslqln dghhipqfgl gtwktpneea pqlirsalem gyrhidtaaa ynneegvgqg
       61 iaesgidrse lfvttklwne rqgfdetlka fdeslsklkl dyvdlylihw pcpkagkfld
      121 twkaflrlre egrvrsvgvs nfrqedleqi iletgvtpvv nqievhpllq qndlrevnrq
      181 knilteawsp laqggellkh plfqelakkh gktpaqvilr whvelgsiif pkstnperir
      241 enadifdfsl dsddmqkiaa ldegkrlgpd paefc
//
LOCUS       WP_010796547             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Fur family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010796547
VERSION     WP_010796547.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..161
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17348
     Region          19..159
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mtsiplasrp hdhshcvtha lgeaeslctk sgvrltdlrr rvlelvwqsh kplgaydila
       61 vlseqdgrra apptvyrald fllenglvhr iaslnafigc nhpghahqgq flicrhchva
      121 ieleqpaihe aiqagagtvg fkvegqtvev iglcsacqda q
//
LOCUS       WP_010796517             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified Pseudomonas].
ACCESSION   WP_010796517
VERSION     WP_010796517.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..231
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25676
     Region          3..227
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtirlitfdl ddtlwdiapv ihsaedalrt wmeteasrlg pvpvehlwqi rdrllerdpg
       61 lrhrvselrr rvihgalqda gyeepeagql aeagfaiyla arqqvtlyed vhetleqlsl
      121 rydlgvltng nadvheigla dyfrfalcae elgigkpdph pfnealrrag vtadaavhvg
      181 dnpvddilga qqaglraiwl nptgkpwsge napdaeirsl nelpavlerw n
//
LOCUS       WP_010796596             292 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YihY/virulence factor BrkB family protein
            [Pseudomonas].
ACCESSION   WP_010796596
VERSION     WP_010796596.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..292
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32469
     Region          7..288
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mlgfslrglg pldvlkravk efneddmaty asalayqmff smfpfilfli slvgflhlpd
       61 ffnwlreqan yvlpaqaleq vnpvidqlqq nqqggllsvg iivalwsasa avrslmtaln
      121 maydveegrp vwkrlplsvf ytiglalmli saaalmvtgp qflnwltsyi gleqvfitvw
      181 twirwpvavi llmlavaiiy yaapdveqdf rfitpgsvla vvvwiaaslg fafyvqnfgn
      241 ynamyggigt iiimllylyi ssavllfgae inaviehhsn egkekgdkkl de
//
LOCUS       WP_010796619             474 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar porter family MFS transporter [Pseudomonas].
ACCESSION   WP_010796619
VERSION     WP_010796619.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..474
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51503
     Region          33..458
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(44,162,165,169,283..284,288..289,292..293,382,
                     386..387,391,414..415,418)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 miktpsslas panaepsttd ssptnhkrkm qiittistfg gllfgydtgv ingalpfike
       61 dfgltpfses lvasslvfgg aigaaisgrl sdargrrkii lllsiifilg tlgstlapna
      121 eimvlarfil glavggasvt vpvylaemsp ahkrgqmvtr nelmivsgql laftcnaaia
      181 hffegshiwr wmlviatlpa vvlwlgmlvm pesprwlask grfgemlrtl kevraehqah
      241 keakevrqaa qedskakegs wedlktpwir kifligigia vvqqitgvns imyygtqilk
      301 esgfdtqaal taniangvis vlatflgiwl lgrvgrrpml itgligtttc llliglvsmn
      361 mapgterafi ilgltvsfla fqqgaispvt wlmlseifpm rirglalgft ggvlwlttfl
      421 vgffflqlva wfsisttffm ffafgllaia fvvrylpetr nktleaieee fkka
//
LOCUS       WP_010796628             595 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [Pseudomonas].
ACCESSION   WP_010796628
VERSION     WP_010796628.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..595
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=65414
     Region          5..588
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 makvmqkada vivgfgwtga imakelteag lsvvalergp mrdtypdgsy pqvideltys
       61 irrklfvdts ketvtirhnv sqtalpyrql gaflpgdgvg gaglhwsgvh lrvdpvelrl
      121 rshyeerygk nfipdgmtiq dfgvtyeele pyfdfaekvf gtsgqawtvk gelvgkgkgg
      181 npfapdrsdh fpltpqkntv saqlfqkaaw dvgyhpydlp santsgpytn pygcqmgpcn
      241 fcgycsgyvc ymysksspnl nilpalrqep kfelradahv lkvnltddkk latgvtyvda
      301 qgneieqpad ivilgafqfn nvrlmllsgi gkpydpktge gvvgknfayq nmatikayfd
      361 kdqhftnpfi gaggngvavd dfnadnfdhg phgfvggspf wvnqagtrpi agvsnppgtp
      421 nwgsqwkaaa adyynhqlsm dahgahqsyr dnyldldpty kdaygmpllr mtfdwkendi
      481 kmthfmvdkm kriaeamnpk ainvqvkapg thfntvsyqt thlnggaimg tdpktsalnr
      541 ylqswdvhnv fvpgasafpq glgynptglv aaltywsara ireqylknpg plvqa
//
LOCUS       WP_010796738             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: elongation factor Tu [Pseudomonas].
ACCESSION   WP_010796738
VERSION     WP_010796738.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..397
                     /gene="tuf"
     Protein         1..397
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43227
     Region          1..397
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makekfernk phvnvgtigh vdhgkttlta altkvcsetw ggsarnfdqi dnapeekarg
       61 itintshvey dsatrhyahv dcpghadyvk nmitgaaqmd gailvcsaad gpmpqtrehi
      121 llsrqvgvpy ivvflnkadm vddaellelv emevrdllnt ydfpgddtpi vvgsalmale
      181 gkddneigvs avrklvetld ayipepvrai dqpflmpied vfsisgrgtv vtgrvergiv
      241 kvgeeveivg ikattkttct gvemfrklld egragenvga llrgtkredv ergqvlakpg
      301 tikphtkfec evyvlskeeg grhtpffkgy rpqfyfrttd vtgncelpeg vemvmpgdni
      361 kmvvtliapi ameeglrfai reggrtvgag vvakive
//
LOCUS       WP_010796773             485 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: catalase [Pseudomonas].
ACCESSION   WP_010796773
VERSION     WP_010796773.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..485
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54352
     Region          2..485
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 msqnntltta sgipvadnqn srsagergpl llddfhlvek lahfnrevip errvhakgsg
       61 aygtftvtqn ithlssarlf esvgkqtpvf lrfstvgger gsadterdpr gfalkfytee
      121 gnwdivgnnt pvfflrdplk fpdfihtqkr npqtnlkspq mmwdfwshsp eslhqvtilf
      181 sdrgipdgyr fmhgfgshtf svineagerr fvkwhfkskq giknlspaea trlagtdpdy
      241 aqrdlfdaie rgdfpkwrvc iqvmdeaeaf srtenpfdvt kvwsqkafpl ievgelvlnr
      301 nplnyfaeve qaafapsnvv pgvglspdrm lqgrvfayad aqryrvgtny qqlpvnvprs
      361 pyqnyqrdga mrfdgnggaa pnyepnsfsn apkqapqyre pamtlsgaad rydhrldedy
      421 ysqagalfrl msdaqkalli dnitgamrsv trdvqcrqia hflkadrayg egiasglgvs
      481 lseve
//
LOCUS       WP_010796857             274 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: (Fe-S)-binding protein [Pseudomonas].
ACCESSION   WP_010796857
VERSION     WP_010796857.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..274
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30205
     Region          <10..271
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mselfynaap natriappip kqreypaqkp qhvylfgtcv vdlfypeagm dsirllereg
       61 itvhfpqsqs ccgqpaytsg yteearevar aqlglfrqdw plvvvsgsca gmirhhysel
      121 fkhepatlrq iealadrtye laefllnvck vdlkdrgapt kvalhtscsa rremnthlhg
      181 rallaqleav qrvdhdhese ccgfggtfsv rmpdisgamv adktralqes gaaqivtadc
      241 gclmningal ekqnatlrgq hlasfiwqrt gdsv
//
LOCUS       WP_010796776             462 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010796776
VERSION     WP_010796776.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..462
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48740
     Region          20..393
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(27..28,31..32,35,68,118..119,121..123,126,148,
                     151..152,155,224,227..228,231..233,236,264,268,312..313,
                     317,321,344,347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 mhdklsdrms alerraavgl alvfafrmlg mfmvlpvlat ygqeladatp aliglaigay
       61 gltqavlqip fgtlsdrigr rpviiagllv faagaavaan ahsiwgvilg rviqgggais
      121 aavmallsdl treqhrtkam atigmsigvs favamvsgpl ltrsfglsgl fwatsalali
      181 glllilflvp kgsrvmqhre ssvakqalgk tlrnkdllrl dlgigvlhav lmssfvalpl
      241 alaehaglpk eqhwwvylta lvvgfftmvp fiiygekkrq mkrvlvgaia vlalcelfff
      301 afdesltalv igivvffaaf nlleaslpsl vskvapaggk gtamgiysts qflgsaaggi
      361 lggwlfqhgg lntvflgcaa lcvvwlliav tmreppyvts lrmplvpsva qdaaltdrlm
      421 alpgvtdavv vaeeaavyvk idtkqvnrea lerlvnpaav ah
//
LOCUS       WP_010796866             420 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010796866
VERSION     WP_010796866.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 420)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..420
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45493
     Region          18..232
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          143..416
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mylfrlalas lsnrrftall tvfaialsac lllavervrt eakasfasti sgtdlvvgar
       61 sgavnlllys vfrignatnn irwdsytqla enpkvkwaip lslgdshrgy rvlgtsqayf
      121 ehyhygrnqa ltlsegkpfq diydvvlgae vaqalhyklg dhivlahgvs tislvehgdk
      181 pftvvgilar tgtpvdrtlh islqgmealh vdwqngapar gagkisadqa rqmdltpkai
      241 tavllglnsk vatfglqrai neyrgeplma ilpgvalqel wslmgtaeqa lfivslfvvl
      301 tgligmltai ltslnerrre mailrsvgar pwhifsllva eafalalagv vaglallyva
      361 iaiaqapvqa yyglylplew psryewtllg giliaallmg cvpawrayrq sladglsvrl
//
LOCUS       WP_010796938             355 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I mannose-6-phosphate isomerase [Pseudomonas].
ACCESSION   WP_010796938
VERSION     WP_010796938.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Jensen,S.O. and Reeves,P.R.
  TITLE     Domain organisation in phosphomannose isomerases (types I and II)
  JOURNAL   Biochim Biophys Acta 1382 (1), 5-7 (1998)
   PUBMED   9507048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..355
                     /product="class I mannose-6-phosphate isomerase"
                     /EC_number="5.3.1.8"
                     /GO_function="GO:0004476 - mannose-6-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009298 - GDP-mannose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38581
     Region          4..329
                     /region_name="ManA"
                     /note="Mannose-6-phosphate isomerase, class I
                     [Carbohydrate transport and metabolism]; COG1482"
                     /db_xref="CDD:441091"
ORIGIN      
        1 mdwyplrlst pirshmfggh aiaeilgrrg lpagriaetw evsdvegsia nvtegslagq
       61 slrdlvkryp telvgpgfdg pyfpllskfi dgcgmlpvhl haddetarrl ecqpngktea
      121 whilwaepga talvgikpgi nrdtlrsali aqdydavmrr lpvragetiy vpggtlhsfg
      181 pgtliyeieq tsdtqqqamp wqmsdgspls hqdwidgidq lleecylepq peftpgfrlp
      241 qgndidrlic taspyfaler wrvagagarp ltyrfnkatl lsnvgtpiri qagnwsgvlg
      301 aaetlllpaa lgeiqlagpa dvlfgyvpdl eqdirtplra agygdqafav lgath
//
LOCUS       WP_010796986             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NRDE family protein [Pseudomonas].
ACCESSION   WP_010796986
VERSION     WP_010796986.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Bard,F., Casano,L., Mallabiabarrena,A., Wallace,E., Saito,K.,
            Kitayama,H., Guizzunti,G., Hu,Y., Wendler,F., Dasgupta,R.,
            Perrimon,N. and Malhotra,V.
  TITLE     Functional genomics reveals genes involved in protein secretion and
            Golgi organization
  JOURNAL   Nature 439 (7076), 604-607 (2006)
   PUBMED   16452979
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..248
                     /product="NRDE family protein"
                     /GO_process="GO:0007030 - Golgi organization [Evidence
                     IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=27721
     Region          1..245
                     /region_name="Tango2"
                     /note="Uncharacterized stress-responsive protein, TANGO2
                     (Transport and Golgi organisation 2) family, contains NRDE
                     motif [General function prediction only]; COG3332"
                     /db_xref="CDD:442561"
ORIGIN      
        1 mclivfawrp edneslilaa nrdefyarps apldtwddqp diiggrdlta ggtwlavgrd
       61 grfatvtnir dpsqpvsdrs rgelpvrfle rdisaeeyvh evaqrsdeyt gfnlllgdrq
      121 slwhlnarsr kphrlppgvy gvsnadlntp wpkllraras leqaletpsd ealfalladt
      181 wrpdpvtlph tgisheleml lssvfisseh ygtrastvlr qqvdgqtvit errfgaygks
      241 lgesrrtl
//
LOCUS       WP_010796987             260 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Pseudomonas].
ACCESSION   WP_010796987
VERSION     WP_010796987.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..260
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27186
     Region          1..260
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mefvlylilg acagvlaglf gvgggliivp vlvfsftahg mdtdvlthla vgtslativf
       61 tsinsilahh rqgavqwplm vwmtvgiilg sfvggvtasy iqgpilqkii gtfailvslq
      121 mvldlrpkss rpvpgkpvlt fagvvigwas aifgigggsl tvpfltwrgv smqravatss
      181 acglpialsg alsfmvvgws epglpewslg yvylpalvgi altsmffarf garlahtlsp
      241 rllkrlfall lfsvglsflv
//
LOCUS       WP_010797029             808 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [Pseudomonas].
ACCESSION   WP_010797029
VERSION     WP_010797029.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..808
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=88924
     Region          1..800
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mrllkfiwws clgivcsvfl glsgaflyls pslpsvdalr nvqlqiplri ysadgkliae
       61 fgemrrsplr fseippdfih allsaeddnf anhygvdvks lmravaqlvk tghiqtggst
      121 itmqvaknyf ltsersfsrk fteillalqi erqltkdeil qlyvnkiylg nraygieaaa
      181 qvyygksine ltlaqkamia glpkapsryn pivnperske rrnwilerml klgyidqray
      241 etavaepida yhhvavpela apyvaemara emvgrygsda ytegykvttt idshlqnvan
      301 aavrnglidy dqrhgyrgae ahypnksrse wlnllqshrt vgglepaivt qteksgilvl
      361 tandkeeava wenmkwarpy isansmgpkp napgdvvkvg dlirilrqed gslrfvqvpk
      421 aqsalvsldp qdgaiqalvg gfsfeqsnyn ratqarrqpg ssfkpfiysa aldkgytaas
      481 lvndapivfm dssmdeawrp kndtntflgp irlrealyrs rnlvsirllq aigidyainy
      541 vtrfgfekdl lprnlslalg tpgltpmeia ngwtafangg ykvnsyiisk vesrdgqlly
      601 qanpprvpqn antaaaapen vqvtpasvtn adgtmsqtpa iapqiidprn ayimtsmlqd
      661 vikrgtgrra lelkrgdlag ktgttndskd twfsgynady vttvwvgfdq pdtlgrhefg
      721 gnvalpiwmq ymgsalegkp dhlpaeppgi atlridpvsg raappgtpda yfelfknedt
      781 pppmdelgpg sspgtplpsd esapmdlf
//
LOCUS       WP_010797031             195 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilN domain-containing protein [Pseudomonas].
ACCESSION   WP_010797031
VERSION     WP_010797031.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..195
                     /product="PilN domain-containing protein"
                     /GO_process="GO:0043107 - type IV pilus-dependent motility
                     [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=21724
     Region          1..187
                     /region_name="PilN"
                     /note="Type IV pilus assembly protein PilN [Cell motility,
                     Extracellular structures]; COG3166"
                     /db_xref="CDD:442399"
ORIGIN      
        1 mahinllpwr eqlreerkkr flvviggmfv lsaaiiflgd kyftsaienq darnayiqge
       61 iavldsrike iselktrrqq llermkiiqd lqgnrpvigh vfdqlvrtlp dgvyftglkm
      121 qgdtisivge aesnnrvsnl mrnfensewl aspnltevka ltsgavdqnn afqmtvkqtk
      181 pavptpavpa qggks
//
LOCUS       WP_010797143             479 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cytochrome ubiquinol oxidase subunit I [Pseudomonas].
ACCESSION   WP_010797143
VERSION     WP_010797143.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..479
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53126
     Region          4..441
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mfglealdla riqfaftvsf hiifpalsig masflavleg lwlktndsty kdlyhfwlki
       61 favffgmgvv sglvmayefg tnwsgfvdfa gavtgpllty evltaffiea gflgvmlfgw
      121 nrvgrglhfl stimvaigtl mstfwilssn swmhtpagye ivdgrvvpvh wlevifnpsf
      181 pfrwahmtia aylsvaflvg asaawhllrg nnnpairkmf smamwmalfv apiqafvgda
      241 hglntlehqp akiaaieghw enppgeatpl ilfglpdmer eetrfkveip vlgslilths
      301 fteqipalkd fpkedrppay vvfwsfrimv algllmiaag vwslflrwrh klyetkaflr
      361 limcmgpagl iallagwftt evgrqpwivy gllrtkdgva nhsvtqlsit lvsfvivyfa
      421 vfgigtvyal rmigkgphtg egdlptqggp ghdrhpkrpl satdegteka hshdqltgh
//
LOCUS       WP_010797133             159 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010797133
VERSION     WP_010797133.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..159
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18076
     Region          3..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdkldrydlr ilaelqrdar isnqelaeri glspspcsrr vkqleddgyi nrqvalldrk
       61 klglsltvfv ligmdrhtpe rfehfqsiir qcpevlecsl vtgmdadyql kvvvpdmdhy
      121 qklllgtltr iegvssvrss fvlnqvisst elplehlrg
//
LOCUS       WP_010797207             405 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [Pseudomonas].
ACCESSION   WP_010797207
VERSION     WP_010797207.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..405
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=44150
     Region          9..405
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 madkalkmsa ftwegtdrkg vkikgemtgl npalvkaqlr kqginptrvr kksvsifsrg
       61 kkikpmdial ftrqlatmlg agvpllqsfd iisegfdnpn mrklvddikq dvaagnslss
      121 slrkkpqyfd dlycnlvdag eqsgaletll drvatykekt eqlkkkikka mtypaavvvv
      181 aivvsailli kvvpqfqsvf egfgaelpaf tlmviglset lqewwfivll alfalgfgfq
      241 mahkrsekfr davdrfvlki pvvgailyks aiaryartls ttfaagvplv daldsvsgat
      301 gnvvfrnavd kikqdvstgm qlnfsmrtta vftsmavqmt aigeesgald emldkvaafy
      361 eeevdnmvds ltalmepmim avlgvlvggl iiamylpifq lgsvv
//
LOCUS       WP_010797424             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CinA family protein [Pseudomonas].
ACCESSION   WP_010797424
VERSION     WP_010797424.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..158
                     /product="CinA family protein"
                     /calculated_mol_wt=16135
     Region          3..155
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mtidelsael gkrlsalkaq vvtaesctgg giaeaitrva gssawfeagf vtysnaqkta
       61 qldvpdhlfm evgavsqavv eamvrgaqar sgarfavavs giagpgggsp ekpvgtvwla
      121 wgngsdiyse khffpgdraa vraqtvvaal egllrist
//
LOCUS       WP_010797441             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_010797441
VERSION     WP_010797441.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..248
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26983
     Region          1..239
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 msacislndl tvayerhpav hhvsgcfeag sltaivgpng agkstlikam vgmlrpvggg
       61 vdrkalsasa igylpqaaei drtfpltvld tvamgawrri gifggmsrgq lqqahealia
      121 vglegfghrl igslsagqfq rvlfarlllq dasvilldep fnaidarttr dlldlvrrwh
      181 gegrtviavl hdleqvkqhf pstlllaret iawgdtrtvl tqenlrrarn maedwdeqad
      241 vcderrra
//
LOCUS       WP_010797629             278 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HDOD domain-containing protein [Pseudomonas].
ACCESSION   WP_010797629
VERSION     WP_010797629.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..278
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=30807
     Region          14..226
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mimlaeqvaq elneaiendq lvlptlpeva lrvreaaedp dvtsadmgkl igndtaltar
       61 iikvvnspll risneitdlh tainrlginy tcnlaiglam eqmfqattda vdhkmrevwa
      121 ksteiagisy vlckhftrls pdqaalaglv hqigvlpilt yaeehsslla nsltldrvie
      181 eihpkigkri lkawdfqesi vnvpqdyldf erntpkvdya divqvaylqs lsgtehpltk
      241 mdwtpiasfr klgldpstdi kadedlgeal eqskhflq
//
LOCUS       WP_010797665             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-dependent oxidoreductase [Pseudomonas].
ACCESSION   WP_010797665
VERSION     WP_010797665.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..206
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=23328
     Region          17..205
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 maeprtgatp legdgkrvlv iqgspksesf chalsaayiq garqhnhvvr elrlgelsfd
       61 pvlregydks qileedllea qrlihwaehl lfvypiwwgg lpallsgfie rvflpgfafa
      121 yrdqiwggeq llsgrsadli vtadslptpw krlrglsphr lmmrealdvc giqirehlef
      181 apirasseeq rlrwlqdvqr mgshln
//
LOCUS       WP_010797677             319 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010797677
VERSION     WP_010797677.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..319
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35952
     Region          3..312
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mairigfliw petrpltval aeeafrvarr qqasaeyvle liridqaeqr lthiswpaql
       61 ehfqrvflla devpqslsvp lstalkqcar sgvqvgaisa gvfplaqsgl ldgyraavhw
      121 rwlddfaeqy pkviatnhlf ewdrdrlsac gglaildmvl amlnhdhgad lagvvseelv
      181 veriregner qriplknrlg sshpkltqav mlmeanieep lttdeiaqhv cvsrrqleri
      241 fkqylsrvps qyylelrlnr arkmlmqtsk siiqiglscg fssgphfssa yrnffgvtpr
      301 ddrnqrrgag pdvavvter
//
LOCUS       WP_010797719              61 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Trm112 family protein [Pseudomonas].
ACCESSION   WP_010797719
VERSION     WP_010797719.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   van Tran,N., Muller,L., Ross,R.L., Lestini,R., Letoquart,J.,
            Ulryck,N., Limbach,P.A., de Crecy-Lagard,V., Cianferani,S. and
            Graille,M.
  TITLE     Evolutionary insights into Trm112-methyltransferase holoenzymes
            involved in translation between archaea and eukaryotes
  JOURNAL   Nucleic Acids Res 46 (16), 8483-8499 (2018)
   PUBMED   30010922
REFERENCE   2  (residues 1 to 61)
  AUTHORS   Bourgeois,G., Letoquart,J., van Tran,N. and Graille,M.
  TITLE     Trm112, a Protein Activator of Methyltransferases Modifying Actors
            of the Eukaryotic Translational Apparatus
  JOURNAL   Biomolecules 7 (1), 7 (2017)
   PUBMED   28134793
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006712
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..61
                     /product="Trm112 family protein"
                     /calculated_mol_wt=6593
     Region          1..59
                     /region_name="Trm112"
                     /note="RNA methyltransferase activator Trm112/YbaR
                     [Translation, ribosomal structure and biogenesis];
                     COG2835"
                     /db_xref="CDD:442083"
ORIGIN      
        1 mdlklldila cpitksplkl sedktelisk aaglaypird gipvmlesea rvlsvderld
       61 k
//
LOCUS       WP_010797739             261 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Pseudomonas].
ACCESSION   WP_010797739
VERSION     WP_010797739.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..261
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28810
     Region          3..257
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mklidshchl drldltahng sldaaleaar ergvghflci gvsaenaadv ktvaerypdv
       61 hcsvgihpld vsaekepale wllreldhpr vvaigetgld yhyepesael qkqsfrlhle
      121 agritgkpvi vhtrearadt lallreadlt aagvlhcfte dwemakaald lgfyislsgi
      181 vtfrnaealr evarqvpadr llvetdspyl apipyrgkpn lpqyvrevae flasvrgvel
      241 ealaeqtten fyrlfplaka v
//
LOCUS       WP_010797746             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit beta/FixA
            family protein [Pseudomonas].
ACCESSION   WP_010797746
VERSION     WP_010797746.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26402
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkvlvavkrv vdynvkvrvk pdnsgvdlan vkmsmnpfce iaveeavrlk ekgiateiva
       61 vsvgptaaqe qlrtalalga dravlvetne elsslaiakl lkavvdkeqp qlvimgkqai
      121 dsdnnqtgqm lgaltgfaqg tfaskverdg dvlnvtreid gglqtvalnl paivttdlrl
      181 nepryaslpn imkakkkpld vltpdalgvs tastvktlkv eapagrqagi kvksvaelve
      241 klkneakvi
//
LOCUS       WP_010797767             835 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010797767
VERSION     WP_010797767.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 835)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..835
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90096
     Region          8..835
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mtrppffrll rqasrqlmre vragelrvlf falviavass caigyftarl neamvlrate
       61 flggdlalrg tsaarqeqid aglaqglkha qtiefssvia geqaiqlssv kavsgsyplr
      121 gqlkstltpq gqetvgglpd pgeawvearl lpalelkigd tidvgrktlr isriltyepd
      181 ragdfysltp rvlmnsadlp ateviqpgsr vryrdlwsga tdqleryrat lersldvnqr
      241 iedprdgnrq lgsaldraqr ylglaslaav llagvavams anrfavrrfd asallrclgl
      301 srrealilys vqlamlglaa svlgavlgwl aqfllfhlma gllpatipsa glfpalagmg
      361 tglialagfa lpplaalgrv pplrvlrsdl lpvpprswiv ygtallalgl imwrlsldlr
      421 ltlallgggl aatvvlgglm llglkglrrm lasaplawrl glgqllrhpv aaagqalafg
      481 lillamalia llrgeildrw qdqlpadspn yfalnilpae kdafaaqisq lspnpkplyp
      541 ivqgrlvlin gepasevves esrgdratrr dlsltwadtl psgnvitagr wwdvtpptrd
      601 lpgvsveael akslkvgigd hlsfniagki ieaqvsslrt vdwnnfqpnf fmifqtgtft
      661 nvpvtyltsf yippghdram velarqfpaa tllpidaila qlrsilgqvt iavefvllfv
      721 laagmtvlfa glqstlderi rqgallralg serrllirtr rvefallgat sgllaalgce
      781 iitallyrlv fdmpwqphpw llllpligaa miaaagllgt rraltvsplr ilreg
//
LOCUS       WP_010797773              94 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas].
ACCESSION   WP_010797773
VERSION     WP_010797773.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 94)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..94
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10682
     Region          7..85
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mnesfsidhd lsshqfvihv dgqraylaym dlgkqtmdfy rtfvpdnlrg rgiaaalaeh
       61 altyaesrgy svipscsyve ryierrqqkl taph
//
LOCUS       WP_010797776             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Pseudomonas].
ACCESSION   WP_010797776
VERSION     WP_010797776.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..163
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17809
     Region          1..155
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 miqsilyatd lgiysssvlq halslarahd aklyvvhave plglfadsil qtymdastla
       61 qlnkqgfntv lanieqrvie clrdemgeaa qefdrirlvr vvqgdpaqvi ldqshdlavd
      121 livlgshshg sawdtplgrt agkvlqmadv pvylvpmlqh rsh
//
LOCUS       WP_010796482             347 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfotransferase family protein, partial [Pseudomonas sp. HPB0071].
ACCESSION   WP_010796482
VERSION     WP_010796482.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HPB0071
  ORGANISM  Pseudomonas sp. HPB0071
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Begolli,G., Markovic,I., Knezevic,J. and Debeljak,Z.
  TITLE     Carbohydrate sulfotransferases: a review of emerging diagnostic and
            prognostic applications
  JOURNAL   Biochem Med (Zagreb) 33 (3), 030503 (2023)
   PUBMED   37545696
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Pseudomonas sp. HPB0071"
                     /db_xref="taxon:1203578"
     Protein         1..>347
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
     Region          26..254
                     /region_name="Sulfotransfer_2"
                     /note="Sulfotransferase family; pfam03567"
                     /db_xref="CDD:427369"
ORIGIN      
        1 mskqnnlsif ndknlteylk wnsylsekhk llyiatpkaa ctslkwwfat legyskklne
       61 kiessesdpe lsihdtfykv apnvtglsaq dlsepllsds yfrfavvrnp ykrifsawqs
      121 klllreplqi spylkydffy rpikelndis iafeeflehl inneapsywd yhwtpqadll
      181 rpdlinyskl vriedreeln kalikrlgey apspfsgrrt neslipylpe iitdraseli
      241 cklyakdfdi fgydthppka sekfseeqfd ltlkaiklir grhqklaern dqivhlrevv
      301 nfkteeaikl sqavvardgq itelsqavid rdskvaelsq avvardg
//
LOCUS       WP_010797779             320 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010797779
VERSION     WP_010797779.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..320
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35423
     Region          15..73
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          103..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(117..118,120..121,124,128,130..136,231..236,
                     242..243,245..246)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mipslnsiss rlrvrqlkll ialeehgslh kaaeqvaitq pgatkalhei eatlgatlft
       61 rtsqglvpnd lgrcvtryar liqsdiahlr eemigilhgq ggrlsigvim gavpllmqsl
      121 nrlrqkqpel sihiaedtsa rllalldqgr vdvvicrtsv strpdayekl iehpeslalv
      181 ahpnhplana slssldeltg yrwvvypsnm pmrlaleqqf rlagldfpry pietastftm
      241 lsllqedphl lavmpsdval fserfgllkr fsidlqinse pysvvirqgm dvtapakmli
      301 eelrqdmglt vqphrqeita
//
LOCUS       WP_010797829             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MOSC domain-containing protein [Pseudomonas].
ACCESSION   WP_010797829
VERSION     WP_010797829.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..268
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29758
     Region          1..268
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mfhlsglyry pvkstapepl eradidclgv agdrrwmvve astgrfltqr llpsmgqiva
       61 rwisngclsl dapgmstlei svplpdealq gvtlwrdtfq vpeageeana wlstfldrpc
      121 rlvympesra rqvdtayasp gdyvnfadgf pllligqasl ddlaqrvgrp ldmrrfrpnl
      181 vvegskayae dkwthirige vefrivkpcs rcvlitvdpv tsvrshdrep latlktyreh
      241 egavyfgqnl iqlnpgavni gmpvevla
//
LOCUS       WP_010797708             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycerophosphodiester phosphodiesterase
            [Pseudomonas].
ACCESSION   WP_010797708
VERSION     WP_010797708.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..247
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27667
     Region          1..238
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mtviyghrga kgeapentla sfeqclqvgv trceldlhls sdgelmvihd ptlkrttgrr
       61 gkvaelpadt lvtydarlag pswprpcpip rledlfkqvd fehwqlevks asrvraarti
      121 kaidelakrf nlsdritits ssrevlraln rdtpwlqrgl vaeyawldpl kvaanygchl
      181 lalnwtlctp erllkaqrqg lhvsvwtvne pslmrrlidf gadslitdyp alartvlddh
      241 kpqakpa
//
LOCUS       WP_010797973            1623 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD-glutamate dehydrogenase [Pseudomonas].
ACCESSION   WP_010797973
VERSION     WP_010797973.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 1623)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1623
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..1623
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=182907
     Region          5..1613
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mafftaaska dfqhqlhlal aqhvdeptls rltpfadqff givaleeltq rrlsdlvgcv
       61 lsawrllerf npvqpqvnvf npeyerhgwq sahtavevlh adipflvdsv rmqinrsghs
      121 vhtlqnsvls vrrdetgrll evlpkgtqge gvsqesvifl eidrcasasd mkalesalle
      181 vlgevrlavn dfnpmkqrva hlldqldtma gpnvaaeeld evktflawln dnhftflgye
      241 eftvenegeg grifydessl lglsrqlrig ltaedahiqt eslqyfrepl llsfakaalp
      301 srvhrpaypd fvsirqcdeq ghvirehrfm glytsnvynq sveaipfirr kaaevrrrad
      361 fgasahlgke laqvlealpr ddlfqtpvdd lfatamsivq iqernkvrvf lrrdpygrfy
      421 yclayvprdi ystevrqrmq qilmerlhgt dcefwtyfse svlarvqfil ridpgqkpei
      481 dpsriekemv qacrswkddy asliidtlge aqgtavladf pqgfpagyre rfaphlavvd
      541 mrhllnlses rplimsfyqp lgysggdnvl hcklyhadtp lalsdvlpil enlglrvlge
      601 fpyhlrkkdg reywihdfaf ttvaglhvdl qqlndtfqda fihivngsae ndsfnrlvlt
      661 aglpwrdval lrayarylkq irigfdvgyi astlnnhvdi areltrlfrm rfylarrmsp
      721 edledkqqrl eqailaaldn vavlnedril rryldlikat lrtnfyqpde ngqpkgyfsf
      781 kfnpraipel pkpvprfeif vysprvegvh lrggkvargg lrwsdreedy rtevlglvka
      841 qqvknsvivp vgakggfvpr rlpvggsrde ilaeaiacyr ifisglldit dnlkegeivp
      901 pvgvvrqddd dpylvvaadk gtatfsdian giaaeygfwl gdafasggsa gydhkkmgit
      961 srgawvsvqr hfrergidvq kdpvtvlgig dmagdvfgng llrseslelv aafnhlhifi
     1021 dpnpdaarsf aerqrlfdlp rsswtdydas lisegggifs rsakrieisp qmkerfdiqa
     1081 dqltpnelih allkapvdli wnggigtyvk asfeshadig dkandalrvn gnelrakvvg
     1141 eggnlgmsql arveygltgg acntdfidna ggvdcsdhev nikillgdvv ssgdmtlkqr
     1201 nqlmgemtde vgelvvnnny mqtqalslae rrarthlmey krlivdlegr gkldralefl
     1261 psddvlaera sqgigltrae lsvlisyski dlkeqllkss vpddeylsrd mhtafpqrlt
     1321 eefgeamqrh rlkreivstq iandlinhmg itfiqrlkes tamsaaditr ayvvmrdvlh
     1381 lphwwrqiea ldykvpadvq lslmdelmrl grratrwflr srrgeldaar dvahfgprva
     1441 algvrlnell egeprsqweg ryqhyidqgt pellarvvag tthiytllpi iqaadvtghd
     1501 piqvastwfa vgnaldltwy qqqlnelpve nawqalarea frdeldaqqr iitiavlqmp
     1561 eapednaarl alwmehnrtm verwrgmlsd vraasgkdfa myavaarelm dlaslgsats
     1621 stm
//
LOCUS       WP_010798008             295 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [Pseudomonas].
ACCESSION   WP_010798008
VERSION     WP_010798008.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..295
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31853
     Region          2..292
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mlselfavma pvligagigy fwkrwgyeyp tdfisrlvfn vaspclvlat lghahidkhs
       61 fgqmalacvi icaimglaay glarvfkrdw kvlapafmfp nvgnmglpvc lyafgeqgmt
      121 lavafylvls ignfslgifw msgerslkml lgnpimisva ialslmmlda qlprwiantv
      181 dlmsglaipl mlitlgvsla sirpqhlgsg flfggirlcl galvgwlvgw alhlpplaha
      241 vlvtqssmpv avfnylyalr anrspqevas lvlcstilaf gflplmlaww lpatg
//
LOCUS       WP_010798024             248 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Pseudomonas].
ACCESSION   WP_010798024
VERSION     WP_010798024.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..248
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25754
     Region          31..248
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mdvtaivldi llgsvlgvvg glfgigggli aipvlgllfg ldqqlaqgta lvmvvpnvlv
       61 siikynqrnr idwrragils gagilsaiag amlavgldad lmrkgfvvfl lflvaynlwq
      121 lrmkshtvtn ppgvawlavl gvfaglvggl fgvggaviat pmltsvfgls qvvaqglslt
      181 malpatsitl atyaihhevd wligmplaig gffsvgwgvr mahalperll rglfcgfllv
      241 caillalk
//
LOCUS       WP_010798048             213 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: precorrin-8X methylmutase [Pseudomonas].
ACCESSION   WP_010798048
VERSION     WP_010798048.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..213
                     /product="precorrin-8X methylmutase"
                     /calculated_mol_wt=22993
     Region          4..194
                     /region_name="CobH"
                     /note="Precorrin-8X methylmutase CbiC/CobH [Coenzyme
                     transport and metabolism]; COG2082"
                     /db_xref="CDD:441685"
ORIGIN      
        1 mpfdyqrdpe aierqsfeqi rtltdlsrfd pdqaqiamrl vhtcgepeiv ealhfspham
       61 eaglaaveaq asilcdvemv rhgltrrlfg erplcflnde rvpalakatg etrsmaalsl
      121 wepylpgsiv vignaptalf rllehletgg srpalvigmp vgfigaaesk dalmahgqal
      181 giewialsgr rggsalaaat lnalarvqqg irw
//
LOCUS       WP_010798072              69 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Pseudomonas].
ACCESSION   WP_010798072
VERSION     WP_010798072.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..69
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7475
     Region          4..69
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mstrqtgtvk wfndekgfgf itpqsgpdvf vhyraiqstg fkslkegqav sflvvqgqkg
       61 lqadevqvv
//
LOCUS       WP_010798087             246 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PIG-L deacetylase family protein [Pseudomonas].
ACCESSION   WP_010798087
VERSION     WP_010798087.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..246
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27169
     Region          42..217
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mttlntrtle eksasaqewa awprfagipe vdanhlvppg rraviiaphs ddeilgcggl
       61 laqlaelgrk vllvsvtrge ykqglgsqpv fhvptlpesr easrrlcles vdicrldfsd
      121 giasneeqrl seqlaaliks tdtvftawre dghadheatg raasfacvvt garcievplw
      181 awqwlrpgdd rfpwerarrl pldesslaak ryaveafnta ngpapepilp shvlsrlfrp
      241 weiflv
//
LOCUS       WP_010798140             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TerC family protein [Pseudomonas].
ACCESSION   WP_010798140
VERSION     WP_010798140.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..231
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24261
     Region          13..188
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mtdlmnnpdl wlavgqiili dillggdnav vialacrklp eaqrnkailg galgaillri
       61 vliffalell tlpylkliga lllawigvkl mlpegedeha dlkaspkllg aiwtiivada
      121 lmsldnvvav agashgqlel vifgivvsip iiiwgsklvl rlmerfpiii klgaallgwi
      181 aggmavadts lpalpswahy aagvtgaliv vaigtllgry qqhralrsgg a
//
LOCUS       WP_010798147             324 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Pseudomonas].
ACCESSION   WP_010798147
VERSION     WP_010798147.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..324
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35928
     Region          1..273
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mdvvrwgmig cgdvterksg pafykapgsa lvavmgrrae avtdyaarhg iariytnaqa
       61 liddpdvdav yiatppdshh aysmqvatag khccvekpma lsstqseemq qafdkvgrhl
      121 fvsyyrrslp rfqrirewlt qghigevrql twslikppsq kdleqqanwr tdpavagggy
      181 fadlashgld lfqyllgdiv avsgftarqa glyaaedavv aswrfssgal gmgcwnfvad
      241 rhedrveiig srgrilfsvf gdepvrldae etvseyiqhp ehiqwyhvlg mnahirgerd
      301 yaalareavk tdrvmdqilg raka
//
LOCUS       WP_010798157             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [Pseudomonas].
ACCESSION   WP_010798157
VERSION     WP_010798157.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..245
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25861
     Region          5..242
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mkglegkvia itgassgige atarylaaqg gfvilgarrt erletlvaei raqggkadyr
       61 rldvtaledm esfvqfaqqq ggrldvlvnn agvmplskle alkvdewnrm idvnirgvlh
      121 giaaglpvmq qqrsgqfinl ssigghavsp taavycatkf avraiseglr qevgadirvt
      181 vispgvtese ladtitdpta qaamdafrrg aispesiara iafaieqpae vdvseiivrp
      241 taspy
//
LOCUS       WP_010798199             318 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010798199
VERSION     WP_010798199.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..318
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34990
     Region          2..309
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrvgymlsn gfqilslatq tvfeyanvva gepfyevenf sleggevrss lgltvgsral
       61 gpdsqadtwi vagvnnplag pspdavlgfi qdastqarrm taictggfvl aeagllagrr
      121 atthwayare lqrrypeirv eedriyitdg pmwtsagmta gldltlaive kdlgnevars
      181 vahklvmhqr raggqsqhse mlnlapksdr iqnalnyarq hlsrplsvee laesvhlspr
      241 qfsrvftaet gqspakaies lrleaarlmi eqsrhsldvi aketgfrdrr hmreafirgf
      301 gmppqairrg namteeml
//
LOCUS       WP_010798225             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: O-methyltransferase [Pseudomonas].
ACCESSION   WP_010798225
VERSION     WP_010798225.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..204
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22236
     Region          44..201
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mdekintvle tyharihkeq saprelppgg rdggqdqrmr avgpqtgqli nilaksletp
       61 tileigtsfg ysgiwlgeaa ratggqlitl elheykslya remaekagla dyidfqvgda
      121 vqliealpgr vdfvlldlwk dlyvpcleaf ypklnpgaii vadnmirpgn ddvkrygrai
      181 rakagitsvl lpvgtglevs rfea
//
LOCUS       WP_010798257             457 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010798257
VERSION     WP_010798257.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..457
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48918
     Region          19..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(32..33,36..37,40,79,137..138,140..142,145,165,
                     168..169,172,254,257..258,261..263,266,294,298,351..352,
                     356,360,376,379..380,383..384,387)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mttgtpspra tssgrkhyri aglasmagtt iewydfflyg taaalvfnkl ffpaldpmsg
       61 vlaafatyav gflgrpmggi vfghfgdrig rksmllltlm lmgvptiaig liptydqigy
      121 waalllvvmr flqgmavgge wggavlmave hapegkkgfy gslpqtgvga glvlaslamg
      181 avatlpeedm lawgwrlpfl asvvllgigw lirvkvaesp dferlkqegr kvkvplftvl
      241 kehpretlai igartaenaw fymavtfala yaanqlqipr asvlnaitag aalslvtmpf
      301 cgylsdrvgq rrlyftglll lcafvypffa mlgtrepllv wwamvlavgv vfpilyapes
      361 llfarqypaq irysgislsv qfagvlgggf apmiattlls lgegnpryvi vyllvmgaia
      421 llctalmkpd pqvgrsaist tasrpvgmvn stsgesl
//
LOCUS       WP_010798258             508 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [Pseudomonas].
ACCESSION   WP_010798258
VERSION     WP_010798258.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..508
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54233
     Region          15..491
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(72,74,78,81,85,118,121..122,131..138,143,146,149,
                     242,246,249,252,254,427,429..430,432..433,436,439..440,
                     442,444..447,456,460,462,476,483..488,490..491)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(158..161,169,184,187,217,234..237,240,258..260,292,
                     392,394,420)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(161,258,289,292)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnaplndaka disqvkllin gewvdskthe wrdivnpatq qvlarvpfat tdevnaaiaa
       61 aqqaftrwkr tpigarmrim lkyqalireh mkpiaqtlsa eqgktvadae gdifrglevv
      121 ehacsvgslq mgefaenvag evdtytlrqp igvcagitpf nfpamiplwm fpmaivcgnt
      181 fvlkpseqdp lstmqlvela leagippgvl nvvhggkdvv dalcthpdik avsfvgstav
      241 gthvynlagq hgkrvqammg aknhavvlpd ankeqtlnal vgaafgaagq rcmatsvavl
      301 vgkarewlpe lkakaeqlkv nagsepgtdv gpliskqare rvlgliesgv aegasllldg
      361 rnvqvpgyeq gnfvgptlfs gvttdmriyt eeifgpvllt levdtlddai alvnrnpfgn
      421 gtglftqsga aarkfqseid vgqvginipi pvpvpffsft gsrgsklgdl gpygkqvvqf
      481 ytqtktvtar wfdddsvsdg vnttitlr
//
LOCUS       WP_010798326             129 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RidA family protein [Pseudomonas].
ACCESSION   WP_010798326
VERSION     WP_010798326.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..129
                     /product="RidA family protein"
                     /calculated_mol_wt=14056
     Region          20..127
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msikrygveg gsgtggqhlp faraveadgw lyvsgqtpmv ngevveggiv tqtrqcldnv
       61 mailkeagyg pehvvrcgvw lddprdfmsf nrifkeyfge hpparacvvs smvidckvev
      121 dcvaykkpe
//
LOCUS       WP_010798350             805 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudomonas].
ACCESSION   WP_010798350
VERSION     WP_010798350.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13372683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..805
                     /product="chemotaxis protein CheA"
                     /calculated_mol_wt=88389
     Region          1..>149
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          <371..805
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mnallqqfiq esrealesig stllamerep gdtaplgelf rlvhtlkgns glfdfpalts
       61 vlhaaedvmd avrngeldfn qqladqllnt adyvseflde ieqngqpgdg fqvpprelvd
      121 glrawltsse tavvaadakn gtsesespaw atelndevrq hiadrlkdeq cvyrveyrpa
      181 adcffqgtdp lhlvrqlpdi fwrrvtavep wavasqlday hcnlriefll aireedlaeh
      241 fryvsdqvsw eavtaalfaa papaeeaqqs lshgneaidp lvrdvvgtqq ialaaclsqp
      301 wrsgqhaaiv rtltnvlmay palnetlqrs vmdadqqrsa tpimawfqah wqagadsise
      361 askeeegrth eamsawlsaq ldpaapvvpv veaarapsda sagrrqeeag nhvtskvlki
      421 eqekidrlmn ligeivvakn glpylaerae dqygqrelar eikaqyavvn riaedlqdai
      481 mqvrmmpvsf vlqrfprlvr diarklgkkv nlilegedte adksmieala dplvhivrns
      541 mdhglelpee rtnagkpetg tlrirasqna dhvviviedd grgidpqkik akvagkglve
      601 qtaldamsdq elvnlvflpg fstaeqisdl sgrgvgmdvv rsgiekvggq lrltsqvgkg
      661 tqlsltlpls mavtqvmvie sggqrfgipm dqvmetvrlp kdsihtikhq ptaqlrgrti
      721 plkslnqmla vseeqvlned deyalmvlrs rgelvgliid dfhgsidiil kpmvgilgel
      781 sgysgtavmg dgsilmilnp telfe
//
LOCUS       WP_010798328             286 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_010798328
VERSION     WP_010798328.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..286
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31198
     Region          1..277
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdilyqirar lehmsageqr iarliledvp faasasldel atraevssat lsrfarsagc
       61 kdlrdlrlql aqasgvgarf lgrthapehs affgnivsdi eatlrqhlar fdeqtfarav
      121 alvhearmvy afgmggcsti fsdelqyrlv rlgypiaayh dpvlmrltaa tlgqdqvvia
      181 csmtgitpel veslqlakgy garilaiape tslvaqladv vlplflaetd fiykptaary
      241 gmmlavdila telalsapea nqerlrrikl amddyrggde rlplgd
//
LOCUS       WP_010798345             386 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methionine ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_010798345
VERSION     WP_010798345.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..386
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42562
     Region          41..381
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtgsitsirq arstheaead qpshalpypl tstaleraet hirfqdmgkt yngeqgpvra
       61 lhgidlavrr geifgiigrs gagkssllrt inrleqpseg qvlidgedig rygtselval
      121 rrrigmifqh fnllsaktvr qnvelplkva gvprqerqqk vasllklvgl enkhdaypaq
      181 lsggqkqrvg iaralvhdpd illcdeatsa ldpettqail sllrdinrsl gltivlithe
      241 mevireicdr vvvlecgevv eqgpvwrvfg dphhdvtril lsplqqtlsd dlkarlqtqp
      301 lrqndallle lrlsgsssre pdlgslfnal ggqltlirss iqrlqgrtvg hllvsirrsp
      361 haqeelikra rhifddvevl gyvaad
//
LOCUS       WP_010798347             403 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Pseudomonas].
ACCESSION   WP_010798347
VERSION     WP_010798347.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..403
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=44030
     Region          <136..344
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnnqaylkag lllaivalgl sspvwsawla qqstvacmgv avffsiplll mtwrlsqnsa
       61 hvperieegs tyavlfdktv atanavpgls rivqrnlkev sdeternvlc aierlnnihl
      121 tgqklsetvs egcgcaqtls readehqqrn ektlatlsaf ekerkeslss diermrrlye
      181 evnatgplia lisdiakqtn llalnaaiea aragdsgrgf avvatevrnl sartaeaahs
      241 isttiqnlas rfeeestaaq nrqedflars glehvgnelr smvrylqeaa ecmtsvvsgv
      301 kglssevnnd lqgvlsclqf qdplrqrleq sshmldtlsd vmeaygvgla spetcqpgel
      361 pdldarmqkh lnsyvthsqh kghleeigrg hevqseglki elf
//
LOCUS       WP_010798353             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HEAT repeat domain-containing protein [Pseudomonas].
ACCESSION   WP_010798353
VERSION     WP_010798353.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..207
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=22297
     Region          64..202
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mplvrntlad qagddqpsgf eqlldtldsp dtaarrlaar aiarfpnass alidrleeea
       61 epsvreaiit slaaiadvss vtalldclrs edaalrndai ealktagvqh pgliqnalqd
      121 ydadvrilai gileslkhpd velwlidlle hdphlnvcac avdllceigs eravpaleac
      181 lerfpdeayl rfavdlaiqr lrgesal
//
LOCUS       WP_010798355             514 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheW [Pseudomonas].
ACCESSION   WP_010798355
VERSION     WP_010798355.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..514
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56922
     Region          20..164
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
     Region          190..342
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
     Region          362..511
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mtqttaneal vvrgeggddd elaqghqfvt ftvgeevfav emlpvqeiir vpevirvplt
       61 ppalnglanl rgnvlpiicl rtlfnmeard addstraivl nlgqplgfvv drvasvimve
      121 ddqiepvshv qstintrllt gllkqvgghe lvmildfqal irdsfsensl lqrtvmassm
      181 svlpdtaded edsdelqlvs ftvdsqeygi aiedvqeivq vpehivsvpk tashvrgvmt
      241 lrqrllplvs lremfhlpsq etdersrilv vslagvsvgi ildsvnevlr vpgsqvepmp
      301 pmlardqnma eltglcrlqn gkrlvsvvsa erlfqhqsvq rvlntndkep svdeelldqi
      361 dnddeeqlvv frlgneefgv pidsvqeivr vpenlthvpk apsfvegvmn lrgvvlpvid
      421 qrrrfglpsi enndrqrimv fvindlrtgf ivdsvaevlk isrnliepap alsseqqrlf
      481 grvanlpkqk rmiqlveprq llgeqelsal ssva
//
LOCUS       WP_010798392             344 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TerC family protein [Pseudomonas].
ACCESSION   WP_010798392
VERSION     WP_010798392.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..344
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=38396
     Region          17..323
                     /region_name="R_switched_Alx"
                     /note="integral membrane protein, TerC family; TIGR03718"
                     /db_xref="CDD:274743"
ORIGIN      
        1 mpdafdfltt pfmgaaawlw lsfliivlll lifdlgvlqr nhheigikes llmsagyisf
       61 giafggwiwy efgatraley ytgylveqsl smdnvfvmal ifsffqiprk yqhevlfwgv
      121 lgaivmraim igvgaalvqr fdwilyvfga fllisgikml fsrhddqpdl aqnpmlrflr
      181 khirvtdqlh gdrflirkek egfskplvya tplllalili emadlvfavd svpaifsitq
      241 epfivytsni cailglraly falaamisrf aylkyalalv lifigakifa hsligpvpap
      301 lslgvtfsll aggivlslfk trghaehlkt gtsknnsgsw gdhk
//
LOCUS       WP_010798519              85 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Pseudomonas].
ACCESSION   WP_010798519
VERSION     WP_010798519.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..85
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9246
     Region          <25..79
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mndkdilnal tqvfsdvfdd ddivlapdmt adnidgwdsq thvilivaae qrfgikfrta
       61 eleslknvgh faqliqskle gaavs
//
LOCUS       WP_010798444             367 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas].
ACCESSION   WP_010798444
VERSION     WP_010798444.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..367
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39800
     Region          1..366
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maalelknvr ktygnaaqea lkginisiet gqflilvgps gcgkstlmna iagledissg
       61 aimlggedvt avepkdrdia mvfqsyalyp tmtvreniaf glkirktpan qiaaevdrva
      121 kllqiehlle rkpsqlsggq qqrvamgral arrpklylfd eplsnldakl rvemrteikl
      181 mhqrlktttv yvthdqieam tlgdrvavmk egevqqfgtp qeiynnpanl fvasfigspp
      241 mnfipvaleq engrpvarlq ghgertaigl pmlqtaladg reailgvrpe qicirsgqig
      301 dlplvsarvq vveptgpdtl vyvevngvqv ccrvapvdtp eigsivtlel dverlvlfep
      361 asgaria
//
LOCUS       WP_010798525             284 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010798525
VERSION     WP_010798525.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13673967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..284
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32354
     Region          18..153
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          <164..274
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtddrkswvh lnqdaetgie tirahfegha ydphwhdsyl vgfteqgvqq fscrnalhvs
       61 tpgkvfmlep geihdghapa eggftysmly lepqwierel rmlhedapvq clpsfgatlt
      121 dqtelmiaia dafkaleyne lrivrqtald qllikltdhv kwrmrgaydp rlplvayrvr
      181 dylhahmqdd vgldelantv gvdrfrltra fkaafglaph ayliqlrlak arfmlakgdq
      241 paevamrlgf adqshmgrwf rraygltpas yrkrcsnlpd asrs
//
LOCUS       WP_010798541             133 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Pseudomonas].
ACCESSION   WP_010798541
VERSION     WP_010798541.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..133
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13779
     Region          18..>108
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mdtrtasyaa lllrlalgim flahgltklf vftlpgtaqf fesvgfpgvl aypvtvfeil
       61 agamltlgil prwvaavaav qllaassvhf gngwsftaad ggweypvfla vtaaalallg
      121 pgalalkpsl rkd
//
LOCUS       WP_010798573             303 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010798573
VERSION     WP_010798573.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33684
     Region          9..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,147,161,163,225,242,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,190,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mslaqlwelq afcavvdrhs fvsaarllgr spstvtraiq sleaqlghel lqrsqkqvrl
       61 teageayygy arqmlslqae aeeslsvqgt laqgwircsa peslmmdflp svmaefgrrn
      121 pqisidiqvs daahdpiadk ldfairggfa ypseligapl wsyrrhlyas ptylairgvp
      181 eapealvehd llmhtspril kdwyfrqgda qvrykaqpry rlssgvalyn aavqglgicr
      241 ladwlaepav qagrlvrvcs hyrltsstgh dpqihavyas tqlpqrvraf leaiksaark
      301 rya
//
LOCUS       WP_010798597             383 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dienelactone hydrolase family protein [Pseudomonas].
ACCESSION   WP_010798597
VERSION     WP_010798597.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..383
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42294
     Region          98..364
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mnilkslvlc gislaatana qaqsasapit adalpgnyll lkqkmtypds wlsghykhfs
       61 kwrtyaqtll realltpdsk rafnaqvidq qqrsgysaqk irftltdesr vnallllpdt
      121 pgphpavlml hdhgarfdig kekmvkpwgd qtvsasaqqw adkyfsgrfp gdelakrgyv
      181 vlsvdalgwg ergpvtyeqq qalasnffnl grslagtmay edmrsvdfla tlpmvdarri
      241 gvvgfsmgaf rawqlaalsd kvaataaisw fgtyqglmtp gnntlrgqss yymlhpgipa
      301 rldipdvagi aaprplllfn ggkdtlfsse sveaayakvh riwrsqqael nlttqlwpel
      361 ghvfvqeqqe aafvwldqwl kpr
//
LOCUS       WP_010798644             125 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Pseudomonas].
ACCESSION   WP_010798644
VERSION     WP_010798644.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163535
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..125
                     /product="VOC family protein"
                     /calculated_mol_wt=13708
     Region          3..125
                     /region_name="GLOD5"
                     /note="Human glyoxalase domain-containing protein 5 and
                     similar proteins; cd07253"
                     /db_xref="CDD:319916"
     Site            order(3..10,27..28,43..47,65..76,81..82,85,94,101..104,
                     113,116..117,119,121,125)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319916"
ORIGIN      
        1 mqidridhlv ltvcnlertc dfytrvlgmd vitfgegrka lafgeqkfnl yeagkelepk
       61 aerpapgavd iclitrmpie dvvthlhstg vtvidgpvrr tgatgaivsv yfrdpdgnli
      121 kvsny
//
LOCUS       WP_010798631             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Pseudomonas].
ACCESSION   WP_010798631
VERSION     WP_010798631.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..206
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22303
     Region          4..206
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpiidnvvaf tlaatlltlt pgldtalvlr taavegraqa iraalginag cliwgtavaf
       61 glgaliavse laydvlkycg aaylcwlgln mmvrprnsmv addttrvqnt nwflkgmlgn
      121 vlnpkvgify vsflpqfipq ghslilwtfg lvsihvvigf iwsmaligat rplaqilrre
      181 kviqwmdrlt ggvfllfaar lalskr
//
LOCUS       WP_010798690             285 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas].
ACCESSION   WP_010798690
VERSION     WP_010798690.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..285
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30795
     Region          10..118
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          158..276
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 msiaevpirf rpmvtedlih ahelsravgw phrlqdwqwi hhvsqgivae dahgilgtal
       61 cclqgdyvsl glvivdvrrq gqglgrklvd qvlnhtsprt pllvatpqga plyssqgfit
      121 yehihqhqta sapalphhel pvghtlheit sqhfpqliel assatgmnrg lvlaallkis
      181 qyvigierdr qqvgfallrp fgrglaigpv vaesaeqakv livallsrva gqfvrldvth
      241 ssglsnwltd igipqtdkva qmvkgsppip lgnalqmala nqalc
//
LOCUS       WP_010798713             260 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Pseudomonas].
ACCESSION   WP_010798713
VERSION     WP_010798713.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..260
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27205
     Region          8..260
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mdfgaggfvv aglvvgfivg mtgvgggslm tpillwfgin paaavgtdll yaavtkaggv
       61 wvhqrnknid wsvtgwlalg slpaaaltlw llsrlhsdpq alnaiikhgl givlfmtafa
      121 ilfkkqlfaf vgrhandsfh lspkklntlt fitgvvlgam vtltsigaga lgtvalfmly
      181 pflatrrlvg teiahavplt liaglghasm gnmdwpilgy llmgslpgif mgshlsgrip
      241 dgilrpclav mlmvigykll
//
LOCUS       WP_010798700             941 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010798700
VERSION     WP_010798700.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 941)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 941)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..941
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=102063
     Region          <8..99
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 mampidnagt srsnfrtalh sfsafikrsq etprpegdap rlpeshlqqq kvvvepgdtm
       61 tgiakkhyvs lheaaqhnpq isdidhihag dvvflpppap eqlavqpdgk tlflenlqsr
      121 gnaiehanta dgaidyavet eqlnqdvqtf lsalpaaern dsaqwlfdhd wtdsgpaqia
      181 ieqgaeqmgl vltpsshkgp dveaqvreiv qqinaspnpv aaletlgkay stvtpdvkev
      241 llqsstgqei fqsagqyald alnqqdnqsg qlvpmktvfe rldnmtqnld phlaakvvea
      301 aipglekvli epsdnpvppm vgssgayhlv nvtgriagqp gaeetikrlv elglyertgt
      361 vqsiaeganp ayplqvlsfv gqgdiryvle gdilpgldqf qkkvtddlqa ygkqmeelnw
      421 ltlnggavmt teqrdnaiqd yldsrppewe eqtqalkdqv aedgrdllyq lqalqnlpad
      481 fkgdrkaied qirrtldnpd aitamssava qypeltndld qwkligqfgk ttdrgrkfle
      541 evatqvlrhk vmpefqnvka gdaaslqsal nkleglkkgp vadlfgipdk dlnkaidalk
      601 ealprpgeta eqitdrlarf nlklddikst ngvrtfdnqt ragqtlrmig aagaaavlas
      661 sgvalhkhqs peailkvcld aagtaqktte lligmgkipk dgwvntlagg ssrpavkvlg
      721 vasslldlvn agkaaesgdt vgaslytlsa aggvtsalgt gtvfgpiglg vvllstitlg
      781 trdvikhhem anrfqtpets qflthaglde aaakalsdqs gdgynvlpll sryaelkgld
      841 lqdnqdqqaf vtwinnmpne sllllrdnlh rvldrrkgsy ddfpesqsqs nswiydtsdt
      901 yfsqrlkenp hfvemgvayp nsvyqldqtl dmldldrlav s
//
LOCUS       WP_010798729             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_010798729
VERSION     WP_010798729.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 219)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 219)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..219
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23014
     Region          12..215
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mdfvtsfnhi dwmevlhltq qhitlvaiav glavlvgvpl gvlmarfpwl agplqgiatv
       61 vltipaialf glllpvystf gqglgplpai tavflysllp ilrntylals svepgireag
      121 tgigmtfwqr lrmvdlpiav pvilagirta vvmnigvmti aatigagglg vliltsisrs
      181 dmatlivgav lvsllaiaad lflqwlqrrl tprglcasv
//
LOCUS       WP_010798776             444 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TrkH family potassium uptake protein [Pseudomonas].
ACCESSION   WP_010798776
VERSION     WP_010798776.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..444
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47148
     Region          9..439
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mlrntikhpa rlvplaflit iligtsllml pvarageasa pfltalftav satcvtglvt
       61 vdtatywsgf gqviilvlfq iggigimsga tllgllvnrr lqlssrllaq setrllglgd
      121 vvevlrlvla vtltveltia allafhlhfa yqeawgsaaw ngifhaisaf nnagfstysd
      181 nlmgfvadpi vilpitaali iggigspvly elrhirrknr pwsvhtritl lgsallliig
      241 tvamlgyewn nagtlgpldt gakllaaffh saaartagfn sldvgqftte tlaihyilmf
      301 igggsagtag gikvttffll ffvvwaeirg ntdtavfnrr iasetqrqal vvvllgtamv
      361 asatlilisv tsfplekiaf etisafatvg lstgitadlp pigqvviivl mfvgrvgtit
      421 vatalalrsr nkpyrypeer pivg
//
LOCUS       WP_010798791             625 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sigma-54-dependent Fis family transcriptional
            regulator [Pseudomonas].
ACCESSION   WP_010798791
VERSION     WP_010798791.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..625
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=68676
     Region          18..621
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 msqrphtsip pfskappslp sgstdpvvvr swqrclehyq ldpaspqapc vieqprlvdh
       61 replcnllgl argqmntlyq qlggaghtil ltdaqgvvie svfheaeqvl leraglwlga
      121 vwnediegtn gvgtclverq pitifreehf rsrhtgltcs ampvfdpagn lqavlnvstv
      181 reqqsrqsqf htmalttlsa kliengfflq hckqdyllrf htqpeflgll segllafdgg
      241 gritavnepa lnllasrrea llgqslegvl dirldellay aqpqpstyws ictlggvllh
      301 aqvrgiqlrt vvtpppvrra kieglcladh alhaafdral kvlehdvpvl lygetgtgke
      361 afatalhras sragkpfial ncaaipeali eselfgycgg tftgarkegm agklqhangg
      421 vlfldeigdm plalqtrllr vleerhvvpl gstvpqpldi rlisashrdl kalvaagqfr
      481 edlyyrltgl qvtltplrer sdkaelidhl lreeargkei rvesaarqal laqpwpgnir
      541 qlrnllrtlv alsegcwigl rdvaavlple tpaenacnpl gtaerdalva alqaehwhrg
      601 hvaerlgisr ntlyrklrkh glinr
//
LOCUS       WP_010798830             341 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: WD40 repeat domain-containing protein [Pseudomonas].
ACCESSION   WP_010798830
VERSION     WP_010798830.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Jain,B.P. and Pandey,S.
  TITLE     WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions
  JOURNAL   Protein J 37 (5), 391-406 (2018)
   PUBMED   30069656
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Schapira,M., Tyers,M., Torrent,M. and Arrowsmith,C.H.
  TITLE     WD40 repeat domain proteins: a novel target class?
  JOURNAL   Nat Rev Drug Discov 16 (11), 773-786 (2017)
   PUBMED   29026209
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Smith,T.F., Gaitatzes,C., Saxena,K. and Neer,E.J.
  TITLE     The WD repeat: a common architecture for diverse functions
  JOURNAL   Trends Biochem Sci 24 (5), 181-185 (1999)
   PUBMED   10322433
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Neer,E.J., Schmidt,C.J., Nambudripad,R. and Smith,T.F.
  TITLE     The ancient regulatory-protein family of WD-repeat proteins
  JOURNAL   Nature 371 (6495), 297-300 (1994)
   PUBMED   8090199
  REMARK    Erratum:[Nature 1994 Oct 27;371(6500):812]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12822048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..341
                     /product="WD40 repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=36641
     Region          <13..297
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          23..59
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          64..100
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          107..138
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          145..176
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          184..210
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          225..248
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          262..>334
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          270..296
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          311..334
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 msdstavqrl qslwqvegge hintlvwspd ntrlatayad gsvavydtan grevwrhavh
       61 glatsalaws pdgnllasgg qqggiilwep dtgskvhqld sgrswveflc wsaegglasa
      121 agrqiqlwta egqlkqsfgq tastvtgllw ladatllssc yglvnqwsae reqplrhfpw
      181 kdsllslsvs pdqrfiaagc qdnaihlwyl ksgedfrmsg ypskvrhfdw sadsryfatg
      241 gaasliiwdc sgkgpqsskp vvlpvhtkpi ssivfshads rlasggddgl tvifdlargq
      301 plaglldeag vssmawsedd qvlaigyssg rlrlcpvpvk p
//
LOCUS       WP_010798845             369 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Pseudomonas].
ACCESSION   WP_010798845
VERSION     WP_010798845.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..369
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39284
     Region          138..343
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mrlqpsrlkn gillmaavgm gvslaacsnr spdkrplsel aisgakssvr ndadmqkvln
       61 qyarfdpkai ekitptearq qptiadavka vlekegrdsa pealvpgvks vdtsvsgaag
      121 tlparvytpe gkgpfpvily fhgggwvyad rnvydagarg lakqanaivv svdyrlapeh
      181 kfpaahddai aayrwviqna gslggdpkrl alagesaggn lavataiaak kagltapkhi
      241 lsvypvaqtn thtesydkya damplnrpmm lwfvaqatks pvdlndprid lvhadlkglp
      301 pvtiinaemd plrddgaqle talrnadvav drqlysgvth effgtaavve karqaqqyag
      361 eqlkadltr
//
LOCUS       WP_010798863             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HIT family protein [Pseudomonas].
ACCESSION   WP_010798863
VERSION     WP_010798863.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..143
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15935
     Region          9..139
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mslisdrval artgandkvi crmasgwavm gdvqflpgyc lllpdpvvps lndldaesrt
       61 tyllemtrig davleatgal rmnyeilgns epelhchifs ryasepeqhr kmpvwfydwk
      121 aappyteevh gnlrkkiaql las
//
LOCUS       WP_010798889             415 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010798889
VERSION     WP_010798889.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..415
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45730
     Region          5..386
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(15..16,19..20,23,55,109..110,112..114,117,137,
                     140..141,144,223,226..227,230..232,235,259,263,314..315,
                     319,323,339,342..343,346..347,350)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mrkdylaffi slflsrladq illfivplvv fqttnsasla glaffveslp rflvfplcga
       61 lcdkyppiki lhisqiyrai lcvlamtlyv ifdgigwlvl lsalcgvltt qgvmarevlm
      121 phifqhysyt ktlsysqiad qtglvlgplv aalmlevwaw hwvvlwiagl flladlsmla
      181 wqrlsritle vfeqhqdiwl qplriafghi rrmaelkkii tlavgvnliv gvtlstsaam
      241 vigqygagkd tyaglqaaga vttivilfll arivlplrvl ggvgysmiai gafmsalspn
      301 ligyvlgfll ivgfdkmfnv ymrtirqrvi ptrdfgktvg vitllnnmsq plagllvafl
      361 aaplgtqnvi lilavlttll gvfamwwyak ergrfptpif eadqeagkks vsakr
//
LOCUS       WP_010798521             320 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease Z [Pseudomonas].
ACCESSION   WP_010798521
VERSION     WP_010798521.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Redko,Y., Li de la Sierra-Gallay,I. and Condon,C.
  TITLE     When all's zed and done: the structure and function of RNase Z in
            prokaryotes
  JOURNAL   Nat Rev Microbiol 5 (4), 278-286 (2007)
   PUBMED   17363966
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Schiffer,S., Rosch,S. and Marchfelder,A.
  TITLE     Assigning a function to a conserved group of proteins: the tRNA
            3'-processing enzymes
  JOURNAL   EMBO J 21 (11), 2769-2777 (2002)
   PUBMED   12032089
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869904
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..320
                     /product="ribonuclease Z"
                     /EC_number="3.1.26.11"
                     /GO_function="GO:0042781 - 3'-tRNA processing
                     endoribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35207
     Region          3..307
                     /region_name="RNaseZ_ZiPD-like_MBL-fold"
                     /note="Ribonuclease Z, E. coli 3' tRNA-processing
                     endonuclease ZiPD and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07717"
                     /db_xref="CDD:293803"
     Site            order(36,61..62,64,66..67,139..140,209,229,268)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293803"
ORIGIN      
        1 mdllflgtsa gvptkkrnvt glalqeemgs dwflidcgea tqhrllrtrl slhdlqaifi
       61 thvhgdhcyg lpgllasagm sgrkkplpii apsgiaewfn atrqftqlyl pfdveflpae
      121 algqwafprw tvdatplshr vpsfsyrfte tarephlnte klnaegiarg piwgqlrkgi
      181 dvvhegqtfk sadyvyypqa arclvvcgdn dqpellrtfc qpaqvlvhes tytqdvadra
      241 gdtfghssaa giasfaqssg lpnlvlthfs aryqanpeqs psiedirsea ahhyqgslfl
      301 aedlaryrla ktgvlslvsv
//
LOCUS       WP_010798932             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Pseudomonas].
ACCESSION   WP_010798932
VERSION     WP_010798932.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..187
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=20888
     Region          6..187
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mlepnewith ygylavmvgp liegdglail agvaarhgyl nffltilmta igamisdqfl
       61 ffigrrygdp vlkkfhrhqh rierarqliq rypslwvigt rfaygfrtig piiigtsgip
      121 arrfvplniv gaflwatimv sigygvgefv qrlfatqpha glwlagiaat llaivaaiwf
      181 vrrrrha
//
LOCUS       WP_010798985             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010798985
VERSION     WP_010798985.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34217
     Region          9..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mrgqnyaelq afvaiaergs fvraaeelqv spsalsqtir sleermgvrl fnrttrsvsl
       61 tiagehller lrpalqevas avenaclfge kpsgrlrvha lrlasrvfle pifqpfseay
      121 peieldvvld drpvdivaeg fdatlrlgel ieqdmvgikl gpelrqipaa spsyleqygy
      181 petpydlenh rcinwrwpgq ihpyrwefkr dtewfaiavk gplivndqrv aieaavngvg
      241 iafwledqme pfinagtlvp llqewcapfd gfylsyprqr qqlaslrafi dflkkdsarr
      301 r
//
LOCUS       WP_010798989             306 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [unclassified Pseudomonas].
ACCESSION   WP_010798989
VERSION     WP_010798989.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..306
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33841
     Region          19..278
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtlsssasai ehlilpavrd lgdgfkvrra lpsaqrrtlg pfifldsfgp tvfkagegld
       61 trphphigls tmtylldgem lhrdsehyvq tirpgeinlm tagkgivhse rstdavrqtg
      121 gtvfgfqswl alpvaheead pgfqhvsage ipviedegvt vrvlagalhd kqaptrtfsd
      181 lfyadvvlea garyrihkeh veraiyvvsg evtvsgqdgr fgrdqlvifk peteivlsat
      241 gltrlillgg eplpekrhif wnfvssrrer ieqaaedwrl qrfpgvpgeh efiplpetri
      301 rlkatv
//
LOCUS       WP_010799008             440 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Pseudomonas].
ACCESSION   WP_010799008
VERSION     WP_010799008.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..440
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47020
     Region          1..419
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mahlqrtlsl gavmlfgiay mtpiivlgtf gilaqntggh vpsaylvalv amlftaisyg
       61 rmaaafpvsg saytyvrkai spklgfiagw avlldylflp maiwligaay lssafpavpq
      121 avwvlgfial ttvinvvglk lastintalm lvqflvlaaf vvlcvhyvqg sgeplftlap
      181 ftdghlqwpl imsgaaiacy sflgfdavst lteetrnaer tipkaillvt lvgglvfila
      241 sywvqrvhpg mafanvdsaa yeiarniggd ifvslflmgl ivgqftsgma aqasvsrllf
      301 amgrdgvlpq sffgqlsrrf gtpvnnlalc gvvallalkl dvatstsfin fgaflafslv
      361 nlavifhfyl gatqrgirqi llflicpllg lsadlylmis ldsmaillgl swlalgviyl
      421 gklthgfrtq ppemqfseae
//
LOCUS       WP_010799034             480 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amidase [Pseudomonas].
ACCESSION   WP_010799034
VERSION     WP_010799034.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..480
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51104
     Region          8..476
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mndidhlldt ldatalsllv rqgevtpiel ldaaiqrldr vnpqlnaise rcydvarqma
       61 qrpearqgvl agvptlikdl fspvqgarmt qgsrvmgear adldcevvar lrragcvfag
      121 tttspefgts yttestrfga trnpwnters aggssggaaa lvaaraipfa hgndgggslr
      181 vpasccgvfg lkptrgrlps gplvgegwag mgtphaitls vrdsalllda tagadlgapy
      241 aapaqampfv qavsadpapl riavieqlgp wptspealka vrhtarlceq lghhvefatl
      301 pvnlpglldh lfniigpstr nfldmvgqlr gqpvadeeld prtriilrer gdipaaryaa
      361 avesihalgr qlayflidhd liltptltre ppligdldaf dpslslaevi eafhsyspft
      421 alfnasgqpa msvplywten glplgshfaa rfgeehtlla laaqleraqp wanrkplvca
//
LOCUS       WP_010799024             435 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pseudomonas].
ACCESSION   WP_010799024
VERSION     WP_010799024.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47040
     Region          22..424
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,256,259..260,263..265,268,296,300,351..352,
                     356,360,376,379..380,383..384,387)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 maqaidtlsv sekndatyrh itwrlmplll vcyvfahldr inigfaklqm ssdlhfsdtv
       61 ygfgaglffi ayalfgvpsn lmldrvgprr wiatlmvawg ilstgmmfie satgfytlrf
      121 llgvaeagff pgilvylnrw fpahrrasvt alfaiavpma gviggplsgw ilelfkdsgg
      181 lrgwqwmfml eglpvvllgl vvlkalpdsf esvswleptq krqlrdalag eeqrktitsf
      241 sgivrngqvw llvaiyfavm lavntlafwm palihgagig qdsnvgmlsa ipylagcffm
      301 iaagrssdrh rerrwhlcvp llmgaagiai aglapqnttl vmlglviagm gassalpmfw
      361 qlppaflssg tqaagiamis sfgsvasfla pyfigwmrdt tqsaslalyv laaliavgaf
      421 lvlrtpaaiv npqgn
//
LOCUS       WP_010799074             302 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010799074
VERSION     WP_010799074.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33607
     Region          13..71
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..296
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(111,115,154,168,170,231,248,275)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(112..113,117..118,120..121,124,128,130..136,197,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mtvnqeetqa mqfedlrlfv ttineqsfta aaeklglskq yvsrrtmale eelgvrllnr
       61 ttrslkptdl gmtlyeravr ildevnetqe lvssqgvnvr gtlrvsapmt fgtlhvspll
      121 prfmqenpli sleldlndra vdlvaegydm airggmleds tliakrlmdi pmtacaspay
      181 lerhstpetp ddlrhhecll yghvksvewk fqtqgqlvcv pvkgklrtnn gevvrdaava
      241 glgiaylpvf ivsdalndgr lqpvlqahqp ptsafyavyp qhrqssravq tfanflkdhl
      301 av
//
LOCUS       WP_010799112             741 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: xanthine dehydrogenase family protein
            molybdopterin-binding subunit [unclassified Pseudomonas].
ACCESSION   WP_010799112
VERSION     WP_010799112.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..741
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80399
     Region          4..739
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mndiigagpr rvdgrlkvtg haqytadhgl krmayaygvy stiasgrvtr idtdeaqrmp
       61 gvlgifhhgh ftelyrppkm klnpakidrl vkvdesrlpf eddrvyyagq fvamvvadsf
      121 eqaraaayrv kveykeepal atlaqakkeq spktagsdys rgdpqagfdk aahridftyt
      181 tpvethnpme mhattayweg drlfvyestq svivhrntla rifglspdkv elqspfigsg
      241 fgstlwawph spatcavarl vgrpvqfvvp rpqmftttgh rpateqrlrl atddqgklls
      301 vrhesvnsts ftdqntescg svtkslyscp nlavthatlq vnhgtptsmr apgaapglfa
      361 lesamdemae avgmdplafr klnastrdes kdmpwssnhl qeafdkaaak fgwdkrtpep
      421 gsmrdghevi gyglaacnwd amrcacearv slradgtayv tcgaqdigtg tytivaqavs
      481 kitglpleni tvqlgdssfp pgpvsggswa tasvlpavae atrdaieqlk sfaiedgpfk
      541 gadpkvlefa ngrlvkdgea ldfanllttr rlssaegear tqtadksdvs irsfgahfve
      601 vrwdpgisrl rvsrvvsaid vgqvinakaa anqvegaivm aigmamfeat sydernampt
      661 nndyaeymvp vhadqppeld villdypdya lnefgargig eigitglaaa ianavyhatg
      721 krirdlpitl dklmdeipqa v
//
LOCUS       WP_010799085             339 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: transketolase family protein [Pseudomonas].
ACCESSION   WP_010799085
VERSION     WP_010799085.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..339
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36251
     Region          29..339
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mntptsatvt aepakkrltt samiasiase gqptrpapfg halaalaeqr kdivglsadl
       61 akytdlhifa kahpdrfyqm gmaeqllmsa aagmaregft pfattyavfa srraydficm
      121 aiaeenlnvk ivcalpgltt gygpshqatd dlaiframpn lmvidpcdal eieqavpaia
      181 ahngpvymrl lrgnvplvld rfdykfeigk aktlcpgkdv liistglmtm raveaadrlr
      241 adgidasilh vptikpldeq tilaearkpg rlvvtvenhs imgglgeava slllrngvtp
      301 tfrqialpda fldagalptl hdrygistqa vaaqikgwl
//
LOCUS       WP_010799193             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Pseudomonas].
ACCESSION   WP_010799193
VERSION     WP_010799193.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21687
     Region          7..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnekprqrrp afdreqgiai aqalfhqrgf davsltdlte amnikppsfy aaygskaelf
       61 eramhryade nalpmdkllg sgrppaealt allvaaarqy grdrtlrgcl itegmraddp
      121 tarnmaekls dagiqavrry ldqvrpdaaq vladyvlitl rglsaaacsg mssmrlveaa
      181 qlagklisle feasdsatnp
//
LOCUS       WP_010799169             302 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010799169
VERSION     WP_010799169.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33487
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..287
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,222,239,266)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mlnrmeliri fsvaaqsttf rdaatrlgts pqtvtraike lertlgellf hrstrqihvt
       61 afgaklalqa retlelvdql fiahstqeak givgitapha igklyliefl kplmrenpgl
      121 sidlslddql tdavankidi girvgavqdr ryiartvahv alkivaappl ldtvqrpgni
      181 edlkrlplsm lidrnngrpw pwvlaegqaf lpaspaftcd dpetereivl agiafgqmpd
      241 ylaepylseg rlvevmqhda pppselimyr pqsgpvasrv rlvydhlvnc fsdprifaqs
      301 kr
//
LOCUS       WP_010799439             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [unclassified Pseudomonas].
ACCESSION   WP_010799439
VERSION     WP_010799439.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..279
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30333
     Region          1..267
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkvlslistk ggagkttvaa nlgglladag lkvllldlds qptlssyyal cksreagsye
       61 lisqrltvae qiisvttipr lelivsndra ghlgtvllha pdgrlrlrnl lpafadqydv
      121 livdtqgars vvvemailas dcalcplppe mlaarelrrg tlglfeelep yrylgvylpp
      181 vklllnqvna nrrdtclimq slrntfaadp hvsvcktvip drvaylnaas lglpvhries
      241 kaaprsrsrc aadvmralan elfpeweqrl aqprgrars
//
LOCUS       WP_010799440              71 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AlpA family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010799440
VERSION     WP_010799440.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10531836
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..71
                     /product="AlpA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=8121
     Region          13..63
                     /region_name="Phage_AlpA"
                     /note="Prophage CP4-57 regulatory protein (AlpA);
                     pfam05930"
                     /db_xref="CDD:399137"
ORIGIN      
        1 mqpaspapas adrhimrrde veqktgfkrs hiynlmkagl fpqcrrigtr avgwdsleie
       61 qwvqdrlsvr e
//
LOCUS       WP_010799510             189 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein
            [Pseudomonadaceae].
ACCESSION   WP_010799510
VERSION     WP_010799510.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadaceae
  ORGANISM  Pseudomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Pseudomonadaceae"
                     /db_xref="taxon:135621"
     Protein         1..189
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=21315
     Region          84..189
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msfdlkklap wnwfkneqee qqaaaslpvq rndqpvagga vspilqlhre idrlfddafr
       61 gfgfptlamp rwpaewpgml kpavdiqetd tqyriavevp gveekdiqit ldndvlvvrg
      121 ekrqeqekke ggfhriersy gsfqralnlp gdanqdsika nfkngvltit mdkrelrspq
      181 agrtiaies
//
LOCUS       WP_010799534             304 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Pseudomonas].
ACCESSION   WP_010799534
VERSION     WP_010799534.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..304
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33599
     Region          4..295
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 msiapvivst nhkggvgktt ssrtlaqsla eiksftkgkp illvdldpqg ntsrrwrlit
       61 pqpngsyipk pnpnigesad syssicdlwl nllgqgeali pepyttsnpm ihvvpaheel
      121 mfeaisvske drpklgvamr swlrskeiae tycavivdtq ptktplidaa liaathvyvp
      181 fvpepqaveg vysiisyiyn lskqrgsdvp leilgllpnk vkntklhklq mkkieqlgeh
      241 pvfgrylmpv klsdrisyae tddwssvpdq vtdlegtniq hearrfakyv vsriqksanq
      301 eakv
//
LOCUS       WP_010799980             339 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010799980
VERSION     WP_010799980.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..339
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=38727
     Region          89..336
                     /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"
ORIGIN      
        1 mqdtviisll qkyikdqcte qelrtllqwl kspdnhidld lvvqplwdai dkdmshpnee
       61 renelrrevs sllseikqkn kftsnsgvrs knrlngfyrv aaililafsv tlgllkvldr
      121 pqpvvtyaek msakgekksl lladgtkvil nsdtkliips nfnkeeriie megegffdvt
      181 pnpdkpfiir sgearvkvlg tsfdfksyke defikltvst gkvrvnvadq dlqlavspne
      241 hlsinkidgn vrkesieenn yikwihgsly fnkepirevi ktinrtynrk vilqckncdy
      301 ritgthdnks ieavieaicf ttglrskreg gniilyekh
//
LOCUS       WP_010800069             425 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleotide sugar dehydrogenase [Parabacteroides].
ACCESSION   WP_010800069
VERSION     WP_010800069.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..425
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=47006
     Region          5..417
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mqtkkicvig lgyvglplar lfstrfetvg fdmsqarvda lngghdatle vddellqaal
       61 angfrcttwl ddikdcnfyv vavptpvden nrpdlrplwg asetvgkvis kgdivvyest
      121 vypgvteeec lpvvekisgl kfnkdffagy sperinpgdk ehtvekikkv tsgstpeiad
      181 ivdqvyntvl ingthkapsi kvaeaskiie nsqrdvniaf mnelakifna mgidtndvie
      241 aaaskwnfik lkpglvgghc isvdpyyliq kaqvygvlpr vmfaarrlnd gmgeyvahqv
      301 iklmnkkgvl vknakilllg itfkencpdi rntkivdiyt tlseyskcit vydpwanpvr
      361 vkheygidic dvpldelegq ydavilgvah kefkdmdvrs flsndngvvy dvkgvmdrsv
      421 idgrl
//
LOCUS       WP_010800078             365 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MraY family glycosyltransferase [Parabacteroides].
ACCESSION   WP_010800078
VERSION     WP_010800078.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..365
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40434
     Region          40..311
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            109..110
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            232..235
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133463"
     Site            order(288,302..305)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 miylliliaf visivfsmli iprilivalt krlfdipder kihtgavprl ggisfapiil
       61 ftlafisais ylgylqglpi ppniishvtp dfylltcgli llylagikdd liglhystkf
      121 iiqilaasll plsglwlnnl yglfgmhelp awlgmpltif vivficnain lidgidglas
      181 glsgvslmvl gvlflhnqmw tyatlafstl gvlipffyyn vfgqvehgrk ifmgdtgslt
      241 lgyilaflci ryavynpevt pystsailva fstlivpmfd virvmlirfr snkglfspdk
      301 nhihhkflkm gckphgally ilgisiffsg lniilapfan inilfltdii lwtalnlcld
      361 klkci
//
LOCUS       WP_010800096             793 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Parabacteroides].
ACCESSION   WP_010800096
VERSION     WP_010800096.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 793)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 793)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 793)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13784517
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..793
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=88669
     Region          17..239
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          160..762
                     /region_name="ADOP"
                     /note="Acidobacterial duplicated orphan permease;
                     TIGR03434"
                     /db_xref="CDD:274576"
ORIGIN      
        1 mnirrslrii frnkiysfln ilglaigits aaliflwves kvnfnkaipn srniyvsash
       61 yfpvsnecit sfesnsmlsk vledefpevk scsrysaqpv vfvpenttds feekgayads
      121 tlfnligmkf isgdassvfe pqysivlsrs markiyneed pigkgliheg viyqvtgvfe
      181 dmpgntsfqf ewlipfrvfv eemkkvfnvn ewgaswlqty velepgvdle qlneklkgla
      241 frkagpaces iqiflyplnk mllygqfkdg ietgggyikt vslffligvl illiacinfm
      301 nlstarsqkr alevgvrktf gtkrkhlirq flvesglits ialllsvgli wlslpwfnef
      361 igvqlsfsll dptivtglva iglfctflag sypalylssf nplttlkmqk vskggsaawi
      421 rqglvifqft mafilicstf viylqiqlvq krdigikken lvsfpateel cnassavrne
      481 lintgvvenc gfsaspilks smrtnpwywn gkdpeddayi sfnfvsegli davgiklldg
      541 tdidpakknn kggagiline tlakrmgreg rvggqigqsp dhkweivgim kdfvfddfyt
      601 lepasalffy dpqrtyilfv rlkpdidtye aigrvqtvlr sftpyhafep tfmtdrfddl
      661 fedehlvekl salfamlaif isclgllgls afsaeqrtke igvrkvlgak iidilfllgk
      721 aymvlllisf vigipvslya anhylkdyay ritlgwdifa gvallitlia lltvsfqslr
      781 aalnnpvksi kte
//
LOCUS       WP_010800115             382 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: leucine-rich repeat domain-containing protein
            [Parabacteroides].
ACCESSION   WP_010800115
VERSION     WP_010800115.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..382
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42716
     Region          74..381
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          87..108
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          109..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..151
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..171
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          172..193
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          194..214
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          235..255
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          309..328
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 mkntiililq iiilgivssc ekneegitfv dfsdnvfyew clssfdldgd qelsfrelyl
       61 vtemnipaqy ngqtikslgg ienfayleql tcsdntelts ldlskcsylk kadchncnis
      121 slnlsgcsrl eelycysnsl nelnlsdfes laylycdfnv ltsldftnnp dlkeiscsgn
      181 klqgdlnlsk ctkleallce knsielidit ectslktlic ysnkltaidv yskaleilsc
      241 sgndiswlhv ancenlqely csenpsmqil gikgcvslkt lecysnnlss lnmsdskdlt
      301 hidchnnvls sitlnstlit yldvsqnllq tldislcpai kclyftlnrp lnnggvsklr
      361 hisffilkiv vplflsmrlf lq
//
LOCUS       WP_010800125             331 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
            [Parabacteroides].
ACCESSION   WP_010800125
VERSION     WP_010800125.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..331
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=37335
     Region          6..328
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
ORIGIN      
        1 mklpgkiaim gggswatala kivlstqdsi nwymrrqdqv ddflktghnp sylsavkfdt
       61 dkikfytdin daindsdtli fatpspflkq hlmkvttpln dkfiisaikg ivpdenmlia
      121 dyfteyynvp meniaviggp chaeeialer lsyitlacsn idnaravahv fqnqylnnyc
      181 ckdvrgieya svlknvyaiv agichgmkyg dnflavficn aieemrnfln svhslerdvt
      241 dsvylgdllv taysrfsrnr tfgtmigkgy svkiaqleme miaegyygtk ciheinekyk
      301 vnmpildaly dilyerkspt tvirqltetf k
//
LOCUS       WP_010800133             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Parabacteroides].
ACCESSION   WP_010800133
VERSION     WP_010800133.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..197
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22742
     Region          21..184
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 metdgylakl ladlpeslar devfvselkn ittvvavdkg dyllrtgeic qdayfinkgl
       61 finlyvsekg decvtgfssd yqypflsaig yftqapsefe ikaleagell rlsrthiedl
      121 slryplfasy yqnamltiis klysmfairq sctaeefiky lynhymwimq rvpdkyiaqy
      181 mgisnawyck lkkrifn
//
LOCUS       WP_010800151             294 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Parabacteroides].
ACCESSION   WP_010800151
VERSION     WP_010800151.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401161
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..294
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34229
     Region          16..99
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
     Region          <201..286
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 miplyqelpf tsnsyinfyk edlphfivpw hyhpeieimy ilegtgtrfv gdhidryqeg
       61 dvcmvgpklp hewrnddeff kqgaglkasc lclfflkdif eenlirlpem nnirqliers
      121 rrgikfmgks rdtigsfiqr svndtgaari tnfisllemm attdeyella svgftesvns
      181 sdferfdkvy qymmknftkp ikleevaslv gltpnafcry frgrtkktfv qylndirigh
      241 akklliegrm kistlsmeag fnnlsnfieq fkrstqmsps eyqkkfgvkn rkvi
//
LOCUS       WP_010800198             295 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Parabacteroides].
ACCESSION   WP_010800198
VERSION     WP_010800198.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..295
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32537
     Region          19..284
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtikkvesii appappaphm vgdgfrvhnf iphleelsre rmnpfilldy nakmefsprk
       61 eprgvgvhph rgfetvtivy kgkvahhdsr gnsgvigpgd iqwmtaasgv lhkeyheesf
      121 srkggefhiv qlwinlpard kkadpkyqsi ensqipkvel pdntgmvevi agryqntngi
      181 astftpmhlf naklnkggna efsfpadynt ailvvegsvk innnelvptd yfalfetkge
      241 tftihavnka tvlimsgepi kepiaaygpf vmnnvaelkq ayidlgagkf gkldd
//
LOCUS       WP_010800158             543 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010800158
VERSION     WP_010800158.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..543
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=60847
     Region          41..492
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          290..539
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mklkkyislg laslccvwat sclgdldqep ildkssssih neadcqsfla kiysgfglsg
       61 nssdtnvepd lqggdqgslv flrgllslql fpsdeaiwnw adegivelcq lnwdytlpya
      121 ysfyqramln vryckefldv yaadsdipdi qkyrdqvrgl ramnyyylid lyrnpgvvwd
      181 dsptddkswk psqmgaealf dkivaelidl sengnldetp smatygrvtr pvintllakm
      241 ylnaevytgk pmydkaavya qkvidagfgl ednyanlfcg enhltgmhkn eiiyaipfdn
      301 vnaksygsti mltaaayggd mdqtwfgmss swtclkptqq migffnespd tgtdshgslv
      361 kkdkryafyd gagtrtpesk mqdwntgylc hkftnlgwdg aavtptpdpn tdfplfrlad
      421 iyliyaecav rnaagtnkeq aveyvnqlre rangdksani tasdlsldfi lderarelyw
      481 egqrrsdlvr fgkftkdyaw aykggtlegv anidsrfniy pisdrdltan pnlvqnpgye
      541 slk
//
LOCUS       WP_010800233             634 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010800233
VERSION     WP_010800233.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 634)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 634)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..634
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=72661
     Region          107..>246
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          316..634
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mksiykyivc vctalaatsc dfldvvpdnv ateehafadr ytvekylasc ywrvpkaasm
       61 senpgihgam emilnteysg dtgmklglgq dsptsalmny wassyslyag irdcntfmmg
      121 igdvkdldey ekkrmiaevk mlkayfhfyl lsyygpicpl respavnest qavrvyrekv
      181 ddcfsyvldl mdevieseal plilsnptte lgrftqpaay mlkakillyw asplfngntd
      241 ynsfrdhnge pffnqtydas rwttaaeack kavdicetag irlyrtsdyi sakklsdqtl
      301 qvqtlrgvis hrwnaeliws ntsypvdggf qsdcftyfes altlgtkqrl svplstvewf
      361 yskngvpiee dimydytnry slrtgdegnr yyiqkgeqta glnfdreprf ystlgfdrgk
      421 wygnsyknip dddaeclypk nrfgeyssaa dpgnynatgy wpkklvsins syrdansvtw
      481 esypfpdmrf adlllmcaea lnesknvpda evykyidmvr eragldgvlq swrkysnhpe
      541 kpttkegmre iiqrerkiel acegsyywds rrwktalqeq nrliqgwnin asdaenyytv
      601 tpvyeqsfsf knylapipes divknpqliq npgw
//
LOCUS       WP_010800236             339 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit alpha/FixB
            family protein [Parabacteroides].
ACCESSION   WP_010800236
VERSION     WP_010800236.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..339
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36701
     Region          3..336
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mnnvfvycei egttvadvsl elltkgrkla nqlgcqleai vagsgledve sqvlpygvdk
       61 lhvfdapglf pytslphssv linlfkeekp qiclmgatvi grdlgprvss altsgltadc
      121 tsleigphed kragityenl lyqirpafgg nivatiinpe hrpqmatvre gvmkkeilda
      181 nykgevvkhd vakfvpetdy vvkvidrhve kakhnlkgsp iviaggygmg sregfdklfe
      241 lakelhaevg asraavdagf cdhdrqigqt gvtvrpklyi acgisgqiqh iagmqdagii
      301 isinndenap intiadyvin gtveevipkm ikyykqnsk
//
LOCUS       WP_010800242             340 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Parabacteroides goldsteinii].
ACCESSION   WP_010800242
VERSION     WP_010800242.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides goldsteinii
  ORGANISM  Parabacteroides goldsteinii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Parabacteroides goldsteinii"
                     /db_xref="taxon:328812"
     Protein         1..340
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38786
     Region          108..306
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mkknlfllfl ffmtsasfaq kqekttpfwg kqevylvnqt ekifrlvdvl lkenmpsvge
       61 palarksall lldgifhdtr ldgskvlsdf advrlnsvle dlklpltegm kvyklyndgf
      121 ivrtksatva fdlyrggkmk egghlisdgk mraiaeqcdi mflshnhpdh vdpvvvkmft
      181 dagkevvapt dvlmgngavt hvrseqimdk kfklkrsklk vkilpghqse mmnnihvvtt
      241 segftfvqtg dqynkedlkw lltvykkipe vdvlmincwa nrlsdtidgf npklvltghe
      301 nelghtidhr esywasyvkl edvrkpnclm twgecfwykk
//
LOCUS       WP_010800254             405 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Parabacteroides].
ACCESSION   WP_010800254
VERSION     WP_010800254.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43859
     Region          8..393
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(18..19,22..23,26,58,113..114,116..118,121,141,
                     144..145,148,225,228..229,232..234,237,261,265,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mnnwkkvfai iwtgqffsil tssivnfaii lwlsfetksa evlafaaiaa mlpqsvlglf
       61 tgifidrwkr krvmiladsf iafctlilav lfyldiakie hiyimlalrs vgsafhmpam
      121 qasvpllapk seliriagin qiiqsacnia gpalaalfis fmemtnilll dvigaalact
      181 sllfvkipdp dntektqkvh llkeakealt evraqnglsw lfilsiiatf fimpvsvlfp
      241 lmtldhysgn afqislveaa wgigallgga flgmkkfkln eislinwmyi llgvtfglsg
      301 ilpvsgyplf vvltavggis gslymasftt vvqtrinpvv mgrvfsfyms vsllpsmigl
      361 lstgfladti gigntfiigg glvgmiglis falpaikelk kgfdk
//
LOCUS       WP_010800261             424 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Parabacteroides].
ACCESSION   WP_010800261
VERSION     WP_010800261.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 424)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..424
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47969
     Region          70..424
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mllhilklik tqrrsntwvf iellvvfvll wyavdrmtms ritqaqpmgy sfedvykvtl
       61 avrpstsasy ityeqgsqga gedfmriirq leahpdvqvv glaneasmpy tymsnsdtyf
      121 qekdsiyrna fdfsvtpdyf rvfdihaadg gspdelasai qegillsepm amkcfsstqv
      181 ggrellilqd dtlryrvkgv teavkreefs qppsivfkem kersilrmse qelgkmqicf
      241 rvrpgaaaes aseyavrfkk emkhrlaagn fwlanvqyyp dvrtnylets mntsggkldi
      301 avnifllinv flavigtfwf rvnrrrnelg lrmavgssrr rlqqlligeg lmiltitavp
      361 allicvnvaf agllstevme vtvgrlllvs lltwlllavi itlaiwypsr kaarlepaea
      421 lhye
//
LOCUS       WP_010800262             435 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Parabacteroides].
ACCESSION   WP_010800262
VERSION     WP_010800262.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 435)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..435
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48201
     Region          4..432
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mykqyfkqaw nlmrqnrfys gvyiigtgla ismvmviaiv yhirtaditp evhrgkylyi
       61 dqmkyergkg nsnffwgirs akeclmplks akevalmtnt aitsllygdt yvqipggddp
      121 qkvqvmgtnn sfwrlfsfsf vegkpfseee fqsgfprvvv seslarrifs tatgvtgksi
      181 llddteysvs gvvkdvsavt psvyadmwvp ytsmplvmga sderdvsvgl ltvcilpadg
      241 mgvdevsrel eemidryntt ladgklsmmn gvethlthvi rqfvmggsvt avylmllfli
      301 flfllipaln lsglnasrmq driselgvrk afgarknrll tqilienlll mlpgglvgll
      361 vsygmvalfq qllltpgiia mvqgsvqtel tvgmllspav fgyafgvcfl lnlmssmipa
      421 wrairvnite slnhy
//
LOCUS       WP_010800265             432 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Parabacteroides].
ACCESSION   WP_010800265
VERSION     WP_010800265.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..432
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48645
     Region          4..360
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mfrqyliqal nlmkqnrffs fvyilgtala ismvmmmaiv yyirtadiap evnrgrlcll
       61 daatsvskdg qsnwtgnlsf ktirevyypl rtpelvsayi rpgiftynvg emqlripggk
      121 dkfeinlsat daaywqmfrf tfidgkpytp adfesglrri vlsetrarql fgkpdvagqg
      181 vllndveytv agvvrdisav ntitcadawv pftlypelmi sdgaegvlgm lelcircrsi
      241 ddlsvlrkei dqnrkryntt lkdweyiane rgdvrtwrtf ilskldwrts pskqlmqygl
      301 llcifllvpa vnlsglsssd mvkripelgl rkafgasrat livqvltenf lytflggivg
      361 llfsfllvfl lrnllfgieq mtgevslspg mllnlpvffi tfgfclllnl lsallpawls
      421 trvsivkain dk
//
LOCUS       WP_010800276             105 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system RelE/ParE family toxin
            [Parabacteroides].
ACCESSION   WP_010800276
VERSION     WP_010800276.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..105
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12558
     Region          4..95
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mqiklkwlpr aiallddiye yyseksersa iriynkllds aeplktfpya giseplleef
       61 pqnfrslvve khfkliytis ptqieihaiw dcrqdnwrlk emfhr
//
LOCUS       WP_010800289             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Parabacteroides].
ACCESSION   WP_010800289
VERSION     WP_010800289.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..224
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=26388
     Region          3..165
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkledivehy gtmvatiahr miqnreiake aaqevwyevf kslpsfnads elstwiytia
       61 krtisryaqn ekvatlvkle qfralqeiey tgsdeerkew vkercdwclt alnhclnnda
      121 rlififkeni glshkeigei memsvenvrk iysrsidkis hfltdtcply npagtckcri
      181 ckqvffidld keyttvakmi rladlyqkfe kdlprknywe kfld
//
LOCUS       WP_010800295             107 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin
            [Parabacteroides goldsteinii].
ACCESSION   WP_010800295
VERSION     WP_010800295.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides goldsteinii
  ORGANISM  Parabacteroides goldsteinii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Parabacteroides goldsteinii"
                     /db_xref="taxon:328812"
     Protein         1..107
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12802
     Region          1..99
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mkiiwhpfas ndfdqiiyyy rdafgvktaq kvrdtlhhdi yhllclhpfl gfcetclsdv
       61 dqlsyrslvs ghikiiytvh dkyiyihmlw dcrrnpkqlq seikerk
//
LOCUS       WP_010800301             576 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010800301
VERSION     WP_010800301.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..576
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=64478
     Region          38..488
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          263..576
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkiyklllll vvgfsscenn ildlesltep vddvfyknge elnlalngty nslrlttdyk
       61 iplmvamdng atdigvsrgv csammnqgqg tqsstnggfl tiysdhykgi aranallenm
      121 vrskdvvset iykqieaqal firafhymyl telfgdvpfl nkvikvpteg lipreskkvi
      181 idqiladlkk aaevlpyswk geperitkga alglharisl yngyyaeaaa stkeimdneq
      241 afgyslhany gelfqlagqa saeimfimpf kyeyyitqfs vtqgsrnkga vsvmvptqsm
      301 vdsyecidge tidkskvysp krpfenrdpr lkasiitpqs ewagmifesh pdsttyrlvn
      361 gaiggsnsdc rtvswpaafc gylwkkntie etqvkiqswd dhnfilmrya eilltyaeak
      421 imqgevdesv ltainrvrar aygvdvsata dypaittmdv aklktiiqre rkveladegf
      481 rlfdirrwki aekvmpvtiy grildtetat gipqidedgf vsysgiasqy dlntdarfpn
      541 avrvfnssrd ylcpipqqei dtyarfgitl gqnpgy
//
LOCUS       WP_010800442             606 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010800442
VERSION     WP_010800442.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..606
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=68870
     Region          108..540
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          311..606
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mknlinilvv tftlccssca dldiasdgrv slndifnrye rtsayysncl gympqvgfty
       61 entntplasf cdeahdandn qdgpvskwyk gyttpeynpl tasymdpwsh yfegirrcnt
      121 fllcindpem atytfnevek ngwiaevrva rafyylqlik ryggvpliet pyetnhdfsi
      181 dkrasfeeca dfiisecdka latvesegqs igfrwqindn ergkltrafa cavksqtaly
      241 aasplwneng sskytwektt eitkealdlc lqhgfelysq apdlaiaqna yayyfitrsd
      301 psrswdreti yettswrsnv wkfagtpitn gmekagagps qelvdsyemi dgtqpilgys
      361 daehlrpiln tassydpknp yanrdprfya svyyngairy ldqpngdvve tyvggncgis
      421 dkvtdirytr tgyymrkfnn fksgigqdad glmrifrlae lylnfaeaay qavgpdgqvv
      481 skvgaealsa rdavnkirvr agipalssgm skdsfekryr nerrvelafe ehrffdvrrw
      541 kilnetddfv tgmkivkeed gtftynrikl asrgtnadky llypikqtev akmlkhtgan
      601 wqnpgw
//
LOCUS       WP_010800461             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase
            [Parabacteroides].
ACCESSION   WP_010800461
VERSION     WP_010800461.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..429
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47708
     Region          10..402
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mgfniaktnk krvviigggf gglklanklk gsnfqvvlid knnfhqfppl lyqvassgle
       61 pgsiifplrk ifqkqkdfyf rmaevkaiia ernlietsig eltydylvia sgtitnffgn
      121 ktieekalpm ktiqealelr ntllsnfeka tictdpeerq almnvvivgg gatgveisgv
      181 laemkrfvmp kdypdlkqsd mhiylvegsp qllgvmspea sanaekflkg mgvniilnkr
      241 vtdyqdgkvi lddnstiatq tlvwvsgvta thfehidkea lnrggritvn efnqmpgman
      301 vfaigdvcfq teedypnghp qvaqvaiqqg nlladnlkrl esgkelkafh ylnlgtlatv
      361 grnkavadlk klklqgfiaw mvwmgvhlrs ilgvknklmv liewiwsyft ydqsirlily
      421 ipkkkvgks
//
LOCUS       WP_010800481             287 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endonuclease/exonuclease/phosphatase family protein
            [Parabacteroides].
ACCESSION   WP_010800481
VERSION     WP_010800481.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..287
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32405
     Region          28..284
                     /region_name="EEP-1"
                     /note="Exonuclease-Endonuclease-Phosphatase domain;
                     uncharacterized family 1; cd09083"
                     /db_xref="CDD:197317"
     Site            order(33,69,161,195,197,249,276..277)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197317"
     Site            order(69,276)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197317"
     Site            order(161,197,277)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197317"
ORIGIN      
        1 mkkillsils vllfagflsa kqpvaplkvm tfnirmdtna dgdnqwsnrk dlaanlvkfy
       61 ntdifgaqev lnhqltdllt rlpeyayvgv gredgktkge yapiiykkdr feledsgnfw
      121 laedmnavgk kgwdaacerv atwgifkdke sgkkffflnt hldhmgkvar hegaslvlee
      181 ahklskglpv ivtgdfnatp dddpikvltd ksdprhviht revadlkygp ewtfhdygri
      241 plekrewidy ifmkgdikvl ingvltdtln hlypsdhcpv iatlvik
//
LOCUS       WP_010800485             298 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tyrosine recombinase XerC [Parabacteroides].
ACCESSION   WP_010800485
VERSION     WP_010800485.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11493900
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..298
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=33956
     Region          4..295
                     /region_name="recomb_XerC"
                     /note="tyrosine recombinase XerC; TIGR02224"
                     /db_xref="CDD:274042"
     Site            order(133,147..148,219,221,240,275)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271179"
     Site            order(147,240,243,266,275)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 mlvdsfldyl ryernysnyt ieayskdlrq feeyvklnke svfvpgdvda dlvrswivsl
       61 mdekispvsv nrklsslksf fkflmkqgsi svnplrlitg pktkkplpyf vrdkemelll
      121 dgdgfdedfe gvrdrlilem lydtgirrse ligiqdsdvd fgamqirvtg krnkqrlipf
      181 aeglknliqa ytevrnrevg sesgwffvrk ngeqlsagiv ytivkkklse iptlakrsph
      241 vlrhsfatsm lnngaelnav kellghssla stsvythttf eelkkvyhah prakkegg
//
LOCUS       WP_010800502             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Parabacteroides].
ACCESSION   WP_010800502
VERSION     WP_010800502.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..322
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35000
     Region          29..284
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mkqvkllfsi ifsfitvvcf gqlmpladea vtlntqngai hgkillppgm ksspvvllia
       61 gsgptdmdgn saigqmtnns lkylaedlae qgiaslrfdk rgiassapag kkesdlrfed
      121 yvndvkgwid ylgkdsrftg itvighsegs ligmlacrnd pkvkafvsla gagrpayeii
      181 ekqlssqpes vrnmiasind slkqgklvpn vpfgmealfr qsvqpymisw ykynpqqvik
      241 elkipvlivq gkndiqvlve daellkkaap satllliekm nhvlkdcdtt dpqkqmavya
      301 npslpvnatl isslssfike kk
//
LOCUS       WP_010800517             362 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010800517
VERSION     WP_010800517.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..362
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=41166
     Region          140..359
                     /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"
ORIGIN      
        1 mnnseenkks seedlrllkr kirvvdegls seakaelwtk iesairrpkr msvsfsmflr
       61 yvavvailci atyyiytgls preeidynsi lsntqlpdda snnvmvilgd kdkiefedkd
      121 vqvshdedgn mrvnqkqidl pepsrreynq livphgkttr vtlsdgsaiw ansgtklvyp
      181 avfasdrrei yvegeiylev arnekypfvv ktdmmevnvl gtsfnvsayk ndkqqfvala
      241 tgsvavkvan kkntttikpn qlytlekstf atriedadiy eyicwkdgfl ifhnesladv
      301 lkkieryynv vltfdpaeis kvtvsgkldl ksdiretfri isitapieyd kegdvikisv
      361 kq
//
LOCUS       WP_010800505             774 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GH92 family glycosyl hydrolase [Parabacteroides].
ACCESSION   WP_010800505
VERSION     WP_010800505.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..774
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=86430
     Region          1..774
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mkkkislcll vlgaiyiscg svkdrseeqq alssyvnpfi gastsmdagg syhglgktfp
       61 gatapfgmvq vspntitggd ngsgysdeht siegfaftqm sgigwygdlg nllvmptvgk
      121 lhtfsgasdd pdkgyrsryd ksseeasagy yavmltdyqi kaeatalphs gmlrftfpes
      181 kesriqidla rrvggtstwq avevindhti rgemkcppeg ggwgngdgka dytvyfyaef
      241 srpfrshgvw sadipddwtc krgdiesery qevvrnarii pdvtsyvgkh lgfyadfete
      301 tgdqilmksg isftsmrnae enlhsemnaw dfdatlascr qlwndalski svsggtedek
      361 hifytalyht midprvcsdv ngeymgadkq vhvtdqfskr tifsgwdvfr sqmplqtiin
      421 ptlindqins lveiadqsgn nylerwelln aysgcmlgnp aisvlcdays kgirsydidk
      481 ayqyalntsr mfgnnengyt pgsishtley ayndwcmarl aewlgkeadk dvfdrragty
      541 ttlydpdygw frprnekgey lplpeqgrla egygcvesna yqqgwfvphd vegmiklmgg
      601 rekvladltd mfeqtpanyl wnqyynhane pvhhvpflfn rlgapeltqk wtrdicrnay
      661 knsvlglvgn edvgqmsawy vlaasglhpv cpgdqryelt spvfekvvfn ldpnyaegkt
      721 fvieahnnsp eniyiqqatl ngkpydkcyl ihddlmkggt lvlqmgaeps dwgk
//
LOCUS       WP_010800548             269 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Parabacteroides].
ACCESSION   WP_010800548
VERSION     WP_010800548.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..269
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=28619
     Region          60..262
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mktnqsvisk tsngvsagiv iiicfilavc ffhfvlgnps nfmdnnpdnh plpgnyagti
       61 ykggfivpvv itllltvitl sverfiainr skgkkallgf vrtikkdled gnldaaqkac
      121 keqqgsvanv vnaaltrytd venradqtke qkmviiqkei eestalelps meqnlpviat
      181 istlgtlfgl lgtvlgmirs faalanagap dsvalstgis ealvntalgi atgamaiisy
      241 nyftskidni tyaideigfs ivqtfaakh
//
LOCUS       WP_010800605             537 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010800605
VERSION     WP_010800605.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (residues 1 to 537)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   5  (residues 1 to 537)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 537)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..537
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60940
     Region          39..478
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkkynillil filfttascs glldedprgd vagsnfftde enalsnindl ynafgdanvy
       61 srqammvmef gtdlgtrsps dnwptldpia tythdasaqr iwwvwrdsyk yirnanlsia
      121 sienmdaslf khagkerlla earfirgfly fhltnffgdl pvitepaedl nsllhlsrtp
      181 asqirkeivl admqyaadhl pefdeyssnd agrisrstai gmmakvylfe kdyakcaelc
      241 ktlysegkrg llnqyadvfd skynnskesl laiqsliekk espaqttcyg dftedddspy
      301 nngsaiapll pfasyyvpke dqwydtendn rwgfnfrlas eskykelidg tgtsakhlga
      361 gikykgeivr mpyivkfcdv nnrrpdrsgt slnfpilrws dvllmyaeal neqgntgeaf
      421 tyinevrkra ytnkdntlnp gwelkglsqs elrtailker alelcfeghr kfdlsrtgtl
      481 eaaikgvthl ddieflfsea yypkeaarnv hswhrlfgvp tseitlnsnl lpqnegy
//
LOCUS       WP_010800635             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhomboid family intramembrane serine protease
            [Parabacteroides].
ACCESSION   WP_010800635
VERSION     WP_010800635.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..197
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22336
     Region          2..187
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mityiiigit vlvsylcfnn aelfrklali pyrtvknnew yrlithgfvh admthllvnm
       61 ftfwsfgtyi ekvfgylgfg twgflglyfg gmifasiydl vkhhndpyyv sigasgavsa
      121 ilfsyilfdp wskillfaii pvpgiifgvv ylaycqymak ragdninhna hfygavygfl
      181 fpallnpsli kaflshf
//
LOCUS       WP_010800670             638 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: beta-N-acetylhexosaminidase [Parabacteroides].
ACCESSION   WP_010800670
VERSION     WP_010800670.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..638
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=72269
     Region          1..603
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mkkslhaflm tgivcisisc srqsvserdt lalipvpqem kvnsdsftlt rnaaitldqs
       61 nqalvgiaey lnekispatg felpvekhgk iefklvedas lgdegyqlkv khsdilitan
      121 kpagifygvq tllqmfpaei ksktvqpedk kwtipcaeit dkpqfpwrgl mldvsrhwft
      181 keevlkyide laeykmnvfh whltddqgwr leikslpklt evgawraprv gqwwqrerqq
      241 pgeettyggf ytqedvkevl ayaakryvrv ipeidvpghs vaalvaypel acmkapdavn
      301 vgnkfygede ntlcigkdyt fefmdkvlte vaalfpdeyv higgdecfkg fwhkcprcqa
      361 rmkaenlkne eelqsyfihr mgdllkskgk klvgwdeile gglapdanvm swrgmeggik
      421 aakaghhvim tptehcyldl wqgepsvepd tysmcrlkds ysfnpipegv paemvlggqg
      481 nlwaeslptf rhveymtwpr gwalsevlws gpsktdwekf wprvekhfvr adqadinyar
      541 smynaivspy lqdgvlqvel gseiagtdiy ytfdntdpds htpkytdpls ipknatwlri
      601 vtyrdgkpvg kvitlttkel akraesdkrt ghgnltvd
//
LOCUS       WP_010800703             545 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010800703
VERSION     WP_010800703.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..545
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62325
     Region          44..480
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkrlkyiayt alcaslflss cdlerypltd lseenfwdae kngslaltsl yrgnitngle
       61 ysvsdfwsyh gllftehltd ngfdrrgenn pffkissgql qndnsfisgy wssaykrigm
      121 cnrflagies atesesktrm iaearflrat qyhylasyfk dvplvttvlt geesnnvtke
      181 tqanilnwca tefkeaandl prfseiksse tgrackqasl aflgrtymlm kewakgaety
      241 keiidlgdnd lhskyselfy pgtgvgnken iyyiayleny fgcglpqhgl sakdggwsls
      301 nptaglfesy aftdgtpfsy ddprfnpdnl genrdprldy tiyyngstfm gseyrmhpdy
      361 daskkervdy sseasktgfm wrkyydenpi ndlqsysavt piiryaevll sylecmiesg
      421 qsinqnvlda tinkvrgrsd vkmpgttetn pdklrkivrn errielayeg irfwdimrwn
      481 iahevlvgei wgapypgstt yaastkfvdp tghyrwyagr rdfrspqdyt wpiplseqni
      541 npnlr
//
LOCUS       WP_010800710             291 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010800710
VERSION     WP_010800710.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..291
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32972
     Region          1..288
                     /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"
ORIGIN      
        1 mtpendnfdk ileqlvastr sprgrfsakn swkilerris pasgkikflr iagsvaasil
       61 iclaswytyd yiqsgtiqti stlaeirdit lpdqsvvtln rystlsfpsr frgakrevrl
      121 tgeayfdvek dtrhpfivka esvnvqvlgt qfnveayped peikttlieg svavsipeen
      181 rrivlspnes aiynrlqksl qheinpkssn divwrnghfl fdylplqeit rqlshafnvk
      241 ieitdpelrs yhiranftng esleemlell kgagnfnyti tnntiiistk l
//
LOCUS       WP_010800728             327 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Parabacteroides].
ACCESSION   WP_010800728
VERSION     WP_010800728.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..327
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37432
     Region          <187..302
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mklfktrkty ylynpntlsy drvypsardr ffivlrhlsi gaaigigvff immytidspv
       61 eslmkkenkl lqtqyevlsl rltnalevld diqqrdenly raifqaesip esvrksgfgg
      121 tnryehllnl snpelvvstt qkmdmlskql yiqsnsleel iklgknqeer srcipaiqpi
      181 snkdlrrtas gygvridpiy rtprfhsgmd fsakvgteiy atgdgvvtfa awkqgygncl
      241 midhgygfqt lyghmskyrk rvgqkvtrge vigevgntgk stgphlhyev ivrgkhdnps
      301 ryyymdltpe eydrmiqiae nhgqvmd
//
LOCUS       WP_010800743             770 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Parabacteroides].
ACCESSION   WP_010800743
VERSION     WP_010800743.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..770
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86201
     Region          34..121
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          108..717
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mnkiitlilc lccavtvara tgddekmnas danvfghvld ketgehlpfi tvmlkgttig
       61 tttdnsghyf lknlpegkft lefkylgykt vtrevtlvkg ktqeinvele edrialdgvv
      121 vsanrsetsr rlaptlvnvi dsklfkttna vnlvqglnfq pgvrvetncq ncgfqqvrin
      181 gldgpytqil idsrpifsal sgvygleqip anmidrvevm rgggsalfgs saiagtinii
      241 tkeplrnsge lthtissigg ssafdnnttl naslvtdnsk agmyifgqnr hrsgydhdgd
      301 gytelpklkn qtvgfrsylk tstyskltfe yhhmneyrrg gnlldrpphe adiaeqlehs
      361 idggglkfdl fssdykhrls vftsaqntdr dsyygtaqdp naygkttdlt fmagtqyays
      421 fdkflfmpsd ltagleynyd hlkdemigyn rytnqkvhie slflqnewkn kmwsflvgar
      481 mdkhnmidnv ifspranvrf nptedinira syssgfrapq afdedmhisa vggeiamiqr
      541 akdlkeeksq slstsvdfyh rfkngiqtnf liegfytsls dvfvledigk deqgniiker
      601 rngsgakvmg ltlegksvls swlslqagit lqrsrynepe kwsdnenvpt erkmfrtpnt
      661 ygyftstltp lkhftaalsg tytgsmlvqh lagyipidka vktpdffdmn iklsydfhiy
      721 kdinlevnag vqnifeayqs dfdqgrkrds ayiygpaapr syfagvkisy
//
LOCUS       WP_010800749             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Parabacteroides].
ACCESSION   WP_010800749
VERSION     WP_010800749.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..254
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27658
     Region          3..254
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgkiialanq kggvgktttt inlaaslaal ekkvlvvdad pqanassglg vdirsvelsi
       61 yeclvnseda kgaiipteve gldiipshid lvgaeiemln menreqilkq ilvplkdmyd
      121 filidcspsl glitvnalta adsvmipvqc eyfalegisk llntikiiks klnpaleieg
      181 flltmydsrl rlanqiyeev krpfrdlvft tviqrnvkls eassygkpvl lydaeskgal
      241 nhmqlaqeli dknk
//
LOCUS       WP_010800753             444 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF3575 domain-containing protein [Parabacteroides goldsteinii].
ACCESSION   WP_010800753
VERSION     WP_010800753.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides goldsteinii
  ORGANISM  Parabacteroides goldsteinii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13393515
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Parabacteroides goldsteinii"
                     /db_xref="taxon:328812"
     Protein         1..444
                     /product="DUF3575 domain-containing protein"
                     /calculated_mol_wt=51128
     Region          <30..109
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          271..433
                     /region_name="DUF3575"
                     /note="Protein of unknown function (DUF3575); pfam12099"
                     /db_xref="CDD:432330"
ORIGIN      
        1 mkrviivfhl ilfyfsisls aqdtnihrdt lfanikfrqg ysqldstfnd nqmhlnqlit
       61 lldstaldss lvlksitikg saspegstpm nrqlsekraq smkayivdht tlndfnikvd
      121 ssdvdwefls emiastdlpw rdeavkiian tpiwvfkdkk ivdgrkkqlc mlqgghawey
      181 msknffpalr arfrimcewe isrpannrgd ecktdeceti vnqpsteerl advgkdsvat
      241 slvpdmrntv stdslaftak sekdrkfvml lktnmlydvm aipnigieip itpkwsasan
      301 wmyawwsndt rhrfwriygg dvelrrwfsp rrdtrsllcg hhlglygqml tydiewggrg
      361 ylgdrwswav glsygyslpl gkhfnidftl gvgylegdym kyhpedgcyf wdsthrqkwf
      421 gptkaevsli wfiggrnqqk ggeq
//
LOCUS       WP_010800758             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Parabacteroides].
ACCESSION   WP_010800758
VERSION     WP_010800758.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..187
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21438
     Region          2..176
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdeqkwiksi lagdtksfsc lvvkyqqmaf tiafrilenr eeaedvvqda fvkmyralps
       61 fqfgskfstw fykivyntai taqrkqsvfd syddaiatdl ttsevdsata ileredrkei
      121 iarvlkklpa deslvlnlfy leecsiadig qitdltpsni kvklfrgrkh fyetlqlmmk
      181 netanvl
//
LOCUS       WP_010800792             150 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GatB/YqeY domain-containing protein
            [Parabacteroides].
ACCESSION   WP_010800792
VERSION     WP_010800792.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..150
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16087
     Region          1..149
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mdlfekvsed iknamkakdk valetlrnvk kffleaktap gandtltdad alkiiqklvk
       61 qgkdsaeiyt qqgrvdlaea elaqvkvlet ylpkqmtaee levevkaiia qvgaagpkdm
      121 gkvmgvaska lagkaegrai setvkrllns
//
LOCUS       WP_010800843             403 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Parabacteroides].
ACCESSION   WP_010800843
VERSION     WP_010800843.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..403
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44269
     Region          15..394
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(25..26,29..30,33,66,116..117,119..121,124,143,
                     146..147,150,227,230..231,234..236,239,266,270,327..328,
                     332,336,352,355..356,359..360,363)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mdsnnhvays kehirfavls fflaqglcfs swasripdik eiftvndaly wgivlfmipv
       61 gkfvaiplag ylvsklgsri mvqisimgya lslfaigtal niymlggglf cfgvfwnlcd
      121 islntqgigi erlygrtima sfhggwslaa clgaligfim ivsditpfwh ftliaalill
      181 ltmvsrrylq ddvftaevke eavedksekw qyikrpemll iklglvglfa lvvesamfdw
      241 sgvyfesvlq vpkslqigfl vfmvmmtvgr flanyayriw gkqrvlqlsg afifigffts
      301 allgstvdsm alkvivnsfg fmlvglgiss mvptiyslvg aksktpvgia ltilssisfi
      361 gslvapllig aisqafnmey aymvvgllgl cillmttfsk afr
//
LOCUS       WP_010800628             531 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: beta-N-acetylhexosaminidase [Parabacteroides].
ACCESSION   WP_010800628
VERSION     WP_010800628.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..531
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59647
     Region          1..525
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mktniltflc fvflcacqap pveeyaiipq pqeisytpgf fkmgnhpvis ysgdlnneag
       61 llqkalssdf slsatvkdtg kgdinlvldp avlpdkpegy qlevssgkve ikagtpagil
      121 ngvqtlrqii kekdgkymiq rasvsdypaf swrafmldeg ryfkgkdvvl klldemsqlk
      181 mntfhwhltn dqgwrieikk ypklteigaf rdsseinhfg sdvydgkrhg gfytqedike
      241 ivdyaskrhi tivpevsmpg hasaaiasyp wlgtsgkqik vpgkfgvhye vlnvsdpkvl
      301 qflddvtnev ialfpspvfh iggdevkydq wkaspairsy makkglktpa elqiyftnei
      361 snmlavkgkr mmgwneitgd klheyqseed tkeaeqqlak gtivhfwkgd palikktidk
      421 gydvvnsyhe ytyvdynyes iplskayafn pvpeglspee qsrvlglgcq mwgefiptve
      481 smnrltypri aayaetgwsg sdkkdynrfl ksldyfknkw aaegivigpt e
//
LOCUS       WP_010800885             525 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Parabacteroides].
ACCESSION   WP_010800885
VERSION     WP_010800885.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18415305
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..525
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=59578
     Region          48..284
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          54..80
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(56..57,60..61,63,87,90..91,94..95,97..98,121,
                     124..125,128..129,132)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          85..115
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          120..144
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          156..183
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          190..219
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          226..249
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          227..364
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
ORIGIN      
        1 mmhkytvlll lsvlslmgqa qslsfqelln kkkftevial adsltpadsa dyvtmsaigq
       61 ayegvleyne ayrcyqhclq mdttnvdals svarvamnlg kasvaqdcfr kvlesdstdf
      121 yanyqlarly sqigdyenav lqfnvlrdqd ttkvnpviyr niadcymkmn aipaaticyf
      181 qaynvnrena glasalvncl yrmggpniqd glsicdtalf ynpgnhalrr skamgfymnk
      241 qyaqadtlyg elfaegdtsf ltlkyggasr ylagramdai dllewaygkd ttdvetnlll
      301 gaalgktydr krafllfdqa eklmqpneal vnmlltsrse tlfkdgrqre aegllykawl
      361 ankdrldllf riereysnwg peyksaedlg ralfakvtfl reyfltgkkm qgfqryrsil
      421 qylyedafft nktelvmiap dnkkskisae dlksiidrlp disqlpever khyqqmeevf
      481 kkrkengvgs tksepldens eafkagmkaa qkyldsqkke eqkse
//
LOCUS       WP_010800918             564 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010800918
VERSION     WP_010800918.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..564
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=65202
     Region          39..489
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          273..562
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkqiivyigv aavlsltacn dsflerspqs indktfwntp sdleayvnnf yswlpsgvts
       61 iadgesddqv pngisqyfwg qyttptpeas swcnwskgaw epirltnyfm thyktvvgse
      121 adinkyvgen rffralqyag lmrtfgdlpw vdkelgtdsp elydaklkry eimdkiiedf
      181 dfaiqwlpek paagrigkdv arhlkartcl heatyyryht elgwqdkaer llklaadetd
      241 aiinsgryei yntgkpekdy yemfvmedkt nlkeailpvt yldgkrkhgm srtlweantg
      301 fskdfmegyl ckdgkpisls syykgddnmr netadrdprl kqtvltwdfp trvtvstnds
      361 tfiteeskfi dqycytgyks ikyfiptdka feannntydg iayryaetll inaeakaelg
      421 tisqvdldkt invlrdrvgm phlttnvgft dpnwtkwgye lspllqeirr errvelageg
      481 rrwddlmrwk agkicdnikt yvgkrqpekd gkyaivypny tnedysyeag ksrtwddrly
      541 lrpiptaelq rnpnllpqnp gwdk
//
LOCUS       WP_010800929             638 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010800929
VERSION     WP_010800929.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..638
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=73021
     Region          98..>278
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          355..638
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mksiyqyliy ictafsiasc nyldvvpdnv ptldnafsdr ytaeqylatc ywgmpksagw
       61 nenpgifgsl emifnkegst sggmkfglgt dsptsaliny wggtgsmirs lyagirecnt
      121 fmegivgvkd lnqyeikrmi aevklikaym hfylltyygp icplrenipv nestqgvrvy
      181 rekvddcfay ilelldevie gdplplvien qtselgrfar paaymlkakv lvywasplfn
      241 gntdynsfrn yngepffnqt ydetrwqkaa eackeavdic esagirlyqi sdyiatktls
      301 detqlvqtlr gsvsdrwnce lvwgnssypv nsglqgecic yleqatslny gtrmsvsmat
      361 veqfyskngv pieedkeydy snrfnvrtgd edhkyyiqkg eqtaamnfdr eprfystlgf
      421 drgkwygnsy knvpdddaec lypknrfgef ssvanpgnyn atgywpkklv sinssfrnan
      481 diswenyafp dmrfadllll caealneskd apdaevykyv dmvreraglk gvveswqkys
      541 nqankpstkv gmreiiqrer kielacegvy ywdsrrwkta qkeqnrliqg wnvnakevvd
      601 yytlttvytq sftyknyfap ipesdivnnp qlvqnpgw
//
LOCUS       WP_010800946             326 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010800946
VERSION     WP_010800946.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..326
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=37434
     Region          <126..324
                     /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"
ORIGIN      
        1 mehdytelvi gylqgnlske etdlfydwvn esasnketff eikamydagl flgkpldtas
       61 swqrllnkkk nsqtrrfnlw yqissyaava liavaissvf flfirdddkt lyskyiggdg
      121 leadvielpd gthvslgskt tfhydknfgk dkrivylege ayfevakqkn kpfivktkeq
      181 diealgtkfn vmaypmdsmt ittllegsvr lttmhiakqt ilesnqqfvy nrntesailr
      241 kvdarqfvsw tsgyyyfheq slkaildrls hvygvefavs sktlnkrtft gtfyrgqsik
      301 dimeiinlsi pvkykiddhh vtiser
//
LOCUS       WP_010801121             328 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010801121
VERSION     WP_010801121.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..328
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=37705
     Region          75..323
                     /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"
ORIGIN      
        1 mnedlliqyl shrctpaeir eldkwiaadq anadwlfeme riwglkdelr fsdkkeieta
       61 yirfiselqk kevtheprtr sfsffwikya vaavliglls vniyiqlqde paqmnvvevp
      121 ggqrvsltls dgtkvwlnsr tkftyptrfs skersvtllg egffevahne kspftvhvdl
      181 lkvkvlgtkf nvkayeness fvtladgkve vvtndnehkv tmkpdqqvay skknglvind
      241 kvdtnviksw tlgeaayinq rldeivnele rkfnvrieit dqelsaeift crfketatig
      301 qvmallkdtr kldyrihgdq ikicnptk
//
LOCUS       WP_010801122             504 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Parabacteroides].
ACCESSION   WP_010801122
VERSION     WP_010801122.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..504
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56490
     Region          38..344
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtnisrrtfi ktgafaaagl tivpghvlgr sfgftapsdk lniagigvgg mgrrnlanms
       61 tenivalcdv dwhyadktfk dypnarrfkd wrvmfdeigs sidavmvatp dhthagvtah
      121 aitlgkhcyt qkplthsvye srlltrlakk ykvatqmgnq gnsfdwcrqv aewiqsgiig
      181 dvyevhcwtd rpiwpqglqe pktvvkcpkt ldwdlfigpa rkrpynpvyt pwnwrgwwdf
      241 gtgalgdmac himdplywal dlkyptsvig sstlsnlysp phaqvvtytf parpskgnvk
      301 mpevkvywyd gglmpprpee lkdgemmgde nggiifvgtk gkimtgcygm nptllpfsam
      361 enfnqpkpti prvkggngdi wntnaheqdw irackepags rteassnfqf sgpfnemvvm
      421 gvlavrlsgl yglhrelqwd genmrftnis pndkikivtv ddfkvidgdp rfdrryadfs
      481 aadmasewir htyengfslp dmpe
//
LOCUS       WP_010800503             466 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: C1 family peptidase [Parabacteroides].
ACCESSION   WP_010800503
VERSION     WP_010800503.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Nagler,D.K. and Menard,R.
  TITLE     Family C1 cysteine proteases: biological diversity or redundancy?
  JOURNAL   Biol Chem 384 (6), 837-843 (2003)
   PUBMED   12887050
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of cysteine peptidases
  JOURNAL   Methods Enzymol 244, 461-486 (1994)
   PUBMED   7845226
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..466
                     /product="C1 family peptidase"
                     /EC_number="3.4.22.-"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53068
     Region          28..462
                     /region_name="Peptidase_C1B"
                     /note="Peptidase C1B subfamily (MEROPS database
                     nomenclature); composed of eukaryotic bleomycin hydrolases
                     (BH) and bacterial aminopeptidases C (pepC). The proteins
                     of this subfamily contain a large insert relative to the
                     C1A peptidase (papain) subfamily. BH is...; cd00585"
                     /db_xref="CDD:238328"
     Site            order(65,72,74..76,185..186,250,252,254,260,403)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238328"
     Site            order(87,93,386,408)
                     /site_type="active"
                     /db_xref="CDD:238328"
     Site            462
                     /site_type="active"
                     /note="G bulge [active]"
                     /db_xref="CDD:238328"
ORIGIN      
        1 mkrnnlwitt lalgialsay gqqadggisa emlqqikqsy kgtptdkaih naisnndink
       61 lavnaesknn fdtyfshkvn gkgitnqkss grcwlftgln vfraqaiaky nmgdfqfsqn
      121 ysffwdqlek anlflqgiid trekpmddkm vewlfknpls dggqftgisd ilgkygvvps
      181 dvmvetnsse stgrmanlis lklkefglql rdqsakgakv aaleknktem lgtiyrmlvl
      241 nlgepptkft wtrkdakgdp vetkeytpqs ffdeyigkdl tnnyvmlmnd psreyyklye
      301 idfdrhrydg knwtyvnlpi edikemaias ikdstmmyfs cdvgkffdre rglldvnyyd
      361 ygslmgttfg mdkkqriqtf asgsshamtl mavdldsngq pkkwmvensw gpgannghli
      421 mtdewfneym frlvvdkkyi tdkvknvlkq tptrlpawdp mfaden
//
LOCUS       WP_010801155            1052 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Parabacteroides].
ACCESSION   WP_010801155
VERSION     WP_010801155.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..1052
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114758
     Region          3..1047
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mknivkfavs npvticmvvl ailllgkisy dqlsvdllpd lnnprlfiel kagerppeei
       61 ekqfvknmes mairqsdvtq vssvvkagsa ritveytwtk dmdeafldlq kamnpfaqnk
      121 ditelkitqh dpnqspvili gmshqnitdm aelrkvaesy irnelirleg vaevtlsgqe
      181 estltirtdp ykldafglki ediasriean nqsisggrvs elglqylvks sslfgseedf
      241 enlivgykqv akqetgtnas agtatasgdk aplflrevat vtfenarpdn ivringkrsi
      301 glsiykemry ntvkvvdgvs rqlgvieqal pgyqfkvitn qgtfiknaig evkdsavlgi
      361 vlavvvlfvf lrrfgttliv smaipisiva tfnlmffngl tlnimtlggl algagmlvdn
      421 aivviesifr nqekglsire aairgtseva gaviastltt ivvflpivyl hgasgelfkd
      481 qawtvtfslv sslfvailvi pmlydrlmnt ppapsregsr ipsdakkeag neagrgiqll
      541 gyshllrsli ghrwivisaa vglmvltvfl lpfigtefmp rmeskaftvv vkmpegtkle
      601 rtssavanle ellytitgds lltvyshige gsgsenaife gentammkvv lssecrvape
      661 avieqfvhta enpdglelti kqeenslssl lgsegapivv evkgeeldei aditeevksr
      721 mqevpglyni vssiedgape itisinrtia ginnlsvstv ieqlkqqlsg keagkmeyrg
      781 emrdivikvp diplralgdl vikngeqefr lreiatfges qapkeiyrrn qnriskiman
      841 mdagksldkv aeeirqamkg ielpvnysvt vtgeeekrqe smnsllfala lsvilvymvl
      901 asqfesllhp ftilltipla vvgaillffl tgttinmmgv igivmlvgia vnnsiilvdr
      961 inqlkadgtg ltdaivqagq qrirpiimtt lttilallpm tfsfgegasl rspmaiavig
     1021 glvtstlmsl mvipcvyyvl erlknswnrg nk
//
LOCUS       WP_010801157             498 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Parabacteroides].
ACCESSION   WP_010801157
VERSION     WP_010801157.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..498
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57741
     Region          153..475
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mqrelvwmkk milvvvllsg iplfshgqls ltiekaldia eensptlrrs hmnldryqet
       61 liaqraslks kfslnlnpld ysknrsfdnr lsqwytnekl stsgtfrvdq pilwtdgeis
      121 lintfgwqdn nsnidgdkns nkafnnnlyl qlsqpiftyn krkmelkqie ydyenahisy
      181 alqrlntekd itnqfysvym aqsqlaitre elvnaqqsyd iiknkveadl sakdelfqae
      241 lnlatarssv eeqqvslena kdklkqalgm nldddlmvfa eidikpidvn lqqaiahgle
      301 srlelrqrei eseeldfqmi ktkalnefkg dislsfglig dnkrfqniye nptqnprvai
      361 sftvpifdwg ekkarvraqk vaqninkldf hedkvdieln irqvwrslen lrtqieiaeq
      421 nvlnaqrtyd lnltryregd ltgmemsqfq tqlsnkkisy tqalinykie llnlkilsly
      481 dfelnapivp mkdfisek
//
LOCUS       WP_010801163             829 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: T9SS type A sorting domain-containing protein
            [Parabacteroides].
ACCESSION   WP_010801163
VERSION     WP_010801163.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..829
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=92075
     Region          237..435
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
     Region          763..829
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 mnryrlfyhc iyisiiclfl fcpgkaksqi seggkpvsfn yqnplkswqp avqipvnfsv
       61 edriavdewr vsqgaplavs alidtdlnme nagewrvlpg gekiwqlrlq akgaialmly
      121 yetfylpegg klfiynaekt hllgaytsqt npdgksfate fvagddiile yeppvsdeka
      181 riainqigyg ynhlhvttdl rstgpgtsgs cmvninceeg eewqhekngv cmmvekigka
      241 gylcsgslvn ntakdmkpyi lsafhctqdy dngttasetd lnqwvfyfhf ehtgcenasp
      301 iaghktmtgc rrivsipieg gsdgllllln dkipaeynvy fngwdrseta tssgvnihhp
      361 sgdymkistf gnhpvktttw idnlskagal nahwnvifdk ttnghsiteg gssgsplfne
      421 nkqivgtltg gnstcrltsg nnlygkfsyh wdkysqadtg rmdiwldpln tgattipgls
      481 qtgeegslin yksptnvtaq sissnnvliq wnapvytqli swgtqnsdaq igyhgtpfyf
      541 gqrweskeli nihkkklvnv kfipvysvny aifikqgert yqqeitnlta nrsntielkt
      601 pytidanqdl ivsiyarkyg rsvypafvdn gpavngkgnl vsfdgnewey lldeefninf
      661 ilsatvtsee geptlplpaa nsdiqipafp aitgyniykd qmllasvpas tlqhtdknvt
      721 ggkhdysvsa lydskesraa tataetnvnt esiqettdfh itpaifkdri qinnyqqvks
      781 leiyssdgkl irkltdpaew ietgnlpqgv yffklsndkt fktirgikq
//
LOCUS       WP_010801250             715 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GH92 family glycosyl hydrolase [Parabacteroides].
ACCESSION   WP_010801250
VERSION     WP_010801250.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..715
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=81444
     Region          1..713
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mknsffagll sltimiscqp dkqltnyvnp llgtatlwet kdlgyerhlk trtwgaevfp
       61 gssvpnamvq lspvtqfrsg agyqyedtvi ygfshtnkgh wnllhlpvlp vtgnvssgdy
      121 astyshsnes arpgyyqvfl erygvnaelt stlrcayhky tfrpdddkkv lvditrtnng
      181 vrdwsiqkvd dytfsgnqda egnirfyavs nykiedirql kdgehevsvv sfadskgskp
      241 lelkigfsfv sidnakmnle qemkdksfvq vrkeadktwe nllskievtg gterekgify
      301 sclyrsflwp alrsdvngey tdakgnvvnn gfryytdpsf wddyrnklil lgmispdvtt
      361 dviksitdkg ekrngymptf fhgdhasvfv agnylrglkd fdlnraykll vnnatvpgkg
      421 grpyldeyie qgwiaekdtt nvptwdeyka avtktveyay ddyatallak elgdesiykt
      481 lmersgnykn lfdpgtgfwr gkiadgswik dfdpyypyya ymyreanawq slffaphdpe
      541 gmialypgek aveqkldslf tepwrnyeah nmtgfignyc hgnqpdhsvp ytyyfigkqe
      601 kaqcvldsim nhyydmgkek laysgmddag emsawyvfna iglytyspad peyivtvplf
      661 dqvkftlgdn nqfaivkngn grkitdisyd gqkikgwfis hdllkqgkql titte
//
LOCUS       WP_010801268             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010801268
VERSION     WP_010801268.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..321
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=37167
     Region          66..315
                     /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"
ORIGIN      
        1 mneqldkyfl gelsdtekkd lfdqiesspe kkaefirmqn tvtisklgeq ngddkwaslk
       61 ieelgsrinr kqarrlylnl akyaavvail liniwlltdk fipeekaply tkievpkgqr
      121 ifmtlqdgte awlsprsvik ipnefskder sveldgegff svtkdskrpf ivktqrydik
      181 vlgtrfnvfa yseserfetn lvkgsvqvtn nskpeeniil kpnemvslsn gnliktaasf
      241 nneeylksgi fyfsnkkfse ildyltlwyn vkfdvkssar idqyvsgkfr qsdeierilk
      301 alqgvhhfqy kiinneeiei y
//
LOCUS       WP_010801280             457 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar porter family MFS transporter
            [Parabacteroides].
ACCESSION   WP_010801280
VERSION     WP_010801280.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..457
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50304
     Region          10..442
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(22,142,145,149,271..272,276..277,280..281,366,
                     370..371,375,398..399,402)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 mkrttaylll iclvsamggl lfgydwvvig gakifyepff glegsaalrg wamssaligc
       61 lagallsgew sdkygrkkml iiasflfvls aygtgavdsf nwfiiyrivg gfgigiasni
      121 spvyiaevap asvrgkfvsl nqltivlgil maqlanwqig eyftqggetl sansiewawr
      181 wmfwaelipa glffilsfii pesprwlatv qkttqarail lriggeqyad qtldelaqlt
      241 dkkeekvnwg allkpgvrnv liigivlaif qqwcginvif nyaheifsea gyavsdvlmn
      301 ivvtgvtnvi ftfvaiytvd kwgrrslmfv gsaglaviyg ilgtcyffev sgwpmlllvv
      361 maiacyamsl apvvwvvlse ifpvrirgma maistfflwa acflltytfp ilneavgasg
      421 tfwlygaicl sgfffirakl petkgktlee lekeltk
//
LOCUS       WP_010801282             928 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 2 protein
            [Parabacteroides].
ACCESSION   WP_010801282
VERSION     WP_010801282.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 928)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 928)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..928
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=104135
     Region          29..>484
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mlkfflsici tlmlltscqk psseislagk wqfamdstdv gitekwfers fadkiqlpgt
       61 tdeagygipn tlppsvekpq ilhltrknsy vgpawysrev sipsdwggks ielklerviw
      121 qtsvwvddnp vqgsceslis phrfdltgyl tpgkhkltir vdnrkqhdit vndmahaytn
      181 etqimwngii gdisliakea lsiedlqvyp dvsgkqirik gkvsntgeat egslsikven
      241 qksglvvsal kqkvdfqsge nlvnltcsmg dsiemwnefn pvlykvdlev nagsvkters
      301 tkfgmrefsr nqsdlllngn kvflrgtlec cifpltgrpp mepegwkkvf ltarewglnh
      361 lrfhswcppe aafqvadslg fylqvelplw svkvgedsht ndflyaeadr ilaeygnhps
      421 fcffslgnel qpdfeflsrl lkhtkeqdpr hlytttsftf erghgdwpep dddffitqwt
      481 kkgwvrgqgv fdsqspsfdk dyiasvegmn vplvtheigq ysvfpnlkei gkytgvldpl
      541 nfkgvkqele kkglldkadd ylkasgylaa ilykeeiera mktagcsgfq lldlhdfpgq
      601 gtalvgllda fwdskgvtda etfrqacspv tplvrfpkav ytsgesftas vevanftdke
      661 lkdqsvswil kdekgkeigk gmmscpslsi glnrlpeait cslaqqeaar lllsvaldnt
      721 pyknewsiwv ypsqlnpvkd dvvvtrdlre tqkaladgkk vlynpdykki eglegkfvpv
      781 fwspvhfpkq agsmgilcda shpafahfpt gnytdwqwws llkqsktivm dtlpsvtplv
      841 evvdnfannr rlsnlfeakv gegkllfcsm dilsdweqrp earqlyfsll eymksdsfdp
      901 ssamesdvla qllksglssg asnpediy
//
LOCUS       WP_010801305             169 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Parabacteroides].
ACCESSION   WP_010801305
VERSION     WP_010801305.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..169
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19355
     Region          14..167
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdslqfqqkl igiqdrlmnf alkltanred aldllqdttl kvlnsqekft dnvnfagwvm
       61 vimrnlfinn yhkmvraqts vdqnvdlynl nitcdsisgs pdkiyqikei tkaiaalned
      121 ykipfslfvn gykyqeiadk lnlplgtvks riffarkelq skldgfqya
//
LOCUS       WP_010801309             111 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system RelE/ParE family toxin
            [Parabacteroides].
ACCESSION   WP_010801309
VERSION     WP_010801309.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..111
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12906
     Region          20..97
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 megtkkkpvv vsllffssvd qifeygkinf gekkaieyen liyetvrqlt sgyllnaeyp
       61 ylptkdkryr railpahfil yritkdriev lnilhqavsi tqakknrnik p
//
LOCUS       WP_010801353             430 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleotide sugar dehydrogenase [Parabacteroides].
ACCESSION   WP_010801353
VERSION     WP_010801353.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..430
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=47564
     Region          5..422
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mdkmriaiig lgyvglplar lfatkysvvg fdvkqervsa lslgedttke vseeslksvl
       61 sdhlpeeget glyftsdped lvscnyyvva vptpvdthhs pdltplyras etvgkvlkkg
      121 diviyestvc pgiteeecvp ilaktsglvy nedffagysp erinpgdkeh tvekimkvts
      181 gstpdaaekv dalyrsvita gtfpvssirv aeaskvient qrdiniafvn elskifhlld
      241 idtnevlaaa gtkwnflpfr pglvgghcig vdpyylirka qdygyhpgli lygrrindtm
      301 geyianrvvk cmikkdvpvk naevlvlgft fkencpdvrn tkvgdvvrvl kdyginvsvy
      361 dpwaraeevr deygieltgs lskgrkydvi vlavahkefl eldipslvse nhvvydvkgc
      421 lnpewvddrl
//
LOCUS       WP_010801406             752 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GH92 family glycosyl hydrolase [Parabacteroides].
ACCESSION   WP_010801406
VERSION     WP_010801406.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..752
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=84297
     Region          1..750
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mkktilffqv vlvcllvgck papnsgllsd eikyvdpfig tgfhghtfpg atrpfamvqv
       61 spdthimgwd assgyhyddc eiygfshthl sgtgigdlgd vallpfsggd sikpvglfnk
      121 dtekatpgyy avrldnfgvn veltstdkvg fhkytydnpk drrvmldlgh ilqpnwghkl
      181 vdnsylfvnd stvegtvrtq gwahfhsvsy ritfsepiet vyqyiggklr qdslflrint
      241 eedlkfhykf pekaeplyvk valsmvdtdg aeknleaelp gwdfeatrik saeiwndaln
      301 aieiqsadpt vmvnfytaly htmiapfayq dvdgrylgmd kkvhkaepgy vnysvfslwd
      361 tfralhplmt iinpelaadw gkvlvqgyke ggilpkwpla ssytgcmvgy pavsvladlv
      421 skdladgdlk twaeagarss vyredlaekf kgtreldlit lhpyfkekyg fvpadsvpes
      481 vswglemaye dwcisqiaak agldslaqay aakgeyykry ldpetkmmrp imsdgsfrtp
      541 fnprysahmr sdytegnafq wsffaphdmd nfiatiggkk eletrldtlf ttssqvdgeh
      601 asgditglig qyahgnepsh hmaylynwtd spwkgqerld yimrefytnk pdgiignedc
      661 gqmsawyvms algfyqvapg ipvytlgrpm vdralihvkg gifeivvknn spenkyirtv
      721 tlngkeletp ffshaemakg gklvfemtnt hp
//
LOCUS       WP_010801414             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Parabacteroides].
ACCESSION   WP_010801414
VERSION     WP_010801414.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..190
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22472
     Region          1..179
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mleerrllke ltegsefsfn alynlwasrl yhfafsylks dsaakdvvqe tfvkiwsnrt
       61 sinpdasfka ylftisyhfl lkelrrqlnh pqmedyldfk kdlistdnve akydfdlflk
      121 elevakqklt prqreifvln keynlsvtei asrlsiteqv vrnqlsaalk vlrnelsnys
      181 ylfilftiyf
//
LOCUS       WP_010801436             332 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010801436
VERSION     WP_010801436.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..332
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=37592
     Region          87..331
                     /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"
ORIGIN      
        1 mvqienyiqs flngtldaeg hvtlkqwike apenrtyfhd tvavwkaggi vsnaddfnve
       61 kaiskfkken kssnrinfyk yafrvsavai vfllcgissl fflwqsekta veaveeykey
      121 vvevpagaks kvtfpdgsvv wlnagskvky dsnfakesrn valsgegyfe vskneelpfv
      181 vntgnlsvkv lgtkfnlksy eedsevkvtl kegavrvgdf ladaapvvlk pnqrftlrka
      241 dlamqvdlvd ashienwrng amifdkvsle eiakelqrly dipvriekes lkrivyysdf
      301 qenvtvekvl eilssgnkfr yevkpeliri yk
//
LOCUS       WP_010801438             547 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010801438
VERSION     WP_010801438.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 547)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 547)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..547
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=61155
     Region          69..497
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          276..546
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkrviniila sallvgstts csdflqkdpp sspsqsifwq kksdfdsala gsfsmmyewp
       61 gvmsqivacf dnltdnsicq hnestygssq tialgdldpn tggyvsymyd hcyrgiarih
      121 lvmenletyq gadmseadks fimaqckalr ayyyswlyqc yrevplvtss lttenmyqpk
      181 atraevyaqi ikdfdeaiaa lpdkpysdsq msgyftpgam kafkarlmla eayddngnad
      241 askmgaivtl legiqgyela drmrdnfisa qqlaspeimf svrylapntt hsmdlyygaw
      301 ttcgvtrdlv nafectdglk wgespltatv desllatgal sdankaerek lfsgtngvhi
      361 rdrrlyetvc hsgvalfpde gyeengpiti tnqmqtgfgm mkllqpttem psystisdad
      421 vvilryaevl mmiaeaenea ngptqkvyda vnkvrvrsgq pelpagltkd qmrerirnew
      481 rvefvfeghr yfqlkrwklm dklvngasdp alptyvkvfk pafyyfplpq seidkaggvl
      541 vqdpnyk
//
LOCUS       WP_010801508             456 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Parabacteroides].
ACCESSION   WP_010801508
VERSION     WP_010801508.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..456
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49421
     Region          61..455
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mknniillsv atlsllsgcg iyksyqpets vpdnlfreea pvtdttnign ldwrelftdp
       61 qlqaliekgl enntdlrtah lrvqeaeaal mtsrlaylpa lnltpqgtis sfdgskaaks
      121 yqlaasaswe idifgrltna krsaqaaleq tksykqavrt qliatiansy ytlllldkql
      181 visertaslw kenvqamqal kkaglaneaa vsqseansls veaslltlrq qinemensls
      241 nllgevpqrv ergnldrqef petlstgvpl allgnrpdvr qaeyslaqaf yttngarsaf
      301 ypninlsgva gwtnsgggii anpgglllqa igsltqplfn kganiaqlki akaqqeeasl
      361 afqqsilnag sevnnaltqw qtargritla drqivslqka vkstqllmdh gnitylevlt
      421 aqqsllqael sqaadrfdei qgvinlyhal gggqee
//
LOCUS       WP_010801502             629 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010801502
VERSION     WP_010801502.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 629)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 629)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..629
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=71618
     Region          102..544
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          303..628
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkkiiyslmi maglaampgc nddfmehspk dslteetvfs tystfktyaw glynvftngn
       61 mlrrpgtggs yasavsyqgd inagylmrrl gsgnsyafqt itdaasgngw nfsfvrnanl
      121 mldnidnssm sdvdkehwrs vgyffrayyy meliarfgdv pwvehilgds dtevaygprt
      181 prkevadkvl enllyaeqhi kpegdgdnti nvhvvralis rfalfegtwr kyhelgdyek
      241 yfdacikase slmaayptvh ssfgemltsd lagvpgvily qeyvpkiftn yvlthverts
      301 thnvempqhi vdmylcedgk pistsssyew gktdktmyst frhrdyrlle tvappykvvr
      361 knnnnsweyt dnpadkeymd lmgittytgy gggngeagkh kvfplmnwsa svlegiphfs
      421 tnnwgqgfiv arsgnyvyry ynvwddsren qgttdvplfk ieevllnyae akfekgefnq
      481 gvadatinkl rvrakiasmt vseindsfdl ardpsvapvl weirrermve lmgegfgfyd
      541 irrwkkaewf vnkvqygqwa tkeqignsgq fidlntgfad asgktegyvy myndpvktgk
      601 gwlekyylyq iptneialnp nlkqnpgwn
//
LOCUS       WP_010801503             357 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RluA family pseudouridine synthase [Parabacteroides].
ACCESSION   WP_010801503
VERSION     WP_010801503.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..357
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=40852
     Region          43..120
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(43,55..56,58..59,61..62,65..66,68,75..76,77..81,83)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          110..347
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mdeffdemdd eqvddlleqn eedvprlyeh frfvadrgqs llrvdkflvd rmmgatrnri
       61 qlaadagcim angkpvksny rvkpedvvti mmsrprrdla iipenipiki iyedddllvv
      121 dkpaglvvhp ghgnytgtlv nalawylkdd ptydpndpal glvhridkdt sgllvvakkp
      181 eakahlsmqf fnkttkreyr alvwgivkdd egriegnigr dprdrmqmtv fpegdqgkta
      241 vthysvlerl gyvtlvkcrl etgrthqirv hmkyightlf nderyggnei lkgttftryk
      301 qfvqncfaic prqalhaktl gfvhpttgee mffdseipad mtqliekwrv yantkei
//
LOCUS       WP_010801541             409 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Parabacteroides].
ACCESSION   WP_010801541
VERSION     WP_010801541.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..409
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=47576
     Region          10..405
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 midkthfkre yikrpvyter ikpflgkdii kiligqrrvg ksyimyqlmd yientlpdsh
       61 iiyinrelkp hefiqtdddl yqyahsnlqe gkknflfide vqeiqrfeya lrsllaegvc
      121 ditctgsnas mlsgelathl agryiefpih slgyeeflrf fnlddnnqsl ykyltiggmp
      181 ylrvigteea yafeylrnvy stillkdvva renirnvsfl ndlveyladn ignlfsasni
      241 skylksqrtt vstqtvlnyl npllnaffih kvsrldingl kifeigdkyy fedlglrnvi
      301 rgcdlnkdiq kllenavylh llcsgydvkv gqqgnyeidf vgikngsriy iqvaylilde
      361 ktrerefgnl mnipdhypky vismdefnag tndkgikqlh vrdflkmei
//
LOCUS       WP_010801577             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Parabacteroides].
ACCESSION   WP_010801577
VERSION     WP_010801577.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..182
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20565
     Region          2..173
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdeqlliagc krgeswarke vyelyapamm svcmryvnnr etardllqdg fikiftkigs
       61 ytgtgafpgw vrrvfvttal eylrkndair lsvnfddcgd ladevdvsal drlsaddlha
      121 ciarlpngyr tvfnlyaieg yshseiaeml hisevtsrtq firarkvlqk svqslimhed
      181 aq
//
LOCUS       WP_010801579             421 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LVIVD repeat-containing protein [Parabacteroides].
ACCESSION   WP_010801579
VERSION     WP_010801579.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Adindla,S., Inampudi,K.K. and Guruprasad,L.
  TITLE     Cell surface proteins in archaeal and bacterial genomes comprising
            'LVIVD', 'RIVW' and 'LGxL' tandem sequence repeats are predicted to
            fold as beta-propeller
  JOURNAL   Int J Biol Macromol 41 (4), 454-468 (2007)
   PUBMED   17681373
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..421
                     /product="LVIVD repeat-containing protein"
                     /calculated_mol_wt=46920
     Region          61..407
                     /region_name="COG5276"
                     /note="Uncharacterized secreted protein, contains LVIVD
                     repeats, choice-of-anchor domain [Function unknown]"
                     /db_xref="CDD:444087"
     Region          63..97
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          103..136
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          294..337
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          384..417
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
ORIGIN      
        1 mkklmslfcv sliclfcgcn ddmkvretit ytvnkpvyms advfrssvkv ttqpeeitqk
       61 gkicfyegyl yvsergkgih iidnrnpssp asvgfielmg nadlairnnl lyadsyvdlv
      121 wfdisnpalp alknrlenvf lqsfppieeg iidsevfsea grakgvvvgw tqeevtetye
      181 yykdeiyynd mgaisesssg ggstgvngsm srfglykdyl yvvlnnqmdi fdlsgaepvv
      241 aaetipvgwn vetifsykdc mfmgtptgml iysvkdplkp eyqsslthvy gcdpvvvedd
      301 iayvtvhsgn ncgqnfneli iinvsdvkrp qpivsytmtk pkglgidngt lflcddglki
      361 ynandpqtlm anrlahysgm egydvipynn vlmmiaedgi yqydysdlee irllskiavk
      421 k
//
LOCUS       WP_010801625             432 aa            linear   BCT 01-JAN-2025
DEFINITION  S41 family peptidase [Parabacteroides goldsteinii].
ACCESSION   WP_010801625
VERSION     WP_010801625.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides goldsteinii
  ORGANISM  Parabacteroides goldsteinii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Parabacteroides goldsteinii"
                     /db_xref="taxon:328812"
     Protein         1..432
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49331
     Region          <183..426
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mskikiniwi latllallta crdeaddviq pgmlegkdtl teqfdiiwsg inqnyvfwei
       61 dptdwdavyt qyrprfeeld kkdtvptadl qklyeevcgt lidhhmnikv knlkpapgdq
      121 tdivsvhpgg mevlqredff ldipregfqv yrnklkaagr itndyefvnn npeanfdhlf
      181 tyvidndily lrfsnfaiie qiskadnpen teareakevy ceymnqlvfn qeikgvivdv
      241 rnngggilwd mftvlgpllk edihvldtkt kiglgrldyg ewnpfnaqvt tqrqvgemld
      301 wdgklpetnc igdrklvllt dnwsvsmsem taaavkqlpy atvigqrtfg glgplttkth
      361 tsfsgqfgdr nlentsyfvy tstwmsrthd geqlegigit pdipvkqdfe rftkqhiddq
      421 leyainflhg kk
//
LOCUS       WP_010801628             431 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Parabacteroides].
ACCESSION   WP_010801628
VERSION     WP_010801628.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..431
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45899
     Region          1..430
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mlkkllgfds ttmtlrtesi agittfltms yilavntsil sstgmdkgav ftatalatal
       61 stlllafmak lplaqapsmg inaffaftlv qgmgypwqva maalfvegli filitffnvr
      121 eivlnsipat lryaisvgig mfiafiglkn agiivsdpat fvtfgpftpv svlaltgill
      181 sgllvvkqvk galfysilic tligiplgvt tipegflpis tphslaptfc qfdfsqlftl
      241 dmaviiftll fmdmfdtigt lvaltyrigi vkengeipra ketmladaig stfgailgcs
      301 tittylesas gvaeggrsgf tslvtggmfl laiffapifl lipgaattgt lvlvgvfmme
      361 sitridmkni aealpafiti itmvltysva ngiilgmlcy vllklgmgrh revsptmyvl
      421 svlfllkfif t
//
LOCUS       WP_010801673             777 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Parabacteroides].
ACCESSION   WP_010801673
VERSION     WP_010801673.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 777)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 777)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 777)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..777
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=88516
     Region          5..401
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
     Region          407..777
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 miqhyltval rnllknkgqt lisaaglavg lfcfalctyl lrywmnedne fnnkkriaei
       61 vlvqddghlv sgtpaflgvd irnkqfpiie citratynnp enlsfeises ktlpyqlyvm
      121 etdtnfitvf drhlvcgdis ainkqpntll lsqsaakriy gdenpvgkkv igqdqkayti
      181 ggvfenfpan nsispyepie altlsvldgf leqqikertg cntyaltlpn fkpddldkql
      241 rdlnlrvllf dknpslvraf qlghtkyknt gyalfygfif liglliflss llnyysfitg
      301 nfynrtkefs irkgigedkk hlffllftes clslffttif alclvellap gfqfsffriq
      361 vdfdslslsg qiveyllgci mlsaiicgiv clrldrisli egihfsrhrv rntllgiqyf
      421 ialfflsgaa iatlqtrage qqlfsslnnd ekeriffvrt dyqymestyp vllskwkans
      481 miedilevhd klpntrinsy twengekqtl ggilyasanv gsflhlkpia gsllldeqsl
      541 linetfmnai kenpvnkivr innapkeyki ngvtsslirf vdgseyfasl aigllqkqgn
      601 cyvrlqpgke kegkayleqt vkeflpesiq peihtlkdec triqtterml rnvftffatv
      661 cliitllgiy aaisqdterr qkevairkin gaslknisyl fmkfylglll iatlfvfplm
      721 wmitdemlkn wiirfnynnp lfwlgiffvi tiftavvilv kilrtarinp advikae
//
LOCUS       WP_010801678             770 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Parabacteroides].
ACCESSION   WP_010801678
VERSION     WP_010801678.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 770)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 770)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 770)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..770
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=87550
     Region          5..380
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
     Region          401..770
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mlkhylkiai rnllkyrsqs fisifglaig ftcfalgtlw ihyemtydsf hkdadriylv
       61 rqkslisngg ltdtpkplaa slkqklpeie ascaiylrdy klvsngvqiq tnwisadssf
      121 mdlfgikils gnshflqvdn kewaiteala kklfgnespi gkeldivdse ekvkicavvn
      181 gwtghsnipf dliaspssrn nwaslshetf vklypntnid kfveklretk ieedsmplts
      241 lvvnpltslr yesprtptev kfnhillfsl agglvilcsl fnflmlfvtr iytrkkelal
      301 rqicgssykg llalfsiefl ilfftsllig mvlielvypf fkelaeihsn ktllltealc
      361 yagfvvlcsy ilvvvilgyl ryktlsfsik gatkgqgnsf frkscilfql iisfwiifcs
      421 fvivkqlhfl rntdigmtrk ncasiasypy qkeleqilsq ipgvteimpe qacllpynsr
      481 mslyitdwtd kkenaphvnl evicgvksla sfyelrllkg emvldddnsn dvmineaaak
      541 lfdwqdpigk sinsfkikgl ikdtynaspt tppnptlyis peksktqyyf spqsilfkyk
      601 egswnsikkk leeinqekkk edvhitihna meeyekylqs ektllkmlyf ttavcimisl
      661 fgvfslvtlt ceqrkkeiai rkvngatigs ilkiffyeyl lliavsaaia fpigylamrh
      721 wlesyvkqte inswiypllf isvglviaac isgkiwitak rnpaeiihse
//
LOCUS       WP_010801684             799 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Parabacteroides].
ACCESSION   WP_010801684
VERSION     WP_010801684.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 799)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 799)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 799)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..799
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92030
     Region          4..355
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
     Region          390..799
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkllilairp llrfrtytfv niiglalslt cfiiisryvy sewqtdhfyp dldrvfttic
       61 eddkhpgeim ycgisnpnke ktfnsllehp gvecaskirk eeeisywyne neylgktlia
      121 dsnffhiary pllvgtntls kpeeavitem larkifgnes algkqlrlsi gktvtitgvi
      181 gvpatassie fdlviseqls dwqrmsnhlv rlqpqadyrq inrqynqfml mkhwkysvry
      241 qlyplsevyl nrnnyenhff rlgnpthiyv lsmvalmill vgifnfiniy svvilkrgre
      301 wgmkkvfgag slmmfvqlyl envlmmafai llgwvfieva splvqnqmel tfvtnstfdl
      361 llnsgilfll plfttlmpfi ryrreapivs lrsvnrnggs vvsrklflva qyiititliv
      421 cslffikqlk fmldadpgfr ikdviasrff qprrinnisr edwekererk khlreviqqr
      481 ldaspliekw tygpspikdk msggfkfkvs dgefkeftlt fiapswlnlf nieviegkai
      541 dpkeepdldy glyltesgkk llgitdiqst dvqperrlwf ssgtdmdsnp pyrilgvvkd
      601 ftpghwgkft nppiiiphrs npeesllvip iaghkqevlh fleelhkelf ggsfeysfie
      661 dehkalyqkd rqltvvysvf aliailissl glfslslfdv qqryreiair kvngattsvv
      721 mrmllikyyk llgiaflias piawlainry ledfahkapv swwifavall itagislatl
      781 iwqirkaart npaeaikae
//
LOCUS       WP_010801752             122 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Bacteroidales].
ACCESSION   WP_010801752
VERSION     WP_010801752.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..122
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14141
     Region          1..122
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 meqltkreee vmnkfwerge atvkeiiaty peprpsrtai stfvkflvek gflghkpagn
       61 ngfiyyplie rdeycgnnlk nvvqryfnns irgvistlvr drkmsddevr elinqviegn
      121 rq
//
LOCUS       WP_010801756             250 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: inositol monophosphatase family protein
            [Bacteroidales].
ACCESSION   WP_010801756
VERSION     WP_010801756.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..250
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27489
     Region          26..250
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mdiqriislv ketkgiitnr emaalvkekg vadyvtqvdv avqdflkkal htlapdiqfl
       61 geetglqrmd tdsywildpv dgttnlmhdy qhsvvslalc sqkeivmgiv ydpfhdelfs
      121 avkeegsfln gkpihvssat klsetiigig takrelaken farflkvyen sqdvrrlgsa
      181 alelaytacg rqggyfeiyl npwdyaagml lvqeaggkvt dwngnaldpa kgshvvgtng
      241 qvheeilkll
//
LOCUS       WP_010801760             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Bacteroidales].
ACCESSION   WP_010801760
VERSION     WP_010801760.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23216
     Region          4..156
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 melketekrl ldavshiien dgftkigvnr iasqagcdkv liyryfggld gllvewakrh
       61 dyysfaysef idtikqsekk dirqivkdvl frqlhylkdn vlmqqllvwe lsghssfkgi
      121 leererigyk lqeelnksld igndndmsva iiisainyiv lftrqypkln gidfskpeaw
      181 srmeamisky vdfifddskl
//
LOCUS       WP_010801764             121 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Bacteroidales].
ACCESSION   WP_010801764
VERSION     WP_010801764.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..121
                     /product="VOC family protein"
                     /calculated_mol_wt=12851
     Region          1..118
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 miaffeiptn dfdksvafyq alfgeelevs qfgdermacl mkdgksvcsi ssapsfsgfa
       61 pseggvlvyl kardldadvk taidngatlv tpktkiqvdg wgsfaiiadp vgnriglygd
      121 k
//
LOCUS       WP_010801832             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010801832
VERSION     WP_010801832.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..222
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=25705
     Region          2..220
                     /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"
ORIGIN      
        1 mqteqtpial qtitvpagqr initladgtn vwlnarttiq ypitfneker lvkldgeayf
       61 dvtkdkskpf ivqtnnynve vlgtkfdvds yseteifett lmegsvkiss ltdaneslml
      121 tphnkaylhd gklrvkpvdd ytpyrwregl icfknetfas imkdfekyyg iniyitnkqv
      181 qkylytgkfr qtdgvdyalr vlqkdikfay erdddnhiiy ik
//
LOCUS       WP_010801893             376 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010801893
VERSION     WP_010801893.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..376
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=42988
     Region          <23..>79
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
     Region          <167..359
                     /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"
ORIGIN      
        1 mnndlvirfi erqctieear evlrwieate enkavfcqmq avhasigidh sdrtekvspe
       61 dvrkimkeis rkryrllpya aavvcavvav llfiisplne rnlseyekvl agiedkkeit
      121 ltvnndkeie lsdtsivvty dkkgqilind tvavpgeken ldhlnmirvp ygkrstlila
      181 dgskvylnsg sslvypavfa kdkrevyldg eayfevskea rrkfvvqtay kavevlgtkf
      241 nvsvdkrqsl feavlvtgki glesntgkie lipnqyygyd pdsgqdelkt vdtrdyiswi
      301 egrlrfnrep ldkvihrlek synikieild skylkyqisg nldlkstpee tmnvlmrili
      361 pgynsqkqkl yqikek
//
LOCUS       WP_010801908             789 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Parabacteroides].
ACCESSION   WP_010801908
VERSION     WP_010801908.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..789
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87922
     Region          34..123
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          108..649
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 myrtilflll fisplsqgka ysqkttgnqp sqtirgtvid kasghsmpdv timlsdmpgt
       61 gtttdergqf vlpeipvgrh nvqasflgye pgifseilvt sakevyldis lkenvnelse
      121 vvvrpqinke qplnkmaatg arilsveeas ryagglddpa rlvssfagva anlssngisi
      181 hgnaphllqw rmedveipnp nhfadisilg ggilsslssq vlgnsdfftg afpaeygnav
      241 sgvfdmklrn gnnrkmentf qvgilgidva segplsknhq asyifnyrys ttgllnsiyp
      301 gldmggtlny qdlnfkfnip trkagtfavw gtslidkyen dfeddplewe htrdnfqsta
      361 kqymaaggis hryffpnnam lkttlaatys gmnatedaha adhtvtpfty qknnttnltl
      421 tssynrkfsa rhtnqtgfty trlfynmrln lapfetapln tlskgkgqtd lisaytsssf
      481 gitdrlsvnv glncqvltln nswtleprlg mkwapttkss falayglhsr mekmdvyfvn
      541 skstgkesvn kdldftkahh lmltfgykls dnlllkvepy aqflydvpvi adssysvlnr
      601 refyveealv nkgkgrnigv ditleqylnr gfyylvtasv fdskykggdg vwhntrfnrr
      661 filntligke wmvgskrqni lsanakftlq ggeryspldh aaslahpdke alydetrays
      721 eqypvmfian ftvsykinrk kvahefaika lnvtgteeyy gyhynlksgv merngnsipi
      781 snisyklef
//
LOCUS       WP_010801931             586 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: S41 family peptidase [Parabacteroides].
ACCESSION   WP_010801931
VERSION     WP_010801931.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..586
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=65804
     Region          41..354
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mfkkvrrerl iglfclllla gsilpgqaqk dnrfevsknl difnalvkev emfyvdsvdv
       61 ektvrrgina mlsgldpytv yypeqdmdel kimttgeygg igsyirerkd ggvyiiepfe
      121 gmpaalaglk agdrilaidt vdtsnktsse vsellkgvpn tkmvlkiqrp nekkprevel
      181 vrkqilvdqv tyygvrgdgv gyiylkgftd ksaqevknal edlkknhqik slildlrnng
      241 ggllesatqi vgmfvpkgke vvstkgkvsq wdrtyrtsne pidtvmpmav lingnsasaa
      301 eivsgalqdm dravlvgqrs ygkglvqstr elpyegrlkv tmskyyipsg rciqqmdysh
      361 rkadgsvaai pdsltsvfyt skgrpvrdgg gvrpefeiee eemptimyyl vtdfvlvdfv
      421 tdwaqkhkti psveeftvsd edfeafknya keknftydrq sekilknlke vaqlegytdr
      481 dstiftelea rltpnldrdf dlykdqikkl laseivkryy fqkgellesl kddevldkai
      541 evlsnlelys ktlstpeege tkpadekads stkggdiayv fdktvg
//
LOCUS       WP_010801965             162 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: regulatory protein RecX [Parabacteroides].
ACCESSION   WP_010801965
VERSION     WP_010801965.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Ragone,S., Maman,J.D., Furnham,N. and Pellegrini,L.
  TITLE     Structural basis for inhibition of homologous recombination by the
            RecX protein
  JOURNAL   EMBO J 27 (16), 2259-2269 (2008)
   PUBMED   18650935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..162
                     /product="regulatory protein RecX"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /calculated_mol_wt=18866
     Region          2..154
                     /region_name="RecX"
                     /note="SOS response regulatory protein OraA/RecX,
                     interacts with RecA [Posttranslational modification,
                     protein turnover, chaperones]; COG2137"
                     /db_xref="CDD:441740"
ORIGIN      
        1 meqitepeml rraaaycsta erciqdvqkk ikaaglsqee geriiarllq ekfidehrfa
       61 ryfvndklrf nkwgrikiay elqkrnipap irsealegid ekeyadilqs llkakkkstk
      121 gkderdiyik llrfaagrgf esreasrclk qlfngndyee df
//
LOCUS       WP_010801935             634 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010801935
VERSION     WP_010801935.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 634)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 634)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..634
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=71402
     Region          82..>250
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          267..632
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkkifnlltl aavfgvatsc tdildtapnd klssgtmwtt eesvdqgvig vyyslqrpfh
       61 gnqiigadam igyygydafg mtgqgeygmq nlftksvnps ngfflktwqw mydgvhrana
      121 aiagienapi neakkarlia eckvlraffy drlnilfgng glgvplytep vnpsecdkpq
      181 sseqevwaqv ikdlsdaiae pnlpdnqiqg egrvskgaay alrgkayllt keydkaiadf
      241 akvgecgykl fpdykqlfkv anerceeiil avqyiedptg ygtgiqkyca aftqgakdsr
      301 gcwgdlqvtp alvnlyeevn gqtvkkfawe dylsdwkkvt dmetaeghtk yrkvffirdk
      361 fvngkeihst vtkavdtela klpaeiqaiy lpegnearlk tayanrdprl aynvvtpyan
      421 ylgvnsnsta eawytfrwpv agkyyadqan aepnanpelp sdyyasgfmn aqaefkyihr
      481 kfigegleyl rreqnpvdep iiryadvllm waealveknd lagamakvke vrdradiptm
      541 assfadqtia rnyvrderrr efvneginff demrwrtlke tkfsekvaqh awggtestgg
      601 tvydwigdqw ytwpvpkset elntnltptp gwey
//
LOCUS       WP_010801985             261 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Parabacteroides].
ACCESSION   WP_010801985
VERSION     WP_010801985.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..261
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29554
     Region          3..256
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mklidthnhl yledfdpeqd vlvnaaresg idtlllpnvd vetigrmhdl cdrfpdfayp
       61 mmglhptsvd gnyagnlktt esylgkrayc gigeigidly wdktylkeqk ivfeeqlrws
      121 idldlpvaih treaysevld sihkvgadkl kgvfhsftgt tdeleeigkl knfklgingv
      181 itfknsklse tiqctdmnhi vletdapyla pvpyrgrrne pvyiwktvek vadtfgltld
      241 etvqitrkna ldlfkipnkk a
//
LOCUS       WP_010802017             450 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Parabacteroides].
ACCESSION   WP_010802017
VERSION     WP_010802017.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..450
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50450
     Region          29..449
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkqiissval asflfclpag aqeaakqwsl eeciryaien nidlkqkele qksrevdlht
       61 skyswlpsvn asvgenfgfg rseskdgliv drnsanttag iqlsmpifdg lkipndiaar
      121 kldlkasiet lnkakedlsi nvasyylqvl ynkemlkiaq lqvdlsseqv tktealynag
      181 kipvsqlydm kaqlakdevt ltesqnnvkl alldlaqsle leragenfdv lepengdaie
      241 rymssiippd qvydhavtfk pqikeqqyll esqkkalria qagyypklnl sagystgyyh
      301 nfgdgdynna pfsdqlknng qksiglslsi pifnrfqvrn svrtarlsit nrelmmensk
      361 kslykeiqqa yytataaqek yissdksvda skvafsyaee rygagkstvf eyseaktkya
      421 qslaeqtqak ynfifrtkil dfyngtpitl
//
LOCUS       WP_010802125             390 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Parabacteroides].
ACCESSION   WP_010802125
VERSION     WP_010802125.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..390
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44265
     Region          143..373
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          288..388
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(293..294,327..328,332,336..337,340,382)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mkkylfimvl fsiiqtsfaq tkegqslepa rkatfinngf wdhwfigaga ganiyfgdrn
       61 sdadffhrft vapeiqfgkw inpylgtrik gagltnlhtf ndnatimsrn ryasvqadlm
      121 wsmtdyfmky nskrvysfvp yvgfgwafgw dyanqpayag ghtrvngmtl nagivnnfkl
      181 sdrvtlsief aatavksefn qvkssgnydi lgtasaglif nvgksatfse aelrnpqeid
      241 elnsrinely aqnqelakrp idcpdcpepe vitekvvefe enplinnvvl fkinqtkvdp
      301 yqgvniynia qylkdnpqfk vrvigytdrk tgtsqinekl saeraqnvar ilisdyninr
      361 drvivewvgd keppfdkpew nravilyveq
//
LOCUS       WP_010802203             331 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010802203
VERSION     WP_010802203.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..331
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=38137
     Region          67..331
                     /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"
ORIGIN      
        1 meennkikql mqlyfgkhfs rygrilfgrw lraddakaek eemlqdlwkk sqpevtdsth
       61 sdwkalqrhl svlpvrersv pfyrqwlkya avivlmimta gttywatdrf kpvrhvemaq
      121 vfvpygeseq vvlpdgskvw vdagtllvyp kdftdtdtrt vyltgqasfs vrknpeqpfv
      181 vkttyldvqa lgtvftveay pgdscsmatl eegsvlvsvr nediqptvlk pdqqlvyshs
      241 ehtvmvhsid aslynmerng ylifentsfs rlmaslerkf nvtihynsqk fageyynvkf
      301 spdekledvl nilqqligih ykikgkvvfi n
//
LOCUS       WP_010802156             136 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Bacteroidales].
ACCESSION   WP_010802156
VERSION     WP_010802156.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..136
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15189
     Region          <6..134
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgsdgviaai saldylfvpi kadrlvlest lnfattindr liktglsslk rlclfwnmvd
       61 rrerttlydi yqqgfsllgl dclqtripvr snftkdlsst ggpvyrstlf apdaaftrec
      121 gfdmfmdeim gilkne
//
LOCUS       WP_010802286             622 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010802286
VERSION     WP_010802286.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 622)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 622)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 622)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..622
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=70672
     Region          104..541
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          332..620
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkkanilcll svalltvscs tdfldtksqt eimaddiwke kslaeaymyd iyfafqdagf
       61 teelqasacd eamfthgref vetnagavtd vnlgwfsktq sghqwqrlyl nirscndfie
      121 hvddatfadd akkqlkgeay flrayflhrl trgfggvpiq lkvtqltddp esfllsrssy
      181 tdcigqvldd idkaaeclkd htfdntqkgr atlaavkalk vrvltdaasd lhdqatasak
      241 ssllasyknp ellfytqgsr terwqavkva akdlldnpmg haiptyggtg lsteekaqai
      301 wrfflaesad hifsryfidt kdesgtkmpi fngpsgyhgw ggntpvqdlv dafamedgsk
      361 fdwnnsqhan npygnreprf yatimydgmq wiqrpddyas ieptgkiqtg yyqldpsvtd
      421 dskfyagmds rsgggenwna tytgyylkky inpadgdhrn kinavfpfir lsevyfcyie
      481 acielgelde akkylneyre hvnlpavttn nkdelrkiyq nerrlefsfe eirywdvrrw
      541 mtapdlpgln slkgirvtat lksgagvqyk ytadpdiwnm hykvidlnne grqfvdkcyf
      601 lpimrdekns npnliqnpgy en
//
LOCUS       WP_010802301             195 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Parabacteroides].
ACCESSION   WP_010802301
VERSION     WP_010802301.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..195
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22666
     Region          5..177
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mnvaeediik klvqgdresf dyiytcyvnn lyaygkgfgl sddelydvlh dlflsllsnt
       61 kifegvrnik sflftcfknr llnvlkipye ysdieqcehl fvvevdllde lidreqaamr
      121 vqivksllnt ltdrqreaiy lrymqklsyd eiadmlgltq kgarklvarg iehmreeats
      181 svillflvif ppdwi
//
LOCUS       WP_010802302             391 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010802302
VERSION     WP_010802302.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..391
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=44952
     Region          <184..391
                     /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"
ORIGIN      
        1 mkkkvnndfw qderfvrnrl lsdeestayw etylkeypdn qelyeeachd fekiqlnnys
       61 lseekqkell dkvyrshnaq kkkqkqhnly lygalvaacl igvlflipvy mshnssvgqd
      121 sltvlpvsdt vhtevtlitd raetieiedn aiiaydstvy vqnakgqkny lseskvdpke
      181 kmvyntlvvp rgkrsslqlp dgskvwvnag svlrfpstfa sekrmiqvqg eiyievvrde
      241 skpfyvqtpk ftvnvlgtsf nvsaysdeel qsvvlvkgqv avktemneei klipnqklem
      301 ndhknkvvpv dvydytswkd gilqfkgetv aevlkrlsry ynveikcdps vagrrcggel
      361 ilfddvnqvm kslsllyeft yrfesetiii e
//
LOCUS       WP_010802338             338 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Parabacteroides].
ACCESSION   WP_010802338
VERSION     WP_010802338.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..338
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=38953
     Region          79..324
                     /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"
ORIGIN      
        1 metfnidkie eilprycsge atieecrmve ewigqsedny rivkqmyaid qamgtvrmes
       61 qvnteralas vnrkmskers lvnwftwvqr vaailfvpll iiwgiehftp rteiarmiei
      121 ktnpgmtttv dlpdgskvyl nsessltyps sfsgekrnvq lkgeaffevq kdpehrfivs
      181 gpcqtqievl gtsfnveafe rdsfisttlv egkvrfayqk nqklatvemk pgqkllydtt
      241 ssqvkllrts getetawkdg kivflatplp ealrmlekrf nvnfvlsndr lrseafngtf
      301 tnqrlerile ifkissnikw ryldtqnttn erarieiy
//
LOCUS       WP_010802359             349 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Parabacteroides].
ACCESSION   WP_010802359
VERSION     WP_010802359.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..349
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38040
     Region          38..297
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mknvflisvl lsaflgactp amqkselfme lpddcptpdg maiapngdli lacpnfadls
       61 kpaclmritk dgkiskwmnv pileetgwaa pmgitfddeg nlficdnqgw sgaekarnkg
      121 rilclkldgy elkevievat gmehpngirf rngklyvtqs slssiqdpsg llvsgvycfd
      181 kndknikvtn tkadknlltt vitknkavqy gldgivfdkk dnlyvgnfgd gtihritmdp
      241 kgnvigneiw aqdpsqlrtt dgmcmdddgn iwvadfsena varidkngri qriaqspdcd
      301 gsdggldqpg epivwngqvi vscfdivtgp dkvntkhdkp ftlaklqln
//
LOCUS       WP_010802402             379 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: 8-amino-7-oxononanoate synthase [Parabacteroides].
ACCESSION   WP_010802402
VERSION     WP_010802402.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..379
                     /product="8-amino-7-oxononanoate synthase"
                     /EC_number="2.3.1.47"
                     /GO_function="GO:0008710 - 8-amino-7-oxononanoate synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_process="GO:0009102 - biotin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42391
     Region          8..376
                     /region_name="PRK05958"
                     /note="8-amino-7-oxononanoate synthase; Reviewed"
                     /db_xref="CDD:235655"
     Site            order(43,105..107,131,175,179..180,205,207..208,236,239,
                     360)
                     /site_type="active"
                     /note="substrate-cofactor binding pocket [active]"
                     /db_xref="CDD:99747"
     Site            order(105..107,131,175,179,205,207..208,236,239)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99747"
     Site            239
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99747"
ORIGIN      
        1 mkdytlilkq lneagnlrsl pdivhtgnri erdeqvmlnl ssndylglas rsdlreaffe
       61 ewkekgypls ssssrlltgn ftvyteleql maecfnreaa llfnsgyhan tgilpaladk
      121 qtliladklv hasiidgill sgapfqryrh ndynqletll kknagqyeql fivtesifsm
      181 dgdvadlrrl velkksypnv clyvdeahai gvrgknglgi aeeqdcirei dllvgtfgka
      241 lasmgayvvc srtireylvn cmrplifsta lppaqiawtr fiferlpefs slreeltlts
      301 hllsdalegk ggeiseshii pyiigenndc iskaeelqrk gfyclpvrpp tvpkgtarir
      361 fsltaditta qltqlikei
//
LOCUS       WP_010802416             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tRNA1(Val) (adenine(37)-N6)-methyltransferase
            [Parabacteroides].
ACCESSION   WP_010802416
VERSION     WP_010802416.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..238
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26262
     Region          5..234
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 manpyfqfkk ftirhdkcam kvgtdavllg awtdtasckn ildigtgtgi ialmlaqrsc
       61 adidaididk eaciqaeenv aaspfagrik vipascadfa rsmaqkkydl ivsnppyfin
      121 slkcpdnkrs varhtdslpl selvenaral lsspgrialv lpyeqleevr etaqknslhi
      181 crqtnvipvp gahpkrllve lspvstdtkn rntltieear hqytpeyial tkdfylkm
//
LOCUS       WP_010802420             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphatidate cytidylyltransferase [Parabacteroides].
ACCESSION   WP_010802420
VERSION     WP_010802420.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..277
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30616
     Region          4..274
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mknlikralt giifvavlvg aicyhpisfl vlfslitglt lwefyglvkh yedasikrav
       61 sslggvylfa atfaytnqlt dgvvflpyll fliytlvael yykapnpinn waftlfaqvy
      121 cagtfsmlnf iaaipdtpgk vvysplfvma ififiwlndt gaylvgsmig krklferisp
      181 kkswegffgg lavvlgasqa lawyapevsw ynwlglsatv vlfgtwgdli esllkrtlgv
      241 kdsgnvlpgh ggmldrfdsl mlaapaayiy ielfirn
//
LOCUS       WP_010802423             235 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Parabacteroides].
ACCESSION   WP_010802423
VERSION     WP_010802423.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..235
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26550
     Region          11..235
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkmvvdkans rgyanhgwlk tyhtfsfany ynpkrvhfgm lrvlnddtva psegfdthph
       61 knmevisipl ngylrhgdsi qnsetitpgd iqvmsagtgi fhsefndsae qqleflqiwv
      121 fpreentkpk ynnydvrsll kknelslils pdgetpaain qdawfsigel dagqikeykl
      181 hkkstgvylf viegevevnn tvlskrdgag fyetdsitie vlkdsrillm evpmn
//
LOCUS       WP_010802450            1036 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Parabacteroides].
ACCESSION   WP_010802450
VERSION     WP_010802450.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..1036
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114592
     Region          1..1020
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mkkiiytaih rrglmfvlfl flavvgyysw trlaidaypd iadttvqvvt qvpglaaeei
       61 eqqisipier amngmpglnv mrskntfgls tvvlvfddgi ddywarqrvq erlvdvelpy
      121 davpglnplt sptgeifryv lesdqldire ltdlhkwvvi prlkqvtgva dvsnfggitt
      181 qyqievnphk meqynvtlgd itekieknnv naggsmlsrg dlsyvirgig lvkdlkdlgr
      241 iviktengvp vylddlgtlk ygslerkgvl gfydgvrdys dgvegivqml rgenpsqvle
      301 gvhqavdeln netlpkgtrl hvfmdrtnlv dttlhtvsht lfegmvlvvl vlilflgswr
      361 gallvaltip lslliafilm hltdipanll slgaidfgil vdgaivmmet ilkkrerhpd
      421 eiltedsilr ratevarpif fstliiitay lplfafehie kklftpmayt vgyallgala
      481 valflipgla fyayykprki yhnrwleklg eiynrqiial lekpkrvllp lflilvaagv
      541 lsytvgkdfl ppldegaiwv qvqlppgisi ekskamgael rktlkqfdev syvmtqvgrd
      601 degaeafsls hiecgvglkp ydtwkfgktk adlieemsek lltmpgytvs fsqpiidmvm
      661 dqiagahsdl aikvygddia dtrhiadkvv nvlrtipgaa dvaidqeppl pqlqiiadrd
      721 riaqyglnfs dvadmielai ggkaisqifv gsksydvicr fddasrnspe sisnllltng
      781 agakiplsqv aevkmttgas tisremnkrh ltihvnlrgv dlteflnkan rlidrdidyn
      841 hdtvhlqwag qfenqhrayn rlaavvplal gimllllfaa cgkfrqaalm mcvvplalfg
      901 gmlalnvrgm tlnvssavgf ialigvaiqn gvimishinn lrsrdrgfkq siitgakhrf
      961 rpilmtatva vlgllpasls tgigsdvqrp latvivygll fatvitlyvl palyylvekh
     1021 yldeeivssd vkntnv
//
LOCUS       WP_010802461             648 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Parabacteroides].
ACCESSION   WP_010802461
VERSION     WP_010802461.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..648
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73589
     Region          4..532
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          562..635
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 misvegltve fggftlfddv sfvvnkkdri alvgkngagk stmlkifagl qsptsgtvsi
       61 pkettigylp qqmqltdsrt vreeaeqafg hiqemekeie rlnlelaert dyetesyqkl
      121 idkvthlseh fqlmggsnyh aelertligl gfnrsdferp tsefsggwrm rielaklllr
      181 rpdvllldep tnhldiesiq wlenfiatra navilvshdr afidnttsrt ieielgsiyd
      241 ykvkyseyve lrkerreqql rafenqqkkl adteafierf rykatksvqv qsrikqlekv
      301 erievdevdt amlslkfppa prsgsypvim envakrygdh lifkdvtlti nrgdkvafvg
      361 kngegkstlv kcimeqidye gklqlghnvk igyfaqnqaq llddnltvfd tidyvaqgdi
      421 rtkirdilga fmfggeasek kvkvlsgger srlamirlll epvnllilde ptnhldmrsk
      481 dvlkdalref dgtvivvshd refldglvdk vyefgnqrvv ehlggiyefl ekkkmdslre
      541 lerstqaasl vadtdvqptq nklsyearke qskaikkvek avaeaenkit elensiaaie
      601 arlatpegas dtslyndyss lkkelsdtmd twteltmele elnekasr
//
LOCUS       WP_010802480             172 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HdeD family acid-resistance protein
            [Parabacteroides].
ACCESSION   WP_010802480
VERSION     WP_010802480.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..172
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=19073
     Region          8..172
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mkrinnsvlr safamilgfv lvlwpeaavt ylvitigicf iipgifslln yftrekvege
       61 pspmfpidga gsilfgawlv impeffvnil myilgallvi agvqqiamlv sarkwsmvpf
      121 gfyvmpalil ltgimiiayp fgaaantfvi fgvasifygi ielinwykfr qr
//
LOCUS       WP_010802485             486 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010802485
VERSION     WP_010802485.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..486
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55227
     Region          38..437
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkkiwiflwi vccalysscs llevepvsti tsqsfwknsg dakayltgiy nkvralnnts
       61 lygedrgdaf kvgeigpstn awaqnllenn apsyrdayni ihhtnlllyk idglsftnea
      121 dknrikaety ylraqtyffl vriwgdvpil ldpvlsdkie lkprspkeev mkqilsdieq
      181 slslfpeegf vnknysskpa ayalkadall wkakvlsggd sdlneavnai neveksgvel
      241 lpeyasvfnn ankrnaeiif slyferyetg nlsiatntts rtdnlsmavn ldeaatspnq
      301 srhvyapsek trvlylkypg dkryqsamid lvdkdgnlil tqtnkfrgkv ytddryfddd
      361 livyrwgdll llraeanaal nkiqdalsdl navrqragld nyagpadkas vekelcderl
      421 relfieqkrw fdlvrfhsgg ainiynevpn lndkpdfply wpinyndmvl ndqlkqtdgy
      481 esdvqr
//
LOCUS       WP_010802512             183 aa            linear   BCT 01-JAN-2025
DEFINITION  DsbA family protein [Parabacteroides goldsteinii].
ACCESSION   WP_010802512
VERSION     WP_010802512.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides goldsteinii
  ORGANISM  Parabacteroides goldsteinii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Parabacteroides goldsteinii"
                     /db_xref="taxon:328812"
     Protein         1..183
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21182
     Region          29..180
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mllirnqivt amylevnknd hvqgpvnapi elieyadyqc pyckkayhiv kdiqkklgdk
       61 vkfvfrnfpl telhphalha aiaaeiaash gkfwemhdfl fenqnalddy ylleyarklg
      121 inaaefetdf gkdrfyqkvk ddydsglend vqgtptffvn geqfdgnwmn sefleylesl
      181 ivk
//
LOCUS       WP_010802537             778 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GH92 family glycosyl hydrolase [Parabacteroides].
ACCESSION   WP_010802537
VERSION     WP_010802537.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..778
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=87164
     Region          22..778
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mksvrclalf lsaalaggtl waqekvsfvn piigtngmgh tfpgacvpfg lvqlspdtdt
       61 iphnvdgkyq prsyeycagy qhkdssivgf shthfsgtgh sdlgdilimp atgclklnpg
      121 tatdpdggyr srfshdteis rpgyyevmls dygvkaqltt tkrvgvhkyt fsgdggnqri
      181 ildmihgiyn ydgkvlwtni rvendtlvtg yritngwart nytyfamsfs kpvihygcee
      241 kakvnyrggy gkfnmkenfp diggrkivay fdfdpatske levkvalsgv stdgalknlr
      301 aeasgysfdq laakasdtwn kelscieakg nndqlsmlyt slyhtminpc vytdvdgqyr
      361 gldgnihkad dftnytvfsv wdtyralhpl fniinrqvnt diarsmlkhc eqsvhkalpv
      421 wshmanenwc migyhsvsvl adavakglpl dkeevlqamv ssstipyydg tkeymekgyv
      481 aldhngsags ltleyayddw tiyntarlag ndrvanqykk raanyinvfd tsigyarpry
      541 sdgrwkenfs llsthgegfi egnalnysfy vpqdvnnmiq lmggdksfvs kldslftmhl
      601 pdeffaeted vtkegllggy vhgnepshhi pflyvwttqp wktqywqrei mnkmyrnnid
      661 glcgnddcgq msawyilsam gfypvcpgtd qyvlgapylp ymkvslengk tfevradkvs
      721 dknryvksvr lngkpytkay itqqdimngg eltfemtssp nkkrvftgdd kpyslsan
//
LOCUS       WP_010802538             762 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GH92 family glycosyl hydrolase [Parabacteroides].
ACCESSION   WP_010802538
VERSION     WP_010802538.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..762
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=86411
     Region          1..759
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mkklfilaia fcsslftmka adktelvdyv nplvgsqski slstgntypa iampwgmnfw
       61 mpqtgkmgdg waytydadki rgfkqthqps pwindygqfa impitgkvvf dqdkraswfs
      121 hkaevakpny yrvyladhdv vteitptera amfrftfpet dksyvivdaf drgsyikiip
      181 eenkiigytt rnsggvpenf knyfvvvfdk pftykatvgd seirkgetea qenhtgaiig
      241 fstrrgevvh arvassfisp eqaelnlkel ggrsfdeiad agrktwnevl grirvnddnv
      301 dklrtfyscl yrsvlfprsf yevdangniv hyspyngevl pgymftdtgf wdtfrclfpf
      361 lnlvypsmnv kmqeglvnty kesgflpewa spghrgcmvg nnsasvvada ylkglrgydi
      421 etlweavvhg annvhpkvks tgrlgydyyn klgyvpydlk inesaartle yayddwaiyk
      481 lgkalgkses eiavfakham nyknlfdket klmrgrnedg tfqspfnplk wgdaftegns
      541 whytwsvfhd pqglidlmgg ksgfnammds vfnvpplfdd syyggvihei remqimnmgn
      601 yahgnqpiqh miylynysge pwkaqywvre vmdklyfatp dgycgdedng qtsawyvfsa
      661 lgfypvcpgt dqyilgsplf ksvtlnleng kkvvinannn daanryistm kvngknytrn
      721 ylthedllrg mtinctmsat pnktrgteek dapysfskei kn
//
LOCUS       WP_010802692             396 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: uracil-xanthine permease family protein
            [Parabacteroides].
ACCESSION   WP_010802692
VERSION     WP_010802692.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..396
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40845
     Region          7..381
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mdskkslspa qktivgvqfl fvafgatvlv pllvgldpst alftaglgtl ifhlvtkgkv
       61 piflgssfaf vapiikatel yglpgtmsgl vavgavyglm salvkwrgig fiktlfppvv
      121 igpviiligl slagsgvnma kenwplalia lltailasll gkgmiklipi fcgiivgyia
      181 gavfgvidfe pivaapwfaf pqfvkpelsw gavifmipvt iapiiehigd vyainevtgk
      241 dfvkdpglhr tmlgdglaci aagliggppv ttysevtgai sltkitdptv iriaavtgiv
      301 fsvfgkisaf lksippavlg gimlllfgti aavginsliq nrtnlgdtrn liivsliltf
      361 giggaaiefg gftmagigls allgvllnll lpkgnk
//
LOCUS       WP_010802745             433 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phenylacetate--CoA ligase family protein
            [Parabacteroides].
ACCESSION   WP_010802745
VERSION     WP_010802745.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 433)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..433
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48887
     Region          1..429
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 miwnetiecm dreemrklqs irlkrvvehv yhntpfyrkk mqemgitpdd iqsieditkl
       61 pftvkqdlrd nypfglmavp mseivrlhas sgttgkpivv gytrkdlsiw sevvarclta
      121 ygitkndsvq vsygyglftg glgahggven iggtvipmss gntqkqiqlm hdfgakglac
      181 tpsyalylae tihnsgiple efqlrvgafg aepwtenmrk eleqklnika ydiyglteic
      241 gpgvggecec qngthlwedh ffpeivdpvt lqpvpegeqg elvfttltke gmpmiryrtr
      301 dlthliyekc ecgrtavrmg rilgrsddmm iirgvnvfps qvesvllemp efephylivv
      361 drvnntdtfq iqvevrpdyy sdemnkmial kkkiaarmqs vigiqpdiki veprslersm
      421 gkakhvidnr klv
//
LOCUS       WP_010802706             566 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RagB/SusD family nutrient uptake outer membrane
            protein [Parabacteroides].
ACCESSION   WP_010802706
VERSION     WP_010802706.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Gray,D.A., White,J.B.R., Oluwole,A.O., Rath,P., Glenwright,A.J.,
            Mazur,A., Zahn,M., Basle,A., Morland,C., Evans,S.L., Cartmell,A.,
            Robinson,C.V., Hiller,S., Ranson,N.A., Bolam,D.N. and van den
            Berg,B.
  TITLE     Insights into SusCD-mediated glycan import by a prominent gut
            symbiont
  JOURNAL   Nat Commun 12 (1), 44 (2021)
   PUBMED   33398001
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10420855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..566
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=64094
     Region          17..476
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          252..566
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkrnniiicl fsgitlltac hdldlnplsy gstenwysne teiemavnel yrdtfwplde
       61 egntdwsddn iyresltpfq natlngqtdk vtdlwskqyk visrangvil kahraveaga
      121 seakingfia eahfhracay aklsskfggi plveddidie agmamgrtdi avvkqfvyde
      181 fdvaaetlpv sysgaqratk gaalalkary alymgdydiv vaatkavmdl giyslhkdyg
      241 dlfltntkna eesifliprs ieynvvmnvr gwlprnsggy avpnptwell asytcidglp
      301 idesplfdsh dpfknrdprl smtivpfgen flgiefnphp ealevmnyks gkmisnndsr
      361 avaqyasyng lvwkkgmdes clenahnidp dkiiiryadi llmyaeakie lnqidqsvld
      421 amnevraray gvdksavsqy paftmtnqnk lrselrmerr vefakeglry mdlmrwklmd
      481 kvmnkkvymm lypaslliek vvsqgdwfwp yapdidengl adftkmesag kiavvaqkkw
      541 derqylwpip tteilinpnm kqnpny
//
LOCUS       WP_010802773             382 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [Parabacteroides].
ACCESSION   WP_010802773
VERSION     WP_010802773.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 382)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..382
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43413
     Region          1..376
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mitkisieny ksitkldfsp grfniligen gggksnllea isfglaasld kldneflglr
       61 girvtkpqfv mssfennppk eivisfltdr ktssiicrid pktkkaelfa gfpisgnaea
      121 eplsyetish iknilskegi yvnkldirst laaeahpfyg kvdpelgrfv fycpeesalr
      181 tfrdeyqllp lgrkgegvfk ylkelsqsee gklvlneine nlslldwfdh ievpatglsn
      241 dytvyikdry ltdtmsyfdq rstnegflyl lfyftlfisk dtpaffaidn iessfnpklc
      301 tkiievlqkl avkhnkqvil tthnpfildg ldlsdedqrl fvvrrndegh tkirhieykp
      361 erkkklselw msgaigglpd nf
//
LOCUS       WP_010802785             771 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GH92 family glycosyl hydrolase [Parabacteroides].
ACCESSION   WP_010802785
VERSION     WP_010802785.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..771
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=87396
     Region          4..764
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mnkknvlaia lvamtawigk pamaapgnda fdpveyampl mgtqssfels tgntypaiar
       61 pwgmnfwtpq tgkmgdgwqy vytankirgf kqthqpspwi ndygqfaimp vvgapefdqd
      121 kraswfshks evvkpyyyka yladhdvite ltptdraalf rftfpendhs yivvdaldng
      181 syikvipeen kiigystkns ggvpenfkny fiiefdkpft yeatfadntl kegskeqtss
      241 hvgavigfkt kkgeivqakv assfisfdqa ainmkelgnd nfdtlvskgk qawndvlgki
      301 eveggtldqy rtfyscmyrs llfprkfyei daagnvvhys pyngevlpgy mftdtgfwdt
      361 fralfpflnl mypsmnkemq eglintykes gffpewaspg hrgcmvgnns asilvdaymk
      421 gvkvddletm ykglihgten vhptvsstgr lgheyynklg yvpydvkine naartleyay
      481 ndwciyqiak elgrpkkeld lyakramnyk nlydkesklm rgknadgtfq spfsplkwgd
      541 aftegnswhy twsvfhdpqg lidlmggkds fvmmldsvfa vpplfddsyy gqviheirem
      601 qimnmgnyah gnqpiqhmiy lynyagqpwk aqywvrdvmn kmytptpdgy cgdedngqts
      661 awyvfsalgf ypvapgttqy vlgaplfkka tlhfengknl vinapensdk niyiesmsfn
      721 gvnytknyld hnellkggvl dikmgdkpnl nrgvnpedfp ysfsvdekkk k
//
LOCUS       WP_010802818             468 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Parabacteroides].
ACCESSION   WP_010802818
VERSION     WP_010802818.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..468
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52313
     Region          61..345
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msinrrqflr rslagsaaiv vgkemnaant pvsgssfsqt edlsppakgk svlglrckpl
       61 stvrigvvgl grgagaverm aqiegteiva icdlnperie nsqktlknsn rkeavaytge
      121 edwkkmcerd didliynatp welhvpialy amdhgkhvai evpaaltvkd cwalvdkaee
      181 tqlhcmmlen ccydffelat lnmarqgllg eiihtegayi hdlrgskfkg yykhwrleys
      241 kyhtgnpypt hglgpvaqil ginqgdrmdy lssvstnqfg lalwakenlk dderitqser
      301 yalgdmntti ihtvngksim iqhdttsprp ysrihlvqgt kgmavkypeq kvavqpdths
      361 flkegpqkev madyehplsk yigerakkvg ghggmdfimd wrliyclrng ypldqsvyda
      421 aawscivels ersvlnkscs vavpdftrga wrdykpwpvi dmkdilhg
//
LOCUS       WP_010802886             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Parabacteroides].
ACCESSION   WP_010802886
VERSION     WP_010802886.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..146
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16727
     Region          <22..99
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 meqqqdafsd sryhldchid pvndlllgfi aywrfdsyty vehfaihpne rgkglgglil
       61 knlieqesgr vlleidpvtd nvsaarlhfy qlhgfvenpy phthpayrng ypdhslvvls
      121 sgetipdiey krfasdlnrv imkkgr
//
LOCUS       WP_010802938            1044 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Parabacteroides].
ACCESSION   WP_010802938
VERSION     WP_010802938.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..1044
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113070
     Region          1..1031
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mvkffinrpi fatvlaliiv vaglvtlnvl piaqypditp ptvqvsavyp gadaqtvaqt
       61 vglpieqqvn gvdgmlymss nssssgaysl titfavgtdi dmatvmvqnr vsiaqsslpe
      121 avivqgittk kqssnivmml sltsrdslyd glylsnyasl nltdqlarlp gvgsvsvmga
      181 gnysmriwld pevmrirnlt pdmvfqaist qnrqvsagyv gqpiaeannp yqytltvkgr
      241 lttpeefgni ilrteqggki lrlkdiarie lgsssynvts rlrgqqaaai aiyqlpgsns
      301 levskavrak meeiastlpq gveygvtldt tevinaside vlvtfletta lvvlviflfl
      361 qnfraviipc lsipvsligt lavmgalgfs vntltlfgli laiaivvdda iivvenssry
      421 mdtgkytare avtkamselv gpvigvvlvl lavfipttfi ggisgqlykq faltiaaatv
      481 lsginsltlt palcalflrv tndpkfvvfk afnkvydktq kiyddvvdrm lkhqlvtlii
      541 flivsataav mfmrwpstfi peeddgyfii ssqlppassl prteavsqki nkildtypev
      601 ktymgingfs vmgggelsnt gtyfvvlknw serkgkghta advvarfnre aygiqeaqif
      661 alvppaipgl gasgglqlql edrknlgpte mqhaiqtlle tyrtkpqlls lssmyqanvp
      721 qyrlnidrdk vqllglqlsd vfstlsyymg aayvndfvef griyqvkiea ggqaqkvidd
      781 vmrlslenss gkmvpfsaft eakqqlgldq inlynmyssa sitcianpky ssgeaiqame
      841 eliqeqlgdn fgyewtsvay qetkagsttm lifgmallva flvlsaqyes wtsplaaimg
      901 lpiallgail gcfimgvpvs vytqigiill ialsakngil ivefardyra agnpireaal
      961 eaghvrlrpi lmtsfafvlg vmpllfatga gaasrvslga avvfgmaint ifatafipsf
     1021 yewmqtfqek wldkaspnkt atka
//
LOCUS       WP_010802953             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HdeD family acid-resistance protein
            [Parabacteroides].
ACCESSION   WP_010802953
VERSION     WP_010802953.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..192
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=21378
     Region          13..186
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mntfderiss avknwwvsll lgllyiliai clmftpmasy valsllfsva mfvsgtleil
       61 favsnrkhis swgwylaggi idlilgiylm aspglsmtvl pfilafwlmf rgfsstgyam
      121 dlkrfgtgnw gwymafgila iicsiaiiwq pglgvftlvy miayalliig ifrvmlsfel
      181 rslhkkattp lq
//
LOCUS       WP_010802971             342 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein
            [Parabacteroides].
ACCESSION   WP_010802971
VERSION     WP_010802971.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..342
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39514
     Region          1..177
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mklsiittiy naaadlprll dsmmaqkspd lefflidngc vdnsrsicee yakrdsrfti
       61 fvikdnvgyi rarnigikev nadyigfcds ddyleigayd raitkiketg cdlyitsyrt
      121 ingdraidnk lpydcgfyng edvknnilpl afgpckgrgm lhgfmwkeif chdllfvnnl
      181 sfevelkpye dqllnvqvis lcktvyvddn piynyvmnpl sitaqlvehp dyrkewnriv
      241 slyeskakyt insvtccana natlnfvygl ilsivkseqn prksllalie ddfiqeilsh
      301 tevrgffyyv rfcmkhqlyr ilfftmslal kvrwllnnfy dk
//
LOCUS       WP_010802972             505 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: lipopolysaccharide biosynthesis protein
            [Parabacteroides].
ACCESSION   WP_010802972
VERSION     WP_010802972.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..505
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56382
     Region          4..419
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 minkqfalnt taiglnllvq ftinffltsy lvrtvgstay gfftlantmv nyaliistal
       61 nsmsarfvgi eyhkqnfkea tgyyssvlyg dlifvlllvm pasvliwnig dvinvpdnli
      121 eevkilfylv flnmcinvlg avfsgvfvik nrldiasyis vvsnlfkagl liilyvcfps
      181 sivylgiatv ittlflvscn yyynkkllie ihlsrkstkw nlmriiiiag vwnsfsqlsi
      241 yllhgldllf cnimvnavsm gylsiagtmp navsscvstl ssvfipkfle yfsknqfeel
      301 vlevknsikf mtiiscvplc flvgfghtfy klwvpstdvd lvyllsicvv fpnftgavin
      361 stnylytvtn kvkwpsivlf ingllnvatv ycllrwtclg vlaivlvsav lgfvrniifn
      421 apyaarcigq pyyvflpdlf ksfglicvas gicyyvnnsv nistwlqlif igggtvfgia
      481 livssvvlsk nqikyiynrf nnklr
//
LOCUS       WP_010802977             327 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein
            [Parabacteroides].
ACCESSION   WP_010802977
VERSION     WP_010802977.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..327
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37882
     Region          3..217
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkspkvtviv pvynvatyie kcavslfaqt ldsleilfvd dcspdnsidi iketlkkypv
       61 rnsltriirm psnsglaavr rqgiieatgk yvihcdgddw vdldlyerly rtaiernadi
      121 vvcdeiheyn dgahlceits lpehckdvvk nwyqftlsmf chnklvnrsl ytkydilpwi
      181 glnmwedngl itrlfyygdk laqihgscyh ynrtninamt sgygikqveq migiaehlte
      241 ffstkldakd fektvmafqf larinlvtds ftnlhryndt fkgseaiipy ldsnafsikg
      301 rfrfrmvkyh lswlfvlmfk iknlfnk
//
LOCUS       WP_010803003              92 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HU family DNA-binding protein [Parabacteroides].
ACCESSION   WP_010803003
VERSION     WP_010803003.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..92
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=10551
     Region          1..91
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mnktqivrml aerlditlvd sriylntlld ivvegvitde kvgihefgki filpqsrrlv
       61 rnprtgekvm lnprktirlk pcealiekin kq
//
LOCUS       WP_010803162             853 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-dependent Clp protease ATP-binding subunit
            [Parabacteroides].
ACCESSION   WP_010803162
VERSION     WP_010803162.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..853
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=95871
     Region          3..840
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mknnyskrli dvieysreea arlqnsyigp ehlmlgiird gdgkamqllh dlhadvfdik
       61 krieqeiknt feteeselhd iaisktterv lrmsmlesrl fktdetgteh lllailkeef
      121 nvaakvlgea ginyrnvynn langtnmnrm eeleeideis dgytddedde eedfssrkes
      181 prsssgtgaa qskspndtpv ldnfgtdmtr aaaenrldpi vgrekeierl aqilsrrkkn
      241 npvligepgv gksaivegla lriiqrkvsr vlfdkrvisl dmasivagtk yrgqfeerik
      301 ailnelsknp niilfideih tivgagsasg smdaanmlkp alargeiqci gattldeyrk
      361 niekdgaler rfqkvivdpt taeetlqilk nikpryeehh nviytdeald acvklteryi
      421 sdrnfpdkai daldeagsrv hisnitvpks ieeleakied tkteklaavk sqnfelaasf
      481 rdkerqyllq leaakakweq elqehretvd edkvaevvam msgvpvqria kaenlrllem
      541 adnlkkqvvg qddavqkivk aiqrnrvglk dpnkpigtfm flgptgvgkt hlakklaeyl
      601 fdsadsliri dmseylekfa vsrligappg yvgyeeggql tekvrrkpys vvlldeieka
      661 hpdvfnlllq vldegrltds lgrridfknt ilimtsnigt rqlkdfgrgv gfssqaagem
      721 dkdfsrgviq kalnkafape flnrvddiim fdqldkdaih kiidielqgl ykrvcglgye
      781 lvltdeakdf iatkgydvqf garplkraiq kyledemael iirasvgegd kivvdfnkde
      841 qkivtsvqkk gqe
//
LOCUS       WP_010803192             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Parabacteroides].
ACCESSION   WP_010803192
VERSION     WP_010803192.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18798650
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..255
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28397
     Region          <14..106
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Site            order(27,30..31,34..35,37,61,64..65,68..69,71..72,95,
                     98..99,102..103,106)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          27..54
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          59..89
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          194..>254
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 mktnikikni lfflliqcla wtayaqdaai keaetaytke dygkaielye gilksngdsp
       61 eiyynlgnay ykagkiasai lnyeralvld pgdadvrfnl qmarqktvdk iepvdgffls
      121 rwfesiqnmg aadswakmgi vcfilfigcl ilfffsrqir lkkvgfyigv llllcvimtn
      181 ifaanqksel vnrthaivfa ptvtvksspd asgtdlfvlh egtkvsvrst lgdwseiale
      241 dgnvgwmptk dieti
//
LOCUS       WP_010803256             168 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: outer membrane protein [Parabacteroides].
ACCESSION   WP_010803256
VERSION     WP_010803256.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..168
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18923
     Region          1..168
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mkkfiglvvl ltislssfaq kgdfsllgnf gyqtdfkrvm igaqgrynlt nhvrlapdlm
       61 fffpknkvtg fdidvnahyv fnlhednlsl yplagfnlqn nfqgkqtikg ddgkettlds
      121 hsstnfgfnl gagltynldk rnflnveyky vfgkdnnsvi afgwgyrf
//
LOCUS       WP_010803300             392 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide pyruvyl transferase family protein
            [Parabacteroides].
ACCESSION   WP_010803300
VERSION     WP_010803300.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10514996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..392
                     /product="polysaccharide pyruvyl transferase family
                     protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45178
     Region          14..320
                     /region_name="PS_pyruv_trans"
                     /note="Polysaccharide pyruvyl transferase; pfam04230"
                     /db_xref="CDD:427804"
ORIGIN      
        1 mktvgiitvh hygnhgsslq ayasqkifek lgydtyiidy rspnayyatd kymnydsrdd
       61 sywkklekrk sgflkravka vlsrphiaql lyhklgvtkg vdlnqfwlkn lkmtcrydsl
      121 qklfadpphf diyvvggdql wnthitfnnp afflafaded akkisfstsi gipaipenal
      181 psfkrgiknl ssillreeeg vaylrsmgyk adrvldptlm ltkeeweqmq nkhykppyer
      241 yilayfldpt swtmdlvetv rkqtglsviv igerkgydni dsysfvgtie tatflslfan
      301 aeivvtnsfh gmaftlifek llvatyrgee sdtsmnsrhr nivnmfglss clyerthfsp
      361 ekltykmdyn rihlllneyr gqsldllkka ls
//
LOCUS       WP_010803427             260 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide biosynthesis/export family protein
            [Parabacteroides].
ACCESSION   WP_010803427
VERSION     WP_010803427.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..260
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29521
     Region          47..229
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mkiinylfav lfcsllfssc gkvkdiaylq gddlfkrmdv sdsveikirk ndildisvsc
       61 aepellqpfn nlswgnnysg nygagynnrg ylveqdgtin fpllgrlkiq gltrrqliel
      121 iqdklkkgdy ikdpvvtvrf qnfriqvlge vnrpgsynit sdqvtlfeal alagdltihg
      181 rrnrvavvre tdgvrtilyh dlrsrdvfns pdfylqqndl vyvepnrvra eastqnqftn
      241 vgtwlslisf lmstcvlifk
//
LOCUS       WP_010803507             393 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Parabacteroides].
ACCESSION   WP_010803507
VERSION     WP_010803507.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..393
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43908
     Region          83..391
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkqfivitll asaalsvngq nsidavlrsi eannkelqan nqltvskkle akldnnlpdp
       61 svsyvhqygn regmgiqgel vasqsfdfps vyvqknklak skaasfdrqg aefrqqillq
      121 akeicldlvl lnqqralldq rrqnaeqlae lyamrletgd aniletnkid lellnaktea
      181 rmnesariak lqelatlngg iaidftdtty msdgdilsfe elcaeavtsn pqlltlkseq
      241 vaarrqlsvn kskslpsfel gyrmntatgg erfngflvgi siplfsnrnn vkqakaqaly
      301 tdlqlesttt tveselhqly nqsvalktsm deyntvlksq nslallnkai qtgqismiey
      361 fvdvttfyqs mqnymqlqne yqkvmaqlyk ykl
//
LOCUS       WP_010803657             153 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Parabacteroides].
ACCESSION   WP_010803657
VERSION     WP_010803657.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17548
     Region          3..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 metldkkdlq ilrtlqenar lttkelaarv nlsstpvfer lrrlenggyi kkyiavldae
       61 klnlgfvvfc rvklsklnre iateftriiq dipevtecyn isgsydyllk ihapnmkyyq
      121 efilnvlgti dslgslestf vmdevkhdyg ihi
//
LOCUS       WP_010803718             192 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Parabacteroides].
ACCESSION   WP_010803718
VERSION     WP_010803718.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..192
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22150
     Region          22..186
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 megfntyidl ldcsgltgff ykkgekrilk rkefflrqnd sslyagyvek gafrltrigd
       61 ngkeavvgys fekeficdys sflkrttsvv niqattesvv yvvslsdyle ylntgpeeqr
      121 frhkaaealf emvymrlles ycdtpeqryv klmqrcpnlk ekvplkeias flgvtpetvs
      181 hirkklsype ks
//
LOCUS       WP_010803761             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Parabacteroides].
ACCESSION   WP_010803761
VERSION     WP_010803761.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..253
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28395
     Region          8..224
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkketsyvaf stqkggvgkt tftvlvasyl yylkgynvav vdcdypqhsi samrkrdael
       61 vngddyykql afhqfkalgk kaypvlcssp deaiktadey lasagmdydv vffdlpgtvn
      121 segvinslsg vdyiftpiaa drvvlessls favaihkllv kneacrlkgl hlfwnmvdgr
      181 ektdlytlye qtigelelpl mkvfipdtkr fkkeldaqrk tvfrstlfpa dkrlvkgsnm
      241 eeliteiayl ikl
//
LOCUS       WP_010803779             164 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Pandoraea].
ACCESSION   WP_010803779
VERSION     WP_010803779.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..164
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17923
     Region          9..150
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mntpqnqser seitfrflae paavnfggkv hggslmkwid evayacaatw sgrycvtvsv
       61 gnirfrrpil vgnlvelrar ivatgrtsmh ihvsvhagdp kwgelrqttd clmvfvavde
      121 snhpvgvpsf epkteeqkal akyamdvkaa ldaivelkpe nvsn
//
LOCUS       WP_010803835             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Pandoraea].
ACCESSION   WP_010803835
VERSION     WP_010803835.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..145
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15533
     Region          3..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlfthilipt dgselsqkav tgglelaral garvtgyccl aeypyspfse yvleapatfs
       61 eriaeeacah ldklaeaaaa agvpfdrdss tfpapylgii daaerhrcdv ilmashgrrg
      121 ltslllgset qrvlvhskip vlvyr
//
LOCUS       WP_010803925             406 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010803925
VERSION     WP_010803925.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..406
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=43143
     Region          9..402
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mpsmthsrrw qwqgtdadgr rcrgeviapg eavarlmlrd qrltithira grrhtpagrv
       61 gaadatdlvr rlatllgtgv pltaaldvla rgahtrglkr lasavgsdva qghplaqama
      121 rtshrfssvd cqliaagels gqlgptlarl saqydhtrav keklqralay pstvlvvavt
      181 vviallqwvi peferlfasa agggvplppl trwlidmsra sltngpwlla glgatglvvt
      241 aawrrsarir rlrdrlilrl pgagriirmm saarwartlg tlvdagvalp damdaaasac
      301 gnlvmqqaah dvhravarga rlassleaht rwplviaqlv vvgeesgtlg rmlnqaagll
      361 deeashalvs acatlepmmi tflglliggm vlamylpmfq lgygva
//
LOCUS       WP_010803949             311 aa            linear   BCT 01-JAN-2025
DEFINITION  carbohydrate kinase family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010803949
VERSION     WP_010803949.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..311
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33154
     Region          4..289
                     /region_name="ribokinase_group_A"
                     /note="Ribokinase-like subgroup A. Found in bacteria and
                     archaea, this subgroup is part of the ribokinase/pfkB
                     superfamily. Its oligomerization state is unknown at this
                     time; cd01942"
                     /db_xref="CDD:238917"
     Site            order(52,249,252)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238917"
     Site            order(191,219,247,250..251,254,276,279)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238917"
ORIGIN      
        1 mttvicgsla ydnimtfegr fgehilpdqv hilnvsflvp tmrrnfggca gnigyslhll
       61 ggspvvmgtv gddgaayler fqslgmttef vrtvtdsmta namittdldn nqitafhpga
      121 mmfsaenrva dvkgatlgiv apdapdamlt haegfaatgv pfvfdpgqgl pllsaealrr
      181 mvelatylav ndyeakllcs ktgwsmedlq srvealvvtr gehgalifad gkqhdipavs
      241 akrivdptgc gdafrgglly giekgldwpt tgrlaslmgs lkiaeqgpqt yaparseiea
      301 qfaeafghrf e
//
LOCUS       WP_010804009             361 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pandoraea].
ACCESSION   WP_010804009
VERSION     WP_010804009.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..361
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39779
     Region          1..359
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mphidiqgit krygdatvld gldlhirnge fltllgasgc gkstllrlla gldlpdsgdi
       61 rrnhqsilaq tpserdcamv fqsyalyphm tvganictpl lmrqlsfwqr lplvrhaspa
      121 vrrthtqveq sgrkvaqtlg idhlwerkpa qlsggqrqrv alaramvrsp slflfdepls
      181 nldanlrqsl rgeiralhrq lgvtfvyvth dqheamsmsd rvavmkngri lqldtpealf
      241 qrpvskevar fvgsprinil slrslpegta qatpapavev gvrphqflwh aasgawpvkv
      301 rvqsveyags ekvvaartas eeeitvvada mqpvregdat tlyippsqav ffdaqgrrve
      361 a
//
LOCUS       WP_010804048             356 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Pandoraea].
ACCESSION   WP_010804048
VERSION     WP_010804048.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..356
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38536
     Region          7..355
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 msshsdqrkf fhlmlfvvti vfgwilfplf gavfwgtila vlfqpvqrrl lirmrgrpnl
       61 aslatlalil livilpltlv vgmltqeist alvrfradlp qltiafqqll drlpasvhrv
      121 mdlagvqdvn aiqqklgdga aqigrlvavy lvsigqntaq llvsfgvmly llffllrdgt
      181 aigatvrral plderhksll irqfttvvra tvkgniavav aqgalggfif avlgiqgyvl
      241 aavvmaflsl lpavgaavvw vpvgvwllls geiwrgvvlf vfcgtivslv dnvlrpilvg
      301 kdtklpdwvv listlggmsl fgltgfvigp liaalfiasw niytrlrddd tqadag
//
LOCUS       WP_010804139             402 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: elongation factor Tu [Pandoraea].
ACCESSION   WP_010804139
VERSION     WP_010804139.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     gene            1..402
                     /gene="tuf"
     Protein         1..402
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43639
     Region          1..400
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makekfertk phvnvgtigh vdhgkttlta aiatvlsskf ggqakkydei daapeekarg
       61 itintahiey etaarhyahv dcpghadyvk nmitgaaqmd gailvcsaad gpmpqtrehi
      121 llarqvgvpy iivflnkcdm vddaellelv emevrellsk yefpgddvpi ihgsaklale
      181 gdkgplgeea imkladaldt yiptperaid gtflmpvedv fsisgrgtvv tgriergiik
      241 vgeeieivgi amdgdkpkid kttctgvemf rklldqgqag dnvgillrgt kredvqrgqv
      301 lakpgtikph rkfsgevyil skdeggrhtp ffnnyrpqfy frttdvtgsi alpadkemvm
      361 pgdnvsiqvs liqpiameeg lrfaireggr tvgagvvaki ed
//
LOCUS       WP_010804167             396 aa            linear   BCT 01-JAN-2025
DEFINITION  elongation factor Tu [Pandoraea sp. SD6-2].
ACCESSION   WP_010804167
VERSION     WP_010804167.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     gene            1..396
                     /gene="tuf"
     Protein         1..396
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=42821
     Region          1..396
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makekfertk phvnvgtigh vdhgkttlta aiatvlsskf ggqakkydei daapeekarg
       61 itintahiey etanrhyahv dcpghadyvk nmitgaaqmd gailvcsaad gpmpqtrehi
      121 llarqvgvpy iivflnkcdm vddaellelv emevrellsk ydfpgddlpi ikgsaklale
      181 gdkgelgeqa imqladalds yiptperaid kaflmpvedv fsisgrgtvv tgrvesgvik
      241 vgeeieivgi tptvktictg vemfrklldq gqagdnvgil lrgtkreevq rgqvlakpgs
      301 itphteftge vyvlskdegg rhtpffnnyr pqfyfrttdv tgsitlpedk emvmpgdnvs
      361 isvkliapia mteglrfair eggrtvgagv vakiva
//
LOCUS       WP_010804180             341 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Pandoraea sp. SD6-2].
ACCESSION   WP_010804180
VERSION     WP_010804180.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..341
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36623
     Region          11..107
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(55,58,62..63,72,89,93,99,103,106..107)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mkdsavclna sdaarrlgvs nkalrlyeqh glvspgrtaa gyriygpddm araaevvalr
       61 alglslaqva rvlsggdpqt lasalaaher vlddeirdrl rrletvrslr aglaagrmpa
      121 egelpglveq aapsvafelp wpwggewfew rdirplnyii gslgsgktrl amrlaqalpd
      181 atflgldrlg egchaarhal erdvalrarv dhatawlrde gaaacdaltv llvslegera
      241 galvidlieq dlvrstqeal irylrryinm rrqplfvmtr ssaildlaav gsdeaivlcp
      301 anhsppvrvv pyagapgfea vatclaspev rariaappqt v
//
LOCUS       WP_010804196             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Pandoraea].
ACCESSION   WP_010804196
VERSION     WP_010804196.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..155
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16723
     Region          1..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mferilvaid gsptadeafd yalalavark arlhvlfvvd ipvayvadad pfpfieamrl
       61 qgenirkltg erlkgagveg dveirellpl ggdvphqinl aaeewhadvi vigthgrrgv
      121 rrlalgsvae ncvrqatrpv ilipgtktqa ndevl
//
LOCUS       WP_010804214             217 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Pandoraea].
ACCESSION   WP_010804214
VERSION     WP_010804214.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..217
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=23203
     Region          3..144
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
     Region          <179..216
                     /region_name="BON"
                     /note="BON domain; pfam04972"
                     /db_xref="CDD:428229"
ORIGIN      
        1 mktdsqlqrd vmdelardts ihaneigvev qdgivtlsgn vasflekcea ervaarvaga
       61 raivvslevl ptskdrhtda diakaalavl kwhaglpvds mhvkvesgwv tiegsvesyt
      121 qrvlaenavr tlrgvrgvin dikvqdsprr sevvghiaaa larqalreah hieisllgng
      181 evlltgkvhs laekeairga amtthgvcav vdrmtve
//
LOCUS       WP_010804216             153 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Pandoraea].
ACCESSION   WP_010804216
VERSION     WP_010804216.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..153
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16022
     Region          1..148
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myhnimvafd gsepsktalv haaklaralg aslrvayvev dpalyfplma aalpsvaevr
       61 nvqsaetlav reaalnllar egvaagflal plvdshmhia drllseakrv gadlvvtgth
      121 grrglarltl gseanrvlqh adlpvlvvks acp
//
LOCUS       WP_010804289             125 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Pandoraea].
ACCESSION   WP_010804289
VERSION     WP_010804289.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..125
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13723
     Region          14..119
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mtapslitfa pdqageavfd hpaearrvsg npqrvtrpfy tdalgefdcg ewtcepgawr
       61 iafgahrqey fsviegriri sdldgnasef gpgdacvipa gfegvfevve pvrkhfvmfe
      121 rktqs
//
LOCUS       WP_010804301             299 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pandoraea sp. SD6-2].
ACCESSION   WP_010804301
VERSION     WP_010804301.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32180
     Region          6..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..284
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(105..106,108..109,112,116,118..124,214..219,
                     225..226,228..229)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdvtflanll livdsgsmae aarrigvtpa avaqqvqale relgvellvr sgrtvtptea
       61 ghrvierarg lvrefselka falegeaage lrigtittal lslvpdvlsg faasfphtnv
      121 liragtsmel yealqrgdvd vavclhpafa lpkaynwhll reeplvvlap srlsahaphd
      181 llarepfiry drslgggkqa dqylraakiv phelfelnsl maiammvdrg lgvslmpdiv
      241 spltthlnva klslpvqtep rrfgvlwhra sprgrliggf lacadavles erkgaggvi
//
LOCUS       WP_010804311             779 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Pandoraea sp. SD6-2].
ACCESSION   WP_010804311
VERSION     WP_010804311.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..779
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83907
     Region          65..742
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mklqtlrnpr hahparpvrl afalsaphlt ltaialavla stahaqsasp itdigdvsas
       61 digapvnvta tksrkaptea aakaltqapl eatspqtqis sdyianqinp qadygtilri
      121 apsysssspn glglseaknq tlrgfpdgqf nvtydgipfg dtndfshhtt syfpaatigg
      181 vtidrspgna ttlgyatfgg svnlfsptls ptrkieysqt igshatwqen lgvttgimpg
      241 lldsniflnv qrtdsngals nsglrntnif lkgvtpigss tlvtwvyayd kihfnnpgga
      301 tlnqvaqngy nyglngdpks pnywgynyqd kntefayldv khdfdsgwsl nnklytyyyy
      361 nlshelngdn tssplsalsa akpfsagqsg sdiagalkln eyrtygdtls athtgtygtf
      421 tggfwvehtr nprnrfayda ttgqsvkqna tygntyydmv devntaqafs qyawkatdal
      481 tvtpgiryqh ferslsasvl qnnlpgtsas kswnsvlpsl dvnyrftslw sgyaqvsrga
      541 lgpnlntlys anpagnnnvn pqtsmayqig tvfkadrftf nadayliefs nyitkngsga
      601 natyfnaggv rytgveaegn vllgsgfsfy angslnnaty tqdgtgsqiw ksgqrisfvp
      661 qytaaialnf dqgpwhagin tkfvgsmyqg sngaadgsiy kvgpynvtsm miardftnls
      721 svlkkvrvsf gidnlfdthr itdnlgpaat dtskgtdanq flyyfvpgrs vyvnlraei
//
LOCUS       WP_010804325             413 aa            linear   BCT 01-JAN-2025
DEFINITION  lytic transglycosylase domain-containing protein, partial
            [Pandoraea sp. SD6-2].
ACCESSION   WP_010804325
VERSION     WP_010804325.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         <1..413
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
     Region          125..343
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 kdmglvlsde qlkraaayne qmikleasgt klkysfgeam apalertiav vqrlvdqyga
       61 vaatkvaeyv erfakwleqv dwektasevs gfvdaiggvk gvavalaait faapiagivs
      121 iignltslat vavpsavaal gtlgaagvaa wgalklakaa glpdtnsakg asdvaagnww
      181 aasaslpams flgagwdrlt gksnadiaag lrlqsgtgks saesdalfsr letqyglpkg
      241 lldsvwaqes grgtnmlssa gakghfqfmd atakqygldd pndlsksata aaqmyrdllk
      301 qnggdlskal agynwgqgnl qrkgmenapq etrnyveqvq armggtglys nspriaaanl
      361 pgqspspvta dggrvhvdvv ihqdgrpata kvrsqgnata takvqtpkme vvv
//
LOCUS       WP_010804363             310 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010804363
VERSION     WP_010804363.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33501
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..296
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,228..233,
                     239..240,242..243)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdlrqfryfv avaeerhfgr aaqrlsmtqp plsqqirale aslgaplfvr tnrsveltav
       61 grqllpevrr iladadalpa laqglahgev gtlslgfvst adygilppll refgeryprv
      121 rlqlleatsd vqvealmdgr idaglfippv paryanelsy lpivreplml alpaarddva
      181 adapqgepvs ladfadeplv ifprrvapaf ydiimgcyaa lgltprvgqe aiqmqtivsl
      241 vsagmgvalv pqslchlrrt gvtyralret stlietgllw rtaevtpvle gfletargva
      301 htppgatlss
//
LOCUS       WP_010804366             122 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [Pandoraea].
ACCESSION   WP_010804366
VERSION     WP_010804366.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..122
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12718
     Region          35..121
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mkefagksas atlgawlmia agtalaqtsa qatdasdaha mekfarernc mtchatdrtl
       61 lapsyraiak ryagqtgaae eiarsiadgs hgkwgsipmp aspqvapdea arlarwilgm
      121 ar
//
LOCUS       WP_010804377             258 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010804377
VERSION     WP_010804377.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..258
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26502
     Region          37..242
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mslwleplsg fgvgllvglt gvgggslmtp lltlllgyaa pvavgtdlaf aaitksfgtv
       61 ahrshghvkw hivrrltlga lpaalvtilf lkrlggidda alhvikltia asvlltvlsl
      121 lfrakllavl rahpnwqltg rpqavatvmv galigglvti ssigagavga tlilmlypql
      181 epaevagtdi ayavpltaia alghiwldtv hwallgslli gslpgiwlga kltrhlperi
      241 vrgalaatlt laavklvg
//
LOCUS       WP_010804467             376 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: porin [Pandoraea].
ACCESSION   WP_010804467
VERSION     WP_010804467.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..376
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=40204
     Region          14..376
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkpnfriaaa gcclafassl pmpalaqsnv qlyglidsgv efltnadkna agntvnltri
       61 tsgnlagsrw gikgtedlgg gnkalflien gfnlgngqsl qggrefgrla yvglsnsslg
      121 tvtigrqggv fldwvskfnp lnnavyaikm qdtafsdrld nslrytaklg afdamvqysk
      181 gyddvsfgsa tpgdnrraqv vdagvryang plsfvlaydq knggstlpka amtpkvggye
      241 gnidrriaaa vqyslqsvdl yvgyrylnak aihlsalnks pveassyywl gttwhampal
      301 dlsatamyqd fygtnrdpls fqvsadynfs krtdvyvnlg yvvnrngsdl glngfgnnvv
      361 agknqfgtma gikhtf
//
LOCUS       WP_010804468             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Pandoraea].
ACCESSION   WP_010804468
VERSION     WP_010804468.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..231
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24582
     Region          9..>225
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtsdtrasqg vsvslralhq tfgatrvleg idldvpagtt tallgpsgcg kstllkllag
       61 llaptggeir fddtvvasds ichaperrsl gmvfqdyalw phmsvaanva fplemrgvkr
      121 aersdrveea lslvglaglg prrpqalsgg qqqrvalara ivsaprlllf deplsnldrd
      181 lrtrlcadig allsrlgtta vyvthdrdea ealadqivil ahgrvdkrit r
//
LOCUS       WP_010804580             539 aa            linear   BCT 01-JAN-2025
DEFINITION  GMC family oxidoreductase [Pandoraea sp. SD6-2].
ACCESSION   WP_010804580
VERSION     WP_010804580.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..539
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59618
     Region          5..538
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mpdiatqkad vivvgsgvag sivahqlala gksvilleag prmprweive rfrdqpdktd
       61 fmapypssaw aphpeygppn dylilkgehk fnsqyiravg gttwhwaasa wrfipndfmm
      121 ktvygvgrdw piqyddlehy yqraeeelgv wgpgpeedly sprnrpypmp plplsfneqt
      181 iktalngynp kfnvvtepva rnsrpydgrp tccgnnncmp icpigamyna ivhvekaeqa
      241 gaklienavv yrletapnkr itaavykdkt gaehrvegky fvvaangiet pkilllsanr
      301 dfpngvanss gmvgrnlmdh pgtgvsfyss eklwpgrgpq emtsligyrd gpfrateaak
      361 kihlsnmsri nqeteklfkg gtlmkseeld arirdrsary vqfdcfheml pspenrivps
      421 ttatdaigip rpeityaidd yvkrgaahtr eiyataakvl cgtdvvfnde fapnnhitga
      481 timgaeards vvdkdcrtfd hpnlfissss tmpsvgtvnv tltiaalalr madtlkkev
//
LOCUS       WP_010804620             286 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fumarylacetoacetate hydrolase family protein
            [Pandoraea].
ACCESSION   WP_010804620
VERSION     WP_010804620.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..286
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30926
     Region          71..277
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkllrfgpkg rekpglldad gqvrdlsnvl aditpetlsp qglaalrald vrslpvvasp
       61 grlgvpfsgl gkflavglny sdhaaeagla vptepvlftk wenclngpnd pvvlprnsvk
      121 gdwevelgfv igttaryvpl eraldyvagy civndvsere yqierggtwd kgkgfdtfgp
      181 vgpwlvttde irdpqqlglw ldvngvrrqt gntstmifsv aylvhylsqf ttlkpgdlvt
      241 tgtppgvglg qkppvflkpg dvmrlgvdgl geqtqevhay dtrwld
//
LOCUS       WP_010804629             188 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Pandoraea].
ACCESSION   WP_010804629
VERSION     WP_010804629.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..188
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19642
     Region          40..178
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msrlplhtle tapeasrpfl ekslaangfl pnlvaslana ptaletylsv gaingraslt
       61 laerevvqit aagihgcgfc vaghtavalk kaqlpealvn dirdqnrlsd akldavavft
      121 raviatrgav sdaefadfks agfddaaale vvlgvslatl cnfannlsqn elnpqlaayr
      181 wepkeqaa
//
LOCUS       WP_010804664             209 aa            linear   BCT 01-JAN-2025
DEFINITION  SOS response-associated peptidase [Pandoraea sp. SD6-2].
ACCESSION   WP_010804664
VERSION     WP_010804664.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..209
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=23402
     Region          1..209
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mctnyrvpdr qlfseyygtp ppigewrdev ykdyfapiir rdaggrrsdl asfgmvprek
       61 ippgvhvfdt mnaraetvge krsfsgawkk qqlcliptqv ffepdyetgn avrwavgmad
      121 gspfaigglw rewegeggar lsftmltlns dhhplmkrfh kpgsekrsvv iikpadyddw
      181 lgarsmdear lfvtlpdaat msavpapka
//
LOCUS       WP_010804700             280 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pandoraea].
ACCESSION   WP_010804700
VERSION     WP_010804700.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..280
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31319
     Region          <39..96
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <95..275
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          194..275
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mskstvacpy pstfwrdpal pflearevld grrvcyalhs hetfsigavt ggrstylngr
       61 aretvgrgsv vvmnpdavha cnpigdeawa yrmlfvdtaw lrdlqrelgf ghghdlhlfd
      121 pmsstdpvly aglnrlydvg tdttrdrler esvvqqffid aherlnpapq pmhddshklr
      181 daadfirahc realtlaqic aaaglsasyl trafrvqygl tphaflmnqr iqyargrlrr
      241 ghaiaevald agfadqahfq rtfkqllaat pghyreprva
//
LOCUS       WP_010804763             348 aa            linear   BCT 01-JAN-2025
DEFINITION  ornithine carbamoyltransferase [Pandoraea sp. SD6-2].
ACCESSION   WP_010804763
VERSION     WP_010804763.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..348
                     /product="ornithine carbamoyltransferase"
                     /EC_number="2.1.3.3"
                     /GO_function="GO:0004585 - ornithine carbamoyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005543 - phospholipid binding [Evidence
                     IEA]"
                     /GO_function="GO:0016597 - amino acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042301 - phosphate ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0006593 - ornithine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38291
     Region          1..343
                     /region_name="ArgF"
                     /note="Ornithine carbamoyltransferase [Amino acid
                     transport and metabolism]; COG0078"
                     /db_xref="CDD:439848"
ORIGIN      
        1 mtrnwlapdl tmsapdyral ldaalsfkrr yprstedalr grtiyflfyn aslrtrssfq
       61 tglsrmggha ivldphhgiy tpalpeaeip ystervadva rvlssygdai airmygapag
      121 wvygaahrhl eafsqwsrap iinmecdrfh pcqaladvmt mreqlgglag rrlcisways
      181 gswhkpvavp qslllaavka gmdvtlahpa sfgldpqvmq aatqfaeqtg asirvthdlr
      241 dgvsdahavy akswcslahl plrhgdavde tamresferh rdwrvdadvm rlaapgagyl
      301 hclpadrgqe vtdevidgps swvfqqagnr lhaqnavmah llnpgcle
//
LOCUS       WP_010804728             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [Pandoraea].
ACCESSION   WP_010804728
VERSION     WP_010804728.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..322
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34624
     Region          24..293
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mfkqclaaaa lcaaslhafa ddlvrlgnlk fahygavsym kvigpkyglk ieermfakgv
       61 dimpaivagq idvsasalda aiagraqgap iyavagfakg gvrlvakkgl pitkvadlkg
      121 kkvgvargga qelilyaela kagltwsdqp gkdvqimfma fadlnqalaa gsidamcqse
      181 pqasqainkg fgvevlkpyd tpigepvral viteklykek pdvaqrlmya fveatdyfik
      241 npqaaekyvr edmfknqitt qdftdaigns pysydlsiah vqlttdlmkk ygvgklqdpv
      301 pkaedwvkld llakaktkln ik
//
LOCUS       WP_010804730             264 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010804730
VERSION     WP_010804730.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..264
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29286
     Region          1..252
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mlieidnvtk qfpvpggtve alknidlnig agefvcllgp sgcgkstlln alagfvqpts
       61 gviridgrsd aaaepgpdrg mvfqeyalfp wmtvaqniaf gleikgmrra einervdlll
      121 gklnlrefrd rfprdlsggm rqrvaiarvl aldspillmd epfgaldalt rrtlqdellr
      181 iweefkktiv fvthsieesi yladrvvvmt yrpgtvkrdm vielprprdt agsefnelkk
      241 alaqmvmeeq mrfaqseicg vtad
//
LOCUS       WP_010804765             318 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-dependent oxidoreductase [Pandoraea sp. SD6-2].
ACCESSION   WP_010804765
VERSION     WP_010804765.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..318
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=34639
     Region          5..305
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
ORIGIN      
        1 mtrqriivlg agvsglttav tmalagcdva ihaaegpgqt tsalaaaiwh pfyqapdfvy
       61 lerarqtyat marlsadtss gvlmrtltey frrdagvpww aecardlkrl petdvpsrfa
      121 cayrmavpva dtgiylrylm nmflelggrf eqqrvddpap llddadyvvn ccgygsrqfg
      181 dnalslsrai vlrarrdaav rgcfiddsdp aaptyiverd ddivlggtad peltstvigd
      241 rqiadivrrc tqlcegvavl rvieartgfr pmrrvarvav derhsrllhn yghggggftl
      301 swgcandvlr laglatan
//
LOCUS       WP_010804779             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SCO family protein [Pandoraea].
ACCESSION   WP_010804779
VERSION     WP_010804779.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..200
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21974
     Region          47..200
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mnlaviwlrr amllmgltvl laacgkdgpt fqslditgnk efaqdfslqd pqgktrtlad
       61 ykgkavvmff gythcpdvcp ttmaelnqvm qklgadaqrv qvlfvtvdpq rdtpelmgqy
      121 vpafnpafvg lrpaddaalk evtksfrvvv nkvegstpnn ytidhtagiy vfdpngqlrl
      181 fmrpdepvda makdlktlls
//
LOCUS       WP_010804766             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Pandoraea].
ACCESSION   WP_010804766
VERSION     WP_010804766.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..214
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22729
     Region          14..189
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 meldpatlde asiynfmmst ilprpiawvs tvdrqgrpnl apyayfmgvc cvpmtvlfcp
       61 vvppapkrkk dtlrnveavp efvvnvasas cidavnlsaa plpagesefd ltgvtpvpss
      121 rvrpprvlea avayecrvrd iieisaapgg gwvvlgtvla ahvddalldp vthqvdlqgl
      181 rpvgrlgggs fvnaasdtft ltryktladl aark
//
LOCUS       WP_010804819             251 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Pandoraea sp.
            SD6-2].
ACCESSION   WP_010804819
VERSION     WP_010804819.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27344
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlaeqrqqyv leqlaktgal aisdlvrelg vsretvrrdl ntlaarglll mthggalaad
       61 rsepdwtlre nlnaagkrai gvraaelvpd gasviidygt ttravaqall skhrlriytn
      121 dwqiarllgr hhdnrvtllg gelqdnedav qgwdainqis qyhadfafig vggvtedggi
      181 tdfnraaael rarmllcanv savvadhtkf grvtpvrirh feaarylisd aaphksmlaq
      241 lrargpelli a
//
LOCUS       WP_010804871             306 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010804871
VERSION     WP_010804871.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33902
     Region          13..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..302
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(104,106..107,111,169,206,277)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(105,108..109,112..113,116..117,119..120,123..124,
                     126..130,132,195,227..231,234..235,238..239,242,256)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mnlrsldlnl llvfesmlrt rsttvtaeel nltqsavsna lkrlrlafgd plfvktpqgm
       61 wptdlalala ppvteglgli rgaveapqdf vpanaqrtfr lylsdigqli fmpklmatla
      121 aeapgvrivt vdttpreaqn amamgdidlt lglftrfssg fhqqrlfreh yvalvrdghp
      181 tireqltgea flsaahavyr ptaghhdvfe tavehwfaqa grqrhvalrm ahsmglsali
      241 aasdlvvcvp trlgralkaa adlrtyalpf dgpefdisql wherfhtdag hrwlrstlfr
      301 lfhged
//
LOCUS       WP_010804877             324 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pandoraea].
ACCESSION   WP_010804877
VERSION     WP_010804877.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..324
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35720
     Region          46..196
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <211..311
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhlvknppre aaqsefaddp sltarnelvg lleratrale gttptavdgl fvhrilhpgg
       61 pkpalqqpaf aviaqgekrl qigeehyayd pmhymvtsvh lpvvaqvsga seqspylglr
      121 lnlaaedvts ligdehlppp apsasgrgly vnrldaalld avlrllrlle tprdipilap
      181 mirreivyrl lmngqgvllr qmalqdsqmn riaravrwlr ehyaqplrve alaqevhmsv
      241 sslhhhfklv tamspvqyqk qlrlqearrl ifgadiavaa aaqavgyesa sqfsreyarv
      301 fgeaplrdkr rwlqdgdggg atrg
//
LOCUS       WP_010804885             232 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fumarylacetoacetate hydrolase family protein
            [Pandoraea].
ACCESSION   WP_010804885
VERSION     WP_010804885.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25111
     Region          25..232
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msfvfappat vaipvvgsnd qfavrrvycv grnyaahare mgfdpdrepp fffckpadav
       61 lpvaygetle lkypsqtsny hyeaelvavi gkagsdipld qalehvwgya vgldmtrrdl
      121 qmkmremgrp weigkafdas apigpihpvs svghiekagi sltvdgvqkq ksdithliws
      181 vaetvsylsq ffrlepgdli ytgtpegvgp vkagetmvta veglgaitvr vv
//
LOCUS       WP_010804920             618 aa            linear   BCT 01-JAN-2025
DEFINITION  ferrous iron transporter B [Pandoraea sp. SD6-2].
ACCESSION   WP_010804920
VERSION     WP_010804920.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Marlovits,T.C., Haase,W., Herrmann,C., Aller,S.G. and Unger,V.M.
  TITLE     The membrane protein FeoB contains an intramolecular G protein
            essential for Fe(II) uptake in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 99 (25), 16243-16248 (2002)
   PUBMED   12446835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     gene            1..618
                     /gene="feoB"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0015093 - ferrous iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
     Protein         1..618
                     /product="ferrous iron transporter B"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0015093 - ferrous iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66559
     Region          3..618
                     /region_name="FeoB"
                     /note="Fe2+ transporter FeoB [Inorganic ion transport and
                     metabolism]; COG0370"
                     /db_xref="CDD:440139"
ORIGIN      
        1 mastsmrial ignpncgkta lfnqltgarq kvanyagvtv erkegafitp agktirvldl
       61 pgtyslapts ldekvthdvl hgiysgelap elivcvvdat nlrlhlrfvl eilalgrptv
      121 lalnmmdsar rrgievdvpa larelgvpvv etvaiarpgv raltdtldai aqagdssdha
      181 arhittpdth dlhaevrrim giavrvpdmt nglderldrv alhpvigtvl laivmflifq
      241 avyfigkpmt daigdgfgwl geqagiylpd gplrslvvdg ifgglgtvlg flpeilvlff
      301 filvleesgy lpraaflldr mmvevgltgr sfipllssfa caipgimgtr siadprqrlt
      361 tilvaplmtc sarlpvyall igafipsrpv lgvfklpglv lfamyiagia gamavgwvsk
      421 rlrgarsqpp llmelpsyrm pkvrnlalgl wergwmfvrr ltgvilaltv imwfistfps
      481 appgatgpai dysfagyigr alqvifgtlg fnwqisislv pafaaretav talatvyava
      541 ggaddtagla aalssnfsva talsllawfa fapqcmstla virretrswr yvlisfsymf
      601 glayfvsfvt yrlaswll
//
LOCUS       WP_010804926             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YbhB/YbcL family Raf kinase inhibitor-like protein
            [Pandoraea].
ACCESSION   WP_010804926
VERSION     WP_010804926.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..182
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=18837
     Region          25..181
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mkigkfiftf faglfvvsna iaggfaiqsd diagghfdna qisdgfgchg gnispaisws
       61 gepagtqsfl vtmydpdapt gsgfwhwvva nlpasvhtld lgagsevgrl pkgamavrnd
      121 tgkaaylgpc ppegeshryi itvaalkvps lpvdstatpa vvgfvahyqe lakatitiqy
      181 ar
//
LOCUS       WP_010804952             469 aa            linear   BCT 01-JAN-2025
DEFINITION  lactate utilization protein B [Pandoraea sp. SD6-2].
ACCESSION   WP_010804952
VERSION     WP_010804952.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..469
                     /product="lactate utilization protein B"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51928
     Region          1..454
                     /region_name="LutB"
                     /note="L-lactate utilization protein LutB, contains a
                     ferredoxin-type domain [Energy production and conversion];
                     COG1139"
                     /db_xref="CDD:440754"
ORIGIN      
        1 mntgqrvdha knaeaflakt ehvafhdkrl wdlrmkrdaq aasigewetl rtlasqikeh
       61 tlsrlgdyld qfatqaeang vkvhwaldaa ahnaivhgil aahgvrtlvk sksmltdece
      121 lreyleprgi hvmetdlger iqqldkqpps hvvvpavhkl rgdvarlfgr tlgtdpandd
      181 vhylaesqrq ttrpafleag agmtgcnfav aetgtvvvct negnadlsan vppvhivsig
      241 ieklipriad lgvfvrllsr salgspitqy tshfrvprpg temhfvivdn grsarlamdd
      301 fwyslkcirc gacmntcpvy rrssglsygs tyagpigail npaydlkrys alpfastmng
      361 sctnvcpvri niheqlykwr qivaeegelp rvkrslikva gkllanpvly rtsvksmnta
      421 lhrlpnmvly nplntwgkgr dlpdapkqtf rdwydanrks pdtgrkdps
//
LOCUS       WP_010804953             260 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: (Fe-S)-binding protein [Pandoraea].
ACCESSION   WP_010804953
VERSION     WP_010804953.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..260
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27925
     Region          <2..242
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mkvalfvpcf idalfpevai atlelleklg vtvdyprrqt ccgqplanng ceadatgtet
       61 lfvenfagyd yivspssscv hhvrkhltaa geservaavr antyeltefl hdvlkvrdfp
      121 waafshtvgl hnscsairhl haasaseipg epwskartll egvrgirfaa prrpdeccgf
      181 ggtfsvseqa vsvkmgqdkv rdhldagaqf ivsadmsclm hqkgcaartq tpmrflhiaq
      241 vlngvdvgap aaatpnevta
//
LOCUS       WP_010804964             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pandoraea].
ACCESSION   WP_010804964
VERSION     WP_010804964.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..157
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17308
     Region          4..144
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mhhieidrid vrllgilqsn grisnlelae aiklspaqtl rrhrrleemg vikgydtrld
       61 aqrlgfgvva fvhvtmergh irdlsnfkgl vaelaqiqec fsvtgdidyv lkvvardlka
      121 lsdflldtlm ripgvsavks svcldeikct savplsa
//
LOCUS       WP_010804972             319 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Pandoraea].
ACCESSION   WP_010804972
VERSION     WP_010804972.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..319
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34760
     Region          24..234
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16282"
                     /db_xref="CDD:293840"
     Site            order(79,81,83..84,166..167,185,222)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293840"
     Site            order(79,81,83,166,185,222)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
ORIGIN      
        1 makafasqad leakkvtftq lsentwayta egdpnsgvii gddgvmivdt tatpamaqdl
       61 iakirtvtdk pikyvvlshy havrvlgasa yfaegaqqii asrgtyemiv ergeadmkse
      121 ierfprlfag vetvpgltwp tlvfekeitl flgklevkia hlgsghtkgd tvvwlpsqkv
      181 lfsgdlveyd aacytgdaql aewpatldal aalgaeklvp grgpalttpe evakglaytk
      241 dfvttlfeag kqaveqkldl kgamaltrsq mdpkfghvfi yehclpfdvt rafdeasgit
      301 hpriwtaqrd kemwtalqn
//
LOCUS       WP_010805017             467 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Pandoraea].
ACCESSION   WP_010805017
VERSION     WP_010805017.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..467
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49564
     Region          2..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 manrdsgahl qsslkqrhms mialggviga glfvgsgvvv haagpaavls flitgalvvl
       61 vmrmlgemac alpavgsfye yarlawndkp vggelagflt gwmywyfwvi vvaveavaga
      121 nliqfwlpgi pawaislall vvltltnlvs vasygefefw fasikvaaiv vflflgalfv
      181 sglwpgavas tgnllshggf mpngigpvma gavaatgfyf gaeivtiaaa eaaepqqava
      241 ratnsvigrv lffyigsill vvmlvpwnsa gmatpyvsal eamripaaah imnavvltav
      301 lsalnsglya ssrmlfaltr rgdaprslar lnargvpvra ilvgtvfgyv avvmsyvspd
      361 tvfaflvnsy gtvaifvyvl iafsqlklrk rlerdapgkl kvrmwgypyl twvaitgmls
      421 ivtamafipd qrtplalgia sltvllvaft vrsiwrklrs pdpgfei
//
LOCUS       WP_010805027             503 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [Pandoraea].
ACCESSION   WP_010805027
VERSION     WP_010805027.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..503
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54322
     Region          12..487
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(67,69,73,76,80,113,116..117,126..133,138,141,144,
                     237,241,244,247,249,423,425..426,428..429,432,435..436,
                     438,440..443,452,456,458,472,479..484,486..487)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(153..156,164,179,182,212,229..232,235,253..255,287,
                     388,390,416)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(156,253,284,287)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mqafndtadv vhyiqgqrvk gnsertqpvf npatgasarr lvlgetsdvd aavasakaaf
       61 pawsdtppir rarvmlkfle lmnkhrdela aiitaehgkv fsdaqgevsr gidviefacg
      121 ipqllkgdyt eqvstgidnw ttrqalgvva gitpfnfpcm vpcwmfpvai aagnafvlkp
      181 serdpsaslf madllkqagl pdgifnvvqg dkvvvdallt hpdvkavsfv gstpianyiy
      241 etgakhgkrv qalggaknhm vvmpdadldq aidalvgagy gsagercmai svavlvgdva
      301 dkimdrlaer artlvikngm epdaemgpiv trqsleries yialgveega klvvdgrglk
      361 vpgheagfft ggtlfdhvtp emriykeeif gpvlacvrvk dfteavdlin ahefgngvac
      421 ytrdghvare fgrrievgmv ginvpipvpm awhgfggwkr slfgdmhayg eegvrfytkq
      481 ksimqrwpes tekgaefamp tak
//
LOCUS       WP_010805031             421 aa            linear   BCT 01-JAN-2025
DEFINITION  M20 family metallo-hydrolase [Pandoraea sp. SD6-2].
ACCESSION   WP_010805031
VERSION     WP_010805031.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..421
                     /product="M20 family metallo-hydrolase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44041
     Region          24..416
                     /region_name="M20_bAS"
                     /note="M20 Peptidase beta-alanine synthase, an
                     amidohydrolase; cd03884"
                     /db_xref="CDD:349880"
     Site            order(95,106..107,140..141,148,202,205,225,227,300,
                     368..369,394)
                     /site_type="active"
                     /db_xref="CDD:349880"
     Site            order(205..208,211..212,227,238..242,244,247,251..252,
                     254..256,258..260,262..263,265..266,273..280,284..285,
                     287..290,298,300,367)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349880"
ORIGIN      
        1 msmlfpatsp dgamsdlrid lprllariaa laevgaidgg gcsrlaltdd dgegrkrvvg
       61 wmrdlgltvs vdaignvvgv ragredgppv mtgshidtvr tggrydgnlg vlagleviaa
      121 lndagivtrr plavgfftne egarfspdmm gslvyvggmp lddalgtvgi dgttvsenlt
      181 rigfagqrpv gkpdvhafve lhveqgpvle hegitigavt gvqgihwtef tvegvsnhag
      241 ttpmrmrhda gyaactiasf arevarelgg aqlatvghvs vspnlinvip nravftvdlr
      301 ntdaevlaea vrrvfakada vaeaegvrit hrsladfapv qfderivarv eslararghs
      361 vrrmpsgagh daqmlarvcp agmifvpsvk glshnvaeft hdtdigagan lllaimtela
      421 a
//
LOCUS       WP_010805035             445 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Pandoraea sp. SD6-2].
ACCESSION   WP_010805035
VERSION     WP_010805035.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..445
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47987
     Region          1..444
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msftslglid pllrnlqern yqtptpvqak aipavlsgkd vmaeaqtgtg ktaafalpll
       61 qrlvqhgpav ssnrarvlvl vptrelaeqv lqsfvaygkg ldlrflaayg gvslnpqmmk
      121 lrkgvdvlva tpgrlldlnr qnavqfdqvq tlvldeadrm ldlgfsreln avfaalpaqr
      181 qtllfsatft ddiramassi lrspvnvsvn ppnttvskik qwvvtvdkkn kpdlfmhlva
      241 enhwqhalvf vktrngvdyl aaildeagya vdtihgdkpq parlralerf ktgevqmlva
      301 tdvaargldi ddlplvinvd lpivaqdyvh rigrtgraga sgvavslvca deapqlaaie
      361 alirqtlpre evpgfeaehr vpqtsatgqi ikkpkkpkkp kvpratpggl papskkprsq
      421 pagkpatgsr kpagklaggh gkrrp
//
LOCUS       WP_010805043             531 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Pandoraea sp. SD6-2].
ACCESSION   WP_010805043
VERSION     WP_010805043.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..531
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56527
     Region          33..423
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(34..35,38..39,42,73,123..124,126..128,131,152,
                     155..156,159,284,287..288,291..293,296,324,328,381..382,
                     386,390,406,409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mapspstphs agqvlpfrqs lvamlglcfc tmmvaldqtv vgtalptiva elkgfeyyaw
       61 vatsylltsv itvpifgrlg dfygrkpfvv aaiivftaas vlcgaatsmp flviaralqg
      121 igggmlvgta facipelfpd shvrlrwqvm lssafgiana igpslggflt egygwrsvfy
      181 vnvpvgllgl wfvarhlphm raeghgkasl dwlgallita algslqmlve wlpadglsrg
      241 vvtllvvlav ssyalywwek rtshpilpfe mfrdkslapl fvlsvfagfa mfgvlfyapl
      301 mlqggfglsp retgllitpm vvcitvgsiv ngrlitrlrn pnvmlyggff llalacagvv
      361 tthrgtphgl iatymllagl glgfvmpnlt vfaqevagra hlgiatalmq slrmiggmlg
      421 taivgtlvnh sytarvkeal avsegsqwta qlsdpqilvn tqaqndfmmt lahmgqngal
      481 fiesartslv aaihngqmvs laaalaglwf vrrvplirlt rgakpqapag e
//
LOCUS       WP_010805061             145 aa            linear   BCT 01-JAN-2025
DEFINITION  HIT family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010805061
VERSION     WP_010805061.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..145
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16096
     Region          1..116
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mecpfctgdg gevvwrdpvl rvvlanepgy pgfarviwha hvaemsdlpe aarehvmrvv
       61 fgvetalrtv mspdkvnvas lgnrvphvhw hvipryrddv hfpdsvwsap qrevpqpvla
      121 eraawmpalr gaivaeldrv pawpa
//
LOCUS       WP_010805098             456 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Pandoraea sp. SD6-2].
ACCESSION   WP_010805098
VERSION     WP_010805098.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..456
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50242
     Region          37..433
                     /region_name="OapA"
                     /note="Cell division protein YtfB/OapA (opacity-associated
                     protein A) [Cell cycle control, cell division, chromosome
                     partitioning]; COG3061"
                     /db_xref="CDD:442295"
     Region          223..416
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mwpklrdffa relltlidpt qpkhrrrkvq ivatvgsalt lgmvtafgva pmvpeaarng
       61 asvtlpltfp dlakqiqqld aqsqtfihqv alrrgetlgd mlsrlsiqdp taerfirena
      121 varrligvpa gqvvqaetdd dgklvslstv lstgstgaqq lvierndddr lrarmeqltn
      181 dtewamrsga iadnfftamd dagvpdavva qmvnifsgvi nfqrdvrrgd rfrlvyevvk
      241 qqdrtvrtgr vlavefinqg kthqaiwyae pqgapegayy gfdgrnlkqa flrtpvefsr
      301 issafggreh pfqhqwkkhe gvdlaapigt rvfaagdgvv tfvgsqsgyg nlvmidhagn
      361 yqtryahlsg fgqgmkagtr vtqgqvigfv gqtgwatgph lhyelryngv prnpfstdva
      421 avaplsgarl kvfdmyaenl lkridlmrtv qvaerd
//
LOCUS       WP_010805102             238 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010805102
VERSION     WP_010805102.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..238
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26565
     Region          11..207
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mtgttttltl irhgetdwnr vkriqghtdi alstegerqa vllgeriare vaahghvfdh
       61 vltsdlqrav qtaapvahac glplvrtasl rerhygtfet rmpdeiqaaf pqeysrwqsr
      121 dpdfvipgge strgfytrit dfvvqlvrey egqhlalvah ggvldccyrl amelalsepr
      181 sypllnasvn rlaydgarwq vlswgdvthl ddavrdesnd kpvdvhgrat drvdprvv
//
LOCUS       WP_010805150             450 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [Pandoraea].
ACCESSION   WP_010805150
VERSION     WP_010805150.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..450
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50203
     Region          15..429
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 menlllivaa illvflngff vaaefglvkl rqtrvqiiar qrgwrgrila kvhgkldtyl
       61 sacqlgitla slglgwigep afariltplf aalgvssael ihalaffiaf ftisylhivv
      121 gelapksmal rvpeavsiwt aaplyafywl mypaiwvlnh sanrllrwtg ldpshgadah
      181 ysadeiklim rrgassekls rddwnvvaya idfsdltvsd lmhpmsevaa frrnatfeqn
      241 mdtayghrys rypffdndge tvlgvvhlkd lflaehhgqs iqdlgsmarp vervrpdmpa
      301 relfgrfrrg aphfaivgwp dqkpigfltl dnllsalvgk irdefrqted dwtrmedgtl
      361 igrgslpilt leralgidip seraesvggl imdtlaylpr egqkidfngf svvvkkmqgp
      421 rivlvriypd gvreargepp sdaatqqrde
//
LOCUS       WP_010805153              67 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Pandoraea].
ACCESSION   WP_010805153
VERSION     WP_010805153.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..67
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7228
     Region          1..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 metgivkwfn dakgfgfitp daggedlfah fsevkvdgfk slqenqrvsf evktgpkgkq
       61 aanikpi
//
LOCUS       WP_010805157             224 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Pandoraea sp. SD6-2].
ACCESSION   WP_010805157
VERSION     WP_010805157.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..224
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=24006
     Region          1..224
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mqellaviti tvlavispga dfamvtresw rygrragmwa avgiaagvqv hviytlvgvg
       61 lliaqvpwlf avikwmgaay lmyigwrtlr drapvadvir eegatgatga sarcaglgvs
      121 gpthweeaas alrkgfftna lnpkttlfvv stftqivhpg tgwalglayg vfmsfahwaw
      181 fslvalgfsa gwmraamvrr qhivrrtigg alitlgglla mtnr
//
LOCUS       WP_010805176             233 aa            linear   BCT 01-JAN-2025
DEFINITION  SH3 domain-containing protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010805176
VERSION     WP_010805176.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..233
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23455
     Region          5..97
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
     Region          <133..>186
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 mnqwtlplvl agaatlvmlp daataqsgqa vinapanvra gpasaypiva qagagmpvtv
       61 ygclsdyswc dvglpgtrgw vyaallsypy qgnpvpvlny gtmiglpivt fsigtywgny
      121 yrnrpwyhdq rywhrpppgs rppawggpgr ppghypgpgs rppghgagpr ppgygashgp
      181 gprppshgag pgprppgggg ghgprpsggg hggghggghg ghppgggpgg pnr
//
LOCUS       WP_010805203              67 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Pandoraea].
ACCESSION   WP_010805203
VERSION     WP_010805203.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..67
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7197
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mdtgtvkwfn dskgfgfitp daggddlfah fsevrgdgfk tlaenqkvty etkrgpkgmq
       61 aanitpq
//
LOCUS       WP_010805211             465 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Pandoraea].
ACCESSION   WP_010805211
VERSION     WP_010805211.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..465
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49160
     Region          36..439
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(49..50,53..54,57,89,139..140,142..144,147,167,
                     170..171,174,272,275..276,279..281,284,312,316,366..367,
                     371,375,391,394..395,398..399,402)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnptlasqas qsaaggdnaa aldsriaqet igqlfrrilp flilcyivaf ldrvnvgfaa
       61 lhmngdlgft atvygfgagi fsigyfvfev psnlilhrvg ariwiarimv twgfvsagfa
      121 fvsgetsfyv mrfllgvaea gffpgivlyl slwfpgrama rataifilgl plavligapl
      181 stailtsfhd faglrgwqwm fllegalavv vgviayfvlg sspdkitwlt etqrdwlvrt
      241 laqeraakes arqysvmqtl lsgkvlllal aifcnitalf gitlwmpqii kgiggldntr
      301 agllsavpyv cagiamvina rhsdktgerr whilvpaaig avglvmagsa tspyvgiigl
      361 ciaaagilas nilfwplapm fltgaaaaag iglvnsvgnl ggfvgpyltg wakdtfggys
      421 asmntlsvmv liyglllfaf ltvttrragi vsahaatpvr gtaar
//
LOCUS       WP_010805212             506 aa            linear   BCT 01-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Pandoraea sp.
            SD6-2].
ACCESSION   WP_010805212
VERSION     WP_010805212.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..506
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54510
     Region          3..502
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mniantlara avrhpahiat ylgespqfdy atlarrcagi agglrslela dgarvalwmr
       61 nrpeylewly aiwwaglvav pinaklhpre aafivgdsqa evvlaeaeda qalaeclatp
      121 ticlspeddr vrewvkadas qsvpvasren tdlawifyts gttgrpkgvm lshrnlwsma
      181 acyiadvdav gredrtlyaa pmshgaglys vvfmmqaagh vfpasggfda qemfaladsl
      241 ggiscfaapt mvnrlvrhaq aagassegfk tivygggpmy tadieralsv mgsrfvqiyg
      301 qgespmtisv lprdciatre hprwpqrlas vghahamvev evvdsdgvpv psgtagevvv
      361 rgdvvmqgyw rnpeataktl rngwlwtgdi gvldddgflt lkdrskdvii sggtniypre
      421 veevllradg vaevavigep dpewgevvva yvvctpgaal esaeldkhcl ahiarfkrpk
      481 ryvpvdalpk nhygkilkta lrvgga
//
LOCUS       WP_010805326             312 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010805326
VERSION     WP_010805326.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..312
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32862
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..296
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(117..118,120..121,124,128,130..136,226..231,
                     237..238,240..241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdrlkcmevf vqvvragsls agaaacgmsa vtaarhvqvl earlgqpllr rngrrqvpta
       61 lgqryfaeca evlarvenad algdagpaga smpgaisrpv gqlrvsaptt vgshllmpif
      121 aeylqshpdv aldlalkdrv vdleeegiha afqaggnpvp glvahtlrgv trvacaspay
      181 larrgvprqp vdlaghdclg fryddvlgrw vftqagasgg tvrdarliah nplaqlqaav
      241 hgmgiallpe yllapevqag rlvrvleadv qlsepmhlvh lagrfvsskl ddfvrymvak
      301 lgpeacpaat sa
//
LOCUS       WP_010805057             740 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Pandoraea sp. SD6-2].
ACCESSION   WP_010805057
VERSION     WP_010805057.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Thurner,C., Vela,C., Thony-Meyer,L., Meile,L. and Teuber,M.
  TITLE     Biochemical and genetic characterization of the acetaldehyde
            dehydrogenase complex from Acetobacter europaeus
  JOURNAL   Arch Microbiol 168 (2), 81-91 (1997)
   PUBMED   9238099
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18097562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..740
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78735
     Region          <49..206
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          201..735
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mrelrfsqrp gvavgdftgl trraflktsa iaagglmlem slpgavrtas aqgaaatpvv
       61 psafvhigtd ntvtiqvnrl dfgqgvqtal pmlvaeeldc dwskvrsela paadvykdpl
      121 fgiqmtggsg svahswlqyr rigasaraml iaaaaqqwkv paaqlrteng vvlgpngqra
      181 tygslaaraq tlpvpadval kdpsafrllg kptgrldara kstgvpmygm dfklpnlkva
      241 vvarppvfga kvkrfdakaa ravkgvrdvl eipddrggta vaviadgywq aktgrdalna
      301 twdtgsvehv dttaqlakfi emaktpgtva idgdisklkg apktlvaeys fpylahapme
      361 plnctvqlsd rgaevwtgtq fqtvdqaaia rtldlkpeqv klhtlmaggg fgrravptsd
      421 ygveaaqvak awrraghrep vkviwsredd irggyyrpmy vhraeiglda kgnvlawnht
      481 ivgqsilqgt pfekmmvkng idgtsvegvl gtpyavplrl tlhspqvnvp vlwwrsvgnt
      541 htafvmetli delaknagqd pvayryalmg dkhprhreal alaversgyg kaklpagqaw
      601 gvavhesfds vvayvvvaem rngsprlisa tagvhcnfav npltvaaqve gaalmglgtt
      661 lpgaaitlkd geveqsnfhq ymvarltdmp aisvhvvssg daptgmgepg lpplapayan
      721 alfgltgkrq ralpfevtqa
//
LOCUS       WP_010805342             167 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Pandoraea].
ACCESSION   WP_010805342
VERSION     WP_010805342.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..167
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=18867
     Region          1..167
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 madspraklr ellvqrygql ktllsrklgs sdlagdalqd twlrlenten iepvrnpgay
       61 lyrmayhaai dkqraedrrl svgeietmld lvspepgpaq iaeansdlna larvleqmpq
      121 rrrdillavr ldglaqreva erfgislrlv elelkraqef cadqmer
//
LOCUS       WP_010805388             376 aa            linear   BCT 01-JAN-2025
DEFINITION  LVIVD repeat-containing protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010805388
VERSION     WP_010805388.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Adindla,S., Inampudi,K.K. and Guruprasad,L.
  TITLE     Cell surface proteins in archaeal and bacterial genomes comprising
            'LVIVD', 'RIVW' and 'LGxL' tandem sequence repeats are predicted to
            fold as beta-propeller
  JOURNAL   Int J Biol Macromol 41 (4), 454-468 (2007)
   PUBMED   17681373
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..376
                     /product="LVIVD repeat-containing protein"
                     /calculated_mol_wt=41852
     Region          4..372
                     /region_name="COG5276"
                     /note="Uncharacterized secreted protein, contains LVIVD
                     repeats, choice-of-anchor domain [Function unknown]"
                     /db_xref="CDD:444087"
     Region          21..59
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          66..110
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          117..158
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          175..219
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          227..285
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          296..336
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
ORIGIN      
        1 makawntrlv shidcpgggq vwvdrnilyv shmrppagts iydvsdpkhp rllatlevpm
       61 gwhshkvrvq dgvmlvnyek fregapdfgg glgifditrp seprlisrwy sggeaggvhr
      121 ydfdgrfayi sptaegfvgn ivkildlaqp erpeevgrww ipgqnvgage eypwddyvrp
      181 rchhplrmgd rlyvsywhhg ffildisdms spklisgins gpahphptht alpipglvkg
      241 rrvmvvaded vaklrpspps fawvyditde rqpmpistfq vagvdpdgsp repmsgchqp
      301 serfvgttlp fawfakgmrl vdlsdpfapr eiafyepdap agcerassnd vtiddrglvy
      361 lldrqqgidi iecfpg
//
LOCUS       WP_010805359             325 aa            linear   BCT 01-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator [Pandoraea
            sp. SD6-2].
ACCESSION   WP_010805359
VERSION     WP_010805359.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..325
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35805
     Region          <1..308
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mlatlsrarm lidrqlpili lgetgtgkey lsralhdyst rrrasmisvn cssipenlie
       61 selfgyrrga fsgalnsgmk gkveqadggt lfldeigdmp aaqqtrllrv lserevtpig
      121 athpvavdlq licathqnle arvqagsfre dlyyriavgi vnlpplrlrq drawllnsmf
      181 itesqgnatl dsldsetrel lltyawpgnl rqmraavqya cavksddtir lrdlpanlvh
      241 satsaataia pmpvavaaap ldslspiahg ereiiirvls srrwnisaas relgicrtsl
      301 yrklrelhip hvrdmgsdvl rgpqr
//
LOCUS       WP_010805395             303 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010805395
VERSION     WP_010805395.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33358
     Region          9..>160
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdsvenvraf lavvemgsft aaarrldvsa pvvtkrvsal ekeldvllfq rttrsltlts
       61 sgrdmlgsar dflsayerla eraavddrsl ggrlrvkapa sftnhflgkl lnefflshpk
      121 asielqltnr avdpvlenfd fvitglpvty dgveefplcp fkrhvyaspg ylaqhgtpgh
      181 psdlpghrcl lysyqstvrt wtftdaragd iqvsvdggfa tndidamhna cldgmgvail
      241 pryrandsvq agrlvqllpg fglpdywikv lrpanhhnpk lfhalldflv tglarleqqg
      301 tyl
//
LOCUS       WP_010805433             378 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pandoraea sp. SD6-2].
ACCESSION   WP_010805433
VERSION     WP_010805433.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..378
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42120
     Region          4..376
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mssdvvirvv qsiedvpada wdalaganpf vqhaflhamh tsgcaskrtg wqpayllmha
       61 gdtlvgampl yvkshsrgey vfdhawadaf arhglnyypk llcavpfspv tgprllarth
      121 adrvalarga iafakqlels sihvlfthdd dlaalteagy llregvqfhw enpgfatfdd
      181 flaqmnqekr kklrqdrrrv rdagvtyrwl rgadideaal dffyqcydnt yrehwnapyl
      241 sraffgqvha smpdalvlvm aerdgaplac alnvvsgdtm ygrywgttdf vsgmhfetcy
      301 aqgieyciah glrsfeggaq gvhkmsrgll ptptwsahwi adqrfadaia efldseasam
      361 dehigeleah tpfkrpas
//
LOCUS       WP_010805494             249 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Pandoraea sp. SD6-2].
ACCESSION   WP_010805494
VERSION     WP_010805494.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26453
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvpvkrv vdynvkvrvk sdgsgvdian vkmsmnpfde iaveeavrlk eagvatevia
       61 vsagvaqaqe tlrtalaiga drailiesde elqplavakl lkavvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaklpqa tfaskvtvad nraqvtrevd ggletvslsl pavittdlrl
      181 nepryvtlpn imkakkkple tlkpadlgvd vsprlktlkv aeppkrsagv kvadvaalvd
      241 klkteakvi
//
LOCUS       WP_010805487             274 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010805487
VERSION     WP_010805487.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 274)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..274
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29156
     Region          5..271
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mstpllqtha ltlragkrvl vdwldlavaa gecwclagpn gagkttllnt laglrpiddk
       61 pqrdatiags grvdiagkpl aqwrpaplar mralmpqqtr dafgatalev alagrhpyla
      121 qgrwgawesd ddiasamaal aqvgledfaa rdvttlsgge rqrvslaavl aqatplllld
      181 epvshldlhh qidaleqlaq haqradaaai fschdlnlar rfathallld grggwragpv
      241 hdvlsaehcs nafgyplrli rdggdealvp vrra
//
LOCUS       WP_010805495             489 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: catalase [Pandoraea].
ACCESSION   WP_010805495
VERSION     WP_010805495.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..489
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55114
     Region          5..485
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mskekdssdt gsttgagapa asdrntlsvg adgplllhdv hfieqmahfn rekvperqph
       61 akgagafgvf ettedvsryt kaslfrkgak vemlarfstv agesgspdtw rdvrgfslkf
      121 ytdegnydlv gnntpvffvr dpmkfphfir sqkrlpdsgl rdnhmqwdfw tnnpesahqv
      181 tylmgdrglp rtwrhmngyg shtylwinas gekfwvkyhf hteqgmeffs naeaatmsgq
      241 dadfhrrdlf daivrgehps wilrvqvmpy adakqyrfnp fdltktwshk dyplikvgkm
      301 tlnrnpenff aqieqaafsp gntvpgigls pdkmllgraf ayndaqrnri gtnfhqlpvn
      361 rpkvpvqsym fdghmafehs gnaptyvpns ggrpyadqtg paedgwesdg amvrsaytlh
      421 kedddfsqpg nlvrhvfdda artrlvetvs gallagvrsp vlerafdywk qidkdvgari
      481 eqavkrark
//
LOCUS       WP_010805497             365 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: saccharopine dehydrogenase family protein
            [Pandoraea].
ACCESSION   WP_010805497
VERSION     WP_010805497.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..365
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39147
     Region          1..>34
                     /region_name="PRK12409"
                     /note="D-amino acid dehydrogenase small subunit;
                     Provisional"
                     /db_xref="CDD:237093"
     Region          26..358
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mkkiallgag higqtiarll hdsgdyrvtv fdrnplasav vheyadafve ltgsdtgslr
       61 kaisghdavv nalpytmats aataavaagc hyfdltedva athaiqqlae gastalmpqc
      121 glapgfiaia ahhlaaafdq vdsvkmrvga lpafptnslk ynltwsvdgl ineycqpcea
      181 irdgvrltvq pledlehfsl dgveyeafnt sgglgtlcet lsghvrdldy ksvrypghga
      241 lmkvllnelr lkddqetlkt mlkravpstl qdvvlifvvv sglrsgvltq evfarkifae
      301 rnnghsasai qittasaica avdmffagql pqrgfirqeq ialpdflanr fgqayahstr
      361 iesls
//
LOCUS       WP_010805521             131 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydroneopterin aldolase [Pandoraea].
ACCESSION   WP_010805521
VERSION     WP_010805521.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Illarionova,V., Eisenreich,W., Fischer,M., Haussmann,C.,
            Romisch,W., Richter,G. and Bacher,A.
  TITLE     Biosynthesis of tetrahydrofolate. Stereochemistry of
            dihydroneopterin aldolase
  JOURNAL   J Biol Chem 277 (32), 28841-28847 (2002)
   PUBMED   12039964
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..131
                     /product="dihydroneopterin aldolase"
                     /EC_number="4.1.2.25"
                     /GO_function="GO:0004150 - dihydroneopterin aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=14817
     Region          11..130
                     /region_name="FolB"
                     /note="Dihydroneopterin aldolase [Coenzyme transport and
                     metabolism]; COG1539"
                     /db_xref="CDD:441148"
ORIGIN      
        1 mhsalshprl mdcrrmflrd yevfinigvh dyekrgeqrv linvqlfvpl aestpvadkl
       61 devvdydfmr etiakrvgqg hihlqetlcd dvasallahp rvravgvste kpdvypdchs
      121 vgievfkmkd a
//
LOCUS       WP_010805556             241 aa            linear   BCT 01-JAN-2025
DEFINITION  urease accessory protein UreF [Pandoraea sp. SD6-2].
ACCESSION   WP_010805556
VERSION     WP_010805556.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..241
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25816
     Region          16..241
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mtaslasplt epvataslqs laallhlasp alpigafsys qgleaavehg ivhdapsaer
       61 wiasqldgvf ttgemallar qwrhwqandi asltrvndwl latreaaelr aeteqmgwsl
      121 tqlalalewg epaqrehlaa lrpmalataf afaalthgap ladtlvayaf swlenqvaga
      181 lkavplgqla aqrvivalrp rvveaarraa slpddeintf spalailasr hetqysrlfr
      241 s
//
LOCUS       WP_010805592             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010805592
VERSION     WP_010805592.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..222
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24291
     Region          10..221
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mlhptpttvq lremilkgdl apgerlaeak laeqlgvsrm pvrqalpvla eeglvvragq
       61 rgyavrahtr eesvealhlr galegyaarl laekgasael lhqlrdllae gdsllaghtm
      121 taevqigyas lnarfhdllv tgarnplleg fiarcnlvpf vaprtvafgh ddrrqyadii
      181 ayahrqhhai veaiaarqpd raefmcrehi vtqehsmgaq ll
//
LOCUS       WP_010805589             446 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pandoraea sp. SD6-2].
ACCESSION   WP_010805589
VERSION     WP_010805589.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..446
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=47331
     Region          42..101
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          146..204
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          234..435
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(249..250,252..253,256,260,262..268,364..369,
                     375..376,378..379)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 msidaavslt ntpaaprlac hergtwsrap qsneaallcr klrglramva vlecdsvara
       61 armlhlsqsa varsisdiea elgfplfhrs grglipnaag qrlgvrasra laelangyre
      121 afaatasqad ggaraasrfa avvapqhlts fiavaelgsg plaasrlqcs qptiqrnldq
      181 ledligiklf rrtprgtrlt deaqallgpv kralaelaia edelapfggr qqgtvivaal
      241 plssgfllpk aidsllhksp ylsvtvvdgt yealvrqlrq advdlivgal randvppdir
      301 qealfedhls vvaradhpcl ssgctptlae lagygwvspl pctparsvfe rvfhaeglpl
      361 pqtqvhasss pvvrgllsss drlallspvq itselrtgel avvpvplyha rraigvamrr
      421 dgllspaaeq lldelrglvp tmqhpt
//
LOCUS       WP_010805630            1053 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pandoraea sp. SD6-2].
ACCESSION   WP_010805630
VERSION     WP_010805630.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..1053
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112508
     Region          1..1013
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnlselcirr pvmtillcva avvagliayg qipisalpsf nspviqvtat lpgaspetma
       61 asvaapmekq fstiagvavi sstntqgtts iiiefdsdrd idaaavdvqa alfraqrklp
      121 vemttppsyr kvnpadapil flamnspsms laelddyaen lvsptlstlp gvaqvlifgq
      181 krfavrvkar pdalaarklt lddvaralas ananspvgtl dgtrqtltie anrqmtkaeq
      241 fanliiasvn gspvylrdva evqdsvesvk tgswvngers ivlavlrqpn antvatvdqv
      301 kaalprlaeq mpqsiqvkll ndrsvsires iddvqftlgl tvilvtlvif lflrrlaatl
      361 ipvmslpvsl igtvalmkgm gysidnisll gitlavglvv ddaivmleni vrhiengvpp
      421 lraalvgsre mgftilsisi tlvavfipif fmpgviglmf hefavvvsla ilvsaavslt
      481 lipmlcsrfl kheqdeglgl ratqwfedgf vwvqngyvrs vdwclahrqw vmaaaaatfv
      541 atgvlfatip kgffpsedig qvqvtaegaq disftamsal lrqagdiira npavetvivs
      601 asdsnqgrmf vnlkphgerp hmsevleglr rdvkqvpgln vyfnpvqnlq lggkqsksry
      661 qyvmqsvkpg emqlwsgrlm tlmradpifr dvttdaqmkg lqaqltidrd kantlgvaig
      721 dirsalysaf gerqvstiyt psdsyqvilq addndrrdeg afdkiyvrgk ggalvplsav
      781 atverkmgpv svnhqgqlqa itlsfnlapg aalgdaaqki vgfqrqlgfp psiitswggd
      841 aaafqksqss qivllvgall viyvllgvly esyihpitil aglpsaavga litlrlfgmd
      901 lsliavigvl mligivkkna immidfalda qrnggmtptq airqacalrf rpimmttlaa
      961 lmgalpialg lgagaelrqp lglavvggll fsqvitlyit pviylyldrf agkgplvlpg
     1021 dkaandsret dhnggnahgs arvvdgthad aap
//
LOCUS       WP_010805708             326 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [Pandoraea].
ACCESSION   WP_010805708
VERSION     WP_010805708.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..326
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36019
     Region          122..323
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mgntpfyifa vllflavvla vegiyywwss qhsaaakrvk ariralsagg nvdrehisil
       61 ksrllsgspg vermllrmpr vhaldlliqq sglswsvahl lmwmlvhglg lamlvlllpl
      121 twrlavpagl igaslpalyv srrrgkrler lerqlpetad tiaralragh afpaaiemig
      181 nemaepigge frimfdeiny gvgindalrn latrvpiddl ryfitavmiq resggnlaei
      241 mtniaeltre rlkllqkvrv lsaegrlsai ilevlpfgaa gllmivnptf levlwkdpag
      301 ikisvtalgl malgmlwmrr ivrihv
//
LOCUS       WP_010805721             311 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010805721
VERSION     WP_010805721.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10627418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..311
                     /product="phosphatase PAP2 family protein"
                     /calculated_mol_wt=32279
     Region          95..272
                     /region_name="PAP2_3"
                     /note="PAP2 superfamily; pfam14378"
                     /db_xref="CDD:433919"
     Site            order(164,172,214..216,248,254,258)
                     /site_type="active"
                     /db_xref="CDD:238813"
ORIGIN      
        1 mnwlqinltt valaalalgw lgmgvelasl ampglaclal aclwavytwc rpdarigaaa
       61 ghviglivft haaaaldyav vatgaplvdq vlttldgrlg fdwtawhatv rgsrmlslvl
      121 playdsgmpq ialvvlllsf tgrfaelrqf anamtgacla tiaisglipa agafvhfggs
      181 pgelatlshf aplrahtltv vdlsalqgli smpsfhavma vllayavrrc raafavlapl
      241 nalvllstls egghylvdvl agialaivai kltrrhgvpl ktpslptpal tsepvhergl
      301 aatrqvsget s
//
LOCUS       WP_010805737             136 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Pandoraea].
ACCESSION   WP_010805737
VERSION     WP_010805737.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..136
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14193
     Region          15..135
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 maadaivtah lgaagftthl tdgkhewsad epatlggadl gpvpaallls slgactsitl
       61 qmyarrkewp lkdvkvtlam npdgkppagt tqitrkiela gdlseeqrqr lleianacpi
      121 hkvlsgtiai dstlve
//
LOCUS       WP_010805741             234 aa            linear   BCT 01-JAN-2025
DEFINITION  energy transducer TonB [Pandoraea sp. SD6-2].
ACCESSION   WP_010805741
VERSION     WP_010805741.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..234
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24240
     Region          154..232
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mstavppsgl altqiqdplt spraiaiaaa ivvlhiaalv glshlrsdpe katiepttft
       61 atiipltpap tppqpappkp qpeppkpkva qplpkpreqp knaitqkaep vappqqqvep
      121 vqnaaptppa ppapapapap sgpieglavk ceeprtvypt qsrrvgeegt vtlrlvidtr
      181 gvvssanvvk ssgfprldqa artaalamrc appmqngrav eaaatkpfnf nlnd
//
LOCUS       WP_010805776             280 aa            linear   BCT 01-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010805776
VERSION     WP_010805776.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..280
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30254
     Region          65..278
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkllrfgerg qekpgvldaq gdirdlssiv sdiggeallp eelerlrgmd lsalprvdqa
       61 prlgpcvggi gkficiglny vdhaeesgmp ipsepvvfnk wlsavcgpnd dviiprgskr
      121 tdwevelgvv igkagsyide ahalnhvagy clindvsere yqlerggtwd kgkgcdtfgp
      181 lgpwlvtsde vpdpqklemw ldvdgtryqs gntsrmifsv aqivsylsrf mslhpgdvis
      241 tgtppgvgmg qkppvylrag qvmslgiegl gqqrqhlvqg
//
LOCUS       WP_010805809             317 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010805809
VERSION     WP_010805809.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34914
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdaidqaraf lvvaetggfs aaakhlqvvp svitkrvsql eaqigrqlfv rttrrvelta
       61 tgkavlshar dlvqahdrmm gdisndvael sgrlrvkaps altylhfski inrflvqhpk
      121 vilelllidr pvnpvtegfd lvitglppsy dqieeialfp iqrmlfasps ylaqkgtplq
      181 aedlanhrcl qysylspgvt wtlkgirgqv dvhvnstfqt ndikvmyqav vdglgigilp
      241 nyvaqeaids gtlvqvlenf alpefwfraq farsqrqrrl lmvlidhiqd elrslglagp
      301 agcgitsdvp taiapre
//
LOCUS       WP_010805837             306 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Pandoraea].
ACCESSION   WP_010805837
VERSION     WP_010805837.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..306
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=32293
     Region          3..304
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 msltlfimqc lnglqlgvll flmaagltlv fgimnfvnla hgslymmgaf iaatvynhtg
       61 sfalaaiaiv pamlllgliv efvalktlyd rdhldqvlat fglilffnel armiwgpspy
      121 ymevpewlsg tvdlfglayp ayrfliivvg lavalgcyll ihrtrigmli ragathrqmv
      181 galgvnivll nsllfglgai lagiaglmag pilsvqpgmg epililtmvv iviggigsvr
      241 gaflaalivg vvdtvgrtal ptllrsller stadtagpal asmliylvma avlavrpqgl
      301 fpvkhg
//
LOCUS       WP_010805857             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Pandoraea].
ACCESSION   WP_010805857
VERSION     WP_010805857.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..308
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34604
     Region          7..182
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(10,12,96)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(43,95..96)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            94..96
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mselysvvip vynssgivae tvrqvreyfl tagrsfeiil vndgskdnsw pvicdlarky
       61 seivsinllk nygqhsanlc gfreskgdyv itmdddlqnp pgeigklida ardeydlvig
      121 kfeakrhsiv rrigsqfvgw lnrkvfdvsd dliltnfrii rrdvvdrvcr dnsyapyipg
      181 lvlkysgrrc nvlvrhqpra egksnytvrr ilrlvasilf nhsvlplrcc aalgfvisav
      241 gfalgfyfli qaiangtrap gwaslavlls ffngililll svmgeylgri lrelgaqrsy
      301 evretvrq
//
LOCUS       WP_010805899             221 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF799 domain-containing protein [Pandoraea].
ACCESSION   WP_010805899
VERSION     WP_010805899.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..221
                     /product="DUF799 domain-containing protein"
                     /calculated_mol_wt=23075
     Region          2..221
                     /region_name="COG4380"
                     /note="Uncharacterized conserved protein, DUF799 domain
                     [Function unknown]"
                     /db_xref="CDD:443506"
ORIGIN      
        1 miarlckwmt vaalaavmtg cavhqakpyd ytafkeskpk silvlpplne spdidatysv
       61 lsqvtvplge agyyvmpval vdesfrqngl tvagdihqvs paklreifga daalylkitq
      121 ygtkymvlds atvvtvsael idlrngaklw sgaasasnne gnnnsgggli gmlvtaavkq
      181 ivnsvsnagy tvagtanarl lsagrangll ygprspkygt d
//
LOCUS       WP_010805881             474 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Pandoraea].
ACCESSION   WP_010805881
VERSION     WP_010805881.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..474
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50010
     Region          30..469
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mdsslsppag taapdaahds trvagaqpvs tldryfgita lgstfrtevi agittflaam
       61 yiivvnpail sktgmafpaa ltatvlisff gscamglyar npvlvapgmg lnalfaftmv
      121 hgvgmpwqta lgcvfwsgil fallaalnvr rfvveaipan lryaiscgig lfitviglvn
      181 aklvigdpvt vvrlahlspp tvtfliglal ttvlvarrvn galmigivlt tlmaipigrl
      241 wgdgtayfpk eiatatlvnf hgffaapdfs gigqldllga lkvaylpfif vmlftaffdt
      301 lstfmsiaea gnmkdrdgnp rnmrqamivd sfsvlisgpl gtspanayie saagiaqggr
      361 tgltalvcal lflpflflsp mlslvpaiat apalilvgvf mmesvariew hrldeaipsf
      421 iavvmipisy sitdgiaysf lafvvlklft grvkeikpam wivaalavll ltqm
//
LOCUS       WP_010805908             499 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HDOD domain-containing protein [Pandoraea].
ACCESSION   WP_010805908
VERSION     WP_010805908.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..499
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=53838
     Region          14..259
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 msltkektle llwqrmaerg dfpslqrsvt givsamqsen tstadlassv lsdfaltqkv
       61 irlansamya pfgcnvttvs raimilgvdt ighlalslkl legfgevaah rddmarelar
      121 atlagafard itakngirdg eeavvctllh hvarllvtyc fpdewmeiqa iaaaqgisds
      181 daceqvlgis fpelseaaar kwglpetiat smrpidlegd aplshadwlc avanmsnemv
      241 teltrgadpa rlaelaerya erlalnigev vsvgeemvrd tshqefiais tgasntrqpp
      301 agkpldsarr ladglsevra atgetdavgl lnltleailq slgfvncaaf vrasaskvfe
      361 mrfgigrdvq sllgltfpea fepdvfhlal tngrailidn areprivpri pmwhrqhfsn
      421 vksffllpvr qrnqtvally gdwggalctg gigakemefl hhmgeeisck lesvaqqnas
      481 tgnttdslar rpsgttgar
//
LOCUS       WP_010805936             330 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD:protein FMN transferase [Pandoraea sp. SD6-2].
ACCESSION   WP_010805936
VERSION     WP_010805936.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..330
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=34936
     Region          24..312
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mskmsiealp daqlklwrls gatmgtryta afhaspttde kelaarlaaa vgavdeqmsn
       61 wkessdlsrl ncaeldcwvp vsrslavlla raleigrdth nafnigvgdl vgmwgfgpsg
      121 eqrahhpgav etsraspcss vsdlidvdvq qcrvrkrgsv aldlcgiakg fgvdelarvl
      181 nehgigswlv gidgemracg skpdgslwai aleapdderh tamsvielsn aaiatsgdyr
      241 hwadidgvrv shtmdprtga plcssvasvt viaptcadad ayatallvlg vdagrdyaqr
      301 rrldalfvvr dggalrmigt gcfaneqqad
//
LOCUS       WP_010806025             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pandoraea].
ACCESSION   WP_010806025
VERSION     WP_010806025.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..301
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32909
     Region          17..295
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 maetlqvpra daapatrapw haflpmwvms apamllfval vlipllmtfa ltfyqfdpas
       61 gpiaafqfen ykevlfdsyf htifvrtfgi sltvtavcav vgtfeayvls rmgdpwrslf
      121 llvilspllv sivvrafgws mllssgglin qafgllgmgp ykmeytnfai vvalvhvmlp
      181 fmvipvwtsl qrldpqtena alslmaspat tlrrivlpql vpgilsgslm vfglsasafa
      241 ipsllggrrl kvaatavydq flsslnwplg atiavlllaa nlivmltyyr llerrysrsm
      301 g
//
LOCUS       WP_010806106             373 aa            linear   BCT 01-JAN-2025
DEFINITION  epoxide hydrolase family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010806106
VERSION     WP_010806106.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..373
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41852
     Region          5..110
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          76..>197
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 midlikpfql nvsereltel rerlqrvrwp dretvndtsq gpqllklqal vahwiegydw
       61 rrcesmlndf gqfkttidgl dihflhirsp epdaipllma hgwpgsvlef rkviapltnp
      121 saqgddprqa fhliipsmpg fgfsdkpgep gwdmsrigra yvqlmrrlgy drwamhggdf
      181 gagvtdeias lalpeligih lnfamfmptq demrdatpde qrmldsaryf wstlsgyaqq
      241 qqtrpqtigy aladspvaqa awiyamfqdt cgtagnaeas ftldeilddi mlywipnasa
      301 ssarlywelk rsnwssaart drpigvplds pclpanrcvn rdaglnnata mcgtslstsg
      361 aatlprwkir mlw
//
LOCUS       WP_010806162             469 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amidase [Pandoraea].
ACCESSION   WP_010806162
VERSION     WP_010806162.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..469
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49602
     Region          5..467
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mpkddqlwty saselatgfg rgeytpidvl esvitrmegi nprinavvtt dldtariaak
       61 asaqrwrngc psgaldgvpm tvkdnvpvag mratwgself gtyvpsedel cvarlraaga
      121 vivgktncpe ltvqgytdna ifgltrnpfd ldltpggssg gavaavaagi cpiaiatdgg
      181 gsirrpasyt gligmkpsrg rvaradgfaa ilhdcevvgp iartvadvrr vmeiigrphf
      241 rdplsvllad dayeaacpkp crilylpefg sspvdrqiad svaqaadlls slghrveaga
      301 vpfdidalgm awttisqtgl twllkrhssg gnrvgadiqa myeagsrlra eqyyealaml
      361 aelkstlael yeaydlimsp saaampwpag eafpniiddq pvgprghaif tgfvnmsgca
      421 ainlpsapna rgvpigfqlv gpvgadkllc digeqyesaf rppriwplr
//
LOCUS       WP_010806198             358 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Pandoraea].
ACCESSION   WP_010806198
VERSION     WP_010806198.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..358
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38733
     Region          46..350
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mfyreagqfk tsyeadsqif pirqdrvavc tvlaiafgvl pwiateywlt ailvpflvfs
       61 laalglnllt gyagqlslgt aafmavgaya synfqlrieg mpilasfalg gvcaalvgia
      121 fglpslrikg fylavatlaa qffvlwvltk fpwlsnnsss gvitaqkisi lgvdvdtpvr
      181 kylfvlgvvt vmalvaknlv rshigrawma vrdmdvaaev igiplmrvkl lafavssfyc
      241 gvagalyayc ylgsvepdgf sldlsfrilf miiiggvgsi lgsflgaafi lllpilldst
      301 lpaiatflhl pftnatvshi qlmvfgglii fflivephgl arlwqiakek lriwpfph
//
LOCUS       WP_010806226             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YbhB/YbcL family Raf kinase inhibitor-like protein
            [Pandoraea].
ACCESSION   WP_010806226
VERSION     WP_010806226.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..187
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=18385
     Region          32..186
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mkwlsstgat caasvaavam alaagtarae gmsvsssafa dggllpaiha glgecggknv
       61 sppvewknlp qathsvvvtm kdpdgakggg vvhwvaynip atvsslaaga gnetgrqvtv
      121 gknvsgamay rgacppvgdt phhyiitvta tdiepgqlpa gldanglsaa laghtlngst
      181 ivarygr
//
LOCUS       WP_010806234             234 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fumarylacetoacetate hydrolase family protein
            [Pandoraea].
ACCESSION   WP_010806234
VERSION     WP_010806234.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..234
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24664
     Region          23..229
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msqfvisapp qasvavagsd arfpvrrvfc vgrnyaahar emgsnpdrep pfffmkpada
       61 vvaaegtlpy ppltselhhe ielvvaigad genvdashal slvwgygvgv dltrrdlqqq
      121 akdtrrpwdw gkafdasapc gplhavaevg hpkqgrvwld vngenrqtgd lneliwsvpd
      181 liaeisrsvk laagdliftg tpagvgplep gdkvsagvag vgeiaftigk kpaa
//
LOCUS       WP_010806232             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010806232
VERSION     WP_010806232.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32858
     Region          2..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..300
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,215..220,
                     226..227,229..230)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mirylktfvt aaetasfsaa garlgltqsa vsaqiqrlee dlgvqlfert gravslsddg
       61 rrllaqaqgv iagyqamrge agthdaqaal apihvgailt vqlgllpgav qrwtalgamp
      121 hlnivpgmsv qllgqldake ldlavmirpr igvpadmkwl tlmqepyvai apkgtrgtva
      181 dwvaempfvr ynrrsyggdl verylrrhrf wvregvelde pevilrlvra rlgwsivpat
      241 liglpvdgqa agkagkagaa avhgvqvlpl sgapltrelg vlvrqsalkr apvatlmtcl
      301 adeaqslg
//
LOCUS       WP_010806248             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Pandoraea].
ACCESSION   WP_010806248
VERSION     WP_010806248.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..267
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28572
     Region          9..267
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlsrqlinaf lgatfalasl gaaaqtadkp lkvgtmagsd aqifevvkkv ahqrgleiki
       61 vefsdyaqpn aaldagdlda ngfqhkpfld sqikdrgyki vsagltyvsp lgfyskkfks
      121 lgdlpngakv giqndpsngn rallllqkeg liklragldg knatpldivq npkklkivel
      181 eaaqlpralp dlaaasintn faaqaglvpq rdaiaiedlk gpyanliavr aqdankpwvk
      241 qlvdayhsde vkkfietqfk galiatw
//
LOCUS       WP_010806290             278 aa            linear   BCT 01-JAN-2025
DEFINITION  ZIP family metal transporter [Pandoraea sp. SD6-2].
ACCESSION   WP_010806290
VERSION     WP_010806290.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..278
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29334
     Region          17..237
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mlslagaasl slgllsrlid kmvsfsagvl lgtallhllp esleshvdah vitrwllggl
       61 lgffllekls llrhshhheg dghhhehghd aheagkggwm ilvgsaihnf adgvviaaaf
      121 ladprlgvaa tvsitvheva hklgdfmvll nagfkrrkal vltlasslta laggvlgyfm
      181 ldrlqslipy llalaassfi yiavsdlmpq mqrrtsprda lpqilliavg ltlvvwlngh
      241 dhehehghdh kdggsalams asasgdgsra satgksph
//
LOCUS       WP_010806320             338 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Pandoraea sp.
            SD6-2].
ACCESSION   WP_010806320
VERSION     WP_010806320.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..338
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35684
     Region          23..312
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mrdlrwivlf gvviaallat lqsgvwlsfv mmtlytvlls qswnilggfg gqlsfghalf
       61 fgvgayaqai aqlrwgwspw lampfaiamg tvvavaigai tfryglkgsy falvtlafae
      121 vfrilavslp ftgagvglmv plhqsvgnlq fasprgyaal lfvfvmaall vtawlrhsrf
      181 gawlqavrdn enaaravgvn plrvklgaia lsgvfmsaag mcyvqmfqyi dagiafgsti
      241 svealvgviv gglgtlwgpv lgaavlyalg eftrnlfgel pglsmviygv vliaivmflp
      301 rgitgagasv rrvlgmdkkt vaapdaqaaa theenarv
//
LOCUS       WP_010806321             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Pandoraea].
ACCESSION   WP_010806321
VERSION     WP_010806321.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..290
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30352
     Region          6..290
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mfdpvillsa vlnglttgav yalialgltl vygvlhiinf shgaalmial yavwllkekl
       61 gidpyvalpf vtlgmfalgy glqrcviera shgkdenill vtlglaivle nlalvwfksd
      121 thtidtpytl atvdigpvml svpklvafgg alaaaallfw imratdlgra iravarekhg
      181 aklmgidver vyalsfgigm acvgaaacfl mptyyvnpqv gsgfvlvaft ivvlggmgsf
      241 agalagglli gvveslgglw lgdslgqmgi faifiivvll rpqglfgara
//
LOCUS       WP_010806327             281 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Pandoraea sp. SD6-2].
ACCESSION   WP_010806327
VERSION     WP_010806327.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..281
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30435
     Region          10..257
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(24,105,107,109..110,138,189,210,213,226,228,257)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 msvsafpsqq vgdftvtais dgyltasldf lsnieaseas rmqrdagqtv pdavhincyv
       61 vrgagrtili dggaggikqw ggrlkdnlll agiepssvdt illthahpdh vgglvnaagq
      121 iafpnaelva hrrevgfwqd egnlsraser argnfriarq vfdgygdrlr tfddgevlpg
      181 iramslpght dghtgylves rdqsllvwgd vvhfphiqie rpdvsiafdq dptraattrs
      241 rlldmvsseg lliagmhlge lgfarikrtr seydllyvte a
//
LOCUS       WP_010806341             204 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein,
            partial [Pandoraea sp. SD6-2].
ACCESSION   WP_010806341
VERSION     WP_010806341.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         <1..204
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
     Region          1..203
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 avrlkeagva teviavsagv aqaqetlrta laigadrail iesdeelqpl avakllkavv
       61 dkeqpqlvil gkqaidddsn qtgqmlaala klpqatfask vtvadnraqv trevdgglet
      121 vslslpavit tdlrlnepry vtlpnimkak kkpletlkpa dlgvdvsprl ktlkvaeppk
      181 rsagvkvadv aalvdklkte akvi
//
LOCUS       WP_010806422             463 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid permease [Pandoraea sp. SD6-2].
ACCESSION   WP_010806422
VERSION     WP_010806422.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..463
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50117
     Region          2..452
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mqqnslsqsl kqrhitmial ggvigaglfv gsgaiiatag paailsylvg glivtfvmfm
       61 lgemasrnpd sgsfstyast ylgewagfav gwlywfkslm titieaillg silneflpwl
      121 pvwggavvml itlivsnays vrsfgeaeyw lsfakvativ ifmlfglsil fglqakipap
      181 gfgnltshgg fmpngispvi agimvvifsl ggseiaavaa gesenprknv vrairsvifr
      241 vlvfyigsvs iiilclpwtd kanlaspyvs lfsmagfpna alamkavlfv sfmsvmnsfl
      301 fsnsrmlysl sqrgyappmf artnsrgvpi nalglsfaic lgilavhfvs ggdlflmlak
      361 ssgafvmtvw ifiivahfvm rlkmarqpvq emeassfkaw ffpfsnaiaf ltlvavlisq
      421 afnpdsrfqf wfmvgtalmi vglyfmlrrr pnfglvnvsa rln
//
LOCUS       WP_010806427             230 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Pandoraea sp. SD6-2].
ACCESSION   WP_010806427
VERSION     WP_010806427.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..230
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25263
     Region          3..219
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mnqtqrtpal sdsaynaira livsgeirag ealseralse rfgvsrtpvr eairalandg
       61 lleivpmrgt fvrqlsvrdl seihevrlal egmaawlaaq kgvtpalqev avrlraldaq
      121 geqglpldvd itqrvgwqfh eamfaaadnv rltetyhalr tqnglalqri phydaertra
      181 avrehlaifd aiaagrpeaa qrhvwdhlth amqarlqalv pptvppgtqr
//
LOCUS       WP_010806443             296 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Pandoraea sp.
            SD6-2].
ACCESSION   WP_010806443
VERSION     WP_010806443.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..296
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30960
     Region          11..291
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mnpfdiplpa llsqlmlglv ngcfyavlsl glsvifglln vinfahgalf migalvawmg
       61 gqylglnywa mlviaplaag llgaviergl lsriykldhl ygllltlglt liieglgrsa
      121 ygvsgmsfeg pallagatrl pfmvlpnyra wvvaaslaac altwfvvert rigallragt
      181 enarlvetfg vnvplmvtlt yafgaalaaf agvlaapimq vspimgqpmi vtvfaivvig
      241 gmgsiagsvv tglalgvleg ltklwypeas atvvfvimal vllvrphglf ggyayk
//
LOCUS       WP_010806586             243 aa            linear   BCT 01-JAN-2025
DEFINITION  alanyl-tRNA editing protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010806586
VERSION     WP_010806586.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26406
     Region          3..243
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mttealfrqd aylrqceari thidetgiml drtvfyplgg gqagdaggfv ladgtrltia
       61 dtrkskqega tpddavhvpa egqedwlarv svgdtvraei dwerrfrhmr lhtashlmca
      121 vlphpvdgcs itteyarldf vtnepieret veaglaalva aarpvaidsi sdeemaarpe
      181 lvrtmsvkpp vglgrvrlvr iegidlqpcg gthvantaei galrvakiek ktsrtrrvvl
      241 afa
//
LOCUS       WP_010806641             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pandoraea].
ACCESSION   WP_010806641
VERSION     WP_010806641.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18309
     Region          3..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mldldqfdla lldalqrngr ethhqlaerv alspsqigrr lqklesdgii egyrvvlrpe
       61 algltvtaft slrlkhhgdk pienfqkqie llpevlecha vvgeadyllr ivvpdlnals
      121 tfvmkrlmqv pgvenvrsni vlsafkrsna lplhyvvtkq tqr
//
LOCUS       WP_010806727             162 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Pandoraea sp. SD6-2].
ACCESSION   WP_010806727
VERSION     WP_010806727.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..162
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=17525
     Region          1..146
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mlflrfaiat dhyvieaqhv aevlpwlalk rmpaapawva gafsyrgepv pvidltrlat
       61 gavaperrst rlvlvhypap gpnarrlgil veratdmlra dasafqasgv dlpegrylgp
      121 vldtdeglvq wvrvdqlltd earallfdas rdalaeapea ss
//
LOCUS       WP_010806755             464 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Pandoraea sp. SD6-2].
ACCESSION   WP_010806755
VERSION     WP_010806755.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..464
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47722
     Region          29..458
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mqtstperdt arptaratpl gqtapaqggw lerrfaiarr gssvrtevla gittflaaay
       61 llvvipslla tggmdrgaat tavmlvfvlf svlmglyanl pfvvgpgigg svivgvtlaa
      121 tehvawqtgi aiaflsgmlf llltvvgars vvarliptai klglgasigl fiavlgvrna
      181 gmvvanaktn afalgdfskp gtivaliglg tavllqgrkv pgailwsila aavagvplgv
      241 tklpesfvsl phsiapvafq ldlssaltia alpylfaffa aeffstlgtt lavggkagll
      301 dehgnmenin rpflvdsiaa tggallgipa ltalvesaag veaggrtglt siaaavmfal
      361 mcffvpvala ipkeatapal iliglsmfst irhvpfddfs dafpvlamvl ltllsnsfgt
      421 giaggllcyv lvkalmgrfk elpwglyvla lplayyfwtv vgrh
//
LOCUS       WP_010806774             257 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Pandoraea sp.
            SD6-2].
ACCESSION   WP_010806774
VERSION     WP_010806774.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..257
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28109
     Region          3..241
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 msmlafenvd kfygehhvlk ginatigrge vvvvcgpsgs gkstlirtvt rleaiqkgri
       61 lfegqdvtar dvklnqlrar igfvfqsfnl fqnlsvrqnl ilgptkvlgm srdeavaqaq
      121 tllakvglah kidampanls ggqqqrvaia ralamkpplm lfdeptsald pemvqevlqv
      181 mrslagdglt mmivthemgf ardvssrvwf mdqgelleds ppaeffsrpk haraqrflqd
      241 vlrpspmigm pidavpa
//
LOCUS       WP_010806767             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pandoraea].
ACCESSION   WP_010806767
VERSION     WP_010806767.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24026
     Region          30..183
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtpnkavpqa apprkrargr ptcdcthgad alllnarrif aqrgfyassv rqiaeasgvd
       61 aalishhfgs kealwvavvd qiaslthsli eqtdalqhsp lgpaerieqa vrvfvdavfe
      121 npdvgmffst aateegerld vltqrlvrpy rnvmvplvad wleaqkrpva dadvmffmlt
      181 saisktvsyr hmmgpflppe gmadlkrtvl dcamalirq
//
LOCUS       WP_010806779             286 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Pandoraea sp. SD6-2].
ACCESSION   WP_010806779
VERSION     WP_010806779.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..286
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31717
     Region          30..268
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mtdhkaiapd staarvalwr alhlevdatp hvltddiglk lleppddwre rgdmdpeftr
       61 pfrasivara rfiedlvmeq lrhgvtqyvi lgagldsfaq rhpelaaslt ifeidrpgpq
      121 rwkydrlial gygvqdwlhf vpvdfeagqs wrdallqhgf dasrpavivs tgvsmyltre
      181 analtlrevs sfapgstlam tfllplemad pevrpglema ekgaresgtp fisvftpqdm
      241 mafarengfk dashvsaatl tqryfsnrdd glrppanaee lliatt
//
LOCUS       WP_010806828             302 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010806828
VERSION     WP_010806828.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32470
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..295
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(103,107,146,160,164,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(104..105,109..110,112..113,116,120,122..128,191,
                     221..222,226..228,235..236,239)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 maeqlsdlta fmavaraggf reaaraggvs asslsealrr letrlgvrll hrstrsvspt
       61 eagarllerl gpalgeieaa ldvvngfrdr pvgtlrlnvp asaarlvlps lvppflaayp
      121 dilldvvvee gfvdilsagc dagiryeerl aqdmiaipig prrqrmataa aptylaargc
      181 pnhprdllnh aclrgrfasg ampawefqrk aevvtvepgg pliyrisggv dlaidaavsg
      241 cgvihlfedw lrphldsgal vpvletwwqp ftgpflyypg rrhlpaplra fvdfvqaqri
      301 ga
//
LOCUS       WP_010806891             162 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pandoraea].
ACCESSION   WP_010806891
VERSION     WP_010806891.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..162
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18201
     Region          5..150
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mskleldkid rrilallqsn grlsnleiae qvrlspspcl rrirrleeag virgyvalle
       61 ptrlglglla yvnvrldkrh pgdgeggsvi ehfrrvvetw tevvgcyama gdmdyllrvh
      121 vrdmahfsqf mqtqlivhps vvdvktsfvl dqlkettalp lp
//
LOCUS       WP_010806906             278 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cell division protein FtsQ/DivIB [Pandoraea].
ACCESSION   WP_010806906
VERSION     WP_010806906.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..278
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30639
     Region          27..237
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mwhnvrllna iasalvalvv laalaagghw liqrpiftlk aiqidgdvsh ingptlrana
       61 vsrlkgnfft idldatraaf eavpwvrhas vrrvwpnqla itieeykpla twndgrlvsa
      121 dgelfaanla eaedegklpe fagppgsekd vtaryydfvk wfaplnmkpe avtlsnryaw
      181 gvrlaggvql algrertpet latrsrrfvq aypqvaarwg nqieyadlry pngfavraag
      241 mrflseeqak klaatpaqnr dsrkpavaqp aarqkrsq
//
LOCUS       WP_010806995             412 aa            linear   BCT 01-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator [Pandoraea
            sp. SD6-2].
ACCESSION   WP_010806995
VERSION     WP_010806995.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..412
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44849
     Region          <59..394
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpahlavapa parpvghasp igtasantaf aniaalaeri arvpaapaaa rrmrpdylai
       61 ddlcgtdarm rdllargkrf vdrglpvlil getgtgkefl aralheyser raqafvaint
      121 aslpehlves elfgyqrgaf sgalpggmkg klqqadggtl fldeigdmph alqtrllrvl
      181 serevtplga shavpvdvql icathqdlat avaqgtfred lyyriavgil tlptlrerdd
      241 kreliarmlc dewpelhedq vlarvspdal srllmhawpg nlrqlraalr yacavmsgnq
      301 lcaddlppel vtssshtwms gndtfaeqrs hdignavvsa prvqtvetia qmprhdsere
      361 rilqalaqhr wnisaaartl gfcraslyrk lkqlsiphvr dcgdalsagh fa
//
LOCUS       WP_010807019             427 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Pandoraea sp.
            SD6-2].
ACCESSION   WP_010807019
VERSION     WP_010807019.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..427
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45567
     Region          22..303
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mpytnydnla assealdkha varhstwvsi wvnivltaaq ivigifarsq aliadgihsl
       61 sdivsdfvvl aaarssarap dadhpyghsr yenaaslflg villvvgagm lwrgierllh
      121 peeipevhiv alvvavivlv skeglfryml raaqrarsam lvanawhars dalsslvvac
      181 gilgnlagyr ildplaaalv glmigrtgwk fgwnalqdli drgvddattv tirehllatp
      241 gvhaidmlrt rrmgdeivvd vhilvdarls vseghyiaeq artavmrepq ildvlvhvdp
      301 esdtkgtalq qwparaavvg aanalcrang lalhevnlhy lnngleadvi veslrepaca
      361 dtqavegddg mepapqavad alaarfalry vrvlrvtget savsgeagta yreaaranat
      421 aagpaie
//
LOCUS       WP_010807033             105 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pandoraea sp. SD6-2].
ACCESSION   WP_010807033
VERSION     WP_010807033.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..105
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11234
     Region          10..94
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mttsstppsv qdnpakhrfe yvsqgerava iyslegnvit fvhtlvpeal qgqgiarqlv
       61 laglasarer glrvvpqcpv faaymrahpe thdlladegr allgl
//
LOCUS       WP_010807035             220 aa            linear   BCT 01-JAN-2025
DEFINITION  DsbA family oxidoreductase [Pandoraea sp. SD6-2].
ACCESSION   WP_010807035
VERSION     WP_010807035.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..220
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23797
     Region          6..208
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(14,17)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mpsveiqity dficpwcwig rrhlqaalaq mpdtavsiry vpyelnpgmp kegadrkayr
       61 sakfgswars qamdadvtla gqhagvafhy drvtmtpntr lahrlmvyat rrgdaartea
      121 lfesvfhayf segrdigkad vlatlagqag fdakeardfl dspagerevv aaerqaqang
      181 vrsvptlrig ntsisgaqps stliqalrqa aaqcavvpav
//
LOCUS       WP_010807044             151 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Pandoraea].
ACCESSION   WP_010807044
VERSION     WP_010807044.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..151
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16887
     Region          10..140
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mqrlnfinaa prpyehlgtl shyfhdcglp dglvelvwlr asqlngcafc idmhvadalk
       61 igidprrlhl lvawretely spaeraalaw teavtnvqdg hvpddvfdel rahydnkqia
      121 dltfavatin awnrvaisfr salpktpqgv r
//
LOCUS       WP_010807052             740 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Pandoraea].
ACCESSION   WP_010807052
VERSION     WP_010807052.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20650304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..740
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83107
     Region          70..347
                     /region_name="FUSC-like"
                     /note="FUSC-like inner membrane protein yccS; pfam12805"
                     /db_xref="CDD:432799"
     Region          371..636
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mdyqtdikkf lyshyffsgt rqavgvvlpa lvlfwgmdqh llgievasga lcasvvding
       61 plrhkhtell sctllgaltv litgmataaq pwqlwitsli ltfglsmlvv ygyrasmvsf
      121 aclmmmvlnv eadltrhqav ldagavlagg lwytyfsliv crvwwfrieq qtlaecffvt
      181 aeyleakaaf ydtstdiddc yrrliasqvn vvekqqaare iilrnlprlr sgtleprrtm
      241 lfnlfinivd lhevvvsvht dypmlrrefa nndvllffrd mirkianevd aigyaiatne
      301 psraqrswra efraieyeie lmrkqslpqr apeayqalts tfrrvwsstr ivermhrntn
      361 latagaatev qidqallrft srqsfspkll wknltfssps frhalrvtia isaglmicen
      421 wsllagqahs ywvlltiivi lkpgfsltkq knaqrltgtl lgcvsvllil sfvhkpwmll
      481 almffcmvmg nslslfnygl svvfmssyvl llfhfllpgs lsvigeraid tligsavalv
      541 csylfpywey rlmgplirqa vqstrayles cagregkrdd fayrmarkdm hiafgnfgaa
      601 fkrmmlepks kqvsvgelnd llvqnhvmas yitgmadvlp rqiaadksge lgqvvsaisd
      661 llsqavaapa asvptdtqaa sdamrdytrr ldalvvaqeq qpdasethvq eikqvvhqlk
      721 qmlragelil rdmrgirlpa
//
LOCUS       WP_010807121             157 aa            linear   BCT 01-JAN-2025
DEFINITION  aromatic-ring-hydroxylating dioxygenase subunit beta [Pandoraea sp.
            SD6-2].
ACCESSION   WP_010807121
VERSION     WP_010807121.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..157
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=18064
     Region          24..157
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mvdfatfqav ielnaayaaa ldaqqwdawp dfflddcvyr iqprenfdmg lplatlsfes
       61 kgmlrdriyg irdtlfhdpy yqrhviglpa irqldddtlr veanyavfrt kpdqltdils
      121 vgryldvlkr tgdgwkfasr qcifdsemip nsliypi
//
LOCUS       WP_010807131             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: HD-GYP domain-containing protein [Pandoraea].
ACCESSION   WP_010807131
VERSION     WP_010807131.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..243
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26204
     Region          <56..229
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mpdpapardi cattlslapd asrdtcrpes rnndphhryw ladarlmssl ppatwtlfrl
       61 aeqkrgstat hmwrvgalaw rfaqalgmpa vkaqalglaa alhdtgklci snailekpgr
      121 ltpdemdvmr mhpqlgadml gaiggaactl aatvarthhe rydgggypyg lsgnriplag
      181 rivalvdvfd alashrpyrs alrpaqivaa mlaergrhfd pwlldrfler slgsaleisg
      241 gar
//
LOCUS       WP_010807096             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Pandoraea].
ACCESSION   WP_010807096
VERSION     WP_010807096.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..316
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=33015
     Region          1..316
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mdifiqqiln glvlgsvyai ialgytmvyg ilgiinfaha dvmmigamva lstinlllkv
       61 apnmhpalml aiatlvcmpt calanfvier vayrplrnap rlaplitaig vslllqtiam
      121 liwsrnplsf pqllptdamt iipqrgdhpg avtngtgivi vvvaflvmfg ltqlvnrtkl
      181 gramrataen rnvaglmgvn pnfvisatfa lggalaalag vmmasnygna hfymgfipgm
      241 kaftaavlgg ignlqgamvg gvllglieal gagyigdltg gvfgsnyqdv fafvvliivl
      301 vfrpsgllge rvadra
//
LOCUS       WP_010807134             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Pandoraea].
ACCESSION   WP_010807134
VERSION     WP_010807134.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..204
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21798
     Region          1..198
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mfaviqaagw piwplliasv ialalivera lslrrarvlp sgvlenaitl arrgsakqda
       61 tealargsml grvlatgvrf vahnpqgpre sakealeetg ravahelerf lpalgtiasv
      121 aplmglfgtv igmieifgaq datgtdpaql ahgisvalyn tgfglmiaip amifyryyrt
      181 rvdaflvele tqavhfldat lprh
//
LOCUS       WP_010807137              68 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Trm112 family protein [Pandoraea].
ACCESSION   WP_010807137
VERSION     WP_010807137.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   van Tran,N., Muller,L., Ross,R.L., Lestini,R., Letoquart,J.,
            Ulryck,N., Limbach,P.A., de Crecy-Lagard,V., Cianferani,S. and
            Graille,M.
  TITLE     Evolutionary insights into Trm112-methyltransferase holoenzymes
            involved in translation between archaea and eukaryotes
  JOURNAL   Nucleic Acids Res 46 (16), 8483-8499 (2018)
   PUBMED   30010922
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Bourgeois,G., Letoquart,J., van Tran,N. and Graille,M.
  TITLE     Trm112, a Protein Activator of Methyltransferases Modifying Actors
            of the Eukaryotic Translational Apparatus
  JOURNAL   Biomolecules 7 (1), 7 (2017)
   PUBMED   28134793
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006712
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..68
                     /product="Trm112 family protein"
                     /calculated_mol_wt=7412
     Region          1..52
                     /region_name="Trm112"
                     /note="RNA methyltransferase activator Trm112/YbaR
                     [Translation, ribosomal structure and biogenesis];
                     COG2835"
                     /db_xref="CDD:442083"
ORIGIN      
        1 mdnrlfeilv cplckgpley dkkaqelich adklaypird gipvmladea rqsvegtpvp
       61 lnddksas
//
LOCUS       WP_010807188             391 aa            linear   BCT 01-JAN-2025
DEFINITION  AAA family ATPase [Pandoraea sp. SD6-2].
ACCESSION   WP_010807188
VERSION     WP_010807188.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 391)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..391
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42790
     Region          1..384
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mlsalaidny rsiqslvmpl trlnvingan gsgksnlyra lrllastard givaplareg
       61 glnsvmwagp eeisermqrg evpveggprr krsrlrlgfs sdsfgyavcm gyvggsgpas
      121 afaldpefkr eslwagdflr pantlvdrdg gvvrrkagkg wdiltsslpr yeslfshian
      181 daacpevftv rermrdwrfy dhfrtdidap arapqigtrt svlhqdgrdl aaawqtirei
      241 gdqaaldeav sdafpgahve idaqpgglfs lafhqhgllr plsaaelsdg tlryllliaa
      301 lltarppelm vlnepesslh pdlmpalgrl irraakhsql wivshshrla aaleddpecn
      361 aitlekafsa ttilgqrale rpawrwadng r
//
LOCUS       WP_010807191             150 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010807191
VERSION     WP_010807191.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..150
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15917
     Region          34..139
                     /region_name="DoxX_3"
                     /note="DoxX-like family; cl46314"
                     /db_xref="CDD:480654"
ORIGIN      
        1 matvlpspdp spplgregis lpgwaywlal lllcsaylqg gidkaldfpa aiaemhhfgl
       61 apaapfaaav ialeigasll iltgrwrwlg alalaaftla asfmanrfwa appgervmla
      121 naffehlglv ggfiavvwyd lrtrasrrts
//
LOCUS       WP_010807261             276 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010807261
VERSION     WP_010807261.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..276
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29825
     Region          11..258
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mkdesnpgae srtsiqvier mmrlldalag hadpvslkel aqatelhpst ahrilndmva
       61 crfvdrcdpg tyrlgmrlle lgnlvkarls vrdaalapmr glhritgqtv nlsvrqgdei
      121 vyierayser sgmqvvraig ghaplhltsv gklflaadea srvrayaart glsghtrnsi
      181 tdlqklerel thvrksgyar dneelelgvr ciaagiydds gklvaglsls apadrlqdaw
      241 lanlnetalh istslgfhvp npdaggssqs qnstae
//
LOCUS       WP_010807274             692 aa            linear   BCT 01-JAN-2025
DEFINITION  M3 family metallopeptidase [Pandoraea sp. SD6-2].
ACCESSION   WP_010807274
VERSION     WP_010807274.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..692
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=77251
     Region          3..692
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 mntpqtnpll dieglprfae irpehvtpav dvlleqarva vdraaapstp atwanildav
       61 edgteglgra weivghlnav adtpelraay senlprvtef sasvgqnlal fekykaiaag
      121 sefaglspar kkildnemrg frlggaelpe dqkprfaeiq erqaylaksf sdhvldatnk
      181 fslvvtdeqa lsgvpdddka aaraaaerdg legwkftlhf psyfpvlqya dnralrekly
      241 ranvtrasel gpqfgdgeag wdnteivveq lslrreeahm lgfknyaevs lepkmaespa
      301 qvlefledla rrarpyaekd weelqafaaa slgidklqpw dtayaseklr qqryafsete
      361 vrqyfplpkv ldglfrvaga lfgvtirpqd aetwhpdvrf frierdgelv aqfymdlfar
      421 egkrggawmd sartrkrlhd gelqtpvayl vcnfpapvgd kpallphddv itlfhefghg
      481 lhhmltqved agvagingve wdavelpsqf menfcwewdv lehmtahvdt gaplprtlfd
      541 kmiaarnfqs glmmlrqlvf sdfdmhlhyd fdprgnesvl alskrindrl hvtpqaefsr
      601 wpntfshifa ggyaagyysy kwaevlsadv yaafeeaaqv sgsvldtatg aryrdeilav
      661 ggsreamesf iafrgrapqv dallrhsgms as
//
LOCUS       WP_010807312             452 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sigma-54 dependent transcriptional regulator
            [Pandoraea].
ACCESSION   WP_010807312
VERSION     WP_010807312.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..452
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49835
     Region          2..119
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <141..444
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mandtgrtli yasrkhndgl lsflgeqgwq vvpaksasdv grilnpgvts aalidlasgy
       61 sdremgafes cmqpatvgwv aatnpeqltt tairrlirdy cfdyvnvpct ndqlahsigh
      121 awgmaslsev ptftpqvggd qemvgtceam qqlfrtirkv antdapvfis gesgtgkelt
      181 avaiherslr akgpfvainc gaipphlmqs elfgyergaf tganarkigr veaanggtll
      241 ldeigdlpfe sqasllrflq qgaierlggh evipvnvrii sathvdleea vkegrfrmdl
      301 yhrlcvlrve epplrargqd ieilahhvlq rfkgdnhrki rgftqcavqa myeyhwpgnv
      361 relinrvrra ivmadsrtis akdldllpwv ptlvrtleei raeaertaie qallrhchrl
      421 tdvaaelgis ritlyrlmcr ygmrgdesgv pa
//
LOCUS       WP_010807376             280 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010807376
VERSION     WP_010807376.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..280
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31141
     Region          48..280
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mnanvrdtsn ttppvdapqr qdstrdaapa sqapqgaaap gasptfsply qqikglitqs
       61 lqagewkpge iipsevdlaa rykvsqgtvr kaidelaaen llvrrqgrgt fvathhedrv
      121 qfrflrlapd sgephhppsr liecrrmrap aeiarqldlr agdgvilirr mmdfsdrptv
      181 ldeiwlpgal frgltaerln dykgpmyglf edefgtrmir avekvravaa ddvtadllkv
      241 pkgfpllsve rvsytygdkp vevrrgwyvt tehhyqnels
//
LOCUS       WP_010807396             111 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YegP family protein [Pandoraea].
ACCESSION   WP_010807396
VERSION     WP_010807396.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..111
                     /product="YegP family protein"
                     /calculated_mol_wt=12210
     Region          2..50
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
     Region          54..110
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
ORIGIN      
        1 msgkfelkrs pngefhfhll adsghiilss etykarasaq ngiesvrkns vedhrferkt
       61 stsgrpyfvl karngeiigq sqmfstaeqm edgitqvkrd apaasvsdls h
//
LOCUS       WP_010807417             334 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Pandoraea sp. SD6-2].
ACCESSION   WP_010807417
VERSION     WP_010807417.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..334
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35407
     Region          1..332
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,126,130,133,156,159..161,180..181,185,200,
                     224..225,246..247,249,271..273,321,326)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaieitqyg apevlkpter prpelkpgev likvaasgvn rpdvlqrigq ypvppgasdl
       61 pglevageiv egaldgadnr wglkigsrvc alvqgggyae ycaaplaqvl pvpeglsdve
      121 aaslpetfft vwsnvfdrah lgetetgeke tllvqggtsg igvtaiqlgv alghrvfata
      181 gsdekarace algaerginy ktedfvaiak eltqdrgvdv vldmvggdyl prevqalafd
      241 griaiiallg gskatldmga llrrrltvtg stlrprsvaf kaaiaqrlyd nvwplfaagk
      301 irpviyqtfp aeqadkahal metsthvgki vltw
//
LOCUS       WP_010807496             304 aa            linear   BCT 01-JAN-2025
DEFINITION  lytic transglycosylase domain-containing protein [Pandoraea sp.
            SD6-2].
ACCESSION   WP_010807496
VERSION     WP_010807496.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..304
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=31817
     Region          5..231
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mtfrlsalrr qvslrkfagl alaaallgat pfahaelygy vdengvahla arkldaryrl
       61 vvgaggnadl rasqggvvsg tdrsrlydal arhpnlkkla pliaqaaqrf qvdaallkav
      121 iaaesgfdsa avspkgavgl mqvlpatger ygvradakrt vaekladpdi nvltgarylr
      181 dlqarypdrl elvlasynag egavarhadq ippyaetrdy vaavlelyrr fnpeasnaap
      241 gsgvirasgd vgqvgrarvs gsrngrihvi lgapsglpvv patlpnasvr dsapkvlssa
      301 lptd
//
LOCUS       WP_010807629             310 aa            linear   BCT 01-JAN-2025
DEFINITION  transketolase family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010807629
VERSION     WP_010807629.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..310
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32929
     Region          1..302
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mraafsdalv saalanpkil lltgdhgyal fdafrracpn qyincgvaeq nmvgvaagla
       61 ragfrpvvyg laafvpvrvl eqikidicye nlpvmligdg agfvyshlga shqsmedvav
      121 trplpgltil spadryemaa tmqlafdtrg pvylrmgksd rgdvhngalt ltpgtalkvr
      181 ernreivlia tgsmvsaavn lvdagmqadv wsipsikpld ttalrgigar akdifvleeh
      241 vvagglgscv aesladlgad tprvhrigve drfsaycgty eyllsehrld tptirkrieg
      301 ilsssggvat
//
LOCUS       WP_010807646             588 aa            linear   BCT 01-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Pandoraea sp. SD6-2].
ACCESSION   WP_010807646
VERSION     WP_010807646.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..588
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63836
     Region          33..585
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mahrqgesrl ssrigrgvsi ksvrdrkvvv rfvavslsai sllstqqaws dgspvrgdpl
       61 qslpkieapk apaasfqiqp ptqedalksl larkitpqrf giegvkslsf esvaglfapm
      121 agkevtigdl vekanqvtkm yqdagyllsf afvpaqdfne gfvrvtvveg yisstkitgk
      181 pgpseqrlrd iaahieaerp lkratferyl nlltlvpgmk ikadvqpptq tdgatelsld
      241 vsrqpvalgt slsynnpgvr gvftvssnal tplgeqiqlt aiapkghnde efyaasyiqp
      301 lgsdglqarv dashyrgqpd dqalagltrh ldtkrvavsv sypillnnqr sltvsggmyg
      361 vnsrdryevp nspnninsqt nvragqvqla ynevtdkqtr saalgvfkgf ngmgasqsyt
      421 tqpaglpqil gpydlafwrf tldgkqgvvl pwdfgvivsa gaqyssntlp tseqatfggq
      481 rfglgypage iagdkgwgas ielnrmfrtd frflktiqpy lmldtarvyv nagqlfhnql
      541 asvglgvris dskyysldls lakpmadapt nspkrplrfn anwsyqfe
//
LOCUS       WP_010807654             302 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pandoraea].
ACCESSION   WP_010807654
VERSION     WP_010807654.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..302
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31288
     Region          1..274
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mslfsmmgal eiglifslva lgvlisfril nfpdltvdgs falggavaai liaggtnpfa
       61 atvaamaaga lagfitgwln vrlkimdlla silmmialys vnlrvmgapn vplitsptvf
      121 tmilpenapn wlpdyvlrpl lllavvvvvk lgldyffssq qglamrstga nprmaraqgv
      181 ntgheilagm alsnslvala galfaqsqgg adismgigti viglaaviig etilparrli
      241 lttlavvvga vlyrffiala lnsdfiglka qdlnlvtall vavalvlpat rrklfarkng
      301 ga
//
LOCUS       WP_010807766             299 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParB/RepB/Spo0J family partition protein [Pandoraea].
ACCESSION   WP_010807766
VERSION     WP_010807766.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..299
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32074
     Region          44..297
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 matktnalkk kglgrgleal lgahadnhng aaeagadgap svmsleriqa gkyqprtrmd
       61 egalqelaas iraqglmqpi lvrrvdseky eiiagerrfr aariaglaev pvlvrdvsde
      121 aaaamalien iqredlnple eaqgiqrllg efnytheqaa eslgrsrsav snllrllnla
      181 qpvqtmllag dldmgharal lavdaatqit lanqvvnkrl svrdterivn aslkpqgdgi
      241 rrrsaeeggr dvtrledels dllasnvkik vgrkgagqlt idfgsldald gilarirae
//
LOCUS       WP_010807698             298 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Pandoraea].
ACCESSION   WP_010807698
VERSION     WP_010807698.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..298
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=31577
     Region          51..274
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpylvdpaaq aarrrasldd tlharaatpv sdqpaardit lpaesashta rasarplaqa
       61 varkidaare aertrlaqei hdglgaqlta lqlavarlam rppvdaaewq slctqiqnaa
      121 taaqdaadel vgrsrppald aglvpalrtw lrgfgeqsgl tciwrcddvt rdrvanlspd
      181 avlalyriaq ealtnvarha rasrvvvald gghrslklti sddgcglrrg arrkqghfgl
      241 vgmrerctal ggtlrigsaq gsgtlvsarl pwhqilpapa glhgpdshal hgythhda
//
LOCUS       WP_010807836             266 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Pandoraea].
ACCESSION   WP_010807836
VERSION     WP_010807836.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..266
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29205
     Region          12..245
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msetakqteq evlftqigrv avitlnrpqa lnawtiamre liiealerfn adesvaavim
       61 tgagrafsag qdlaeakhfd gdtaiewikg wehyydvirs lkkplvmaln gtaagsafqv
      121 sllgdirvgh pgvrmgqpei nagiasttgp wimnhmlgls rtieltltgr lmeaeechrl
      181 glihhlvpee kvfekaleia sdlaekppva mrldkqrfre mtegtfqdai eagmriqres
      241 yesgeparmm aaffakraak aeaaka
//
LOCUS       WP_010807839             581 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease subunit [Pandoraea sp. SD6-2].
ACCESSION   WP_010807839
VERSION     WP_010807839.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 581)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 581)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 581)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..581
                     /product="ABC transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62814
     Region          13..292
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
     Region          327..580
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mwlvqrlpqa gpriawpqhl arwlpalpal lflavffivp vveilqggly dgdgvlsvaq
       61 farmthsavy vkvlastfwi afltaalsvl lgypvaylla rlparsrerw llwivlpfwt
      121 sylvktyawm lllsktgllt vvathlglid ststlapslt gvligmvham lplavmtmlp
      181 imrginmqlv qaaqtlgadr atgfftvflp lsgagaaaag llvfisslgf fivpallgsp
      241 resmvaqlvi ssvlelfdlr fagalssvll lcsivvfyvy drvvglssla geaperrags
      301 ggrmlpalia igrlagklsw grerveggfg lktytwavvl alvlpiafvv plaftkqsfv
      361 afppelftmk wfvaflessv wqaallrslg vgfataalal vlgfgaslal vrlpsrwrkp
      421 lfavfiapli vprivvavgl lylfarwela gtnaglvigh tvlaipyvvv tlsasfkrfd
      481 wrlddaakml gasaftrvrt vllplmaasl gsaflfafiv sfddltiaif vsgginttlp
      541 kqmwddiqla vtptlaavat slvflmvfiv wlssifkrks y
//
LOCUS       WP_010807842             413 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Pandoraea].
ACCESSION   WP_010807842
VERSION     WP_010807842.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 413)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..413
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45264
     Region          122..389
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 malglslptl dlptlqfvtf llsiatgilf mldalrrdea esprwwslaf llatfspily
       61 llaarsprla vlyplgnava tlafamvwsg arrfyarsvq wvtvfggpav llwgtwlfar
      121 pldawsggvl ffsllafysl maakefwqas glrlpssivl avvavlhgsf yavravalvw
      181 lgpgdpqflm wfgpqvstte mlvlivvasf lmvslgkers eialhraatr dgltqafnrl
      241 eftrlareqm rrhsaarapv alllldldhf krindtyghp fgdtvlllfa rtasqqlrsd
      301 difgryggee falflpgvga peaqtiaerv reaferagrm vqgetvaatv sigiacders
      361 rgelsslvqr adralyqaka agrnrcvryt petampatds raevqalraa agg
//
LOCUS       WP_010807896             193 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Pandoraea sp. SD6-2].
ACCESSION   WP_010807896
VERSION     WP_010807896.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..193
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21394
     Region          1..86
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          92..176
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mplahalmts lleksssgyd larrfdksig ffwhathqqi yrelarmeaa gwidsmaapd
       61 ggrtrkrvyr vldagrdell awaatptaps dlrddlmvrl radaaigplg lqpelrrraa
      121 lhaqklaayr aieardfpqg etptrdaalq rhilllgvry eqgwldwtrd alallehwdg
      181 taagdgtpaq nav
//
LOCUS       WP_010807975             216 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Pandoraea].
ACCESSION   WP_010807975
VERSION     WP_010807975.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23434
     Region          19..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtatpitrgr rpkhlpdgra allsaaihaf aqfgydganl rgiartakvd aslvrvhfgs
       61 keqlwracvd tleaalvepg erlralsldt srpvtdrlke aisivavhai dhpehkqfis
      121 qhasetgerg avlhrhlvmp vyecmeplit qgmqagvvra ehpemyfcll vhalhpppgs
      181 pvlmqliape vggeafgpal lkqvemvffa tpdakp
//
LOCUS       WP_010807984             416 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pandoraea sp. SD6-2].
ACCESSION   WP_010807984
VERSION     WP_010807984.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 416)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..416
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44933
     Region          <192..414
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mpasihatsh apasaeglaa yrrvqrrasm ralmlalpli vfllstfiap ialllarsvq
       61 nqeiadgmpq laraldawdg sgvpgeatfa qlaaglkqah esgqlgtiar rmnfaqpefr
      121 sllmrtarav ggdappawkp alieiderwg spetwrllkr aavsptpdyl lagmdaqvtp
      181 qgviaalpen asvyraafvr tisisatvtl lclvfgypva wllanlpekq snrlmlfviv
      241 pfwtsllvrt tawyvllqpg gvinsllssl gitthpvpli fnrtgvligm thvllpymil
      301 aiysvmksvp pvymraaksl gahpftafvr vyipqtlpgv gagcflvfvl algyyitpsl
      361 lggagdemis qliamqtntq lnwglagals aylviftavf yfifnrivgi drlrfg
//
LOCUS       WP_010807985             275 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Pandoraea sp. SD6-2].
ACCESSION   WP_010807985
VERSION     WP_010807985.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..275
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29346
     Region          10..271
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mpdkrntvlt ervaarwvrl htaltlffli apilaivpls fnagsyfsyp ltgfsmrwyq
       61 qaltspdwqr allnslgiga astliatclg tlaalglsrs qfplrsvimp iiispmivpi
      121 vvvaagfyli faplglvnsy pgvilahaal gtpfvvitvt asllsfdqsl lraasglgat
      181 pwttfrrvtl plitpavatg svfafatsfd evivilfigg pdqktvprqm wsgirdaidp
      241 silavatmli vfavllfasi nwlrgrataa shams
//
LOCUS       WP_010808021             190 aa            linear   BCT 01-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010808021
VERSION     WP_010808021.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..190
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=20237
     Region          1..178
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mlrllskyww llvlrgvlav ifgiaafalp gvtiavlvlc fgafsfvdgi fslggawsar
       61 kehadwwlpl lqgiagivig vltylnpalt avalliyiva wsfvtgvlqv aagialrrev
      121 egelwvilsg vfsilfaifi mwqpgagala liwaigswai iwgvllvvag fklrgvthga
      181 sqapsghlrs
//
LOCUS       WP_010808069             146 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Pandoraea sp. SD6-2].
ACCESSION   WP_010808069
VERSION     WP_010808069.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..146
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15846
     Region          7..127
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 msalsirsgf idrlgiells aeggeselrl slasqhlnsw evmhggvtma mldvalstac
       61 rsvapegsgv vtiemktsfm qpgtgemraf grllhrsttm aycegevrda ndklvakamg
      121 tfkylrrlav grdvreqrrp ddprgd
//
LOCUS       WP_010808075             327 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Pandoraea sp.
            SD6-2].
ACCESSION   WP_010808075
VERSION     WP_010808075.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..327
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=33440
     Region          11..326
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mhllsatagl vlvngvsygl llfmlssglt lifsmlgvln fahasfymlg ayfayalsaa
       61 vgfwpalvaa plivgvigaa fergvlrrlr trgalaella tfglayivve laqlawgrgp
      121 vdygvpvafe gvlvhvagia vpayrlflmg lacaiallvw vafratragl ilqaalsqpa
      181 mtqalgydvp alytgvfacg aalaalagaa ggnvlvtepg maatvgsvvf vvvvvgglgs
      241 lggafvasll igllqtwavt sdaslaqwwp qsaagaenar galnafraav apmshltvaq
      301 lapavpyllm vavllwrprg lfgvreg
//
LOCUS       WP_010808126            1061 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pandoraea sp. SD6-2].
ACCESSION   WP_010808126
VERSION     WP_010808126.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..1061
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114036
     Region          1..1043
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mniskffidr pifagvlsvi tllagliavf qlpiseypev vppsvvvhaq ypganpkvia
       61 etvaspleeq ingvenmlym qsqansdgnl tttvtfrlgt dpdkaqqlvq nrvsqalprl
      121 pddvqrlgvt tikssptltm vvhlispndr ydmtylrnya linvkdrlsr ikgvgevqlw
      181 gagdysmrvw ldpakvaqrg ltasdvvkai reqnvqvaag vigatptgpn tplqlnvnar
      241 grlnteeefr diilktspdg avthlsdvar vqldassysl rslldnkpav glginqapga
      301 nslqisddvr aamadlqkdm ppgveyriey dptqfvrssi savvhtllea ialvvlvviv
      361 flqtwrasii pllavpvsiv gtfalllgfg ysinalslfg mvlaigivvd daivvvenve
      421 rniaaglspk eatyqamrev sgpiiaialt lvavfvplaf msgltgqfyk qfamtiaist
      481 visafnsltl spamaalllk dhhakpdwlt rqmnrylggf fgafnrvfhr gsekyghgvt
      541 rvigrkavmm aifavllgvt vllgkvvpgg fvpaqdkeyl iafaqlpnga sldrtetvir
      601 dmsaialktp gvksaiafpg lsvngftnss sagivfvtlk pfserkdksl saaaiaakln
      661 geysknkdsf iavfppppvl glgtlggfkl qvedrgalgy ealndatqaf ikkasqtkel
      721 gptfssyqin vpqlnvdldr vkakqlgvpi tdvfdtmqiy lgslyvndfn kfgrvyqvrv
      781 qadapfraha ndigllktrn gngdmvplss lvkvtptygp emvvryngyt aadinggpap
      841 gyssgqaqaa veriaaetlp rgvkfewtdl tyqqilagds alwvfpisvl lvflvlaaqy
      901 esltlplavi mivpmsimsa lfgvwltrgd nniftqiglm vlvglsakna ilivefarel
      961 emqgrtaiaa aieasrlrlr pilmtsiafi mgvvplvtss gagsemrham gvavffgmig
     1021 vtgfgliltp vfyvllrtla gkkplhsaha stmpanvkae v
//
LOCUS       WP_010808134              70 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Pandoraea].
ACCESSION   WP_010808134
VERSION     WP_010808134.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..70
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7682
     Region          1..69
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mstgivkwfn dskgfgfikp ddggddlfah fseiqpqgrt efrslqenqh vsfdvtrgpk
       61 glqasnikpt
//
LOCUS       WP_010808216             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Pandoraea].
ACCESSION   WP_010808216
VERSION     WP_010808216.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..187
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20421
     Region          18..165
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtgqdlpsll pgllprlwaf alritgdhhd aedlvqracv halervpqwq pgtsalswmy
       61 sivhttwine irarrvrsrg slawddadve aipdlqastp edlasfhqvf gavdrlpeaq
      121 rfvvllvave glsyqeaalv ldvpigtvms rlsrarrtig dqfrhparqp rgadgagpas
      181 gaceeda
//
LOCUS       WP_010808245             153 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pandoraea].
ACCESSION   WP_010808245
VERSION     WP_010808245.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16176
     Region          8..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtlsttalde ldrsllallr vnarestanl arrlgvartt vvarigrleq agviagytvr
       61 lgqdaagggl qacvgisvqp rsgrdvmrrl nkmpevhllc tvsgefdyva wlhaaspdql
      121 dglldtigei dgvtrtttsv vlarkidrgg vlp
//
LOCUS       WP_010808319             467 aa            linear   BCT 01-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010808319
VERSION     WP_010808319.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..467
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=52274
     Region          10..177
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mvrlillllg vdylrrrara liwigaiffa fglalifdal dgvvhfplkv fawllllegl
       61 atlaivtigv ggqrivrglk ggaftvaall vlffdqrsgn fwlsmlfgtl fladgllqcv
      121 aayvvryprw awamagglle iavaiffyqp ypthykgtlp yaiglglaft gwnvlvlamr
      181 arrmrrdfrv eqilgspedk rhlweerpra prwegppads epaltvhvwt psgsakapar
      241 rhpvidryia avdkngvist ghaalesheg iyvslypake idrspdqfgq llratrendv
      301 pgvfqpdyat eskawcpstv kvrirnyspr qlsafwqtyq qnatynlthr ncsssvakal
      361 eaaiegrvgr lqdgadagww tfvrlwltpe lwvaaqlrkr aktmawtpgl vldyaravsm
      421 lvdprpfgwi tmsslalrrm rrsrrawrea aeqaavaqtq gnqashg
//
LOCUS       WP_010808344             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Pandoraea].
ACCESSION   WP_010808344
VERSION     WP_010808344.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..239
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26292
     Region          10..237
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mldirkaadr gvadhgwlss rhtfsfanyy dpkqvgfsdl lvinddrvap aqgfgkhphr
       61 dmeifsyvle galehkdtmg tgsviepgdv qlmsagrgva hsefnhspts pvhfmqiwiv
      121 pnqtgiapey qqrrftpeek rgrlrmiisp dgsddslrih qdarvyaglf dgdesatltl
      181 apnryayvhv argsvslngv algegdgvrv rdetaltlsn gtdaevlvfd lrpeetpnf
//
LOCUS       WP_010808349             519 aa            linear   BCT 01-JAN-2025
DEFINITION  TolC family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010808349
VERSION     WP_010808349.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..519
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56097
     Region          98..476
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mtvshpfpgl plscvdrrat pvvsrprhph hrrapwaaav latlalsgca tfssdggfga
       61 vadatqqhlg qpvtwardda aaqdlakard dllsrpldid aavrltlfnh rglqatyeel
      121 giaeaslvqa grlpnprfsf qrlqgggdis iertwgldfv rvltmplasr iearrfaqvq
      181 aqvaqaiieq atltrrawie avaaqervqi leqtslatqa aseladgmar agnfsamrrt
      241 qenlvyadta arlarareqa gtareqlarq mglwgqqlpf tlparlpalp rtrpvwpdae
      301 aqalrdradi raaraaldst asdlgltrit rfvnvldtay rnnsatgsps ergyeislev
      361 plfdwgtarv agaqaryrqs vdrladtava aradvrtrra qtlaawdiae hyrvtilpmr
      421 qrvsdewllr yngmlasvfd lltdareqrd tvlayidata gfwlaeasfr eslgggeags
      481 hdtagtasap aapqgtaspp travspsqps sahqhggga
//
LOCUS       WP_010808438             994 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Pandoraea sp. SD6-2].
ACCESSION   WP_010808438
VERSION     WP_010808438.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..994
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=106712
     Region          46..993
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrrgflkas vvagisvyia plgsrafaal fedknltpva wdaakgqakf ridgtakvtg
       61 akifardvrs rdmpgwpaqq ahafilrttl adrpylgfdl srlddglqpd rvvsaddlar
      121 dgvafpefyg edmllpagkt paylghavai liyrdfarfr fakdklkfhn eiirygdvtg
      181 plerdpwgsf ryvrvggkta ydddvysslk dapifpsmmr khlpvwpdgn dhgkldeqgm
      241 ayagkigesl thppanwlvm sreyrtqsvd taalepdnan cwydaatqtl hmvvptqsps
      301 evaenaaama akghfpvkrl ivypcytvgy gskdhynmpf yglaaalygd glpvrlandr
      361 yeqfqtslkr haftmryrig vdkesgllqa faadmecngg grmnfspsva mvgataaqsi
      421 yyfpqsdlas vaiasraida gsargygtlq smaatemmid emaaqlgvda idfrlknalr
      481 sgmkntqgai pagavrvdev larakahplw tqrdkkkaey eaahpgrryg vgfacvqkdf
      541 gtgaetsfar veidetgkis lrhtaaeigt gtstsqavav akwlgmpatd vhiaitdwpe
      601 lpvvtsgdpy lmsqadqdkl aanprwspgy aspssatnsa fyfthstrea arllflqglw
      661 paalsiwrrg lgggqaaplv vraedarwve gklsaaglea lplpmlakta helglvtgat
      721 vhvfnrwqwa eadwdlgdgv tqrlpvdgia lrfgkggtna apaaptpltp tpaakaahrs
      781 sgnaqaksga aassadaaag kgakgapsln agsagmqvaa ptpgtgyrti drkrvyyppv
      841 qrnnaavtyy savgtlvels vheasgkvel lthhsimecg nqispqlvsg qlqgglamgi
      901 ghalheylpl yedgpgngtw nfnryhlpra vdvavwtqtg evlppisetd vpkgiaevvm
      961 ipvvgaivng lahaighrft dlpvtpekiq evla
//
LOCUS       WP_010808535             362 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: porin [Pandoraea].
ACCESSION   WP_010808535
VERSION     WP_010808535.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..362
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38405
     Region          10..362
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mksaipasla ilsaacglaf sttataqsav tlygivdqsv ryqtnanann dalwqvtnga
       61 vtnsrfgfkg sedlgggtka ifqlesginp qngqltngpr lfdryafvgl qnqygaikig
      121 rqateafnvy gdfdpltign yannswmyni trgrvdnavs yagtfgglsv gatygfgnta
      181 gtmaasnywg traaytmgpl qvagvyqqar daakrvqqmw glggiysvsi akvfvgymgg
      241 rdrsgwldgt lndpahavtt gnlndnprkd mtfylgttiq ampnlaitga ayfddiknin
      301 aqasdagsgr rytyvllaey alskrtqvyg tvdynkvsga arvelpgnat qvgvatgirh
      361 if
//
LOCUS       WP_010808504             282 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Pandoraea sp. SD6-2].
ACCESSION   WP_010808504
VERSION     WP_010808504.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..282
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30416
     Region          25..279
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mvvvktslsa ftgapahgvp pshderkfvt alargldllr afgpddallg nrdfaartgl
       61 pkatvsrlay tltalgylry daelgkyald agvlalgyaf lsgtdmltla rphmralake
      121 mgcsislgcr egidmmylet irsdsahltl gltagsrlsm ltssmgrvyl aampsieret
      181 mladlrdayd anpaalrnvg wdvlqsgvek giesyrregc cysfrewheg vnavavplrd
      241 vrqnrwlais csgpsssipd alfreeigpr lkqlaarlsg qa
//
LOCUS       WP_010808536             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pandoraea].
ACCESSION   WP_010808536
VERSION     WP_010808536.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..157
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17595
     Region          1..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mnldladlri lrhlelngri snqeladavg lspsaclrrv klledrgvis gyrcivdaqh
       61 iglefealvq itlrpdvdqw hekflacvqn wpevvtariv tgsanyiltv rarnlahysd
      121 fivnelyrap avmsiqsniv lktikhtqsl vdlvkpk
//
LOCUS       WP_010808556             374 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010808556
VERSION     WP_010808556.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..374
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41118
     Region          81..370
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mplqrfiarr lgaltepstr ipyawvyhep dvfmqrtssl svakkylhrr lrlaisgqsn
       61 revrhvapna rvlwiyggka svgdavmdms grallrgreg pvdllitpgl kalfegddif
      121 rhvyddpasv npgeydvivl qefnyptlrl krkffpslpf aclfrffhgp drnqtqfsfa
      181 avndvfslgl asddlfarak pylrreselp eavaqqlpag pflvlamggv eprrtyaqwr
      241 eflqaydiay qpgmpagivl lgsgngadaa kalmtakfvn lqlasyvgql tlreakrvia
      301 naalfvgadg glmhvahtts tpsvtlfaka eppylrltpq cqsvplqtds dvsavdpeel
      361 aetvvatlas vplr
//
LOCUS       WP_010808561             298 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Pandoraea].
ACCESSION   WP_010808561
VERSION     WP_010808561.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..298
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31516
     Region          1..298
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 msqiyavlvd gvmyaawlfl valgltlvyg vlkilnmahg slyalgayag vtligpwvaq
       61 ggnlyvsyll lvlaaivagg aigfimergv lkrfygqdpv vlllvtyalf limedaiklv
      121 wgvdpytvse pysflgnfdl gdlsypnynf livgvalvag igltsflkft rsgrllravi
      181 hdrevsqamg irvsryfvvt fmagavlaai ggaltaptvs vapgmgveiv vltfavvvig
      241 glgslpgaaf gallvglvra savhywpqge lfsiyivmal vlavrpkgif apmearki
//
LOCUS       WP_010808587             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010808587
VERSION     WP_010808587.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33634
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mhqldamrif vrvtetgsft qaadslglpr asvsnaikql eaklgtrllh rttrrvqltq
       61 dgqaclercm dlladmeewe tmfaardeal tgrlridlpa tlarttvipq lpgflaqhpa
      121 lrvelsstdr rvdlvregfd cvlrvgaiad stliarplgh mrqinvaspa ylerygvpht
      181 lddlrkhqli hytttlgtrp vgweyfdger ytqwpmegvl tvnnadayqa aclaglgliq
      241 apesgarehl aigalqevlp ehqaeplavt llyanrrhlp rrvhafmnwl tdlltprlth
      301 l
//
LOCUS       WP_010808590             159 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pandoraea].
ACCESSION   WP_010808590
VERSION     WP_010808590.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..159
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17519
     Region          1..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 meldaidlki lrelqadarl tnvelasrvs lspspclarv kaleaagyir qrvtlldpsr
       61 lglhinvfih vtlenqnrdr ldafeaavta lpnvmecylm sgdadyllrv mvsdmsayet
      121 litdrlsrip girnirssfa lkqvmyttav pvpdtsgda
//
LOCUS       WP_010808607             338 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Pandoraea].
ACCESSION   WP_010808607
VERSION     WP_010808607.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..338
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=36157
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..310
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,236..241,
                     247..248,250..251)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 midritamrt fvrvaevgsf tkaaasldip rttattqvqh lerwfgvalf trstrrvalt
       61 megaayferc aailadveev esglfgaqaq lrgrlavvlp pviarevvmp slvefqaryp
      121 gleialdatp ahgdwrgdgv dcgvvlgelp dsrlvarhlg dlprvtcasr ryldmqgtpa
      181 dldalamhts vkwltapaes laspsalapa tslttrcgdl rlmvggratc vrtrgqlhvg
      241 devaylaagl eglgliqptl laaapyltsg rlvpvlpecp ppplrlsaay paqkrvsprv
      301 rafvdwlaqi ceplgnardy aplppvppva rrsftlpa
//
LOCUS       WP_010808609             154 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Pandoraea].
ACCESSION   WP_010808609
VERSION     WP_010808609.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..154
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16892
     Region          3..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mneldaidqa ilaivqrdgr isnarlaerv alsetpcarr lkrleaegyi tgyraelshr
       61 alglgvtafv hvrfavhdra lseqferevq aidrivschn isgsadyllg vvatdlddyg
      121 mftrdvlral pgvssiesml slrevkrdtg apll
//
LOCUS       WP_010808617             208 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Pandoraea].
ACCESSION   WP_010808617
VERSION     WP_010808617.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22014
     Region          2..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mptfatlttf vvvvlglfli pgpavlltit rtvqggrrag imtgmgialg dlvhtlcaav
       61 glsavlmtsa lafdvvkyvg aayliylgik alrerpsdpq lpvapevspg rafvqavate
      121 vlnpktalff lafmpqfvha segdvfaqfl glglvfvams alytaaials vrplgkvvrr
      181 frgllrwqgk iigtifiglg lrvamqqr
//
LOCUS       WP_010808682             490 aa            linear   BCT 01-JAN-2025
DEFINITION  SLC13 family permease [Pandoraea sp. SD6-2].
ACCESSION   WP_010808682
VERSION     WP_010808682.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..490
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50666
     Region          110..483
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mptvnpsssa rapvatataa dtfaprhlwr hallagisaa aglglyaagl rgdtlavavi
       61 vlfclgywat gwlpdflvsl almfllatct slgasvvfsg ftssafwlvf sgavigmalg
      121 vtglgervas rladhcghay gialagfvti afvlgivmps tlgriailtp ivlsfcerig
      181 ltrgrpgrtg lllatalasc elstailpan lpnlvmagta etvlglrlgy geyaialvpv
      241 lalvrgvvlv avamrlfpdr ltplaeatml dnvdnvnnac tamrpaewrl laalalmlgl
      301 wltepwhhia agwvglgval lclgplrlvn pdaflkqvkl aplwfvaaii gltaavdhag
      361 lanalrpvls rldlaqmsga saylvlvals valtflvtsn aapalytplv palalgaplg
      421 vkavlltqav gistialpyq applvlamal agigirdatr ycvasalial vtvvpltalw
      481 wqligllrlh
//
LOCUS       WP_010808706             370 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Pandoraea sp. SD6-2].
ACCESSION   WP_010808706
VERSION     WP_010808706.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..370
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=39892
     Region          102..368
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mlaiiallha yigwrllppl pvglgwkvlg gmwlaastvl iplglmsrai qreplatllt
       61 wtgmtaigvf stlfvltllr dvvlgvamal saldaqlvtr savivlglta lstllgfyna
      121 rrlarvvdvd vpianlppel kgftivqlsd ihvsstirrr yitaiveatn elkpdlvait
      181 gdlvdggvpa lrdhiaplaq ltsrhgtyvc tgnheyysga pawveelrri gltvlenehv
      241 vldhegaslt vagvtdftah hfdpekrsdp laaiagapdg vprlllahqp rsasaaqeag
      301 fdlqlsghth ggqfwpwmyf vplqqpyvhg lhrlgrlaiy vsrgtgywgp pkrfgapsei
      361 trlrlvpgta
//
LOCUS       WP_010808721             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide biosynthesis/export family protein
            [Pandoraea].
ACCESSION   WP_010808721
VERSION     WP_010808721.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..238
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25464
     Region          38..206
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mnilrptcvl vltmltacth twvdtkyqqa drfatwvdat pspyrllagd disvvlpfnv
       61 elnykgrvap dgtiampfag nlpaagqtla qfgetvnral atngmtanah aivavtqtaa
      121 hifvggevgk pgelaltpgm svmqavitaq glldtartge ivlirrspdg rpmlrtvdvk
      181 altqqgdpaq divlqsndti fvpkssiaev dlwvdqfink glpfqknvny dingarsf
//
LOCUS       WP_010808744             634 aa            linear   BCT 01-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator [Pandoraea
            sp. SD6-2].
ACCESSION   WP_010808744
VERSION     WP_010808744.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..634
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=69524
     Region          5..630
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpantesaha rrvlnavqgh slhgaaatdp niadswrrcl dthaldpgar maprvlesaq
       61 lrerrsamer lrsvstpvle rlqrqlmnph qavlltapdg vivdsrlhdg qrddfhragl
      121 wpgadwsesc egtngigtcv verapviicq qdhfralhta ltctaspvfa pqgellavid
      181 vsstsadltr qsqfhtlalv nlsakvvese yfflhyrdew llqlqeqadh lggfaqalia
      241 fddagrvlaa nqsalnrlgv prdeivgtrv drwfaqtlda llaqghpaps acwpirthhg
      301 esllamvrap hraarrvshl pmsrqetsap pfsdpalare fsracrvfah dvpvlirget
      361 gsgkevfara vhaasarang pfvalncaai peslieself gyvggsftga rkegmngklw
      421 qanggtlfld eigdmpfamq trllrvledr mvsplgggep vpldirilsa thrdlseria
      481 erlfredlfy rlsglevgvp plreredkid liqrllaqac eqgritvtda aqdrlctyaw
      541 pgnvrqmrsv irtlvalses gvvtlddlpg elrdvervat etpraeaple aaerqalrat
      601 ldacqgqvsa aarklgvsrn tlyrklkrfg llrg
//
LOCUS       WP_010808756             138 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010808756
VERSION     WP_010808756.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..138
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=15115
     Region          22..124
                     /region_name="cupin_bxe_c0505"
                     /note="uncharacterized protein bxe_c0505, cupin domain;
                     cd06980"
                     /db_xref="CDD:380385"
     Site            order(27..33,42,44,46,48,66,68,70,72,90,92,94,111,113,115)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380385"
ORIGIN      
        1 mnsnenkfsh ikpgdtafvs gglrdffvyr dlgisdatgg kviahlvran sapeagtgwh
       61 ihgadfhivy mlkgwakfmy edeetlveag dcvhqrpgir hflfdyspdm eylevvgpad
      121 ftsvgvegpc evpapakw
//
LOCUS       WP_010808762             415 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Pandoraea sp. SD6-2].
ACCESSION   WP_010808762
VERSION     WP_010808762.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..415
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44395
     Region          11..400
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mntnigarwd tsyewkavll lslgfglvgi drfmimplfp immkdlqldy qdlgyitgal
       61 svawgvssif mgnlsdhvgh rrviipaivv fsllaglsgv atglgslvli ralmglaega
      121 ctptsitatl dashpsrhgr nvgiqqmalp lfglglapil vtqllkimqw hsifaivsip
      181 glvvafllwk vlrdtkapsa avhtlthdat ahkwsdvfry rnirlnlvgm lcwltclvvl
      241 talfpnylvd ylhldmqqmg yvlsaigfgg mlgtvtmpal sdrlgrkpvm vlsvigcaif
      301 ltllsrtgak ptqlfvylmm tllfvfsmit ltvgplsaes vpatlmttas glvvgvgeif
      361 gggvapavag yvakhygiqy ilvlgfiala vgffvaislk etapslvekr aaiat
//
LOCUS       WP_010808795             257 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010808795
VERSION     WP_010808795.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..257
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26247
     Region          18..249
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mmntqpltnl vpllslglft fllagfvkgv iglglptvav gllglampta eaaallivps
       61 lvtnvwqlla gprfaalakr lwpmligigi gtwagggwla nggdfagmal gvallayavl
      121 glaavrlhvp kswpgarvsa lggvigvitg lvtaatgvfv ipavpflqal dldkddlvqa
      181 lglsftvstv alaaglahdg ifhghaigvs llalapalgg mffgqwvrtr vsatvfrrcf
      241 fvglamlgae lviqhmr
//
LOCUS       WP_010808799             835 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [Pandoraea].
ACCESSION   WP_010808799
VERSION     WP_010808799.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..835
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=89908
     Region          47..764
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mslkhclppr apsdpahrns piippqapsa hvaspsgpgr qrgfgtfaai lvtlaglaiv
       61 galltgyali vmrpnlppld vitdyrpkvp lriytsdnvl igefgeerrs lvtidqipdv
      121 mkkavlaied yrfydhggvd figilragvs dvlhggaaqg astitmqvar nfflsrekta
      181 trkiyemlla ykiesalskd kilelymnqi ylgqraygfa saariyfgkd lkditlgeaa
      241 mlaglpkaps aynpivnpkr akirqeyilk rmldlgyisr nqyedalhep irtrtsgney
      301 nvhaeyvaem vrqavydeyk ddtytrgltv ittldskkqq aayeavrmgv ldyerrhayr
      361 gpegyvelpa ampdrqqlie dtllehpdng dlvaavvvaa sasqvtaipl sgdavtvngd
      421 gigfaasals akagekvrir pgsiirvmkd arakwrivql pevqgslvsl spddgairal
      481 vggfdfnqsk fnratqawrq pgstfkpvvy saaiekgvsp atmvldgpln lppaqtggqv
      541 wdphdddafs gpmtvreglq rsknlvairl lqfagtqytq eyatrfgfda dkvppylpma
      601 lgagqttplq lagayavfan ggyrvapyli seirdargnv lnkatpviag vnaaraisap
      661 nafimnsllq tvaqrgtgsg tnvlkrtdla gktgttndal dgwfagyqhs lvavawlgfd
      721 qpktlgsref gaqlalpvwt kymgvalngv pqqqmampeg vsvvngelye tdklpgngfv
      781 asigiddngg gfslpffgnn spspaapppa sgqppspggv danekarild mfkrp
//
LOCUS       WP_010808822             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TadE/TadG family type IV pilus assembly protein
            [Pandoraea].
ACCESSION   WP_010808822
VERSION     WP_010808822.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..158
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=16313
     Region          1..126
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mkwsgaqaga rlrcansrgv aalefmlilm illpafyvav sfsinilarq mltqaaseag
       61 ramlragtms qrqayatqai nstltwpsas vvtasfasda sapcpasatn sssqcivrvt
      121 ltltqpmtvs wpgltnlvpq nivgtaaitl dtstlggs
//
LOCUS       WP_010808800             210 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Pandoraea sp. SD6-2].
ACCESSION   WP_010808800
VERSION     WP_010808800.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22462
     Region          4..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpaistwlaf alvaigmalt pgpnmmylvs rslcqgpaag lvslggvalg fvfymmcaaf
       61 gitallfavp faydllrfgg aiylfwlawq alkpggrspf evraldrdsn rrlflmglft
      121 svlnpkiaml ylallpqfvh pehgsvltqs lvlgatqiva svavnasval cagsiarflg
      181 qrpawlriqr wlmggvlgal avrmatearr
//
LOCUS       WP_010808845             393 aa            linear   BCT 01-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Pandoraea sp. SD6-2].
ACCESSION   WP_010808845
VERSION     WP_010808845.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40315
     Region          1..393
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdivivsaa rtavgkfggs iakvaapdlg aividevlkr aklkgedise vimgqvltag
       61 sgqnvarqas ikaglpamvp amtinkvcgs glkavmlaan aiatgdadiv vaggqenmsa
      121 aphvlpgsrd gfrmgdakli dtmivdglwd vynqyhmgit aenvakeygi tremqdafaa
      181 asqnkaeaaq kagrfdaeiv pvsipqrkgd pvvfktdefv rhgvtaesla glkpafakdg
      241 tvtaanasgi ndgaaavvvm sakraeqlgl tplarivaya nagvdpsvmg igpvpasqrc
      301 laragwkasd ldlmeineaf aaqalavnkq mgwdtskinv nggaiaighp igasgcrilv
      361 tllhemarrd ahrglaslci gggmgvalav erv
//
LOCUS       WP_010808855             341 aa            linear   BCT 01-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Pandoraea sp. SD6-2].
ACCESSION   WP_010808855
VERSION     WP_010808855.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..341
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37046
     Region          7..337
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mprlqpvyll vmpntllldi aapaealria nhqqddvrfv lryvgtqrsv atsvglrlsp
       61 ldvlpgdvpd dawlvvagtv ekplpeqvtd dgtmtdlsnl sdapaedaea ravawlrqvv
      121 rpthqlacic tgallaarag lldtractth hgscdelral apsarvadnr lyvhdgnvwt
      181 sagvttgldl mltlianatg plcaaavarq mvvyarraga dpqlspwleg rnhlhpalhr
      241 vqdaiaadpa hdwtlatmad iacaserhvt rlfrehagva pidylhrlri alaremlgns
      301 hldleriaer tgfgssrhlr rvwhkfealp psrarratnd g
//
LOCUS       WP_010808856             188 aa            linear   BCT 01-JAN-2025
DEFINITION  cysteine hydrolase family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010808856
VERSION     WP_010808856.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..188
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20713
     Region          13..179
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 msqnqtaqts rtallvidaq esfrqrpywr eddlatyfsr qqalvdgava rgvpvvqvfh
       61 idsgvfsrds gfvrtleelr iapvftvdkv khsalagstl gawlvehgit rlivsgirte
      121 qccetttraa sdagyevdfv teatltfpmq hprtgrelsv adlkertetv lvdrfarivt
      181 veealaav
//
LOCUS       WP_010808955             550 aa            linear   BCT 01-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Cupriavidus sp.
            GA3-3].
ACCESSION   WP_010808955
VERSION     WP_010808955.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..550
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=58863
     Region          29..534
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mkppalpagd alvapldvlr qyrahdatlt gflaarvaah pdkpalvfeg etwsyrqldq
       61 rigltadwla qamqvgpgdr vgvlstnhps tvvlmfalar igatmvpanp eyrldealyv
      121 frhaqvcglv capgtlatga avaadlggdv wlranedgdh gvptlaasia ahaaqpanaa
      181 pgvdsdrsta liiytsgttg fpkgamhshr gyvltaeafv grlhlqpder vmcvmplfhi
      241 nalmysvgga lacggclvlm rrfsassfwr faaesgatev nlvaaagsil arrpraefvp
      301 ghritkmfia pqtqemvrvm kqefhvprli ecygmteipg vianpfngph klgtmglisp
      361 hpdpavpvpe arivdddghd vapgaagell irtptlmqgy yrdavqteaa frdgwfatgd
      421 lvrqdsdgyy vfvarkkdvi rrkgenvsga eldrifgehp aveeaaaigv padlgeeeil
      481 lavqfrpgqs vepgellawa rdrlavhklp ryvvavdaip htpthkpakh klkadgtlfa
      541 raidmaaash
//
LOCUS       WP_010808965             193 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: peptidylprolyl isomerase [Cupriavidus].
ACCESSION   WP_010808965
VERSION     WP_010808965.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..193
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=20592
     Region          27..193
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mirsrrivla gltagalaly sfsalaqqaa ervqfvtsag kftvelypea aprtvanfle
       61 yvksgfysgt ifhrvingfm vqgggfdrdm kekptrapip leargglknk agtvamarts
      121 dpnsataqff vnvvdnpnld ypqpdgngya vfgkvvegme tidkiksvpt taygpmrnvp
      181 aapiviesat vvk
//
LOCUS       WP_010809009             279 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Cupriavidus].
ACCESSION   WP_010809009
VERSION     WP_010809009.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..279
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30346
     Region          2..258
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mwidthchld asefdadrqq vadaaeaagv rgivvpavaa wnfeavrala rhdvrcvyal
       61 gihplcspga gqadldtlrr evaasmgdpr fvgigeigld ffvagldaeh qtwlyaeqlk
      121 iarefdlpvl lhvrksqdqv gaqlrklgvk rgiahafngs neqarrfveq glklgfggnv
      181 tfsrarqirr latelpleal vletdapdma pawlsddqfg eqhkarntpa evagvarvma
      241 elrgidamtl ahatwrnavd amprlgtfae smaprpglr
//
LOCUS       WP_010809063             132 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [Cupriavidus].
ACCESSION   WP_010809063
VERSION     WP_010809063.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 132)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..132
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13463
     Region          27..126
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mntlktlsfa lgalvlgaaa mpasaadlaa gkalvekgac vachgagmna pispdypkla
       61 gqhadylyha lasyqvsgnp lvgrsnaima gqvnanpavt dkdgkprpft rkelkdmaay
      121 ieslpgdlvl kk
//
LOCUS       WP_010809087             207 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Cupriavidus].
ACCESSION   WP_010809087
VERSION     WP_010809087.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..207
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23042
     Region          21..197
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mqapdpvpsa apgaalsalp dhdlmllvag giieqpvtel frrhnaglyn yvawlcqgnr
       61 geaediaqkt wvklmtrcgd yqpdaafrtf lfqiarntwl dqvrsadarq realddqpae
      121 mpaddlspea elqlrqhahh vhrallqlpv aqrevvvlrf fsdmsveeia qmlgekfetv
      181 rsrlryafar lranlagsvp gsqetps
//
LOCUS       WP_010809131             119 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADH-quinone oxidoreductase subunit A [Cupriavidus].
ACCESSION   WP_010809131
VERSION     WP_010809131.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012780
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..119
                     /product="NADH-quinone oxidoreductase subunit A"
                     /EC_number="1.6.5.9"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=13465
     Region          1..119
                     /region_name="PRK06602"
                     /note="NADH:ubiquinone oxidoreductase subunit A;
                     Validated"
                     /db_xref="CDD:180638"
ORIGIN      
        1 mnleayfpvl ifiifgvvlg valmsigril gpnkpdpakl spyecgfeaf edarmkfdvr
       61 yyliailfil fdletaflfp wgvalrdigw pgfiamgvfl lefivgfvyi wkkgaldwe
//
LOCUS       WP_010809173             468 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleobase:cation symporter-2 family protein
            [Cupriavidus].
ACCESSION   WP_010809173
VERSION     WP_010809173.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..468
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48642
     Region          26..448
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mnsasttvpt dltnerlpsg rllalglqhv lvmyagtvav plivggalkl pkdqlaflin
       61 adlfaaglat liqafgfwkf girlpvmmgv tfasvapmia igtdpnvgll giygaviasg
      121 ifgiliapmm grmlglfppv vtgtvitlig vslmrvginw aaggqpttra vidgvvkevp
      181 nlaygdlanl giagltllii llltkygrgl vancavllgi iagtlvamam gkvsfeglde
      241 asfvavitpl hfgmptfevt ailsmcivml itlvestgmf lalsditgkk lsnedltrgl
      301 radglgtvig gifntfpyts fsqnvglvtv tgvrsryvaa aggiiliafg lfpkmahvva
      361 svpqfvlgga givmfgmvaa tgirilgscd fnrnrhnlfi vaisigagmi ptlaptffqy
      421 lpkwtgpfth sgivlgtiva valnlfyngi qsreeamrna aanshgte
//
LOCUS       WP_010809191             456 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Cupriavidus].
ACCESSION   WP_010809191
VERSION     WP_010809191.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..456
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47992
     Region          171..453
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          353..453
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(357..358,391..392,395,399..400,403,445,449)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mtfglttrka aiglgvvall alagckkkpa dsaaaqgdaq papaavsaqp vasapampaq
       61 tnvaglwsga fvvnrdkedr swypllneip dhagfmrngs rqelvialaq assvdvlrfr
      121 glsdagarsn arharveasa ggtqgpwtvi ydadlpgqdg ydtrvplaqp vkagalrltl
      181 tgnrwpgdqd egqiglqqfm aygkpeaaad kvrqvggiyq fpvefgssgy vllhqdgaav
      241 egcyvegdys nkqmkitqvl gtisggleng allafrrtte gapekgamaf spdgshayaa
      301 lvkgdartfd svreaggwrl adkappcfpk aeaapdpigq alegagrvql ygvnfetdsd
      361 vlsaaarpll draakavlah pdwrlrvegh tdstggdarn qplserraaa vrrylesagv
      421 padrldakgy gathplmpnd tpfgraqnrr velakq
//
LOCUS       WP_010809217             147 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Cupriavidus].
ACCESSION   WP_010809217
VERSION     WP_010809217.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..147
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16794
     Region          11..146
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 meermnwqdv apdaykamig levylarcsl ettlkelvki rasqingcaf cldmhitdar
       61 khgeserrln llpawrevsw ftpreraala wtealtllpq sqapdadyqd lreqfsekem
      121 adltllisai nawnrfgvgf rrqppal
//
LOCUS       WP_010809238             310 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Cupriavidus].
ACCESSION   WP_010809238
VERSION     WP_010809238.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..310
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33081
     Region          33..296
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mdtlattfat vpaaaaetvq rsravdrvvr giatsdgagv kltrvltqnl qrrldpflml
       61 dafgtdskdd yiggfpdhph rgfetityml agrmrhrdsa gnegllqngg aqwmvagagv
      121 vhsempeqed grmegfqlwl nlpaadkmta pwyrdlpaae iptvaldnga tvrvlagath
      181 gvagaitrpv tepvyldvhl pagqtfaqal paghnafvyv yrgevsigsg ddravieaqr
      241 mgvldnagqs dgvivraead arflliagqp lnepiaqygp fvmntqeqiy qtladfrdgr
      301 fatsaattga
//
LOCUS       WP_010809235             216 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Cupriavidus].
ACCESSION   WP_010809235
VERSION     WP_010809235.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 216)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 216)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 216)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..216
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22583
     Region          2..215
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mdlfsylqhs wptllkmtge hlalvgsavg lailigvpmg ivitrfrala tpllalativ
       61 ltlpsialfg lmipifarfg halgyvpavt avflysllpi mrntytalan vdpgiqeagr
      121 gigmtawqrm rlvdlplavp vilggvrtav vmnigvatia aiigagglgv lilqaisqsn
      181 msklavgavl vsllaivada flqwlqralt pkgiri
//
LOCUS       WP_010809240             369 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Cupriavidus].
ACCESSION   WP_010809240
VERSION     WP_010809240.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..369
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38883
     Region          21..366
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 madvrqllpr splslaprgl psrtmayasp vvalaltllf gallflvlgk dpvaalkvfl
       61 adplrdqrai gevllktvpl vlcalglsvc yranvwniga dgqliaggic agatvlyfdv
      121 pgqamngtvv lvlaslagmv ggmlwaslta vlkdrfnane ilvslmltyi aqqlllwvvn
      181 gplkdpngmn fpqskvfsse yllpnlmsgs rlhagfavml vlvavmtvfv frsfagyrlq
      241 vggtapaaar yagfsarsal wsallisgat aglagafevt gpigqllpsi spgygftaii
      301 vafigrlhpv gtvfggimms lfyiggemaq srlglpsaig wvfqgmllff llacdtlien
      361 rlrwratta
//
LOCUS       WP_010809249             759 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Cupriavidus sp. GA3-3].
ACCESSION   WP_010809249
VERSION     WP_010809249.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..759
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80617
     Region          <63..>192
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          196..756
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtatnlqpsa qadaetprtl rlallqatgv llvtrapqaa prpapgqpga asdyvpalpd
       61 ifiavrdsge vlafnghvdl gtgirtalaq ivaeeldvpl ervrmvlght eatpnqgpti
      121 asasiqisal plrraaaqar awlraraaqr lgveagglea edgvfrdpgt qasigygall
      181 agehlelpla ediptkpves yrivgraagr vdipgkvrga ltfvhdvrvp gmlhgrvvrp
      241 pyagrdsgdf vgnsllevdr dsvrdvpglv dvvvqgdfvg vvaereeyav qaarrlrvrw
      301 kpvpplpald dpepalranp atrrellsdg eppasgagtv lqrrfvwpyq mhgsigpsca
      361 vadwhddglt vwsgtqnphv lridlarlcg lgedrievvr meaagcygrn caddvcadaa
      421 llsravgrpv rvqlsreqeh lwepkgaaql mdvsatlgpd gallgydfts rypsndaptl
      481 alvltgavpn aprtlemgdr tavppyayga rrigcddtpa ivraswlrgv salpnafahe
      541 cvidelaaea gadpvdfrlr hlpdvraaal lravaevagw qrgvagsrgi adaegrlrgr
      601 gvayaryihs rfpgfgaaws awvvdlavda gsgritiekv vvgqdtgmmv npdgvrhqih
      661 gnvvqtlsrv lkeqvrfdad gvasrewgsy plltfpeipp ievvlmprqs epplgagesa
      721 slpgapalan alfdalgvrl rrppfvpetv laalaamns
//
LOCUS       WP_010809275             319 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Cupriavidus].
ACCESSION   WP_010809275
VERSION     WP_010809275.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..319
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35224
     Region          42..315
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mtmhtflapa epvrypdarv qalsprfeky hlplaaidri atgcrwsegp vwfgdgryll
       61 wsdvpndril rwdeetgnts mfrspsnhan gntrdrqgrl vtcehvgrrv trteydgsit
      121 vladrydgkp lnspndvvvk sddsiwftdp pfgiagyyqg ekatselper iyridpasgr
      181 ldivaddvsg pnglafspde ellyviesrt rprrirafqv seggealgns rvlvdagpgt
      241 pdgfrvdidg nlwcgwgmgt peldgvrifa pdgepighis lpercanlcf ggrhrnrlfm
      301 asctsiytly vntqgaagg
//
LOCUS       WP_010809281             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010809281
VERSION     WP_010809281.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..267
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29096
     Region          17..263
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpnstvnier ikpgqgkatp nrslergiav lrafragasm lgnseiaert glsrstvsrl
       61 tqslietgml eyvpqcrayr lgvpvlsmah amrdgsqvlr vaapmmaeva mrhkinvgla
      121 vaegdemiyl esfrynrrqs lrtvvsgqri pmaltslgra hlatlapeaf nammramadk
      181 nrgrgwgelr reidaavssv hekgycvasw qpqvvamatp lrfdeyavhv lnvsvsthqd
      241 agaveaalak plmelaaaiq ermprve
//
LOCUS       WP_010809306             152 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010809306
VERSION     WP_010809306.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..152
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16033
     Region          1..150
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 misfqlngkt qqvdvpgdtp vlwvlrdtlg ltgtkfgcgi avcgactvhv dgqqrracvt
       61 rvssiagrql ttiegigedp vgraveeawv rndvtqcgyc qsgqvmsava llrvnrrptd
      121 adieqamsan lcrcgtyari haavkdaaka ig
//
LOCUS       WP_010809327             102 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DUF485 domain-containing protein [Cupriavidus].
ACCESSION   WP_010809327
VERSION     WP_010809327.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..102
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=11069
     Region          2..102
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 mdarqletiq nhpdfirltn grtrlgwslt lvmlaiyfgf illlafspat lgtplgagvm
       61 tvgipvgvav ivsavlltgi yvyranrdld plnervrkec ra
//
LOCUS       WP_010809316             388 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Cupriavidus].
ACCESSION   WP_010809316
VERSION     WP_010809316.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..388
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43493
     Region          11..386
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mieqtqsnnf qeirdairal caefpdeyfr kvdeqraype afvnaltaag wlaalipqey
       61 ggsglgltea svimeeinrc ggnsgachgq mynmgtllrh gsraqkdkyl pkiasgewrl
      121 qsmgvteptt gtdttkikts avkkdgryvv ngqkvwisrv qhsdfmilla rttpladvkk
      181 ksegmsifmv dlheaqkkgl tvrpipnmvn hetnelffed leipeenlig eegkgfkyil
      241 dglnaertli aaecigdgyw fidrvtkyvr erevfgrpig qnqgvqfpia esfieleaan
      301 lmrwkacelf dkhepmgaqa nmakylaaka sweagnaclq fhggfgface ydverkfret
      361 rlyqvapist nliysfvaeh vlglprsf
//
LOCUS       WP_010809356             159 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Cupriavidus].
ACCESSION   WP_010809356
VERSION     WP_010809356.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..159
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17783
     Region          4..144
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mqepeldein irilealqrd asltnvelaa rvnlspspcl arvraleqrg iirqrvtlld
       61 pqklglnvnv fihvslerqa regldafera vralpnvmec ylmtgdadyl iravvadvqa
      121 verlivdeit ripgvanirs sfalkqvmyd talplrnpr
//
LOCUS       WP_010809388             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Cupriavidus].
ACCESSION   WP_010809388
VERSION     WP_010809388.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..143
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15639
     Region          5..143
                     /region_name="COG3565"
                     /note="Predicted dioxygenase of extradiol dioxygenase
                     family [General function prediction only]"
                     /db_xref="CDD:442786"
ORIGIN      
        1 msatssiplf hlafpvrdla earrfygdll gcpegrssea wvdfnfyghq vvahlspeec
       61 ghratsavdg ddvpvrhfga ilpmaeweal aerlraagtq fviephvrfk gqvgeqatmf
      121 fldpsgnale fkafgdlsqv fak
//
LOCUS       WP_010809412             250 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Cupriavidus sp. GA3-3].
ACCESSION   WP_010809412
VERSION     WP_010809412.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..250
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27056
     Region          38..249
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mglasppqrp qpqlagklpg tvpprddala avragawfsq lppalrqall ddgslrrlva
       61 getlfargdr fdglycvasg tmqihasges gkaallglle pgtwfgeicl fdglprthda
      121 ravsattlwh vtrssleqrl aqqpawwqaf gqllaaktrq afnyveeaql lppaariarr
      181 laaiahgygn lpqvqatqrv ripqeqlaqm lglsrqtvnh alreleargl lrleyggiel
      241 ldlpalealn
//
LOCUS       WP_010809450             324 aa            linear   BCT 01-JAN-2025
DEFINITION  sterol desaturase family protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010809450
VERSION     WP_010809450.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..324
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37117
     Region          134..297
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mwetlngwig qvegtlfqdv vlpvvydlgf gryaeeaftg tewllvglvq ivvmalilgp
       61 lekwrpvepv sdragirtdi fytvihrlgl frlamfflla pltdalegdl rlmgwhrinv
      121 edwwpgvtsv plisffvyll lfdfldywyh rlshsfrwww hlhavhhsqr qmtlwsdnrn
      181 hllddmlrdl vfalvalgvg vepsqyvllv alsqllqslq hanvrlhfga igerllispr
      241 fhrthhavgi gheadgapak lggcnygvif pwwdmvlgta vftetyhptg irdqlppplg
      301 kghdygagfl ahqwygikrl lrlr
//
LOCUS       WP_010809519             225 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Cupriavidus].
ACCESSION   WP_010809519
VERSION     WP_010809519.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..225
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23398
     Region          <58..183
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mplrrtript hplraqglla qvrlpllcat alllaacass pssrhaglpr tpgkpmidps
       61 agleeisiqa mslvgtpyry ggntpdsgfd csglvryvvs raanvnlprt teamgvrgss
      121 ldrsevasgd lvffnttgra nshvgiyvgq nrfvhapssg gtvrledmgk pywasrynga
      181 rrvvaavnqp papvaapaap plpepapasa plgvdddpia afanq
//
LOCUS       WP_010809527             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Cupriavidus].
ACCESSION   WP_010809527
VERSION     WP_010809527.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..181
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /note="This protein belongs to a clade of uncharacterized
                     proteins related to peroxidases such as the
                     alkylhydroperoxidase AhpD."
                     /calculated_mol_wt=18684
     Region          40..173
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msrvplvnpa tatgdsqall aeihgafgva pnmfravans paalrsmwra fgalgggvlg
       61 aalgekiava vadrnqceyc laahtalgrk agataqemse aqagraqdar taaalsfalk
      121 lvnqrgqvsd advaqlreag fndeqiveil ahvalnlftn yvnvafavpv dfpkiklraa
      181 a
//
LOCUS       WP_010809633             256 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Cupriavidus sp.
            GA3-3].
ACCESSION   WP_010809633
VERSION     WP_010809633.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..256
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27330
     Region          7..250
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msadaniqvt heghvarivl srpphnfvda dimrrladtl qalddnencr aivlasgvsa
       61 fcagadfsga dqgaiandpg gfyahamrly rnrkpivaav egaaigagmg lalvadfrvt
      121 caearfsanf nrlgfhpgfg msltlprlvg eqqaallfyt grritgtdav eigladelve
      181 kaqvnarama laqeiaasap lavestraml regladriae inqrelaiqh gqfrsedfre
      241 gvaamaarra pvfkrr
//
LOCUS       WP_010809639             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavodoxin family protein [Cupriavidus].
ACCESSION   WP_010809639
VERSION     WP_010809639.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..163
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=17012
     Region          <35..155
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mktllivyht mtggtrqmae aaagaarqqp gitvvlktaa eagpddvlga dgylfatpen
       61 laamagmmkd ffdrcyyaal dringrpyat micagsdgqn alrqieriat gwrlnavapg
      121 livcthaqtp erilapkqie agdlarcael geglaaglgl gvf
//
LOCUS       WP_010809657             392 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Cupriavidus].
ACCESSION   WP_010809657
VERSION     WP_010809657.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..392
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41059
     Region          20..377
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 metlsaadas agaqadwlgl aatlgrtfda rapeidasgq fvsanyddlr ahrffaaavp
       61 qelggaglsh qelgavlrel gkycgstala famhthpvat aawrwrnqqa pvegllkrva
      121 geqmvllgsg gsdwlqgsgk atrvdggfrv darkifasga paadlfmtca vhddpesgpt
      181 vlhfalpmks pgvrvlsnwh tlgmrgtgsh dvllegvlvp dtaiaarrpq gvwhpmmhtv
      241 amialpliya vyvgvaeaar dialqlarqr rlsahaveaa grlcneadaa qlaldamfaa
      301 asgqapgavt tnrimcartl aaravlatve aamdlaggag fyrdaglerr frdaqgarfh
      361 plqagaqqey agrmalgqdl dappgevrpa aq
//
LOCUS       WP_010809764             813 aa            linear   BCT 01-JAN-2025
DEFINITION  TonB-dependent receptor [Cupriavidus sp. GA3-3].
ACCESSION   WP_010809764
VERSION     WP_010809764.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..813
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86891
     Region          60..778
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mpanprpapp gqaprdtvac rrrtsrgavt aiamavalma qrpavaqhdt avpnqdsaml
       61 pevlvvaaap lpgigvdsdl vpytvqtvrg ddldrsragn laeylsrnla gvnvndiqgs
      121 pfqtdityrg frassipgvp qglsvyldgi rvnepfgdvv swdmipeaal asvslvssan
      181 payglntlgg alamttrsgl dspgfeadls ygsgarkrad lsggvrsdsg whafaagtlf
      241 qehgwrdqsg grlgnvfaka gyagdtdsvd vsvlhgrstl tgnglvpgfh asangtlpdl
      301 yqanrhavyt ypdqtrnqvt qvavngrhwf ddktsaaala yvrtsrrdtt ngdvnpayea
      361 yaedcedgfa pdgsplgadc gmtraegaal hpavintthm wqqtvgmals maretdrhll
      421 nagltldrsr ltysqyaqpg tftddrgava dpdapnalfs gvggssrmlg lylsdtwslt
      481 pstfltasar wnhvevsntl rnsdgseqpr esftyrrlnp alglsqklgg gvtvfggyaq
      541 nnrvptvlel gcadptrpcr lpaglqadpy lkqvvshsye agvrwhrgkd tevtasfyrv
      601 dnhddilflr apntqlgyfa nfdrtrnqgl dltarqrvgd vtlrlaysyl qatyqaagql
      661 aagertidir pgmrmaglpr htlklgldwq alagltlgad lvavsgtvss gnedglrsdp
      721 qpgappktad whvpgyasln lraaykvnkr feiyarlanv fdrryetygq iandvfpggs
      781 lvrphvapgd aasalfvapg aprsfwlgav frm
//
LOCUS       WP_010809798             273 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phytanoyl-CoA dioxygenase family protein
            [Cupriavidus].
ACCESSION   WP_010809798
VERSION     WP_010809798.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..273
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29162
     Region          23..264
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mtsldpcadl pssvlsadag alprlvqafh angfvilrgf adepacaale avtrehlaaa
       61 vppvefeadl gypgapaard aagggtvrrl rqaygrdevf rrwasapklv avvqallgep
      121 aritlahhnc vmtkhphygs qtgwhrdtry wsfarpelvt vwlalgdede rngvlrvipg
      181 shqaklepgq ldpaefliea hpasqpllda aqplalhrgd vlffdsrlfh aagrnasnav
      241 klsvafayfg asnrpldgtr saefgsvelp aav
//
LOCUS       WP_010809845             310 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Cupriavidus].
ACCESSION   WP_010809845
VERSION     WP_010809845.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..310
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33668
     Region          10..302
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mtrtpsptvy rgvfpvaptv fdaqggldld gqrrcidfmi dagshgicil anfseqfvls
       61 ddernvlmkt vlehvdgrvp vivttthfss rlcaersraa qdagaamvmv mppyhgatir
      121 vpersiyeff atvsdaidip imiqdapvsg ttlsapflar mareignvsy fkievpqaaa
      181 klrelielgg daivgpwdge eaitlmadle agatgamtga gfpdgirqil dawqagdael
      241 aaqryqqwlp linyenrqgw latskvlmqa ggviasdavr hplqpmhpat regllkiarr
      301 ldplvlrwar
//
LOCUS       WP_010809854             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010809854
VERSION     WP_010809854.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..182
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20728
     Region          1..94
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          101..182
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mstqhallis liekpssgyd larrfdrsig yfwhathqqi yrelgrmads gwiaadetea
       61 aegeagggdr knrkkvyrvl pagreelarw vltpgasldq reeilvklra davigplglg
      121 demrrlialh rarletylai errdfstpdm draqqlryal lqrgirfeqd wvawgeellp
      181 ll
//
LOCUS       WP_010809529             156 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Cupriavidus].
ACCESSION   WP_010809529
VERSION     WP_010809529.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Song,F., Zhuang,Z., Finci,L., Dunaway-Mariano,D., Kniewel,R.,
            Buglino,J.A., Solorzano,V., Wu,J. and Lima,C.D.
  TITLE     Structure, function, and mechanism of the phenylacetate pathway hot
            dog-fold thioesterase PaaI
  JOURNAL   J Biol Chem 281 (16), 11028-11038 (2006)
   PUBMED   16464851
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..156
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15958
     Region          38..149
                     /region_name="PaaI_thioesterase"
                     /note="PaaI_thioesterase is a tetrameric acyl-CoA
                     thioesterase with a hot dog fold and one of several
                     proteins responsible for phenylacetic acid (PA)
                     degradation in bacteria. Although orthologs of PaaI exist
                     in archaea and eukaryotes, their function has not...;
                     cd03443"
                     /db_xref="CDD:239527"
     Site            order(68,99,106..109)
                     /site_type="other"
                     /note="CoenzymeA binding site [chemical binding]"
                     /db_xref="CDD:239527"
     Site            order(69,71,74,100..104,106)
                     /site_type="other"
                     /note="subunit interaction site [polypeptide binding]"
                     /db_xref="CDD:239527"
     Site            order(70,78..79,82..83,99)
                     /site_type="active"
                     /note="PHB binding site [active]"
                     /db_xref="CDD:239527"
ORIGIN      
        1 msqalatlpr qhdrhaavdp rmrimvdnvl igspvaralg vrlaslapdh velempflpt
       61 nvthgsivhg gviatlidia gaaaaasggs addvkggats slsiqylapa kgtalravam
      121 vvrrgrrqvv tdvsvyaeap degvlvakal mssamf
//
LOCUS       WP_010809913             250 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Cupriavidus].
ACCESSION   WP_010809913
VERSION     WP_010809913.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..250
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27386
     Region          1..249
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 miaardlfks fgplevlrgv sltlrkgdvt avigpsgsgk stllrclnhl evidrgtlei
       61 egealtaagp dgtaryvpda evrricrkmg mvfqsfnlfp hmtvlqniie apmtvkglar
      121 davvpkaeel lrkvgllakr dsyparlsgg qkqrvaiara lamepdimlf deptsaldpe
      181 ltgevlrtmr qlaeehmtml vvthemgfar evanhvvfmd egrileegsp eevfgtpaha
      241 rtreflahml
//
LOCUS       WP_010809962             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Cupriavidus].
ACCESSION   WP_010809962
VERSION     WP_010809962.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..218
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=23041
     Region          4..144
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
     Region          75..215
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mkgdrqlqqd vtealiwdpa vhgneigvqv qdgvvtltgh lgtfaekysa eaavrripgv
       61 ralaveldvh lpddarrtda diaraaanvl swdatvpadr irilvehgvv tlsgdvdwyy
      121 qrtaaehava glfgvvgvtn alairpradk qdvaariqaa iarqaasdad qvtvtvrdga
      181 vtltgtlrtl aereaafeaa wsapgvsavv nqievrpg
//
LOCUS       WP_010810013             457 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Cupriavidus].
ACCESSION   WP_010810013
VERSION     WP_010810013.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..457
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49755
     Region          38..449
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(51..52,55..56,59,91,141..142,144..146,149,169,
                     172..173,176,281,284..285,288..290,293,321,325,376..377,
                     381,385,401,404..405,408..409,412)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnpnqpaasv paldslggna rldteaqiek rayskvfwrv mpflmlcyvv ayldrvnvgf
       61 aklqmgqdla fsetvfglga glffigyflf evpsnllmhr igariwiari mitwgiisal
      121 flfvktptqf yvmrfllgla eagfypgvil yltywfpanr rgkmialfms gipiagmfgn
      181 plsgwimdaf ngthgmrgwq wmfllealpa lvigvvtvfv lrdgidkapw ldadekrvlk
      241 rnieedqrga hnaasaagka hghslgavfs drrvwwmcli yfcfvtgqya ltfwmptlvk
      301 asgvtgnlni gllsaipfic avivmnilgh sadarrerrw hlivpalmga tgfaiaasft
      361 nnttvaiaal slaaagvltc aplfwslpts flsgiaaasg iavvnsvgnl agfvspymvg
      421 alkdmtqstq lpmyvlsail vvgavlvwlt paklvnr
//
LOCUS       WP_010810031             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Cupriavidus].
ACCESSION   WP_010810031
VERSION     WP_010810031.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..321
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=33060
     Region          46..318
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mnrisslptl gwiaivlagf aaaplwlssg falnllvmvl lmtlmaqswn ilggfggqfs
       61 fghaaffgtg ayamailqva fgmnawlalv latgvgalag vgvgvlsfry glkgsyfsla
      121 tlavaevlri vanavgftga gagmqlplqp galhlqfagk agylwfiltf vaaglllsww
      181 lrrsrfgacl mavrdsedaa kalgidvlrv klvaiamsaa lmaaagvfyt qylqyldphi
      241 aygpafsvaa lvgaviggta tvfgpllgal alqllneltr nalgdvpgvs lviygallvl
      301 mvmflpqgla gaagsvrkar a
//
LOCUS       WP_010810032             290 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Cupriavidus].
ACCESSION   WP_010810032
VERSION     WP_010810032.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..290
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30708
     Region          12..290
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mfdipilwas wlnglttgai yalvalgltl iygvlhivnf ahgaalmaal ygvyflftrl
       61 hvdpyaallv mvpamfaagy llqrhliara srgneqnvll vtlgisivle nlalylfrsd
      121 tytidtpyal stvellgasi alpkviafag allacgllml mirrttlgra iravarekqg
      181 arvvgidver vyalsfgigl aclgaaacfl lpayyvnprv gdgfvliaft vvvlggmgsf
      241 agalwgglli gvveslgglw lgdslgqvgi flifilvllf rpqglfgaka
//
LOCUS       WP_010810037             311 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Cupriavidus].
ACCESSION   WP_010810037
VERSION     WP_010810037.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..311
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33035
     Region          4..216
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 madiilhqya tspfsekvrl llgakglawh aveipailpk pdllaltggy rrtpvlqvga
       61 diycdtalic evldalapap alyppaqaaa arvaaawfda alftasvtyv fqpagvasml
      121 ghlspaqvqa fsadrkamrg dtnalrmplp eatallhetf gqletqfaag ighvagpals
      181 vadfslyhnl wfirragala qlleayprlq awyarmntfg hgrprvidse daigaarsad
      241 plaldegvvv daglqagdav tvtptdyard pvagvllals arrvtlrrqd pragalnvhf
      301 prqgyqvqra a
//
LOCUS       WP_010810076             370 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkene reductase [Cupriavidus].
ACCESSION   WP_010810076
VERSION     WP_010810076.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38559
     Region          5..336
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(24,26,57,99,228,290,310,312..314)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(24,26,57,99,101,108,176,179,181,228,235,290,310,
                     312..313)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(26,101,176,179,181,313)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            181
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msaslfeplq lgdialanri vmapmtrsra gagdlptglh qayyaqraga gliiaegtyp
       61 srhgkgycrt pgiettaqid awrdvsgsvr slgaamvlql mhvgrvatrh nkapdaqtva
      121 psairargti yadghglvgm empralaahe vttvieeyrq aavnalaagf dgvelhcssg
      181 ylpmqfllpc tnqrtdgygg slmarlrfvv etleaiagai gagrvglric pgnpyndmhd
      241 ddpaatysal ldavapigla ylhvsrspdp aldafalarr hfggavivnd gfdgasaara
      301 vsggvgeavs farhfianpd lparlrhgap laafdrtlly tpgahgytdy paaaelaasg
      361 qilpqgglqp
//
LOCUS       WP_010810092             124 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VanZ family protein [Cupriavidus].
ACCESSION   WP_010810092
VERSION     WP_010810092.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..124
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=13338
     Region          12..118
                     /region_name="VanZ"
                     /note="VanZ-like family protein (function unknown)
                     [Function unknown]; COG5652"
                     /db_xref="CDD:444373"
ORIGIN      
        1 mpmiavptlt plrwrllfwg caaavlalsl mpptqplptt gwdkanhmla favlgvlgrr
       61 aysgrgwavl lglvaygali ellqgqtgyr eadwldllad svglaagmal dwlvrrlssp
      121 rlra
//
LOCUS       WP_010810155             322 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: 3-hydroxyacyl-CoA dehydrogenase family protein
            [Cupriavidus].
ACCESSION   WP_010810155
VERSION     WP_010810155.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..322
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=34162
     Region          17..290
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mpnptapvil srpgaahavv vgggtmgadv avvltralcr ttvvepdagr agampgrvrg
       61 nlaaigreqg aerlavaatl davdwstvdl viecipeqld lkqalfaelv rrarpdtvla
      121 snsssfpisa igagldsrar mlglhffmpa hlvplvevvm gddsdeacad aliafmrrca
      181 mvpvkvrkdl pgflanrlqh alsreafsli drgiaspedv daavrfgfgf rflaagpvlq
      241 rdhagidvha aagatmyptf cnddhparcl seraadgrhg mkrgegfyqw tpetiaaera
      301 rydsllragl aliapelpei ep
//
LOCUS       WP_010810176             201 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Cupriavidus sp. GA3-3].
ACCESSION   WP_010810176
VERSION     WP_010810176.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22041
     Region          1..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mqkgqltrna iveqaldtaa kvgfeqlsla tlaadtnmsk sglyahfksk emlqqavldl
       61 averfgeivi rpamrqprgm prlqglfegy lewlggtvtq grclftalgq eyrdrpgsir
      121 dlvvqslkdw hstvarvvad aideghfgpd tdprqfafel sgigmafqqs fkllgrddae
      181 tmarrafaal vtraaegara h
//
LOCUS       WP_010810231             303 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010810231
VERSION     WP_010810231.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33153
     Region          1..>181
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          93..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     236..237,239..240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mhlkhlkhll mvadmasfsq aaqrlhltqs alsrsiqtle delggrlidr hgkrnvltpl
       61 geltanrarr ivfeeaelhr svelfhhhhl gairvglgag pgavlatpfl rymarhhpgi
      121 qvsvslgtsd almiqlrqrs ldavivevss vapatdlrhe llnalqgrfi crtghplvqq
      181 aaggdavsfd dvmryplasa plstevarnl vkrfgpradp ehclslrcen vrslveavld
      241 sdailfsiva avraeiaagk lcelvttpav ddgpryafft lagrteapsm eifrkftdeh
      301 lrd
//
LOCUS       WP_010810237             222 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010810237
VERSION     WP_010810237.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..222
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24865
     Region          1..217
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtsstdvrnl aervteqirq rivhgefapg qrlseaalse slqisrntlr etfrvltkeg
       61 llkhepnrgv svaipsiaai idiyrvrrmi ecqaiaqayp shparkhlre avemglrcrd
      121 sgdwqgagta nmefhmaive ladserlnvm fahllaelrl afgmlqdpef lhgpyvelnq
      181 hilqlfeagk laecaaalnd ylvqserivl svcarhpifk gr
//
LOCUS       WP_010810242             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010810242
VERSION     WP_010810242.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33994
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..287
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mlsedelall eaireagsls raaarlgkap stvshaarql eqrfdallfd rrgyrlqltr
       61 agellteeaa rlaqdvarvt qrvrqvangw edrlwivtde lmefetlmpv mhafdaqesg
      121 valrvthevl agtwealrdg radlvigatn eppaipnlgw felgviewvf avsprhplaa
      181 arepltreei arhravvvad ssrltggray gmvggqrlla vpsvraktla qrdglgigwl
      241 prhrvgsllq rgeliekrta dprepnllyv gwrgdhegra lqwwleqlrr prlarllvrg
      301 vdaya
//
LOCUS       WP_010810251             319 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010810251
VERSION     WP_010810251.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..319
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34828
     Region          3..313
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mnqiglvlfp gfqmldlaav svfemanlev rvpayeihvv serggavkss mgtaiqttam
       61 dplafdtlmv ggatsvpaps prllrllgha leptrrmasi ctgafilaea gildgrratt
      121 hwhhastlrq rfpavrvedd rifvrdgtvw tsagmtacid lalalveqdl gtdvsravak
      181 klvvhhrrag gqsqfsmlse lesrseriqa altyarnhlh qdlsvellas aanmsprhfs
      241 refrqstgqs paraverlra dtarllveag tltieriask tgfsdpermr raflrifgep
      301 pqslkraara rrseepaav
//
LOCUS       WP_010810265             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010810265
VERSION     WP_010810265.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..316
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34604
     Region          2..310
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhhvalalyp gfqalnlavs tvlefanrsl geplykvhll sehggpvlss ggfsvgtepf
       61 gkrrfdtvlv vgdndvlptp palvkflqra artsrrigat ctgafnlaea gvldgrratt
      121 hwyyaeqlrr rfpnvgveed rifiidgpvw tsagmsacid lalalvekda gaavardvak
      181 llvvyhrrag gqsqfsalld leprsdrira aldfarqnlq qelsveqlad aahlsprqfa
      241 rafrdetgqt pakavehlrv eaarlmmegg rhaidvvard tgfgdrermr raflrafgqp
      301 pqairrmarg delqta
//
LOCUS       WP_010810304             477 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Cupriavidus sp. GA3-3].
ACCESSION   WP_010810304
VERSION     WP_010810304.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..477
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50399
     Region          1..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mslvlklkdl lgpdavltep advaayiedw rgrykgpalc vvlpastaqv aavvqaavqa
       61 svpvlpqggn tslcggavpa pdgtppivis larmrrirai daannsmeve agcvlaaiqq
      121 aaaeqgrlyp vslgaegscq iggniatnag gtgvlrygnt rdnvlglevv lpdgqvwngl
      181 yrlrknntgl dlkhlfigse gtlgvitaat lklhplptah tmawlavstp qaalemlgrf
      241 qqrcgatlsa femlndvqlq ivldhvpgrr aplpashpwh vlveladtgr relldevlqe
      301 vleqgvaegl vddavvaasg aqreamwqvr hsvsegnkka glglntdcav pvsavpqfie
      361 rataaahavl pdlpiivvah lgdgnvhfip lvpfpqwqal perdavaari khaidqvaye
      421 lggtfsaehg igqvlteema qfkpaveiam mhgikrmldp rdlfnpgrll pppssqq
//
LOCUS       WP_010810327             274 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010810327
VERSION     WP_010810327.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..274
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29568
     Region          28..271
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mkqnvqfpfq nrtaaedgav eddarslrvl mvlsslaraq hpqtlsqlsq rlhvpkatlm
       61 rllaamertg fvvrmpaerg yvpgpgaasl alqtlrsppm lrecrailar lvaslgetcn
      121 ltaldgdrvl yvervethep lrlqlspgih vplhctasgk lflsamnrle rqqmlrrldl
      181 aphtprtlsd vpglnteldr lgargigvdh eefvrgmcav avpvrepdge gsgrvvaaia
      241 chaptarasl eallqavptl qgaaremaav lcah
//
LOCUS       WP_010810346             338 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [Cupriavidus].
ACCESSION   WP_010810346
VERSION     WP_010810346.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..338
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36638
     Region          39..322
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msqdnnnhad prrrsvlrla gaaaiaapsl ilgrqawsap rkltfawnqn afcltpivva
       61 qekgffekng lqvdlinysg stdqllesia tgkadaavgm ihrwlkplea gfdvkiigss
      121 hggcvrlvgs kaagvtslqq lkgktvgvsd laapgkhfft illakngidp dkditwrqyp
      181 adllgvavdk geiqaiadgd pnlyllekrt ngayvelatn ltgeyarkvc cvvgargelv
      241 rndrpaatsl araivqatdy vnenpneaar vfaryspkin pedlrklyat ltythhptgv
      301 dlrdeiafya ddfrrigvlk kttdakrlaq hvyanvlg
//
LOCUS       WP_010810482             217 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Cupriavidus].
ACCESSION   WP_010810482
VERSION     WP_010810482.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24279
     Region          29..182
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msqtdtgapp etgatrepgh aggicppkta rgqktreall raaekvfgek gyyaasisei
       61 tqeakvamgt fylyfkdked ifralvahml elvrahlrkh vaaaatqmea erlglkafls
      121 fvsrhknlyr ivldsysvde tiyssyfqvf aelysrrltr aeeqgeivpg daevrawcli
      181 gisnflgmry arwkrppsme kvvdtafdli shglqpr
//
LOCUS       WP_010810487             341 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Cupriavidus].
ACCESSION   WP_010810487
VERSION     WP_010810487.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..341
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35973
     Region          43..341
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mttsttlpaa apsdlpkvrl dwtplalapl lmllayplvg spstwltlti aglamgmiif
       61 vvssgltlvf glmdvlnfgh gafialgayv aasvllpmag wveadslaqn lavfalaiaa
      121 amvaagavgl ffervvvrpv ygqhlkqili tmggmivaeq likaiwgpet ialqvpttfr
      181 gavllgdaai ekyrliamal glvifiamll llnrtrigll iragvenrem vealgyrvrr
      241 lfigvfvaga alaglggvlw glyqqnitaa igaqvnvlif iviiigglgs ttgcfvgall
      301 vglmanytgf lfpkvalfsn illmmlvllw rpqglfpvar r
//
LOCUS       WP_010810528             208 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cysteine hydrolase family protein [Cupriavidus].
ACCESSION   WP_010810528
VERSION     WP_010810528.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..208
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22124
     Region          13..183
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mtgpaytses tglllvdpyn dflseggkln glakpvadkl gtlanlravt saarsrgiqv
       61 fyvphhrarp dehlgwqhas pyqlgasraq vfaegtwggd whpdfrpmag dvivhehwgg
      121 sgfantdldf qlkqhgirqv vlvgllantc ieatgrfaae lgyhvtlvrd ataafspeal
      181 haaheingpt fahailttaa llsalgar
//
LOCUS       WP_010810573             305 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010810573
VERSION     WP_010810573.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33799
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdrfdalqlf trivelgsft gaasaldmpr atathaikel earvgarlle rttrqvrptl
       61 dgqafyersk rvlqdledae tslstqvanp rgtlrldlhg thatmiilpr igefrerylh
      121 idlivssgdr lvdlvgegid cvvragqprd sslvarrlae mpevlcaspa ylaahgkpeh
      181 pselaqhigv gffsrnhdrr ypftltvdge vqefkargwi svsdaecyts aalagcgliq
      241 vprfrveehl ragrlvpvle awpcpdlpvs alypfhrqla prvrvfvdwv aglyverfgp
      301 lrgaa
//
LOCUS       WP_010810565             164 aa            linear   BCT 01-JAN-2025
DEFINITION  arsenate reductase ArsC [Cupriavidus sp. GA3-3].
ACCESSION   WP_010810565
VERSION     WP_010810565.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..164
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=17494
     Region          4..143
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(9,11..16,112,114)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mttnvlilct hnsarsvlse gmlnhwaskl gkdvrafsag sapsgrlnpf alealtsagv
       61 dvsgyrsksw defvgdnape mrivitvcds aaaeqcpywp gspvkvhwgy adpsnalggd
      121 egkrlvfelt reaigyrmlq llalplegms naqlqdalna iakn
//
LOCUS       WP_010810597             136 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Zn-ribbon domain-containing OB-fold protein
            [Cupriavidus].
ACCESSION   WP_010810597
VERSION     WP_010810597.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..136
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15001
     Region          18..133
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mseaqrplpr pteitegywh aaaqgrlvvq gcsacghrqf yprtlclace sdqvdwtevc
       61 gfgsiytfti nhrapnafmk arlpyavaiv eldegvrmma nilnaspeai aigkrvrvvf
      121 ekasddvslp qfelid
//
LOCUS       WP_010810622             135 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Cupriavidus].
ACCESSION   WP_010810622
VERSION     WP_010810622.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..135
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15053
     Region          5..124
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mellinidvd dlprgidfya qglglrlnrk lfdgtvaeml ggntpiylla kpagtrpttr
       61 adtrrdyrrh wtpvhldfvv anleqaiera leagaeiedw pqdfdwgrqa rlsdpfghgl
      121 cfiewkgqgy gavag
//
LOCUS       WP_010810743             310 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Cupriavidus sp. GA3-3].
ACCESSION   WP_010810743
VERSION     WP_010810743.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34541
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,147,163,165,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,192,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mktiewkdwe ifcrvveggg ftqgaelaev pkssasaava rlesqlgirl ferttrrvrv
       61 tergqrlyer vaplfaelhe isaeatsdsa evsgllrist pyevgsqhls esltrvlrah
      121 pglrvqvdvs wdqpdlirhg ydlafvmtdt alhdtsfask rvvlverafy aapaliktrg
      181 lprtpqdlqg wptlgnaddr hweflrdgve iarldvepri cthnaelrlk aaldglgvtr
      241 lsprfvqdav gqgqlvrvlp gyassplkvy vlmparklmp asvrvlldml eqtlgvpear
      301 rpygkrrena
//
LOCUS       WP_010810760             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010810760
VERSION     WP_010810760.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..272
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29069
     Region          57..253
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mattskkaap gaaaktprrp askatlktap kaaanaapee sagpeaaase asateaiyls
       61 lltaimehrl lagtklveer lcevtgasra rirqvfarla heklvtlvpn rgafvssptv
      121 dearevfqar rvvepalaae laqratpakv rslrrhamee dnarargdra amirlsgefh
      181 illaemagna ilekliremv sltcliitly drpgapacae hehrqlidai eqrdaarasa
      241 lmaehlehie gsldlsvpds gapdfysifs kg
//
LOCUS       WP_010810796             410 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Cupriavidus sp. GA3-3].
ACCESSION   WP_010810796
VERSION     WP_010810796.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..410
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=45310
     Region          13..343
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mktettdvvi igagpagsva agllrkhgip vlvieketfp rfsigesllp qsmayieeag
       61 mlravveagf qykngaafsr gtqqtafdfr ekfspgwgtt yqvqrarfdd vlireaarqg
      121 aevrfshlve dvdvsgtqpe vtvrapdgsq ykvrarflld asgfgrilpr llqletpsgf
      181 pvrsaifthv edriptgtfd rnkilisvhp qhqnvwywti pfsdghcsqg vvaekafldr
      241 ytgseterlq alvaeepgla kllanaqwdt parqiagysa nvkslwgngy allgnagefl
      301 dpvfssgvti afksaslaaq clvrqlagea vdweqdfarp lkagvdcfrv fveawyegrf
      361 qtlifhpnat seiremisai lagyawdrdn pfvaeprrrl avleefcnvr
//
LOCUS       WP_010810805             301 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Cupriavidus sp. GA3-3].
ACCESSION   WP_010810805
VERSION     WP_010810805.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32974
     Region          1..>143
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtiramqvf vravelgsls avarelqstq ptiskvvaal ekemgvrlle rsttslspte
       61 agrrfherar rvldeygeav sdargmsrqp agrvrvsapa sfgvlrlnal vlafqqrype
      121 vevellfddr fvdlveegvd iavrlgaslp pnvvarriav sprllvaspd ylarharirq
      181 padlarhqil rftwlaagde ivldgpggqa pvsascryrv nnslamresf lagagfgmtp
      241 awlvqdllds galqrvlprw sgpaqeaflv ypsrryqper vrllldylaq aiaglpgltp
      301 v
//
LOCUS       WP_010810807             217 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Cupriavidus].
ACCESSION   WP_010810807
VERSION     WP_010810807.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..217
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24747
     Region          1..205
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 melyahpfss ycqkvlvaly enaipfefrm lspehaqnmd elarlwplrr mpvlvdgsrt
       61 vfessiiidy ldqhhrgpvr wlpdspdaal evrmldrffd qyvmtpmqri vadylrpaeh
      121 rdaygvaear klldsayawl eptlagrewa aggaftladc aaapslfyad wvhpipdarg
      181 nvrayrnrll arpsfaravd earpyrplfp pgapdrd
//
LOCUS       WP_010810971             459 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Cupriavidus].
ACCESSION   WP_010810971
VERSION     WP_010810971.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49671
     Region          2..452
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 msasaehlqr glgerhirlm algsaigvgl flgagnaikm agpaimlgyl iggaviflim
       61 ralgemavhn pvagsfcrya qdhmgplagy ltgwnywflw lvtcvaeita vaiymgmwfp
      121 dvprwiwala alaamgsvnl mavkaygefe fwfamikivt ivlmliggga mivfgfgngg
      181 iatgisnlwa hggfmpngas gvlmslqmvm faylgvemig ltagearnpk ksipdainsv
      241 fwrilifyvg alfvilslyp wneigaqgsp fvltferlgi ktaagiinfv vltaalsscn
      301 ggifstgrml ynlaqqgqap qafakvdrng vprrallvsi aallcgvlln ylvpeqvfvw
      361 vtaistfgav wtwaiilvtq iqfrrslsaa erkalafrmp fwpygsyial aflalvvalm
      421 ayfpetrval yvgpgwlvll tvcyyaldmr srgpvsyra
//
LOCUS       WP_010810972             369 aa            linear   BCT 01-JAN-2025
DEFINITION  alkene reductase [Cupriavidus sp. GA3-3].
ACCESSION   WP_010810972
VERSION     WP_010810972.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..369
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39391
     Region          3..346
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,55,97,232,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,55,97,99,106,179,182,184,232,239,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,99,179,182,184,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            184
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msplfkpfam aeqtlsnria mapltrsrnp dgvpndlnal yygqradagl ivtegtvisp
       61 saqgflfnpg lytpqqvegw rkvtdavhak rgtiftqlwh vgrvshvsiq pggiqpvsat
      121 dqvakntkaw gytangtpga vdvsaprala sgevygviad faeaaanaia agfdgvelhg
      181 angylieqfl nptvndrtde frgdtlegrt rfvlaaidav aarigahrta irlspygglg
      241 dmaeypeleq tylhladels krniayvhlm dqstrgssat pgdflarfrr rftgalilag
      301 gmtraraeql iaddlidiaa fgepfianpd lvarlennwp lassdrahhy gggaegytdy
      361 paydgaaaa
//
LOCUS       WP_010811035             339 aa            linear   BCT 01-JAN-2025
DEFINITION  TerC family protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010811035
VERSION     WP_010811035.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..339
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=37824
     Region          9..314
                     /region_name="R_switched_Alx"
                     /note="integral membrane protein, TerC family; TIGR03718"
                     /db_xref="CDD:274743"
ORIGIN      
        1 mdtfatapmw agflvlvlgt lvvdvfvlgg rhahrvstre algwtlawst lavlfgialw
       61 wllagsagre tadrkvlefy tgylielsls vdnmfvfami fgyfavppel qrrvllfgvv
      121 gaivmravmi llgvwlisef swilyvfgvf llftgikmlf vsrrapdlsr npivrflcah
      181 mritadyhge hffvrvdglr hatpmflvvl lveatdlvfa vdsipaifav ttdpfivfts
      241 nifaimglra lyfllanlaq hfhylkygla ivlsfigakm laepwfhvpv hwslgavamt
      301 lfvsvlvsra rarrtlahag delgghcapr erragnrrt
//
LOCUS       WP_010811088             228 aa            linear   BCT 01-JAN-2025
DEFINITION  chemotaxis protein CheW [Cupriavidus sp. GA3-3].
ACCESSION   WP_010811088
VERSION     WP_010811088.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..228
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=23726
     Region          79..228
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 maeppgillr tenvddcwrr igvrgdgscp alaehahcrn cptyaraaam lldaqrldvm
       61 pealpdaatf tdddgalpae rgtaqaclvf rigdewlalp taalseitap cpihslphrr
      121 daavlglaav rgnllaclsl arlfdagage sasgsrflil gqgraaialp vaevsgiarv
      181 pqpalqplpa tlarasaryt qalfldqgrs vglldaalvr qalarsla
//
LOCUS       WP_010811116             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Cupriavidus].
ACCESSION   WP_010811116
VERSION     WP_010811116.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..316
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35644
     Region          1..298
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkrfaligaa gyiaprhmta irdtgnqlvs aydindsvgi idsispqsef fteferfydh
       61 awrlrrqpga aldyvaicsp nylhqshisa glrlgcdvic ekplvptpel ldelalvere
      121 tgrrvfnilq lrhhqaildl kdkvgrerng hkheveltyi tsrgkwymes wkgdtrksfg
      181 latnigvhfy dmlhfifgrv qhnvvhhstd nkaagyleye narvrwflsv dagdlpaavk
      241 grkptyrsit vdgaeiefse gftdlhtvsy revlagrgyg lddarhciet vnairsarpa
      301 aprdgeahpf lqqlla
//
LOCUS       WP_010811131             205 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar transferase [Cupriavidus].
ACCESSION   WP_010811131
VERSION     WP_010811131.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..205
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22748
     Region          <27..181
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mkrifdilla vlailllaip llflmgavrl rlgkpvffrq vrpglhgepf hivkfrtmtd
       61 acgpdgellp dperltgfga llratsldel pelwnvvkgd mslvgprpll meylplytpe
      121 qarrhlvrpg itglaqisgr naisweekfr ldvwyvdhvs vwldmvilwk tvtkvvareg
      181 isaagefsap rfkgskpsap dvdaa
//
LOCUS       WP_010811213            1045 aa            linear   BCT 01-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Cupriavidus sp. GA3-3].
ACCESSION   WP_010811213
VERSION     WP_010811213.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..1045
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113536
     Region          5..1014
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msgfnlsala vreravtlfl iilisvagfv affqlgraed ppftvksmif itawpgataq
       61 emqdqvaekl ekrmqelryy drtetytrpg lafttvtlld stppkevpee fyqarkklgd
      121 earslpagvi gplindeysd vtfglfalka rgepqrllvr eaetirqrll hvagvkkvni
      181 igeqaeriyl sfshdrlatl gvtpqdifaa lnsqnvltpa gsidtdgpqv fvrldgafdk
      241 lqrirdtpvv ahgrtlklsd iatvergyqd patfvvrnkg epalllgivm rdgwngldlg
      301 ksleaevakv naelplgmel skvtdqavni ksaveefmvk ffaalivvlv vsfvsmgwrv
      361 givvaaavpl tlaavfvvma atgksfdrit lgslilalgl lvddaiiaie mmvvkmeegy
      421 griaasayaw shtaapmlsg tlvtavgfmp ngfakssage ytgnqfwivg ialiaswiva
      481 vvftpylgvk llpemtkveg ghgaiyatpn yqrfrgllgr vigrkwlvaa ivvglfatsv
      541 vgmgavrkqf fptsdrpevl vevqmpygts ieqtsaaaek veawldkqpe akivtsyigq
      601 gaprfylams pelpdpsfak ivvrtdnqee rdvlkgrlrq aiaeglspga rvrvtqlvfg
      661 pyspfpvafr vmgpdpdklr aiaeqvegvm dasplmrtvn tdwgprvpgl hftlqqdrlq
      721 avgltshdva qqleflltgv pvtevredir svqvvaraag dirldperia gftligangg
      781 rvplsqvgtv dvrmedpilr rrdrtptitv rgdiadnqqp pdvskailaq lqpviqklps
      841 gyriemagsi eesgkankal aplfpimlai tlliimfqvr smagmvmvil tsplgligvv
      901 ptlllfhqpf ginalvglva lsgilmrntl iligqiqgnl keglspydav veatvqrarp
      961 vlltavaail afiplthsvf wgtlaytlig gtlagtlltl vflpamyaiw frirppaqva
     1021 vhdrnaalpr sqkklrvvdd qnscr
//
LOCUS       WP_010811289             555 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [Cupriavidus].
ACCESSION   WP_010811289
VERSION     WP_010811289.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..555
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60067
     Region          1..536
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 metfdyiivg agsagcvlan rltqdadvsv llleaggkdd yhwihipvgy lycignprtd
       61 wlyrteaeag lngrslgypr grvlggcssi ngmiymrgqr edydewarlt gdagwrwdnv
      121 lplfkrsedh hrgpsefhga ggewrvegqr lrwdilerfa daaeeagipr tedfnrgdnf
      181 gvgyfevnqr rgirwntaka flrraserpn ltivtgaqvs gltfdgrrct gvnyigggrp
      241 htvaatqevi laagavntpq llelsgigqa erlqalgipv rhalagvgen lqdhlqlrsv
      301 vkvsgvrtln traaslwgkf cigvqyafnq sgpmsmapsq lgafarsdpa qarpnveyhv
      361 qplsldkfgd plhafnafta sacnlrptsr gsvhvgsadf rqapviapny latdedrkva
      421 adsirltrri vaspalapfq peewlpgpaf qtdeqlaeaa gnigttifhp vgtckmgrad
      481 dpmavvdhrl rvlgidglrv vdasvmplit sgntnsptim iaerasdlir edrrqglaaa
      541 evlvqpapaa aaaga
//
LOCUS       WP_010811303             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Cupriavidus].
ACCESSION   WP_010811303
VERSION     WP_010811303.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..161
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17552
     Region          8..146
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtasgvsldp fdlallavlq adgrtthqql aervhlspsq vgrrlarlea dgvitgyrvn
       61 lssqalglgv mvfisvklah hadtiierfr eeillleevq ecysvagead ylirvvvpdl
      121 ptlaeftmkr lmrvpgvesv rsnivltaik cdgplplshl r
//
LOCUS       WP_010811316             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Cupriavidus].
ACCESSION   WP_010811316
VERSION     WP_010811316.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..206
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21716
     Region          2..206
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mfdiqnytsf vlailvfqli pgpgtiailn atarngmaag mgavcgtllg dlvymlaava
       61 glaavmqanp llfhglqwfg aaylcwmgvq llrtrfaada gvpeprkstr vylrqgftvs
      121 ltnpkvvlff vaffplflrp daspatlaam mahvtvlsla yqaalvlagn avasrlralp
      181 fartlatrla gialvgfglr laasnr
//
LOCUS       WP_010811415             264 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Cupriavidus sp. GA3-3].
ACCESSION   WP_010811415
VERSION     WP_010811415.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..264
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28261
     Region          21..261
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mlnavdnpta vkpttptpae paqpaggadr vlfvlaalaq hgapitvrel vaktglpkst
       61 lyrqlmmlkr wgfvlesdge yapgpislql algfdmashl arealpdmql laqqsdesvg
      121 lvvavkdhvv clemvesrqs lrcsfekgrg vplragasak sllafmrdea rerlvraqce
      181 pgeaerllae laviretgya vsegevdpgv wgvsaplfsr rskadalgsi tlmvpatrrq
      241 gresalidmt vaaamrisar lqsy
//
LOCUS       WP_010811346             504 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tripartite tricarboxylate transporter permease
            [Cupriavidus].
ACCESSION   WP_010811346
VERSION     WP_010811346.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..504
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=52980
     Region          1..493
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mdtlnqlmhg favaitpinl mwalvgcflg taigvlpgig paltvamllp ltakveptaa
       61 limfagiyyg amyggsttsi lmntpgesst mvtamegnlm akngragpal ataaigsfva
      121 gtiatvmlsm fapvaadval qfgpgeyfmi mllafttvsa vlgssllrgm talflglgig
      181 ligmdslsgq trysmnvqel ydgidivvva vglfavgeal fnaffpqpag tfnklssvhm
      241 nksdwkrsip awirgtfigf pfglipagga eiptflsyat ekklsdhked fgkvgaiegv
      301 agpeaannaa vtatlapllt lgiptsntta illaafqnyn lqpgpmlfqt sgdlvwglla
      361 slyignvmll vlnlpaiglw vrmlrvptpl lyggilifag lgaygirqsw fdllllfvvg
      421 llgmvmrrfd fptapvivgm ilgpmaekql rnalsigqgd wtlflrqpis atilaltvav
      481 vviprllrwh atrtsahaqa dnaa
//
LOCUS       WP_010811472             145 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Cupriavidus].
ACCESSION   WP_010811472
VERSION     WP_010811472.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..145
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15322
     Region          12..143
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtteqerlll rdtieagfrq aafvndvgit ladcgpgwce stlaiaprhl qhggivhagv
       61 qatiadhtag aaastileag qhvvtaefki nllravrser lrcradvlks grsiivvead
      121 vfadvhgesv lvsrlnatms vldla
//
LOCUS       WP_010811612             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Cupriavidus].
ACCESSION   WP_010811612
VERSION     WP_010811612.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..163
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17610
     Region          3..158
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mqsknticlw ydrdaldaan fyaetfpdsa vsavhrapgd ypdgkqgdvl tveftvagip
       61 clglnggphf khneafsfqi atddqaetdr lwnaivgngg qesecgwckd rwglswqitp
      121 ralsaaitdp draaakrafd ammtmkkidi aaieaarqgk sps
//
LOCUS       WP_010811616             154 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010811616
VERSION     WP_010811616.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..154
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16501
     Region          1..154
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mpdhqisvng ksvevrsdgc tpllwvlrce lkltgtkfgc gvgvcgacav hvngkmvlsc
       61 qhqasemegk kivtieglvg peasalraaw lkhevvqcgy cqsaqllaas allkrtrnpk
      121 eteiadqmsc vicrcgtytr irraiaeave mlrg
//
LOCUS       WP_010811657             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Cupriavidus].
ACCESSION   WP_010811657
VERSION     WP_010811657.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..228
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25021
     Region          28..186
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msatqsgfta nasfpridtp silqpprqrr areteqallg agrellasrd faavsvaqia
       61 aacqvsvgaf ygrfrdkmay fealralvme etaasteryl aqerwedvpt pvllekatrf
      121 mvlgtlanrg viraslrhas trpeewvphr qsgeaiverm vqllvprlam padtaevrvr
      181 famqavfsvl vnavlndsgp lhlddeqmip elnrlmagyl gvpcaepa
//
LOCUS       WP_010811675             763 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Cupriavidus sp. GA3-3].
ACCESSION   WP_010811675
VERSION     WP_010811675.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..763
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81058
     Region          5..754
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mskaivgsst pqvtarekvm graqyagdik lpgmlhakvl rsphphariv ridtsaakal
       61 pgvklvvtgh dvparnwgph rkeqrilacg vvrhvgeeva avvavseeia rdaldlvrie
      121 yealpalltp eaaladgape ihagtrnigh emhivrgdvd aafeacaavh eatydmhsqy
      181 pgylepmasv aaqdgngrlt lwastqsvfl ararlaeald rpvstirvvq attgggfgak
      241 iveennslic aflasrlerp vrlvnnrled fqgarasvpm kvwlrmglsa dgvilakdvr
      301 itaecgaysg lagdvmhvta mrsdnmhrvq nvrshavmay tnnpprgafr gfggqqmqfp
      361 lnchltvlag mlgmdpvevh krnaigaget svhgwkisst gmaecldmtr kaigwdekra
      421 aprgtgtrrr gvgiaaamhv sgnrtlgnwd gstillkine dgramlqtse cdmgqgantm
      481 lsqicaqelg iplshvtvma pdtdtapfcl gslasrvtii agnallraar earqkllala
      541 aeklgvdaeq laiadgriaa pgqpdksatl aeiarlhifr hggegihvra tydaptvmhd
      601 adyygnvapa hsfaaqavev evdtstgqvt vidsfvaddc gkainplavh gqthgatvqa
      661 igwtlyenlq yedgrlmngn fadytmptad avpmlrtdvv esndpngpyg akgasetail
      721 pgaaaianav fdavgvriqs lpitpekvla glrelkqkea vha
//
LOCUS       WP_010811717             420 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YeaH/YhbH family protein [Cupriavidus].
ACCESSION   WP_010811717
VERSION     WP_010811717.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11148708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..420
                     /product="YeaH/YhbH family protein"
                     /calculated_mol_wt=48097
     Region          13..418
                     /region_name="DUF444"
                     /note="Protein of unknown function (DUF444); pfam04285"
                     /db_xref="CDD:427839"
     Site            order(253,316,343)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238742"
ORIGIN      
        1 matvidrren ggnksavnqq rfikryreqi rqavakavsg rkimdieqsg qvsipvkdis
       61 epifhhgpgg rrewihpgnk kfvkgdsfdr qqqggggtgs rasdsgeged dfvftlsred
      121 flnfffedma lpdlakrhla kiaevrkvra gfsidgtpsn lsilrtmrss lgrrialssp
      181 yqkrlrelel dysealekdg pyaegtlelm ekmrhlraci drvpfiekld lrynnrvlkk
      241 rpqaqavmfc lmdvsgsmde srkdlakrff mllylflkrn yeridvvfir hhtvakevde
      301 edffhsresg gtvvssalkl mvevihdryp psqwniycaq asdgdnwagd selcgrllrd
      361 silplvqyya yvevaseepq nlweeyltvk gqfdhfamqr iigadeiypv lhdlfqkraa
//
LOCUS       WP_010811720             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Cupriavidus].
ACCESSION   WP_010811720
VERSION     WP_010811720.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..259
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28114
     Region          4..252
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 metirfaved giatltldsp arknalslpm rdeigevirr vraddsvral iltaagtdfs
       61 sggdissmqv einaeqgrkr lhkvhgwled liqldvpvia avdgaaygag fslaltadii
      121 latprarfgl pflrmglvpd cgvfytlprm iglqrakalm fsmrelnaqa aqdlgivmei
      181 vpadslqera rtlaqaftea spvavgltkq alnaslnqdl htmlameadg qgiafstayr
      241 reaadrfmak qplryrwpd
//
LOCUS       WP_010811729             231 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Cupriavidus].
ACCESSION   WP_010811729
VERSION     WP_010811729.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..231
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25867
     Region          14..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 medvtsprrv pagakaeqri rdilrvsrev faelgyertt tteiaqrlgi segtvftyfh
       61 gkrelcarvi edwydeiist veqgmphgqs tkvqlefyvr thlrlfliqg tglcalvlse
      121 grakgpglge vfvplqrryt aplmdllara rdngeirddl plsllrsail gpmehilwda
      181 iarqrqvdie ktardmvall wpallpvdve veklrafyge vgaalrragn g
//
LOCUS       WP_010811802             268 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Cupriavidus].
ACCESSION   WP_010811802
VERSION     WP_010811802.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..268
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28128
     Region          4..248
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mgeiraetrn airilticne rirnafdeam svallaafde aeadprirvv vvtgagdlaf
       61 ssghdlkela sgaharstvg eapfvrpltm kkpvlaaing hcwaagfmla lscdlriasn
      121 navfgspgar lgilpeggql yrlpqliapt ralemmltat pmsaydaasc dlvsrlvpng
      181 galaeaiala eviasrspav vqavksgfnl glregsvrae ryeaetahil hqgddaregi
      241 aaflekrapr fadqpalanp lsaehpga
//
LOCUS       WP_010811826             589 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease subunit [Cupriavidus sp. GA3-3].
ACCESSION   WP_010811826
VERSION     WP_010811826.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 589)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 589)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 589)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..589
                     /product="ABC transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62630
     Region          4..281
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
     Region          336..586
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mssaatfrgr wtgpalvapt lifllatvfv pvvlllsasl lgndgfssts ftrlvrtpvy
       61 tqvliqslyl saaaatiavi agfpvaaait ratpgwrqwl wlgvllpfwt sflvrtiawi
      121 vilgrtgvvn sslvnmgvis epmellytnf svvvglvhvl lplailtmlp vfesidrrll
      181 saahtlgaqp gvtfftvylp lsapgvtaaw lstfisalgf fitpallgsp kqtmmaqlii
      241 qqvqemldwg laaalavvtl latliiywly dklvglstmt gdtsntkagn rsgtgfirna
      301 afsacwvagk avdrfigpav srrpkadgaq gisrpiavgi ivalslpvll lipesfttsa
      361 fidwppqgft lhwyeeifas plwtsaiqrs lgvavgtail asvigipaaf afaqqklplr
      421 slvlgailap milpriival glfyvlsrig wlgsslalvi ghtalavpyv vitvsaalrs
      481 ydrrldaaas isgantltrl rlitlpiiap gilsafifaf vtsfddltla lfvsggmftt
      541 lpkqmwddal lkvsptlaav svllfaailm vmaisyllrr ksaklasaa
//
LOCUS       WP_010811902             425 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Cupriavidus sp.
            GA3-3].
ACCESSION   WP_010811902
VERSION     WP_010811902.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 425)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..425
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=44458
     Region          24..310
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 milaqkivva agvavlaalp vllspslvna siqmliavlf avafnllsgq ggmlsfghaa
       61 yfgigsfatv hamsalggng llptpllpla gaamgllagv aagwfatkrs gvyfsmitla
      121 laellhalap hlkgwfggea gistmrmpaw gltfgdsnqv yyltlawvll slallylytl
      181 tpvgrltlgl renanrlrfl gydvhrlgvl vfavsamfsg iagalqainm eaanyvvfda
      241 qasaavvlns yiggvkvflg palgaaamtf fgyavsdltr swllyqgivf vlvmlfmpag
      301 lagliqalag hlrahglrrm lpvslaflls tlllaggivf tvemlqrffs qdyrsialas
      361 gwppialfgr ewdplspltw lvpalvtgag vaiarlagaa wlrlkdaapa rpgahatana
      421 hrnpa
//
LOCUS       WP_010811923             504 aa            linear   BCT 01-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010811923
VERSION     WP_010811923.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..504
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56886
     Region          18..484
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mktisfhasp tivwpnenpy lndawrpvdt ewtatspdle iigeiprdls glyvrnghnp
       61 vhesmgryhp ydgdgmvham afhggkvqyr nrwvrtvgfl aeqaagkslw pgiieprkaa
      121 lrgwgsigam kdnagtdiiv hggkilaams qcsepyrmsp fslettgvep nwaralfprg
      181 icshfkvdeh tghmmffnfg etppymnygv vdrdnqlihf epidlpgprw phdlgmteny
      241 cvlhdlplff dperlrqgsh rlgfwrdvps rfgviprfgk nadvrwfeae pcyvlhlsnt
      301 fedgdevvmd gciqtnplpd lsglptegye rlkamldlhl qkarmhrwrf nlrtgqtree
      361 dlddqvtefp mvnglhngrs yrysynaips kgfwlleglk kydlltgqtq tymlpqgcyl
      421 seapfaqrrg ataeddgylv tfltnlstgk gecaifdard itrgpvariv lpqqvptgah
      481 afwatpdmlp gfdagfeaal qgny
//
LOCUS       WP_010812005             186 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010812005
VERSION     WP_010812005.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..186
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=19723
     Region          32..181
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mnqpinqrld wtpnpellal pavsaqehrg glrnfaaavs ivtarheqar agltatavvs
       61 vtaepprlav fvnknvvaan iimdsgalcv nvlsshqegv akafagmieg vhgderfrhg
      121 gwstmvtcsp alddalvnfd crvvkvydes thhaflcevl atrgcangag qdalvylngg
      181 frqiph
//
LOCUS       WP_010812093             414 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Cupriavidus].
ACCESSION   WP_010812093
VERSION     WP_010812093.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..414
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42769
     Region          16..400
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(27..28,31..32,35,70,117..118,120..122,125,150,
                     153..154,157,230,233..234,237..239,242,272,276,326..327,
                     331,335,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mptptapsry ealrpalpil igasvmlsla mglrqslgif mppltrdigi svsdftiaia
       61 vqnlawgllq plagawatri gfrplmlags llyvtglvll atahsmvgvt lgagvaigas
      121 mactgsalam avaarpvsaa lrstvlglvs gagslgalla apigqmvtqa ygwraglaaf
      181 vllalvmlpa awfagrvdrl plvspagrgq dsarealgta lrhapfvvma layfvcgmql
      241 vfltthlpsy ldvcgmdpml saqalgvigg fnvlgsiffg waggrfnklm llggiytirs
      301 laltwyftsa ptpqstlvfa avmgflwlgv aplvsgwiae tfglrwqaml ggvaffshqi
      361 gsffgafggg lvydalgsyt vawqvgvtlg laaglaqiaf avatrrrppl mats
//
LOCUS       WP_010812126             286 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Cupriavidus].
ACCESSION   WP_010812126
VERSION     WP_010812126.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..286
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=29341
     Region          53..210
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mtnlpttqap rngagarhps rtaglgrasl aaaavlvcat qlagcfpvia gamgtgvama
       61 tdrrpaatqt vdrglqleae ntinsryrgq arvnvtvfnr kvlltgeasn dtvkqqveqy
      121 vrglqnarvv inelevvnsp gfmtqsqday ltskvktllm tadgvpsnsi kvtteksvvy
      181 llgvvtaaeg dratdvarna sgvtkvvkaf dyvndterar ldsastsqnp sfdgnvgtpa
      241 pvqsvpgvgg pidapagaat gttattspva apvtspvtlp pgrnlp
//
LOCUS       WP_010812173             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Cupriavidus].
ACCESSION   WP_010812173
VERSION     WP_010812173.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..157
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17129
     Region          2..154
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 mstytaevlw qrdgqdfagn rysrrhvlrf dggaevpgss sphvvplpms dasavdpeem
       61 fiaslsschm lwflslaakq rfvvdrylda atgvmeknad gqtamtvvtl rpqvtfgger
      121 eptreeldal hhaahgacfi ansvrtevrc epvfaca
//
LOCUS       WP_010811308             171 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SET domain-containing protein [Cupriavidus].
ACCESSION   WP_010811308
VERSION     WP_010811308.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Qian,C. and Zhou,M.M.
  TITLE     SET domain protein lysine methyltransferases: Structure,
            specificity and catalysis
  JOURNAL   Cell Mol Life Sci 63 (23), 2755-2763 (2006)
   PUBMED   17013555
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Dillon,S.C., Zhang,X., Trievel,R.C. and Cheng,X.
  TITLE     The SET-domain protein superfamily: protein lysine
            methyltransferases
  JOURNAL   Genome Biol 6 (8), 227 (2005)
   PUBMED   16086857
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Yeates,T.O.
  TITLE     Structures of SET domain proteins: protein lysine
            methyltransferases make their mark
  JOURNAL   Cell 111 (1), 5-7 (2002)
   PUBMED   12372294
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459262
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..171
                     /product="SET domain-containing protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19248
     Region          19..159
                     /region_name="SET"
                     /note="SET domain-containing protein (function unknown)
                     [General function prediction only]; COG2940"
                     /db_xref="CDD:442183"
ORIGIN      
        1 madkakrkaa degkkktasd rievrqsgvh gkgvyaigqi aegervieyk gehiswkkal
       61 erhphdpsdp nhtfyfsldd gsvidakygg nrarwinhac epncearekk grvfihalrd
      121 iaegeelfyd yglvidaryt aklkkefecr cgspqcrgtm lapkekkkka k
//
LOCUS       WP_010812177             408 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation:proton antiporter [Cupriavidus].
ACCESSION   WP_010812177
VERSION     WP_010812177.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..408
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43109
     Region          18..398
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mnglsqlfps lplapgglfw vglalvgagl agelsrrwlr cprivgyaaa glcagmlgrg
       61 ivdenminqt rilidmalal alfelghrls ltwlranrwl lltsafesll twglvaavlq
      121 wigaspgvai laggiavsts ptivlqlkne lradgqvter lmamaalnsi yaaaivqvat
      181 gwlhseygnl gaallhplyl lvgscllawv vgklghaiyd rmsaddhysf lvlvglvlft
      241 laltrvlkls mpltlmlagv vfkhqdnqph vwpphfgsag slliivmvvs lglpltaqdw
      301 avggvyaial vvlrhvakla gvvslgsfsg lslrqcmalg lalapmsgla yllmhdvarl
      361 ypgtgqplaa iilcalaieq lfgpviaawa lryagevrvd irangggr
//
LOCUS       WP_010812232             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Cupriavidus].
ACCESSION   WP_010812232
VERSION     WP_010812232.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..146
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15251
     Region          1..139
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mtnivlatdg safsdaaarf iaegkllqsg ftvhvvhvap evsgqvrafv sketiddwhk
       61 easekamatv ceilsaakvp ferhplhgfa perivacars vdaaaivmgt hgrgsffdav
      121 igsvagrvla qaecpvllvk apekkg
//
LOCUS       WP_010812241             159 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methylated-DNA--[protein]-cysteine
            S-methyltransferase [Cupriavidus].
ACCESSION   WP_010812241
VERSION     WP_010812241.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..159
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16844
     Region          7..158
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mpatydailp apfgkigvrt dgariraivy lpghvearap adaltqqlaa qleayyanpd
       61 aafdlplapa gsdfqqrvwq aisavprgav ttygtiaeai gampravgqa cgqnpfpivi
      121 pchrvvsarg iggfshhaed gfyldvkrwl lrhegamli
//
LOCUS       WP_010812258             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Cupriavidus].
ACCESSION   WP_010812258
VERSION     WP_010812258.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..206
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22404
     Region          1..198
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mfsiiqaagw piwplllasv ialaliverf ltlkrsrvlp arlyeealaa aqqrratpev
       61 vntleqnspl grvlaaglrh vvlqphtsrd aakdvveeag rvvahelery lnalgtiasv
      121 aplmgllgtv igmieifgsq ggtgaspeql ahgisvalyn tafglivaip alifwryfrr
      181 rvddyvaele fratsfldai lpqrra
//
LOCUS       WP_010812268             382 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metallophosphoesterase [Cupriavidus].
ACCESSION   WP_010812268
VERSION     WP_010812268.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..382
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=40804
     Region          114..381
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mpprttilta alvtallhgy iglrllpamp vpmavkalav awlalscall pagllarrvs
       61 qpwsdlvswi gmlamgffss llvltlvrdv alaaawlagq llgwhapgls agsavavpll
      121 allvtlagyi narrlarvve vdvpvaglpd alhgftiaqi sdihvgptik rpyldrivdr
      181 vnslqadava itgdlvdgtv relsahtapl arlqarhgty fvtgnheyys gaepwiielr
      241 rlgvrvlmne hvvlqhdgda lvlggvtdys agrfheshrs dphraiagap ahagarvlla
      301 hqprtaaaaa eagfdlqlsg hthggqfwpw nlfvpmqqpy taglvrhgsl wiyisrgtgy
      361 wgppkrfgap seitrvrlvk ag
//
LOCUS       WP_010812288             449 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleobase:cation symporter-2 family protein
            [Cupriavidus].
ACCESSION   WP_010812288
VERSION     WP_010812288.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..449
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46515
     Region          21..429
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mqaavhpvdq vlparamatl gfqhmlvsyl gaiavpmiva galkmtpaqt tmlistalft
       61 sgiatllqtv gfwkfgvrlp lmqgvafssv gpviaigadp slgfngvcga iiaagviamf
      121 lapiigklkr ffppvvsgct itavglslfp vsfhwfgggr gasdfgapif fivafgvval
      181 ilfinrhgge lirnlsvvig llvggavawm lgmgsfdeva rapwftmvtp fafgmptfnv
      241 gaittmvivm vvqmvesmgl fiavgdivkr plterdatrg lranglasai ggmfaafpyi
      301 afmenvglvi vtgvrsrwvv atcgamlcav alvpkigalf asipaaalgg atmvmfgvvv
      361 aagiktlgev eydrnpnnls ivsitlgcam mpvmlpgmle klpgflqpfv hssviiacvv
      421 svllnlilng vpareadelp asadnvqgv
//
LOCUS       WP_010812312             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cytochrome c1 [Cupriavidus].
ACCESSION   WP_010812312
VERSION     WP_010812312.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..247
                     /product="cytochrome c1"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27511
     Region          18..247
                     /region_name="CYT1"
                     /note="Cytochrome c1 [Energy production and conversion];
                     COG2857"
                     /db_xref="CDD:442105"
ORIGIN      
        1 mkkllsilal agacfagapa maseggfple papvntadls slqrgaklfv nyclnchgas
       61 mmrynrlkdi gltddqiren llfsadkvge tmtiamqpke akaffgaqpp dlsviararg
      121 ddwlytylrt fyrddsratg wnnlvfpsvg mphvlwelqg qraakfteve ehgekvhkfa
      181 gfeqlspgkl skveydqaaa dlvsfldwma epaqnhrkrl gvwvllflgv ftvfawrlna
      241 aywkdvk
//
LOCUS       WP_010812343             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Cupriavidus].
ACCESSION   WP_010812343
VERSION     WP_010812343.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..272
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29067
     Region          4..246
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mtdsaqnlve ltavdfayad hgkpilsglt mqfprgkvia vmggsgcgkt tvlrliggqv
       61 rpqagtvsfa gtdihtldtr glyavrrqmg mlfqfgalft dlsvfdnvaf plrehtdlpd
      121 smirdlvlmk lnavglrgar dlmpaqisgg marrvalara ialdpallmy depfagldpi
      181 slgltarlir slndalgatt iivshdvhet fqiadyvyfi adgrivaqge pealrastdp
      241 fvhqfvhaea dgpvpfhyag pslaedfagg vr
//
LOCUS       WP_010812355             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PilN domain-containing protein [Cupriavidus].
ACCESSION   WP_010812355
VERSION     WP_010812355.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..219
                     /product="PilN domain-containing protein"
                     /GO_process="GO:0043107 - type IV pilus-dependent motility
                     [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=23509
     Region          9..196
                     /region_name="PilN"
                     /note="Type IV pilus assembly protein PilN [Cell motility,
                     Extracellular structures]; COG3166"
                     /db_xref="CDD:442399"
ORIGIN      
        1 mstntlpsvn llpyhearka arrkkvytml agaavagaav vllggfyidg riasvvalnq
       61 vlstenarld gqirevnslk kdidallqrq kaveslqter nrpvqlleel vrqvpegvyl
      121 tslkqtgeaf tiagvaqsne risellrnls gvawldkael veskavtmtn nlreqrrlfd
      181 fsmrfayrap eaaadgkktv pgasapaaap vpapaagka
//
LOCUS       WP_010812414             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Cupriavidus].
ACCESSION   WP_010812414
VERSION     WP_010812414.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..255
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26555
     Region          1..249
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mdamilvfsa gvfagamnal agggsfvslp aliavgvppv qantsstval fpgglasawa
       61 yrdglrpvgs valralllat lcgglvgayl llrtssaaft fvlpwlllva svalafgrrf
      121 geamrtrwhi hasavlavqf vlgiyggyfg gavgimmiav wrlldncdlk ylnadrtllv
      181 saanavavva fivanavrwp etlimlmgai iggysgarig rratpgtira itllvtfcit
      241 laffvktyaa tllir
//
LOCUS       WP_010812428             157 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Cupriavidus].
ACCESSION   WP_010812428
VERSION     WP_010812428.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..157
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17247
     Region          4..144
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mqsieldrtd rrllgvlqeq grasnlelae aialspaqtl rrhrrleeag lvkryearld
       61 aaalgfgvva fihvtmergh irdlsnfkrl vaelaqiqec fsvtgdidyv lkvvakdlks
      121 lsdflldtlm ripgvsgvks svcldeikct savplea
//
LOCUS       WP_010812434             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: patatin-like phospholipase family protein
            [Cupriavidus].
ACCESSION   WP_010812434
VERSION     WP_010812434.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..300
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31290
     Region          3..265
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mdktafvfag ggslgaiqvg mlrelaawgv mpdivigasa gaingayfac npgvagagrl
       61 dalwrgirrs dilpwswrsv wsmfggnrgh lveaaglrrl laqhfgtlrl eaaelqlhvv
      121 atdmhsgdev llssgsivda vlasaaipgv fppvqfegrt lidggvannt pvstaialga
      181 thvivlpagf tcaerrpprg alehafnals llvarqlvhd lqhfadraqi svvpplcpld
      241 ispydyskcg elidraaatt aqwlqgkgld sqripgalap hshdeatpsc sadipaaaph
//
LOCUS       WP_010812460             187 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SRPBCC family protein [Cupriavidus].
ACCESSION   WP_010812460
VERSION     WP_010812460.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..187
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=20979
     Site            order(34,36,38,47..49,51..52,67,73,75,77,79,95,98,105,107,
                     123..124,126,128,142,144,146,148,163..167,169..170,
                     173..175,178)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176854"
     Region          37..183
                     /region_name="Polyketide_cyc2"
                     /note="Polyketide cyclase / dehydrase and lipid transport;
                     pfam10604"
                     /db_xref="CDD:431388"
ORIGIN      
        1 mlvrhrkpfw glifaaitvg mllaplpwsd rtaihdevvi arppaqvfdy vstplhwpkw
       61 hpaslgvaga tdhplgqger vtetfmvaqr ggavvwtvie sqrprtwsie gvaegrrvgt
      121 ityrltpamt psltpsaert rierefryrs ptllfalinr ltlrervqae steavrrlka
      181 lletqpp
//
LOCUS       WP_010812522             400 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010812522
VERSION     WP_010812522.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..400
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43201
     Region          5..377
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mirdsarqqa lladirrfvl etcipleaei drtdvipepv veqmrrlglf ghsipeaygg
       61 agltteelal vnievsqaat vfrarfggnt giaseslvad gteaqrqryl pqlasgkvtg
      121 cfaltepeag sdatslqtta rqdgdhyvln gskcfitnap iadlftvfar tnpdtpgahg
      181 isafliergt pglstseper kmgqhgspvg dvylkdcrvp asaivggkpn vgfktamkal
      241 nkqrinlagl cvgpairlvd emvryaaqrr qfgkpiadyq lvqqmiadsn telhaaralv
      301 ldtarkrdag edvtmeasmc klfasemsgr vadravqvfg gsgymartva erfyrdvrlf
      361 rlyegttqih qlniarrtme argaalegsg pepdarqpaq
//
LOCUS       WP_010812542             382 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Cupriavidus].
ACCESSION   WP_010812542
VERSION     WP_010812542.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..382
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41911
     Region          17..376
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnvansepaa qqphaqpdta vslekvvkky hdhtvlhels lkirrgeflt llgpsgcgkt
       61 tllnliagfa eadtgeifid gqpvtcepph krqigivfqn yalfphmtve rnigyglrmr
      121 gvgkdeiaqr vkqvmdlvkl dglghrkpre lsggqqqrva laralviqpk vllldepfsa
      181 ldknlrgsmq veireiqrrl rlttvfvthd qgealamsdr iavmsngiir qiaspaelyq
      241 npqdpfvasf lgdvnilpah yhgqtatdvq lrlgsglisv pharladash dgerldvyvr
      301 pehiklehlh sesvlsgtvi nhvyqgdhin tfidvdipmt arqvvtvrsa glgamqqwpi
      361 gsvaglalpd egvsifspqk rt
//
LOCUS       WP_010812571             416 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Cupriavidus].
ACCESSION   WP_010812571
VERSION     WP_010812571.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..416
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43935
     Region          27..405
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mnsstsagpl tgdvrsdapv taleigmflv llasyalnam drqifpliaa dvrrefgfgl
       61 adtgllstif tlgmalagvp tgyllarwsr kavlqigiai fslgtlltay ssgfadmily
      121 raatgigeam qltvviaiaa syfarfrata vgainfsfgv gaivgpllgg hligiernwr
      181 lplvvfgltg fvamaliaat vskrmtekas aiathidtrg attmwnrnta lltvmsiigg
      241 lciygylgmy ptflrehlhy tpsdtgrvms ifgcgvfasi fggwlgdrfh pklvlslsfa
      301 gtgllgfllf sgptgmlvqs vlsfvwglvv sgvlyvnlag yhiksvrssl tnratgvfvt
      361 tlygagafag yiiggiaarf gwstagfaqi tllsvfgivl tvllrtdrms lpvrkp
//
LOCUS       WP_010812556             301 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: fumarylacetoacetate hydrolase family protein
            [Cupriavidus].
ACCESSION   WP_010812556
VERSION     WP_010812556.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..301
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32788
     Region          70..298
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkyqlfnyeg rdgtinvgvh adsrhvqfaa gtvdgllqdw paaqlriarf iaqlplaaet
       61 mepaqirflp plsqpgviyg aganyrdhvv amakavnmdl ttdpkadgvp pwhfikagrg
      121 tlsahrqalp ypshtrmldw eaelavvigk acrnispgda ldcvagytia ndlsardnlr
      181 reqvdasspf rfdwighkcf egscplgpyl tpaafvaspe aldiklwvnd elkqnsntsn
      241 hlytvaeqia ylserltlyp gdvlltgtpa gvgmesgvfl krgdsirvwi dglgeletsl
      301 q
//
LOCUS       WP_010812642             302 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Cupriavidus sp. GA3-3].
ACCESSION   WP_010812642
VERSION     WP_010812642.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..302
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30559
     Region          1..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mtmfgfiglg amgrhmarhl vhrglpvtvf dsnaqavddl vrigatrgas vrdvagraev
       61 vmaclptpdi veqvavgagg vagasavkvf vdhsttgptv arrvaaelsv hgiealdapl
      121 aggvagaeag slsvmvsgda gafaiarpaf eafagdvayl gaqpglgqtl klvnnmiags
      181 alvtaaeavl fgvkagipae ailrvlsrsa targfavqtl ladivlsrkf dfgfrmdlmr
      241 kdmrlalgea eavgapmfas avvkqffdva vadgagsddm trvvqqlekl agatigpacg
      301 qs
//
LOCUS       WP_010812721             343 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Cupriavidus sp.
            GA3-3].
ACCESSION   WP_010812721
VERSION     WP_010812721.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..343
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36863
     Region          26..311
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mkalqgktgw tlllalaiaf plitpnsyyl tvmtlafiya iatlglnlit gytgqlnlah
       61 ggfmaigayt lgiltvdhqv pfwlafvlag vvcmvlgyvv gvvslrlkgh yfsiftmcvg
      121 yiiylliekw eslthgtvgl igipvpaaig plsfdsvqaq yylvlfflav gtflmhrivt
      181 sllgrsfmav rnsdalaeal ginlmrtkvl sfvlsvgyag fagalyagqv rflgpdiart
      241 dltfemvmsm lvggigtifg pllgavlvpw itqslqfmqd yrmlvfgpvl illiifvpdg
      301 ivgswlkkqa rkaaaerrgk laaqfpaqpv tavpttraga dha
//
LOCUS       WP_010812722             287 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Cupriavidus].
ACCESSION   WP_010812722
VERSION     WP_010812722.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..287
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30183
     Region          1..287
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 malflqqfln gltlggvysl valgltlvyg ilhvpnfahg afymagayvs yflmtslgvn
       61 ywlamlgaal vvavlsmaad rlvfhplrns pelhdmiaai gillfleaga qalwgadfhr
      121 mptpygqivd vfgltaplqr lliigaafal mvllhlfltr tmtgatimam aqnregaalv
      181 gidatrvtll vfaisgalaa iaatlyapin lvypsmgnlv itkafviiil ggmgsipgai
      241 vggliigmae sfggfyvstd ykdiiafvll vvilsirpqg lfagkta
//
LOCUS       WP_010812729             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Cupriavidus].
ACCESSION   WP_010812729
VERSION     WP_010812729.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..255
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28414
     Region          1..254
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mrrvvfnqkg gvgkstivcn laaisasegl rtlvidldaq gnstqyllga raaeasptaa
       61 nffetsltyn frpveftsfv hptpfenldv mpahpdldsl hgklesryki yklrdallel
      121 eavydaiyid tppalnfytr saliavercl ipfdcddfsr ralytlldnv keiqqdhndg
      181 lqvegivinq fqpraslpqk lvdelvsegl pvlesrlsas vkireshqha tpmihldprh
      241 klaqeyvalh relag
//
LOCUS       WP_010812586             554 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Cupriavidus].
ACCESSION   WP_010812586
VERSION     WP_010812586.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..554
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60276
     Region          4..538
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 misvrnvtlr rgvnvvldra svtfnpgeki glvgrngagk ssffgllngt lhedsgefsi
       61 paawkmgqva qempetgqsa tdfvvegdtv llaaqaevaa aevsddgmrm ahaymalhda
      121 gahdaparaq alilglgfsa aqlsqpvnsf sggwrmrlql aralmcpsdl llldeptnhl
      181 dldalvwlea wlkryqgtlv vishdrefld avtqvtvhvd naklvryggn yskfedmrae
      241 qlvlqqaala rqadkiahlq kfidrfkaka skakqaqsrv kalermekia pvladaefnf
      301 efkeplnvpn pllsmldasf gypaptgalp gtpptiivrg inrsvlagqr igilgangqg
      361 kstlvktvah alapiageis egkglnigyf aqqeldvlrp ldtpmehmir lakdtpahmr
      421 apgqsgteqs lrtflgtfnf sgdmvhqavs tmsggekarl vlcmivwqrp nlllldeptn
      481 hldlatreal gmalnefegt vmlvshdral lravcdefwl vtkggvepfd gdlddyqqfl
      541 rdearrlreq paav
//
LOCUS       WP_010812745             434 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amidase [Cupriavidus].
ACCESSION   WP_010812745
VERSION     WP_010812745.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..434
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44208
     Region          1..431
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mddfldlpvr tlaamvsrre lsaeavvraa lariaaqdag ilawqhvggd tavaqarrld
       61 aggasgalpg vplgakdlmd tadmpttygs piyaghrpgv daaavalars agavvvgktv
      121 ttefatfqpg ptrnprapad rprtpggsss gsaaavaagm vplafgtqta gsivrpaayc
      181 gvvgykpthg tlplagikpl apsldtvgvl arrvddaaff igtlardaal adastlrhap
      241 lrigicrtph weragadtqa aldtairale riggtvrdfn lpqachglte aqldimafea
      301 laafapeare haedfsaafa rqleagravt gqrfhvalay aeaartafnt amagfdvvla
      361 psaegeapag lgatgdpifc rmwsllgtpc vhvptgtgat gmpvgvtvtg prhadarvlg
      421 mahrleqalg asla
//
LOCUS       WP_010812769             159 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Cupriavidus].
ACCESSION   WP_010812769
VERSION     WP_010812769.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..159
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18120
     Region          11..144
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtqrvnamkq spelfkkyle fgtllqdnai epsirdlvei rasqlngcaf cldmhvkqsr
       61 ihgerelrlh hvaiwrestl fqpreraala wtevltnipp hgvpddlyer vrahlsekel
      121 sdltflvmai ngwnrlnvaf rtvpgsadka ygldkakle
//
LOCUS       WP_010812796             650 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sigma-54-dependent Fis family transcriptional
            regulator [Cupriavidus].
ACCESSION   WP_010812796
VERSION     WP_010812796.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 650)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..650
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=69143
     Region          1..640
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mhraahpaap sdvarqaahv dpadadragl iaraharsag fgldvrhapg fdavspralg
       61 elvdasrdly rhalpvmetl haqiantdsm vlltdssgvi lhslgdgefv ararrvalap
      121 gvswsepskg tnaigtalae arptlihase hflesnhqlt cscapiaspt gailgaldvs
      181 gdhrgfhrht malvrmsaqm ienhlfanhf pdallvrfha rpefvgtlfe gvaafspdga
      241 flaanrsglf qlglaphala dagfaglfgq pvraamqarg gaagslqtlt lpsrvqvfar
      301 ieylaapiav rqpgaedplp palaaldtgd aavaavlrrv rkvsgrditi lvqgrtgtgk
      361 ewlaraihaa spraggpfva vncaaipesl ieaelfgyee gaftgarrrg segkvvqahg
      421 gtlfldeigd mplaqqvrlm rvlqeravtp lgsaralpvd vrvvcathrd lramiadgaf
      481 redlyyrina lavtlpplce rsdlpllvdr ilqrqceeag lpspvhvdaq vlallrrhpw
      541 pgnirqlanv lrtaailaeg eaqigvehlp egfeqecgde aercdaaaav qapapsksar
      601 mrdweaglir qalarhggnv shaarelgvs rntiyrrlre glegdeeaer
//
LOCUS       WP_010812781             308 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010812781
VERSION     WP_010812781.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..308
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32901
     Region          32..280
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mkrtttiptp ppdaahvlvp adaqaghaca ddrnfvtala rgmellrafg pqddylgnae
       61 lsrrtgiprp tvsrltytla tlgyltyiea tekyrlgqga mvlghryvgg agireiaqpl
      121 mqslafasdc tvalampdrh amvylescqp rgalvirlap garlpmatsa igrawlagld
      181 adhreaalae larhygsrwp avrtgidral rdyarrgfcv ahaewdrtvs gaaaplrlag
      241 ssevlalnig gaatrlspei lesnlgprir elaetlqarl wqpggarata rfasaqpdpd
      301 ththasna
//
LOCUS       WP_010812830              67 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Burkholderiaceae].
ACCESSION   WP_010812830
VERSION     WP_010812830.1
KEYWORDS    RefSeq.
SOURCE      Burkholderiaceae
  ORGANISM  Burkholderiaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Burkholderiaceae"
                     /db_xref="taxon:119060"
     Protein         1..67
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7045
     Region          1..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 metgtvkwfn dskgfgfitp daggndlfah fseiqgngfk slqegqkvry vagvgqkgpa
       61 atkiepi
//
LOCUS       WP_010812851             139 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Cupriavidus].
ACCESSION   WP_010812851
VERSION     WP_010812851.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..139
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14345
     Region          12..134
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mnmhpatvps tdnplldylg irlasvgdgr ctfeldlepr hlnrqgsvqg gvtatlldaa
       61 cgyaglpagp dgtlghavtv mltisylska stgrlrataq ltragkslyf asaelttdag
      121 vlvataqgtf krsrtlpea
//
LOCUS       WP_010812939             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Cupriavidus].
ACCESSION   WP_010812939
VERSION     WP_010812939.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..265
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28444
     Region          13..265
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mqrrnllqwi lgaaigatla tgavaqekpi kigvtggpha qimeqvkkva akdglniqvv
       61 efsdyiqpna alaagdldan syqhlpylea qikdrgykft hiaytvtfpm gvyskkiksl
      121 dqlkqgarvg vpndptnggr gllllqskgv iklkpnaglk atpldivenp kkirivelda
      181 aqlprslddl daaaingnya esaglspvkd aiaiegpkgp yanliairea dkskpwvakl
      241 vkayhspeik qyvtstfkds vitaw
//
LOCUS       WP_010813016             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: response regulator [Cupriavidus].
ACCESSION   WP_010813016
VERSION     WP_010813016.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..163
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=17591
     Region          30..153
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mrvaqteenq rvntagaqgl apgvsipdtt aqprrkvlvi ddsstirrta eiflsqagyq
       61 vvlaedgfea lakvgelhpd lvfcdilmpr ldgyqtcsli kksprfhaip vimlssrdgv
      121 fdrsrgrlvg ahdhlakpft reallhavqa clpcqaaghv lpa
//
LOCUS       WP_010813024             458 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sigma-54 dependent transcriptional regulator
            [Cupriavidus].
ACCESSION   WP_010813024
VERSION     WP_010813024.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..458
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=50438
     Region          2..119
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <142..445
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 msaytnrpll ylsqhhdaml crmlaqrgwk isfasnlqdl halppgnqpl aamldlqggf
       61 sdadlesfep wlslphigwi giiagqeslt esarrllgly fvdyytapvq hprlaeslgh
      121 algmaqlrpg aqharpgtar pdgmigscpa mqslfrgiek vsrwdtpvli sgesgtgkel
      181 aahaihrase rasrpfvavn caaipptllm selfgyerga ftgatkrkpg riemaqggtl
      241 fldeigdmpi esqtsllrfl etgrierlgg tesvevdvri isathvdlea aiaaerfrgd
      301 lyhrlcvlrv rqpplrergs dilliaehvl dnvrkqspar irgfspmalr aiqqhnwpgn
      361 vrelinrirh aaamcedgvi qpddlelatp addrpltlaa ireaaeqtai vealqrhher
      421 lidvaaelgi srvtlfrlmr dyklqvkkgd lglicvqg
//
LOCUS       WP_010813051             752 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Cupriavidus sp. GA3-3].
ACCESSION   WP_010813051
VERSION     WP_010813051.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..752
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80043
     Region          <70..>200
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          207..749
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mrirgieala ggqggndgea rqhtgiatld rrsflkltgl aggglalgva plaqaqdaar
       61 prttapapqa fliiapdntv tvavnrlefg qgvhtalpma laeeldadwr nvratlapag
      121 dpykdpafgm qmtggstaln hsfeqyrelg araramlvaa aaqqwkvdpa sckveqgvit
      181 sgshratfge lapaamelpv pqrvtlkdps qfrivgkptp rldargkmda ttpfgidthl
      241 kgmvvavvar pprfggkvks fsadkaravq gvrgvlqvpv drggsgvavi asgywpakmg
      301 rdaleiqwed agskvssqal fdeyarlagq pgtvaragsg digsaingaa rkieadfrfp
      361 ylahapmepl nctlqpevag gkvqsvkvwv gsqfqtvdqa avartlglap dkvvlntmma
      421 gggfgrravp tsdyiveaan vlkawvaagh teplkvvwsr eddirggyyr plhlhrarig
      481 ldaqgkvvgw qhtivgqsil kgtpfepfmv kngvdatmte givendydlp lqmsvhhpqv
      541 dvpvlwwrsv gnthtafvke tlademaaas kqdpvafrla rldekkharh raalqlavdk
      601 sgygkrklsk ghawgvavhe sfntvvayvv dvsvvkgepr vhrvtagvha nrvvnpmsae
      661 aqiqgacifg lamtkpgfai eiengavkns nfpdypppri tdapvvdvff vpsqenptgl
      721 gepgvppiap avanalftlt gkrqrqlpfv ma
//
LOCUS       WP_010813027             340 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010813027
VERSION     WP_010813027.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..340
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38009
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 msgpydvrll slvvpcynes esiskffasv ipvlesidai rfeivlvndg ssddtldkli
       61 aysrrdarvr vvdltrnfgk eaaltaglde algdavipmd adlqdppsli pelvmrwreg
      121 aevvlaqrss rvcdswlkrv tagayyrihn klseqklpvn vgdfrlmdrv vinalkqmpe
      181 rrrfmkglfa wvgyrtvivp yeresrsagr skfsgwrlwn lalegitsfs tiplrswtyi
      241 gvlialgafc ygtfivartl ilgidvpgya sllsvllflg giqliglgvv geyvgriyde
      301 akgrpiylvr rryqetgqdr liasgrrvir idrghvssgr
//
LOCUS       WP_010812938             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit beta/FixA
            family protein [Cupriavidus].
ACCESSION   WP_010812938
VERSION     WP_010812938.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26510
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkvlvavkrv vdynvkvrvk adgsgvdlan vkmsmnpfde iaveeavrlk eagvvtevia
       61 vscgvtqcqe tlrtamaiga drgilvesne dlqplavakl lkalidkeqp qlvilgkqai
      121 dddsnqtgqm vaalaglpqa tfaskvvvad gkasvtrevd ggletlslkl pavvttdlrl
      181 nepryvtlpn imkakkkqld ivkpedlgvd vkprlstlkv vepakrsagv mvpdvatlvq
      241 klkneakvi
//
LOCUS       WP_010813052             154 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [Cupriavidus].
ACCESSION   WP_010813052
VERSION     WP_010813052.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..154
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16110
     Region          1..154
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mttlninvng ktrevdvdps tpllwalrdn lemtgtkfgc gmaacgactv hvngqatrsc
       61 vtpvsaaaga rittiegigt dkvgravmda wlkhdvaqcg ycqngqvmsa igllrtkprp
      121 tdadidqama gnlcrcgtyq riraaikdaa rala
//
LOCUS       WP_010813083             302 aa            linear   BCT 01-JAN-2025
DEFINITION  LysR family transcriptional regulator [Cupriavidus sp. GA3-3].
ACCESSION   WP_010813083
VERSION     WP_010813083.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32564
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mharvlryld evvrrgsirk aaehlhvapt avnrqildle aelgaplfer iskrlrltpl
       61 gemvlahvrq tlrehdalre riedfkgarr gevtvavtag lagslmpslv hdfrqrypgi
      121 vvrvadlpva dittavgqgd adlglgydlp elpafralat sdwqigavvp pghvlaarqs
      181 allsecvgyp lilpapslsi raildaafar naievspvae ststalirql vmlgtgiall
      241 npldvmeera rqalvyvplr drhlqgqtlt lvarargpls aaaelmaeri gdalavlfaq
      301 ar
//
LOCUS       WP_010813166             147 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: thioesterase family protein [Cupriavidus].
ACCESSION   WP_010813166
VERSION     WP_010813166.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..147
                     /product="thioesterase family protein"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16509
     Region          21..140
                     /region_name="4HBT_2"
                     /note="Thioesterase-like superfamily; pfam13279"
                     /db_xref="CDD:463826"
ORIGIN      
        1 marlkldlpa dqfcyathlt vrvtdinsan hlandsmism iseararfly efgsedvrqe
       61 gvgiivtdla tmyrneahar dqlqfevgvm dfnkyggdii fritrpadgt liamaksgfv
      121 ffdyvgkkvv ampegfakrf pkvnwme
//
LOCUS       WP_010813242             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010813242
VERSION     WP_010813242.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..249
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26665
     Region          13..249
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mpdnallqtt ttaaglsryg qiaaelqani vsgawtpgsa ipaegalare fgialgtirq
       61 aiavlvqqgl lervqgkgtf vrkglsgasl mrffrfggvd gapavprsei lscravrldk
      121 amatrfglpt garglaisrr rwledtprll esiwlplprc ealqqlppaq wgdllypllg
      181 sacgitvhra vdevtfrtla adeaalldlp dahpcavvtr hafdlggnci eyrltrgdaf
      241 afrytadvr
//
LOCUS       WP_010813374             310 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010813374
VERSION     WP_010813374.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34502
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrlsqvqdfi avaehgsira garardvsap altksirqle eelhvplltr ttrgvvlsry
       61 gdaflrrarl iatearkase emaqmlgarn gvvrvgttrg pahvllpavv krfrvqhpdv
      121 lvcidswgyp thldelrsgv mdmavspvpd egiereftce plynndsvvm ahrehplrna
      181 rslreligsd wiltgqrmhg pgaaildafr erdlplprva vrcdtigmie hlmqdrhllc
      241 mlprqmvagr laanglvplp iedklpshtv sliyradspm tpvaaqfatl lrrevhylsn
      301 lpdsplrrld
//
LOCUS       WP_010813390             449 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: uracil-xanthine permease family protein
            [Cupriavidus].
ACCESSION   WP_010813390
VERSION     WP_010813390.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..449
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46224
     Region          8..431
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mshpapapvd erlpwrrlfv fglqhvlvma aspiasvflm skalnfppal avqllsatfv
       61 icglgtllqs lgkrgigarl pfvmlpggap ivlfiliaqq tdvqtaagav iltgvfyfcv
      121 lpvfrrclry fppvvvgtml llvainlaqv sgklvaghpa agstvdplnl llafatiact
      181 vaasrllsgm laqlaillgl lggalvagla gafqpghvsm spvfalptpf pfgwphfdvv
      241 aaiplmvfav ismveatgqt laisdavgrp vdqqrdvprt iradaltsll ggmfgtslii
      301 tsgenigivr atgvrsrfvt amsgailvvf gllvpvssli saipeavvgg tglvvfcivg
      361 tmgidmlrkv dlrdhanmyv vavalavgll pilvpgiygg lpanvrilvg ngvamgaita
      421 allnflffht glraaaagav arddaaath
//
LOCUS       WP_010813392             235 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Cupriavidus].
ACCESSION   WP_010813392
VERSION     WP_010813392.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..235
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=24002
     Region          3..235
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mdmtlfsvgv avftgalvqg atgmgfaliv vpvlalaapa mlpgalllam lplnayvawr
       61 erhaidmrga gwisagrlag tfgglwvlva mpmawlnalv ggstiaaavv sllapaftpg
      121 rltfastgli tgvtetatgv ggpplalayq hapvatlrat valcflvgea islvvlalsd
      181 rlgmeqvlya igllpvlmvg mvashlvhkr inqrmlrigv lvfalvsgav vllrg
//
LOCUS       WP_010813514             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Cupriavidus].
ACCESSION   WP_010813514
VERSION     WP_010813514.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..224
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23104
     Region          1..224
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          26..59
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          62..92
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(63,67..68,71..73,75..76,80,83,92,127,129,133..134,
                     137..139,141..142,146,149,158,160,162,166..167,170..172,
                     179..180,184,187,196)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          94..125
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          127..158
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          160..196
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          198..223
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mlaarlsicl alviamlist paaaaggtpe qqlreaaasg naaqvtallg qgasiddrda
       61 qgrtalllat hhnrvqaarv lvdagadvna kdaihdspyl yagargynei lrltlahgad
      121 lrstnryggt alipaaergh vetvrtliaa gvavnhvnkl kwtalleaii lgnggqahte
      181 ivrllvkaga dvnladgdgv splqharqrg ytqieqilsa agar
//
LOCUS       WP_010813515             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleoside deaminase [Cupriavidus].
ACCESSION   WP_010813515
VERSION     WP_010813515.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..155
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17115
     Region          1..149
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mstteaylld sirlamenvr erntwpfgav vvrdgevlar avnqvdatcd psahaemqav
       61 raasralgkp dlsgctvyas gypcsmclsa mylagvkavy yaysnedgep ydlsaergyi
      121 elarpleqre mtlayvpard egidlyeawr eqqdr
//
LOCUS       WP_010813528             333 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Cupriavidus sp. GA3-3].
ACCESSION   WP_010813528
VERSION     WP_010813528.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..333
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35258
     Region          5..331
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mtarasqdsa alpldketll tvyrkmrtir dfeerlhvdf grgdipgfvh lyageeaagv
       61 gilhhlndgd riasthrghg hciakgvdpv ammkeiygkk ggscngkggs mhiadlskgm
      121 mgangilgag aplicgaala akfrgkgevg itfcgdgasn qgtfleslnl aavwnlpvif
      181 vienngyaes tsrdygtavd syvdraagfg ipgltvdgtd ffavheaage virrareggg
      241 pslleckmvr fyghfegdaq tyraageldd irankdclkl fgravtqagv vareeldtid
      301 revaalieha vqeakaapqp gpedlltdvy vsy
//
LOCUS       WP_010813534             129 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [unclassified Cupriavidus].
ACCESSION   WP_010813534
VERSION     WP_010813534.1
KEYWORDS    RefSeq.
SOURCE      unclassified Cupriavidus
  ORGANISM  unclassified Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="unclassified Cupriavidus"
                     /db_xref="taxon:2640874"
     Protein         1..129
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=13838
     Region          10..128
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mtiqatwqps qgnsichltn gtaewqadld asaggdtqyp nphdlldsal aacttltlql
       61 yakrkgyait evhvsvghee angtytmnre vkvsgeltpq ilddllrvan rcpvhktlsg
      121 qfsiqtsia
//
LOCUS       WP_010813562             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Cupriavidus].
ACCESSION   WP_010813562
VERSION     WP_010813562.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..214
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24137
     Region          1..204
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mlriwgrlss invqkvvwca relhldherv digvtkgdld teayvrlnpn rqipviedfr
       61 gtdvggepfv lwesnaivry lcarygegtl wpedvkaras adrwmdwqtt afspamvtaf
      121 lnlvrkpkae rdeaaikasc erteplaell dkalagrefi ggdrftmadi slacaahrwm
      181 glplkhqsrp nlerwlsamr arpaadgile lplr
//
LOCUS       WP_010813572             392 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: benzoate/H(+) symporter BenE family transporter
            [Cupriavidus].
ACCESSION   WP_010813572
VERSION     WP_010813572.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..392
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39864
     Region          8..392
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mttaslklsd lsvsalvagl vatltgytss lvlmiqagha ahltdaqiss wiwalsmgmg
       61 ittislslal rvpivvawst pgaalliasl pgvpyaeaig afllaglmma aagmtgwfdk
      121 lmralpasia sallagilfr isvdvfvqaq hqtvlllamf aayllgrrlw payavpgvll
      181 tgavvagvlg qldfsgvrla lavpvwttpa fslsalvsma vplfivalas qnipglavlq
      241 adgyhvpasr lisitgltsa vlapfgshgv nlaaitaaic tgpqadpdrn rrytaavvcg
      301 vgylvagtla asiaalfaaf pqalvvgvta falmgsiang ltvamqipae reaalltfmi
      361 tasgmtlagv gsafwgvvgg mlafhvlrrr aa
//
LOCUS       WP_010813608             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TerC family protein [Cupriavidus].
ACCESSION   WP_010813608
VERSION     WP_010813608.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..233
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24531
     Region          15..189
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mewftdlftm qfltallsiv vidlvlagdn aivialaarn lpahlqkkai iwgtvgavvv
       61 rsamtigvvw llkipglmli gglalvwiay kllsdegdge ghgsgastlw gamktiiiad
      121 avmgvdnvla vagaahgsfl lvvlgllisi pivvwgsslv lklmsrfpii iylgagvlaf
      181 tavkmivhep mikaffeanp vvnwglyvli vggvlgagyl vqkrrvqqpa gsh
//
LOCUS       WP_010813636             149 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GatB/YqeY domain-containing protein [Cupriavidus].
ACCESSION   WP_010813636
VERSION     WP_010813636.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..149
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=15848
     Region          1..139
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslkarised mktamraret erlgtirlll aaikqrevde rvelddtavl avveklikqr
       61 kdsisqfrqa grndladkes aevevlqaym paalsdeeva aevqqavaat gaagpqdmgk
      121 vmgvlkgkla gradmtavsa lvkaalaak
//
LOCUS       WP_010813696             195 aa            linear   BCT 01-JAN-2025
DEFINITION  YceI family protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010813696
VERSION     WP_010813696.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..195
                     /product="YceI family protein"
                     /calculated_mol_wt=20706
     Region          18..190
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 maaralalaa algitaaqaa pleytidpah ttvyfsashf erssvrgrfg kidgrliyda
       61 dsgagaldvt vdlasvdtgn rtldgvlrsa qffdtaqhpv arlradrflm egrrlaaveg
      121 eltlhgvtqp lrlqaerfrc gevtlfgvsr qvcggdfrae vprsafgmtr flpevgdtvt
      181 lqvaveaspa gstpr
//
LOCUS       WP_010813769             217 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Cupriavidus].
ACCESSION   WP_010813769
VERSION     WP_010813769.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..217
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24055
     Region          5..77
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(16,18..19,21..22,25..26,70,73..74)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(16,55..57,68..69)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(55,67..68,70..71,74)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          90..202
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(93,100,160,163..164,167,171)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(93..94,97..98,101,137)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(100,104..105,108..109,168,171)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mskttltiss ktysswslrg wllarfagle feevlvppdd aaaraeilll spsilvpclr
       61 hhgvtvwdtl aiaeylneih pkagllpedr aarahcraic gemhsgfaam rsalpmnlkg
      121 hfpgmkvwsr aqadidrvta iwtecltryg gpylfgtrtm adamyapvvt rfvtygvmld
      181 pvpvayckqi lsmpelqewi aaareepdei seldvef
//
LOCUS       WP_010813781             271 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Cupriavidus sp. GA3-3].
ACCESSION   WP_010813781
VERSION     WP_010813781.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..271
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29628
     Region          26..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprstrktsv ktpadphkda dtprwsrrka arpqelvaaa ldlfvergya atrledvaaa
       61 agvskgtvyl yfankeelfk svvrenlvpa largsdlvda ydgstpellr ellrgwwgli
      121 gatpvagltk limaesanfp diarfynqev mmpgdelfak vlargvarge frampanptt
      181 tlvcaplvfl mlwqralrat aekdidpeaf ldglldtllf glttgdarnr plppqtgpyi
      241 werirddmla qraaameada epdppaprpg p
//
LOCUS       WP_010813805             342 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010813805
VERSION     WP_010813805.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..342
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39038
     Region          1..197
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mpkvsicipa yqqvaflrqt lqsvmdqrft dyevivtdds pddsvealls efdfggrlry
       61 vrnakqlgsp enwnaalrla sgdylkilhh ddnftdadal gdfvqllddh pdagfafcat
      121 liidvatghq rvhratesqm qalrampevl fagnfvgaps ttiyrrafsl eydirmkwlv
      181 dldfyirilq sgtpfafstr plictptnaa hqvtevcrds gqielyeysi lfekiahkva
      241 eepeiweqwy rlfekyhirs rrgflkygva qpepavyfdq liasyrrkrl ltlqglarif
      301 faiypkvpap vrapirwtkn gvlfvlgrqr klppageygg dk
//
LOCUS       WP_010813858             472 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase, partial [Cupriavidus sp. GA3-3].
ACCESSION   WP_010813858
VERSION     WP_010813858.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..>472
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          1..395
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfselglsd kivravaeqg yttptpiqaq aipailkggd llagaqtgtg ktagftlpml
       61 qllsdsaarg angaqrparl pvralvltpt relaaqvees vrnygkylrl rsmvmfggvg
      121 inpqieqlkr gveivvatpg rlldhvsqrt idlsqvellv ldeadrmldm gfihdirkil
      181 nvlpakrqnl lfsatfsddi raladrllnn pasievarrn ttaetvdqrv ypvdrerkre
      241 llahlvrqhd whqvlvftrt khganrlaeq ltkdglsala ihgnksqsar tralsefksg
      301 tlrllvatdi aargididql phvvnfdlpn vpedyvhrig rtgragaege aislvcvdei
      361 allrdierli krkleqtvlp gfevdpsiap epiqkgrqqr ggggqgqgqg qgrgraqarp
      421 agnegegaqr qrpareaqaa prqaqggqpr traaeggqrg ngaangnrgg qp
//
LOCUS       WP_010813903             265 aa            linear   BCT 01-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010813903
VERSION     WP_010813903.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..265
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29977
     Region          3..240
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mnitqehidt yqrdgvlvlr gaftdwverl rdgfaqnlae pgpfaienvr pgesgrffed
       61 ycnwqritpf ddfirqspaa aiagrimqsq avqvfhehil vkepgtakpt pwhqdlpyyc
      121 vdgtqtasyw ipldpvtqan tlrvvagshr warlvrpkrw assenfyggn dafmempdve
      181 dgsytllape lepgdavvfd frtvhgaagn tgsgrrrafs arflgddvrf mqrpgrtspp
      241 fpgidqqtge rmredwfpvv wraar
//
LOCUS       WP_010813938             114 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FmdB family zinc ribbon protein [Cupriavidus].
ACCESSION   WP_010813938
VERSION     WP_010813938.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..114
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10656
     Region          1..>60
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyayrcda cghgrdvlqk msdapltdcp scgtagafkk qltaagfqlk gsgwyvtdfr
       61 ggsagapaat gaaggaaaaa astpaaaesp aspassasat paaaggcgsa cach
//
LOCUS       WP_010814001             394 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Cupriavidus].
ACCESSION   WP_010814001
VERSION     WP_010814001.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..394
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43443
     Region          223..389
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mlmevsqnqa aahlfaqatv slsefstllg niyqgpmeqv pwgkaleqir rqlnanyctl
       61 ilrspatdrp glminasehg stlpgetsyn nyyyaldpfi glpsdrvvti dehlgpgawc
      121 qselyqqflk digiryilga dlrtddgvec rfrvcrehdg rdfsaadkal ctallphlkr
      181 avdlhsridv vesertvyas aidrmlvgmv ildesgtiik tnaaadeilg akdgirvakg
      241 sldveygqen rkfqrllrqa mmghlgttpa lmeamsitrp sgsarlgvli rtiplsewse
      301 dnrkrpacvv firdperrsq ashevvrqlf dftpaetqla lqlangltld eaadelgisk
      361 ntarahlrai fsktgvtrqa tlvrmllssv islg
//
LOCUS       WP_010814003             318 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Cupriavidus sp. GA3-3].
ACCESSION   WP_010814003
VERSION     WP_010814003.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33155
     Region          77..285
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpldpqarav leamaampsp dfstlraady raalaampaf asgdtvaaqq dltidgaagp
       61 lkarlyrpdd gtalplvvyf hgggfvlcgl dshdnicrgl arrsgalvls vdyrlapear
      121 fpaaaddava avrwaaahaa qlgadparla vagdsaggnl aavacqqlrg gaialrhqll
      181 lypyldcsda aatsasyrec aqgyflsaae ldwyraqyla npadatdvra splhqrelhg
      241 lppatiitae ydplrdqgea ygealqragg satvrrwpgq fhgfismqgm idaasdalda
      301 aaaslrqafg stsrqeaa
//
LOCUS       WP_010814031             367 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: porin [Cupriavidus].
ACCESSION   WP_010814031
VERSION     WP_010814031.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..367
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38625
     Region          18..367
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mnqtashwll aagllpfval aalagtnaha epgvtlygia ssavrytsnl dghhngqaal
       61 vsggmvgsrf glkgdedlgg gnhaifrlea gigsddgrss yntlfgrqay aglsgdwgsl
      121 tfgrqynaln nigwafnpld qgwgnfwsdp lyiggdiffq dyrinnsmvy kktagpftlq
      181 ldygtgeqpg slargitlgg glmfqqgala lgaaydqrks adggntvrny svggsyafgk
      241 ataylghmgr resagdarfn iafaglgyql tpalhvsgay yrywqggnvt tqfqdvpall
      301 gsgnadsiav vadyalskrt svyleadavh arggavgret eywagapaag vdrttrvgvm
      361 lgmrhhf
//
LOCUS       WP_010814103             477 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cytochrome ubiquinol oxidase subunit I [Cupriavidus].
ACCESSION   WP_010814103
VERSION     WP_010814103.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..477
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52726
     Region          4..445
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mfgltaldla rtqfaftisf hiifpaitig laaylavleg cwlrtqrthy rdlyhfwski
       61 favnfgmgvv sglvmayqfg tnwsffsefa gsitgpllty evltafflea gflgvmlfgw
      121 nrvgpglhff atvmvalgtl isatwilasn swmqtpagfe iingrvvptn wfevifnpsf
      181 pyrlvhmsva aflatalfvg asaawhllrg rdnpairkml smamwmlliv apiqavigdm
      241 hglntlkhqp akiaaleghw enkgneglpl llfgwpdmar eetrfavevp rlgslilths
      301 wdgqikglke fapqdrpnst ilfwsfrvmv glgllmillg vwslllrrge rmyrsrgflh
      361 malwmgptgl iailagwftt evgrqpwvvy glqrtadavs phgvpelatt laifvvaylf
      421 vfgvgiaymm rlvrkgpale eakpeggpgr ghtparplsa vdddealapa ttartrs
//
LOCUS       WP_010814116             223 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Cupriavidus sp. GA3-3].
ACCESSION   WP_010814116
VERSION     WP_010814116.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..223
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24262
     Region          14..223
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msldallars pwaaaltpeq rqrvraelre ravpqgayvs rkgdladswl giaqglvkvh
       61 caspsgkrat ltgvpaggwl gegsllkrea lrydvvalrd sriacmpaat frwlqetslp
      121 fnrylldqln erlglfiatv eherlhgieg rvaralatlf hpvlcpldse nvslhltqee
      181 vgllagisrq ranaalgvle gegllavehg avhvldleal rry
//
LOCUS       WP_010814139             130 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RidA family protein [Cupriavidus].
ACCESSION   WP_010814139
VERSION     WP_010814139.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..130
                     /product="RidA family protein"
                     /calculated_mol_wt=13773
     Region          20..127
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mdikrfgveg gtgtggqhmp faravaadgw lyvsgqvpmv sgevidggiv pqthqaiknv
       61 lailaeagyg pehvvrcgvw lddtrdfasf nkifkeyfga npparacvqs smvvdckvev
      121 dciaykkpaa
//
LOCUS       WP_010814176             275 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ferritin-like domain-containing protein
            [Cupriavidus].
ACCESSION   WP_010814176
VERSION     WP_010814176.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..275
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31606
     Region          35..171
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(43,75,78,130,160,163)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 msepstaarp wsvsdinyqa idvervrgdr dlfyllvsas fiesgsdtya gnlatyyarv
       61 pdaadwlaeh weaeelqhgl alrryvehvw pefnwergya rffdeysktc sidqfepteg
      121 lemaarcvve tgtaayyral eqasdepvlr dltrrisnde vrhykhfyqy fnrfaaserl
      181 grlrvlgala rrlleikned aaialrnvlr mergveavse aevralnarv sgvirrnipi
      241 emtvkmllrp lhlhrgvera vrtplvamvs rvmlh
//
LOCUS       WP_010814240             413 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Cupriavidus].
ACCESSION   WP_010814240
VERSION     WP_010814240.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..413
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44804
     Region          10..396
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtpsatpqar prlvvvgngm agmrtveell rlapdlydit vfgaephgny nrillspvla
       61 gektvadiml ntrewyaehg iellagdpvv aidrprrivr sasgrevryd rlllatgskp
      121 filpvpghql dgviafrdiq dvetmqqaar dhrhavvigg gllgleaang llrqgmdvtv
      181 vhlpdslmer qldkpaatll qgalerkglr fllgaqtaei lgidrvtgvr fkdgseipad
      241 lvvmtagvrp nielaagagl hceraivvdd tlqtydpriy avgecvqhrq atfglvapiw
      301 dqarvcaahl agaghrhyvq qatatklkvt gvdlysagdf igaegsedlv lrdprrgvyk
      361 rlvlqdgylv gavlygdvqd gpwyfdmiqr rtpvgalrqr llfgqaqcea laa
//
LOCUS       WP_010814272             307 aa            linear   BCT 01-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010814272
VERSION     WP_010814272.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..307
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31654
     Region          35..287
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mqrrhflgis aaallagcsf gprpapplla ttppaprpvk iglalgggaa rgfahigvik
       61 aleaqgihad lvtgtsagav vaalyasgln gfqlnklalt mdeaaiadwa lpfgtrfggw
      121 lkgealqnyi nrlvqnrtie amklplgiva tdlksgekil frrgntgqav rasssvpgvf
      181 qpvsiqghdy vdgglvepvp vdsargmgad fviavnisad psaqknagqs gvllqttaim
      241 gqsinkmala radvvirpel pdmggsdfna rnrailageq attavmatlr qrleqarlap
      301 agtvavq
//
LOCUS       WP_010814292             309 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010814292
VERSION     WP_010814292.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34255
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..292
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(111..112,114..115,118,122,124..130,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 mtinfnlndl qafravaeln sfrkaatsln vsqpafsrri dkleealgvr lldrttrrvs
       61 lttvgrdfdr kvkeildeld qallgirgvt ttrmgevtia cvpstvyyfl pqvisryhaq
      121 ypkirvkild asanevlsav srseadfgid fvggqepdie frplleerfv aacrrdhpla
      181 errqvtwadl aeydyisvsk asgnrllldq alsnvsrlpq siyetqhvtt tlglveaglg
      241 iaavpsiamp gpdhpllvsv pltdpvvtrk iglirrksrs ltpaaqqlyd flcetrprrg
      301 apagkrrgk
//
LOCUS       WP_010814403             347 aa            linear   BCT 01-JAN-2025
DEFINITION  porin [Cupriavidus sp. GA3-3].
ACCESSION   WP_010814403
VERSION     WP_010814403.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..347
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36640
     Region          2..346
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 malagvlaga scgvtqqaqa qsvstsisvy glidtmvrys dnnrgderla elsegyfsgs
       61 rwgvrgneal gagwsalfnl esgfdlasgt slqgtaasny gqvgtqgtgr lfgrqsylgi
      121 ehqawgkltf grqfttayda tfrfqpyghp npdavailng ytgprqdnmv kyagrwgafs
      181 aaahytfgev pgdaaasssr glalawttar idigalfqst nalateekrt iwgiggssql
      241 grvklalgyl dnryhlsptr nhvltggatv qatpalavsl aagydrqsaa sghrlmltsv
      301 aeyslsrrts vyaeadfnri sgsyalpafm gvrgnkfggg vglrhrl
//
LOCUS       WP_010814439             165 aa            linear   BCT 01-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010814439
VERSION     WP_010814439.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..165
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17085
     Region          3..159
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 maipirltvn gkpvdaqvep ntllvqflre qlrltgthvg cdtaqcgact vhldgravks
       61 cnilavqadg aavttiegla gdkagnglhp mqeafrechg lqcgfctpgm vmsatalvqe
      121 ypgadaatir ahlegnlcrc tgyhnivrav qqgqaamqgt aasae
//
LOCUS       WP_010814471             507 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Fic family protein [Cupriavidus].
ACCESSION   WP_010814471
VERSION     WP_010814471.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..507
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=56378
     Region          177..474
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mshaplgyda lirkfglrvp plrstsalad ktgvlsthtg pdgttrtvyp rnryrggdtt
       61 vdhltfalkk eqldltvlaa lfehapavqa vrewlaatpt sryarlsafy akwlagaqfd
      121 yklpagaprv laldesrylt gpatpdlqfg iqnnhlgpaa fcplvrrtek laqyiaadlp
      181 grvaaaikrl epellaravd ylylaetrst ysieheipdn qrvakfrrll eyagnpaplt
      241 eaqlcewqne iisglraefs yrdkqnwlsr ggrmrniady ippppgqlga mmdgiaavag
      301 lveaqaanpi vaaacvsfgf vfahpfydgn grlhrflihh llrqagvtpd gvvlpvsarm
      361 lkqidtyaal lksysaprta llnyaldsds dtilikspqp gwlyasfdat alcefvfeci
      421 eqcveqdlaq eiqylrayda svarleswld lrqsrlsnli dlivqnhgel srrkrklfed
      481 itddelarie avvrdeftey lelngsr
//
LOCUS       WP_010814475             443 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: nucleobase:cation symporter-2 family protein
            [Cupriavidus].
ACCESSION   WP_010814475
VERSION     WP_010814475.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..443
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44628
     Region          30..424
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mapllfkved rpprlttfll alqhllaalg giiavplvig galklppdqv ialvnaallg
       61 sgivtiiqck gigpvgirmp cvmgtsfafv gaaisvgveh gvagilgsal agslvmilgs
      121 ffmpairklf phtvtsvvvt miglslipva idwaaggqgs srygapgnla iavavlalvv
      181 avvqwgkgml sasaivvgia ggyllclalg lvdftqfhqa piiavpqplh fgmsfpisgi
      241 vamsiaflvt ivestgtfma lgaatqrpis gkclsrgilc dgfgsafaal vsspplstfa
      301 qnvgvvsltg vasrhvvalt gvmlllaglf pvlgalvvti pqpvlggagl mmfamivsgg
      361 iqmlstvkft qrntlivavs igcglavtfr pellsklpaf vhevfgsgit vgslsaviln
      421 lllpggkdep aeqaghgtvg eaa
//
LOCUS       WP_010814520             411 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Cupriavidus necator].
ACCESSION   WP_010814520
VERSION     WP_010814520.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus necator (Ralstonia eutropha)
  ORGANISM  Cupriavidus necator
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Cupriavidus necator"
                     /db_xref="taxon:106590"
     Protein         1..411
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43007
     Region          63..400
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mstipdsaps slppaspvpl padgsphaga dtegaagsrt maemadsvvp adavtaslhr
       61 asvalvvlat lfslyavhia reflipvvla ivlaylldpl vcalqrlglp ralagtvvll
      121 avlsallsga yllqgqvesi vnslpetask lsrsvgalms gddsmwqkvr raatvlsgtg
      181 qpppargtqv vveqapaqih nmllagsvsi ftmagqavvv vfllyfllla gdtfkrkfik
      241 mvghtisekk isvhmldevn rsirrymgml lvtntalgac twlllkwlgv hnagswaiaa
      301 aalhlvpyfg alaiavclgv vtfmqfgtlg maaaatvgsl liatligsvv ttwmtgrmar
      361 mnavavfval llftwlwgvw gmllaiplit iakvvadhie glevvaeflg e
//
LOCUS       WP_010814529             285 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Cupriavidus sp. GA3-3].
ACCESSION   WP_010814529
VERSION     WP_010814529.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..285
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28896
     Region          16..274
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msgatetqqd leggkpqrgi qsldstgqll valvaagrpl alrdlalaag mppakafphl
       61 vslqktglla rdaagnylcg plglelglia lqrlsptrea epevielaga tglsvamavl
      121 gplgptvvrl eesarpqhvs lrvgtvlslv htaigrtaaa ylpanvlagl lekddlrmag
      181 aaaaevlepg gklapayagr laqvraarld nalshpvpgi dtlaapvfdh tgslalviav
      241 mgssgsfdss tagataalvr qaarrlswrf gapdtawaqa iscpa
//
LOCUS       WP_010814530             275 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Cupriavidus].
ACCESSION   WP_010814530
VERSION     WP_010814530.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..275
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28216
     Region          66..249
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 marrkageag tqadepaara dkaqrgiqsv evggrllval avarapmpla alaeaaqlap
       61 aqahaylvsl trlglikrdh lsgryepgpl slqlgmlhle qdaawraaqp rvdalaqasg
      121 fsvaisiagp qgptivryvp asaplhvnlh vgtvmalaat atgrvfcafq ppalwqplwr
      181 aqqpgaaesd laafsaslge irargiersi dtpspavssl svpvldaagv lrlvltlvgs
      241 tgaievdwrg aaaqallaaa adigaalrde egrla
//
LOCUS       WP_010814552             121 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Cupriavidus].
ACCESSION   WP_010814552
VERSION     WP_010814552.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..121
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=12423
     Region          52..117
                     /region_name="BON"
                     /note="BON domain; pfam04972"
                     /db_xref="CDD:428229"
ORIGIN      
        1 mtprfriarl alplavlama asqavaaapt dapaapsstg rtaaprdtaa asdraitaev
       61 qarlanartl dparirvstt dgvvklegtv rddkqrtmam elarsvrgvs avsdelragt
      121 d
//
LOCUS       WP_010814574             565 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Cupriavidus].
ACCESSION   WP_010814574
VERSION     WP_010814574.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19108972
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..565
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60755
     Region          21..226
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
     Region          298..484
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16278"
                     /db_xref="CDD:293836"
     Site            order(359,361,363..364,422..423,441,480)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293836"
     Region          519..560
                     /region_name="BLACT_WH"
                     /note="Beta-lactamase associated winged helix domain;
                     pfam17778"
                     /db_xref="CDD:407650"
ORIGIN      
        1 mtttetsgnr patpapllrt aasllvvrda pagmevllvr rverandrss gayvfpggtl
       61 daqdkalhah ahglddalas erlgmpasgl dfylaalrec yeeagllfac drdgrphsph
      121 qldaagqall reavqrggpg lahaceqlgl rlaadrlayh sywltppglp krfdtrffva
      181 iapegqvavp dgteivehrw irpgeaadpa sglplmhvtr rtlssiaqfe saaacfayys
      241 qlrgiacimp rlatgaagvr pvmpnepcya eigridpdgn thgryelvpg vpvrlservw
      301 rvtanngsvm tgpgtntyli gggarnewav idpgpddgeh vrailaaapg pirwilatht
      361 hldhspaaaa lqaatgatvl graapagqwq dlsfepqrel nhgerlaite dctlrvchtp
      421 ghasnhlcyl leeeqtlftg dhvmqgstvv igppdgdmra yldslaalqd edldwlapgh
      481 gfliarpqda irilvrhrlq reakvvaalr elgpapigel llrvyddvpp rmhpvaqrsl
      541 lahllklrdd gkaqeadgiw snata
//
LOCUS       WP_010814586             291 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Cupriavidus sp. GA3-3].
ACCESSION   WP_010814586
VERSION     WP_010814586.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..291
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31590
     Region          6..265
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mtpthrrpgy wlqlaltlav cafmtvpvvl svlagltnni figlesgltt rwlaevwsly
       61 rntiflslli alaclactlv lgvpaayyma lrrnritrli eellmlpvav pglatalgli
      121 llygtwqalr tswlfiligh vlftlpfmvr svlailsaid irtledaaas lgasrlqrff
      181 tvvlpncrqg ilagalmvvt lsvgefnltw mlhtpttqtl pvgladsyas mrleigsayt
      241 ivffvmiipl lvlmqalsal garsrkyvpe avpasavaat panphtetrh a
//
LOCUS       WP_010814652             388 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Cupriavidus].
ACCESSION   WP_010814652
VERSION     WP_010814652.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..388
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42249
     Region          1..386
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnfdlseeqa siveavqqvc tqfdmeywdr ldksgtyphe fyktlceggw lgvampeafg
       61 gaglgileaa lvmqtisqsg agmtgasavh mnvfglnpvv vfgtdeqkgr flppliagqe
      121 kacfgvtepd agldttklkt farkvpggys vsgrkiwist aqvadrmlll arttplesvk
      181 ksteglslfy tkvdrskiei reidkmgraa vdtnmlfidd lfipeedrig eegrgfeyil
      241 hglnperili aaeaiglgra alaiatqyak ervvfgrpig mnqgvqhpla qawmqlesan
      301 lmmlkaaary dagqscgaea ntakylaaea ghnacqtail tlggmgysre yrverllres
      361 yipriapvsp qlimcfiaer vlglpksy
//
LOCUS       WP_010814655             369 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Cupriavidus].
ACCESSION   WP_010814655
VERSION     WP_010814655.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..369
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40193
     Region          30..328
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdlsipnpva dttkqvdggs paggqpqeid alivgagpvg lfqvfelgll eikahvidsl
       61 kvvggqcvel ypdkpiydip avpictgqel tdnllkqiep feptfhlgqe vavverredg
      121 rffvetslgt rfitktifia agvgsfqprt lkvegidkfd gkqlfyrvkd psrfhgrnlv
      181 iigggdsald wtldlvgkae svvmihrrdg fraapasvak mkelceqmem qflvgqvggy
      241 eekdgvltei kvtgadgvtr rlpvddllvf fglspklgpi aewgldlerk qikvdtekfe
      301 tnipgifavg dintypgkkk lilsgfheaa laafgaapyi fpekkihmqy tttspklhki
      361 lgvdspvfd
//
LOCUS       WP_010814709             219 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Cupriavidus].
ACCESSION   WP_010814709
VERSION     WP_010814709.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..219
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23013
     Region          140..218
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mfdqrflkit lavllfhvgl lyliqsglgr klteavispe ivariiplep pkqeappepp
       61 kpkpkqetpp kqvkvttpkp tppqpkptpq pvaslpptpn apeappappa ppapapepap
      121 apvsaaprav gigeiqctap qpkypsqsrr mgetgkavvr lttdesgkvv ktsvvsssgs
      181 srldqaavea vqamrckpym dngravavta qqpigfeln
//
LOCUS       WP_010814734             701 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Cupriavidus].
ACCESSION   WP_010814734
VERSION     WP_010814734.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 701)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 701)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 701)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..701
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76529
     Region          297..649
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mtepassgwq rlnawrglaq lwrqpeppdf hwrllryfcw trvavglllv gfalmrrgep
       61 asvtaitnai ppvpfdlggl ggiehaaamt iavpylgiav amlagtlwrr hfhlrvrvqv
      121 ladlallalv fsvlgrggqa eglamifllp aleagaltsl lfalfaasis alvvmsgpfm
      181 htillrqada gllgsglfgl vfmiaallmy mlanrqiaqe rlalareqel rlqqlvnrlm
      241 vndmqdgvml vrangavvaa npaavvllgv qpheriysrr lggaagqgge avlfdlrrip
      301 rlqplmemlr dwlhskddvp rilqllpmas gtaladgtmq htrlrlrfvl pglaglrstm
      361 ahgrtvpatl dtaawselsp eaagrlrlai aqneamawsq edeallrnem rdtvlvhies
      421 weriaeqvqq eklaamgrlv asiahqirnp laaisqasel lgdsgrrdpa aqdhggadvd
      481 idarllriin dnvrrldqvv sdvlqmsrrp rtgrstvhla qalpeiverw raemrsrrpr
      541 agetrpagra dinanairlt vdvaqpvvfd asqlqqvlgn lldnawrycs rlpgsirlla
      601 haldqhhael ivwndgaeva rehqrslfep fftsnaqgtg lglfmarelc gandaqvryg
      661 aialpaller tgmlaaaard tlpakafvlt lriesadaaa a
//
LOCUS       WP_010814739             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Cupriavidus].
ACCESSION   WP_010814739
VERSION     WP_010814739.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21677
     Region          13..202
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mevsqlaagt gvfaafagfa lvssitpgpn ntmllasgvn fgfvrtvphl lgvsigfalm
       61 vglvglglgs mfhafpwtwq vlrvvatvyl iwlawklata ggvqdqqvkr pmgfwaaaaf
      121 qwvnpkawvm avgacstyvl hgnlwlnvll lagifgvvnl psvamwalcg salrrwlarp
      181 rvlrafnigm avlllaslwp ilga
//
LOCUS       WP_010814751             423 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [Cupriavidus].
ACCESSION   WP_010814751
VERSION     WP_010814751.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..423
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=46304
     Region          31..423
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 matrapaasa rtaapsraks gkgrkaptqy ifewegkdrk gktftgelra enqaevtatl
       61 rkqgltivkl kkrkaargrk itekdiayft rqlstmlkag ipllqsidii arghvnpnft
      121 qllsdirfdi eagssmaaaf rrhpkyfdtl ycnlidageq ggildsller lslymektia
      181 lkgqiksami ypiavltvaf avtvilmlfv ipafkgvfss fganlpaptl lviaisdffv
      241 qywylvigap vagisfylra lkksekvqra tdrallklpi fgslfrkavi arwtrtlatm
      301 faagtplves mesvagaagn wvyydatrei eqsvrigtsl tnamqathvf dnmvlqmtqi
      361 geesgaldnm llkvaefyer evddavaais sliepliivv lgvliggmvv amylpifklg
      421 qvv
//
LOCUS       WP_010814806             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Cupriavidus].
ACCESSION   WP_010814806
VERSION     WP_010814806.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..267
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28961
     Region          1..262
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mdkfvsienv gqtfktrkgp fvalrdinlh iaegefitli ghsgcgkstl lnlvaglatp
       61 ttgalicagr eiagpgpera vvfqnhsllp wltcfenvyl gvervfaase skpqlkarth
      121 dtlalvglth aenkypheis ggmkqrvgia ralamapkvl lmdepfgald altrahlqde
      181 likivartrs tvvmvthdvd eavlladrii mmtngpaati geilkvelpr prdrvaladd
      241 kayhacrtav ldflyrkqrn palqeaa
//
LOCUS       WP_010814808             291 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Cupriavidus].
ACCESSION   WP_010814808
VERSION     WP_010814808.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..291
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31378
     Region          11..269
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msaiehllkp hvrdlgdftv rrllpaaatq tvgpfiffdh mgpvqlppgg gadvrphphi
       61 glatvtylfe geiihrdslg sdqairpgdv nwmtaghgiv hserspehvr pagarlhgiq
      121 twvalpqehe gaepsffhhp aatlprierp gvrmvviagd afgqvspvkv fsrtlyvaie
      181 ldagasveip adhaergiyp vdgavaldge plpaehmvvl tpgqpatlta ttpsrvmllg
      241 gdptdghrfi ywnfvasskv aieaaaqrwe ddqfphvpge teriplpprk p
//
LOCUS       WP_010814830             137 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Cupriavidus].
ACCESSION   WP_010814830
VERSION     WP_010814830.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..137
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14123
     Region          35..137
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mnffadynnl alialavvsg gllawpaisr strgktvnta tatqlinkrg avvvdirepa
       61 eyakghlpqa ksapladlps raaglakdka apiivvcqtg qrsgkaqaal keagyseiya
      121 leggiaawqq aglplvk
//
LOCUS       WP_010814857             178 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TlpA disulfide reductase family protein
            [Cupriavidus].
ACCESSION   WP_010814857
VERSION     WP_010814857.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..178
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19247
     Region          46..159
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mttaapatks srkpwpivaa vvvlallgwf gyralapant apaatftlls gekvstadlk
       61 gkvyminfwa tscatcvkem pdmvrtyeqf kgkglefvav amnydppmyv mnyartrglp
      121 fkvamdsdgt aarafgnvql tpttfvvdkd grilkryvge pewdalhkll dgalaksa
//
LOCUS       WP_010814861             399 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: D-alanyl-D-alanine carboxypeptidase family protein
            [Cupriavidus].
ACCESSION   WP_010814861
VERSION     WP_010814861.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..399
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43488
     Region          39..387
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mlnrattrls safapaaiaa aivlaaapaa vlaqgvpmpq vaakswmlyd vtsgqalasq
       61 nadariepas ltklmtayla fealkekrlt ldqavvptsv vlkvksdesr mfiepnkpvt
      121 vqdlllgliv qsgndaalal aeavggseeg fvammnreaq rmgmknthft ntdgipdpnh
      181 yttavdlatl ttrlikdfpe yyamysqkef tynkirqpnr nrllyidptv dgvktghtks
      241 agyclissak rplanvpdgs rrlisivigt tteqvrtqes lkilnygfqf fdtlrlydkg
      301 qvlatpdiyk gksgtvkigv qnetfvtvpk gtggrlkpvl erqelliapi sagqqvgmvk
      361 lmdgtnkvae fpvvaleevp eagffgrlwd tirlwfkrk
//
LOCUS       WP_010814872             416 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phenylacetate--CoA ligase family protein
            [Cupriavidus].
ACCESSION   WP_010814872
VERSION     WP_010814872.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 416)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..416
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44527
     Region          1..407
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mpehfdslet rapevreqal laalarqvah ardnapyfae mlggvdprll ssraalaalp
       61 vtrksdltar qralpplggl natplgklrh vfqspgpihe pdghdadwwr varamhaagf
      121 ragelvyntf syhftpagmm metgahrlgc cvfpagvgqt dsqvqalasl qptayagtps
      181 flklllergd elgtpctsla kalvsgealp pslrawfqar gvrvqqmygt advgliayet
      241 eggdgwvvde gvlveivepg gsrpmpeget gevvvtvlgn gdyplirfgt gdlsaivaes
      301 sqrpspcgrt nirlkgwlgr adqatkvkgm fvhpgqvadv lrrhpeiraa rlvvtgdpga
      361 dvmtlrceat redgdlqrav aeslrevmrl rgevafvaag slpqdgklie darsyd
//
LOCUS       WP_010814875             358 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Cupriavidus].
ACCESSION   WP_010814875
VERSION     WP_010814875.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..358
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38761
     Region          45..350
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mfyreagqfk tsyvadsqif pirqdrigfa vlmavafvai pfvgseywfs ailipflifs
       61 laalglnilt gyagqlslgt aafmavgaya aynfqlrveg mpvlltfvma glsaalvgva
      121 fglpslrikg fylavatlaa qffvvwaltk fpwfsnnsss gvitaqrldl fgfaidtplk
      181 kylfvlaivt vlalaaknlv rsatgrawms vrdmdvaaev igiplmrtkl lafavssfyc
      241 gvagalyafc ylgsvepdgf sldlsfrvlf miiiggvgsi lgsflgaafi lllpifldnv
      301 lpslaallhl pftnatvshi qlmvfgglii fflivephgl arlwqiakek lrlwpfph
//
LOCUS       WP_010814917             280 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Cupriavidus].
ACCESSION   WP_010814917
VERSION     WP_010814917.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..280
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29761
     Region          17..267
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 msqaphwshp ltacpqlvlr dvklrtgqrv lverltmtig agqlwciagp ngagkstlmt
       61 vlaglrhadg gsaeidgaaa aqiapavlar qraylpqavh dtfsmsvqda vrvgrhphls
      121 gwgwtgredd rivqeviram diealaardv ltlsggerqr aslaaalaqq aplllldepv
      181 shldlrhqil vleqlaalar agrhaivvil hdltlalrya thallmaedg ttlhgtaarv
      241 ltpehcsral rtaivsvtdg ahtalipdga appiphtrhd
//
LOCUS       WP_010814952             306 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Cupriavidus sp. GA3-3].
ACCESSION   WP_010814952
VERSION     WP_010814952.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..306
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33237
     Region          80..306
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mtdqaslarl aslpsqdpgf ydreynnran vpdnavhmar waqwsagvra rgayladlsy
       61 agedsrhaqd etldyfpaqr angalppllv fvhggyyral dkhdhsfvas alpalgvsva
      121 vvnytlvpav tvpeivrqvl rsvawlyrqa drlghdpdkl flaghsvggh lvamlmaarw
      181 pqlgaelpad lvkgglsvsg lydmeplrra aflqrdlrfs eddvarlspa ymppasgapl
      241 aiavgeleaa eyhrqhalir aawpakvahp aasdlvlpdc hhfnvlegfa spdgaltrav
      301 lrlmer
//
LOCUS       WP_010814958             302 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Cupriavidus].
ACCESSION   WP_010814958
VERSION     WP_010814958.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..302
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33155
     Region          27..300
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mdtvrifder arelplager leqlacratw segpvwlpde davlwsdipn drilrwsaad
       61 gmsvwrtgag ftnghalead gsllhcshgk raivrthrsg arlgedelvv shyqgrrlns
      121 pndivvkrdg tlwftdppyg ilsdreghra dpelrhnyvf rydpavgale vasdlieepn
      181 glafspdedv lyvsdtsaal rddghhhiva fdvvagrvla nprvfaviap glpdgfrvdr
      241 rgwlftssas gvqvfhpdgt rlahipvpek vgnlvfggae gdalfiaast slyrlrlgqr
      301 lt
//
LOCUS       WP_010814966             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Cupriavidus].
ACCESSION   WP_010814966
VERSION     WP_010814966.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..259
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28619
     Region          1..257
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msalsiqqvs rtfsnprggq tlalqpvdfe vrdndfvtil gpsgcgkstl lrivagldtp
       61 ssgrvlldgq pvsapgadrg mvfqsytlfp wltieqnvrf glrergmsaa eqkersdffi
      121 qrvglrgfeh hfpkqlsggm qqrtaiaral andpkillld epfgaldnqt rvlmqelllg
      181 iweasrktvl fvthdideai fmanrvavfs arpgriksei avdfphprhy tvkttpefsa
      241 lkarlteeir aeamasaeh
//
LOCUS       WP_010815054             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Dps family protein [Cupriavidus].
ACCESSION   WP_010815054
VERSION     WP_010815054.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..161
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=17961
     Region          10..161
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 makknemsvn igisdkdrkk iaeglsklla dtytlylkth nfhwnvtgpm fntlhlmfet
       61 qytelalavd siaeriralg ypapgtykey arlssiaeee gvpeatemir klvegqeavv
      121 rtarslfpvi daagdepsad lltqrmqthe ktawmlraml a
//
LOCUS       WP_010815170             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Enterococcus faecalis].
ACCESSION   WP_010815170
VERSION     WP_010815170.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..228
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=26850
     Region          41..228
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mdckncaspi rleitlkmll rfkkcarpsl cqhcqakfqk lpmtgtcfgc srvsqerycf
       61 dcqrwqllyp eysfhnaalf hydegmqewm erykfqgdyr lrtcfneein syfrqqsady
      121 iipvplsekr mqergfnqvi glleaadvpy spflirkeen vpqskktrke rmrlqqpfai
      181 qkenqkklkn csvilvddiy ttgrtlfhaa avindcypks lntftlar
//
LOCUS       WP_010815192             370 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Enterococcus].
ACCESSION   WP_010815192
VERSION     WP_010815192.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..370
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42771
     Region          235..357
                     /region_name="FUSC_2"
                     /note="Fusaric acid resistance protein-like; pfam13515"
                     /db_xref="CDD:433273"
ORIGIN      
        1 miviyffstk sqqffayvwa ifpviafflv sfytldflfs psylimvpvf timfkinykk
       61 dysfvalpkm sirqfvisfl afiasssfsw siilnssvtf livylfyssa tpmryhsylm
      121 mftfcqliqv kgntflmqsq vvafliglfl laltlnawwq tglsqltslk srghvrffks
      181 iqlnmkqqkl avinfwhdlq qtffgitsfk qflespdekv qrfrlairms ftitlsfilm
      241 wsvggikiiw ipmnvflllh pvkaemntri ktrfwgtllg cflslfvvnw lqlplthlvv
      301 ssligifvya lkpgtvlqvt matifglcla tislrgmyaa elrvsfvlla ifvvclidlg
      361 lfvyqrilrf
//
LOCUS       WP_010815262             229 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Enterococcus faecalis].
ACCESSION   WP_010815262
VERSION     WP_010815262.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..229
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25495
     Region          47..222
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mrnemmhrpv vkpelveymr tkqkklpgel geveaeanea gvpiiphetv vflqfllgql
       61 kpknileiga aigfssslma qfvgedghvt tidrfdvmik kakktyqrld leekvtlleg
      121 qaaeilpmle gpydfifmds akskyieflp eclrllpvgg vlmvddvfqa gtildpaeev
      181 pkknraihrk lnqfldvvma hpdltstlvp lgdgvilitk eketiilds
//
LOCUS       WP_010814956             286 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome b561 domain-containing protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010814956
VERSION     WP_010814956.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Tsubaki,M., Takeuchi,F. and Nakanishi,N.
  TITLE     Cytochrome b561 protein family: expanding roles and versatile
            transmembrane electron transfer abilities as predicted by a new
            classification system and protein sequence motif analyses
  JOURNAL   Biochim Biophys Acta 1753 (2), 174-190 (2005)
   PUBMED   16169296
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10171754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..286
                     /product="cytochrome b561 domain-containing protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140575 - transmembrane
                     monodehydroascorbate reductase activity [Evidence IEA]"
                     /calculated_mol_wt=30841
     Region          52..210
                     /region_name="Cyt_b561_FRRS1_like"
                     /note="Eukaryotic cytochrome b(561), including the FRRS1
                     gene product; cd08760"
                     /db_xref="CDD:176490"
     Site            order(57,100,133,183)
                     /site_type="other"
                     /note="putative heme binding sites [chemical binding]"
                     /db_xref="CDD:176490"
ORIGIN      
        1 mppalpaavr wilplgltlc lcilgaraap gwpaqwlsrp isgtaaahhv vlwvawhgrl
       61 mvlswglllp lgilvarffk vtpsqawpav ldrktwwrah lwmqgsgval msvgvllvlg
      121 hgggmpdtla rwhhlggwal vacaalqvgg gllrgskggp tsnclrgdhy dmsarrvvfe
      181 wlhkvigwss lplaiatigi glaladaprw mplllgawwl tlaalalalq ragfcidtyq
      241 aiwgpdprhp gnrrrpigwg itsfpsqpas ssgthrpqaw paehkd
//
LOCUS       WP_010815591             140 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CsbD family protein [Bacillota].
ACCESSION   WP_010815591
VERSION     WP_010815591.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10527613
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..140
                     /product="CsbD family protein"
                     /calculated_mol_wt=14587
     Region          24..76
                     /region_name="CsbD"
                     /note="CsbD-like; pfam05532"
                     /db_xref="CDD:428512"
     Region          81..138
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mkksgiivgf latafglavv nkmhkmntnk dsvkgkakev agkvigneqm qaegtfdqvi
       61 gaskevledl kqsisgiagt gtsekvsgka keavgnvtgd dkqkaegfle qatgqakeai
      121 sntkekaedv agdikdefer
//
LOCUS       WP_010815650             556 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Lactobacillales].
ACCESSION   WP_010815650
VERSION     WP_010815650.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillales
  ORGANISM  Lactobacillales
            Bacteria; Bacillati; Bacillota; Bacilli.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Lactobacillales"
                     /db_xref="taxon:186826"
     Protein         1..556
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=64310
     Region          5..415
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mekfacmylr lsredgdste snsisnqrqi iksyardndi kvvaeyvddg fsgsnfdrpk
       61 fkkmiqdlee kkfktiivkd lsrfgrdyie sgkylqkifp ekgirfisvn dnydsenadv
      121 sdthlilpir nfindsycrd ismkvksske ikrkngefig afapfgymkd sknkhklvvd
      181 tevshiieri fnmkidgyss kaiadflnsi gcvtpskhke nsgdnhttgf ivkdskwdak
      241 mvnriitnkv yigvleqgkt rklnykskre vevneedwiv indshkpiis ksiyalankm
      301 mlrdvkqsad iphilsgmly ckdcgssmvr rkvkskngyn ifyicshynn kgdctrhsik
      361 edylmdmtlf alkdylkkyn ellsqvnkld vskvtfnidf eslnsekrky erlrqslymd
      421 ledelitsee ferfrknyli kireiekqia tkknilanlq ekmknkdslv seivptdlss
      481 lnrltivsfi drieigense infvfnnlet vnllktlike esesksevrk nlisinkvfg
      541 nalenktpmq lvggvl
//
LOCUS       WP_010815703             472 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Enterococcus faecalis].
ACCESSION   WP_010815703
VERSION     WP_010815703.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..472
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53203
     Region          2..457
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mfdivtlari qfamttvfhf ffvpfsigla lvvaimetmy vvkkeeryrk makfwgnifl
       61 lsfavgvvtg iiqefqfgmn wsdysrfvgd ifgaplavea llafflestf lglwiftwdk
      121 mnpkvhvtfi wlvvfgsmms afwilvansf mqhpvgyvin ngraemvdfv avisnpkvwy
      181 efshvimgaf tlggmavvgm aafqllkkrd isfhkasmri glwvtlfgsi gvllagdlqm
      241 kaliegqpmk faamegayed sddpaawtli awaderehkq vfgidipyml silsynklsg
      301 svdgmdtvnk rlvekygddk nyyppvntlf wsfrimagfg almllvaalg lfftrkkkps
      361 lyekkwmlwi valctfapfl anttgwlvte lgrypwtvyg lftieqsvsp nvsvaslits
      421 nviyfllfag lgsvmvylvi lelrkgpdye akklakenep aldpfdkgvf ge
//
LOCUS       WP_010815751             198 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecalis].
ACCESSION   WP_010815751
VERSION     WP_010815751.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..198
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22669
     Region          3..132
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,66..67,70)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(65,113..114,116..117,121)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(71,76..77,109,112..113,116..117,120,123)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94..96,109..110,113..114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94,114,117,121,124,128)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(122,128..129)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 msiygysrvs tsnqdyktqi qklekagsek ifsekytgtk kegrkeleel lsivkpgdkv
       61 lvtkidrlar sivdlnsiis slnnsgvtit fldnaltfep nksdsmqtlm mnmlgsfaqf
      121 erdlivtrtq egkqwhrann knyregrpkr vlndkykhal elmetnsmre verktgisls
      181 tlkrikkqak eeqllsek
//
LOCUS       WP_010815766             236 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010815766
VERSION     WP_010815766.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26545
     Region          9..234
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mveanntnqp lielrdinkf ypvgkekihv lkelnltihq gefilimgks gsgkttlmni
       61 igfldrltyg syhfsgtdvs klsenkksaf rneylgfifq qfflinslnv sqnvqlpcvy
      121 egkksraekk aiaekylkiv gletkakskv telsggqqqr vaiarslvnd pllimadept
      181 galdsetgte imellkelne qgktivmvth dedmkkyasr vihmkdgrfl eeevir
//
LOCUS       WP_010815877             438 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus faecalis].
ACCESSION   WP_010815877
VERSION     WP_010815877.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..438
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=49174
     Region          14..364
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(17..18,21..22,57,60,116..117,172)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(114,117,201..207,236,263..268,295,324..328,330)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mkfdyskepr rdvlcidvks fyasvecver gldplktmli vmsgadnagg lvlaaspmak
       61 kvlgisnvtr kdevpdhtdl livpprmnly mkrnseinnl lkrfvadedh svfsvdesfi
      121 ditaslryfn cdtayrlari iqrviynhmg lyvtigigdn pllaklaldn eakntpdfva
      181 ewryedvqek vwaispitef cgigkrmtac lkmsgiesiy dlahanpyll khrfgvmglq
      241 lfahawgidr sflgekrqva keksfgnsqv lprdyarkyq ielvlkelsd qvatrlrnsn
      301 yqtecvsifv gyskeqvdgl grsgwrkqlk iarsnntkvl tehvlklfre nyvpgmdirn
      361 lgvsfgklvw dttlqlnlft ppeeqiinpq ldflidkirr kfgfktliha sslldgatav
      421 nrsglvggha ggnvglgg
//
LOCUS       WP_010815969             235 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Enterococcus].
ACCESSION   WP_010815969
VERSION     WP_010815969.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..235
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26666
     Region          4..234
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mvqnipiyiq ihdkikedie kgvwsigdrl pserelalkf dvsrmtlrqa vqtladegil
       61 erkigsgtyv arkkvqetmt gttsfteitl sqnrvpssrt vsyfvakpss semeklqlgp
      121 edsilrmeri rfaddipicf evasipyslv sqygkseitn sfyktleaks ghkighsnqt
      181 isavqaseqi aeyleikrgd ailrvrqvsy fenglpfeyv rtqyagsrfe fylek
//
LOCUS       WP_010816000             901 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus faecalis].
ACCESSION   WP_010816000
VERSION     WP_010816000.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 901)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..901
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=97108
     Region          10..899
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mseekktqls eafyaqddtv vlekmntttd glsaqeaqkr letygenvld egkkkslavk
       61 ffeqfkdfmi ivllaaavis avfshdvvds iiilvvviln aifgviqeak aeqaiealke
      121 msspnanvrr dghvitvksd elvpgdivll eagdvvpadl rlleanslki eeaaltgesv
      181 pvekevtile gtdigigdri nmaysnsnvt ygrglgvvvg tgmntevgki agmlaseqet
      241 etplkqnlnq lgkmltiail viavvmfvvg mmngrswidm lltsislava aipeglpaiv
      301 tiilalgtqk makknaivrk lpavetlgst diicsdktgt ltlnqmtvea lytdgqvlsa
      361 steipadnma lkimnftndt kiaqdgslig dptetalvqf gldhafnvte kvaaeprvae
      421 ipfdsdrklm ttvhelktgg flvsvkgapd ellkrcteil sngetsplde tkrqeilktn
      481 tslakqalrv lgmaykyvet ipaemsselv ekdltfaglv gmidperkea adavkvakea
      541 girpimitgd hrdtaeaiaa rlgiikeddd davitgaeln elsdekfaqv vghysvyarv
      601 spehkvrivk awqqegkvva mtgdgvndap alkaadigig mgitgtevsk gasdmvladd
      661 nfstiivave egrkvfsniq ktiqyllsan lgevltlfia tmlnwdtllp vhllwinlvt
      721 dtfpaialgv epaerdvmsh eprgkksnff sggvlssvvy qgitqgaltl ivykmsimfp
      781 ahtaantnls aqalydlqhg daltmafatl gliqlfhafn vksiyqsifk vglfrnksfn
      841 ygilvsflll aativipgfn dlfsvthlda yqwaivagts faiipiveiv kffqrkagkg
      901 a
//
LOCUS       WP_010816028             266 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Enterococcus faecalis].
ACCESSION   WP_010816028
VERSION     WP_010816028.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..266
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29023
     Region          1..266
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mrqrvitaiv aliifipiiw yggfaieiaa valavvgvye lfrmkgltll sfegvlsalg
       61 avflviptik wlnflpemqt nfilfyvtvm lllgasvisk ntytieeagf pvivslyvgm
      121 gfqnfisars agfevllfal fivwatdiga ylfgrrfgrh klmpdvspnk tiegalggil
      181 savvvaalfl vfttnkglfp ypmpvilvlt vlfsivgqfg dlvessikrh ygvkdsgnil
      241 pghggildrf dsllfvfpim hlcglf
//
LOCUS       WP_010816102             267 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus faecalis].
ACCESSION   WP_010816102
VERSION     WP_010816102.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..267
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29695
     Region          4..263
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,193,215..217,219..220)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mkkliaidld gttlnaqsli spkteqtlkk aidnghyvsi atgrpyrmsh qfyqqlgltt
       61 pmvnfngalv hipekkwdle seanierdlv fdilaqkkel qldfvaaenk etfyidtldg
      121 fdpkffaska tldnlltakn lrtnptsmmv rttpnqaekv adtltkqygd yidvrtwggp
      181 mpilemvakg iqkahgvdqv anflsvkpad iiafgdehnd eemlsyagwg vamnnatdki
      241 ksvandvtek tndqvglady lenyldl
//
LOCUS       WP_010816225             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010816225
VERSION     WP_010816225.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..256
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28424
     Region          1..256
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mttegliall ekkrndlski enqvldyilt hmteissqti yevaqalfvs tatisrtakh
       61 lgyrgfqelk yaivqsvqse stesdsrsfq aitqqlianv qdsfqqmdea kvaemlkmie
      121 cantievfgv ggsfpictdf arkltflgkk ayarsdwdeq aaavknldgr dlaifvsytg
      181 etkgilayar vaqeqqvpmi slistkgstl eklstttlfa kgttryhqrv dlssriavic
      241 lfdtvllmya eakqpr
//
LOCUS       WP_010816382             271 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Enterococcus faecalis].
ACCESSION   WP_010816382
VERSION     WP_010816382.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..271
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=30239
     Region          5..270
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mnvylflalf fiiigilsys ffiepnclvi hknqikvtes gktlrivqls dihlkknysv
       61 kalkqivekt ntlqpdivvf tgdlfddyar fgieiqdevs qlfrkinapy gkfaiygnhe
      121 ysgldtnfye tileaadftv lkntgkllpv shrislyvag ledslygqtd laaalvnrpt
      181 gtptlllthe pdiadsavnk nidlilaghs hggqirlpff tyknqlakky thglyhlede
      241 tplivhpgig ttkisarfgv lptielielt i
//
LOCUS       WP_010816386             332 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Enterococcus].
ACCESSION   WP_010816386
VERSION     WP_010816386.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..332
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37046
     Region          1..252
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mihlgvigtn wishqfvaaa letgaydlta vysrklataq efgsrygdve yaidletffg
       61 iahmdtvyia spnslhfeqa kqailakknv ivekpafstp demaeiiela nknrvyffea
      121 arniheqsfq kiaellplkn qilganftym kyssrydqvl egkepnifsp hfsggaladl
      181 gvylvyaalg wfgvpkeshy faskiatgvd glgtiilryd qfdvtlntgk isdsfapsei
      241 yfengtlild svnaissaey hdraheerdv idiqvadnpm ieeardfaav lnnptdkywg
      301 tkyeewvela rnvnkvvtdl rhsagiifda dk
//
LOCUS       WP_010816432             286 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Enterococcus faecalis].
ACCESSION   WP_010816432
VERSION     WP_010816432.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..286
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=31091
     Region          5..281
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mnkekiallv dsgtdvpeal vkqygmyvlp lqiiypekty tdkvditpee vyqrlekeip
       61 stslpdgati qaifdrikea gyekvlavti ssglsgtynv vrllgeqteg ldvfvldtkn
      121 igigagiqai raaelietgl gwqelqqklt eevanakvff nvatleylqk ggriglvtsi
      181 lgnalklnpi iscneegiyy tvaksrgrkk sldktfelvt nfigeaprfr lavahgaaee
      241 eakammerlk aafpqaeeiy fgtispalvv htgpgllgvg iqllnd
//
LOCUS       WP_010816451             202 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [Enterococcus].
ACCESSION   WP_010816451
VERSION     WP_010816451.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..202
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22511
     Region          2..164
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mkkiiglvgt nseqstnrql lqfmqhyfaq eadielveiv dfpmfnkped kvlpeivktv
       61 aekieaadgi iistpeydha vpaslmnals wlsygifpfv dkpvmitgas ygtlgssraq
      121 ahlrqildap elkarimpss efllahslqa fdennalkds eqidklaglf adfcvfieit
      181 eqlkhahaqn kkeaenfswe ti
//
LOCUS       WP_010816595             640 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Enterococcus].
ACCESSION   WP_010816595
VERSION     WP_010816595.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..640
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71373
     Region          326..515
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mklsikkffe vflessways rpiltfdtrq nwfalvlsii ianavgavlt ivfpfafvlv
       61 nvgsflgtvi cvlprhgspq rsaingilmi figaslgill qsssifiill fvlglyfsgi
      121 vrnfsiglyi rclfgtisll agaqlkgnls igqsfeglga iilgmsilcl iyclyskpqn
      181 nearklvadl yeqlyllaqg kparyvhfri kvresvetmp wvnhqktpwi yplvsqadai
      241 agsldstnaa enlpalkail lflkgeqltl plqefalant eiksailliq neqsfkkisf
      301 ksflptkegl aeakeilhsy kgssarfair laltglvchf cslilnymyp lplanhefwv
      361 visgclmvmp gyhgtlgkit srtigsilgg clgiflsqli anltnlnplw pmllscllvi
      421 lyetvrklsq aflmlsvttw ltftlggssa gytrvfdvii galiafvmff ifptwhsqvl
      481 rkninswskt issillalin eettlpsdaw vlayrvqrrv nysiqeivle spiysndasa
      541 eslmqqkqln dqllemqtam eelllelmkt qhylkklapv kpdtlntell nysqqilslt
      601 npqnnrlinq skqsiyfpqi eqslvilkns tanfflanik
//
LOCUS       WP_010816563             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Enterococcus faecalis].
ACCESSION   WP_010816563
VERSION     WP_010816563.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..228
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=26970
     Region          41..228
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mdckncaspi rleitlkmll cfkkwarpsl cqhcqakfqk lpmigtcfgc nrvcqerycf
       61 dcqrwqllyp eysfhnaalf hydegmqewm erykfqgdyr lrmcfneein fyfqqqsady
      121 iipvplsekr mqergfnqvi glleaadvpy spflirkeen vpqskktrke rmqlqqpfai
      181 qkenqeklkn csvilvddiy ttgrtlfhaa avindcypks lntftlar
//
LOCUS       WP_010816640             370 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Enterococcus faecalis].
ACCESSION   WP_010816640
VERSION     WP_010816640.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..370
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42879
     Region          235..357
                     /region_name="FUSC_2"
                     /note="Fusaric acid resistance protein-like; pfam13515"
                     /db_xref="CDD:433273"
ORIGIN      
        1 miviyffstk sqqffayvwa ifpviafflv sfytldflfs psylimvpvf timfkinykk
       61 dysfvallkm sirqfvisfl afiasssfsw siilnssvtf livylfyssa tpmryhsylm
      121 mftfcqliqv kentflmqsq vvafliglfl laltlnawwq tglsqltslk srghvrffks
      181 iqlnmkqqkl avinfwydlq qtflgitsfk qflespderv qrfrlairms ftitlsfilm
      241 wsvggikiiw ipmnvflllh pvkaemntri ktrfwgtllg cflslfvvnw lqlplthlvv
      301 ssligifvya lkpgtvlqvt matifglcla tislrgmyaa elrvsfvlla ifvvclidlg
      361 lfvyqrilrf
//
LOCUS       WP_010816648             439 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            faecalis].
ACCESSION   WP_010816648
VERSION     WP_010816648.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..439
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46539
     Region          23..429
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mdtkqlntqq qtetpngkaa vlglqhllam yagavavpll igtglnfdsq qmtylisidi
       61 fmcgvatllq ltvnkffgig lpvvlgcaiq avaplimigt nkgvgaiygs iiasgifvvl
      121 iagffskikr lfpplvtgtv itvigltlip vavekmgggl atdknfgdpk nlllafvtia
      181 liivvqvwgr gfiksiavli glvggtilaa flglvdlspv gqatwfhfpq pfyfgkptfd
      241 lssivlmiii sivsmvestg vyfalgditg kkigeddlrr gyhaeglavi lggifntfpy
      301 tgfsqnvglv qlsgiktrrp iyfsafflii lgllpkigam aqiipepvlg ggmlvmfgmv
      361 avqgmrmlsk vdysndknll iiaisigfgl gfnimptlfn kvpetvsmft gngivmssit
      421 aiilnllfng lketsesne
//
LOCUS       WP_010816724             252 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010816724
VERSION     WP_010816724.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..252
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27074
     Region          1..252
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mdlavnnlsl ffsamlvvva liistkeklg ftkdiiisvi raviqlvavg yllkyvfqvn
       61 nliltlimvl vivsnaafna kkrsqqlqkg flisfiaigc stgitigili fsgsikfips
      121 qiipisgmia snsmvaiglc yrnldtlfqn qrqavmekla lgatiklasl piiqqsvktg
      181 maptidsakt vgivslpgmm sglifagvdp vhaikyqimv tfmllsatsi gsvittylay
      241 kgyynqqkql vv
//
LOCUS       WP_010816795             221 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Enterococcus].
ACCESSION   WP_010816795
VERSION     WP_010816795.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..221
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25760
     Region          134..208
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mkimvitknv laetafqnrl qhldhqvfct tcligeikes hlfyrkfdai ilsetiprke
       61 qylylkelar vktplflrse diptseelsi syqygilnwl rldatldtlr enlflaelnk
      121 piqredekln vegikltate rallavlyst pkehlpmerl ckliydteet annrkkmtkq
      181 ltklnkkiqv ggfkkqgiqn trykgyklhp qllpyigelf t
//
LOCUS       WP_010816851             181 aa            linear   BCT 01-JAN-2025
DEFINITION  cysteine hydrolase family protein [Enterococcus faecalis].
ACCESSION   WP_010816851
VERSION     WP_010816851.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..181
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20154
     Region          3..181
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mkalisidyt ndfvatdgkl ttgaagqaie talvqqtkhy fdngdfvvfa idghdpldry
       61 hpenklfpph nvlgtdgrnl fgslgdfyqa hkneasvywm dkrhysafsg tdldirlrer
      121 gitelcltgv ctdicvlhta vdaynlgyql miperavasf deqghewalr hfkqtlgati
      181 l
//
LOCUS       WP_010816861             506 aa            linear   BCT 01-JAN-2025
DEFINITION  gluconokinase [Enterococcus faecalis].
ACCESSION   WP_010816861
VERSION     WP_010816861.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..506
                     /product="gluconokinase"
                     /EC_number="2.7.1.12"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046316 - gluconokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /GO_process="GO:0046177 - D-gluconate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54970
     Region          6..489
                     /region_name="ASKHA_NBD_FGGY_GntK"
                     /note="nucleotide-binding domain (NBD) of gluconate kinase
                     (GntK) and similar proteins; cd07770"
                     /db_xref="CDD:466790"
ORIGIN      
        1 meklaigvdv gttqakavaf qangtvvass yvrypliqet egmaeqdpet lfqavvncir
       61 tvtqqvknqp iglisfasam hgliamdaqg rpltqvitwa dtraadyaea lketpaaqlf
      121 yqltgmpihp maplykirwl qenqpavaqs aakfigikdy ifyrffgeyw tdyssasgmg
      181 lfnihtrqwe ssilaylsie eeqlpkvaps tfifpalaps wqemlgveee tvlvlggadg
      241 plsnlglgal gtgvatltvg tsgalryive epflhpqget fcfaldeqhw viggassnga
      301 valdwasqti faeerqqaiq ngtnfydpim akiatvpaga ngllfhpyll geraplwnae
      361 asasflglrk nhhaghlara vvegicfnlk tiledlkqlg gpvqeiratg gfadspvfrq
      421 imadvlgetl sftdsteasa lgavllgwqg lgqlpnlqaa aqqvlihetv tpradqllvy
      481 qelypvfqet qqvlaqsyqk laefrk
//
LOCUS       WP_010817004             406 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Enterococcus faecalis].
ACCESSION   WP_010817004
VERSION     WP_010817004.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..406
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43814
     Region          2..403
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkkpsmitqi aiafvvgilv gllipasgny lkivgdvflr lmqmaipili lgqivqavgs
       61 inpkeltslg grtiavfgis slaaalwgvl mavifnpgyg vkmtgfqdas ikaqeisitd
      121 tilnfvpkni fdsltqgsii qiivfalffg lalnkylqsh petqlfqiiv dfneviitvi
      181 rfvmylaplg ifaliastis hlglqiilpl vkyllvyglg tilflgiwil vitlyckvsp
      241 lrliknmknm svmalattss aitlpvalee tetklglskr itnlvlplgm slnsngsamh
      301 maftvmtiaq myqlefditk miylaitatf vslanavvpg aglvslaviv pqmglpiesi
      361 aifagvewfv gmlrtilnvn sdvysailva ksvdeidytv fnssnk
//
LOCUS       WP_010817074             250 aa            linear   BCT 01-JAN-2025
DEFINITION  Fic family protein [Enterococcus faecalis].
ACCESSION   WP_010817074
VERSION     WP_010817074.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..250
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29648
     Region          66..>240
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mtykllkvdf yknrdsfekk yqerlnfdst lqtklfihpf dkeerktket yelfyvpllq
       61 hsvlqekimk nsqeimryih klpkivqkni ffyqlieeiq stneiegvks srkdiskvlh
      121 klnansterf qgivnmykgi vtdkmlkiet lgqfreiyde lfkadiqeed ypdgllfrks
      181 vvyisdkdkv vhqgssnees iiadleklil fmnqsalpsl lkccishyyf eyihpfydgn
      241 vpsrhllrta
//
LOCUS       WP_010817250             401 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YdcF family protein [Enterococcus].
ACCESSION   WP_010817250
VERSION     WP_010817250.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..401
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45649
     Region          219..369
                     /region_name="DUF218"
                     /note="DUF218 domain; pfam02698"
                     /db_xref="CDD:460654"
ORIGIN      
        1 mqfygdltfl gvyllglffi pswrkkkkeh dwlpwmfgwt vfmffsyvly leiirgtaff
       61 lipiaffglf alfyfkekrr llngtlfnif lvvlatylgi tairtnnyfl itlaiiaila
      121 ilialalgiy aliiflywna vvvmrkegrs lgnlltllla igltllliyn fffqsllptw
      181 lslpltiapf iltyfafvfy nfltvstlyq fnqpkytqdy ivvlgsglin geivppllqa
      241 rinkaiqfyk aqnratlnpp kivmsggqgp dellpesvam kmyaltqgip dddilveahs
      301 kntlenmrfs ketmiedfgn anfqaifttn nyhlfraglf armaglkadg igaktafyfl
      361 pnafirefia ivvmykrrhi ivcglaaigm vmlfltglii q
//
LOCUS       WP_010817316             217 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Enterococcus].
ACCESSION   WP_010817316
VERSION     WP_010817316.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..217
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24126
     Region          127..212
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 metvvrkrwl fgmqllgfli ldqiplmmvs vvqvstenfl frfvsglvav glgayfvylf
       61 vaflkkkkli twtflgiket lpvvllglvi ifcvgifgdf llrleglett snqqsveeiv
      121 qsipkglili fagvigpife egifrvgiqa ffkpaskigi lvssilfalv htptdigsfi
      181 iywgmglals wvylrtgrfe aavlthfiwn vigilml
//
LOCUS       WP_010817397             640 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Enterococcus faecalis].
ACCESSION   WP_010817397
VERSION     WP_010817397.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..640
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71503
     Region          326..515
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mklsikkffe vflessways rpiltfdtrq nwfalvlsii ianavgavlt ivfpfafvlv
       61 nvgsflgtvi cvlprhgspq rsaidgilmi figaslgill qsssifiill fvlglyfsgi
      121 vrnfsiglyi rclfgtisll agaqlkgnls igqtfeglga iilgmsilcl fyclyskpqn
      181 nearklvadl yeqlyllaqg kparyvhfri kvresvetmp wvnhqktpwi yplvsqadai
      241 agsldstnaa enlpalkaiq lflkgeqltl plqefasant eiksailliq neqsfkkisf
      301 ksflptkegl aeakeilhsy kgssarfair laltglvchf cslilnymyp lplanhefwv
      361 visgclmvmp gyhgtlgkit srtigsilgg clgiflsqli anltnlnplw pmllscllvi
      421 lyetvrklsq aflmlsvttw ltftlggssa gytrvfdvii galiafvmff ifptwhsqvl
      481 rkninswskt lssillalin eettlpsdaw vlayrvqrrv nysiqeivle spiysndasa
      541 eslmqqkqln dqllemqtam eelllelmkt qhylkkltpv rpdtlntelf nysqqilslt
      601 npknnrlinq skqsiyfpqi eqslvilkns tanfflanik
//
LOCUS       WP_010817432             577 aa            linear   BCT 01-JAN-2025
DEFINITION  terminase large subunit [Enterococcus faecalis].
ACCESSION   WP_010817432
VERSION     WP_010817432.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..577
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67414
     Region          1..550
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 midmtvnyad kfaksvrrhk erypksihla vkrynkwkkr kdiffdleka nlmlsftesf
       61 ykhstgewsg qpleledwqk fyfsniygwq kwsdkwqrnv rvirksylqv pkkngkslme
      121 gapilygmyg egvkgaqfyc laadfdqaqn vanplatvie ndndlldgtr vyrkekkvtt
      181 isyaffeddf kyqnnlrvls krekvdgknt yivvadevhe wedtsrydgl ksgqaaqpep
      241 lflvcstagk nsgalgvqiy qdskhileed ndddwfimiy epnkgynwed ekvwemvnpn
      301 lyvsfditfl rgefkdalrn pfrkaeflsk hlnvfvnyae nyfdkeqidn clvddlgdit
      361 geqvaigidl srttdltcvs iniptfndag esiikikqmy fvpthnieek eklrnvpyqy
      421 yaeqgfvtlc egrtvdydlv ynyvidmynk yeldiiqiny dpamseklve rfemegfnta
      481 evgqypsvmn emlddfeilv dngrvqtdnp lfifctnntr vvtniqsqka pskrkspehi
      541 dgfvafligh kdsmdlmvev gseeeyeeyi rqlynrk
//
LOCUS       WP_010817748             213 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecalis].
ACCESSION   WP_010817748
VERSION     WP_010817748.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..213
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=24611
     Region          3..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,65..66,69)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(64,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(70,75..76,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94..96,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..195
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(148..150,190..191,193..195)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mtkigyirvs sidqnldrql lemeklqvek ifqekisgkd tnrpefqkll ryaregdilf
       61 fdsldrlgrd yddiketvly frnnnievnf ldapflnfnt gndlldkamf dmflsllsyi
      121 aqnerekird rqrqgiaaak akgiykgrpa vytpdspdpq kqviyhnivs mltadepvak
      181 iakqnhvsre tvykikrklk ssvsesdskp ilk
//
LOCUS       WP_010817905             285 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Bacillota].
ACCESSION   WP_010817905
VERSION     WP_010817905.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..285
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31975
     Region          5..221
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 menilevkgl nksyqhfslq dvsfslpegc itgfiginga gktstlksil gltpkisgdi
       61 rlfglnmdtn ekeikerigi vlddggfyde lslsemkniv asaykswdnk vfqsylerft
      121 lnpkqkigtl skgmrmkyal alalshkael limdeptsgl dplirsqlld ilkefmeygg
      181 rgvffsthit sdldkiadml imidngkivf qeekdillds yrivkgdikd lniemeklfm
      241 nidktifgft aitkyadeik kimpnciier ptiedimlcn vkggk
//
LOCUS       WP_010817914             141 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Bacillota].
ACCESSION   WP_010817914
VERSION     WP_010817914.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..141
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=16723
     Region          <14..140
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mnrptspedv qkvfdcyckk ilkneainiq khyqrmndlq isfseltpeq laelstyddy
       61 stnydlykvm gydvkiknel lsealqelse eerfilllyg lgfndgeiad llkivrrtvn
      121 ykrqrgfekv rkrmeekqhe e
//
LOCUS       WP_010818087             447 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus faecalis].
ACCESSION   WP_010818087
VERSION     WP_010818087.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..447
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=48521
     Region          4..443
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 msfmdkfqsa ierllvplat klnaqrhica vrdafilsfp ltmagslmvl lnnvflsadg
       61 fmfkilqfdk lfpgivkfqa vfapvvkgsa difsilivfl iarnlaklme gddlltglta
      121 isvyfiiypd yfdnegvnyl tnqylgaqgl fvailvgllv gelmsrlaks dkleikmpeq
      181 vpsavarsfk vlipiiitti ffsvlnyfvk maapgglhel iynilqtplt rmsqslfsvl
      241 ilallsqslw amgihgpnti aairdtmfse agnanlldya ksgttwgapf pitysglata
      301 fseyggsgmt lgliiailif sknkesksia klslapglfn inemvifglp ivlnpiyiip
      361 fiiaplvnim igytavmilk imppvtigip wttpgplmpf lgtggnival fvgficlavs
      421 vliyspfvia ankaaiiede meneiqs
//
LOCUS       WP_010818141             752 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Enterococcus faecalis].
ACCESSION   WP_010818141
VERSION     WP_010818141.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..752
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85978
     Region          235..723
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mqgnnlfnng llqpkkppig qeqqkmtryh qlrlvfglvg vllypfailg siplliglav
       61 dkrdkaanvf dmdyesflkr nsivflsfsa vlfvinvfaf ilwiprgyls ayllfplnll
      121 htalrfnwet ivalligssg mgaiflafss fvakrkvisk ederkkvtes keyknrqknk
      181 feesqrftde qekeyqeave svdidkykel snqlllgmse fglsyimnfs efnqhalipa
      241 ttgsgkttll qllvqhavkf nfpvilidgk gardtlesmr eiakfydkev haftddgdmr
      301 ynpvehgndi sirdklvsla etesvfysga akallqvtiq lldefkgakv tlsgdtrtte
      361 tverslpfvq rfllprnvlh lfadailpnn pklfeievek kiqkpkkksv kegseippds
      421 dldkeekeed sqiknskfrn isqlgiaqke tetivlnpet ldldsyylll krnlrylptd
      481 ketgenikqk lferlfirye hkdspfylya tsealqtnin mlldselgkl fdtknaknvl
      541 dvqeivnqrk lvyvsfngli ykeyirtlaq mlvgdvnyfa semyrknvkr evlvifdepa
      601 sylnetfidm vnkgrgagvy giftpqtmad iaklgdklme qlvgnvntlf igktnekgea
      661 eywsetmgty qdidvtsvte qedgysdvgk sdwsgdrgtk rnvdrfkisp nkikelrtge
      721 fiiyrtaenv nlppqkvyvr nalewlqksn sk
//
LOCUS       WP_010818143             164 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010818143
VERSION     WP_010818143.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..164
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=19294
     Region          9..>50
                     /region_name="DnaJ"
                     /note="DnaJ-class molecular chaperone with C-terminal Zn
                     finger domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0484"
                     /db_xref="CDD:440252"
ORIGIN      
        1 mkfikdvttl eelkrvykkl alkyhpdmgg tdkemaqinn eyealfdklk nthtnkegey
       61 yqkettetpq ewqeiihkll tlkmenvsie vigaflwvsg ntkpykeelk alnmkwsnnk
      121 kswylapdgy kkrskkkydm tdirnmygsq vvkeeqvkqk tlta
//
LOCUS       WP_010818174             321 aa            linear   BCT 01-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010818174
VERSION     WP_010818174.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15747380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..321
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37636
     Region          <65..>97
                     /region_name="Cupin_2"
                     /note="Cupin domain; pfam07883"
                     /db_xref="CDD:462300"
     Region          95..313
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 myhfskeqvd hffsyletld cyikseegmi delesfknnq nrkiaalvcq ntqeiltyka
       61 pyirilyvlq gsititldgk kmtyeagcli lankwtvidy qpvkkhtmvi gfyfkpeyfs
      121 dsllnqiire pmlyrffves lsdeleqksh ycvyqfnpld dihfyvllll kqvvkmryfn
      181 nkvtkaafvl lvveisqmse tclqlnasdl sntvltkeil afiennvrta sltnvakkfh
      241 fhpnylsali kkqtgisysd wltnyrmnya knyleqtnls tqqiieevgy sdktfffkrf
      301 kehvgmtpge yrklivvske k
//
LOCUS       WP_010818236             260 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterococcus faecalis].
ACCESSION   WP_010818236
VERSION     WP_010818236.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..260
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28791
     Region          2..256
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mariisvanq kggvskttts inlgaalhft fnkrvlvidm dpqgnatdnf gfdidgtnvp
       61 tiyevlkdea siskailnyk gidvipadia lssaereftq vgsehrlkrv lqpiennydy
      121 iiidcppslg iltvnaftvs deiiipveaa yfslkglvkl netietvkey tnenltirgv
      181 lftkynerfn iskemnktan qisealnvni fdtyirrtit vdeaqaagsd lisfnkasta
      241 eddyiqftke flekvgdlne
//
LOCUS       WP_010818241             747 aa            linear   BCT 01-JAN-2025
DEFINITION  S8 family peptidase [Enterococcus faecalis].
ACCESSION   WP_010818241
VERSION     WP_010818241.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10141191
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..747
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=85413
     Region          263..516
                     /region_name="Peptidases_S8_Subtilisin_like_2"
                     /note="Peptidase S8 family domain in Subtilisin-like
                     proteins; cd04847"
                     /db_xref="CDD:173793"
     Site            order(269,299,349,366,401,484)
                     /site_type="active"
                     /db_xref="CDD:173793"
     Site            order(269,299,484)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173793"
ORIGIN      
        1 mtkknpliin gkvlaevgdt ptqggdskie erkfkrsfse aqkyvlpqit qlkkdiggle
       61 eynrirsiyf rvsyphqfla ktyqvssiyk dskvkligsc qwiddedkeg rsdflmgtee
      121 ninslkeiie stvvqvqqke irrideisll kptitigkdd teenlyelsf ysvidpkell
      181 kkfeelldtn pnnyevlqet ngvlfivakl tknelekikd fnplrasypv nnrdfisasf
      241 skenirnyyi sqdldkders klpwiglidg gvvtneeffs tveqvyesev npseeyiehg
      301 tsvasiilyg dleedghrel lpsfrlqsvr alpseldmef nlltvdrliq eivprfphik
      361 iwnlsigpqg pilddvvssl trildrlsye yniifviaag ntgtdsgfsr riqipgdsvn
      421 nitvsayyrf eektitaqys slgpgregak lkpdiidhgg llpvdpvyti ssygyflnkv
      481 hgtsfaaphv trklglilas ypelnvwqar allehslaln isskrdisid skgelnagee
      541 qllfsnedev rilytgniss kgyvvlplpl peettaksat itwtlvtktk vnpdcpdkyt
      601 eygieddfyp naekytfrhs ekssskdidv steegqelfe tllqegykks sypkkenpky
      661 ieeskrrrdf lkwdtvktqk vnkrisslnk pfirlhglar sdrrerieya lvvtvrykdd
      721 iqmyanvmnk ypilqpiilq nnvsqri
//
LOCUS       WP_010818300             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative ABC transporter permease [Enterococcus].
ACCESSION   WP_010818300
VERSION     WP_010818300.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..255
                     /product="putative ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29692
     Region          8..176
                     /region_name="COG4905"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443933"
ORIGIN      
        1 mekmsqvill ffiysfigwl wetvycslka kkfvyrgflv gpycpiygfg vlsvlyfvep
       61 fennllvlyv gsavlvtile yvtsyglekl fhaswwdyhd vpfnlngrva lpvslfwglg
      121 cvlivkviqp eiakvvsflq vtfgnylalc ivivmgldli ytllnmqgfk klitemgqtl
      181 etnqqefkqr lntkmeiata dwqklkertk kehfqnrlnf qqrrfinnyp kltlknikns
      241 kevrhlledl knkgq
//
LOCUS       WP_010818305             374 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cell division protein FtsQ/DivIB [Enterococcus].
ACCESSION   WP_010818305
VERSION     WP_010818305.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..374
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=42143
     Region          86..316
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mwkisnendi fkkrkplppk kseesqpelt pwqkqnqeyl kkqaeeaalk geneqaevti
       61 tlqeqsqeep qqhlpqetve eeehfadrlp nvkktrnkrl yrrlafiltc lgtailvaly
      121 fvsplsrlse vtvsgnksve sqaiiqqskl etgsglweqy snrnyfsani qkkfpiikka
      181 niklnginsf kidiqeyqiv alaatkggyh pilengktla ettkaaesgk pifenfkedk
      241 lipelmasyn klpqeikqgi seikyapskt nkdlinvymn dgnrvivnis dlsekmayys
      301 qvaeqmdkpg ivdmevgifs ypyekeseet gsevsedsav enqevedpna gvatdeanng
      361 tptngenqev qqae
//
LOCUS       WP_010818352             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endonuclease/exonuclease/phosphatase family protein
            [Enterococcus].
ACCESSION   WP_010818352
VERSION     WP_010818352.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..254
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29064
     Region          2..249
                     /region_name="EEP-1"
                     /note="Exonuclease-Endonuclease-Phosphatase domain;
                     uncharacterized family 1; cd09083"
                     /db_xref="CDD:197317"
     Site            order(7,43,132,166,168,215,241..242)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197317"
     Site            order(43,241)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197317"
     Site            order(132,168,242)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197317"
ORIGIN      
        1 mkiatynvrv dteydqdwqw sfrkeavcql infhdwslcc iqevrpnqvr dlkayttftc
       61 lsaeregdgq geglailyne qkvqaidtgy fwlsetpqqp sihpeagcpr ialwglfket
      121 tqntpflvin vhldhisaha rlagmtvile elhdkiaqyp tllmgdfnae sgeavhqlvq
      181 kkfqdsknla thygprgtfq nftytkpwae leeidyiyak gwqvqktasl tdsidgrfps
      241 dhfpleaevc ieer
//
LOCUS       WP_010818510             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: histidine phosphatase family protein [Enterococcus].
ACCESSION   WP_010818510
VERSION     WP_010818510.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..214
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24214
     Region          3..205
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mklyftrhgk tewnqqkrfq gmtgdspllp tsydeikqlg qylqdipfek iysspllrak
       61 ntargiqqel nrpveivytd slkelglgrl egqyieemrn fygeeldhlr hrldlynpti
      121 fdgepieqai qrisetvaea akqhegpvlf vghgaaltaa iqamagkpls elrtmgglln
      181 nslsiletke asrnmpydlt lwndtsflak ekaq
//
LOCUS       WP_010818631             113 aa            linear   BCT 01-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Enterococcus
            faecalis].
ACCESSION   WP_010818631
VERSION     WP_010818631.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..113
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=13019
     Region          8..113
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 msdetkyipk kgdivwidfd psagkeiqkr rpglvvsrye fnrktmfavi cpitstiknm
       61 ptlytlpdem ethgqvvisq lksldfterk lsqiehlplk dmakidqiie yif
//
LOCUS       WP_010818682             202 aa            linear   BCT 01-JAN-2025
DEFINITION  superoxide dismutase [Enterococcus faecalis].
ACCESSION   WP_010818682
VERSION     WP_010818682.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..202
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22543
     Region          4..197
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mtytlpelpy aydalepyid vetmhlhhdk hhntyvtnln aaiekhpelg eksvedlisd
       61 mnaipedirt avrnngggha nhtffweima snaggqptga ikeaidetfg sfdemkaafk
      121 taatgrfgsg wawlvvnngn leitstpnqd splmdgqtpv lgldvwehay ylkyknvrpd
      181 yieafwnvvn wdkvnelfaa ak
//
LOCUS       WP_010818697             284 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterococcus faecalis].
ACCESSION   WP_010818697
VERSION     WP_010818697.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..284
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32605
     Region          23..276
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mekeelkile elrhilnskn eaivilnnyf kggvgkskls tmfayltdkf nlkvlmidkd
       61 lqatltkdla ktfkvelprv nfyeglkngn lassiihltd nldlipgtfd lmllpkltrs
      121 wtfenesrll atlleplksd ydliiidtvp tpsvytnnai vtsdyvmipl qaeeestnni
      181 qnyisylidl qeqfnpgldm igfvpylvdt dsatiksnle elykeheedn lvfqniikrs
      241 nkvstwskng itehkgydkk vlamyenvff emveriiqle neke
//
LOCUS       WP_010818717             505 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease/substrate-binding protein [Enterococcus
            faecalis].
ACCESSION   WP_010818717
VERSION     WP_010818717.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..505
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55918
     Region          2..208
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          236..499
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(242,244,292..293,296,339,341,419,443)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mqalietffa rkeeylqali ehmqlsfisl lfaaliaipl aiyltshrkl aesllqvtgi
       61 fqtipslall gllipligig rppaivalvi yalfpilqnt ytglteidps leeaaeafgm
      121 skkeklfkfe lqmalpfiis girtatvlii gtatlaalig agglgtfill gidrnnlsli
      181 figalssaal avlfnygihw lekangrrli iggtilglll ggsffwnqqt sskekqltia
      241 gklgaepdii inmykaliee nsdiqvtlkp nfgkttflyn alksdeidly peftgtmiet
      301 flknppqldn qpqvvyeaar aglknqenlt llkpmryent yavavkrsfa kahqlktisd
      361 lqkisnqlka gftlefidrq dgykglqeky hlnlnvqsme palryqainn gevnvidays
      421 tdselkqydl vtleddqalf ppyqgaplik tatlekypel aeilnklagk iseeemsemn
      481 yqvnvegqdp sivakdylke knllk
//
LOCUS       WP_010818729             359 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010818729
VERSION     WP_010818729.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..359
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38798
     Region          126..359
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflgfnemky skgryvlvvl vmvliawlif ilsglangla qgnrlavdqw qanqvvlske
       61 ansnlnvsvl denvketisg gkiapigqqs lairpaddkk aeltnvslfg iekesflmpk
      121 viegnaftdk nqviasetlk nqgfkigdkl tagkydeqle ivgfiskssy nivpviytsl
      181 dtwrsikygd npamvkmvng fivrskdnae vkttnkdsqv lsisdfiekl pgysaqnltl
      241 dgmiyflivi aafiigifif vmtlqktamf gvlkvqgvpt sflakavmlq tallavlgva
      301 iglaltgitv lflpeampya tngprmilfs vllilsalig gafsirtiak idpliaigg
//
LOCUS       WP_010818740             240 aa            linear   BCT 01-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Enterococcus
            faecalis].
ACCESSION   WP_010818740
VERSION     WP_010818740.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..240
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26336
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 miniknlqkt fgknevlkgi dleieagevv viigpsgsgk stflrclnll etptggsvef
       61 egknlldknt nidqlrqkmg mvfqnfnlfp hknvlenlti spvkvkkeaa aeatehalsl
      121 leqvglsdkk enypaqlsgg qqqrvaiara lamrpdvmlf deptsaldpe mvgevlsvmk
      181 nlaiegmtmv vvthemgfar evadrvifmd agiiqeegtp eeifdapqnp rtqdflrkvl
//
LOCUS       WP_010818760             271 aa            linear   BCT 01-JAN-2025
DEFINITION  TlyA family RNA methyltransferase [Enterococcus faecalis].
ACCESSION   WP_010818760
VERSION     WP_010818760.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..271
                     /product="TlyA family RNA methyltransferase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29901
     Region          4..244
                     /region_name="YqxC"
                     /note="Predicted rRNA methylase YqxC, contains S4 and FtsJ
                     domains [Translation, ribosomal structure and biogenesis];
                     COG1189"
                     /db_xref="CDD:440802"
ORIGIN      
        1 mkkervdvla fnqglfetre kakrsvmagl vyndknerld kpgekisvet plhtkgqvmp
       61 yvsrgglkle kalnvfainv qgktmldigs stggftdval qngarlsyal dvgynqlawk
      121 irqdervvvm eranfryskp edftegvpdi atidvsfisl rlilpplhdi lkkggsvval
      181 ikpqfeagke fvgkkgivrd pethqmvvee itrfamnngy dvknldfspi tggegniefl
      241 ahlvsvegeg syqapesiee vvahahqkla e
//
LOCUS       WP_010818764             487 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus faecalis].
ACCESSION   WP_010818764
VERSION     WP_010818764.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..487
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=51687
     Region          1..478
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mnglmawmek yilptaakig aqkhlvalrd afigtlpatm agsvavmina iirdlpqefv
       61 styaaslead kgifavlnvi igingfvwng tlaiaglifa fswgynlaka ynvnelaggi
      121 vslatlisgv afapnntael avkvpekian aingaeigas iannqltvnp wgwlnlnhln
      181 gnafftvmim galstiifck lmqadltikm pdsvppavsk afaailpati alyvvaiinf
      241 tvsklsggql lidliqkyit epflglsqgl gavlivtvfv qifwffgihg pnvlapvleg
      301 iwgqaqlini difqkgyegk tgtaavlaai ddgkaymwvr gsfdafawfg gsggtivlii
      361 aillfskrad yltvgklslg pgifninepi mfglpvvlnp imfipfviap lvattigwva
      421 tylglvapvs qqvawvtppl llsflatgad wrapivalvc mvvtfliwtp fviaankmdp
      481 algeseq
//
LOCUS       WP_010818777            1196 aa            linear   BCT 01-JAN-2025
DEFINITION  PD-(D/E)XK nuclease family protein [Enterococcus faecalis].
ACCESSION   WP_010818777
VERSION     WP_010818777.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..1196
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=138855
     Region          4..1173
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 msvqfirgta vadleapliq atkqwleeda qhevfylvpn hikfeqeiqv lqklrqlqtt
       61 tsdsitstrl qvfsfyrlaw yylqhtpfys advlsdagaa mifrkilvea eeelqifrge
      121 inkpgfiqql fqlyqemreg nieiaelypf lekqtenpkg qdlqlkfqdl tliftrfqlq
      181 msqygyesae iiqhlseylq tvdlsnvqfv isgyqqftar elklievlma qagsvkvall
      241 ldkqyphdlp dprslfyeag qtyhqlyqla rqkqipilsd yvekkevlit npdlqglndy
      301 wiqsqehlpp lsttdwsgdg lflwraenvk eelthvatei rrlvveegyr ykeiqvltrd
      361 ldcyenllep ifaeheipvy vdrdmamdrh plvewieslf aihsynyryr dvlrflrtel
      421 fmpmnqlats eesltdwlnq rnawrrkvdi tenvvlaygy egyywsqekd wefirydfea
      481 eeqedvatme eesnairqsl qrllpsyfqa misaktglea atvfynfllq sgvatqlkmw
      541 rlqaieagql etarnheqtw dalmslldey vtvygessfd fttfqeifvs gleglhyskv
      601 ptaidqvqvr amdltrpgaa kvtfaigmte eifpqkienk tllsdeerqt indtltenqy
      661 lrgttgrkia qepyvaylvf ssarerlylt ypsvkdtaqe vkpspyfkni qkdlnlpvfe
      721 knettifdde ttslahisty rtligeltrl krqrketqeg llpfwlnmek almnqsiapl
      781 tkqvfeslth qnipekidev laeplygkdi ytsvsrmesf yrcqyqyfsr yglrlkerdv
      841 fglspaatge ffhealdqff kllimnqrnl seltdqevnl laeevlnsil gdarfsvltt
      901 ssrmnyiryq lsqtikkvsw alkrqsqrsg mttvqtevlf gqiaakkgis glelplknqg
      961 kihvrgkidr idqlvtpest ylgvidykss hrkfnmteay yglamqmlty ldvalmdavq
     1021 lvgqeakpag slylhvhnpt lsyegkddie qqmlkkyqfd gllmkdpdll dhldtslqak
     1081 qssllfpiee sakeqikpgr rqedkfvtep elgallshnr nkfieagnqi iggevqlnpa
     1141 yqgkeriacr ycpfrsvcdf dvmlkennyh rienlskeei marllnkdee gatede
//
LOCUS       WP_010818784             562 aa            linear   BCT 01-JAN-2025
DEFINITION  ribonuclease J [Enterococcus faecalis].
ACCESSION   WP_010818784
VERSION     WP_010818784.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..562
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=62755
     Region          1..552
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mstikivplg gvrengknmy vaevedeifv ldcglqypen ellgidvvip dftyleense
       61 riagvflthg hadaigalpy llskiqvpvf gteltielak lsvnshaetk kfkdfhvidp
      121 hteidfgqat vsffktthti pdsigvsikt kegnivytgd fkfdqsaiem yqtdygrlae
      181 igkegvlall sdssnaenpa qvaseaqiad evfdtirywe griivacvas nlqrvqqvln
      241 aadrsgrkvv ltgqdferii rtamkleklq lpsedllvkp kemkkyapeq lliletgrmg
      301 epikslqkma nnthgvvrie egdlvyittt pttamettva ktedivyrag atvkqisdnl
      361 rvsghanpnd lqlmlnlmkp kyfipvqgey rqlaahadla heigmpykdi fitgrgdile
      421 ytkgrmsvag sttaenimid gigvgdigni vlrdrrilse dgifvavvti nrrekrivst
      481 akitsrgfvy vktskdlmke ssnivteive khlesddfew sklkqeiren lsrylfeqtk
      541 rrpvilpvim eatqrkrpkn na
//
LOCUS       WP_010818848             380 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Enterococcus faecalis].
ACCESSION   WP_010818848
VERSION     WP_010818848.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..380
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=41840
     Region          1..375
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mtfldlfagi ggfrlgmeqa ghqcigfcei defarrsyka ihdtrkevem hditsisdef
       61 vqslgpvdii cggfpcqafs iagkrqgfsd trgtlffeia rfatllrpkf lflenvrgll
      121 nheggatfet vlrtldglgy dvewqvlnsk ayvpqsrerv flighsrdac teqvfpiiga
      181 sptsdqnirn llninpsnrg mggqvygsdg vaptltgdeg ikialpvndg isvagmlsgn
      241 feqgnrvyev tgtaptlstk qggtkimirk ngteyqevkp gdsvnlafpn stsrrgrlgk
      301 qsvhtlltgd qqavvteqyq irkltprecw rlqgfpdwtf drasqvnsds qlykqagnsv
      361 tvpvifdiar rlkevkiddl
//
LOCUS       WP_010818871             392 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus faecalis].
ACCESSION   WP_010818871
VERSION     WP_010818871.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..392
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45936
     Region          66..388
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 menmsrfkkh itatgkitwy fqafrttrrg fnskreaqla ylemekqhrn kqkrlasndk
       61 fsvvsqkwfe yyrslneqkv atydkreeqv kilnrwiggk klsslsseel qkflfilkek
      121 eidgvnvgya knslqslvqv lnmvfnyckk knlinenpmk fvkmpkyqls lkdlkesvns
      181 ledkflivde lraflnygiv yeelpmsvlf hvlfytgcrv sealalqpqd idferneilf
      241 ykqtavkgks kdfriettkt vssarrvpvt plvmeklqel idvlnktkrn snfvvdetyl
      301 fvyldpgkrg vpyrreyvnd hvkrcvercg inkdfhthla rhtmaslvae ycswdvlkdr
      361 lghtdsttsk iyrhltstek lkpltafnsl eg
//
LOCUS       WP_010818878             218 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Bacilli].
ACCESSION   WP_010818878
VERSION     WP_010818878.1
KEYWORDS    RefSeq.
SOURCE      Bacilli
  ORGANISM  Bacilli
            Bacteria; Bacillati; Bacillota.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Bacilli"
                     /db_xref="taxon:91061"
     Protein         1..218
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23977
     Region          1..203
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mdileiknva ysyanskekv lsgvnqkfel gkfyaivgks gtgkstllsl lagldkpqtg
       61 kilfknediq nkgysnhrkn nislvfqnyn lidylspien irlvnksade siffelgldk
      121 kqikrnvmkl sggqqqrvai aralvsdapi iladeptgnl dsvtageiin ilktlakdrn
      181 kcvivvthsk evadsadiil elsgkklkkv nkmnleve
//
LOCUS       WP_010818937             190 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010818937
VERSION     WP_010818937.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21517
     Region          2..126
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 markktitke qiltaayevv ategfskfta rniankmkcs tqpiylefkn mddlrdalfq
       61 kihkylakev fsvkhtgnti vdlalnyihf atsesklyra lyleeygggk kmqefsyhyf
      121 teavkadpey anlndvqids lhmgtwvvat gvaalmtsgi ihpseeqiih lmkdsieail
      181 erdepididl
//
LOCUS       WP_010818965             319 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus faecalis].
ACCESSION   WP_010818965
VERSION     WP_010818965.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..319
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35351
     Region          8..248
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtkklyqwgi vglggiahef astfkqetsq laavasrtlt kaeqfaadys ipkaygsyee
       61 lladetinvv yiavpnkqha ehilkalqag khvlcekait mnaaelkqal avaekndlil
      121 aeamtifnmp lydelrrlmd agkfgqlkmi qapfgsykep dpknrffnpd laggalldig
      181 tyavsfarwf lssqpdvlas smvpfstgvd eqsvtllrnk enelatislt fqakmpkqgi
      241 vafedayiti tdypradeai vhyndgtvet ivsgysaeam nyeiynmvea ikgtqpnrsl
      301 ffttevidil dqmqklwqn
//
LOCUS       WP_010819016             132 aa            linear   BCT 01-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010819016
VERSION     WP_010819016.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..132
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15035
     Region          32..123
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 msilwvingi llvivlamvf nelylkimvk rsakmlteee fketmrkaqv idvrekdtfd
       61 aghilgarsm pysmlkttig slrkdqpvyl ydqkkalsir aanllrkngy tdnyilkggy
      121 dgwtgkvkkr ns
//
LOCUS       WP_010819025             419 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus faecalis].
ACCESSION   WP_010819025
VERSION     WP_010819025.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45364
     Region          5..412
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtdktkssla ywkkivillc mgwvtiwiyr salspvypqi raslngnasd talgsissfy
       61 flgyvvmqip agflvdkigk krvlipgfil falaalliaq aqtigtiylg sllaglgcgs
      121 fygsayslts qnipqakksf ataivnsgsa vgsglgmils sylvaqkglp wqvmmyisaf
      181 miicmlvafq viirnhkedm aliqptvvde kdngavkekv pfkklfaphm lfayilyfgt
      241 cyayymivtw lpnflsterg fqgvaiglss slvafasipg alffsrladk ymhkkvqfiv
      301 vleflataml lltvqvsnat lllialimyg flgklavepi iiswlgenap kigigttlgv
      361 fnffgmmssv iapaltgkis dttgskvmgf yiavvillig tilfmlvnlk krgadssnk
//
LOCUS       WP_010819031             442 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus faecalis].
ACCESSION   WP_010819031
VERSION     WP_010819031.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 442)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..442
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50358
     Region          57..416
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 marfvfilsn itavvqvffn ylkskvvrln kkitlhsifg lmviailngk iisaigmygf
       61 awiylsiiil gyffisksli kvlginsyiv iisaisdqfv sfikekifga elifssnltm
      121 flhstfrlal sviltilmik gikklekkfs iineclllfn ligigtmiiy ytslvlgkyl
      181 gnnkeiivvn sifltlylvv slisfivyls slknkydiqq keteylenqr ymeamekqfk
      241 eirkfrhdyk nilnsledfi vsgdyeslnd yyfskikkas kcidqngfkl eaignirvre
      301 vksllvskli stqekgmdvq levtepieel aidsislvri lgifldnsie eieflgegkl
      361 viavykdasa vhiiiqnscr knlpkfhllk qrgfslkgtd rgmglsnvqe llqslnnvql
      421 atsisdgwft qkltiennrr ce
//
LOCUS       WP_010819044             520 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010819044
VERSION     WP_010819044.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..520
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59672
     Region          7..139
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          244..516
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msvrvndllk lpslreatvl sgknqldtsv aslsflevsd mslfseklhk tneyhageil
       61 igsfcairhd vvkqcetirh lhelgevgli lyyvgiivpk vaeeviqlad slgfiliqmp
      121 kndptlryne viyevmkllv nknkmasfat dllekvsllp eqnrsvemtl kilsdflkvn
      181 ialttytnei isninwprst klpltkllyq sqekvalget tyfitsqklp qkdgqtlkly
      241 fireeeqlts femnqavevv qmalnlwgkn ydevseyalv qaiindesdk myqlakklmi
      301 dissvetmwl lpiwqqgqei haiqqdlkdf lryyyqttiv qqtenylivl lgnylhkqpe
      361 atiskeylqa tdyqdylgei ilcpkvrntt evrvsyqtan qvapflkrvy pqrkvlsiae
      421 irtvqqmmtc lqageeaiqq rlaviqpllk eseqlmtlgt flldassdfk ecgerlfvhk
      481 ntvkyriski nealgydmtn aaeayevyla milyrlvtne
//
LOCUS       WP_010819195             903 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010819195
VERSION     WP_010819195.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 903)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 903)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 903)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 903)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 903)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..903
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=105148
     Region          1..898
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
ORIGIN      
        1 mkllaveivg fgkwqqqkit fesgnqllyg anevgkstly qfiqamlfgf ptkgkrkrdy
       61 apknggsygg rlwlehpvfg evqverfkek nkgqaiiyyq qqmgdektlq qmlhpltkkl
      121 fqevftfqqe qlitsdklte eelqtsllai gvsgsqqllt yrnayfkeaq kifkgkgqqp
      181 llnqklavyq elkeqiqeke aqqqtfqqle etireteqqr vtlqqqlket qqdllqvaeq
      241 qrhfplyeew qslpeetenv vlgkedqvql eetfqeymyl dkerqrltke lslqsealdv
      301 pegyafyleq ealiqqllnq rydmqqlmte sewmtqtfdq nrqemvllen ewswsperpp
      361 qlfydnetvq kwrqqqvayt qalqkgqeqk aflasqienl edqltdfeka haaffgeatr
      421 aqkaqktsqp lwlllgsila llgfflpspl kwglvlvgvs fiakevlsya trkevssdev
      481 keewqtklsq ldylneqfqq alnqereaql qveqleqava eqaqvhqlgk mqqidtlmnq
      541 relitrylll vqtneelmsq lkenqqkrqg feeqvfplmt hlplqgksls eklhflegfa
      601 eemekvrfaq eyqadgylkq qlrelktkqq ealtriqpll iryrilsiad vpsriqqltt
      661 qqaqvgrgqe latqlgnlfp eavteatlka rslqlmqqqa leesqldkiq eqyqaliyek
      721 qqlmtdgtld elyqrqailk aeikelaqrw sgyqlagqll mdlltelseq qlpsllqyas
      781 syfalltsqr yqsiqvaegq lvavtkeqem fylhelstgt kdqlmmavrf aflavqgeql
      841 vcpiiiddgw lhydhqrkaq laelftkfgq kqqvicfssd qemvsyyqdl kqrvialegg
      901 svk
//
LOCUS       WP_010819204             189 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecalis].
ACCESSION   WP_010819204
VERSION     WP_010819204.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..189
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21061
     Region          5..131
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(10,12,69..70,73)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            12
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(68,112..113,115..116,120)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(74,79..80,108,111..112,115..116,119,122)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(97..99,108..109,112..113,116,120,123,127)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(97,113,116,120,123,127)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(121,127..128)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mtnkiigyir tstssqdlgl evqkkalery epdiiysekv sgrkekrtel ekalenlatg
       61 dtlliynlar lsrsskqlvn lmselnakgi hlksiqesvd tktatgrlff tvlaaiaefe
      121 aenisirtke alansnkklg rpkvknntkk kvlklyqnke lslneiaekc gisvktvynl
      181 akseglsrk
//
LOCUS       WP_010819212            1025 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Enterococcus faecalis].
ACCESSION   WP_010819212
VERSION     WP_010819212.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1025)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1025)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1025)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1025)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..1025
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=116232
     Region          6..1017
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 maeeyhfnen elelvalrwl eevgytsvsa keledsgmsk rkdykevvli drlkealvti
       61 npdvsmavid daiktitvhk hpdmavnnqt fhryitdgie iptrecnrnv tkrillfdfn
      121 eprnndflav nqfiveednq rkrtdiilfv nglpivlfel knatdeavgi sdaynqlqty
      181 kqeipslltf nefmvasdgv qakvgtlssn eerfmvwrti dgkvehgtas sqlevlikgm
      241 cnpevlldll hhfilfktdg dktikilaay hqyhavnrav eeakravste gdnkigvvwh
      301 tqgsgkslsm vfytgklvqe lnnptvvvlt drndlddqlf ltfsqssdll rqtpkqandg
      361 delkellsvn aggivfstmq kfapkegnqm dvltdrrnvi vmadeahrsq ygfsadvnak
      421 dgsikygyak ylrdalpkas yigftgtpis sadkstkavf gdyidvydmt qavedgatvk
      481 iyyesriipv slpdgldidd lvedivegqe ddvasktkak wsrieaitgs qprleklaqd
      541 fvkhfetrqe asfgksmivt msrriaidly qeiiklrpdw hsddddkgki kivmtgsssd
      601 pdywqpfign ktrrdklakr mkddsdelqi vivrdmwltg fdvpsmntmy idkpmqghnl
      661 mqaiarvnrv fkdktggliv dyigiapnlk nalqeytpnd qkqagidtqv avnlvkekyd
      721 litntildkf dysdfnstdy tkklqvitna anyilglddv edvkrfkdlv teitrayalc
      781 vteeevqqyn aeiaffkavk vyliklnfvd gvkspqqide elkqlisksv vtedivdiyd
      841 slglekaels ilsdkfleei kempqknlal qllenllagk iksiqktnvv qaekysellk
      901 ksinkyntrg itseiairel ielakdmktm keegeelglt veekafydvi sknsdedeqv
      961 lkdiavgiak tieenmtidw tkrssekarm rveikrflrk nnfktdleti dlvitqaelm
     1021 aenls
//
LOCUS       WP_010819264             336 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Enterococcus faecalis].
ACCESSION   WP_010819264
VERSION     WP_010819264.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..336
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37922
     Region          2..315
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(33..34,37,88,103,106,136,169,275,278,314)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(241,252,266,275..277,280,302,306)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mkiaafgevm lrftppeylm leqteqlrmn fvgtgvnlla nlahfqleta litklpanrl
       61 geagkaalrk lgisdqwvge kgdhigsffa emgygirptq vtyqnrhqsa fgiseakdyd
      121 feaflaevdm vhicgislsl tektrdaali laqkayacqk kvcfdfnyrp slntanself
      181 mrqqyerilp ycdivfgsrr dlvellgfip redlegeaqe teliqrfmsq ynlewfagtt
      241 rshsqnqnyl sgylytqney qqsekrplln ldrigagday aagilygysq nwslekavtf
      301 atvngvlaht iqgdiplttv kqvnhvlenp nidlir
//
LOCUS       WP_010819305             468 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Enterococcus faecalis].
ACCESSION   WP_010819305
VERSION     WP_010819305.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..468
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49163
     Region          1..467
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mntffklken kttvsteima gvttffamsy ilfvnpsils etgmpfqavf latiiasiig
       61 tlimglfanv pyaqapgmgl nafftftvvf gmgytwqqal amvficglin ilitvtkirk
      121 miikaipesl qhaigggigi fvayvglkna gllsftvqae pqngvvngss ivpalgnfdn
      181 paiilavigl vlttilvvtn vrgailigiv vttlvaipmg vvdtasvdwh anslgnsfke
      241 lgttfgaafg aeglqslfsd sskipqvlmt iiafslsdtf dtigtfigtg rrtgifsked
      301 elaledskgf stkmdkalfa daiatsigai fgtsntttyv esaagigagg rtgltsvvva
      361 ilfalsslfs pliaivpaqa tapalilvgi mmlasfkdin wtdledaipa ffasifmglc
      421 ysisygiaag fifyavvkiv kgkakevspi iwvidalfil nfvilail
//
LOCUS       WP_010819377             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MOSC domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010819377
VERSION     WP_010819377.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..144
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15661
     Region          3..144
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mktgeiiain isprrgtqkk eipevnlikg fglendahgg nwhrqvslls feeimafnek
       61 garvgngafg eniivsgidl rqlpvgtkmk igdselvvtq igkechkhcq iyarvgdcim
      121 pregifavvv teghikkgdq ldvv
//
LOCUS       WP_010819421             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ComF family protein [Enterococcus].
ACCESSION   WP_010819421
VERSION     WP_010819421.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..228
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=27045
     Region          41..228
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mdckncaspi rleitlkmll rfkkwarpsl cqhcqakfqk lpmtgtcfgc srvsqehycf
       61 dcqrwqllyp eysfhntalf hydegmqewm erykfqgdyr lrtcfneein fyfrqqsvdy
      121 iipiplsekr mqkrgfnqvi glleaadvpy spflirkeen vpqskktrke rmrlqqpfai
      181 qkenqkklkn csvilvddiy ttgrtlfhaa avindcypks lntftlar
//
LOCUS       WP_010819469             397 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphoglycerate kinase [Enterococcus faecalis].
ACCESSION   WP_010819469
VERSION     WP_010819469.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..397
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42236
     Region          5..397
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 makktikdvd lkdkkvlvrv dfnvplkdgv itndnrivaa lptikyvien ggkailfshl
       61 grvkteedka gkslkpvaer lsellgqpvt fvpetrgkel edavnnmkdg dvlvfentrf
      121 edvdgkkesg ndaelgkywa slgdvfvnda fgtahrahas nvgiasagip tvagflmeke
      181 ikfigeaven pkrpfvailg gakvsdkiav ienliekadk iligggmayt fmkaqgysvg
      241 lslleedkvd lakslmekag dklvlpvdtv vskefsndap fhtvpsteip ddeegldige
      301 ktielfanel qgaktvvwng pmgvfemsnf akgtigvcea ianledatti igggdsaaaa
      361 iqlgyenkfs histgggasl ellegktlpg lasindk
//
LOCUS       WP_010819530             319 aa            linear   BCT 01-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Enterococcus faecalis].
ACCESSION   WP_010819530
VERSION     WP_010819530.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..319
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35367
     Region          8..248
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtkklyqwgi vglggiahef astfkqetsq laavasrtlt kaeqfaadys ipkaygsyee
       61 lladetidvv yiavpnkqha ehilkalqag khvlcekait mnaaelkqal avaekndlil
      121 aeamtifnmp lydelrrlmd agkfgqlkmi qspfgsykep dpknrffnpd laggalldig
      181 tyavsfarwf lssqpdvlas smvpfstgvd eqsvtllrnk enelatislt fqakmpkqgi
      241 vafedayiti tdypradeai vhyndgtvet ivsgysaeam nyeiynmvea ikgtqpnrsl
      301 ffttevinil dqmqklwqn
//
LOCUS       WP_010819516             713 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GH92 family glycosyl hydrolase [Enterococcus].
ACCESSION   WP_010819516
VERSION     WP_010819516.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..713
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=81491
     Region          3..712
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mniqaidtrh gtanqhsfsn gnclpytgvp fgmnfyapqt tdqkgswwfh pedrtfqgyr
       61 vthqpspwmg dfshllmtpv sgslselslf haqssyrpee slfspveinl tqlryqitsq
      121 lipsmyggil tidyqqkdnh llltlpgryq vkqlddhqva vkvinysgce dpdfsfyfvl
      181 hfeqpltkwf apssgedgki llsfgniaqq vvhfsssfis ekqaqlnlar eislrsteml
      241 qqgiadwhny fdrlkvthen pehtktfyht lyrtflfpqt fyeldenqqp ihydtfsqtv
      301 rpgvlytnng fwdtyktvyp lfsliaqeky eemlegflns ynetgflpkw lspderglmp
      361 gtlidaviad aavkkirpdl mpqfleamkk gatqqseren ygrqgtldyl kygyvpstyh
      421 esvnhtldya ysdfcisqva ktlndsetat fyrqqalnyq qlfnpetgfm qakdtegnfr
      481 pnfldirwgk dyaegsawqs sfavyqdfag liklygsela fekkliqlcn qapnfnvegy
      541 gfeihemsem aaidfgqlai snqpsfhypf lfsyigkpem aqpllkqlmq tfdasptgyp
      601 gdedngsmsa wyifnslgfy pvtpgtgeyv igmplvqtae vklsngkqlt iqtspnkvqq
      661 qfiheiqlnq ekhtapyfth qellnggtld yqlgivpnpq ttaerpfsls tek
//
LOCUS       WP_010819672             155 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Enterococcus].
ACCESSION   WP_010819672
VERSION     WP_010819672.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..155
                     /product="VOC family protein"
                     /calculated_mol_wt=17399
     Region          9..143
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(9..11,27,67..68,71,89..94,96,100,131,141)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mkntqfalfm vlngrateal tfyqeafagd ilfkitnqef kerlnpslti pageehwlsh
       61 silqmdtfql qladnplfag mnttpteqlt lsltiesrhs aktifekltc hpesciiqep
      121 ienefatfya ivkdpfglvt qitqekqadp tkkgs
//
LOCUS       WP_010819711             455 aa            linear   BCT 01-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Enterococcus faecalis].
ACCESSION   WP_010819711
VERSION     WP_010819711.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..455
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50641
     Region          13..437
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mkhqikrrly ispvqtivlg ffllivvgti llmmpfsaqa gqktqwidaf fvatsavcvt
       61 glsplntaeh wspigqviim ilielgglgf ltvatiffsl lrkkaslsvr mlyqealnvs
      121 evsgvfrlmk yimkfaaiiq llgafllsfq fvptvgwkkg mffslfhavs afcnagfdll
      181 gdsmvpyqns pylllvisfl iiagglgfiv wrdifamikg yknkikhrvs ihtrlaltvt
      241 atflvlgtvi fyiseyrhfp admsfwqrlv nswflsvtpr tagfysvdyl kmsnpglivt
      301 ilwmfiggts gstagglktt tfgvlflqfr aifkgkqrve fhertiperv vlqaftlffl
      361 atflcvtasv ilsftetlpl kngieyivfe visafgtvgl tmgltpdltv fgklviiflm
      421 fvgrvgvytv llslikkgle sqskvqypke svmig
//
LOCUS       WP_010819752             903 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Enterococcus].
ACCESSION   WP_010819752
VERSION     WP_010819752.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 903)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 903)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 903)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 903)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 903)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..903
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=105159
     Region          1..898
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
ORIGIN      
        1 mkllaveivg fgkwqqqkit fesgnqllyg anevgkstly qfiqamlfgf ptkgkrkrdy
       61 apknggsygg rlwlahpvfg evqverfkek nkgqaiiyyq qqmgdektlq qmlhpltkkl
      121 fqevftfqqe qlitsdklte eelqtsllai gvsgsqqllt yrnayfkeaq kifkgkgqqp
      181 llnqklaayq elkeqiqeke aqqqtfqqle etireteqqr vtlqqqlket qqdllqvaeq
      241 qrhfplyeew qslpeetenv vlvkedqvql eetfqeymyl dkerqrltke lslqsealdv
      301 pegyafyleq ealiqqllnq rydmqqlmte sewmtqtfeq nrqemvllen ewswsperpp
      361 qlfydnetvq kwrqqqvayt qalqkgqeqk aflasqienl edqltdfeka haaffgeatr
      421 aqkaqktsqp lwlllgsila llgfflpspl kwglvlvgvs fiakevlsya trkeassdev
      481 keewqtklsq ldylneqfqq alnqereaql qveqleqava eqaqvhqlgk mqqidtlmnq
      541 relitrylll vqtneelmsq lkenqqkrqg feeqifplmt hlplqgksls eklhflegfa
      601 eemekvrfaq eyqadgylkq qlrelktkqq ealtriqpll iryrilsiad vpsriqqltt
      661 qqaqvgrgqe latqlgnlfp eavteamlkd rslqlaqqqa leesqldkiq eqyqaliyek
      721 qqlmtdgtld elyqrqailk aeikelaqrw sgyqlagqll mdlltelseq qlpsllqyas
      781 syfalltnqr yqsiqvaegq lvavtkeqem fylhelstgt kdqlmmavrf aflavqgeql
      841 icpiiiddgw lhydhqrkaq laelftkfgq kqqvicfssd qemvsyyqdl qqrvialegg
      901 svk
//
LOCUS       WP_010819797             492 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010819797
VERSION     WP_010819797.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..492
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=58553
     Region          79..156
                     /region_name="Mga"
                     /note="Mga helix-turn-helix domain; pfam05043"
                     /db_xref="CDD:428276"
ORIGIN      
        1 mlkrdflekp ydymndillf lynnkgqatr nelidffnis lptlneylsf leqflkeeql
       61 qesltvtalg dtlylnkapt fsmkamimlf ldksikfhmv qqlfhknein ggyfqqnyai
      121 ssatyyrkiv elndllnefn lrikrgklvg eekqirffff nffwfifeek tdlekelanq
      181 ylglieilqe ipritfdhte ilqiklwmki sfrrmvlepl ptispqdaql drplfeeinl
      241 sihtymkrid rpytineaym fydffcsmhn ysanaafafr lakqqriekt ylnemnrvil
      301 tylkvhgyls hyvlpirlly ienllfqlha qlyyfsgfil pfdywtiqsl lkvlrhpfse
      361 sevyelveia ttnfateati skyqnqftei nytlilnhia elnekkitig vyhslssays
      421 elvaqkiqqs iagkyplkie pynaenhydl llmntnneql vaqydhyyif sdisnrydlq
      481 siekiiqlll gk
//
LOCUS       WP_010819823             764 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus faecalis].
ACCESSION   WP_010819823
VERSION     WP_010819823.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..764
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87972
     Region          4..757
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mkqikrlfqi dpwkirtthl dkenlrlqes ltsigngymg mrgnfeehys gdhhqgtyla
       61 gvwypdktrv gwwkngypey fgkvinainf iamdlqidgq tidlattpye dfsleldmqn
      121 gvlsrqftiq tpknkvrfsf erflslekke aayihltiem legtgtitlh skldgdvqne
      181 dsnyeehfwe eiaietqetl gfvttktipn nfeierftvt agmhhfidga svvptytqqp
      241 laltaeltvs lnegettait kevlvvtsrd vpetqqitrv nelfaemttl ypeakagqaa
      301 awakrwqlad vviegddeaq qgirfnlfql fstyygeddr lnigpkgftg ekyggatywd
      361 teayavplyl alakpevtkn llkyrhnqlp qaihnaqqqg lkgalypmvt ftgvechnew
      421 eitfeeihrn gaiayaiyny vnytgdedyl kdaglevlva iarfwadrvh fsqrhkqymi
      481 hgvtgpneye nninnnwytn tiaawvlryt resylkfqee ttlkitddel akwadivenm
      541 yfpvdnelgi fvqhdtfldk dlmpvsdlpl selplnqhws wdkilrscfi kqadvlqgiy
      601 ffndafslee krrnfnfyep mtvhesslsp sihavlaael gmeekavemy qrtarldldn
      661 ynndtedglh itsmtgswla ivqgfaqmkt dhqqlkfapf lpatwtaysf hinyrnrllf
      721 vevaadqvaf tlldgpaipl tvydqkytlk drlvlpirke evhv
//
LOCUS       WP_010819867             303 aa            linear   BCT 01-JAN-2025
DEFINITION  YSIRK-type signal peptide-containing protein [Enterococcus
            faecalis].
ACCESSION   WP_010819867
VERSION     WP_010819867.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Bai,Q., Ma,J., Zhang,Z., Zhong,X., Pan,Z., Zhu,Y., Zhang,Y., Wu,Z.,
            Liu,G. and Yao,H.
  TITLE     YSIRK-G/S-directed translocation is required for Streptococcus suis
            to deliver diverse cell wall anchoring effectors contributing to
            bacterial pathogenicity
  JOURNAL   Virulence 11 (1), 1539-1556 (2020)
   PUBMED   33138686
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Yu,W., Missiakas,D. and Schneewind,O.
  TITLE     Septal secretion of protein A in Staphylococcus aureus requires
            SecA and lipoteichoic acid synthesis
  JOURNAL   Elife 7, e34092 (2018)
   PUBMED   29757141
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 303)
  AUTHORS   DeDent,A., Bae,T., Missiakas,D.M. and Schneewind,O.
  TITLE     Signal peptides direct surface proteins to two distinct envelope
            locations of Staphylococcus aureus
  JOURNAL   EMBO J 27 (20), 2656-2668 (2008)
   PUBMED   18800056
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Carlsson,F., Stalhammar-Carlemalm,M., Flardh,K., Sandin,C.,
            Carlemalm,E. and Lindahl,G.
  TITLE     Signal sequence directs localized secretion of bacterial surface
            proteins
  JOURNAL   Nature 442 (7105), 943-946 (2006)
   PUBMED   16929299
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Bae,T. and Schneewind,O.
  TITLE     The YSIRK-G/S motif of staphylococcal protein A and its role in
            efficiency of signal peptide processing
  JOURNAL   J Bacteriol 185 (9), 2910-2919 (2003)
   PUBMED   12700270
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Tettelin,H., Nelson,K.E., Paulsen,I.T., Eisen,J.A., Read,T.D.,
            Peterson,S., Heidelberg,J., DeBoy,R.T., Haft,D.H., Dodson,R.J.,
            Durkin,A.S., Gwinn,M., Kolonay,J.F., Nelson,W.C., Peterson,J.D.,
            Umayam,L.A., White,O., Salzberg,S.L., Lewis,M.R., Radune,D.,
            Holtzapple,E., Khouri,H., Wolf,A.M., Utterback,T.R., Hansen,C.L.,
            McDonald,L.A., Feldblyum,T.V., Angiuoli,S., Dickinson,T.,
            Hickey,E.K., Holt,I.E., Loftus,B.J., Yang,F., Smith,H.O.,
            Venter,J.C., Dougherty,B.A., Morrison,D.A., Hollingshead,S.K. and
            Fraser,C.M.
  TITLE     Complete genome sequence of a virulent isolate of Streptococcus
            pneumoniae
  JOURNAL   Science 293 (5529), 498-506 (2001)
   PUBMED   11463916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01168.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..303
                     /product="YSIRK-type signal peptide-containing protein"
                     /note="The YSIRK form of extended signal peptide directs
                     nascent proteins to the cross-wall site, while signal
                     peptides lacking YSIRK direct proteins instead to the cell
                     pole. A large fraction of YSIRK proteins are surface
                     proteins anchored by sortase-mediated processing of a
                     C-terminal LPXTG motif."
                     /calculated_mol_wt=32478
     Region          17..>176
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          17..49
                     /region_name="YSIRK_signal"
                     /note="Gram-positive signal peptide, YSIRK family;
                     TIGR01168"
                     /db_xref="CDD:273479"
ORIGIN      
        1 mvskrnvllr kqkyackvqk ysikklsvgv asvlvgtaly lgnpvsaaev tnievnsdnn
       61 ialteepsgv vtaevekesi vsngttveng veesngvata eiekestvsd gttvengaee
      121 sngvataeie keptvsdgtt vengteepsg vataeieres tvseevtaek vnselnrvad
      181 gdfegsivsn kskwtmkpwg vstivtegnn tfgkingetk deyilqkipt tpgkkylvta
      241 dlkvvarnat ptgayftvke ftenrqqgkv ysqlyldqtl kdwtkqtfef taegaetlvg
      301 ivk
//
LOCUS       WP_010819911            1196 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PD-(D/E)XK nuclease family protein [Enterococcus].
ACCESSION   WP_010819911
VERSION     WP_010819911.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..1196
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=138871
     Region          4..1173
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 msvqfirgta vadleapliq atkqwleeda qhevfylvpn hikfeqeiqv lqklrqlqtt
       61 tsdsitstrl qvfsfyrlaw yylqhtpfys advlsdagaa mifrkilvea eeelqifrge
      121 inkpgfiqql fqlyqemreg nieiaelypf lekqtenpkg qdlqlkfqdl tliftrfqlq
      181 msqygyesae iiqhlseylq tvdlsnvqfv isgyqqftar elklievlma qagsvkvall
      241 ldkqyphdlp dprslfyeag qtyhqlyqla rqkqipilsd yvekkevlit npdlqglndy
      301 wiqsqehlpp lsttdrrgdg lflwraenvk eelthvatei rrlvveegyr ykeiqvltrd
      361 ldcyenllep ifaeheipvy vdrdmamdrh plvewieslf aihsynyryr dvlrflrtel
      421 fmpmnqlais eesltdwlnq rnawrrkvdi tenvvlaygy egyywsqekd wefirydfea
      481 eeqedvatme eesnairqsl qqllpsyfqa misaktglea atvfyhfllq sgvatqlkmw
      541 rlqaieagql etarnheqtw dalmslldey vtvygessfd fttfqeifvs gleglhyskv
      601 ptaidqvqvr amdltrpgaa kvtfaigmte eifpqkienk tllsdeerqt indtltenqy
      661 lrgttgrkia qepyvaylvf ssarerlylt ypsvkdtaqe vkpspyfkni qkdlnlpvfe
      721 knettifdde ttslahisty rtligeltrl krqrketqeg llpfwlnmek almnqsiapl
      781 akqvfeslth qnipekidev laeplygkdi ytsvsrmesf yrcqyqyfsr yglrlkerdv
      841 fglspaatge ffhealdqff kllimnqrnl seltdqevnl laeevlnsil gdarfsvltt
      901 ssrmnyiryq lsqtikkvsw alkrqsqrsg mttvqtevlf gqiaakkgis glelplknqg
      961 kihvrgkidr idqlvtpest ylgvidykss hrkfnmteay yglamqmlty ldvalmdavq
     1021 lvgqeakpag slylhvhnpt lsyegkddie qqmlkkyqfd gllmkdpdll dhldtslqak
     1081 qssllfpiee sakeqikpgr rqedkfvtep elgallshnr nkfieagnqi iggevqlnpa
     1141 yqgkeriacr ycpfrsvcdf dvmlkennyh rienlskeei marllnkdee gatede
//
LOCUS       WP_010819995             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: LCP family protein [Enterococcus].
ACCESSION   WP_010819995
VERSION     WP_010819995.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..389
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=43680
     Region          148..389
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 msrvdrykhi heksrpaehk ktfnprksmg ehreepeela eslqepvyed sytedsrrse
       61 rrhqtdsggg ngsdqpprgk kdkkpkkkrk ksktkrffkw lvillillfa ystvmflkgk
      121 saaehddslp qekvetfngv kssngaknil ilgsdtrged agradtimvl qlngpskkpk
      181 lisfmrdtfv dipgvgpnki naayayggae lvrktlkqnf nldtkyyakv dfqsfekivd
      241 smfpkgvkid aekslnldgv diekgqqvmd ghvllqyarf rmdeegdfgr vrrqqqvmsa
      301 vmsqmknpmt llrtpeslgk lvgymstdvp vsfmltngps llikgkagve slsvpvpdsw
      361 nfgessyags ilevdeqkna daiekflne
//
LOCUS       WP_010820037             106 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Enterococcus].
ACCESSION   WP_010820037
VERSION     WP_010820037.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..106
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11715
     Region          28..99
                     /region_name="Cupin_2"
                     /note="Cupin domain; pfam07883"
                     /db_xref="CDD:462300"
ORIGIN      
        1 mliksaesee mtiffdkenq pntqvqmgii tlqpgekrpl agyarheqde ysyvisgeah
       61 tiledgqdlv gragqaqlie ageghinynd glepavvvwm lvertk
//
LOCUS       WP_010820050             640 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Enterococcus].
ACCESSION   WP_010820050
VERSION     WP_010820050.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..640
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71477
     Region          326..564
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mklsikkffe vflessways rpiltfdtrq nwfalvlsii iantvgavlt ivfpfafvlv
       61 nvgsflgtvi cvlprhsspq rsaidgilmi flgaslgill qsssifiill fvlglyfsgi
      121 vrnfsiglyi rclfgtisll agaqlkgnls igqtfeglga iilgmsilcl fyclyskpqn
      181 nearklvadl yeqlyllaqg kparyvhfri kvresvetmp wvnhqktpwi yplvsqadai
      241 agsldstnaa enlpalkaiq lflkgeqltl plqefasant eiksailliq neqsfkkisf
      301 ksflptkegl aeakeilhsy kgssarfair laltglvchf cslilnymyp lplanhefwv
      361 visgclmvmp gyhgtlgkit srtigsilgg clgiflsqli anltnlnplw pmllssllvi
      421 lyetvrklsq aflmlsvttw ltftlggssa gytrvldvii galiafvmff ifptwhsqvl
      481 rkninswskt issillalin eettlpsdaw vlayrvqrrv nysiqeivle spiysndasa
      541 eslmqqkrln dqllemqtam eelllelmkt qhylkklapv rpdtlntell nysqqilslt
      601 npknnrlinq skqsiyfpqi eqslvilkns tanfflanik
//
LOCUS       WP_010820096             244 aa            linear   BCT 01-JAN-2025
DEFINITION  ion transporter [Enterococcus faecalis].
ACCESSION   WP_010820096
VERSION     WP_010820096.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..244
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=27632
     Region          6..194
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          206..>244
                     /region_name="PRK14160"
                     /note="heat shock protein GrpE; Provisional"
                     /db_xref="CDD:237629"
ORIGIN      
        1 mkinqkiyny sivvlalisi alvifdfsni inisnppfni idnfilitft idyivrfiis
       61 knkikffken ifdliaiipf daifsffria rlfriakiar lakltraigv vgkltrntks
      121 flntngflnv iylssvlivi samiysyaen vpyidafwwa lvttttvgyg dispatplgr
      181 vaaiilmilg igfigmltst iteyfnksnn ededeesndk ieilinkidq lettieqlke
      241 eikk
//
LOCUS       WP_010820099             807 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA translocase FtsK [Enterococcus].
ACCESSION   WP_010820099
VERSION     WP_010820099.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..807
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=88919
     Region          313..801
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 maqkratnkk ksttkkktkk qqqqqerlny mflglifilf gvfglfrlgf lgtllanclr
       61 lvvgntfpfa aillilygll vmiygkdfpl krgrpifgav liyisvllff hafmfrnvsg
      121 sqpdilgntw eflqsdlkan qvtqnvgggm igallyqgty flvaqfgsyl iatllllagi
      181 flmsmwdfqq ivdhfqsiqd rlshvsaksq erqeekeakr aakkeakaae rqakieaaaq
      241 qklqererme qaaaerltkt pvethqpmve epaaptpvqi dsfqqqnqam pvppiaatkp
      301 qreqeeeaad eagvlefeis eeaedrdyql pptdlldtiq atdqsgeyek ieknigvleq
      361 tfksfgvdak vvkaslgpsv tkfevqpavg vkvskivnlt ddialalaak dvrmeapipg
      421 ksligievpn saistvsfrd iveaqpshpd kllevplgrd isgmvqtadl skmphlliag
      481 stgsgksvai ngiitgilmq akphevklmm idpkmvelnv yngiphlltp vvtnprkaaq
      541 alqkvvqeme fryekfaatg vrnitgynql iqqknaedge nrpilpfivv ivdeladlmm
      601 vasnevedai irlaqmaraa gihmilatqr psvdvitgii kanvpsrmaf avssgtdsrt
      661 iidtngaekl lgrgdmlflp mgenkpiriq gafisdqeve rvvafvtdqq eaeyqesmmp
      721 tdepttsggg eapqdelfee aknlvvemqt asisllqrrf rigynraarl vdeleahgvi
      781 gpsegskprk vflqaeseea vpetpeq
//
LOCUS       WP_010820206             189 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: guanylate kinase [Enterococcus].
ACCESSION   WP_010820206
VERSION     WP_010820206.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..189
                     /product="guanylate kinase"
                     /EC_number="2.7.4.8"
                     /GO_function="GO:0004385 - guanylate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006163 - purine nucleotide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21948
     Region          10..186
                     /region_name="Gmk"
                     /note="Guanylate kinase [Nucleotide transport and
                     metabolism]; COG0194"
                     /db_xref="CDD:439964"
ORIGIN      
        1 mikqlqhpff vimgpsgsgk taitskvfpk nykvishttr kkrldevdgv dyyfetkasf
       61 qtlietnqlv eydfyhgnyy gvgvaaivet tkehpaynal tfpgfqavfe rfgesvipvf
      121 fdvskeniyq rlkqresdpk iieerlnlyd qeiliknqle qypnyqrida ngsikevvdf
      181 lqkcikqyy
//
LOCUS       WP_010820227             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010820227
VERSION     WP_010820227.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..240
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27055
     Region          3..218
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnldylkety hltktesqil yyldqqstna adlsirevak hcfsspssii hlakklnlsg
       61 yneliyklke ahfsqpipfe tapsfettne fcqllakhks hlfvilghdf srhlaayise
      121 vfnfhgipsi ttahthsins qnnqnflfii lshsgeekyl ketallakek khpiisfvga
      181 knstlgrlad lvfstdsysp fstsvaqpqm ffgqtlitfe alicaylnhe dsipishknk
//
LOCUS       WP_010820216             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: histidine phosphatase family protein [Enterococcus].
ACCESSION   WP_010820216
VERSION     WP_010820216.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..214
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24197
     Region          3..205
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mklyftrhgk tewnqkkrfq gmtgdspllp tsydeikqlg qylqdipfek iysspllrak
       61 ntargiqqel thpveivytd tlkelglgrl egqyieemrn fygeeldhlr hrldlydpti
      121 fdgepieqai qrisetvaea akqhegpvlf vghgaaltaa iqamagkpls elrtmgglln
      181 nslsiletke asrnmpydlt lwndtsflak ekaq
//
LOCUS       WP_010820338             337 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Enterococcus].
ACCESSION   WP_010820338
VERSION     WP_010820338.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..337
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37651
     Region          79..336
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkrkivrfil wllgiivvic lgvflafqls pkpgawvinq lfageveikd pasydkalpn
       61 vqlqgnqtyp ssrkkntfdl yypqtskqav pvvlwvhggg yvggdksgmk efatrlvads
      121 svafismnye lapdapypsq lqqvnelvqf llekkqaypm ldlsklfigg dsagaqialq
      181 yatvqtnany akelgmtaal pasylkgtls ycgpvdlkqm anqqsdnrfm kffvktvaws
      241 llgtkdwqts aelqevslvd kvtkefppty ltdgnsfsfq eqglalvqrl ktlnvpvsal
      301 ffkdkkatit heyqfdyqtk eakqcyqetv qfvntyk
//
LOCUS       WP_010820352              73 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010820352
VERSION     WP_010820352.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 73)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..73
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8445
     Region          13..72
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mskvekanfv ssihvyraih rmtqqelaek vgvsrqtilq leknrynpsl llafriakff
       61 hvriedifvv nes
//
LOCUS       WP_010820376             217 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010820376
VERSION     WP_010820376.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..217
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25659
     Region          11..213
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mrnvlqdyld ehsfrvvvkk kknyltyegl qdryayilks giiktsvisk dgrefnlryi
       61 nnleivsllr deysefidap fniriespra elyqidrvqf wrdinnskdl qmyvkeyyrd
      121 rlmhsmkkmq qmlmngkfga vctqiyemyd sfgveteegi lidfvvtnee iahfcgitsa
      181 ssvnrmmqql kelgaielrn rkilikdldm irdniiv
//
LOCUS       WP_010820412             764 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus faecalis].
ACCESSION   WP_010820412
VERSION     WP_010820412.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..764
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87994
     Region          4..757
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mkqikrlfqi dpwkirtthl dkenlrlqes ltsigngymg mrgnfeehys gdhhqgtyla
       61 gvwypdktrv gwwkngypey fgkvinainf iamdlqidgq tidlattpye dfsleldmqn
      121 gvlsrqftiq tpknkvrfsf erflslekke aayihltiem legtgtitlh skldgdvqne
      181 dsnyeehfwe eraietqetl gfvttktipn nfeierftvt agmrhfidga svvptytqqp
      241 laltaeltvs lnegettait kevlvvtsrd vpetqqitrv nelfsemttl ypeakagqaa
      301 awakrwqlad vviegddeaq qgirfnlfql fstyygeddr lnigpkgftg ekyggatywd
      361 teayavplyl alakpevtkn llkyrhnqlp qaihnaqqqg lkgalypmvt ftgvechnew
      421 eitfeeihrn gaiayaiyny vnytgdedyl kdaglevlva iarfwadrvh fsqrhkqymi
      481 hgvtgpneye nninnnwytn tiaawvlryt resylkfqee ttlkiaddel akwadivenm
      541 yfpvdnelgi fvqhdtfldk dlmpvsdspl selplnqhws wdkilrscfi kqadvlqgiy
      601 ffndafslee krrnfnfyep mtvhesslsp sihavlaael gmeekavemy qrtarldldn
      661 ynndtedglh itsmtgswla ivqgfaqmkt dhqqlkfapf lpatwtaysf hinyrnrllf
      721 vevaadqvaf tlldgpaipl tvydqkytlk drlvlpirke evhv
//
LOCUS       WP_010820489             534 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus faecalis].
ACCESSION   WP_010820489
VERSION     WP_010820489.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 534)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..534
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=61635
     Region          170..532
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mcvyvtytin lsidsqknna vsqidsyvtn knnaatnmin elagsaskie nmrkymelsp
       61 peyfdytysq wsedrvsthf gnnlstlfst fpdleeviir ldefdqvlfa nrtatngkkm
      121 dmssikkhgf qlmriisdpy tgqplgelyt vfssqellgn qadllkksgi nafiydsagn
      181 qifsekaqft keeerqldkr mhtdsdiqqv fhnryditei essgrstill ltsrrvlfqq
      241 lfmnyaailg iglllivill vglnrlfkry sqqvqlilea traigdgnlk eridtnqvqe
      301 elndiasain fmvdsldqyi hdiytleikq rdahmralqs qinphflynt leyirmyals
      361 rqqeeladvv yafstllrnn inqektttla eeisfcekyv ylyqmrypdq faykfeieet
      421 iadveipkfi iqplvenyfv hgidyqrqdn aikvhayreg ekiivavvdn gkgitanrle
      481 eirerlnqte ieteqsiglr nvherlqrff gesygltieg kegegttirl sfva
//
LOCUS       WP_010820665             746 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Enterococcus
            faecalis].
ACCESSION   WP_010820665
VERSION     WP_010820665.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 746)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..746
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82376
     Region          1..>81
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          106..705
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 micqncqqne atihlyanvn gqrkqldycq scyqklknqa nnspqnmgqd pfgfgslddl
       61 yrslsrqmqq gnpyeqqtpp tqfgdggngg qpprggagag qgllgeygin iteaarqgdi
      121 dpvvgrdqei krvieilnrr tknnpvlige pgvgktavve glaqkivdgd vpqklldkev
      181 irldvvslvq gtgirgqfee rmqklieeit eaenvilfid evheivgaga agdgnmdagn
      241 ilkpalarge lqlvgattln eyriiekdva lerrmqpvqv deptvaetit ilhglqkrye
      301 dyhhvkytde ainaaanlsn ryiqdrflpd kaidlldesg skmnltiqlv dpktidkkla
      361 eaeqqkqqas aeedfekaay yrdqinklqa mkekqisdee tpvitekdie aiveqktgip
      421 vgdlkekeqt qlknlavdlk ahvvgqddav dkvakairrn rvglgkqnrp igsflfvgpt
      481 gvgktelakq lafelfgsed smvrfdmsey mekhsvskli gsppgyvgyd eagqltekvr
      541 rnpyslilld eiekahpdvl hmflqilddg rltdaqgrtv sfkdtiiimt snagtgavea
      601 nvgfgaareg vtksvlgqln nfftpeflnr fdgiiefkal skenlmnivs lmleevngll
      661 akqklhievp tevkeklvdl gydpamgarp lrrtiqeqie dgiaeyyldh penhqlvaal
      721 dnegkiivtg aqevtktets tsdqae
//
LOCUS       WP_010820769             346 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010820769
VERSION     WP_010820769.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..346
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38720
     Region          1..346
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtfvdlkdir vsydgkqdil kdlnismekg elvsllgpsg cgktttlrvi aglikpndgq
       61 ffvdqeeltk vpvhkrnfgm vfqsyalfph ltiaenvafg lklrkeskqt mdqkvtemlk
      121 vcgleslgdr ypkqlsggqr qrvalarali iepkllllde plsnldaklr vamrieikri
      181 qqqlgittvf vthdqeecfs isdkvaimnn gvieqydspe tiyrlprtkf vaefigfenf
      241 fsvekmeagh yrtqtnqivk ttnpepnvtt tvatirpedi eivsepatnt vagtvavrtf
      301 lgksyqyeve talgtllvng tseqlyetne tihlafpaek lvilek
//
LOCUS       WP_010820960             366 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Enterococcus].
ACCESSION   WP_010820960
VERSION     WP_010820960.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..366
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42247
     Region          231..353
                     /region_name="FUSC_2"
                     /note="Fusaric acid resistance protein-like; pfam13515"
                     /db_xref="CDD:433273"
ORIGIN      
        1 miviyffstk sqqffayvwa ifpviafflv sfytldflfs psylimvpvf timfkinykk
       61 dysfvallkm sirqfvisfl afiasssfsw siilnssvtf livylfyssa tpmryhsylm
      121 mftfcqliqv kgntflmqsq vvafliglfl laltlnawwq tglsqltslk srghksiqln
      181 mkqqkltvvn fwhdlqqtfl gitsfkqfle spdervqrfr lairmsftit lsfilmwsvg
      241 gikiiwipmn vflllhpvka emntriktrf wgtllgcfls lfvvnwlqlp lthlvvssli
      301 gifvyalkpg tvlqvtmati fglclatisl rgmyaaelrv sfvllaifvv clidlglfvy
      361 qrilrf
//
LOCUS       WP_010820961             713 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Enterococcus faecalis].
ACCESSION   WP_010820961
VERSION     WP_010820961.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..713
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=81504
     Region          3..712
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mniqaidtrh gtanqhsfsn gnclpytgvp fgmnfyapqt tdqkgswwfh pedrtfqgyr
       61 vthqpspwmg dfshllmtpv sgslselslf haqssyrpee slfspveinl tqlryqitsq
      121 lipsmyggil tidyqqkdnh llltlpgryq vkqlddhqva vkvinysgce dpdfsfyfvl
      181 hfeqpltkwf apssgedgki llsfgniaqq vvhfsssfis ekqaqlnlar eislrsteml
      241 qqgiadwhny fdrlkvthen pehtktfyht lyrtflfpqt fyeldenqqp ihydtfsqtv
      301 rpgvlytnng fwdtyktvyp lfsliaqeky eemlegflns ynetgflpkw lspderglmp
      361 gtlidaviad aavkkirpdl mpqfleamkk gatqqseren ygrqgtldyl kygyvpstyh
      421 esvnhtldya ysdfcisqva ktlndsetat fyrqqalnyq qlfnpetgfm qakdtegnfr
      481 pdfldirwgk dyaegsawqs sfavyqdfag liklygsela fekkliqlcn qapnfnvegy
      541 gfeihemsem aaidfgqlai snqpsfhypf lfsyigkpem aqpllkqlmq tfnasptgyp
      601 gdedngsmsa wyifnslgfy pvtpgtgeyv igmplvqtae vklsngkqlt iqtspnkvqq
      661 qfiheiqlnq ekhtapyfth qellnggtld yqlgivpnpq ntaerpfsls tek
//
LOCUS       WP_010821052             648 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus faecalis].
ACCESSION   WP_010821052
VERSION     WP_010821052.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..648
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73746
     Region          6..534
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          571..643
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 millqanqva rhfgsetlfe nihleiatks rialvgrnga gkstflkiia gidapdsgti
       61 aknktatlgy laqntglesd ktvweemtka fadilemeqr mreletkise mdpttsvyeg
      121 ilkeydqlqh tfsekngygy eneirsvlhg fgfdesfytk diqtlsggqk trlalarmll
      181 qkpdililde ptnhldietl swlesylpsy pgallivshd ryfldkvvne vyelsrkkmt
      241 hykgnyskyl elkaeqlase wkayekqqee inkledfvak nlvrasttkr aqsrrkvlek
      301 mdrldrpqgd eksahflfds ekvsgnvvlq vedaaigydp ehilsepihl dirrkeaial
      361 vgpngigkst llksiidrip fikgsktfgt nvsvgyydqe qanlhgnktv laelwdehpt
      421 tpekeirsil ggflfsgddv ektipllsgg ekarvalakl amdrdnflil deptnhldid
      481 nkevlenali dyegtilfvs hdryfinria tkvvelsekg sklylgdydy ylekkqeeee
      541 iaallaneea akkpepvtak ntfyqnkeqq kllrtlqrki tqveenlaql dttiaqleaq
      601 msqpdilenh vellalnqql ddarqqqdel leqwenfsle leemennn
//
LOCUS       WP_010821035             439 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            faecalis].
ACCESSION   WP_010821035
VERSION     WP_010821035.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..439
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46085
     Region          25..431
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mnekkeqalf eydaklsise aipmglqhvv aavvgivtpg imiakvcqls psdttiliqt
       61 slifsavatl iqlfpifgkv gsrlpvmmga sfayvpilma igadfgiaai fgsqlvgsil
      121 viivglfikk irvlfpplvt gtvilsigls lfpvaikyma ggagsadfgs arnwlvallt
      181 faivfyfnyf skgflklsai lngmvigyli slalgmvsfe pvqnakivqv itpfhfgldf
      241 qlvpiftlvv mfivdavqai gqftattvga mdrdatdeel sggimgsgft nfigslfgsi
      301 pvatfgqnvg lvtvtkvink yvlvfasvil liagfvpkva allttipyav iggatisvfa
      361 sismtgirmi asqemtprnt gvvgtalafg igvtlstgsl agfptwvtti fgnseviltt
      421 lvavllnvil kpkkrvale
//
LOCUS       WP_010821183             520 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010821183
VERSION     WP_010821183.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..520
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59673
     Region          7..139
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          244..516
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msvrvndllk lpslreatvl sgknqldtsv aslsflevsd mslfseklhk tneyhageil
       61 igsfcairhd vvkqcetirh lhelgevgli lyyvgiiipk vaeeviqlad slgfiliqmp
      121 kndptlryne viyevmkllv nknkmasfat dllekvsllp eqnrsvemtl kilsdflkvn
      181 ialttytnei istinwprst klpltkllyq sqekvalget tyfitsqklp qkdgqtlkly
      241 fireeeqlts femnqavevv qmalnlwgkn ydevseyalv qaiindesdk myqlakklmi
      301 dissvetmwl lpiwqqgqei haiqqdlkdf lryyyqttiv qqtenylivl lgnylhkqpe
      361 atiskeylqa tdyqdylgei ilcpkvrntt evrvsyqtan qvapflkrvy pqrkvlsiae
      421 irtvqqmmtc lqageeaiqq rlaviqpllk eseqlmtlgt flldassdfk ecgerlfvhk
      481 ntvkyriski nealgydmtn aaeayevyla milyrlvtne
//
LOCUS       WP_010821201             343 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Enterococcus].
ACCESSION   WP_010821201
VERSION     WP_010821201.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..343
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37107
     Region          <39..177
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mkkilisvlg vlsivvsmvl ssysvnaasn dwswplgkpy agryeegqqf gntafdrggt
       61 yfhdgfdfgs aiygngsvya vhdgkilyag wdpvgggslg afivlqagdt nviyqefsrn
      121 vgdikvstgq tvkkgqlign ftsshlhlgm tkkewraahs swnkddgtwf npipilqggs
      181 tptppnpgpt nfttnvhygl hvlggswlge vtnfnntndg fagypnrqhd mlyikvdkge
      241 mkyrvhtaqs gwlawvnkgn kndtvngvag iqgqaidgvq lnyitpkgek lsqayyrsqt
      301 tkrsgwlkvs adngsipgld syagifgepl dhlqigisqs npf
//
LOCUS       WP_010821184             831 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Enterococcus
            faecalis].
ACCESSION   WP_010821184
VERSION     WP_010821184.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..831
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92530
     Region          1..812
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mdelftesak avlaiaqeea kyfrhqsvgs ehlllalvle pngiagktlr qlntdtedir
       61 eeiehlsgyg tmqspmgnnn lylpysprak qifayagdea krlgaqkigt ehlllgllrd
      121 eeilasrilv nlglslskmr qlllkkmgvs kpngaqrrrn gqsknapqgt ptldslardl
      181 tklareqsld pvvgrgtevr rliqilsrrt knnpvlvgep gvgktaiaeg laqkivnrev
      241 pedmqgkrlm mldmgalvag tkyrgefedr lkkvvdeiyq dgqvilfide lhtligagga
      301 egaidasnil kpalargelq tigattldey qkyiekdaal errfariqva eptpeeaeei
      361 lkglrsryek hhgveitdea lhaavqlsir ylndrqlpdk aidlmdesaa kvrldkadqp
      421 seinelrtei sqlitekeea iqnqsfesaa rirqkekqvm ekleeliavk ekslsgystq
      481 vteedvagvv sqwtgvplqq lekkeserlm eletilhqrv vgqneaveav srairrarsg
      541 lkdparpigs fmflgptgvg ktelakalae amfgseeali rvdmsefmek ystsrligsp
      601 pgyvgyeegg qltekirqrp ysvilldeve kahpdvfnil lqvlddghlt dakgrkvdfr
      661 ntilimtsnl gataireekh vgfnvkdisk nhelmqkrim eelkkafrpe flnridetvv
      721 fhslkqeeih eivkimsqsv vkrmaeqevk vkitpaaiev igkvgfdpey garpirralq
      781 kevedrlsea llsgqiqlgd kvtlgaskgk itlnvrapka pkteakelqt v
//
LOCUS       WP_010821223             260 aa            linear   BCT 01-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Enterococcus
            faecalis].
ACCESSION   WP_010821223
VERSION     WP_010821223.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10053807
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..260
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31270
     Region          16..83
                     /region_name="HTH_ARSR"
                     /note="Arsenical Resistance Operon Repressor and similar
                     prokaryotic, metal regulated homodimeric repressors. ARSR
                     subfamily of helix-turn-helix bacterial transcription
                     regulatory proteins (winged helix topology). Includes
                     several proteins that appear to...; cd00090"
                     /db_xref="CDD:238042"
     Site            order(17..19,33..35,44..45,50..51,53..54,57..58,60..61,
                     67..69,74..76)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(33,36,83)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mkpllynyyi dftkkdktrl iilcllhelr visvqqlidf fqierlsaes tvykhlnllk
       61 tdgliarskn gmhtfyyltk eghnyiggyy tlpkvpeynl qhhlqindyl ikmlelcnnh
      121 shlkavvser rkvyevkdek knqkgvkyfv pdfifmflds igrevewqfe ieltlktkrr
      181 ysqgvfpkyi khlknyedar liyvtpssii keeldmfkey fidkegdeyk evfdrlhvfs
      241 aeefepnmkk lieedtfinw
//
LOCUS       WP_010821340             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: methylated-DNA--[protein]-cysteine
            S-methyltransferase [Enterococcus].
ACCESSION   WP_010821340
VERSION     WP_010821340.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..163
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18139
     Region          19..162
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 makkiyyaqq ewqndhyylg vtdaglafvg sanqsieelk nwypqaqlea sekktapyke
       61 alisylnqds ttfacpidie gtpfqkevwq alqeipyget mtyqeiseki grpravravg
      121 taigknpllm vipchrvigs kgqltgyrgg lamkqalltf eqs
//
LOCUS       WP_010821346             828 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase
            [Enterococcus].
ACCESSION   WP_010821346
VERSION     WP_010821346.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 828)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457611
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..828
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87467
     Region          1..67
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          75..139
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          163..814
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(461,463,769)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(505..507,571,587..589,618,658..660,680,683,686,705,
                     708)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(770,798,802)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mesktfdieg mscascaqti ekattklpgm akasvnlate klsvtydqte vteeeikeav
       61 sdagykaisp aqqrtfaieg mscascaqti ekavnqlsgv qqaivnlate klvvsyddhq
      121 vtsaeiikav tdagyqatee vaagatadqd rekkqkhiae mwqrfwissv ftvpllyiam
      181 ghmiglplpd flnpmthatt famvqliltl pvlyvgreff tvgfkalfkg hpnmfslval
      241 gtsaafvysl ygtvmiflgd tsftmalyye sagviltlit lgkyfeavsk gktsdaikkl
      301 mglapktahi lrdgaeievp vdavqlddiv ivrpgdkipv dgvivsgsss vdeamltges
      361 lpvekkvgda vigasinkng sfqfkatkvg ketalaqiiq lvedaqgska piaqladkis
      421 gvfvpivigl avlsglawff lgqeswifal titisvlvia cpcalglatp taimvgtgkg
      481 aengvliksg daletthkiq tivfdktgti tegkpvvtdi lvadsalsea elltlaasae
      541 qgsehplgea ivgaakerql plaegsdfsa ipghgirvtv nervlllgni klmkeeaiel
      601 stfvqqadrl aeegktpmfv akdgsfagii avadtvkdss qtaiarlhkm gieavmitgd
      661 nkrtaeaiak qvgidrvlse vlpedkalev kklqaegkkv amvgdginda palaqadvgi
      721 aigsgtdvam esadivlmrs dlmdvptave lskatiknik enlfwafayn tlgvpvamgv
      781 lhlfggplls pmiaaaamsf ssvsvllnal rlkgfkpstv krtsgsqk
//
LOCUS       WP_010821354             261 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Enterococcus].
ACCESSION   WP_010821354
VERSION     WP_010821354.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..261
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28278
     Region          68..261
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          68..96
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(98,100,104..105,108..110,112..113,117,120,129,165,
                     167,171..172,175..177,179..180,184,187,197,199,201,
                     205..206,211..213,215,219,223,226,235)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          98..129
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          165..197
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          199..235
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mgllsvvtip llaacqgget psaasknsqt vttqssakte ststtrsvaq ttskeevkep
       61 mktyevgall eaanqrdtkk vkeilqdtty qvdevdtegn tplniavhnn dieiakalid
      121 rgadinlqns isdspylyag aqgrteilay mlknatpdlt khnryggnal ipaaekghid
      181 nvkllledgr edidfqndfg ytalieavgl regnqlyqdi vkllmengad qsikdnsgrt
      241 amdyanqkgy teiskilaqy n
//
LOCUS       WP_010821409             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_010821409
VERSION     WP_010821409.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..143
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16205
     Region          11..143
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mhvaqtkdtm sdlyldavrl rqrvfvaeqg vpeemeidey eahcihfvly tnhvavatcr
       61 llplengimk lqrmavekay rgadygrvim eaaenfakeq gyhkitlgaq vtavgfyerl
      121 gyqktgapfm dagiehyemn kel
//
LOCUS       WP_010821450             488 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MDR family MFS transporter [Enterococcus].
ACCESSION   WP_010821450
VERSION     WP_010821450.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..488
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52145
     Region          14..407
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(21..22,25..26,29,60,110..111,113..115,118,138,
                     141..142,145,269,272..273,276..278,281,309,313,365..366,
                     370,374,390,393..394,397..398,401)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 maketnvklv tvsvfvatfm taiegtivst amptivgslh gmeimnwvfs iylltnamlt
       61 piygkladki grkpvfmigi iifilgsslc gfaqdmltli iaraiqgvga gailpvalti
      121 iadmysldkr akilglnsaa wgiasifgpl aggfivdtvg whwiffinvp iglvllglis
      181 iflvepkrer tkmpmdilgs vtlmavlltl llgfqmisdn gftlvtfgcl slsvlffvaf
      241 vmiekraqdp vidlhlfnqp tfvlvnliaa lisgflmgid vyipmwmqgv lgksagiggl
      301 vlapmsllwm agsfiassfm ekyamkkvlt iglsillvga iflvvmpmav pfwlffvvss
      361 vlgvgfgiti ttttvtaqst vepekmgvat sfntlvrtig qtvmvsifgv ilnagmfakl
      421 easalnvdad vmnqlvnpht anlipaallk plrgilyagl hnvylvgagl vvvalllnif
      481 akaqrvkv
//
LOCUS       WP_010821484             296 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ring-cleaving dioxygenase [Enterococcus].
ACCESSION   WP_010821484
VERSION     WP_010821484.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170060
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..296
                     /product="ring-cleaving dioxygenase"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33523
     Region          4..122
                     /region_name="PcpA_N_like"
                     /note="N-terminal domain of Sphingobium chlorophenolicum
                     2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and
                     similar proteins; cd08346"
                     /db_xref="CDD:319934"
     Region          147..292
                     /region_name="VOC"
                     /note="vicinal oxygen chelate (VOC) family; cl14632"
                     /db_xref="CDD:472697"
ORIGIN      
        1 mhaqfhhvsl larhgqenqs fytkllglrf vkntvnqdnn rmphyfygdy qgtpgslvtf
       61 fivpllgnry eeknylatig lkipqnslsf weqrltenki pfnkkekslh fsdpddthii
      121 ltevpenplk etlvvsndip aavqiiglts tefhvpdsek tlaffetflg wqavgntiil
      181 setesfsvhq ttsdktsrmg rgsmdhiafs vaddealqel htralaqgwe iemyvsrgyf
      241 kslyirepgg nrvefatlap gftldepleh lgetlalppf lepkrtaiea nlykdm
//
LOCUS       WP_010821512             255 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: putative ABC transporter permease [Enterococcus].
ACCESSION   WP_010821512
VERSION     WP_010821512.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..255
                     /product="putative ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29692
     Region          8..176
                     /region_name="COG4905"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443933"
ORIGIN      
        1 mekmsqvill ffiysfigwl wetvycslka kkfvyrgflv gpycpiygfg vlsvlyfvep
       61 fennllvlyv gsavlvtile yitsyglekl fhaswwdyhd vpfnlngrva lpvslfwglg
      121 cvlivkviqp eiakvvsflq atfgnylalc ivivmgldli ytllnmqgfk klitemgqtl
      181 etnqqefkqr lntkmeiata dwqklkertk kehfqnrlnf qqrrfinnyp kltlknikns
      241 kevrhlledl kkkgq
//
LOCUS       WP_010821525             142 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Enterococcus faecalis].
ACCESSION   WP_010821525
VERSION     WP_010821525.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..142
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=16315
     Region          54..>112
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mnnyvenqfd kivtkyqpss vydlvkkanc kilyadidde tggctqtndr chtiivnanw
       61 pehyqkfvil hefshiklhk gastpfyhsl gldtfvskme ceanslamkl llhmqdqsii
      121 hgltkfqimd ylglphelsk yf
//
LOCUS       WP_010821566             487 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010821566
VERSION     WP_010821566.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..487
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=51689
     Region          1..478
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mnglmawmek yilptaakig aqkhlmalrd afigtlpatm agsvavmina iirdlpqefv
       61 styaaslead kgifavlnvi igingfvwng tlaiaglifa fswgynlaka ynvnelaggi
      121 vslatlisgv afapnntael avkvpekian aingaeigas iannqltvnp wgwlnlnhln
      181 gnafftvmim galstiifck lmqadltikm pdsvppavsk afaailpati alyvvaiinf
      241 tvsklsggql lidliqkyia epflglsqgl gavlivtvfv qifwffgihg pnvlapvleg
      301 iwgqaqlini difqkgyegk tgtaavlaai ddgkaymwvr gsfdafawfg gsggtivlii
      361 aillfskrad yltvgklslg pgifninepi mfglpvvlnp imfipfviap lvattigwva
      421 tylglvapvs qqvawvtppl llsflatgad wrapivalvc mvvtfliwtp fviaankmdp
      481 algeseq
//
LOCUS       WP_010821616             294 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YitT family protein [Enterococcus].
ACCESSION   WP_010821616
VERSION     WP_010821616.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..294
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=32480
     Region          7..283
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 meeqrfyfkd vlfivlgsci yafglvtfni andlaeggvt gitlilralf hfnpayttll
       61 inipllligg kilgkrslyy tligtvslsv flwfwqkfpv einldhdlli aallaglaag
      121 fgsglvyrvg gttggtdvia rifekyfgis mgrslllfdv avlllsltyi dvkrmmytli
      181 vsfvfsrvvd svldgayaak gilivsnhse eigqslmasl ergvtylnge gaysqvekrv
      241 lytvvsprei mevkrianei ddkafvsiin vheaigegft yakpskqrrf klkq
//
LOCUS       WP_010821610             238 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [Enterococcus].
ACCESSION   WP_010821610
VERSION     WP_010821610.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26640
     Region          1..226
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 merlqkaiah agvtsrrkae elivkgrvkv ngqvvkelgt qvskqdtvev dgvpiyqeey
       61 gyylfykpkg visavsddkg rkvvtdyftd vteriypvgr ldydtsglll ltndgsfsqk
      121 lthpkhevdk vyvakikgvp tkrdllplak giridgkrta panfqilsad iktgssvvel
      181 tihegrnhqv kkmfqavgfp vqklkreryg eltlqglrpg qyrdltkkei sqllnqak
//
LOCUS       WP_010821710             512 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus faecalis].
ACCESSION   WP_010821710
VERSION     WP_010821710.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..512
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57828
     Region          6..509
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msiltiehlt hrfgekvlye easlqvnkgd hlgltgqngv gkstlikilt gevlpdegti
       61 qwqknckigy ldqhvsveqs ltmvdflkqa fqelfdkeak ltklyeeysq taseklleqa
      121 gklqtdldes nfyqidtiiq dlanglglqa igldkklgel sggqrskvil akllleapdv
      181 llldeptnyl ddthiqwlvr ylnnfegsfl lvshdyqfln evtnciadie fgkltkytgn
      241 veksfaqkeq nkqtylkqyq aqqekiekme ayirkykagn ratmaksrqk qldrlerltp
      301 pgsltkpaie fpyqglvatq alttqklvvg yrepllepld lmvhvgekva lkgfngigks
      361 tliktltkvi psldgefhyp lntkiayftq dlvwpneqlt pldylsdrfp dttikerrsh
      421 laraglpdkl amqslallsg geqtkvklae lmmqtsnllf ldeptnhide aakkslqeai
      481 hvypgtvflv sheadfyeei vdrvidieel vk
//
LOCUS       WP_010821766             196 aa            linear   BCT 01-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Enterococcus faecalis].
ACCESSION   WP_010821766
VERSION     WP_010821766.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..196
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21899
     Region          1..192
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mskllvvkah pltkeesrsv raletflasy retnpsdeie ildvyapetn mpeideells
       61 awgalragaa fetlsenqqq kvarfneltd qflsadkvvi anpmwnlnvp trlkawvdti
      121 nvagktfqyt aegpkpltng kkalhiqsng gfyegkdfas qyikailnfi gveqvdglfi
      181 egidhfpdra eelrrl
//
LOCUS       WP_010821789             244 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tRNA1(Val) (adenine(37)-N6)-methyltransferase
            [Enterococcus].
ACCESSION   WP_010821789
VERSION     WP_010821789.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..244
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27413
     Region          6..244
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mllsgeridq lyaddiqiiq skevfsfsid avllanfpql pkkgkivdlc agngavglfv
       61 srktaamidq ielqprladm gqrsillnkl ekqvtmyerd lkqatevikk dsvdlvlcnp
      121 pyfkerptsq knpnphlaia rheihtslqe vvtvsadllk tngrlamvhr pdrfldilha
      181 menaniapkk arfvypkpgk eanvlliegi kqgkkdgfrv lpplftynek neyeaemkam
      241 lyge
//
LOCUS       WP_010821830             367 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Enterococcus].
ACCESSION   WP_010821830
VERSION     WP_010821830.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..367
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42064
     Region          149..353
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtdrisrrmi slyaslstfi vilitlfsyf hsikqnrwll ellqrkvfyl plivhivlis
       61 lliglltfll islvqkgqyg rieeklrlla ngnyespvln kpttsenqdh ylteveqdiw
      121 siknkllems kelqllnsrp qlmdgqtkee ilenerhrla relhdsvsqq lfaammmlsa
      181 lneqaqrtet pepyrkqlam vaeiinasqs emralllhlr pisleekslr kgieqllkel
      241 qtkikieliw dvedvhlnss iedhlfrivq ellsntlrha kakelevylh qvdknvllri
      301 vddgvgfdmk eqsnkagsyg lnnirervvg mggtvkiisf kgqgtsveik ipvikeetas
      361 dqsnvsg
//
LOCUS       WP_010821845             245 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [Enterococcus].
ACCESSION   WP_010821845
VERSION     WP_010821845.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..245
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26685
     Region          3..242
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mkslsekviv imgassgige atarllarkg aklviaarrq erliaikkel peatilvqqa
       61 dvtkeeevqr vikltmekyg ridvlfnnag vmptapliea pkgewhqmld inimgvlngi
      121 aavlpimveq ksgqiiatds vaghvvypds avycgtkfav raimeglrqe qrenniksti
      181 ispgavqtel yqtisnrvva etlhleqlsw glkaediaqa vvfaidtpdr msisemvvrp
      241 ttqti
//
LOCUS       WP_010821861             402 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010821861
VERSION     WP_010821861.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..402
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43907
     Region          6..402
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkrsiiwkta frsilknkrr slltmlgivi giasvitiva igngfkedmv dklsaekqke
       61 nvkkisfsay ntsdmfsdqa mftdndlgvv rmvpgvekid fdqrevdgtq kgtlnfqagp
      121 knlsvtyela dkttkellvg rqlndgdnak ldktvvvdel vakelyqdpt aavnrtfpyk
      181 eqlftivgvt tntsgaigpg nddsllyfpk ktyehyfgkl kdtstlkltv apgyqpdqvl
      241 ketiktlsqq gtmknsgtyq eynvkdtike mgsllnnltl fisaiaaisl viagvgvmnm
      301 myisvserik eigirralgg tasdikkqfl tegialtlig gitgyllgmi iaylasmalp
      361 fsvrpdlmtv slaigisvfi gvvfsyfpas aaskkdlidi mk
//
LOCUS       WP_010821885             151 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus faecalis].
ACCESSION   WP_010821885
VERSION     WP_010821885.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..151
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16719
     Region          5..146
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 meeqmyknil vgvdgsdqan layeraieva rrngsrviva nilenqvytm mgystlndql
       61 idqetaaaee liadckkyae svdfhnvetv tmfgspkevm shelpekynv dlimvgqsgl
      121 navervvmgs vssyiirqap cdvlivhsee k
//
LOCUS       WP_010821869            1047 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Enterococcus faecalis].
ACCESSION   WP_010821869
VERSION     WP_010821869.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1047)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1047)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1047)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1047)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..1047
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=120694
     Region          8..951
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mklsvndeat venkliailg edrnqwtyra dlkseqdlwr nlrekiiqnn laaigehplt
       61 dqeferiktg llertrtpfe aakwlkgeng iakitiered aslgtmslil ysnrdigggi
      121 ssyevvnqia kkntnsakhd srfdvtllin glpivqielk qvtakdgvfq afnqikkyae
      181 egmfrnnifs tlqlfvvsne qttryfanal pqfmhkkflf swrtkdnkkv enlyefcrqv
      241 lnipdahrli adytivseeq dnkvlmvlhp yqihaiealy vaaskhtsgy iwhatgsgkt
      301 ltsfvstkll arkpgidrti mlldrkdldn qttseftkfa sefntgissg dgkanslivg
      361 tgsakelskt lladansnvv ivttrqklda alkyarkqee qkgtnrfqkl mgqhivfivd
      421 echravsaen mmdvkkvfpr stwfgftgtp ifeenkkqaq gqlartthdq ygevlhtyti
      481 knaledkavl gfqvehedti dseslykkiy dglsnetkya eytpeelane veamdniqke
      541 kmldrsiyen dkhiqevihk mfrpnnaytk fdfgngrprk sailttssid makryyhaik
      601 kmtakenwle eefpkhqirq grtmedpdfp riaityslee naenssaqqd elakimaeyn
      661 ayygtswtlq dieryngdin nrlarkkaef kefgrhvdlv ivvdrlltgf daptiqtlfv
      721 drnleyanli qafsrtnrty pdktkglvvt frkphtmeqn vanatrlyse akeesgliyp
      781 tykeskqrfk kafrkmqefn peeidenqpi dvridyvqsf qalsnsyeal vtydeyndem
      841 ekspalaeqv hlieeqigty etikgslvkv epgpdkdfse iefysdnhak mydidssyid
      901 qllgnysans qgvreeieka lqklnktecv kevyreilna mdnekvdqke dvfvlkrryf
      961 tgtrnqviaq faqewfvsed qlhssaiqym igmnpipnmg diisskdfes ykathpeakp
     1021 fkypqqmkra wrqtldeylv pledelr
//
LOCUS       WP_010821910             442 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus faecalis].
ACCESSION   WP_010821910
VERSION     WP_010821910.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 442)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..442
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50317
     Region          46..416
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 marfvfilsn itavvqvffn ylkskvvkln kkitlhsifg lmviailngk iisaigmygf
       61 awiylsiiil gyffisksli evlginsyiv iisaisgqfv sfikekifgt elifssnltm
      121 flhstfrlal sviltilmik gikklekkfs iineclllfn ligigtmiiy ytslilgkyl
      181 gnnkeiivvn sifltlylvv slisfivyls slknkydiqq keteylenqr ymeamekqfk
      241 eirkfrhdyk nilnsledfi vsgdyeslnd yyfskikkas kcidqngfkl eaignirvre
      301 vksllvskli stqekgmdvq levtepieel aidsislvri lgifldnsie eieflgegkl
      361 viavykdasa vhiiiqnscr knlpkfhllk qrgfslkgtd rgmglsnvqe llqslnnvql
      421 atsisdgwft qkltiennrr ce
//
LOCUS       WP_010821940             165 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Enterococcus].
ACCESSION   WP_010821940
VERSION     WP_010821940.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..165
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19570
     Region          13..164
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mvfdgwkrkk qiraletlvd tkyekmyria fnythskeda ldviqesfek alkaiqkgpd
       61 ikdfeawffr illsvatdyw rkkkreavhi ekdehvlall nnsqrsflei eeiinqldsp
      121 nreiillkff egftlkeial ildinentik tkmyrslnel rslln
//
LOCUS       WP_010822053             337 aa            linear   BCT 01-JAN-2025
DEFINITION  lipoate--protein ligase [Enterococcus faecalis].
ACCESSION   WP_010822053
VERSION     WP_010822053.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000589
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..337
                     /product="lipoate--protein ligase"
                     /calculated_mol_wt=38442
     Region          2..249
                     /region_name="LplA"
                     /note="Lipoate-protein ligase A [Coenzyme transport and
                     metabolism]; COG0095"
                     /db_xref="CDD:439865"
     Region          251..335
                     /region_name="Lip_prot_lig_C"
                     /note="Bacterial lipoate protein ligase C-terminus;
                     pfam10437"
                     /db_xref="CDD:431286"
ORIGIN      
        1 mryvimqsrd irenlatedy llntlsfeep lvlfyiqepc vilgrnqnay eeidlayare
       61 kgivitrrls gggavyddlg nvsfsfvvre ghqafgdfka ftkpiiealh kmgatgaeis
      121 grndllidgk kfsgnamytk kgkmythgtl mydvdlaevk rvltvskkki eskgtksvrv
      181 rvtnlrpyld ekyqqltiee frnrllmelf dveslteiae keyvltkadq qeirklvaev
      241 ygneawifge apkftikkee kfkggivdar ltvekgkiie ltiygdyfak ketaeivaal
      301 lgvdyqyssi wqalaafnfe dyfvnitkee fvhllvd
//
LOCUS       WP_010822130             324 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus faecalis].
ACCESSION   WP_010822130
VERSION     WP_010822130.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..324
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37164
     Region          93..324
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkkksiglll asaylfhtrs rqkslkaclf edslrlsqia rlernpkvtk afyhwqrsln
       61 eqvtlpkhlr hlfplqemtq fptmyrmsns viaptkkavl ylhgggftln laysqldfsy
      121 kliedlpfat dyfipvypla pnksfadiyn hcyaayqeil qhydpedvil lgdsaggtlv
      181 lnvlqnlatd fperlpkaav lispwldghl dipvaksyqk kdkmigmnyl qliaqeiddt
      241 anhstlslnc lsfdyqkfpp lffvggthev fcpsyhqflk qlgprpqdtc rlvpgmqhvf
      301 amkqylpegr qarkqiaqfi qeqw
//
LOCUS       WP_010822153            1047 aa            linear   BCT 01-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Enterococcus faecalis].
ACCESSION   WP_010822153
VERSION     WP_010822153.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1047)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1047)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1047)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1047)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..1047
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=120834
     Region          8..951
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mklsvndeat venkliailg edrnqwtyra dlkseqdlwr nlrekiiqnn laaigehplt
       61 dqeferiktg llertrtpfe aakwlkgeng iakitiered aslgtmslil ysnrdigggi
      121 ssyevvnqia kkntnsakhd srfdvtllin glpivqielk qvtakdgvfq afnqikkyae
      181 egmfrnnifs tlqlfvvsne qttryfanal pqfmhkkflf swrtkdnkkv enlyefcrqv
      241 lnipdahrli adytivseeq dnkvlmvlhp yqihaiealy vaaskhtsgy iwhatgsgkt
      301 ltsfvstkll arkpgidrti mlldrkdldn qttseftkfa sefntgissg dgkanslivg
      361 tgsakelskt lladansnvv ivttrqklda alkyarkqee qkgtnrfqkl mgqhivfivd
      421 echravsaen mmdvkkvfpr stwfgftgtp ifeenkkqaq gqlartthdq ygevlhtyti
      481 knaledkavl gfqvehedti dseslynkiy qilsnetkya eytpeelane veamdniqke
      541 kmldrsiyen dkhiqevihk mfrpnnaytk fdfgngrprk sailttssid makryyhaik
      601 kmtakenwle kefpkhqirq grtmedpdfp riaityslee naenssaqqd elakimaeyn
      661 ayygtswtlq dieryngdin nrlarkkaef kefgrhvdlv ivvdrlltgf daptiqtlfv
      721 drnleyanli qafsrtnrty pdktkglvvt frkphtmeqn vanatrlyse akeesgliyp
      781 tykeskqrfk kafrkmqefn peeidenqpi dvridyvqsf qalsnsyeal vtydeyndem
      841 ekspalaeqv hlieeqigty etikgsliev epkpendfse iefysdnhak mydidssyid
      901 qllgnysans qgvreeieka lqklnktecv kevyreilna mdnekvdqke dvfvlkrryf
      961 tgtrnqviaq faqewfvsed qlhssaiqym igmnpipnmg diisskdfes ykathpeakp
     1021 fkypqqmkra wrqtldeylv pledelr
//
LOCUS       WP_010822166             151 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus faecalis].
ACCESSION   WP_010822166
VERSION     WP_010822166.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..151
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16727
     Region          5..146
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 meeqmyknil vgvdgsdqan layeraieva rrngsrviva nilenqvytm mgystlndql
       61 idqetaaaee lmadckkyae svdfhnvetv tmfgspkevm shelpekynv dlimvgqsgl
      121 navervvmgs vssyiirqas cdvlivhsee k
//
LOCUS       WP_010822231             709 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 65 protein [Enterococcus].
ACCESSION   WP_010822231
VERSION     WP_010822231.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 709)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 709)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 709)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..709
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=82164
     Region          2..701
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mkiyfndydk etlekaetll fngnghigfr anleeeyydf fstnretyin gfyetksiqy
       61 pekmhgftpt getmisvvdg qttlitigde rfsiltgeis rseryvdldr gmtvrkliwt
      121 spkgretkik itrfasftdk nlfvanfdfe klnhdepikl ethlnftpik tidkddprmg
      181 heihsvikek vdlaertcgf htensnlhge ikwqfngvss tiseeptriv isseltgksf
      241 tkmlsyrfan yehegldksy eqllneqtdy lrdfwedari eiesdldlee svnygtyall
      301 qslgtngtts iaakglsgsg yeghyfwdte myifplfltm rpdlaksilq yrintlekak
      361 enrkifgyqt galypwrtis gtessaffea gsaqhhinsd iayafinyfi qtndykfmfs
      421 ggfevlleta rvfleigyfk edafhidkvt gpdeytvlvn dnyytnrmvk hqfewvvrla
      481 diladqdine wqelshrlni sveelatmte aaqkmaivid eeknviaqdr dflnkdfwpy
      541 tkeetkypll lnyhplviyr yqvlkqadtv lalmlfpedy sdelvnsttt yydtitthds
      601 slsfsaygtv yarlnepeks yeyflknart dldnlhhntk dgihsasmgg tfmnilygfc
      661 nlkvqdnelv lrphlpkeir kisfnvnfqg dkyrvevnqd ggnlikttk
//
LOCUS       WP_010822349             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010822349
VERSION     WP_010822349.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..282
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31101
     Region          1..282
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mqqnivlsiq drlqqlpkse rkiaeyilkn tetvismnaq elakqagssp aaiirfchsm
       61 dvngftelkl llsanlgqmk qqmytevtkg estadikqkl qarfvhvver sgqtledvav
      121 neavdllekt evifvyglga sslvaqdiyq kftrlgrtvf ttldhhlfas mlgstekpsv
      181 fivisnsgtn keastladla kqqgipivsi tqdeksvige ksdivlqtss gedvplrsaa
      241 tvslvaqlyv vdvlffayaa knyketleki qisrknierl ke
//
LOCUS       WP_010822465             406 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Enterococcus faecalis].
ACCESSION   WP_010822465
VERSION     WP_010822465.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..406
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43725
     Region          2..403
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkkpsmitqi aiavvvgilv gllipassny lkivgdvflr lmqmaipili lgqivqavgs
       61 inpkeltslg grtiavfgis slaaalwgvl mavifnpgyg vkmtgfqdas ikaqeisitd
      121 tilnfvpkni fdsltqgsii qiivfalffg lalnkylqsh petqlfqiiv dfneviitvi
      181 ryvmclaplg ifaliastis hlglqiilpl vkyllvyglg tilflgiwil vitlyckvsp
      241 lrlitnmknm svmalattss aitlpvalee tetklglskr itnlvlplgm slnsngsamh
      301 maftvmtiaq myqlefditk miylaitatf vslanavvpg aglvslaviv pqmglpiesi
      361 aifagvewfv gmlrtilnvn sdvysailva ksvdeidytv fnssnk
//
LOCUS       WP_010822525             337 aa            linear   BCT 01-JAN-2025
DEFINITION  lipoate--protein ligase [Enterococcus faecalis].
ACCESSION   WP_010822525
VERSION     WP_010822525.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000589
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..337
                     /product="lipoate--protein ligase"
                     /calculated_mol_wt=38370
     Region          2..249
                     /region_name="LplA"
                     /note="Lipoate-protein ligase A [Coenzyme transport and
                     metabolism]; COG0095"
                     /db_xref="CDD:439865"
     Region          251..335
                     /region_name="Lip_prot_lig_C"
                     /note="Bacterial lipoate protein ligase C-terminus;
                     pfam10437"
                     /db_xref="CDD:431286"
ORIGIN      
        1 mryvimqsrd irenlatedy llntlsfeep lvlfyiqkpc vilgrnqnay eeidlayare
       61 kgivitrrls gggavyddlg nvsfsfvvqe ghqafgdfka ftkpiiealh kmgatgaeis
      121 grndllidgk kfsgnamykk kgkmythgtl mydvdlaevq rvltvskkki eskgtksvrg
      181 rvtnlrpyld ekyqqltiee frnrllmelf dveslteiae keyvltkadq qeirklvaev
      241 ygneawifge apkftikkee kfkggivgar ltvekgkiie ltiygdyfak ketteivaal
      301 lgvdyqyssi wqalaafnfe dyfvnitkee fvhllvd
//
LOCUS       WP_010822528             281 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Enterococcus faecalis].
ACCESSION   WP_010822528
VERSION     WP_010822528.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11573834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..281
                     /product="VOC family protein"
                     /calculated_mol_wt=31043
     Region          9..132
                     /region_name="VOC_BsCatE_like_N"
                     /note="N-terminal of Bacillus subtilis CatE like protein;
                     cd07255"
                     /db_xref="CDD:319918"
     Region          170..279
                     /region_name="VOC_BsCatE_like_C"
                     /note="C-terminal of Bacillus subtilis CatE like protein,
                     a vicinal oxygen chelate subfamily; cd16359"
                     /db_xref="CDD:319966"
ORIGIN      
        1 mvqalpsnig iqqvtlkvad ldkmvnfytk tiglkllkqg egrawlapqg tndailvlkg
       61 ltageenqgt tglyhiafll ptrkdlgnml lwllqenvqi gaadhgysea lylsdpenng
      121 ieiywdkpee vwdirpngei igvteeldgd rlaaeadghw lgisegskig hihlkvadld
      181 ttetfyknlg fglksnfgqq akffaagqyh hhigtntwsg kqlptiqenq fglenytfrl
      241 ptaadleivq anaeeaklhf iakdhllale dpsgmiiqft y
//
LOCUS       WP_010822759             140 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010822759
VERSION     WP_010822759.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..140
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=16216
     Region          35..109
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cd02208"
                     /db_xref="CDD:380338"
ORIGIN      
        1 mlqkyieilt rdevifrkkp dgtevnyflf pefeihinsl pgktvqgwhk hhkieevllv
       61 qsgkvkieev enqqivsric aegeliqmhn slhrisnpdt lsasftvfrf vpqgknqqec
      121 ikndkeefsd atvqrllknk
//
LOCUS       WP_010823097             648 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus faecalis].
ACCESSION   WP_010823097
VERSION     WP_010823097.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..648
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73839
     Region          6..534
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          571..643
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 millqanqva rhfgsetlfe nihleiatks rialvgrnga gkstflkiia gidapdsgti
       61 aknktatlgy laqntglesd ktvweemtka fadilemeqr mreletkise mepttsvyeg
      121 ilkeydqlqh tfsekngygy eneirsvlhg fgfdesfytk diqtlsggqk trlalarmll
      181 qkpdililde ptnhldietl swlesylpsy pgallivshd ryfldkvvne vyelsrkkmt
      241 hykgnyskyl elkaeqlase wkayekqqee inkledfvak nlvrasttkr aqsrrkvlek
      301 mdrldrpqgd eksahflfds ekvsgnvvlq vedaaigydq ehilsepihl dirrkeaial
      361 vgpngigkst llksiidrip fikgsktfgt nvsvgyydqe qanlhgnktv laelwdehpt
      421 tpekeirsil ggflfsgddv ektipllsgg ekarvalakl amdrdnflil deptnhldid
      481 nkevlenali dyegtilfvs hdryfinria tkvvelsekg sklylgdydy ylekkqeeee
      541 iaallaneea akkpepvtak ntfyqnkeqq kllrtlqrki tqveenlaql dttiaqleaq
      601 msqpdilenh vellalnqql dyarqqqdel leqwenfsle leemennn
//
LOCUS       WP_010823103             214 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: histidine phosphatase family protein [Enterococcus].
ACCESSION   WP_010823103
VERSION     WP_010823103.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..214
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24199
     Region          3..205
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mklyftrhgk tewnqqkrfq gmtgdsplls tsydeikqlg qylqdipfek iysspllrak
       61 ntargiqqel nhpveivytd tlkelglgrl egqyieemrn fygeeldhlr hrldlydpti
      121 fdgepieqai qrisetvaea akqhegpvlf vghgaaltaa iqamagkpls elrtmgglln
      181 nslsiletke asrnmpydlt lwndtsflak ekaq
//
LOCUS       WP_010823107             237 aa            linear   BCT 01-JAN-2025
DEFINITION  HAD family hydrolase [Enterococcus faecalis].
ACCESSION   WP_010823107
VERSION     WP_010823107.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..237
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27666
     Region          1..227
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mrtivfdvdd tlydqqqpfr namskifpnv atedmhelyl rfrhhsdetf pkvlanewsl
       61 dfmrffrmne tlkdlnypgi sqeegkifqq vyeeeldnit mhpevtklld tlqkkeipmg
      121 iitngptdhq fkkvkqlnle kwvpsqniii sqstgfqkpe keifdlacnq fcmepehtly
      181 vgdsydndiv garnggwhsl wfnhrsrelp scqpashlae vtcftelcpt veklfnl
//
LOCUS       WP_010823228             170 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_010823228
VERSION     WP_010823228.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..170
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19694
     Region          3..147
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          86..170
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mgeikkltie dapalqeisi etytdtfgpy ntpenmqayl veaynleklq kelanphsdf
       61 yfifvdnqla gymklnreka qtepmgpekl everlyilpa fkgkklgtql lelaeekare
      121 fgknalwlgv wehndaarsf yktigyryys qhsffmgdde qtdfillkel
//
LOCUS       WP_010823295             337 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Enterococcus].
ACCESSION   WP_010823295
VERSION     WP_010823295.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..337
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37715
     Region          79..336
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkrkivrfil wllgiivvic lgvflafqls pkpgawvinq lfageveikd sasydkalpn
       61 vqlqenqtyp ssrkkntfdl yypqtskqav pvvlwvhggg yvggdksgmk efatrlvads
      121 svafismnye lapdapypsq lqqvnelvqf llekkqaypm ldlsklfigg dsagaqialq
      181 yatvqtnany akelgmtaal pashlkgtls ycgpvdlkqm anqqsdnrfm kffvktvaws
      241 llgtkdwqts aelqevslvd kvtkefppty ltdgnsfsfq eqglalvqrl ktlnvpvsal
      301 ffkdkkatit heyqfdyqtk eakqcyqetv qfvnkyk
//
LOCUS       WP_010823320             306 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidase U32 family protein [Enterococcus faecalis].
ACCESSION   WP_010823320
VERSION     WP_010823320.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..306
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=34324
     Region          1..298
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
ORIGIN      
        1 mieliataes veqavellat gvdtlyigee tfglrlpvsf trdeqreivk rahemdkqvl
       61 vavngimhpe kmklvpeylt flkeinvdki tlgdpgivfi mqrdgleipy vydgetlvts
      121 srqinfwskr gaigavlare vpfeemvame enlavpaeil vygatcihqs krpliqnyyn
      181 ytkndkgvtk deglfisepk kpethysiye dshgthifan ndvnlmnelt nlydhhyrtw
      241 kldglytpge nfvaiarlfa eakaaleagt wsedqaahat aeieklhptg rgldngffdl
      301 sadaik
//
LOCUS       WP_010823415             284 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterococcus faecalis].
ACCESSION   WP_010823415
VERSION     WP_010823415.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..284
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32652
     Region          23..276
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mekeelkile elrrilnskn eaivilnnyf kggvgkskls tmfayltdkf nlkvlmidkd
       61 lqatltkdla ktfkvelprv nfyeglkngn lassiihltd nldlipgtfd lmllpkltrs
      121 wtfenesrll atlleplksd ydliiidtvp tpsvytnnai vtsdyvmipl qaeeestnni
      181 qnyitylidl qeqfnpgldm igfvpylvdt dsatiksnle elykqhkedn lvfqniikrs
      241 nkvstwskng itehkgydkk vlsmyenvff emveriiqle neke
//
LOCUS       WP_010823485             433 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus faecalis].
ACCESSION   WP_010823485
VERSION     WP_010823485.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..433
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48676
     Region          1..400
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mkfleqlpea wqeqwqasgf nepstiqeks ftplregenv lgisptgtgk tlaymlplll
       61 tvekgqgnql liiapsqela mqiaevartw akplqltvqt ligganvsrq idklkkrpev
      121 ligtpgrile lmknkkvkaq llktivmdev dqlfqeeels ltkqilthtp teyqlvfysa
      181 tadrvvnqaq slsqklqvid vteedtsagq vahyfirlap rkkadylrrl ahteafrsmv
      241 ffnqvadlga aegklvyenv paiglasdqs kqlrklaidq fkaervklll ttdiaargld
      301 ftgvpyvvnv dvplteesyi hrsgrvgrmg aqgavitfin dgtkrdyqrl mkqlaipyqe
      361 iflydgalhe qpkakdelek knvakdtyse kkstkerkpe tvnsvvkepq etrkkkknkk
      421 kntknkgark akk
//
LOCUS       WP_010823557             143 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus faecalis].
ACCESSION   WP_010823557
VERSION     WP_010823557.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15747
     Region          4..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msvyqhilva ldgsdqseka fheavriake eqatlylati indaefttcp fsfeelydle
       61 khkseemlte kakqaseigv ktvkkivelg spkrylanti senyaidliv lgatgrgaiq
      121 rtligsttdy vvnhalcnvl vvr
//
LOCUS       WP_010823595             286 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DegV family protein [Enterococcus].
ACCESSION   WP_010823595
VERSION     WP_010823595.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..286
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=31090
     Region          5..281
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mnkekiallv dsgtdvpeal vkqygmyvlp lqiiypekty tdkvditpee vyqrlekeip
       61 stslpdgati qaifdkikea gyekvlavti ssglsgtynv vrllgeqteg ldvfvldtkn
      121 igigagiqai raaelietgl gwqelqqklt eevanakvff nvatleylqk ggriglvtsi
      181 lgnalklnpi iscneegiyy tvaksrgrkk sldktfelvk nfigeaprfr lavahgaaee
      241 eakammerlk aafpqaeeiy fgtispalvv htgpgllgvg iqllnd
//
LOCUS       WP_010823643             477 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Enterococcus faecalis].
ACCESSION   WP_010823643
VERSION     WP_010823643.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..477
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52230
     Region          24..472
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,280,283..284,287..289,292,320,324,376..377,
                     381,385,401,404..405,408..409,412)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mekiksyqed sevqknrwwi lvsvamftfm stldssivni alptiskems vpmnqaewvv
       61 siylmvvcac lllfgkigds fgkikvyrig tviftigsll cgfnqslsfl lfarvvqsig
      121 asmtmatnsg iitevfplne rgralgavga fvslgaiagp gigglilsnf swsyifwinv
      181 pvglitilig ekflpkditk tkekidfsgf aciaiaimtf fggiflgqes gfgslqsyll
      241 fiiavialgl fimverkrks plikfaifkn kiftlsllsa vlifasnffv nvvipfylqd
      301 arklsasyag llmmvfpllm vvgaplsgyl tdkigpailt fggllllcct slmymfldmn
      361 spiwyyviat aimglgnalf qspnntmvms svekqdlgva gsmnsfarnl gmvigialst
      421 tilyrgmsea ygervttyla nrpdifivgm retffvafll cvaafiltil rfrkttk
//
LOCUS       WP_010823666             778 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus faecalis].
ACCESSION   WP_010823666
VERSION     WP_010823666.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..778
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=85722
     Region          10..659
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(300..302,365,384..386,411,463..465,509,512,515,534,
                     537)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(594,598..599,601..602,627,630..631)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
ORIGIN      
        1 mlnkvdlkkg lsteevakqk elglqnnyee nvakstkdii fdnvmtlfnf lnfaiavcll
       61 fvgaysnlaf laiiivnmsi gifqeiharn lvqklsivak envhvvrngv qqeidtkelv
      121 mediviisag eqvssdmevi dgkveaneal ltgesdliek eigdtllsgs fivsgqayar
      181 vihvgaenya vkitqeakvh kpiqselvns irkvskftsw viiplgiilf veafwlrdag
      241 iktsvvasaa allgmlpkgl vllisialtt gviklakkri lvqdmysiet lahvdtlcld
      301 ktgtitegkm kvqkaiilhd kyeelfpqii gsylsestdn nitmqairdh yevsnrfgak
      361 evlafsserk wgaiefpeig tvylgaperl vddsrlpeav ftaqengyrv lmlaiaeqqp
      421 lnetkmpyle plaileiddp irqnaketla ylkkegidlk visgdnpvtv sniarraglt
      481 gyesyidlst ktteaevrea vqqytvfgrv spqqkrtivr elkdtehvva mtgdgvndvl
      541 alreadcsia maegdgatrq isnlvlldsd fttlpdvlfe grrvvnnvtr vssvffikti
      601 ysfilsiica ltaiafpfip iqvtlidlai egypafflsf egdkrkvvgk flptalknas
      661 vnallvvani iavyligqnq gfssldtttl myyllvgisc mavvraclpl nplriflvfs
      721 tiigiyvaam lfhnileigf ltsqtmglff immainivvr vaigfvqmkr agktikdl
//
LOCUS       WP_010823734             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Enterococcus faecalis].
ACCESSION   WP_010823734
VERSION     WP_010823734.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..228
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=26939
     Region          41..228
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mdckncaspi rleitlkmll rfkkwarpsl cqhcqakfqk lpmtgtcfgc grvsqeyycl
       61 dcqrwqllyp eysfhnaalf hydegmqewm erykfqgdyr lrmcfneein fyfqqqsvdy
      121 iipvplsekr mqergfnqvi glleaadvpy spflirkeen vpqskktrke rmqlqqpfai
      181 qkenqeklkn csvilvddiy ttgrtlfhaa avindcypks lntftlar
//
LOCUS       WP_010823792             442 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus faecalis].
ACCESSION   WP_010823792
VERSION     WP_010823792.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..442
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47157
     Region          1..437
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mekkqlkrei ttfgalstvm gtvigagvff kaasvvghaq saslaifawv lggalticag
       61 ltsaelatai petggavkyi eytygklagf llgwaqsiiy ypanisalsi ifstqlinlf
      121 hlsanllipi ailagtsiti inllgtkias lvqsttlvvk lipialislv glftpgqvav
      181 slfpiettan tgflvafsga lvatmfaydg wlgvgnvage mkrperdlpk aiifglllit
      241 liyalinfvf lktlpieqia gnlnaasdas vaifgpiggk ivtigilisv ygalngytmt
      301 giripyalal dnlmpfsrqf qklskrfvvp yvagifqlav aiimmffgtf dlltdmlvfv
      361 mwlfnllifl avfilrkrep elnrpykvpg ypiipiiasl ggifilvtts itqpilalig
      421 vgitllgipv ylvnkqktkp kt
//
LOCUS       WP_010823794             807 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA translocase FtsK [Enterococcus].
ACCESSION   WP_010823794
VERSION     WP_010823794.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..807
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=88863
     Region          313..799
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 maqkratnkk ksttkkktkk qqqqqerlny mflglifilf gvfglfrlgf lgtllanclr
       61 lvvgntfpfa aillilygll vmiygkdfpl krgrpifgav liyisvllff hafmfrnvsg
      121 sqpdilgntw eflqsdlkan qvtqnvgggm igallyqgty flvaqfgsyl iatllllagi
      181 flmsmwdfqq ivdhfqsiqd rlshvsaksq arqeekeakr aakkeakaae rqakieaaaq
      241 qklqererme qaaaerltkt pvethqpmve eptaptpvqi dsfqqqnqam pvppiaatkp
      301 qreqeeeaad eagvlefeis eeaedrdyql pptdlldtiq atdqsgeyek ieknigvleq
      361 tfksfgvdak vvkaslgpsv tkfevqpavg vkvskivnlt ddialalaak dvrmeapipg
      421 ksligievpn saistvsfrd iveaqpshpd kllevplgrd isgmvqtadl skmphlliag
      481 stgsgksvai ngiitgilmq akphevklmm idpkmvelnv yngiphlltp vvtnprkaaq
      541 alqkvvqeme fryekfaatg vrnitgynql iqqknaedge nrpilpfivv ivdeladlmm
      601 vasnevedai irlaqmaraa gihmilatqr psvdvitgii kanvpsrmaf avssgtdsrt
      661 iidtngaekl lgrgdmlflp mgenkpiriq gafisdqeve rvvafvtdqq eaeyqesmmp
      721 tdepttsggg eapqdelfee aknlvvemqt asisllqrrf rigynraarl vdeleahgvi
      781 gpsegskprk vflqaeseea apetpeq
//
LOCUS       WP_010823836             319 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Enterococcus].
ACCESSION   WP_010823836
VERSION     WP_010823836.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..319
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35321
     Region          8..248
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtkklyqwgi vglggiahef astfkqetsq laavasrtla kaeqfaadys ipkaygsyee
       61 lladetidvv yiavpnkqha ehilkalqag khvlcekait mnaaelkqal avaekndlil
      121 aeamtifnmp lydelrrlmd agkfgqlkmi qapfgsykep dpknrffnpd laggalldig
      181 tyavsfarwf lssqpdvlas smvpfstgvd eqsvtllrnk enelatislt fqakmpkqgi
      241 vafedayiti tdypradeai vhyndgtvet ivsgysaeam nyeiynmvea ikgtqpnrsl
      301 ffttevidil dqmqklwqn
//
LOCUS       WP_010823926             229 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Enterococcus faecalis].
ACCESSION   WP_010823926
VERSION     WP_010823926.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..229
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25423
     Region          47..222
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mrnemmhrpv vkpelveymr tkqkklpgel gsveaeanea gvpiiphetv vflqfllgql
       61 kpknileiga aigfssslma qfvgedghvt tidrfdvmik kakktyqrld leekvtlleg
      121 qaaeilptle gpydfifmds akskyieflp eclrllpvgg vlmvddvfqa gtildpaeev
      181 pkknraihrk lnqfldvvma hpdltstlvp lgdgvilitk eketiilds
//
LOCUS       WP_010823962             669 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Enterococcus].
ACCESSION   WP_010823962
VERSION     WP_010823962.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..669
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=76677
     Region          24..649
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnykisylld eyagqkials laqqitdlsq relvtqlsti ggevqqnivs ipnlsanewg
       61 kqlfqqrqvi yseterqali flltyseiee lsvyhyqnfl dvskgtilad ikkvrhqlat
      121 enialsyerk rgfylegdef rirrfgknwl arllqqksgt falfcwlsqh qmsqyakmrd
      181 giqlavqeaq lqlvpsrlde isyflafsqk rlgkyetvvw penqliqslr aypvsrrils
      241 dlvgpvanae teslffticl mtalqgelrd tkleflldis geiirkmell avvqfeqpre
      301 llmnvyyhlv payfrinygf ylpnvlikdi rqsyrslyhl ceqalaplek ltkrsippee
      361 igfftilfgg eifgqkneqr qeklkalivc psgissslil qselrrlfpm iefketnavr
      421 eienvseksy diifstvpie takkvyltkp imssleknql mhqvqsdwll pgismpdvkd
      481 ildalkpyis lkkgvteaql yrvlhrkmnk ilekeedlrp mlsellttet vqvlpevadw
      541 ragiteaakp llkngsitek yidamiqkve sfgpfihicp dvalpharpe dgvnqlgmsl
      601 lkiqksvdll edpkheihlf iclaasdnet hlralssltk ilskkeslhr lvaaetvpei
      661 lsiiqegek
//
LOCUS       WP_010824006             275 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus faecalis].
ACCESSION   WP_010824006
VERSION     WP_010824006.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..275
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30206
     Region          4..265
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,196,218..220,222..223)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 miklvaidld gtllnsqkei slrnkqalma akqagvkvvi ctgrplaaig pyleelglqd
       61 egdysitfng glvqkndtga iiektlmple aihelyqlat tlnmpfdvls devvmqlpsa
      121 pnypsiyssl nklltfesyk leeltpnriy nkvvvaiyea ylnerikeip asfyerfeii
      181 ktrnnllefm pkgitkaygi sllakdlgir aeeimtlgde endlpmieya glgvamanai
      241 plvkeaadvv tdtndqdgva kavekyiltp leggq
//
LOCUS       WP_010824038             181 aa            linear   BCT 01-JAN-2025
DEFINITION  cysteine hydrolase family protein [Enterococcus faecalis].
ACCESSION   WP_010824038
VERSION     WP_010824038.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..181
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20212
     Region          3..181
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mkalisidyt ndfvatdgkl ttgaagqaie malvqqtkhy fdngdfvvfa idghdpldry
       61 hpenklfpph nvlgtdgrnl fgsladfyqa hkneatvywm dkrhysafsg tdldirlrer
      121 gitelcltgv ctdicvlhta vdaynlgyql miperavasf deqghewalr hfkqtlgati
      181 l
//
LOCUS       WP_010824160             429 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Enterococcus faecalis].
ACCESSION   WP_010824160
VERSION     WP_010824160.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..429
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48828
     Region          8..217
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd07732"
                     /db_xref="CDD:293818"
     Site            order(92,94,96..97,167..168,189,217)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293818"
ORIGIN      
        1 meskakttvt fhsgiltigg tvievaykda hiffdfgtef rpeldlpddh ietlinnrlv
       61 pelkdlydpr lgyeyhgaed kdyqhtavfl shahldhsrm inyldpavpl ytlketkmil
      121 nslnrkgdfl ipspfeeknf tremiglnkn dvikvgeisv eivpvdhday gasallirtp
      181 dhfitytgdl rlhghnreet lafcekakht ellmmegvsi sfperepdpa qiavvseedl
      241 vqhlvrlele npnrqitfng ypanverfak iieksprtvv leanmaalll evfgievryy
      301 yaesgkipel npaleipydt llkdktdylw qvvnqfdnlq egslyihsda qplgdfdpqy
      361 rvfldllank ditfvrlacs ghaipedldk iialiepqvl vpihtlkpek lenpygeril
      421 pergeqivl
//
LOCUS       WP_010824187             149 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Enterococcus faecalis].
ACCESSION   WP_010824187
VERSION     WP_010824187.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..149
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17136
     Region          16..147
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 menlelvikd tkellplefl kiikervrvf vveqncayqe vddkddtarh vyfksndkiv
       61 ayaritldqn attisfgrvl vvkeyrnlkl gkkivtetia eiqklyptkv ikisaqsylk
      121 kmyesfgfqa vsgiyleddi phismvlnt
//
LOCUS       WP_010824369             267 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Enterococcus].
ACCESSION   WP_010824369
VERSION     WP_010824369.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..267
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=29032
     Region          74..267
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          74..102
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(104,106,110..111,114..116,118..119,123,126,135,171,
                     173,177..178,181..183,185..186,190,193,203,205,207,
                     211..212,217..219,221,225,229,232,241)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          104..135
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          171..203
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          205..241
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mnkkilmgll svvtipllaa cqggetpsaa sknsqtvttq ssaktestst trsvaqttsk
       61 eevkepmkty evgalleaan qrdtkkvkei lqnttyqvde vdtegntpln iavhnndiei
      121 akalidrgad inlqnsisds pylyagaqgr teilaymlkn atpdlnkhnr yggnalipaa
      181 ekghidnvkl lledgredid fqndfgytal ieavglregn qlyqdivkll mengadqsik
      241 dnsgrtamdy akqkgyteis kilaqyn
//
LOCUS       WP_010824567             390 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Enterococcus
            faecalis].
ACCESSION   WP_010824567
VERSION     WP_010824567.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..390
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=43969
     Region          2..390
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mklqvtkkae hkfkkgypli qkedlqqvpa qlptdwltli dskgqrlaeg ylgeqnkgig
       61 wllswhgpin qsffqqlfei srekrtsfek dslttayrlf ngegdgiggl iidryadyav
      121 fswynetlyq kkaelltafr tvypdiigay ekirfstkdl pesqflygeq apepllvten
      181 gvqfatylne glmtgifldq kevrgrlvdg favgktvlnm fsytgafsva aamggavatt
      241 svdlakrslp ktteqfevnh lnlaaqkiiv mdvfdyfkya srkglsydmi ildppsfarn
      301 kkkvfsvakn ygelvkdsid iltdkgtlia stnaanlsla kyqkmvital qeknvrykit
      361 dtyqlpadfq vnpnfpegny lkvlfieiek
//
LOCUS       WP_010824742             640 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Enterococcus faecalis].
ACCESSION   WP_010824742
VERSION     WP_010824742.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..640
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71471
     Region          326..515
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mklsikkffe vflessways rpiltfdtrq nwfalvlsii ianavgavlt ivfpfafvlv
       61 nvgsflgtvi cvlprhsspq rsaidgilmi flgaslgill qsssifiill fvlgfyfsgi
      121 vrnfsiglyi rclfgtisll agaqlkgnls igqtfeglga iilgmsilcl fyclyskpqn
      181 nearklvadl yeqlyllaqg kparyvhfri kvrefvetmp wvnhqktpwi yplvsqadai
      241 agsldstnaa enlpalkaiq lflkgeqltl plqefasant eiksailliq nkqsskkisf
      301 ksflptkegl aeakeilnsy kgssarfair laltglvchf cslilnymyp lplanhefwv
      361 visgclmvmp gyhgtlgkit srtigsilgg clgiflsqli anltnlnplw pmllscllvi
      421 lyesvrklsq aflmlsvttw ltftlggssa gytrvfdvii galiafvmff ifptwhsqvl
      481 rkninswskt issillalin eettlpsdaw vlayrvqrrv nysiqeivle spiysndasa
      541 eslmqqkqln dqllemqtam eelllelmkt qhylkklapv kpdtlntelf nysqqilslt
      601 npknnrlinq skqsiyfpqi eqslvilkns tanfflanik
//
LOCUS       WP_010824793             568 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010824793
VERSION     WP_010824793.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 568)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..568
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63105
     Region          3..532
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mkkpiitfnn fsfqyhsqse ptlkgiqlti yegekvlivg psgsgkstla qcinglipni
       61 yegeiqgtat vagkniqets lfdlsfdvgt vlqdtdgqfi gltvaediaf alendaveqa
      121 emkkavhkws eivelnqllq hrpqdlsggq kqrvsmagvl inqskillfd eplanldpra
      181 gqetmtlidt iqqetkatvl iiehrledvl cesvdriivm negaiisdtt pdellrqdtl
      241 tqqgireply vtamkyagid ltkvshldkl aevsgetvlp kmtqwsvqps svsavkgael
      301 lrleqvsyqy drhgekvldd fsvtihhgem isivgkngag kstlskiicg fitpqsgkil
      361 wegqdfsnys ikeradkigy vmqnpnqmis kkmifeeval glvlrdvpqa eieervtnil
      421 hicglypfrn wpisalsfgq kkrvtiasil vlepellild eptagqdfkh ytemmtflee
      481 lnrlgvtilm ithdmhlmle yttralvvcd grlladatpv avltdekliq aaslketslf
      541 tfakalglen pllftekfva ydrevrfg
//
LOCUS       WP_010824829             439 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            faecalis].
ACCESSION   WP_010824829
VERSION     WP_010824829.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..439
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46141
     Region          25..431
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mnekkeqalf eydaklsise aipmglqhvv aavvgivtpg imiakvcqls psdttiliqt
       61 slifsavatl iqlfpifgkv gsrlpvmmga sfayvpilma igadfgiaai fgsqlvgsil
      121 viivglfikk irvlfpplvt gtvilsigls lfpvaikyma ggagsadfgs arnwlvallt
      181 faivfyfnyf akgflklsai lngmvigyli slalgmvsfe pvqnakivqv itpfhfgldf
      241 qlvpiftlvv mfivdavqai gqftattvga mdrdatdeel sggimgsgft nfigslfgsi
      301 pvatfgqnvg lvtvtkvink yvlvfasvil liagfvpkva allttipyav iggatisvfa
      361 sismtgirmi asqemtprnt gvvgtalafe igvtlstgsl agfptwvtti fgnseviltt
      421 lvavllnvil kpkkrvale
//
LOCUS       WP_010824844             240 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010824844
VERSION     WP_010824844.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..240
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27024
     Region          3..218
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnldylkety hltktesqil yyldqqstna adlsirevak hcfsspssii rlakklnlsg
       61 yneliyklke ahfsqsipfe tapsfettne fcqllakhks hlfvilghdf srhlaayise
      121 vfnfhgipsi ttahthsins qnnqnflfii lshsgeekyl ketallakek khpiisfvga
      181 knstlgrlad lvfstdsysp fstsvaqpqm ffgqtlitfe alicaylnhe dsipispknk
//
LOCUS       WP_010824996             409 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010824996
VERSION     WP_010824996.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..409
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44445
     Region          4..407
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mianlfvstf lslkahklrv fltmvgiiig itsvvtisal gegmkrqvvk assavnadvl
       61 kihytmldgs sdnfmsyeep dytfsrvdlk klqdiqgies iypqygesmm gggdnlfvpm
      121 dyfgaqanls itstkgqndi lygrdfqpsd antdaivlnh difetqirld dpsqligkav
      181 siggymykvi gilapkdlds lgmnddwata mssfvsresy nklaktkais ginikvrega
      241 dreailgqai tilsenhpev kgtfkendqd qqlqqqmeem vtgmtmflma itaisllvgg
      301 igvmnimyvs vterkreigi rraigakprv ilfqflmeaa fitligglig vgcgyllatv
      361 vggyisitpi itpsifaist lvsvftgiff giipaigasr mdpikaiyn
//
LOCUS       WP_010825014             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Enterococcus].
ACCESSION   WP_010825014
VERSION     WP_010825014.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28075
     Region          1..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlieerlaki qkivneqksi smealaeqvs vskdtirrdl irlekeghlk rthggaisvq
       61 seatiydyaq rivkhpekkq aiaqkvwani pkqasiffds sttveaaira menspihait
      121 nslshallla qmdqtkitvl pgqlhkqqlf lfgaetvakv gefapdytll gvfalseqgl
      181 fihteeegqv krrmiqqgkq vialadqtkl nktglfkice lteidclvtd arpdekfceq
      241 laqagvtliv ade
//
LOCUS       WP_010825099             433 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Enterococcus faecalis].
ACCESSION   WP_010825099
VERSION     WP_010825099.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..433
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48784
     Region          1..400
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mrfleqlpea wqeqwqasgf nepstiqeks ftplregenv lgisptgtgk tlaymlplll
       61 tvekgqgnql liiapsqela iqiaevartw akplqltvqt ligganvsrq idklkkrpev
      121 ligtpgrile lmknkkvkaq lvktivmdev dqlfqeeels ltkqilihtp teyqlvfysa
      181 tadrvvnqaq slsqklqvid vteedtsagq vahyfirlap rkkadylrrl ahteafrsmv
      241 ffnqvadlga aeeklvyenv paiglasdqs kqlrklaidq fkaervklll ttdiaargld
      301 ftgvpyvvnv dvplteesyi hrsgrvgrmg aqgavitfin dgtkrdyqrl mkqlaipyqe
      361 iflydgalhe qpkakdelek knvvkdtyse kkstkerkpe tvnsvvkepq etrkkkknkk
      421 kntknkgark akk
//
LOCUS       WP_010825290             228 aa            linear   BCT 01-JAN-2025
DEFINITION  ComF family protein [Enterococcus faecalis].
ACCESSION   WP_010825290
VERSION     WP_010825290.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..228
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=26987
     Region          41..228
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mdckncaspi rleitlkmll rfkkwarpsl cqhcqakfqk lpmigtcfgc srvsqerycf
       61 dcrrwqllyp eysfhnaalf hydegmqewm erykfqgdyr lrmcfneein sffrqqsvdy
      121 iipvplsekr mqergfnqvi glleaadvpy spflirkeen vpqskktrke rmqlqqpfai
      181 qkenqkklkn csvilvddiy ttgrtlfhaa avindcypks lntftlar
//
LOCUS       WP_010825382             713 aa            linear   BCT 01-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Enterococcus faecalis].
ACCESSION   WP_010825382
VERSION     WP_010825382.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..713
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=81535
     Region          3..712
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mniqaidtrh gtanqhsfsn gnclpytgvp fgmnfyapqt tdqkgswwfh pedrtfqgyr
       61 vthqpspwmg dfshllmtpv sgslselslf haqssyrpee slfspveinl tqlryqitsq
      121 lipsmyggil tidyqqkdnh llltlpgryq vkqlddhqva vkvinysgce dpdfsfyfvl
      181 hfeqpltkwf apssgedgki llsfgniaqq vvhfsssfis ekqaqlnlar eislrsteml
      241 qqgiadwhny fdrlkvthen pehtktfyht lyrtflfpqt fyeldenqqp ihydtfsqmv
      301 rpgvlytnng fwdtyktvyp lfsliaqeky eemlegflns ynetgflpkw lspderglmp
      361 gtlidaviad aavkkirpdl mpqfleamkk gatqqseren ygrqgtldyl kygyvpstyh
      421 esvnhtldya ysdfcisqva ktlndsetat fyrqqalnyq qlfnpetgfm qakdtegnfr
      481 pdfldirwgk dyaegsawqs sfavyqdfag liklygsela fekkliqlcn qapnfnvegy
      541 gfeihemsem aaidfgqlai snqpsfhypf lfsyigkpem aqpllkqlmq tfdasptgyp
      601 gdedngsmsa wyifnslgfy pvtpgtgeyv igmplvqtae vklsngkqlt iqtspnkvqq
      661 qfiheiqlnq ekhtapyfth qellnggtld yqlgivpnpq ntaerpfsls tek
//
LOCUS       WP_010825315             686 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus faecalis].
ACCESSION   WP_010825315
VERSION     WP_010825315.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..686
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=79099
     Region          19..629
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkkinnrlgl flffvllfwa ktilayyldf slgvkgslqr eilwfnpvat tlllfgfsly
       61 fkkhktfmls ltllnvlntl ilylniifyr eftdfitiqs vfgfskvseg isgdllalmr
      121 vhdvfywldt lvllvlvfys fkqrrnhqvf vtkpinrrla isisclsvll fsvnlflset
      181 drpqllqrif drnyivkylg ldaftaidgv ktamsnevra eassnelpei mkftkqnnlp
      241 lnpqyagiak gknvfvihle sfqqflinmk vqgqevtpfl nqlyqnkati sfdnffhevg
      301 qgktsdaenm letgtfglpq gslftqlgsd ntfeaapavl gqkgyttavf hgnvgsfwnr
      361 dhvyknlgyq yffdrsyfsk ddkmlgygil dkqllresas elehlqqpfy akfltvtnht
      421 pyytddqnfp fpklntgnsi vddyvrtahy ldqsleqffh ylqttslynh sifviygdhf
      481 gisdannkdl ckafnrdpkt wtnydnaqlq rvplmfympg ytqgkimhey ggeidvlptl
      541 yhllgvddkn yihfgtdlls pqykqvvpfr ngdfvtpqfs ylggeiynnq gkkldqvpad
      601 lkaevtkdnd wvkkslslsd klnqenllrf ykpqgfqevq pkdynydvtf eknkvlevek
      661 qknaqstslf sqngnqttvq nypttp
//
LOCUS       WP_010825436             389 aa            linear   BCT 01-JAN-2025
DEFINITION  CDP-glycerol glycerophosphotransferase family protein [Enterococcus
            faecalis].
ACCESSION   WP_010825436
VERSION     WP_010825436.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..389
                     /product="CDP-glycerol glycerophosphotransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=46056
     Region          12..386
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mkkflensih qaikacfffl gklpkkklfi fesfhgkqys dnpraifeyi rdncpeyqci
       61 wavkkgyeip fveenvpfvk rlswrwlwlm praqywvfnt rmpawmyknq ttiyiqtwhg
      121 tplkklgldi etvkmpehet esykleviqe akrwdylisp naystrvfrq afhyegeile
      181 igyprndllv cenkdkiafs vrnqlglavn kkiilyaptw rddesirkga yrftnhlpve
      241 qlleidssiv iltrlhylia esfdisafgs rvidvssypd inqlyliadl litdyssvmf
      301 dfaltkkpml ffmydkekyq nstrgfyfdp tailpgkivt dtdslvtsvk nvlfskteqe
      361 qrlyvqffre fclenqdatr qliseilkr
//
LOCUS       WP_010825476             244 aa            linear   BCT 01-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Enterococcus
            faecalis].
ACCESSION   WP_010825476
VERSION     WP_010825476.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..244
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27383
     Region          6..244
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mllsgeridq lyaddikiiq skevfsfsid avllanfpql pkkgkivdlc agngavglfv
       61 srktaatidq ielqprladm gqrsillnkl ekqvtmyerd lkqatevikk dsvdlvlcnp
      121 pyfkerptsq knpnphlaia rheihtslqe vvtvsadllk tngrlamvhr pdrfldilha
      181 menaniapkk arfvypkpgk eanvlliegi kqgkkdgfrv lpplftynek neyeaemkam
      241 lyge
//
LOCUS       WP_010825512             324 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Enterococcus faecalis].
ACCESSION   WP_010825512
VERSION     WP_010825512.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..324
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37136
     Region          93..324
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkkksiglll asaylfhtrs rqkslkaclf edslrlsqia rlernpkvtk afyhwqrsln
       61 eqvtlpkhlr hlfplqettq fptmyrmsns viaptkkavl ylhgggftln laysqldfsy
      121 kliedlsfat dyfipvypla pnksfadiyn hcyaayqeil qhydpedvil lgdsaggtlv
      181 lnvlqnlaid fperlpkaav lispwldghl dipvaksyqk kdkmigmnyl qliaqeiddt
      241 anhstlslnc lsfdyqkfpp lffvggthev fcpsyhqflk qlgprpqdtc rlvpgmqhvf
      301 amkqylpegr qarkqiaqfi qeqw
//
LOCUS       WP_010825585             648 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Enterococcus faecalis].
ACCESSION   WP_010825585
VERSION     WP_010825585.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..648
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=71678
     Region          3..393
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
     Region          <532..625
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtkqnivvvg agyagvsatk flakkfkkdt dvtitlidrh syhtmmtelh evaggrvepe
       61 aiqydlqrlf srkknvklvt dtvtgidken kvvktlagsy pfdqlilgmg gepndfgtpg
      121 vkengftlws fddavkirhh ieatvakaai epdaevrkam ltfvvcgsgf tgiemvgeli
      181 dwkdrlakda kidpdeitlm vveamptiln mlsrndaaka erylekknvq lllnspivev
      241 aadhiklkdg sevpthtliw tagvkatsda adfgleaarg srlvaneymq akgyedkniy
      301 iigdlvyyee tpntptpqiv qaaeqtghta aanivadikg gekhafkgny qgfmvsigak
      361 wgvanlfdki hlsgflaiim khivnlkyff dirsgyymfq yimheifhik ddrsvarght
      421 srygnvlwsv plrvfygmvw lvesmkkivg ngdylkpstw fgdgswftdk vvfpfpwlqe
      481 qvttgasqtt etattaasga adaaasggad aatqaahfgl syaygetpmq vfdhmpkwfe
      541 svmkfmmpnq evalfmqkfm tivevciala liaglftwls saatigltia fclsgmfywv
      601 niwfifvafa lmngsgravg ldrwvipwiq rklgkawygt pkaryggk
//
LOCUS       WP_010825674             752 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Enterococcus faecalis].
ACCESSION   WP_010825674
VERSION     WP_010825674.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..752
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85872
     Region          235..723
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mqgnnlfnng llqpkkppig qeqqkmtryh qlrlvfglvg vllypfailg siplliglav
       61 dkkdkaanvf dmdyesflkr nsivflsfsa vlfvinvfaf ilwiprgyls ayllfplnll
      121 htalrfnwet ivalligssg mgaiflafss fvakrkvisk ederkkites kaykdreknk
      181 feesqrftde qeeayeeave tvdidkykel snqlllgtse fglpyiinfs efnqhvlvpa
      241 ttgsgkttll qllvqhavkf nfpvilidgk gardtlesmr eiakfydkev haftddgdmr
      301 ynpvehgndi sirdklvsla etesvfysga akallqvtiq lldefkgakv tlsgdtrtte
      361 tverslpfvq rfllprnvlh lfadailpnn pklfeievek kiqkpkkksv kegseilpds
      421 dldkeekeed sqiknskfrn isqlgiaqke tetivlnpet ldldsyylll krnlrylptd
      481 ketgenikqk lferlfirye hkdspfylya tsealqtnin mlldselgkl fdtknaknvl
      541 dvqeivnqrk lvyvsfngli ykeyirtlaq mlvgdvnyfa semyrknvkr evlvifdepa
      601 sylnetfidm vnkgrgagvy giftpqtmad iaklgdklme qlvgnvntlf igktnekgea
      661 eywsetmgty qdidvtsvte qedgysdvgk sdwsgdrgtk rnvdrfkisp nkikelrtge
      721 fiiyrtaenv nlppqkvyvr nalewlqksk sk
//
LOCUS       WP_010825727             652 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus faecalis].
ACCESSION   WP_010825727
VERSION     WP_010825727.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 652)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..652
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=75404
     Region          11..642
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mheiskrqhk llrllleqkd flpvnhfski lsisdrtlyk didelnkalk krkieilkrq
       61 gkgiflsksd lsndeilkif geastqidfn qlplerqikm aeylllrnkk vsyqllsdef
      121 lvsrtsisnd ldqiqtvieg ssvtirsdnn gtkvngnese iqkaikqyay fiidksdltn
      181 syrvqfpsll fsflpkdiik kvsgllqtnn hfnidklsdd hfqslvlsis ifvlrlqegf
      241 hieyqdnflf enveslktff lanelvenle ldnsikldsn dfeyfnrqlv ahgfeprlrd
      301 laiqkeydav vrkmiqkmsd siqvdltrde klymnilyhl vsmiyrskln vpvsnpllee
      361 ikreysvlys ttwlilagie keldirltdd evafmmihfq gaidrlsanr kilivcptgi
      421 gtselianrl krvfspqdiv evvslrtlyk rdlnkidlvi ssvqlekidv pvtyvsplms
      481 kqdlkkvsat yldlfyeeev ndqpfehlgk iidsdlifln etvatkeqci kritqkllqn
      541 dfvtdsfeqa iwdreklgvt dlpigaaiph pspstvkesk lvimtlvkpi rwnfrmintv
      601 lmicvaekdl khikgilsei yrivetkkni drfifskdee eivkvlggqt id
//
LOCUS       WP_010825776             171 aa            linear   BCT 01-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Enterococcus faecalis].
ACCESSION   WP_010825776
VERSION     WP_010825776.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..171
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=18917
     Region          8..168
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mfqtfrenfr rhtllrdavf ivigsaivfn pgaffqfvgy liagylmllg liniyddykk
       61 kkqtgswglg fvtglifvvl avaflffapv ivsilpfllg isivinglvq ltfalntrqt
      121 galiysilvl iagavlvfnp fksllvlmqv fgfilifmgv ieiighfrnk a
//
LOCUS       WP_010825839              61 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010825839
VERSION     WP_010825839.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 61)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..61
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7266
     Region          1..60
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mrewlvdirl knkltqeqva eradiersyy nmiergkrrp sveiakkian vlsidwtiff
       61 k
//
LOCUS       WP_010825882             402 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010825882
VERSION     WP_010825882.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..402
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43873
     Region          6..402
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkrsiiwkia frsilknkrr slltmlgivi giasvitiva igngfkedmv dklsaekqke
       61 nvkkisfsay ntsdmfsdqa mfndndlgvv rmvpgvekid fdqrevdgaq kgtlnfqagp
      121 knlsvtyela nkttkellag rqlndgdnak ldktvvvdel vakelyqdpt aavnrtfpyk
      181 eqlftivgvt tntsgaigpg nddsllyfpk ktyehyfgkl kdtstlkltv apgyqpdqvl
      241 ketiktlsqq gtmknsgtyq eynvkdtike mgsllnnltl fisaiaaisl viagvgvmnm
      301 myisvserik eigirralgg tasdikkqfl tegialtlig gitgyllgmi iaylasmalp
      361 fsvrpdlmtv slaigisvfi gvvfsyfpas aaskkdlidi mk
//
LOCUS       WP_010825884             127 aa            linear   BCT 01-JAN-2025
DEFINITION  potassium channel family protein [Enterococcus faecalis].
ACCESSION   WP_010825884
VERSION     WP_010825884.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..127
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=14130
     Region          37..100
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mlsllisvkk lfssflgilk kedtralffl lattllsgti fystveklsp ldslylsfmt
       61 lttigygdvh pvtdlgkift miyatvglgi mamfisvvsk sylyskqshh hhhhknkehs
      121 aekssek
//
LOCUS       WP_010825924             197 aa            linear   BCT 01-JAN-2025
DEFINITION  LemA family protein [Enterococcus faecalis].
ACCESSION   WP_010825924
VERSION     WP_010825924.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..197
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22135
     Region          19..189
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mnkknkflsi ivvvvviiga fvmkaynqli tldnkveaew sqvenvmqrr adlipnlvss
       61 vqgsmtqeke vlkeiteark ayagakssse kgqaneqiek glgnfvtvln edypklasse
      121 nvktlmtqle gsenrisver rnyiqavety nqqiskfpdk iiakllgfek ktnyvateqg
      181 kevpqvkfnm icqikle
//
LOCUS       WP_010826122             640 aa            linear   BCT 01-JAN-2025
DEFINITION  FUSC family protein [Enterococcus faecalis].
ACCESSION   WP_010826122
VERSION     WP_010826122.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..640
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71488
     Region          326..515
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mklsikkffe vflessways rpiltfdtrq nwfalvlsii ianavgavlt ivfpfafvlv
       61 nvgsflgtvi cvlprhsspq rsaidgilmi flgaslgill qsssifiill fvlglyfsgi
      121 vrnfsiglyi rclfgtisll agaqlkgnls igqtfeglga iilgmsilcl fyclyskpqn
      181 nearklvadl yeqlyllaqg ktaryvhfri kvresvetmp wvnhqktpwi yplvsqadai
      241 agsldstnaa enlpalkaiq lflkgeqltl plqefasant eiksailliq nkqsskkisf
      301 ksflptkegl aeakeilhsy kgssarfair laltglvchf cslilnymyp lplanhefwv
      361 visgclmvmp gyhgtlgkit srtigsilgg clgiflsqli anltnlnplw pmllscllvi
      421 lyetvrklsq aflmlsvttw ltftlggssa gytrvfdvii galiafvmff ifptwhsqvl
      481 rkninswskt issillalin eettlpsdaw vlayrvqrrv nysiqeivle spiysndasa
      541 eslmqqkqln dqllemqtam eelllelmkt qhylkkltpv rpdtlnielf nysqqilslt
      601 npknnrlinq skqsiyfpqi eqslvilkns tanfflanik
//
LOCUS       WP_010826139             397 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphoglycerate kinase [Enterococcus faecalis].
ACCESSION   WP_010826139
VERSION     WP_010826139.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..397
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42306
     Region          5..397
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 makktikdvd lkdkkvlvrv dfnvplkdgv itndnrivaa lptikyvien ggkailfshl
       61 grvkteedka gkslkpvaer lsellgqpvt fvpetrgkel edavnnmkdg dvlvfentrf
      121 edvdgkkesg ndaelgkywa slgdvfvnda fgtahrahas nvgiastgip tvagflmeke
      181 ikfigeaven pkrpfvailg gakvsdkiav ienliekadk iligggmayt fmkaqgysvg
      241 lslleedkvd lakslmekag dklvlpvdtv vskefsndah fhtvpsteip ddeegldige
      301 ktielfanel qgaktvvwng pmgvfemsnf akgtigvcea ianledatti igggdsaaaa
      361 iqlgyenkfs histgggasl ellegktlpg lasindk
//
LOCUS       WP_010826270             506 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: gluconokinase [Enterococcus].
ACCESSION   WP_010826270
VERSION     WP_010826270.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..506
                     /product="gluconokinase"
                     /EC_number="2.7.1.12"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046316 - gluconokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /GO_process="GO:0046177 - D-gluconate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54998
     Region          6..489
                     /region_name="ASKHA_NBD_FGGY_GntK"
                     /note="nucleotide-binding domain (NBD) of gluconate kinase
                     (GntK) and similar proteins; cd07770"
                     /db_xref="CDD:466790"
ORIGIN      
        1 meklaigvdv gttqakavaf qsngtvvass yvrypliqet egmaeqdpet lfqavvncir
       61 tvtqqvknqp iglisfasam hgliamdaqg rpltqvitwa dtrasdyaea lketpaaqlf
      121 yqltgmpvhp maplykirwl qenqpavaqs aakfigikdy ifyrffgeyw tdyssasgmg
      181 lfnihtrqwe ssilaylsie eeqlpkvaps tfifpalaps wqemlgveee tvlvlggadg
      241 plsnlglgal gmgvatltvg tsgalryive epflhpqget fcfaldeqhw viggassnga
      301 valdwasqti faeerqqaiq ngtnlydpim akiatvpaga ngllfhpyll geraplwnae
      361 asasfiglrk nhhaghlara vvegicfnlk tiledlkqlg gpvqeiratg gfadspvfrq
      421 imadvlgetl sftdsteasa lgavllgwqg lgqlpnlqaa aqqvlihetv tpradqllvy
      481 qelypvfqet qqilaqsyqk laefrk
//
LOCUS       WP_010826362             516 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide deacetylase family protein
            [Enterococcus].
ACCESSION   WP_010826362
VERSION     WP_010826362.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..516
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58198
     Region          316..495
                     /region_name="CE4_CtAXE_like"
                     /note="Catalytic NodB homology domain of Clostridium
                     thermocellum acetylxylan esterase and its bacterial
                     homologs; cd10954"
                     /db_xref="CDD:200578"
     Site            order(321..324,374..379,412,414..415,433,439..440,463,465)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:200578"
     Site            order(323..324,374,378,412..416,433,465)
                     /site_type="active"
                     /db_xref="CDD:200578"
ORIGIN      
        1 msdkniyarr sqrhkqepdi cenanqlnea vkpktgnenk qpkipkkksn yskyifalft
       61 alilvivatg gyivytlkqq eveaqakyet avknlmasiq eeqdqsgist kidtindgen
      121 kcliyrpvye stvpfknanq lldelaqkqq kkhrekevlt vvrikatais skigqyriea
      181 dsfiwdrske nfkkpdsise kaiyvsektg keitnkdlip degsllgiqq viqqsildha
      241 kepkkiidav ltmdrisyes kmtytpdelt idlpknttgt tkvilkyrdi apfidtdlvs
      301 qesikdalpa ldenkkyval tfddgpnnss tldllnilkt nnvkatffml gqmvdqnpdv
      361 akqvhdeghe vachsyshpq lntlstdelq semnkankai fkatgvlprn irppygaidk
      421 ksaetigmpi iqwnidsldw ktrnpeainn vvkqnvfnga iilihdihhe svkavsglit
      481 mlknegyefv tidqllsgkq kplhqyfgmn derlvd
//
LOCUS       WP_010826370             281 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Enterococcus faecalis].
ACCESSION   WP_010826370
VERSION     WP_010826370.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11573834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..281
                     /product="VOC family protein"
                     /calculated_mol_wt=31046
     Region          9..132
                     /region_name="VOC_BsCatE_like_N"
                     /note="N-terminal of Bacillus subtilis CatE like protein;
                     cd07255"
                     /db_xref="CDD:319918"
     Region          170..279
                     /region_name="VOC_BsCatE_like_C"
                     /note="C-terminal of Bacillus subtilis CatE like protein,
                     a vicinal oxygen chelate subfamily; cd16359"
                     /db_xref="CDD:319966"
ORIGIN      
        1 mvqalpsnig iqqvtlkvad ldkmvnfytk tiglkllkqg egrawlapqs tndailvlke
       61 ltageenqgt tglyhiafli ptrkdlgnml lwllqenvqi gaadhgysea lylsdpenng
      121 ieiywdkpee vwdirpngei igvteeldgd slaaeadghw lgisegskig hihlkvadld
      181 atetfyknlg fglksnfgqq akffaagqyh hhigtntwsg kqlptiqenq fglenytfrl
      241 ptaadleivq anaeeaklhf iakdhllale dpsgmiiqft y
//
LOCUS       WP_010826371             446 aa            linear   BCT 01-JAN-2025
DEFINITION  MATE family efflux transporter [Enterococcus faecalis].
ACCESSION   WP_010826371
VERSION     WP_010826371.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Kaatz,G.W., DeMarco,C.E. and Seo,S.M.
  TITLE     MepR, a repressor of the Staphylococcus aureus MATE family
            multidrug efflux pump MepA, is a substrate-responsive regulatory
            protein
  JOURNAL   Antimicrob Agents Chemother 50 (4), 1276-1281 (2006)
   PUBMED   16569840
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..446
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49449
     Region          12..430
                     /region_name="MATE_MepA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Streptococcus
                     aureus MepA; cd13143"
                     /db_xref="CDD:240548"
ORIGIN      
        1 meqtqqnhft alfyknvllg ilsmaaqsif iladtffian gigtealagl nivlplvnii
       61 nglgwmfgvg gatlfsttva qkeikkanqy fsltiglvfv igslftlasl tfsdqiirgl
      121 qgtgvlfgla keyymiylsc sllfilnncl itflrndhnp rlatiafvsg givniildyv
      181 fiyqfgwgma gaaiatvmsp ltslilitlh kwspqrvlrf ekfkvkfqdv reimsigfss
      241 flnefssafv mflfnivlln lvghvaisay aivanlniiv iaiftgigqg aqpllsryyg
      301 lgetkvlrkf vklsfitylv agflfflisq vftgqiievf nsegndqlaq iartairlya
      361 isflftglnf mgiyyfsavr kpkmalmiss lrgfflivpv lfilvkllgl tgvwlampvv
      421 efvtfglmlv gylayrnylk kretvt
//
LOCUS       WP_010826374             324 aa            linear   BCT 01-JAN-2025
DEFINITION  ring-cleaving dioxygenase [Enterococcus faecalis].
ACCESSION   WP_010826374
VERSION     WP_010826374.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170060
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..324
                     /product="ring-cleaving dioxygenase"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37700
     Region          4..128
                     /region_name="PcpA_N_like"
                     /note="N-terminal domain of Sphingobium chlorophenolicum
                     2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and
                     similar proteins; cd08346"
                     /db_xref="CDD:319934"
     Region          155..321
                     /region_name="VOC"
                     /note="vicinal oxygen chelate (VOC) family; cl14632"
                     /db_xref="CDD:472697"
ORIGIN      
        1 myaqihhisi lnrlikptfd fyhntlglkl lmktinqddh tmyhlffsdn eqrtgteltf
       61 felndgqdqs fgtntierti lkvptrtsld fwaerleqag ichygvetfn qhpilrfeap
      121 dntqmalvpl refenaedyf paehaeipve hailgidaiq lrvqyaaatk qplvdylhwh
      181 eketvpffet ahevtvlenh hpqfyqevhi iddrtnplvi egiggvhhva fkvedtqelt
      241 qvdslldekn ftnsgikdre ffkslyfrep nhllfevatq kglldaeaye nqssnfdeip
      301 lylphfladq rerieailaq qrhe
//
LOCUS       WP_010826378             505 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease/substrate-binding protein [Enterococcus
            faecalis].
ACCESSION   WP_010826378
VERSION     WP_010826378.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..505
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55870
     Region          2..208
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
     Region          236..499
                     /region_name="PBP2_ChoS"
                     /note="Substrate-binding domain ChoS of an osmoregulated
                     ABC-type transporter and related proteins; type 2
                     periplasmic-binding protein fold; cd13610"
                     /db_xref="CDD:270328"
     Site            order(242,244,292..293,296,339,341,419,443)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270328"
ORIGIN      
        1 mqalietffa rkeeylqali ehmqlsfisl lfaaliaipl aiyltshrkl aesllqvtgi
       61 fqtipslall gllipligig rppaivalvi yalfpilqnt ytglteidps leeaaeafgm
      121 skkeklfkfe lqmalpfiis girtatvlii gtatlaalig agglgtfill gidrnnlsli
      181 figalssaal avlfnygihw lekangrrli iggtilglll ggsffwnqqt sskekqltia
      241 gklgaepdii inmykaliee nsdiqvtlkp nfgkttflyn alksdeidly peftgtviet
      301 flknppqldn qpqvvyeaar aglkkqenlt llkpmryent yavavkrsfa kahqlktisd
      361 lqkisnqlka gftlefidrq dgykglqeky hlnlnvqsme palryqainn gevnvidays
      421 tdselrqygl vtleddqalf ppyqgaplik tatlekypel aeilnklagk iseeemsemn
      481 yqvnvegqdp sivakdylke knllk
//
LOCUS       WP_010826466             143 aa            linear   BCT 01-JAN-2025
DEFINITION  universal stress protein [Enterococcus faecalis].
ACCESSION   WP_010826466
VERSION     WP_010826466.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15707
     Region          4..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msvyqhilva ldgsdqseka fheafriake eqatlylati indaefttsp fsfeelydle
       61 khkseemltg kakqaseigv ktvkkivelg spkrylanti senyaidliv lgatgrgaiq
      121 rtligsttdy vvnhalcnvl vvr
//
LOCUS       WP_010826480             359 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Enterococcus faecalis].
ACCESSION   WP_010826480
VERSION     WP_010826480.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..359
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=40532
     Region          5..351
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 miritnltlg slfdgigvfp laaqkqgitl swaseiekap iritkkqfph mihlgdltkl
       61 hggkippvdi vtfgspcqnl stignregla gkksnlfyea iriieemrda tngkyptlai
      121 wenvmgafss ndrmdfkavl eafvqtevpi ppsrqwanag mvrgrnvdvc wrvldsqywg
      181 vpqrrrrifl vadfrdfrar eilfdtqgmq shletcdqnr lsspkdnrsl ttkagrqlfl
      241 ypfqerrmrt yakekntkgf vssfgqstdp fptllagtvd tfaywqegfe tegfvrklip
      301 lecerimglp enwtqygfdn qlisdsaryk algnsivvpc aefilsnvak iygkgesyg
//
LOCUS       WP_010826602             443 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            faecalis].
ACCESSION   WP_010826602
VERSION     WP_010826602.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..443
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46393
     Region          28..438
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 msekkqnnlh ltvgpedsvs fgqatmlgiq hvlamdvyvv pviiasiigi staqtssliq
       61 atfiaaglat iiqshfcmrl pvaqgpsfip igaiagiyfa nnqqgngwga vlgaslvgai
      121 vviilgftgi fnrlitkfvp pivggtiifv vglslmpval sdniyhakge lgqnillafi
      181 aagtliffal lgsalkkgri frvssvilal lfgsiaaqll gvldlsavse aawfslpqlp
      241 lvnfsfqfdw saiatmlviy lvlmaettgt wfavshvvae plteekinrg vigeglgclv
      301 ssfiggtpvt systnagiis itgvasrkvf vaagawfvlf glsgklstli saipapvigg
      361 vfvvvcgiis vsgmkvmsdv tihekemyii avpiimtlal tllpkeflet lpqflqylfs
      421 spvatasiva illqailpnv qeg
//
LOCUS       WP_010826627             648 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Enterococcus faecalis].
ACCESSION   WP_010826627
VERSION     WP_010826627.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..648
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73737
     Region          6..534
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          571..643
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 millqanqva rhfgsetlfe nihleiatks rialvgrnga gkstflkiia gidapdsgti
       61 aknktatlgy laqntglesd ktvwdemtka fadilemeqr mreletkise mdpttsvyeg
      121 ilkeydqlqh tfsekngygy eneirsvlhg fgfdesfytk diqtlsggqk trlalarmll
      181 qkpdililde ptnhldietl swlesylpsy agallivshd ryfldkvvne vyelsrkkmt
      241 hykgnyskyl elkaeqlase wkayekqqee inkledfvak nlvrasttkr aqsrrkvlek
      301 mdrldrpqgd eksahflfds ekvsgnvvlq vedaaigydq ehilsepihl dirrkeaial
      361 vgpngigkst llksiidrip fikgsktfgt nvsvgyydqe qanlhgnktv laelwdehpt
      421 tpekeirsil ggflfsgddv ektipllsgg ekarvalakl amdrdnflil deptnhldid
      481 nkevlenali dyegtilfvs hdryfinria tkvvelsekg sklylgdydy ylekkqeeee
      541 iaallaneea akkpepvtak ntfyqnkeqq kllrtlqrki tqveenlaql dttiaqleaq
      601 msqpdilenh vellalnqql ddarqqqdel leqwenfsle leemennn
//
LOCUS       WP_010826632             278 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010826632
VERSION     WP_010826632.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 278)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..278
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31358
     Region          2..263
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqkkkfkwsy vylfvvfall yapifylify sfndtqtmnq ftgftldnyr nvfedtrllt
       61 ivlntfllaf lsaliatiig tfgamgiyyt krrknrntll sfnnillvsp dviigasfli
      121 fftavgfisl gftsvllshi afsipivvlm vlpklqemnd smvdaardlg annvlvikni
      181 ilpflapgii agyfmaftys lddfavtffv tgngfstlsv eiysrarqgi sleinalsal
      241 vflfsmilvv gyyfiskdnt pkrlkkmrre qsevaklk
//
LOCUS       WP_010826746             193 aa            linear   BCT 01-JAN-2025
DEFINITION  histidine phosphatase family protein [Enterococcus faecalis].
ACCESSION   WP_010826746
VERSION     WP_010826746.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..193
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22542
     Region          5..186
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mkktlylmrh gqtlfnqqkk iqgwcdsplt kqgieqakia keffekngiv fdgahtstle
       61 rasdtlelit einyerhkgl kewnfgrlea eheylnpplp yrdffvqygg eeeiefrkrv
      121 tkclvnimqk eqgktilvvs hgaacrqfir ewaylsditp qapigncsim kfcfendqfy
      181 leeiinhdfs hle
//
LOCUS       WP_010826901             271 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metallophosphoesterase [Enterococcus].
ACCESSION   WP_010826901
VERSION     WP_010826901.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..271
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=30206
     Region          5..270
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mnvylflalf fiiigilsys ffiepnclvi hknqikvtes gktlrivqls dihlkknysv
       61 kalkqivekt ntlqpdivvf tgdlfddyar fgieiqdevs qlfrkinapy gkfaiygnhe
      121 ysgldtnfye tileaadftv lkntgkllpv shhislyvag ledslygqtd laaalvnrpt
      181 gtptlllthe pdvadsavnk nidlilaghs hggqirlpff tyknqlakky thglyhlede
      241 tplivhpgig ttkisarfgv lptielielt i
//
LOCUS       WP_010826959             343 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Enterococcus faecalis].
ACCESSION   WP_010826959
VERSION     WP_010826959.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..343
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37237
     Region          <39..177
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mknillsilg vlsivvslaf ssysvnaasn ewswplgkpy agryeegqqf gntafnrggt
       61 yfhdgfdfgs aiygngsvya vhdgkilyag wdpvgggslg afivlqagnt nviyqefsrn
      121 vgdikvstgq tvkkgqligk ftsshlhlgm tkkewrsahs swnkddgtwf npipilqggs
      181 tptpqnpgpk nfttnvrygl rvlggswlpe vtnfnntndg fagypnrqhd mlyikldkgq
      241 mkyrvhtaqs gwlpwvskgd ksdtvngaag mpgqaidgvq lnyitpkgek lsqayyrsqt
      301 tkrsgwlkvs adngsipgld syagifgepl drlqigisqs npf
//
LOCUS       WP_010827275             556 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010827275
VERSION     WP_010827275.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..556
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=63968
     Region          6..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          238..552
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mmtvndllha eelpgltllt hetnldapil qanilenpda fdwltpgeil lttgyifkdq
       61 pclqkrliqe lanmncaalg fkvqryfnev pqemiqland vglpilsipy nynfsqiisl
      121 vnrrvnqpde tisqhsvhmh nkfytiikag gkstqllevl saaiqapvml lderfqimnh
      181 fdlpdaptri tsilnnatlk kqfetalkaq nnelllfyke pltvefslan hqlslrilpi
      241 kkknlslsyl viwqttkklq tidllsvevc ahyllpqlql essenlttrq kigalfqdli
      301 qqkntnpqaw qefsnylqln ekdtfslllv aieqleqlfn ptiqmnsigh qlnhilegyr
      361 qkitafptqt gfilllenpa qeeatylaqt thlaknlleq lmklnpklsf klaigptvkk
      421 itnlcdsykl aqetfhlaqa sqelqqrtil nyddlffyrl mietltkqak qkiyqrliep
      481 lekedqkhes slletintyf qsnknislta tnmyvhrnti iyrlkkieei lhltlefpds
      541 slqlslavyl ykqkll
//
LOCUS       WP_010827269             267 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Enterococcus faecalis].
ACCESSION   WP_010827269
VERSION     WP_010827269.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..267
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29701
     Region          4..263
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(8..12,42..43,193,215..217,219..220)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 mkkliaidld gttlnaqsli spkteqtlkk aidnghyvsi atgrpyrmsh qfyqqlgltt
       61 pmvnfngalv hipekkwdle seanierdlv fdilaqkkel qldfvaaenk etfyidtldg
      121 fdpkffaska tldnlltakn lrtnptsmmv rttpnqaekv adtltkqygd yidvrtwggp
      181 mpilemvakg iqkahgvdqv anflsvksad iiafgdehnd eemlsyagwg vamnnatdki
      241 ksvandvtek tndqdglady lenyldl
//
LOCUS       WP_010827379             420 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010827379
VERSION     WP_010827379.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 420)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..420
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45798
     Region          1..409
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
ORIGIN      
        1 mskfwiiatd vykknvksls flimilapfl lvgivylags lasgfsgdtt iglvsenqav
       61 vkeltknkte dfsfkavsse kkaqeqlkde kidayllldt tdnqisgqly serslgnate
      121 mlipqmlnql qtmananrln ltaeqvamln qqatfkkaki sfdengkikt gedntgiqma
      181 lamgitillf vfissyssii aqeiasekgt rimevilsst kaqthfygkl tgvilvaltq
      241 ifiygvafvl gysqlknldf mksllsgisp qsifsstfif tlgffiigil vfavlaalcg
      301 slvskpedta kavqpimyig ligymigitf gtndpqnivv kvtsfiplis syimpvrlat
      361 etastmeaiv slvilavfgi iltifsarly ksnvlvyseg gmiqslkqsi silkneqkhk
//
LOCUS       WP_010827502             686 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus faecalis].
ACCESSION   WP_010827502
VERSION     WP_010827502.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..686
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=79132
     Region          19..629
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mkkinnrlgl flffvllfwa ktilayyldf slgvkgslqr eilwfnpvat tlllfgfsly
       61 fkkhktfmls ltllnvlntl ilylniifyr eftdfitiqs vfgfskvseg isgdllalmr
      121 vhdvfywldt lvllvlvfys fkqrrnhqvf mtkpinrrla isisclsvll fsvnlflset
      181 drpqllqrif drnyivkylg ldaftaidgv ktamsnevra eassnelpei mkftkqnnlp
      241 lnpqyagiak gknvfvihle sfqqflinmk vqgqevtpfl nqlyqnkati sfdnffhevg
      301 qgktsdaenm letgtfglpq gslftqlgsd ntfeaapavl gqkgyttavf hgnvgsfwnr
      361 dhvyknlgyq yffdrsyfsk ddkmlgygil dkqllresas elehlqqpfy akfltvtnht
      421 pyytddqnfp fpklntgnsi vddyvrtahy ldqsleqffh ylqttslynh sifviygdhf
      481 gisdannkdl ckafnrdpkt wtnydnaqlq rvplmfympg ytqgkimhey ggeidvlptl
      541 yhllgvddkn yihfgtdlls pqykqvvpfr ngdfvtpqfs ylggeiynnq gkkldqvpad
      601 lkaevtkdnd wvkkslslsd klnqenllrf ykpqgfqevq pkdynydvaf eknkvlevek
      661 qkntqstslf sqngnqttvq nypttp
//
LOCUS       WP_010827399             778 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus faecalis].
ACCESSION   WP_010827399
VERSION     WP_010827399.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..778
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=85743
     Region          10..659
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(300..302,365,384..386,411,463..465,509,512,515,534,
                     537)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(594,598..599,601..602,627,630..631)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
ORIGIN      
        1 mlnkvdlkkg lsteevakqk elglqnnyee nvakstkdii fdnvmtlfnf lnfaiavcll
       61 fvgaysnlaf lviiivnmsi gifqeiharn lvqklsivak envhvvrngv qqeidtkelv
      121 medivvisag eqvpsdmevi dgkveaneal ltgesdliek eigdtllsgs fivsgqayar
      181 vihvgaenya vkitqeakvh kpiqselvns irkvskftsw viiplgiilf veafwlrdag
      241 iktsvvasaa allgmlpkgl vllisialtt gviklakkri lvqdmysiet lahvdtlcld
      301 ktgtitegkm kvqkaiilhd kyeelfpqii gsylsestdn nitmqairdh yevsnrfgak
      361 evlafsserk wgaiefpeig tvylgaperl vddsrlpeav ftaqengyrv lmlaiaeqqp
      421 lnetkmpyle plaileiddp irqnaketla ylkeegidlk visgdnpvtv sniarraglp
      481 gyesyidlst ktteaevrea vqqytvfgrv spqqkrtivr elkdtehvva mtgdgvndvl
      541 alreadcsia maegdgatrq isnlvlldsd fttlpdvlfe grrvvnnvtr vssvffikti
      601 ysfilsiica ltaiafpfip iqvtlidlai egypafflsf egdkrkvvgk flptalknas
      661 vnallvvani iavyligqnq gfssldtttl myyllvgisc mavvraclpl nplriflvfs
      721 tiigiyvaam lfhnileigf ltsqtmglff immainivvr vaigfvqmkr agktikdl
//
LOCUS       WP_010827667             241 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010827667
VERSION     WP_010827667.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..241
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28486
     Region          1..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mnignslkmr rnelgltqse vaeklyvtrq tisnwennks ypnidcliel snlyemtldr
       61 llkedntmve klskdiregq kykklflill iivlciggyf tilqlrlnnl ysgvkewnqn
      121 gqtynliedn iqyhvvkidn ynlftipeel elmssyisen ekfnmyysgd dsnikiywtt
      181 galnglelsf dkefifdtvn qrnkfsyeiq elinknldkd kkeltilykq tknkweeinl
      241 k
//
LOCUS       WP_010827728             575 aa            linear   BCT 01-JAN-2025
DEFINITION  terminase large subunit [Enterococcus faecalis].
ACCESSION   WP_010827728
VERSION     WP_010827728.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..575
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66214
     Region          1..572
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 miepgvnyad lfakevrkhp kkypktvrla idrwyrwkkr kdiwfdvdra nemmdwvesf
       61 ivhtkgdmvg kpfllepwek fiyswiygwv kenekgqvvr vtreayvqip kkngktliav
      121 galgyamyge galsvdcyac asdfaqaqya akpfaatiln npvlldgtki fkgpkgtvss
      181 itydylhgdm aytnkfivqt knidniegsn pyfvlndelh kqekmeqydn fksaqislpq
      241 plmfnistag kgsssvgirv ykeakevlkr ddndsnfvli yepnkgydwt drkvwemcnp
      301 nwgisvdlsa lesafktaqr sahskaeflt khldvfvnga dnffeqdqve pclvptnelg
      361 nlsgepcwig ldlsksrdlt cvslnfptwd aegkailkvk qlyfipseni dfrekednvp
      421 yselaeqgfv efcdgklidq eqifhfiedc mdfydvqqvn ydpamsdrlv eklenlglec
      481 vqvdqyarvl nspledaerl fyeqrimfdn plflycalnv vvkmdfqgrk vpsknqskrk
      541 idgfvaflca hketmdqmid vkeddmdeyl dsiyr
//
LOCUS       WP_010827936             383 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide pyruvyl transferase family protein [Enterococcus
            faecalis].
ACCESSION   WP_010827936
VERSION     WP_010827936.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10514996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..383
                     /product="polysaccharide pyruvyl transferase family
                     protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44450
     Region          14..317
                     /region_name="PS_pyruv_trans"
                     /note="Polysaccharide pyruvyl transferase; pfam04230"
                     /db_xref="CDD:427804"
ORIGIN      
        1 makigiitln gdfnygnrlq nfalqyvlkn kdisvdtiiv retkskkikr elllgkisnt
       61 kdlkyvvnki arkltpksts krlrykkmqk ekyqtinpft rkyissinve kedlnkidek
      121 ynlfivgsdq vwnpniiefd tthfltftss qkrysysasi gvssipevpm klnnhykhfl
      181 sqmkyisvre lagasivkem inkevdiapd ptlllekeew lnafnfkenp eknyillyfi
      241 sgipveikks idlfakqkkl kviqimgdly ddshiivspd qfiqlindah yfftdsfhgt
      301 vfsiimetnf ltfgrsdgkd insrietlle kfrlpqlltc nsrdvflvdq lnsfdnvkmi
      361 hqqekkrgie iisnnilknl geq
//
LOCUS       WP_010828043             250 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010828043
VERSION     WP_010828043.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..250
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27912
     Region          10..250
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mketkpygtv llkaakimdc lsvqpdqtlq eiakntemta staikiletl tligyvqkdt
       61 nktyrlgtkl iryanqsveq idlaeiavpy lenlqntvde tihlgilnnn eilyinklep
      121 knqtirmssk vgitrplyns amgkavlaef seeqvqqyld tqtlipyten titnplrlkk
      181 elkqvqqtgv ayddeeieqd ifcsgvslmk dgeiagafsv smpkyrltee nkttinqall
      241 atkaaieakl
//
LOCUS       WP_010828111             556 aa            linear   BCT 01-JAN-2025
DEFINITION  PucR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010828111
VERSION     WP_010828111.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..556
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=64045
     Region          6..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          238..552
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mmtvndllha eelpgltllt hetnldapil qanilenpda fdwltpgeil lttgyifkdq
       61 pclqkrliqe lanmnyaalg fkvqryfnev pqemiqland vglpilsipy nynfsqiisl
      121 vnrrvnqpde tisqhsvhmh nkfytiikag gkctqllevl saaiqapvml lderfqimnh
      181 fdlpdaptri tsilnnatlk kqfetalkaq nnelllfyke pltvefslan hqlslrilpi
      241 kkknlslsyl viwqttkklq tidllsvevc ahyllpqlql essenlttrq kigalfqdli
      301 qekntnpqaw qefsnylqln ekdtfslllv aieqleqlfn ptiqmnsigh qlnhilegyr
      361 qkitafptqt gfilllenpa qeeatylaqt thlaknlleq lmklnpklsf klaigptvkk
      421 itnlcdsykl aqetfhlaqa sqelqqrtil nyddlffyrl mietltkqak qkiyqrliep
      481 lekedqkhes slletintyf qsnknislta tnmyvhrnti iyrlkkieei lhltlefpds
      541 slqlslavyl ykqkll
//
LOCUS       WP_010828214             465 aa            linear   BCT 01-JAN-2025
DEFINITION  catalase [Enterococcus faecalis].
ACCESSION   WP_010828214
VERSION     WP_010828214.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..465
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52530
     Region          2..446
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mknqhlttsq gspvgdnqns ltagefgpvl iqdvhllekl ahfnrervpe rvvhakgaga
       61 hgvfkvsqsm aqytkadfls evgketplfa rfstvagelg ssdtlrdprg falkfytdeg
      121 nydlvgnntp iffirdaikf pdfihsqkrn prthlkspea vwdfwshspe slhqvtilms
      181 drgiplsfrh mhgfgshtfk wvnaagevff vkyhfktnqg iknlesqlae eiagknpdfh
      241 iedlhnaien qefpswtlsv qiipyadalt mketlfdvtk tvsqkeypli evgtmtlnrn
      301 penyfaeveq vtfspgnfvp gieaspdkll qgrlfaygda hrhrvgansh qlpinqakap
      361 vnnyqkdgnm rfnngnsein yepnsytetp kedptakiss fevegnvgny synqdhftqa
      421 nalynllpse ekenlinnar qidlftfcll fnafystlyn vyyvn
//
LOCUS       WP_010828150             107 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010828150
VERSION     WP_010828150.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..107
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12416
     Region          3..101
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mkqtellkgi leglvlaiiq rketygyeit kilydqgfte ivegtvytil lrleknqwvi
       61 aekkpsekgp mrkfyrltss geaeladfwq rwtllskqvn kmkkmeg
//
LOCUS       WP_010828261             472 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Enterococcus faecalis].
ACCESSION   WP_010828261
VERSION     WP_010828261.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..472
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53046
     Region          2..457
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mfdivtlari qfamttvfhf ffvpfsigla lvvaimetmy vvkkeeryrk makfwgnifl
       61 lsfavgvvtg iiqefqfgmn wsdysrfvgd ifgaplavea llafflestf lglwiftwdk
      121 mnpkvhvtfi wlvvfgsmms afwilvansf mqhpvgyvin ngraemvdfv avisnpkvwy
      181 efshvimgaf tlggmavagm aafqllkkrd isfhkasmri glwvtlfgsi gvllagdlqm
      241 kaliegqpmk faamegayed sddpaawtli awaderehkq vfgidipyml silsynklsg
      301 svdgmdtvnk rlvekygddk nyyppvntlf wsfrimagfg almllvaalg lfftrkkkps
      361 lyekkgmlwi valctfapfl anttgwlvte lgrypwtvyg lftieqsvsp nvsvaslits
      421 nviyfllfag lgsvmvylvi lelrkgpdye akklakenep aldpfdkgvf ge
//
LOCUS       WP_010828266             568 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010828266
VERSION     WP_010828266.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 568)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..568
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63079
     Region          3..532
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mkkpiitfnn fsfqyhsqse ptlkgiqlti yegekvlivg psgsgkstla qcinglipni
       61 yegeiqgtat vageniqets lfdlsfdvgt vlqdtdgqfi gltvaediaf alendaveqa
      121 emkkavqkws eivelnqllq hrpqdlsggq kqrvsmagvl inqskillfd eplanldpra
      181 gqetmtlidt iqqetkatvl iiehrledvl cesvdriivm negaiisdtt pdellrqdtl
      241 tqqgireply vtaikyagid ltqvshldkl aevsgetvlp kmtqwsvqps svsavkgael
      301 lrleqvsyqy drhgekvldd fsvtihhgem isivgkngag kstlskiicg fitpqsgkil
      361 wegqdfsnys ikeradkigy vmqnpnqmis kkmifeeval glvlrdvpqa eieervtnil
      421 hicglypfrn wpisalsfgq kkrvtiasil vlepellild eptagqdfkh ytemmtflee
      481 lnrlgvtilm ithdmhlmle yttralvvcd grlladatpv avltdekliq aaslketslf
      541 tfakalglen pllftekfva ydrevrfg
//
LOCUS       WP_010828265             249 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010828265
VERSION     WP_010828265.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..249
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27318
     Region          1..236
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mrkrfnlavq altvqyqgrt alnnihvtip sgkitgiigp ngagkstfik gllgliktke
       61 rdvllnnqai dqqkttiayv eqrsaldlsf pisvfetvll gtypnlgllk rpgkkekqaa
      121 maalkmvqle dyaqrqigel sggqlqrvfi arvlaqgaev ifldepfvgi dmssekvimd
      181 ilkslknqgk miiivhhdlh kvshyfdeli vlknrliaag pveqtftaet lqeaygdllg
      241 dlliqgvak
//
LOCUS       WP_010828273             160 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Enterococcus faecalis].
ACCESSION   WP_010828273
VERSION     WP_010828273.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..160
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=18696
     Region          3..154
                     /region_name="SRPBCC_CalC_Aha1-like_6"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of an uncharacterized subgroup of CalC- and Aha1-like
                     proteins; cd08899"
                     /db_xref="CDD:176908"
     Site            order(14,16,18,27..29,31..32,37,45,53,55,57,59,63,65..66,
                     68,71,77,79..80,85..86,88,90,101,103,105,107,112..113,
                     115..121,123..125,128)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176908"
ORIGIN      
        1 mkdtfrlenq tiyfgterai saspqtiwry ltetdklkqw fseleigelg vngfwrfilp
       61 dfeetmpftd yaeekylgvt wdtgiiyfdl keqaphqtll vfseslpenf ttprhkdiag
      121 wsivlnrlkq vvetpdaape kidfpqienh ylekltnlen
//
LOCUS       WP_010828295             402 aa            linear   BCT 01-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Enterococcus faecalis].
ACCESSION   WP_010828295
VERSION     WP_010828295.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..402
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=44314
     Region          3..389
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mpnkvkkrhl ldysifipyl ilsivglimv ysstsalqvm kgfsptsfvi nqvafwvvgl
       61 vamffiykmk tsvfqnrsfi mfaiavitvm vlavripgig keingargwi eiggfsmqpa
      121 eylkimvvwy lsyilarrqk tinggmdqfk qaagrplmlv fvlialvaiq pdfgnaailt
      181 litivmvlas ginymytylv gglgilgslt aiqllimskg kifparyqyi ynrfavfknp
      241 fldernlghq lansyyaisn ggwfgkglgn svqkkgflpe ahtdfifait leelgiiggl
      301 ailgllmfmi ariilvgvrs kkpfnslmci gigtmlliqv finvggitgi ipltgitfpf
      361 lsqggnslli isiavafvln isadetrqkl eneyylsleq nq
//
LOCUS       WP_010828399             437 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Enterococcus faecalis].
ACCESSION   WP_010828399
VERSION     WP_010828399.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..437
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45783
     Region          1..434
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mkekissyfe leqlntnmkr emlagfttfi smayilfvnp tvlgasgmde gavftatala
       61 salgcilmgv lakypiatap alginaffay svsvgmgipw qttlagvfva slifilitif
      121 klreliidai padlkfaisg giglfiaflg lsqgglivan datlvglgpl nvgstwvtiv
      181 glvvtaillv rrvpdgifig maistivgla tgvipmpdki issapslept flvalghvkd
      241 intiqmwvvv ltfllvtffd tagtlvglan qagfmkdnkm prvgkalaad stamlagsll
      301 gtspvgayve ssagiavggr sgitaittgi lfifsllfsp llavvtsqvt apaliivgvl
      361 maqslskikw nemeiaipsf lillgmplty sisdgialgf ilypitmiaa krgkevspim
      421 yglffvfvgf mwilnaq
//
LOCUS       WP_010828416             161 aa            linear   BCT 01-JAN-2025
DEFINITION  cupin domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010828416
VERSION     WP_010828416.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..161
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18078
     Region          1..142
                     /region_name="CFF1"
                     /note="Predicted sugar epimerase, cupin superfamily
                     [General function prediction only]; COG3542"
                     /db_xref="CDD:442763"
ORIGIN      
        1 mteqmwiekl gleahpeggy fkqtnkseql iptkrgeral htailfllnt espshfhrlk
       61 adelwffhdg qpltvhcifp dgtyqavqig kdlvqgqqls fsvpagtifg stvatgfalv
      121 scvvtpgfef edfelftqae llndypqhse iiqhlayrel p
//
LOCUS       WP_010828512             828 aa            linear   BCT 01-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Enterococcus faecalis].
ACCESSION   WP_010828512
VERSION     WP_010828512.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 828)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457611
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..828
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87451
     Region          1..67
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          75..139
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          163..814
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(461,463,769)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(505..507,571,587..589,618,658..660,680,683,686,705,
                     708)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(770,798,802)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mesktfdieg mscascaqti ekataklpgm akasvnlate klsvtydqte vteeeikeav
       61 sdagykaisp aqqrtfaieg mscascaqti ekavnqlsgv qqaivnlate klvvsyddhq
      121 vtsaeiikav tdagyqatee vaagatadqd rekkqkhiae mwqrfwisav ftvpllyiam
      181 ghmvglplpd flnpmthatt famvqliltl pvlyvgreff tvgfkalfkg hpnmfslval
      241 gtsaafvysl ygtvmiflgd tsftmalyye sagviltlit lgkyfeavsk gktsdaikkl
      301 mglapktahi lrdgaeievp vdavqlddiv ivrpgdkipv dgvivsgsss vdeamltges
      361 lpvekkvgda vigasinkng sfqfkatkvg ketalaqiiq lvedaqgska piaqladkis
      421 gvfvpivigl avlsglawff lgqeswifal titisvlvia cpcalglatp taimvgtgkg
      481 aengvliksg daletthkiq tivfdktgti tegkpvvtdi lvadsalsea elltlaasae
      541 qgsehplgea ivgaakerql plaegsdfsa ipghgirvtv nervlllgni klmkeeaiel
      601 stfvqqadrl aeegktpmfv akdgsfagii avadtvkdss qtaiarlhkm gieavmitgd
      661 nkrtaeaiak qvgidrvlse vlpedkalev kklqaegkkv amvgdginda palaqadvgi
      721 aigsgtdvam esadivlmrs dlmdvptave lskatiknik enlfwafayn tlgipvamgv
      781 lhlfggplls pmiaatamsf ssvsvllnal rlkgfkpstv krtsgsqk
//
LOCUS       WP_010828561             746 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Enterococcus
            faecalis].
ACCESSION   WP_010828561
VERSION     WP_010828561.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 746)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..746
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82348
     Region          1..>81
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          106..705
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 micqncqqne atihlyanvn gqrkqldycq scyqklknqa nnspqnmgqd pfgfgslddl
       61 yrslsrqmqq gnpyeqqtpp tqfgdggngg qpprggagag qgllgeygin iteaarqgdi
      121 dpvvgrdqei krvieilnrr tknnpvlige pgvgktavve glaqkivdgd vpkklldkev
      181 irldvvslvq gtgirgqfee rmqklieeit eaenvilfid evheivgaga agdgnmdagn
      241 ilkpalarge lqlvgattln eyriiekdaa lerrmqpvqv deptvaetit ilhglqkrye
      301 dyhhvkytde ainaaanlsn ryiqdrflpd kaidlldesg skmnltiqlv dpktidkkla
      361 eaeqqkqqas aeedfekaay yrdqinklqa mkekqisdee tpvitekdie aiveqktgip
      421 vgdlkekeqt qlknlavdlk ahvvgqddav dkvakairrn rvglgkqnrp igsflfvgpt
      481 gvgktelakq lafelfgsed smvrfdmsey mekhsvskli gsppgyvgyd eagqltekvr
      541 rnpyslilld eiekahpdvl hmflqilddg rltdaqgrtv sfkdtiiimt snagtgavea
      601 nvgfgaareg vtksvlgqln nfftpeflnr fdgiiefkal skenlmnivs lmleevngll
      661 akqklhievp tevkeklvdl gydpamgarp lrrtiqeqie dgiaeyyldh penhqlvaal
      721 dnegkiivtg aqevtktets tsdqae
//
LOCUS       WP_010828529             253 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            faecalis].
ACCESSION   WP_010828529
VERSION     WP_010828529.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28104
     Region          1..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlieerlaki qkivnkqksi smealaeqvs vskdtirrdl irlekeghlk rthggaisvq
       61 seatiydyaq rivkhpkkkq aiaqkvwani pkqasiffds sttveaaira menspihait
      121 nslshallla qmdqtkitvl pgqlhkqqlf lfgaetvakv gefapdytll gvfalseqgl
      181 fihteeegqv krrmiqqgkq vialadqtkl nktglfkice lteidclvtd trpdekfceq
      241 laqagvtliv ade
//
LOCUS       WP_010828565             250 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Enterococcus
            faecalis].
ACCESSION   WP_010828565
VERSION     WP_010828565.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..250
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27718
     Region          1..242
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlteerhqki lqlldqksvv ksqelaslfn asestirrdl qeledanlle rihggakril
       61 nlgfeqnmte ksiknthekq kiaslaascv qdgdmiylda gsttlemipf lvgkqihvvt
      121 nsvhhaakls dmeiptimlg gtlklstkai igatsmeqlq hfrfnkaflg tngahlefgl
      181 ttpdpeeaal kalaihqaet ayvlldhtkf nevtftkvee lesvtlltdy cpaeslqefq
      241 qktilmeank
//
LOCUS       WP_010828468             232 aa            linear   BCT 01-JAN-2025
DEFINITION  XRE family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010828468
VERSION     WP_010828468.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..232
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25977
     Region          1..69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          111..227
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mdtniighqi tllrkkfglt qedlalklgy skqtisnwet glktprmgai qkisdlfnvs
       61 ksfiiegdql sntlthitni sakldekrqk kvlayaeeql heqntsdikv vplvgksaan
      121 psvleygdtd ieqrsfayvp dnadcaiyiq gdsmeplikn gsivfykkqc dvengeiaiv
      181 eidgdgvtck klikdyener iilrsinkky ddrvlrgeei riigkvvtpd kd
//
LOCUS       WP_010828835             301 aa            linear   BCT 01-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Enterococcus faecalis].
ACCESSION   WP_010828835
VERSION     WP_010828835.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..301
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34323
     Region          97..299
                     /region_name="CE4_SmPgdA_like"
                     /note="Catalytic NodB homology domain of Streptococcus
                     mutans polysaccharide deacetylase PgdA, Bacillus subtilis
                     YheN, and similar proteins; cd10944"
                     /db_xref="CDD:200569"
     Site            order(102..105,156..161,201,203..204,229,235..236,269,271)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:200569"
     Site            order(104..105,156,160,203..205,229,269,271)
                     /site_type="active"
                     /db_xref="CDD:200569"
ORIGIN      
        1 mrhkkrkfki ngyvlfsali livlvfiqtf lltqpkitsk nddttqtstk nstakkdspt
       61 klekesthmt isskkyaysa dkirkyitge epykgeklvf ltfddgvnnq itpqvldtlk
      121 kynvhatffl vgntltsenq kivkrevaeg hsigfhssth dyatlypngi vnteeiqaei
      181 atmknslkki lgetfqttlw rypgghmswg gteksdelfk qlgihwidwn amvgdaepld
      241 rqpttvieml afhqhslevy pdynirvvlm hdsvdkeltk qalpqliefy qangyqfgvl
      301 y
//
LOCUS       WP_010828890             241 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Enterococcus faecalis].
ACCESSION   WP_010828890
VERSION     WP_010828890.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..241
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26782
     Region          5..191
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(8,10,95)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(44,94..95)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            93..95
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mkvlliipay neeenilrti asietfkqev thfqhelnyv vindgstdgt kqileanqin
       61 aihlvlnlgi ggavqtgyky aleneydvav qfdgdgqhdi nslpillepl aegkcdfsig
      121 srfipgneas fqstkmrrfg irllsfcirm asgktiydvt sgyragnrkv iaffakrypt
      181 nypepesivh likkrfvive rpvnmmerlg gvssiralas vkymlevgsa iliaafmkeg
      241 d
//
LOCUS       WP_010828905             443 aa            linear   BCT 01-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Enterococcus
            faecalis].
ACCESSION   WP_010828905
VERSION     WP_010828905.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..443
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46368
     Region          28..437
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 msekkqsnlh ltvgpedsvs fgqatmlgiq hvlamdvyvv pviiasiigi staqtssliq
       61 atfiaaglat iiqshfcmrl pvaqgpsfip igaiagiyfa nnqqgngwga vlgaslvgai
      121 vviilgftgi fnrlitkfvp pivggtiifv vglslmpval sdniyhakge lgqnillafi
      181 aagtliffal lgsalkkgri frvssvilal lfgsiaaqll gvldlsavse aawfslpqlp
      241 lvnfsfqfdw saiatmlviy lvlmaettgt wfavshvvae plteekinrg vigeglgclv
      301 ssfiggtpvt systnagiis itgvasrkvf vaagawfvlf glsgklstli saipapvigg
      361 vfvvvcgiis vsgmkvmsdv tihekemyvi avpiimtlal tllpkeflet lpqflqylfs
      421 spvatasiva illqaillnv qeg
//
LOCUS       WP_010829054             406 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Enterococcus faecalis].
ACCESSION   WP_010829054
VERSION     WP_010829054.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..406
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=45121
     Region          1..402
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mkfldlfagi ggfrlgmesa ghkcigfcei dkfarisyka ihdttgevem hdittisdef
       61 irgigsvdvi cggfpcqafs iagkrkgfed trgtlffeia rfasilrpry lflenvkgll
      121 nheggatfet ilrtldelgy dvewqvlnsk dyvpqnrerv fiighlrger trkvfpfern
      181 dqsiiklsrq qssvntitar ygeaagvgsy iveskqqkki aipvltpdrl ekrqngrrfk
      241 engeemftlt aqdrhgimia gnlpgnheqn srvyetkgva ptlstmqggg qepkilvkea
      301 tvkgyaealp gdsvnishpn sntrrgrvgk giantlltge eqavvtnnfr irkltprecw
      361 rlqgfpdwaf dkakevnsds qlykqagnsv tvpviadias rldvng
//
LOCUS       WP_010829082             669 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus faecalis].
ACCESSION   WP_010829082
VERSION     WP_010829082.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..669
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=76712
     Region          24..649
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnykisylld eyagqkials laqqitdlsq relvtqlsti ggevqqntvs ipnlsanewg
       61 kqlfqqrqvi yseterqali flltyseiee lsvyhyqnfl dvskgtilad ikkvrhqlat
      121 enialsyerk rgfylegdef rirrfgknwl arllqqksgt falfcwlsqh qmsqyakmrd
      181 giqlavqeaq lqlvpsrlde isyflafsqk rlgkyktvvw penqliqslr aypvsrrils
      241 dlvgpvanve teslffticl mtalqgelrd tkleflldis geiirkmell avvqfeqpre
      301 llmnvyyhlv payfrinygf ylpnvlikdi rqsyrslyhl ceqalaplek ltkrsipsee
      361 isfftilfgg eifgqkneqr qeklkalivc psgissslil qselrrlfpm iefketnavr
      421 eienvseksy diifstvpie takkvyltkp imssleknql mhqvqsdwll pgismpdvkd
      481 ildalkpyis lkkgvteaql yrvlhrkmnk ilekeedlrp mlsellttet vqvlpevadw
      541 ragiteaakp llkngsitek yidamiqkve sfgpfihicp dvalpharpe dgvnqlgmsl
      601 lkiqksvdll edpkheihlf iclaasdnet hlralssltk ilskkeslhr lvaaetvpei
      661 lsiiqegek
//
LOCUS       WP_010829165             280 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010829165
VERSION     WP_010829165.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..280
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29851
     Region          4..274
                     /region_name="ABC_perm_SloB"
                     /note="metal ABC transporter permease subunit; NF040927"
                     /db_xref="CDD:468860"
ORIGIN      
        1 miqnfinglh efhflqnali tsvfigivsg tigcfiilrg mslmgdaish avlpgvaisy
       61 ilginffvga ilfgllasii itfikgnsii kgdtavgitf ssffalgvih igvansstdl
      121 fhilfgnila vqdidkwitl gvsllvmivv ilfykellit sfdplmakam gmnvdfyhyl
      181 lmvlltlvav tamqsvgtil ivamlitpaa taylyansls tmiliastlg asssllglfi
      241 gysfniaags sivltsatff aisfivspkq kflrkkvtni
//
LOCUS       WP_010829213             438 aa            linear   BCT 01-JAN-2025
DEFINITION  Y-family DNA polymerase [Enterococcus faecalis].
ACCESSION   WP_010829213
VERSION     WP_010829213.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..438
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=48958
     Region          14..364
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(17..18,21..22,57,60,116..117,172)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(114,117,201..207,236,263..268,295,324..328,330)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mkfdyskepr rdvlcidvks fyasvecver gldplktmli vmsgadnagg lvlaaspmak
       61 kvlgisnvtr kdevpdhpel livpprmnly mkrnseinnl lkrfvadedh svfsvdesfi
      121 ditaslryfn cdtayrlari iqrviynhmg lyvtigigdn pllaklaldn eakntpgfva
      181 ewryedvqek vwaispitef cgigkrmaar lkmsgiesiy dlahadpyll khrfgvmglq
      241 lfahawgidr sflgekrqva keksfgnsqv lprdyarkdq ielvlkelsd qvatrlrnsn
      301 cqtecfsifv gyskgqvdgl grsgwrkqlk iarsnntkvl tehvlklfre nfipgidirn
      361 lgvsfgklvw dttlqidlfs ppeeqiinnq ldflidkirq kfgfkaliha ssllegatav
      421 nrsglvggha ggnvglgg
//
LOCUS       WP_010829382             607 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus faecalis].
ACCESSION   WP_010829382
VERSION     WP_010829382.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..607
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=66526
     Region          16..446
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 madlkrlfig kplksaende hklsrfaala llssdalssi aygteqivvv lvtlsaaaiw
       61 yslpiaafvi illisltlsy rqiihayphg ggayvvnsen lgrnagllag gsllvdymlt
      121 vavsvsagae aiisaipaly ghqvaisigi vilitlmnlr glresasflm lpvysfiaii
      181 tllivvglfk ivtgaqplna talpgavvpg isialvlraf ssgsssltgv eaisnavpff
      241 kkpraknaag tlalmatilg fffvgitfin ywygivpkee vtvlsqigka vfgqnilyyl
      301 lqfatalila vaantgfsaf pvlaynlakd kfmphmymdr gdrlgysngi ltlaagsivl
      361 llifqgster liplysigvf ipfalsqsgm vvkwrketkn wlpksianiv gafisfaiia
      421 ilfiyrlgdi wpffiimpvl iyafyrvnth yknvaeqlrl edgaqlhefd gntvivlvgn
      481 vtkanvgaln yarsigdyvv amhvsmdenv ekekeiqeef kkhfpdvrls ivhssyrslq
      541 npilryvdlv sknatkhnys ttvlvpqfvp nkrwqnilhn qtslrlrirl awreniivat
      601 ysyhlkk
//
LOCUS       WP_010829473             104 aa            linear   BCT 01-JAN-2025
DEFINITION  thioredoxin family protein [Enterococcus faecalis].
ACCESSION   WP_010829473
VERSION     WP_010829473.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..104
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11848
     Region          8..100
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(28,31)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 miypnsleel atyvekgknv ffftadwfgd crfikpvmpe ieeafpafqf ievdrdqfid
       61 vaaewsifgi psfvviengq elgrlvnkdr ktkeeisafl tslg
//
LOCUS       WP_010829502             296 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParB/RepB/Spo0J family partition protein
            [Enterococcus].
ACCESSION   WP_010829502
VERSION     WP_010829502.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..296
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33832
     Region          27..290
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mkkskglgrg idalfqdlen letvdvkddt vvqlplnelr pnpyqprktf eevslqelan
       61 sieqsgvfqp iivrrsavkg yeiiagerrf rasklaeket ipaivrdfde eammqvavle
      121 nlqredlnpl eeaeayemlm knlkltqaev asrlgksrpy ianylrllsl pdlvkemvqd
      181 qrlsmgqart llglknktli lklanravte nltvrqleql vsdlnqndgk ekkkiprlak
      241 ekpyyirese drlmdkfgts vaiqekdgkg kieieylsqk dltrildild iqfdee
//
LOCUS       WP_010829511             368 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010829511
VERSION     WP_010829511.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..368
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41042
     Region          6..327
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 menqtilsve nisvsfhvrh relkairnvs lelkeketla ivgesgsgks vltktftgml
       61 eqngnitsgt irykdkilse lkkdeewedi rgkeiatifq dpmtslnpik tigsqisevi
      121 ikhqkksake akrlavelme ktgipnaakr ydeypfqysg gmrqriviai alacrpkili
      181 cdepttaldv tiqaqileli kelqeeyqft tifithdlgv vaaiadkvav myagqiiesg
      241 tveeifydpk hpytwsllss lpqlaqkgdv lysvpgtpps lykdiqgdaf aprsayamkv
      301 dftseppmfq vsethfaktw lldprapkvl kpkqienlhe kmialaaeld seeqdggeas
      361 cqlikklc
//
LOCUS       WP_010829523             879 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus faecium].
ACCESSION   WP_010829523
VERSION     WP_010829523.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 879)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 879)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 879)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 879)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..879
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..879
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95399
     Region          4..869
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 meeykqtiee vkkvteadpd tglssqevde rrkkqglnkf deapkesmik kffrslsdft
       61 tiillvaavi sfytafateh gdlfegllii aivvinsvla ivqegnaeka leslqdmnkq
      121 tatvirdakv ttveseqlvv gdilvlesgd aisadarlie asqlrveesa ltgeseavek
      181 daafiaeede slgdqlnmvf kgctvaagrg kaivtaigma temgkiadll nentmqktpl
      241 qvrlnqlgkr ismialaaaa lvfvigelqg epllemfmts islavaavpe tltvivtltl
      301 aygvqkmark haiirqlpav etlgtanvic sdktgtltqn emrvrrvwsk edevtnieds
      361 mtnsameilk maalctdvtv eqedddlvik gnptevaivr aveenyhtka eleekyprvn
      421 elpfdserkm mttvhqmgek yisitkgafd vlaprfssgd veqaaivndr fgkralrvia
      481 vgyatydeep qdissealek dlrligligm idpprpeskg aikrakkagi ktvmitgdhv
      541 vtasaiakel gilndpseal sgselhqlsd eeldarvkal svyarvtped kirivkswqr
      601 tgavvamtgd gvndapalka snvgcamgit gtdvaqsaad miltddnfat ivdavsqgrs
      661 vyqnirkain fllscnisei fivliamllg wgapftavql lfvnvvadgl pgfalgrepa
      721 ehgimdqppi pknegifarg llqkiainag vftivtlfgy ylgsyvdtis pwvdasqhvg
      781 qtvaflilay ssilhvfnvr ssqsifkvnl atnkalvema llalaittav allpftqelf
      841 glvhislnhw flvgilsivp iavnelikfh rlpeaeeee
//
LOCUS       WP_010829527             429 aa            linear   BCT 01-JAN-2025
DEFINITION  S1C family serine protease [Enterococcus faecium].
ACCESSION   WP_010829527
VERSION     WP_010829527.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..429
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44741
     Region          125..415
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mdrknvtpkm kksknnslwr klglglvggi vgglltagif yaamgtgnns statsgnqns
       61 agetvvenvk vnvdsditka vdkvqdavvs vinlqsqnqs sgfgglfgqq eessssddsn
      121 leaysegsgv iykkdgntay vvtnnhvvdg qqglevlmkd gtkvkaelvg tdaysdlavl
      181 kinsdkvetv asfgdssalk vgepaiaigs plgseyansv tsgiisslnr qvtstnesne
      241 tvninaiqtd aainpgnsgg plvniegqvi ginsskiast sestsnvsve gmgfaipsnd
      301 vvniinqlek dgkvtrpalg itmvdlsavs tqqqeqilki pssvtngviv tnvqtatpae
      361 kaglkkydvi tkiddkevss gvelqsalyk kkvgdsvkit yyegskektt tveltidqsa
      421 lkqnqnsen
//
LOCUS       WP_010829552             446 aa            linear   BCT 01-JAN-2025
DEFINITION  PTS sugar transporter subunit IIC [Enterococcus faecium].
ACCESSION   WP_010829552
VERSION     WP_010829552.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..446
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=48731
     Region          1..428
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdkfigiieq kimpvanrig tqrhmtairk giiatmplti vgsfftilln ipiesiaavi
       61 epyreildip frytvgilal yatfgiassl aksyrldslt agilalmsfl ivaapptril
      121 edmgevtagr yinianlgsg slfgaivtai isveiyrffi ekkitirmpd gvppevtnsf
      181 valipgavil iffwiirhml gfdlngflsq llmplkgvla gnslfggllt vflicffwvl
      241 gihgpaimgp virpfwdisi aenidafnag tsahampnif teqflqwfvw iggagttlal
      301 vvlfmfsksk ylkslgrlsi lpglfninep mifgapvvmn pvlgipfila plvtttlsyi
      361 ltvsgvvpmm varlpfampa piaawmstnw svaagllvig nflitlaiyy pffkvfekqq
      421 lareaeeqak eqaditltdg vteerl
//
LOCUS       WP_010829593             822 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: cation-translocating P-type ATPase [Enterococcus].
ACCESSION   WP_010829593
VERSION     WP_010829593.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..822
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=91024
     Region          32..687
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(323..325,392,410..412,439,491..493,536,539,542,560,
                     563)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(620,624..625,627..628,653,656..657)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
ORIGIN      
        1 mknkwtnrsk kkkvtqrssd kvirlfpsyk egltadqvke riekgaands vdptfktnqq
       61 ivleniftyf nliflilail lclvesyknl tflpviiant giaifqeirs kkildelnvl
      121 ntakvnvird gieqtidied lviddivile tghqipadae vvegklqvne alltgeadei
      181 tkeigdplms gsfivsgkay arldkvgads yisqltvkak tmgegeqsem iaslnqlikw
      241 igiiiipigi llfsqsyffn gntikesvva meaaligmip eglyllttia lalsatklak
      301 qrvllhnmks ietlarvnvl cvdktgtite nkmsvqkviv skkqeiisqs dqleaciady
      361 akamagdnat meavkayftk ttdqsyhhvi pfssvqkfss valadkvyvl gapemvlrdq
      421 lpeyaeefvs faekgyrvlv fgvydgilee pvlteavtpl gyilianpir kearatfdyf
      481 kkqqvaikvi sgdnpltvsn vavqagisha dqyvdaskls eeeyeaavek ytvfgrvkpe
      541 qkkifvqllk rnntvamtgd gvndilamke adcsiamasg neaamqasqv vlldsdfsrm
      601 pevvaegrrv vnniersasl flvknifsfl lslfsvifal typlepsqit lislftiglp
      661 sfllaleenk krirgkfimn vmekavpggl tdmivvgalv icgvtlnlnk tdvstastml
      721 liavgflvly kicsplnkfr sqiilfcasg iffsvvflhk lfsitgisav sllllsilff
      781 sadsifrhlt tlveylferk nekeseiinq mprflrlfkr nk
//
LOCUS       WP_010829557             697 aa            linear   BCT 01-JAN-2025
DEFINITION  LTA synthase family protein [Enterococcus faecium].
ACCESSION   WP_010829557
VERSION     WP_010829557.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..697
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78648
     Region          14..632
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mtqlkklcqn rlaivltavf ffwlktiiay yadfslgveg tiqyfilwin piattllffg
       61 lslyikkpkp alailliidi lntlllylni ifyreftdfi tvksvlgfsk vsqglsgssf
      121 slmkphdviy wldiavfigl lvwlkvkkip iksnpvgkpm aiavtclsgl ifsgnlalse
      181 anrpqllqrt fdrsyivkyl gidaytiydg iktgmtssvr ahassngide vldytkkhya
      241 epnpetfgia kgknvivlhl esfqqflinm kvdgqevtpf lnsifqnqat isfdnffhev
      301 gqgktsdaen mletgtfglp qgslftelgs dnvfqaapai lgqkqgytsa vfhgnvasfw
      361 nrdhvyknlg ydnffdrsyf desdetlgyg ildkdlfses aqylehlqqp fytkflsvtn
      421 htpyytddkn fdfpslntgn stvdnyvrta hyldqsleqf ftylkksgiy qnsifviygd
      481 hfgisntdnk dlasalgkdp dtwdefdnaq mqrvplmihm pgytkgtvnh eyggeidvlp
      541 tllhllgidd kdylhfgtdl lssqhdqvva frngnfvtpk ytvlggkayn nqtgeiidtk
      601 aagideeisk dqekvktals lsdklnqenl lrfyvpngfe tidpkkydyk neaerneaie
      661 kqkgehstsv fskngnkttt nlypvtrtdv eqqknnq
//
LOCUS       WP_010829600             300 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010829600
VERSION     WP_010829600.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..300
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33601
     Region          4..223
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mailtlekvs ksfgtnklld dlsfsveeqt ifgfigknga gktttmklil glikkdsgti
       61 rvngkeveyg qtttnqeigy ladvpffydy mtaseylifc geltgmpkqr ikektnells
      121 lvglsnekkr ikkfsrgmrq rlgiaqalln epkllicdep tsaldpvgrk eildilssvk
      181 eqttilfsth ilsdvvricd kvafldngki vlsgsvdelk kqtnasgfei vffskkereq
      241 feellpggmi rselriaypq kskeemlfam dllakyqlpv qsvqmeeptl eklflevvqs
//
LOCUS       WP_010829650             263 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Enterococcus].
ACCESSION   WP_010829650
VERSION     WP_010829650.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..263
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30364
     Region          1..256
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mndvlirikq gmedfspnhq eiakyilenp dcletctare laektysvps siisfskkig
       61 ysgfqemkfn ygnspfdcdn kerdflrpfq lvnkllntkv yndtvnilin anriyilafq
      121 msqvtaldfy lkvhkvdptk imffrsfdeq vrsipllnkd dvvlmisnsg ecqeiidcqk
      181 ylpegikkil vtngiestls efcthelsig cfekniltfk eiptdsrnal lylmdrlfkd
      241 mikqnyddal ekikksslff sni
//
LOCUS       WP_010829658             597 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Enterococcus faecium].
ACCESSION   WP_010829658
VERSION     WP_010829658.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..597
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70145
     Region          21..>592
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mnkteyprpq fvrkkwqnln gewlfafddq cvgmkekwgs hpkyydqkil vpfvyqcles
       61 gindqtpydi vwyyrefdin kqdgqrailh fgavdyyadi fvnghhvgrh sgghtsfsfd
      121 itdyltnekh qqlsvraedp hkdesiprgk qfwqekpegi wytnstgiwq tvwlevvedv
      181 yfshlrftpl fdegkvvael elnefreglt vdcciafkgr ivaklshsfv ekrviltvdl
      241 lqnyifrtnf hhegwswtpe tpnlfdvefv lkqkenikdv vssyfglrki hqengmiyln
      301 nkpyyqklil dqgywptglm taptddalak diqvakemgf ngcrkhqkte dprflywadk
      361 lgylvwgeca apavfthdss krlmqewtei vdrdynhpci vtwvpinesw gvpkisfdrq
      421 qqhfsqslyh ylhsldttrl visndgwamt etdicaihhy ghgeekeedk yqdfvttlst
      481 redllnrpst pwpifangfi yqgqpillte fggigfdfsg qkgwgytsvk neidfiknyr
      541 riinavyrsk rlwgfcytql tdveqeingl ltydrqpkcd lkeikkinns frtpyle
//
LOCUS       WP_010829691             483 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Enterococcus].
ACCESSION   WP_010829691
VERSION     WP_010829691.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 483)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..483
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55061
     Region          27..475
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mtkslsikqi faqankamll faviplllsi llysqqlliy qqtianiqka daialkvdqr
       61 vlesmwdlis gqvsvdefkk enileelrnd irqiksntnt lkeistldvs lrtidtledy
      121 qnelinnila kdfmdtneei inqvdsvtql lsdilqdfvr veidlaskkn ttlvrslill
      181 tivelgvlst iffyakknrr flerkvqepi nqliemseql ssgnlgfrlt lpetlelqtl
      241 tasmnkmaed lnqslrenal kqyhlaqsev rvlqaqitph fiynsldaii slieqdcfee
      301 altmthalsg ffrtslskgq dwiplekeis hindylvilk iryghmldyk idipetlfpv
      361 silkmilqpl ienavyhgtk yvrhkgfiri tackidemiq fkvtdngigi paeklaeirk
      421 elakgidsdf sigyglynvn krlllyygnd qkpitidsky regttvtlmi plspktiggn
      481 khv
//
LOCUS       WP_010829730             553 aa            linear   BCT 01-JAN-2025
DEFINITION  xylulokinase [Enterococcus faecium].
ACCESSION   WP_010829730
VERSION     WP_010829730.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..553
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60745
     Region          17..476
                     /region_name="ASKHA_NBD_FGGY_BaXK-like"
                     /note="nucleotide-binding domain (NBD) of Bifidobacterium
                     adolescentis xylulose kinase (XK) and similar proteins;
                     cd07809"
                     /db_xref="CDD:466809"
ORIGIN      
        1 mkevnvqsml dvidgrtslg iefgstrika vlidssftpi aagsyewenk lengiwtysl
       61 ediwkglrvs yrkmaaevfe iygenlttig sigfsammhg ylafdskeql lvpfrtwrnt
      121 iteeaerilt ekfqynipqr wsiahlyqsi lnkeehvkei nflttlagyv hwqltgakvl
      181 gvgdasgmfp idpstktyhq emknifgqli ekahvaidld hilpkvlvag eeagklsesg
      241 aylidptgnl rpgipvcppe gdagtgmvat nsvakrtgni sagtsafami vlekelenvh
      301 peidmvttps gelvgmvhtn ncssdinawv sifeeftnsl gmeisrdklf tvlfnkaleg
      361 dtdcggllsy gyfsgenitg vnegrplfvr tpgsrfdlan fmrihlasaf gamrigmdil
      421 ksenvqidrl vghggifktp evgqrilasa meapvtvmdt ageggawgia llaaymmdrh
      481 gkslenflae dvfgqdqgit itpsaeeiag yqifmrryre gidiektaih qlqekgvien
      541 agtterrsip sks
//
LOCUS       WP_010829547             564 aa            linear   BCT 01-JAN-2025
DEFINITION  class I mannose-6-phosphate isomerase [Enterococcus faecium].
ACCESSION   WP_010829547
VERSION     WP_010829547.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Jensen,S.O. and Reeves,P.R.
  TITLE     Domain organisation in phosphomannose isomerases (types I and II)
  JOURNAL   Biochim Biophys Acta 1382 (1), 5-7 (1998)
   PUBMED   9507048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..564
                     /product="class I mannose-6-phosphate isomerase"
                     /EC_number="5.3.1.8"
                     /GO_function="GO:0004476 - mannose-6-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009298 - GDP-mannose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64950
     Region          217..564
                     /region_name="ManA"
                     /note="Mannose-6-phosphate isomerase, class I
                     [Carbohydrate transport and metabolism]; COG1482"
                     /db_xref="CDD:441091"
ORIGIN      
        1 myekrpriil keqistftgy tkiinellkd kktkkialec ypgidsekva heiralkmed
       61 lfitttnqfy qssneikekl tevltddrvf grltdatfld flakeknesl nqadrvllig
      121 vgaaelidad mvvyanltkr niqlklkaga enwqadnaqe eflkkvkray yfewpaader
      181 kklvlpssqy lidlneentp kmiktkdyyn alrhfsnqpf rlvpyfepgi wggkwmqkkf
      241 dvgkeevnla wcfdgvpeen svifeigtvt fevpgndlvl fypvsilgek vfgrfgsdfp
      301 irfdyldtma ggnlslqvhp tldyayrkfg lkytqdesyy imdceedayi ylglkeevgt
      361 pdfiqalees ritgrldvek yinkikvkkh dhflipagti hcsgencvvl eisatpnrft
      421 fklwdwervd ldgiprpihi ehgkqvines mktnrvfsel vnqvvdltit enihiertgl
      481 hqlepiethr ltfcvpieqt tegsvnmlnl vegegivies taetfeplki nygetfiipe
      541 niknyvirpi vdketcivmk afik
//
LOCUS       WP_010829810             680 aa            linear   BCT 01-JAN-2025
DEFINITION  BglG family transcription antiterminator [Enterococcus faecium].
ACCESSION   WP_010829810
VERSION     WP_010829810.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 680)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467273
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..680
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=79237
     Region          8..506
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
     Region          539..676
                     /region_name="PTS_EIIA_2"
                     /note="Phosphoenolpyruvate-dependent sugar
                     phosphotransferase system, EIIA 2; pfam00359"
                     /db_xref="CDD:459780"
ORIGIN      
        1 mnkrireilk liiknpemkl stltseldlt rrqinyainq fneelktkni pliqrshsgn
       61 itvpveviqm isqpdydigd dqelvvltds erqalivmtl ianidyisld hlvdavdvsk
      121 ttvmedikrt epfirnyslt irynrmngyq lvgsehrilq llsdlvkrfp ifrremirrk
      181 laqdvseeei vhlihnmeqm lhlsysdesv dylqtsarfl vsrgikmsdk haffpddvtd
      241 tpefrmlmil vhekgwslsk symewftllf ltsnifeskt tqnydsdqel rklisqmven
      301 fqnqtlilid dredferril shlrpacfri rynlslgvys idslikdsnh ailidlmkel
      361 iipienwlnk afpndeldll syyfgyqlsn hnklnkqrqr avvvctngvm vsklvranme
      421 klfpeihfla slsvrdfykf eadydlvftt tplkssmlqf miepimtyqq qislryrvls
      481 dlgitkvdra mdelltiirk yanitnpvsl reelqyflik edgstpldnf kvlpsltyyl
      541 rpsyvqivee emsweravev acrpllehqi idsrfiadcl dqirqpgyag ylgmktciph
      601 ttvdkgvisd gvsilvckkp irfpngedvs lilplsffdl tkhlrainqi adiakddsli
      661 eqlliaddek tvyqllrqrs
//
LOCUS       WP_010829754             259 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Enterococcus].
ACCESSION   WP_010829754
VERSION     WP_010829754.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..259
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27935
     Region          4..238
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mkgllyffvi ilantigsvs gmgggviikp vldffaldsv vaisfystva vfvmsivstt
       61 rqiqngielk wkkviwlslg aiiggiigsa lfeellrlfs qdtvqlvqiv ltigtlvfaf
      121 lytrfnwesf elqssiwyvi cglvlgftas llgigggpin vsllmllfam pikdatvysi
      181 ctilfsqlsk ittialttgf arydlsillf vipaailggl igakasalfs prkvvvifqg
      241 viiivllini yngivviyk
//
LOCUS       WP_010829858             256 aa            linear   BCT 01-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010829858
VERSION     WP_010829858.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..256
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28501
     Region          1..256
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mstegliall ekkrnhlski enqvldyilt hmteissqti yevaqalfvs tatisrtakh
       61 lgyrgfqelk yaivqsvqse stesdsrsfq ditqqlianv qdsfqqmdea kvaemlkmie
      121 rantievfgv ggsfpictdf arkltflgkk ayarsdwdeq aaavknldgq dlaifvsytg
      181 etkgilayar vaqeqqvpmi slistkgstl eklstttlfa kgttryhqrv dlssriavic
      241 lfdtvllmya eakqpr
//
LOCUS       WP_010830163             295 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_010830163
VERSION     WP_010830163.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..295
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31173
     Region          1..292
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mivsaigqgm lwallglgif mtyrilnfpd mttegsfplg gavcvtaitt gvspfvatll
       61 gvgagmlagl vtgllftkgk ipiilagilv msglnsvilf vmkspnksll nqpkiqdvfq
      121 kmalpdyydt iflgisvlav vmilllfffn tslgqayiat gdneemarsi giqtdrmkil
      181 glvlsnglig lsgaliaqnd gyadvskgtg viviglasli igevlfgelt fgerlmaivv
      241 gsiiyqllil lgiklgfdtt ylkifsavil aiclmipqlk kalrlhgfsd kgetk
//
LOCUS       WP_010830201             324 aa            linear   BCT 01-JAN-2025
DEFINITION  ring-cleaving dioxygenase [Enterococcus faecalis].
ACCESSION   WP_010830201
VERSION     WP_010830201.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10327061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..324
                     /product="ring-cleaving dioxygenase"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36656
     Region          7..131
                     /region_name="VOC"
                     /note="vicinal oxygen chelate (VOC) family; cl14632"
                     /db_xref="CDD:472697"
     Region          158..314
                     /region_name="PcpA_C_like"
                     /note="C-terminal domain of Sphingobium chlorophenolicum
                     2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and
                     similar proteins; cd08347"
                     /db_xref="CDD:319935"
ORIGIN      
        1 mntqilglhh vtamtssaek iyhfftdilg lrlikktvnq ddietyhlff addagspgtd
       61 mtffdfpglp kgtkgtntif rtsfrvkdda aldywvsrfn eyaidhgeiq erfgkkylef
      121 edfdnqryql isdeknqgva agtpwkksnv psehaliglg pafvtvenye hlqlvltevl
      181 gfklidaegs fhlfevgegg ngasiivehr edlpaaqegy gnvhhlalrv adeealrfwi
      241 ekinrlefpn sgfverfyfk seyflaathv lfelatdgpg fledetyeha geklslppfl
      301 epkragieef vrpfdtsdan vqrn
//
LOCUS       WP_010830214             458 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Enterococcus faecalis].
ACCESSION   WP_010830214
VERSION     WP_010830214.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..458
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50379
     Region          7..453
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 megkkkfslt sailsvicvv fvaeaaapva aignsqffww iflliafllp yglisselgt
       61 tyigeggiyd wvtkayghrw garvswyywi nyplwlasla vmtpelltti tgikfstpmm
      121 iiveliftwi vvwisfypvs dsiwilngaa vikmvlavli gglglyvalt kgvaneftlk
      181 smlptfdlrs lsfisviifn llgfevictf addmenpkkq ipqaivaagl viaaiyifsa
      241 fgigvaiptd qistgsgmmv sfklltgste gwfimlmafl flltlfgnmi swslgvnnta
      301 cyaaengdmp kffekrskkn dmpigaalmn givasvvivl apilpnqdlf waffslnvvl
      361 fllsyipvfp afyklrkidp dtprpfkvng kpgflkvlvv lpmimiiisl iftavpldfs
      421 paalneklpi tigaiifilf geviiyvkki kkgtkeng
//
LOCUS       WP_010830252             350 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Enterococcus faecalis].
ACCESSION   WP_010830252
VERSION     WP_010830252.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..350
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40026
     Region          12..335
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mslyqkfiqn erlrrfcvla liifvlylsr smittilltf iftylavrlv hfvqrymkip
       61 tivivllnya lvvfliylai tkyvpvlvnq ttqminsvvd fyqsphtdtn qvlqfidqyl
      121 eksnllsqlq ngasmilryi qdigavglsf vmsfilsfff miekkqmadf sklflksdfd
      181 wffqdiyyfa nkfvntfgvv meaqffiavv ntvittlala iigftqlpsl aimifilslv
      241 pvagviisci plsfiaysqg glndviyila litivhlfes yvlnpkfmss ktelpifytf
      301 villvserlf gvwglivgip vftffldvlk vkpirglkrl pnvkknssae
//
LOCUS       WP_010830309             648 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Enterococcus faecalis].
ACCESSION   WP_010830309
VERSION     WP_010830309.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..648
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=71618
     Region          3..393
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
     Region          <532..625
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtkqnivvvg agyagvsatk flakkfkkdt dvtitlidrh syhtmmtelh evaggrvepe
       61 aiqydlqrlf srkknvklvt dtvtgidken kvvktlagsy pfdqlilgmg gepndfgtpg
      121 vkengftlws fddavkirhh ieatvakaai epdaevrkam ltfvvcgsgf tgiemvgeli
      181 dwkdrlakda kidpdeialm vveamptiln mlsrndaaka erylekknvq lllnspivev
      241 aadhiklkdg sevpthtliw tagvkatsda adfgleaarg srlvaneymq akgyedkniy
      301 iigdlvyyee tpntptpqiv qaaeqtghta aanivadikg gekhafkgny qgfmvsigak
      361 wgvanlfdki hlsgflaiim khivnlkyff dirsgyymfq yimheifhik ddrsvarght
      421 srygnvlwsv plrvfygmvw lvesmkkivg ngdylkpstw fgdgswftdk vvfpfpwlqe
      481 qvttgasqat etattaasga adaaasggad aatqaahfgl syaygetpmq vfdhmpkwfe
      541 svmkfmmpnq evalfmqkfm tivevciala liaglftwls saatigltia fclsgmfywv
      601 niwfifvafa lmngsgravg ldrwvipwiq rklgkawygt pkaryggk
//
LOCUS       WP_010830325             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: single-stranded DNA-binding protein [Bacillota].
ACCESSION   WP_010830325
VERSION     WP_010830325.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..158
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=17420
     Region          1..106
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 miqlsaigrl tkgaelrttt ngksvanvtl ackrkrpdtn gnvpttfiqc vlwgkpaqvf
       61 akytqkgalv gvngelqtrs yddqqgvthy vtelvvedfe flesketvqk reekqhavpq
      121 gqstptvneq pamnqaptqq nvyqqpsmng lseygynq
//
LOCUS       WP_010830340             477 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Enterococcus faecalis].
ACCESSION   WP_010830340
VERSION     WP_010830340.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..477
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54952
     Region          <277..466
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 myylsyficl lfpelsfydw dkttilvtil ptgvvyilvk ereiilsekf llafcilvys
       61 affflilevi givlwksfil tilfalvcyl thlsinairs nkvkqlknnf rnlnneklev
      121 ldqvtysqfl nnvsellldk leeltasqrl avfveskegc yllcqkgetv fnslkkeihs
      181 lkkqkqkikf rkkeytcipi iisgytvwlf fenndndidl ksihktveqh gtliitvrll
      241 hlnsksyvkd pievcqllri klfnsmeiek knyanylhdn ilqsviglht lisnlsgdvm
      301 vtdlineefs klvssirsei fntypstlyh ltfkenlqil iddfnkkypk tefildysie
      361 eiipqhviap lyrivkelne nigkhadaei gkvtveidna eiqliveddg vgvgnilefe
      421 ksliqtndhi gllsikndin wlngsfkmls lpgpnsgtkv wvtipcmkge qyenits
//
LOCUS       WP_010830344             321 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Enterococcus].
ACCESSION   WP_010830344
VERSION     WP_010830344.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..321
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35685
     Region          1..248
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mdkirygims taqivprfva glresaqaev rgiasrrlen aqkmakelai pvaygsyeel
       61 ckdetidiiy iptynqghys aaklalsqgk pvllekpftl ntaeaeelfa iaqeqgvflm
      121 eaqksvflpi tqkvkatiqe grlgeilwvq svtaypnvdh ipwfysreag ggalhgsgsy
      181 plqylqyvlg keiqtvtgta tyqqgatdsq cnlalkfaeg tlgnilinvg lkipsemtic
      241 gtkgqivipn fwktdcayyt daqgntvkws eqftseftye inhvnqclqd kkltspvmtk
      301 eltiatvkiv esfyqewfdn e
//
LOCUS       WP_010830434             250 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterococcus faecalis].
ACCESSION   WP_010830434
VERSION     WP_010830434.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..250
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27738
     Region          1..247
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkvisllnlk ggvgktttai nlakglsnng kkvllidtdm qanatsifle eemqqdsyrs
       61 fsdllsdeen kiekyiypin nnlkmigadl siadtelnlr nsfgrdtani lknnlkniea
      121 efdyciidca ptinlitmnt iissdeviip ikidkfalkg yettyknisk vissygldtk
      181 ikvlftmvnr nnidkgiies ipmahyesti rfqakpites sfnssalids gdsgvkddyi
      241 lfleefeggk
//
LOCUS       WP_010830607             336 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar kinase [Enterococcus faecalis].
ACCESSION   WP_010830607
VERSION     WP_010830607.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..336
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37937
     Region          2..315
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(33..34,37,88,103,106,136,169,275,278,314)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(241,252,266,275..277,280,302,306)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mkiaafgevm lrftppeylm leqteqlrmn fvgtgvnlla nlahfqleta litklpanrl
       61 geagkaalrk lgisdqwvge kgdhigsffa emgygirptq vtyqnrhqsa fgiseakdyd
      121 feaflaevdm vhicgislsl tektrdaali laqkahayqk kvcfdfnyrp slntansalf
      181 mrqqyerilp ycdivfgsrr dlvellgfip redlegeaqe teliqrfmsq ynlewfagtt
      241 rshsqnqnyl sgylytqney qqsekrplln ldrigagdsy aagilygysq nwslekavtf
      301 atvngvlaht iqgdiplttv kqvnhvlehp nidlir
//
LOCUS       WP_010830514             901 aa            linear   BCT 01-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Enterococcus faecalis].
ACCESSION   WP_010830514
VERSION     WP_010830514.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 901)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..901
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=97007
     Region          10..899
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mseekktqls eafyaqddtv vlekmnttsd glsaqeaqkr letygenvld egkkkslavk
       61 ffeqfkdfmi ivllaaavis avfshdvvds iiilvvviln aifgviqeak aeqaiealke
      121 msspnanvrr dghvitvksd elvpgdivll eagdvvpadl rlleanslki eeaaltgesv
      181 pvekevtile gtdigigdri nmaysnsnvt ygrglgvvvg tgmntevgki agmlaseqet
      241 etplkqnlnq lgkmltiail viaavmfvvg mmngrswidm lltsislava aipeglpaiv
      301 tiilalgtqk makknaivrk lpavetlgst diicsdktgt ltlnqmtvea lytdgqvlsa
      361 steipadnma lkimnftndt kiaqdgslig dptetalvqf gldhafnvte kvaaeprvae
      421 ipfdsdrklm ttvhelktgg flvsvkgapd ellkrcteil sngetsplde tkrqeilktn
      481 tslakqalrv lgmaykyvet ipaemsselv ekdltfaglv gmidperkea adavkvakea
      541 girpimitgd hrdtaeaiaa rlgiikegdd davitgaeln elsdekfaqv vghysvyarv
      601 spehkvrivk awqqegkvva mtgdgvndap alkaadigig mgitgtevsk gasdmvladd
      661 nfstiivave egrkvfsniq ktiqyllsan lgevltlfia tmlnwdtllp vhllwinlvt
      721 dtfpaialgv epaerdvmsh eprgkksnff sggvlssvvy qgitqgaltl ivykmsimfp
      781 ahtaantnls aqalydlqhg daltmafatl gliqlfhafn vksiyqsifk vglfrnksfn
      841 ygilvsflll aativipgfn dlfsvthlda yqwaivagts faiipiveiv kffqrkagkg
      901 a
//
LOCUS       WP_010830521             272 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus faecalis].
ACCESSION   WP_010830521
VERSION     WP_010830521.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 272)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..272
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30156
     Region          1..270
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkrtlwlvi tvavavlilg acgnkksdds vlkvgaspvp haeilehvkp llekegvkle
       61 vttytdyvlp nkalesgdid anyfqhvpff neavkendyd fvnagaihle pvglyskkyk
      121 slqeipddst iyvsssvsdw prvltileda glitlkegvd rttatfddid kntkklkfnh
      181 esdpaimttl ydneegaavl insnfavdqg lnpkkdaial ekesspyani iavrkedenn
      241 envkklvkvl rskevqdwit kkwngaivpv ne
//
LOCUS       WP_010830655             335 aa            linear   BCT 01-JAN-2025
DEFINITION  XdhC family protein [Enterococcus faecalis].
ACCESSION   WP_010830655
VERSION     WP_010830655.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..335
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37223
     Region          2..335
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 mrevfqrlkq ailekqdtml ltigtssgst prsqgarmlv saegriagtv gggavefqae
       61 qvakklllek enaqrqfila pnniadlgmv cggnvtiffh ylswetpflk elcesiethf
      121 qnnqqgwlmt eldqnnlgkv sfysetgeli gstswegels llpkgihceq keeitfltea
      181 ilqvgkvyif gsghvaralv pilnylsfyc vvvddrpefl taqafpqaee lrviplenla
      241 afieitaddy givitrghnf dfivakklle tpakyigvmg skhkiasqvr rlkevgytmt
      301 eierifmpig ldiaaetpee laisiageli qqryq
//
LOCUS       WP_010830645             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Enterococcus faecalis].
ACCESSION   WP_010830645
VERSION     WP_010830645.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..277
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30305
     Region          1..271
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkfskligl igvlaftiag casgsakdtk tetvklgvvg tkndewesvk erlkkknidl
       61 qlveftdytq pnaalaekei dlnafqhqif ldnynkehgt klvsigntvn aplgiyankl
      121 kditkikdgg eiaipndptn ggralillqt aglikvdpak qqlptvsdit enkrqlkite
      181 ldatqtaral qdvdasvins gmavdagytp dkdaifletv nekakpyvni vvareedqen
      241 klyqkvveey qqeetkkvia etskganvpa wetfgkk
//
LOCUS       WP_010830717             435 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PTS sugar transporter subunit IIC [Enterococcus].
ACCESSION   WP_010830717
VERSION     WP_010830717.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..435
                     /product="PTS sugar transporter subunit IIC"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=47135
     Region          1..431
                     /region_name="CelB"
                     /note="Phosphotransferase system cellobiose-specific
                     component IIC [Carbohydrate transport and metabolism];
                     COG1455"
                     /db_xref="CDD:441064"
ORIGIN      
        1 mdkltnwveq avvpkvsrit slryfqalrn gffaimplti igsifmlitd fpvagygdfm
       61 agifgadwad mispayratf nmmgiifagt msyklaesye mdrltslilg ivayvvvlpk
      121 tvttesgevv tkvlsfdwlg tqgvitaiim silsveltrf cikkklvikm pdsvpsmvsq
      181 afsalipgif vvavalling iglsfadsfp qliyaviqap lqgligtpfa iiivaglngl
      241 fwwfgihptv insmlypily anadknqsla elgqltaqsg nfgtvqmldq fatiggagct
      301 iglaiamaiv ghssrmkams kisfvpaffn ineplifglp vifnplllip iavapivsvl
      361 iaflsmkigf mpmftniqap watpflfsgf lvgkwqgavt qvlavaasvv iyypfvkald
      421 rqyqkeeahe vpetl
//
LOCUS       WP_010830875             438 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Y-family DNA polymerase [Bacilli].
ACCESSION   WP_010830875
VERSION     WP_010830875.1
KEYWORDS    RefSeq.
SOURCE      Bacilli
  ORGANISM  Bacilli
            Bacteria; Bacillati; Bacillota.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10109377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Bacilli"
                     /db_xref="taxon:91061"
     Protein         1..438
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=48881
     Region          14..364
                     /region_name="PolY_Pol_V_umuC"
                     /note="umuC subunit of DNA Polymerase V; cd01700"
                     /db_xref="CDD:176454"
     Site            order(17..18,21..22,57,60,116..117,172)
                     /site_type="active"
                     /db_xref="CDD:176454"
     Site            order(114,117,201..207,236,263..268,295,324..328,330)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176454"
ORIGIN      
        1 mkfdyskepr rdvlcidvks fyasvecver gldplktmli vmsgadnagg lvlaaspmak
       61 kvlgisnvtr kdevpdhpdl iivpprmnly mkrnseinnl lkrfvadedh svfsvdesfi
      121 ditaslkyfn cdttyrlaki iqrviynhmg lyvtigigdn pllaklaldn eakntpgfva
      181 ewryenveek vwaispitef cgigkrmaar lkksgiesiy dlaradpyll khrfgvmglq
      241 lyahswgidr sflgekrqvv keksfgnsqv lpkdyarkdq ielvlkelsd qvasrlrnan
      301 cqtecvsifv gyskgqvdgl grsgwrkqlk iarsnntkvl tehvlklfre nyvpgmdirn
      361 lgvsfgklvw attlqldifs ppeeqiintq ldflidkirr kfgfksliha sslldgatav
      421 nrsglvggha ggnvglgg
//
LOCUS       WP_010830841             520 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecalis].
ACCESSION   WP_010830841
VERSION     WP_010830841.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..520
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=59863
     Region          26..433
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mteknimvip arkrvgstaa kekikklrva aycrvstete eqnssyevqv shytefikkn
       61 newefagifa ddgisgtntk khdefnrmia ecmdgnidmv itksisrfar ntldclqyir
      121 qlkdknisvy fekeninttd akgevlltim aslaqqesqs lsqnvklglq yryqqgkvqv
      181 nhkrfmgytk dedgnltivp eeaeiikriy reylegqslv gigralekdg iltaagkprw
      241 rpesvkkilq nekyigdall qktvtvdflt kkrvkneghv pqyyvenshe aiipkelflq
      301 aqeeihrrsn iytgegknkr iysskyalsa itfcgdcgdi yrrvywnihg rkefvwrcvt
      361 rieqgpevck nrtvkedely gavmtainkl laggnnmikt leenihavig etteyqisei
      421 nnsleekqke liklankgqd ydhladeide lrdkrqillv edaslsgene rineliefir
      481 knkfrtleyd dklvrkiiqs vtvyeghfvi afksgiemei
//
LOCUS       WP_010830862             204 aa            linear   BCT 01-JAN-2025
DEFINITION  recombinase family protein [Enterococcus faecalis].
ACCESSION   WP_010830862
VERSION     WP_010830862.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..204
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23436
     Region          2..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(7,9,65..66,69)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            9
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(64,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(70,75..76,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93..95,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..198
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(148..150,190..191,193..195)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mkiayirvss idqneqrqie emekfgaeki fiekqsgati shrpifqeal dfvreqdifi
       61 veaidrlgrn ydeiidsvny lkkknvrlii tslpimaeai gnplldkfik dliiqilami
      121 aeqerskskr rqaqgikiak angvykgrpk lysadtkdpq rrlvyksive dlkkgvaiak
      181 iakdynvtrq tiyrikkdid qliv
//
LOCUS       WP_010830919             166 aa            linear   BCT 01-JAN-2025
DEFINITION  J domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010830919
VERSION     WP_010830919.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..166
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=19454
     Region          9..>50
                     /region_name="DnaJ"
                     /note="DnaJ-class molecular chaperone with C-terminal Zn
                     finger domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0484"
                     /db_xref="CDD:440252"
ORIGIN      
        1 mkfikdvttl eelkrvykkl alkyhpdmgg tdkemaqinn eyealfdklk nthknkegey
       61 yqkettetpq ewqeiihkll tlkmenvsie vigaflwvsg ntktykeelk alnmkwsnnk
      121 kswylapdgy kkrskkkynm sdirnmygsq vvkeeqakqk tltata
//
LOCUS       WP_010830877             283 aa            linear   BCT 01-JAN-2025
DEFINITION  ParA family protein [Enterococcus faecalis].
ACCESSION   WP_010830877
VERSION     WP_010830877.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..283
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32549
     Region          3..278
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 maakkyvign fkggvgkstc aqmfgfesak fkelktliid ldmqgntsdv mnlthmnfsk
       61 eegggegeli eytntitdvl isnvdphdsi ykiidnlyil padmsfelyd dwikdrfpns
      121 idkfkymeek lsplfndfdv iyldvppsis iysksamyia dwaivvlqtq vksmrnamqy
      181 leymdfftne fdtnlkvagv vpfmlesgds vdkemyqqaq eiygehlikn vvlknarlkr
      241 ydgsgittel tkkgklkqwd kkchelfini ldeleehehw yeg
//
LOCUS       WP_010831041             213 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Enterococcus].
ACCESSION   WP_010831041
VERSION     WP_010831041.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..213
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=24643
     Region          3..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,65..66,69)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(64,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(70,75..76,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94..96,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..195
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(148..150,190..191,193..195)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mtkigyirvs smdqnldrql lemeklqvek ifqekisgkd tnrpefqkll ryaregdilf
       61 fdsldrlgrd yddiketvly frknnievnf ldapflnfnt gndlldkamf dmflsllsyi
      121 aqnerekird rqrqgiaaak akgiykgrpa vytpdspdpq kqviyhnivs mltadepvak
      181 iakqnhvsre tvykikrklk ssvsesdskp ilk
//
LOCUS       WP_010830934             764 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 65 protein [Enterococcus faecalis].
ACCESSION   WP_010830934
VERSION     WP_010830934.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..764
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87976
     Region          4..757
                     /region_name="PRK13807"
                     /note="maltose phosphorylase; Provisional"
                     /db_xref="CDD:237517"
ORIGIN      
        1 mkqikrlfqi dpwkirtthl dkenlrlqes ltsigngymg mrgnfeehys gdhhqgtyla
       61 gvwypdktrv gwwkngypey fgkvinainf iamdlqidgq tidlattpye dfsleldmqn
      121 gvlsrqftiq tpknkvrfsf erflslekke aayihltiem legtgtitlh skldgdvqne
      181 dsnyeehfwe eiaietqetl gfvttktipn nfeierftvt agmrhfidga svvptytqqp
      241 laltaeltvs lnegettait kevlvvtsrd vpetqqitrv nelfsemttl ypeakagqaa
      301 awakrwqlad vviegddeaq qgirfnlfql fstyygeddr lnigpkgftg ekyggatywd
      361 teayavplyl alakpevtkn llkyrhnqlp qaihnaqqqg lkgalypmvt ftgvechnew
      421 eitfeeihrn gaiayaiyny vnytgdqdyl kdaglevlva iarfwadrvh fsqrhkqymi
      481 hgvtgpneye nninnnwytn tiaawvlryt resylkfqee ttlkiaddel akwadivenm
      541 yfpvdnelgi fvqhdtfldk dlmpvsdlpl selplnqhws wdkilrscfi kqadvlqgiy
      601 ffndafslee krrnfnfyep mtvhesslsp sihavlaael gmkekavemy qrtarldldn
      661 ynndtedglh itsmtgswla ivqgfaqmkt dhqqlkfapf lpatwtaysf hinyrnrllf
      721 vevaadqvaf tlldgpaipl tvydqkytlk drlvlpirke evhv
//
LOCUS       WP_010831123             257 aa            linear   BCT 01-JAN-2025
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Nocardioides sp. CF8].
ACCESSION   WP_010831123
VERSION     WP_010831123.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..257
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27554
     Region          15..232
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mpttltlaah leglraalla lvryvdragl aapvpttpdw tvrrlvaheg mvhrwaaavv
       61 tgseqapdrw eqegreapdp lewlrdgaie vvtaisqapd dldtlvflad apaprhfwar
      121 rqchettiha idalsaalgr ypvagdvtwi stevaldgid ellggflprp vtrlrseagq
      181 riavrpdegs ggwlvelsaa ppvttrftga apeadvdltg savalyltlw nrsdeatpaa
      241 gpgggwdewr dsaqvvw
//
LOCUS       WP_010831043             274 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Enterococcus].
ACCESSION   WP_010831043
VERSION     WP_010831043.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..274
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31439
     Region          2..267
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mtkiittgnl kggvgkttna vllsytlakk gyktclldfd mqadatdlvf ttmefvykqd
       61 isdkfeytfy saikkgqprk siihvtenwd lipsdtdlvn yqdflddnlk tkkekdffln
      121 silngikesy dyiiidvppt iniytdsaiv asdyilivlq tqmksyrkav ryanylsqlr
      181 dtydlnvkal gilpvlmenn seydeqiinq akeefgieni fknpikqlrr ikrfdwtgit
      241 nnltdahdnk vhslydsvan elitrigkde indk
//
LOCUS       WP_010831128             332 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Nocardioides sp. CF8].
ACCESSION   WP_010831128
VERSION     WP_010831128.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10606006
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..332
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=35971
     Region          117..263
                     /region_name="Methyltransf_23"
                     /note="Methyltransferase domain; pfam13489"
                     /db_xref="CDD:404385"
     Site            order(133..139,156..157,174..176,189)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 msdtsacqfc tstsaagpve vaemmfgwde rftyvtcssc gsvsqvdvpd dlgryypqdy
       61 ysvdvdpaha lgrpgvrqfa gqvaqsvlfg ssrrasaaqr vvrmrqfysy vsvlhsiaaa
      121 glplgkqtrv ldvgcgsgim iyalalagvr kpvgvdpfap adrhfdngaq llrrdladve
      181 dtfdlimfhh slehvpdpat slklamtkla pggqilvrmp tvsseayeiy gadyygldap
      241 rhvsipsrag vdalaervgl rvvktrddst asqfwaseqv rrgiplmapn shmvseadsp
      301 fskaeiaawa krslelness rgdqsawvle rv
//
LOCUS       WP_010831152             917 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Nocardioides sp. CF8].
ACCESSION   WP_010831152
VERSION     WP_010831152.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..917
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=99343
     Region          211..887
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 msfvpvtgpa tfraaepprd glvefsderr tvalpirgal pvltkahnrd dlhpsvalls
       61 gaallgmrlv aagkfgpdps glswqvaale radedritql aaarshdgld aataegivra
      121 vldavadamp raapiatrrp pvaggqagpr aprvdpdftr rlqervarar arssddrpql
      181 vsialriead edelvagsvr ivlqvhasdn aahvcdaavl wtesgldash gfgdrartha
      241 sialraaada wpvlerflel rvpdeltldt delvslldsg vtalkeagvd vlwprhldrd
      301 vtakveltea rkgpqreeal qtglfgpeal fgfqwqlalh gdalseeemd qlagaatpii
      361 kirdnwtvvd pamlkrakrr mirtvqpaaa laatltnvvs veeveheaiv gasllkvrdr
      421 lqaagkgepv avppglaatl rdyqrqgltw maeltdlglg acladdmglg ktvqvialhl
      481 hrgngptlvv cpasllgnwe aeirkfapgv pvrrfhgsar sleglgsdsl aslaaqpaer
      541 gfvlttygtm rrdaealagv gwdlvvadea qhvknaqsst sralrtipsa arvaltgtpv
      601 ennltelwai ldwaipgllg srnafrkvwa apieagvdpa vtrrfadlig pfllrrrksd
      661 pgiapelppk tetdhllglt reqvvlyety vrdcmrriee adeetrrglv lklltglkqi
      721 cnhpahflkq tnpklagrse kldlldelig tvlaedgavl lftqyvamar lleqhlskag
      781 vthqflhggt pvaerermva rfqegetpvf llslkaggtg lnltradhvi hvdrwwnpav
      841 edqatdrayr igqtkpvqvh rfitegtiee kiaellarkr sladsvlarg etaltelsnd
      901 dlrdlvtlrr tpgaedd
//
LOCUS       WP_010831166             405 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Nocardioides].
ACCESSION   WP_010831166
VERSION     WP_010831166.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 405)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 405)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 405)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 405)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10588955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..405
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43053
     Region          18..205
                     /region_name="AAA_16"
                     /note="AAA ATPase domain; pfam13191"
                     /db_xref="CDD:433025"
ORIGIN      
        1 mdpirnpyap gagqrppela grdeqlaafd vvlervvkgr perslvltgl rgvgktvlln
       61 alrsaavrrr wgtgklearp dqglrrplss alhqavrelg htdadsvdhv lgvikafahr
      121 dagagaklkd qwspgidaav vrgradsgdi eidlvelftd vgglaadvgk giaifidemq
      181 dlgpddvsal caacheisqs glpvivvgag lphlpavlsa sksyserlfr yqridrlard
      241 aadlaltapa qdedaaftad alaamyaatg gypyfiqayg kavwdraprs pitlddvlva
      301 tpeaeselav gffgsryera tpgereylra madvaaasea tppvelvetq gvptadvaaa
      361 ldkkpqslsp ardallkkgl iysgergria ftvphfgryl rehvg
//
LOCUS       WP_010831255             299 aa            linear   BCT 01-JAN-2025
DEFINITION  sugar ABC transporter permease [Nocardioides sp. CF8].
ACCESSION   WP_010831255
VERSION     WP_010831255.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..299
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32445
     Region          27..299
                     /region_name="MalG"
                     /note="ABC-type maltose transport system, permease
                     component MalG [Carbohydrate transport and metabolism];
                     COG3833"
                     /db_xref="CDD:443045"
ORIGIN      
        1 mssmppatat etpaavtppr vrgredrsll asvalhgtli vatfialfpv lwvmlssikp
       61 aseirrteis lfasptleny rkvlfdtnfp qwflnsviva aftmvigiam sasagyalsr
      121 fnfpgkrglm wvflltqmfp vailivpiyt imanlglidt kaslviayct vavpfcawml
      181 rgyfdtipre ldeaaaldgl gpfgtfyrvi lplarpglav tafytfltaw gevayaiafm
      241 qtddhytlga glqqfvpqfs prwdqltaga vlitipaaiv fffaqkhlva gltaggtkg
//
LOCUS       WP_010831292             266 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Nocardioides].
ACCESSION   WP_010831292
VERSION     WP_010831292.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..266
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27463
     Region          12..190
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16278"
                     /db_xref="CDD:293836"
     Site            order(69,71,73..74,124..125,143,186)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293836"
ORIGIN      
        1 mtwdggtfgs satcvlapna dimtldgtnt wvlssgsqsl vidpgpsies hlaavsavgq
       61 dvvgvllthh hldhseaare fasahgcgvr aldpayrlgs eglgagdvvt vgslevhvva
      121 tpghtadsls fvvpsesavl tgdtvlgrgt tvvahpdgsl gaylssldrl halcseqgit
      181 siwpghgpvi dnalgaldyy iahrrtrldq vrdavatlta qphpegiaad elprrvvelv
      241 yddvdpvlwg aaelsvraql aylass
//
LOCUS       WP_010831335             518 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Nocardioides].
ACCESSION   WP_010831335
VERSION     WP_010831335.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..518
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54806
     Region          110..>288
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
     Region          417..514
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mkklvvvllv falvvttfya fasafirsdd ggprsdrpgs rssspaaepd easapspelr
       61 dfygqaldwe scesdvecat levpldyaep tgetieiall kvpargdsqg alvvnpggpg
      121 apgtdyaaaa nrvfrepllr afdivgfdpr gtgesapvdc ltddqldtyl ssdpspddaa
      181 eeqefaslir gfgrgcaels gdavnhvsti eaardmdvlr aalgeetlty lgasygtklg
      241 atyaelfpdr vgrlvldgav dvsldnrqlg leqaagfeta lrayiqncvd ttdscflges
      301 vdaglatisg lladveaspl ptgddrelqi gnafygivtp lynrdywfll saalrsaldg
      361 sgtalmelad lyasrgpegy tdnsseaifa inclddpssv pfrkvaaelp ayeeasptfg
      421 sifawsltsc raskarttea pieirgegaa pilvvgttrd patpmkwaea laeqldsgvl
      481 lrrdgdghta ynsgnecidt aiesylldgd vpkdqtdc
//
LOCUS       WP_010831358             218 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Nocardioides sp. CF8].
ACCESSION   WP_010831358
VERSION     WP_010831358.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..218
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22133
     Region          4..>178
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mnkpvylvlg agpglglata rrfadtghtv vlvgqtddqm eplaaglreq gaiaeglgad
       61 ltdpaavtal vagvverhgr idvlhfnpsa wreadvlhlt pdqlfedlal gvapllpavq
      121 aaveampaga rllvtgsmaa dqpnpaapsl gvqkaavrnl vtsldatlsg rgiravavqv
      181 ngslakegpf appavsaalh aatirsddew tahvgydg
//
LOCUS       WP_010831438             859 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ATP-dependent Clp protease ATP-binding subunit
            [Nocardioides].
ACCESSION   WP_010831438
VERSION     WP_010831438.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..859
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94798
     Region          1..808
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mferftdrar rvvvlaqeea rmlshnyigt ehillglihe gegvaakale sldisleavr
       61 aqveeiigqg qqapsghipf tprakkvlel slrealqlgh syigtehill gliregegva
      121 aqvlqklgad lnrvrqqviq llsgfqgkes aasgasqtgs gaeapssslv ldqfgrnltq
      181 aaregkldpv igreqeierv mqilsrrtkn npvligepgv gkttivegla qdivkgnvpe
      241 tlkdkhiytl dlgalvagsr yrgdfeerlk kvlkeirtrg divlfideih tlvgagaaeg
      301 aidaasilkp mlargelqti gattldeyrk ylekdaaler rfqpiqvaep siahtiemlk
      361 glrdryeahh rvtitdealv saatladryi sdrflpdkai dlideagsrl rirrmtapad
      421 lreyddkiad vrkrkeaaid gqdfeaaarl rdeekqliar kaeretqwrs gdmdevaevd
      481 eeliaevlav atgipivkls eeessrllnm eeelhkrvig qeeavkalsr airrtraglk
      541 dpkrpggsfi fagpsgvgkt wlsktladfl fgdedsliql dmsefsekht vsrlfgsppg
      601 yvgyeeggql tekvrrkpfs vvlfdeveka hpdifnsllq ileegrltds qgrvvdfknt
      661 viimttnlgt rdiskgqnlg fqqsgdgsty drmktkvaee lkqhfkpefl nrvdeiivfp
      721 plsqdqivsm vdnmiagvel rlkdrdmqle ltqpaknlla ergfdpvlga rplrrtiqre
      781 iedvmaekml fgeigpgqiv lvdiegegps atftfkgqkv sampdmppfe tadvvgdpes
      841 plegpddsag pvdvekssd
//
LOCUS       WP_010831587             416 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Nocardioides allogilvus].
ACCESSION   WP_010831587
VERSION     WP_010831587.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides allogilvus
  ORGANISM  Nocardioides allogilvus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Nocardioides allogilvus"
                     /db_xref="taxon:2072017"
     Protein         1..416
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=45407
     Region          1..411
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 magylqriad relverlgyi gavliegpka cgktatatqh aetvirlded qaarrlmtla
       61 perlfdnptp ilfdewqvep aiwnkvrrqv ddregkglfi ltgsatptdd asrhsgagrf
      121 svmkmrpmsl fesghsngem slakliagdr qtglgthltf dellkrivig gwpelidade
      181 tgarrwlrdy ltnivevdiq klgsrrdpsn lrrlleslgr svaqatkave lakdvggedg
      241 piaketltay ltalerlhll dnspawlphm rsrarlrtap vryfidpslg paalglgtsd
      301 lrhdfnglgl hyealvirdl riyaqpldar veswrdadgh evdaivsvgp nkwgafevkl
      361 spdavddaaa allrfkakvd tsrhgepacl gvitstgagg lredgvhvip igclgp
//
LOCUS       WP_010831668             226 aa            linear   BCT 01-JAN-2025
DEFINITION  SRPBCC family protein [Nocardioides sp. CF8].
ACCESSION   WP_010831668
VERSION     WP_010831668.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..226
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=23334
     Region          3..147
                     /region_name="SRPBCC_5"
                     /note="Ligand-binding SRPBCC domain of an uncharacterized
                     subfamily of proteins; cd07823"
                     /db_xref="CDD:176865"
     Site            order(3,5,7,16..18,20..21,33,41,43,45,47,62,64,74,76,
                     91..92,94,96,106,108,110,112,126..130,132..134,136..138,
                     141)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176865"
ORIGIN      
        1 melshrftvp tgveetwahf ediasvaecf pgaqvtsaeg dtfagtvkvk lgpialvysg
       61 sgtfvekdes akrfvvdakg kdkrgngtag ahvtvtmtda ggstdvsvdt dlaitgkpaq
      121 fgrgvmqdvs dkllgqfvdc learltgpae sagavpggap atvpdgetva epppgttppr
      181 ptpirppele aldlgsavlp vlaksywkqa lgalaalalv wrrirr
//
LOCUS       WP_010831665             154 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [Nocardioides].
ACCESSION   WP_010831665
VERSION     WP_010831665.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..154
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16256
     Region          1..154
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 marieltvdg akvsddvepr mllvqylrek lgktgtvigc dtsncgactv hldgrsvksc
       61 nvlavqangr evttieglad gdqlhpvqea frechglqcg fctpgmimqa vdllgenpsp
      121 teaevregme gnlcrctgyh nivksvlhaa ggak
//
LOCUS       WP_010831675             240 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010831675
VERSION     WP_010831675.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..240
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26183
     Region          37..236
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mdtvdvrlae sglkhvqvre yvrsllaeap pgaaapsere lvarfgvarm tvrqaldvlv
       61 tegllervpg rgtfvahprr rvgrlssyte dmkvrgllpe sqtlvarreq agpgvarald
      121 ispgdavihw krlrradqqv vciedaylne vllpgflqsg mptslydald erglrptwae
      181 daisadgata deaallelqp gapvlhlsrr alcgdkvvnv srtafrpdrf tmfvqlgdlv
//
LOCUS       WP_010831698             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: elongation factor Tu [Nocardioides].
ACCESSION   WP_010831698
VERSION     WP_010831698.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  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 :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     gene            1..397
                     /gene="tuf"
     Protein         1..397
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=43612
     Region          1..397
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makakfertk phvnigtigh idhgkttlta aitkvlhday ptlneasafd qidkapeerq
       61 rgitisiahv eyqtesrhya hvdcpghady iknmitgaaq mdgailvvaa tdgpmpqtre
      121 hvllarqvgv palvvalnkc dmvddeelie lvemevrell seyefdgdni pvvrvaahpa
      181 lmgdekwgqs vlelmaavde siptparetd kpflmpvedv ftitgrgtvi tgriergivk
      241 vneeveiigi rdtaqkstvt gvemfrklld egqagenvgl llrgtkredi ergmvvikpg
      301 tttphtnfea nvyilskdeg grhtpffnny rpqfyfrttd vtgvvtlpeg temvmpgdnt
      361 emsveliqpi amdeglrfai reggrtvgag rvtkitk
//
LOCUS       WP_010831699             281 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: phosphotransferase family protein [Nocardioides].
ACCESSION   WP_010831699
VERSION     WP_010831699.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..281
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=30369
     Region          3..249
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 myaaaitwar shldhdvtev vpllggrtsa mlalhdrtgr asvlrlitqe pwrshghdlv
       61 tresvtqrtl aatdipapls latdptgeat ghpahlmslv pgtsdearfd easlaavaal
      121 lasihgvvta paprdfqswa wpakwvvppw asrpalwraa fdllateppa feptflhrdf
      181 gphnllwadd titgivdwve tstgpawldv ahcssnlalr hgspagerfa aaytqvtgve
      241 repywdvmdi vgflpppggt imfddpaqla rleehlawal g
//
LOCUS       WP_010831734             416 aa            linear   BCT 01-JAN-2025
DEFINITION  FHA domain-containing protein [Nocardioides sp. CF8].
ACCESSION   WP_010831734
VERSION     WP_010831734.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..416
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=43746
     Region          309..411
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 matqwgeeav vvvetryaag dgvllgagdh wvlmtdpgdd dvldeiwdvv sgarasdssv
       61 teqvlaivdk afageppgla ivdlaqggst svsrgrghvr vsgadrilsl dggadpaavp
      121 rlrrlaggvv aasratlspl ahrvspprvh aspapiaggp lidgipdeil aatgpdgppp
      181 rprrrptdea ghdtgplgdt tepgpgfver isegahttiq patadvasgl ldphvddadd
      241 dhdgstvhrp elashlrhgt sdtvlavscq tghltpadsk vcrvcrqpva pqeprrvprp
      301 vlgglrlptg evvpldrgvv lgrkpapleg stdwphlvhl psdhtfvsrm hlhieldgwn
      361 vlardldsrg gtmltmpgre permrareay vlepgcsldl aevyevrfev gpvvpr
//
LOCUS       WP_010831733             463 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: serine/threonine-protein kinase [Nocardioides].
ACCESSION   WP_010831733
VERSION     WP_010831733.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..463
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=49493
     Region          8..270
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,32..33,62,68,73..76,90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,71,89..92,96,98,134,136,
                     138..139,141,151..152,155,171..173)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,71,89..92,96,136,138..139,
                     141,151..152)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,96,98,134,136,138,155,171..173)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(151..159,168..170,171..173)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msapviagft fvehlgsggf advflyeqhw prqrvavkvv rpdvplndre kqlftaeana
       61 matladhpyi vsvitagvtv eggrpylvmr ycpppdlgvr vrsnpmavvd avstgiklas
      121 aietahrsgi lhrdikpsnv lvttyhepal tdfgiaghia dvegesdvri sypwsppell
      181 dgrsngsvas dvyslgatiw hllvgrspfs ipsgdnstra lsarilhaaa patqrsdvpp
      241 aldrllqqcl aknpahrpqs aldlarslqq ieaaanwprt vvavegdrpd tsvrtpdpep
      301 eedrtvmkav tvisasgprr iataqtepdt derpvsglvw avigvlatva liggliltgg
      361 grgdsptptq pstsdtpspl ipdtltsppn lsgqrsgssv vfrwdsqdsv eagdewiwqe
      421 igtdaferts krsvrvsste qvclevrqvr gsdesptane cvp
//
LOCUS       WP_010831795             273 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Nocardioides sp. CF8].
ACCESSION   WP_010831795
VERSION     WP_010831795.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..273
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28252
     Region          1..228
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msssgavvtg agrglgkeia rllverghtv lvtdvdegaa tataaelger afarvvdvrd
       61 haqveaarde vveragrlev wvnnagilit gpaweqdeaa rrlmlevnal gtingtvaai
      121 gamrdggggh vvnivslagl tavageavya askhaamgfs lstmadlraa giknidisci
      181 cpdgiwtpml fdklddpgsa lsfsgkllqp eevidavrkv ldkprlvtav pgwrgivarv
      241 gdavpsfgla avplvvkqga rvqrkllkaq ape
//
LOCUS       WP_010831846             498 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PH domain-containing protein [Nocardioides].
ACCESSION   WP_010831846
VERSION     WP_010831846.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..498
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=53002
     Region          1..492
                     /region_name="YdbT"
                     /note="Uncharacterized membrane protein YdbT, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3428"
                     /db_xref="CDD:442654"
ORIGIN      
        1 msepdwqrls arnllidpvk vlgqfafpaa ialvgissgd rampwwavpv valgavvfgv
       61 lpwlttfyrt tdtqfqtrsg llnkksktap ldrvrsvdle asllhrlvgl tkvqigtgvd
      121 ddritldslt vreaadlraf llsrrapvtv padadtlpag adevatpggv rtgeparvla
      181 eidwawlrfa pfslarlvvv aaavgalsqf gdqlpvadta esawhwvaqf alslviaglv
      241 igalvswimv avtgyvvqww nmrltreags lqltaglftt rsitveekrv rgvemkepvl
      301 lrlvggaela tlatgvgsgg vtailppcpr svatsvgadv lethepmsva ltqhgpaarr
      361 rawirqlwga llvtaiplva slwlavptwl pvvvgvvala faavsgesay rhlghattpe
      421 hlvvgsgelt rvrtvlehdg iigwvvqqsw fqrrlalatl vattaagaer vvardiplta
      481 airladastp gvlspwls
//
LOCUS       WP_010831877             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DinB family protein [Nocardioides].
ACCESSION   WP_010831877
VERSION     WP_010831877.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Newton,G.L., Leung,S.S., Wakabayashi,J.I., Rawat,M. and Fahey,R.C.
  TITLE     The DinB superfamily includes novel mycothiol, bacillithiol, and
            glutathione S-transferases
  JOURNAL   Biochemistry 50 (49), 10751-10760 (2011)
   PUBMED   22059487
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Cheo,D.L., Bayles,K.W. and Yasbin,R.E.
  TITLE     Cloning and characterization of DNA damage-inducible promoter
            regions from Bacillus subtilis
  JOURNAL   J Bacteriol 173 (5), 1696-1703 (1991)
   PUBMED   1847907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..182
                     /product="DinB family protein"
                     /calculated_mol_wt=20342
     Region          30..178
                     /region_name="DUF664"
                     /note="Protein of unknown function (DUF664); pfam04978"
                     /db_xref="CDD:428232"
ORIGIN      
        1 manpgydgmw lpqdqdprse agpvrgelat lvgyleayrt tlelkcqglt ptqlgtrsvp
       61 psnlsllglv rhmarveqsw frrvieghme iprlfqdedl dagfnwagea ddalvadswe
      121 lwraevehar avldrtdldt lvdvhgepse vrdlvvhmie eyarhcghad lvrecidgra
      181 gq
//
LOCUS       WP_010831866             326 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Nocardioides].
ACCESSION   WP_010831866
VERSION     WP_010831866.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..326
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35277
     Region          7..324
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mvqtvtkvgv llyddclase alglvdvlav anrvaaftgh papfrptiha arpgvvcaan
       61 gvevrarrid htidllvvpg fdlspeqdie rrlpklsaev allrrsaarg iptasicgga
      121 fllgaaglld grrattawlf adelarrhps ssidprallv edgpitttga fsasldlamh
      181 lvrvhagesi arttsnitlt rlgrssqspf vddtlrqrvr qafstgvrrh lldhldqpyd
      241 ltalalahht strtllrrfr aetgqtpldf lqgarvarar hllettnlsv aeiarsvgye
      301 dtssfrrlfs gvvsmtpshy rrtfvg
//
LOCUS       WP_010831886             265 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Nocardioides].
ACCESSION   WP_010831886
VERSION     WP_010831886.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..265
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27350
     Region          7..247
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msleqpvlls venaiatitl nrpdamnsld iatkellrdi vqqvaadeav rcvvltgtgr
       61 gfcvgqdlke hiellrsgas delfttverh ynpivtalat mpkpvvaavn gvaagagasl
      121 alacdmrvla dtagfnfafa gvalaadtga syhlprlvgq akalellyfp stvsateset
      181 lglanqvvpa aelaetvsal atrlaagptv afasirqsva fssqnsfads lanegqamnr
      241 tgatedhaaa vaafvakekp vfhgr
//
LOCUS       WP_010831936             142 aa            linear   BCT 01-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Nocardioides sp.
            CF8].
ACCESSION   WP_010831936
VERSION     WP_010831936.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..142
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=14189
     Region          1..126
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mngrigwrlg rqrdergaat ifvvlftval lavaglvidg gyalgakraa mnnaeqaara
       61 gadalnqgal rdgqtmvdpg ravnaaqayl alvgaqgtvd iaggevtvtv tgqqdtklls
      121 avgvgsipvk atatalsida dd
//
LOCUS       WP_010831998             234 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010831998
VERSION     WP_010831998.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..234
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25222
     Region          28..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtnasklipk vpgvprvpsr raqfssstkr alvevaedlf aeqgypatsl dqivagaqvt
       61 kgalyhhfsg kqalfeavfe rienearksi qaglkgerdp wrkaqaglra fldvvqepgy
      121 rrvviqdgps vlgyerfreh eerstfatvv eivravltag ewdldeemlq tftriffgam
      181 ssagesvass ddpataavrv emaigfilag lqsladagvp ipapqdadtg tdeg
//
LOCUS       WP_010832004             212 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010832004
VERSION     WP_010832004.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..212
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22046
     Region          2..212
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 matetsqtld rglrvlevla eapqgltvte lsqqmgvnrt vvyrlistle qhalvrrdgr
       61 grlcvglgvl hlasavqpll rdlavpvlrs laeaigctah ltvadgdeal alavveptwt
      121 dyhvayrvgs rhpltagaag kaisllsdad taayavtsge lqsgahglaa pvrgleglra
      181 svgivtldga ideklvaprv laaaqqvaer lr
//
LOCUS       WP_010832023             352 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alkaline phosphatase family protein [Nocardioides].
ACCESSION   WP_010832023
VERSION     WP_010832023.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..352
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37446
     Region          34..>258
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
     Region          <221..298
                     /region_name="ALP_like"
                     /note="alkaline phosphatases and sulfatases; cl23718"
                     /db_xref="CDD:474031"
ORIGIN      
        1 msrlgvvlpa ltlvlsggla caaaseapda aarpttaerr idtlgpidtv vaisidglnp
       61 naitklrkrg tpalhrlirt gastlnarte leltdtlpnh tgmvtgrrie aatgghgvtw
      121 nddrrrpstv qaaagheves vfdvvhdagg stayfasktk fslwerswde aidtdviien
      181 nrrltrrfva dlagttrsfr llhlsapdaa ghdhgfmspr yletvtatdr lvgkvlrais
      241 ssptlsghta viltsdhggr gashrapnrp anytvpfmvw gpdvavadly dinptytdpg
      301 rtqstyddat irngdvanla ldllelpavt dsehnvaqdl vtlttdpnpa ag
//
LOCUS       WP_010832029             392 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Nocardioides].
ACCESSION   WP_010832029
VERSION     WP_010832029.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..392
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42068
     Region          168..392
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdgpperpra edtrpeltfg gqawrlavcl afsmlvwsqa vekewsehrs ifwfeialga
       61 tafvvvifrr rapaaiaavt aglsmfsgia agpatlaavs latlrrptpi igigllnfac
      121 amtytlyapf dltepiwvsv vinlvvnagm mgwgmylgsr reliwtlrqr asraeaeqel
      181 rvaqgrsqer eriaremhdv lahriaqism qagalafrdd laaeqlrdgl geiqgkssea
      241 inelrgvlgv lrdrttgelv egpqptyddi aalveesrah gvhvelsdrv drsteavpdp
      301 vgralyriiq egltnatkha pgalvtials gspahgidvv irnplgfatg stpgaglglv
      361 glaeraelrg gtlehgsddg vfvlsgsipw tp
//
LOCUS       WP_010832040             251 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: energy-coupling factor ABC transporter ATP-binding
            protein [Nocardioides].
ACCESSION   WP_010832040
VERSION     WP_010832040.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..251
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26851
     Region          6..232
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mstpvldvrg lafaypdghq alygvdlhvh qgervallgp ngagkttlvl hlngiltaga
       61 gevavsglpv akrnlqeirr rvgivfqdpd dqlflgtvrq dvafgpanlg lkgaaldkrv
      121 mtaldlvgma dfadrpphhl sfgqrrrvam atvlamepei lvldepssnl dpasrrelad
      181 ilrsldvtll mvthdlpyal elcprslvls dgivvadgrt fdvltdaplm aahrlelpwg
      241 fdprsvgslp a
//
LOCUS       WP_010832067             140 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Nocardioides].
ACCESSION   WP_010832067
VERSION     WP_010832067.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..140
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14214
     Region          5..136
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mpttrtasth wegtlfegag kvtlessglg tydvswpara eepngktspe eliaaahssc
       61 fsmafsngla knetpatsld ttaavdftpg tgitgitltv rgvvegidnd kfvalaeeak
      121 agcpvsqals vpitldaala
//
LOCUS       WP_010832076             291 aa            linear   BCT 01-JAN-2025
DEFINITION  Fpg/Nei family DNA glycosylase [Nocardioides sp. CF8].
ACCESSION   WP_010832076
VERSION     WP_010832076.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..291
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=32066
     Region          2..272
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpeghtlrrl addldaafgg slvhvgspqg rfaadaaivd gtrllgahsv gkhlfvefeh
       61 dhlihvhlgl iggfdvhtgv eevplpvgqv rlrivredat ayadlrgatq celigpargd
      121 eirdklgpdp lradadpdra wrrikashra igdllmdqav lagvgnvyra evlfrnrihp
      181 lrpgktlras qwqaiwtdlv elmregvvhn ridtvrpeht peamgreark ddhggevyvy
      241 rrtgqpclvc etpvrtevla grnsfwcarc qprfrsravq ssaapargpr t
//
LOCUS       WP_010832125             537 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Nocardioides sp. CF8].
ACCESSION   WP_010832125
VERSION     WP_010832125.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..537
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55760
     Region          26..519
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(33..34,37..38,41,73,123..124,126..128,131,152,
                     155..156,159,261,264..265,268,302..303,306,334,338,
                     410..411,415,419,435,438..439,442..443,446)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtdtaevtpe vtpeehkrlr walvlislaq lmvvldstia nialpfigqd ldisqsnlqw
       61 ivtgyalafg gllllggrlg dlygrrrifm igvtifaias lagglaqnea mllssravqg
      121 lgaalaspaa lalitttfpa gkernrafav yammsgagaa vglilggwlt gihdlellgt
      181 pvngwrltff ivvpiglvaa afapryfqes erhpgeldip gaitgtlgll glvygfsrag
      241 daahgwsdpv tlaslaggva llaifavies rvehpllpir ifanqtraas faammlmpaa
      301 mfsmffflsl yiqnimgysp lkagvaflpf svgivisati vsnlvsrfdp rfiagtgtam
      361 aavalfgfsr ldvpdgasdv lsaastsafl gadvnywtsi fpfvmlmslg mgavfvpltl
      421 tavhhvraed sgigsgvlnt mqqvggalgl aimstvassa atdhadkiap gvakglagae
      481 psviqglvql gsfptgataa fffgtflmaa gslivwlfln vkheelatdg pasvpgh
//
LOCUS       WP_010832146             297 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: serine/threonine-protein kinase [Nocardioides].
ACCESSION   WP_010832146
VERSION     WP_010832146.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..297
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=31994
     Region          27..278
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(30..31,33..36,38,51,53,85,101..104,108,110,147,149,
                     151..152,154,162..163,166,181..184)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(30..31,33..36,38,51,53,85,101..104,108,149,151..152,
                     154,162..163)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(34,108,110,147,149,151,166,181..184)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(47..48,77,82,87..90,102)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(162..170,178..184)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mtelaeavgs swrladgdai tpeltavrkl gggaayeawl afdevtyspv vvkllrpdql
       61 dsassrrglr revaalaavn hpvvvrglrh dldgprphvv lehidgprls slvrrygplq
      121 eqqylplaid vaaalhylgr igwthldikp sniimgapar lidlsvarpl qdarelrhli
      181 gtdaymapeq cdpgtvrpcg asdvwglgat lfeavagrra fadpqpraea leerfpqlgt
      241 epgalpdgvp revvsvigam lardpearpa pyeivdalap vlarlprgnl agfkvrr
//
LOCUS       WP_010832182             242 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ComF family protein [Nocardioides].
ACCESSION   WP_010832182
VERSION     WP_010832182.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..242
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=25266
     Region          5..225
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mrdvlldlvv gsecvgcarp grmlcprclh alpsvpricw pqptppglvt pwsvadydga
       61 vramvvghkd rgqftfrrvl ggllavsvra amadddgavv lvpapsrpgs srrrgydpmg
      121 alvrtaaarl raegrdvtaa sllvsnrrvv dqaglsager shnlsgsmsc pspglarlar
      181 rrararvvic ddvlttgsta reaqralgav glgpvalatv aatrrripdq tggsllsrgp
      241 rg
//
LOCUS       WP_010832232             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: maleylpyruvate isomerase family mycothiol-dependent
            enzyme [Nocardioides].
ACCESSION   WP_010832232
VERSION     WP_010832232.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..206
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22018
     Region          8..187
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 midvwqtvaa ergaladdla gisaeqwdtp slnhewtvhh tlahmtstah tgparfvggm
       61 vasgfrfgef tergivrhhg ltaaetlanf raiqgsrksp pgprtswlge tlihaedirr
      121 plgishdypa eavalcldff krsnlligak rridglslaa tdqdwqygag ttvrgrgidl
      181 lmamtgrgaa cadltgsgva tlqsrc
//
LOCUS       WP_010832240             188 aa            linear   BCT 01-JAN-2025
DEFINITION  NUDIX hydrolase [Nocardioides sp. CF8].
ACCESSION   WP_010832240
VERSION     WP_010832240.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 188)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..188
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20557
     Region          46..171
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mihddalall aswtppsphd etlrdrylah lrsrpdgllk scfpdhltag aivvspdasa
       61 vllnhhrkad awlafgghie pgdatlaaaa rrelveesgl tdfdfdptpl sldehavdfc
      121 sdrgtvhhld vrfvatavpd ddhvvsdesl dvrwwpvdal pqtfddmyrl idvaitrvaq
      181 stlplsps
//
LOCUS       WP_010832264             415 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sugar ABC transporter permease [Nocardioides].
ACCESSION   WP_010832264
VERSION     WP_010832264.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 415)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..415
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43283
     Region          32..407
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 msdpsastva adladerlir tqglggyahl fwnrlrsgel gslpvviglv iicigfysqe
       61 prflssrslv sisqfaapig iialgivlvl llgeidlsvg svsgftaatm avllvdhgqs
      121 mlvailaama vgvaigalya vlytklgvps fvfslagllg fqgallyvlg kngtinlpsd
      181 sflvqftrfe flspamsyvl vvaigllyva aqlltirqrt aaelssppia lvlvkgallv
      241 gglgaltyyv nidrgwsylw lffvllvvlm dlalrrtrwg rhvfavggne eaarrsgikv
      301 sriyfsvfal csmlaavggl laaglqtsvs qasgttdtnl taiaaavigg tslfggrgsa
      361 ysamlgiivl qaiqtglnlv gvdssvrfmv tgavlliava idsvsrrlrt ssgrg
//
LOCUS       WP_010832269             168 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SigE family RNA polymerase sigma factor
            [Nocardioides].
ACCESSION   WP_010832269
VERSION     WP_010832269.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..168
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18735
     Region          6..161
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mtrniddsfv efvaahrarl frtayllvgd ahraedivqt altklyvaws rvasvdnvea
       61 yarravinah lsehrrpwrr erlvlddiep pavhdpdpge gdalwtalrg lpigqrrivl
      121 lrhywglsva etaadlgige gtvkrqtwta lnslrsvlgt telngghr
//
LOCUS       WP_010832299             197 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase family protein
            [Nocardioides].
ACCESSION   WP_010832299
VERSION     WP_010832299.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..197
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20911
     Region          2..190
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrklivtvls tldgyaageg gnvfvmpidl gfdrynlerm qaaetmvfga tsfhgargyw
       61 ppladdesap avereisrlh ntldkivvsd stapadtepw sgttevvgra haadrltelr
      121 sgdggdivcf gsltawndll aqglvdelhv mvgpgaigag lptfnqpvsq rlslldarrl
      181 ddselvalqy avgptis
//
LOCUS       WP_010832321             184 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: histidine phosphatase family protein [Nocardioides].
ACCESSION   WP_010832321
VERSION     WP_010832321.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..184
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19803
     Region          5..180
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mqqpvylvrh gqsewnvlrl tqgqtthppl talgreqaaa aaedladelt ggvrlltsdl
       61 vravetarii gdrlgvapvl derlreqhlg slegrgyeet waeaerhdws dpelplagge
      121 svadvrrrma avladldpai ptilvshgda irsalahlrg hsltdapwvd vpngsitrle
      181 gvla
//
LOCUS       WP_010832334             346 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Nocardioides sp. CF8].
ACCESSION   WP_010832334
VERSION     WP_010832334.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..346
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38650
     Region          31..286
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(35,38..40,43,54,56,88,107..110,209,211,213..214,216,
                     229..230,233,248..249,252)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(35,39,43,54,56,88,107..110,209,213..214,216,
                     229..230)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(38..40,209,211,214,230,233,248..249,252)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mtsavrdeda fdvdavaqwl kaqgvegpie evrqfsggas nltyllrvpg relilrrapq
       61 gtkakgahdm rreftiqsal apvfpyvapm vgfcddssvi ggdfyamgri dgliprstwp
      121 advplspeqa rqlclnvvev yaelhtvdas aaglsdlgkg tgyvrrqveg wstryrnaht
      181 pdnpeftevm awldanqped iancvihndf kvdnivfshd dptkvvgvld wematlgdpl
      241 mdvggalafw iqaddsdelk ltkrvptdlp gmitreefvq aycermgftl tpeqwrfyev
      301 fglfrnavia qqiyyryfhk qtsnemfalf gpgvqildrr iaellt
//
LOCUS       WP_010832340             293 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: aldo/keto reductase [Nocardioides].
ACCESSION   WP_010832340
VERSION     WP_010832340.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..293
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30982
     Region          11..279
                     /region_name="AKR_AKR13B1"
                     /note="AKR13B family of aldo-keto reductase (AKR);
                     cd19088"
                     /db_xref="CDD:381314"
     Site            order(17..19,48,53,89,131..132,161..162,183,210..216,241,
                     258..263,266,269..270)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381314"
     Site            order(48,53,89,131)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381314"
ORIGIN      
        1 mhtrtlgkhq vgaiglglmt fdqsgtqpre qlldtvraal dagitlldta daygpgderg
       61 vdaqgenerl iaslldelgv rdrvllatkg ghvrtegggw aldsrpehlr savdaslarl
      121 gveqielwqh hrpdpevpyd evigtlheia gsgkvamigl snadpdqira ahavlgaslv
      181 svqnqfsprf rssrpeidvc eelglaflpw splgglgdak eladqhpafa qvaqdrqvsa
      241 qqvalawela qspcvipipg akrptsvrds aqaadlvlsd eelaslsgda sas
//
LOCUS       WP_010832409             619 aa            linear   BCT 01-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Nocardioides sp. CF8].
ACCESSION   WP_010832409
VERSION     WP_010832409.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Burnim,A.A., Dufault-Thompson,K. and Jiang,X.
  TITLE     The three-sided right-handed beta-helix is a versatile fold for
            glycan interactions
  JOURNAL   Glycobiology 34 (7) (2024)
   PUBMED   38767844
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12131601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..619
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=67429
     Region          220..359
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
ORIGIN      
        1 mtrsqprsia iaiaallcla ggllalsgap asaheerpav fpdgsgsvpt flgldnprqr
       61 vvcrpdsder iarmkagalk rrnqsllrqc efhsiqdaid sisrrrtsiy vlpgryveak
      121 hassarsdyc shlrtesndp ldasqyigsi asslsaeeaa dagesnpial syadqrrcah
      181 nlnlialfgd rtpadddiac dshfcgtqvv gtgrrmtdvl vdnrfsklna fradraggvy
      241 lrnmtfqqae fnavyiletd gfvvdrvltr gndeygvlaf asdhglikds eayyngdsgi
      301 ypgsgsdlng dnpdfevsry aieirnnrsh hnalgysgta gnsiwahhnk fyanatgiat
      361 dslfpghpgl pqdharwnrn eiysnninwy ekfvdtgvca kpmeqrgyld gtvcpviptp
      421 vgtgvliagg nfnstdhnwi ydnwrygtmq fwvpaplrde fdpqklfdts hgnrtfdnqm
      481 glakdgtiah ngsdhwwddq gtgncwegna ysrgaqtdnf tiqppgcadg gsvltpglpv
      541 kdagfltcsq ydrndevlrh ppgcewfdtp akptaaapar atsqpagrkv apaapylgvl
      601 pgllfvaglg mvrrarrrs
//
LOCUS       WP_010832412             390 aa            linear   BCT 01-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Nocardioides sp.
            CF8].
ACCESSION   WP_010832412
VERSION     WP_010832412.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..390
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=40536
     Region          <13..54
                     /region_name="PRK07819"
                     /note="3-hydroxybutyryl-CoA dehydrogenase; Validated"
                     /db_xref="CDD:181133"
     Region          110..390
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mteltneqih dtlvlpylnh aarmfeagya savdidnamr fgcgypkgpl tvvdelgaaa
       61 vraglaarfl dsgdplhqpa qvistlated gtfaasgdaa gatapelkqe istvgvvgtg
      121 tmasgivqvf aqagydvvfv grgedkiagv vafidkglsk lvekgrided akaatlarlt
      181 gatdrealad vdivveaiae dlaiktdlyk dldrickpga ilatttssmp italgavtsr
      241 peavigmhff npatimklve vvtteatsad vnqtvlalca kvgkvavscg drsgfivncl
      301 lfpylndavk lvesgaatid eiddavkeqa gfpmgpfall dvvgndvsla iqqelfaefg
      361 ekgfapaatl etlvaegklg rksgegfrty
//
LOCUS       WP_010832413             601 aa            linear   BCT 01-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Nocardioides sp.
            CF8].
ACCESSION   WP_010832413
VERSION     WP_010832413.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..601
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=64018
     Region          12..292
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
     Region          318..598
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mttasserap rtfttigvig lgtmgagiae vfarngfsvi gvelsdeave rgrghlahst
       61 gravsrgkms eadqaeilgr isfatdlsal aeadfvveav iesleikkdl frrlddivkp
      121 dailatntss lpvteistan trpgrvvgvh ffnpapvqnl veivrtvvte pavladvegl
      181 vgtlgknpvv cgdkagfian tllfgylnha asmfetkyas redidaamrf gcgypmgpla
      241 lldligldta yeildtmykq grdrlhapap ilkqmvtagl lgrktgkgfy tyesvdssav
      301 vadvhtpsad dvpqlrrpia tvgvvgtgtm aagivevfak sgldvvyvgr sdakvegvra
      361 tiersldkai qrgkleeatk tevlgrltgs tslddlatvd lvveaiaedl rikttlfenl
      421 deickpgail atttsslpvi alakatarpq dvvgmhffnp apimklvevv stvataedva
      481 etvralcdqv gkvavscgdr agfivnallf pylndavkml eahyataddi dtamkqgcal
      541 pmgpfelldv vgndvslaiq relylefrep gfapaplleh lvtagylgrk tqrgfrdytq
      601 r
//
LOCUS       WP_010832380             303 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Nocardioides sp. CF8].
ACCESSION   WP_010832380
VERSION     WP_010832380.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..303
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=32344
     Region          53..297
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mkssrlarsm rhgvlalvla aaafavpgss veptdvelvr ikraggvsvg pdviwilavg
       61 sdarpgqdml rsrgdalqlv gintrtdaat aigvprdswv sipghgmqki naalyfggpq
      121 amagamanlt gitadyvmvt rfpffedmvd diggievhnp rrfydpylkk dgfkagrihl
      181 ggydamafpr irkslpggdf drsanqqrtl rgiharirsq adrpgfierg vmtvlkhmst
      241 nlgpaelyel aqavaqvepa kittcvirgr igatagqsvv fpdvaqarrl gsaarhdatl
      301 kgc
//
LOCUS       WP_010832441              86 aa            linear   BCT 01-JAN-2025
DEFINITION  inositol monophosphatase family protein [Nocardioides sp. CF8].
ACCESSION   WP_010832441
VERSION     WP_010832441.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..86
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=8658
     Region          <3..77
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mtsttlavaw vaagrraayi sdgtfvdnvh faagigvcra agcvvsdlag dalntrrgli
       61 vaadrdvhdq lvavigphla alddqg
//
LOCUS       WP_010832497             250 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Nocardioides].
ACCESSION   WP_010832497
VERSION     WP_010832497.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..250
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26807
     Region          13..241
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mthdsaplla agdpepkhra lqrtlaalag slepgspmps erslterydi srttvrtaid
       61 slvndgvler aqgkgtfvar drvrsnlhma sfsddmrrrg lapsstlvgv srqpttgava
      121 affggcagwr lervrladga pmalevdwvn adlvtdldah dltgslyall staydtpvda
      181 adqtvwasaa darqaellqv pvgapllafe rrsrsggrpv ehvtswyrgd ryalhmsldp
      241 smrtgpteal
//
LOCUS       WP_010832501             417 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Nocardioides].
ACCESSION   WP_010832501
VERSION     WP_010832501.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..417
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44100
     Region          15..394
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(25..26,29..30,33,65,120..121,123..125,128,148,
                     151..152,155,231,234..235,238..240,243,265,269,321..322,
                     326,330,346,349..350,353..354,357)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtwadavqpl rqrnfawyfg srfvntlgnm manialtfav lditdsaaal gqvlaahtip
       61 mvllllwggv isdrfprelv iqvsnvasal tqgliaflvl tgtaelwmli alsvvhgavs
      121 aisfpamasl lpqlvprdql qpanalmslt rngltvlgpt lgallvvtvg agwalaidaa
      181 twliaallli pvkvpraeks aeqkstiael regwsffigt twlwavvlgf gflnmihnga
      241 lfvlgpvvae dtigrqgwgy vlsaealgll amavvllrvp lrrplfwgml aiafasvpmi
      301 vlgvdphlva lvcaafvaga gievfsmgwn lamqeniddr mlsraysyda lgsfvampvg
      361 qlawgplgaa fgnsrvlvvs giayaaicll vltsrsvrdl prraatddal evatggg
//
LOCUS       WP_010832531             283 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Nocardioides].
ACCESSION   WP_010832531
VERSION     WP_010832531.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..283
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30833
     Region          17..224
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16282"
                     /db_xref="CDD:293840"
     Site            order(69,71,73..74,154..155,173,213)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293840"
     Site            order(69,71,73,154,173,213)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
ORIGIN      
        1 mktdgiitev aprawvahyd wmavnitlig gddglvmvdt hgsekqarvv addvrrlgag
       61 pitalvnthd hwdhwygndv llteygdlpv hatdfaldrm vatqgrhdph ladnsradei
      121 lattlrpatr gfssvvaldl gdrvielihp grghtagdlv vrvpdadviv ggdlveesdk
      181 pfigddsfpl ewpltldlvm glmtdatvvv pghgkvidrd yvqdqrvelg iiaetirdla
      241 srgvpvsqal eqgewpwdpa llasavrlgy ehlpraqkrl plv
//
LOCUS       WP_010832559             161 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: flavodoxin family protein [Nocardioides].
ACCESSION   WP_010832559
VERSION     WP_010832559.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..161
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=16320
     Region          3..159
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 marllivhhs ptptvsalte avvagagdea iegvevvvre alaasaddvl aadgyllgtt
       61 anfgymsgal khffdtiflq aggaladdgs agsatggrkp yglwvhgryd ttgavrsvqs
      121 ivqalgwqqs asvlevlgdv gdeerasgye lggtiaalls e
//
LOCUS       WP_010832567             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter ATP-binding protein
            [Nocardioides].
ACCESSION   WP_010832567
VERSION     WP_010832567.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..262
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27503
     Region          7..228
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mlnalgapvv eaqavtvtig grpvlrgndl tvregefval mgangsgkst lvraltglrp
       61 ltqgsvhlfg tpledfrdrs rigfvpqrat aaggvpasvr evvasgrltr rrllrlpsra
      121 drtaiddale vvglahrahd gvstlsggqq qrvliarala gqpdlfflde ptagvdlpnq
      181 halaaalrtl sergatvvlv ahelgpmasl vdrsvvmrdg riaydgppls eqavhghhhp
      241 apgrhdhvph vgspfdtleg gr
//
LOCUS       WP_010832577             385 aa            linear   BCT 01-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Nocardioides sp. CF8].
ACCESSION   WP_010832577
VERSION     WP_010832577.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..385
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39510
     Region          2..377
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mflmatsaig pgfitqttvf taqlgaafaf aivvsilvdi avqlnvwrvi gvsglhaqdl
       61 ankvlpgsgy vlavlvvlgg avfnignigg talgmnamfg mdvklggais aaiavaifls
      121 kragvamdri vvvlgvlmis mvlyvaivsd ppvgealrqs vlpdevsfli ittliggtvg
      181 gyityagahr lvdsgitgte hismitrgsv tgiivtgimr allflavlgv vaggavlatd
      241 nppasafqha lgdvgvrifg vilwaasits vigasytsvs fmagfmgrlr eqrnllvvgf
      301 itvcavafla lgkapvtllv lagalnglil pvglaiilwa aarrsgdllk gyaypkyllv
      361 igilvwmltv ylgwkslggi salwg
//
LOCUS       WP_010832603             217 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010832603
VERSION     WP_010832603.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..217
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23649
     Region          7..214
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mttpgkaaqa yhdlermivf qelepgslvs eallmertgl grtpvrealq qlsrnrmvei
       61 hpnkgvlipp tsvesqlrml elrrvleala vrlacerata geraamevma grldhgtftl
      121 reyaetvrgt heliaagshn dyladamapl qglsrrfwft hvvaedaeik agatlhstll
      181 vsivsgdvdg aeaashalnd ylvdfayatl srssgrr
//
LOCUS       WP_010832654             301 aa            linear   BCT 01-JAN-2025
DEFINITION  type II secretion system F family protein [Nocardioides sp. CF8].
ACCESSION   WP_010832654
VERSION     WP_010832654.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..301
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=31433
     Region          64..276
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mtplvpaicg alvvagligm vyalrpappk pprpartvtp fgrlgsrinq lsprtrkliv
       61 agtvtgllva lvtgwviavv lvpaaiigip lllspppaaa sieklealee wtrslagklt
      121 agqslrsali kslqsvpapi qdevglmvsr lwngtgtted vlrafaedln dstgdviasq
      181 lilaasgrgq aglakaldal aetvasdvra rrqieadqak prttartvtv itlgvlglla
      241 ftgdyiepyg splgqvilai llsayvatll mmrrmaiakp lprfldlqar naqrqnegaa
      301 a
//
LOCUS       WP_010832658             146 aa            linear   BCT 01-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Nocardioides sp.
            CF8].
ACCESSION   WP_010832658
VERSION     WP_010832658.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..146
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=15334
     Region          3..136
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mnrhllcrrp rdergaisvw fataslvmii lvgmavdlgg kvhtqqhars vaaqaartga
       61 qevqgstavr gedlrvdifa aksaaqdylr aagvegtvsv tggdtlvvrt tdtydskflg
      121 iiglnsmpvt geasarlira eggier
//
LOCUS       WP_010832676             366 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Nocardioides sp. CF8].
ACCESSION   WP_010832676
VERSION     WP_010832676.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..366
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41039
     Region          26..348
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mrllalpgga tdqalasaqd vedfeqelvd qyalamvaag lsdghirnsr atviefarsm
       61 tgplweatcq dadrylaeqr qlgrsvstra gkagtlsvfy dfvidryegt irratgaqve
      121 qpideynrqs gaslgnvrvp psdeevdtlf tawresvpna rkylpaardy faaslwrrlg
      181 lrinetvmld irdwrpdlgg ygklhvrfgk gsrgrgpkpr lipaingadq lidwwlaevr
      241 phygadwtsp dapllpserl dhglgrcgra rpdvlrrtln ahvdqwlpaw sgritphvlr
      301 hycasslyaa gmdlkalqel lghqwlvtts gyihvrsdhi qrawdqaner ledrfgqrrl
      361 pvparn
//
LOCUS       WP_010832704             162 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Nocardioides sp. CF8].
ACCESSION   WP_010832704
VERSION     WP_010832704.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..162
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17689
     Region          36..152
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtnldellas wnekfrphed garlpphhdh clacgpdnph ghhltvqrrg devhavhvfd
       61 erhvgapgia hggavatvld dlfgfllylt gspavtrkle vrydspvilg ttyelaarav
      121 rtegrklfve admsetggpt vafasalflr vdvthfdqgr pr
//
LOCUS       WP_010832715             225 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010832715
VERSION     WP_010832715.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..225
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24711
     Region          23..174
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvevgrwvds tvrrrssrdd qvrarrrqqv asaalqvvde agagagtali aeragiprph
       61 vyryfssred ldddvarlaa qdliacvrph ltrrgtpsqv veglvhacat wadvhphlfr
      121 flaargqsrt lhrarmgrsr lldeiaaaar gytnsaeetf pegilvgvmg mvdatiiwwl
      181 dqrdetldvm vgrlsrhvtl vlhdalaahg idldpavele pfigg
//
LOCUS       WP_010832785             236 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010832785
VERSION     WP_010832785.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..236
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24995
     Region          39..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msvgptdgrq vrweqhnier raailaaale vieatppgde vnvahiaera gvgrtviyrh
       61 ftdraeldra iraailndvw ahllpvltle gtipqiiera vaeyvnwaaa hpalhgvavt
      121 sepgggnpld egvaviagrv veligtalei lglelsader aaidplvhgf vggafgvvrr
      181 wlarpereps aevlaeltta svwfqlhgha galglelrad qpieellagp gpegaq
//
LOCUS       WP_010832813             366 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Nocardioides].
ACCESSION   WP_010832813
VERSION     WP_010832813.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..366
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39754
     Region          20..347
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mttaplrpgt spdldhdepl lvvedltvrf ptqdgevaav qnlsysvelg ktlgivgesg
       61 sgksvssmav lglhdersak isgsirirgr eivglpenkm rklrgaeaam ifqdalaalh
      121 pfykvgdqla eayqvhhssa sdrdarrksi emldrvgipq pdqrindfph qfsggmrqra
      181 miamglindp slliadeptt aldvtvqaqi ldllqelqre fnsaviiith dlgviaemad
      241 dvlvmyagrc veygttkeil thpempytwg llssvpdvta stdarlipip gtppsllnpp
      301 tgcafhprct hrdkvpgdlc ftdmpelspa kanaahvkrc hlpdpdaiyq dvvlpeiapd
      361 lvkdnr
//
LOCUS       WP_010832905             132 aa            linear   BCT 01-JAN-2025
DEFINITION  arsenate reductase ArsC [Nocardioides sp. CF8].
ACCESSION   WP_010832905
VERSION     WP_010832905.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..132
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=13808
     Region          5..127
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(9,11..16,102,104)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mkptvlfvcv hnagrsqmaa gwlqhlagdr vevlsagsap aetinptave amaevgidit
       61 sarpkvltdg avqasdvvit mgcgdacpfy agkryedwhl edpagqgiea vrpirdeira
      121 rvealvaeia pa
//
LOCUS       WP_010832920             240 aa            linear   BCT 01-JAN-2025
DEFINITION  peptidylprolyl isomerase [Nocardioides sp. CF8].
ACCESSION   WP_010832920
VERSION     WP_010832920.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..240
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=24015
     Region          79..239
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mlkrlvaisa tlaclslaac gneggesatd ptteettset tsetpaetes aagaceyveg
       61 gspavrevel ppseptvsge vkvvfqttlg dipatldada tpctvnsfvs laeqgffdds
      121 pcprmataps fgilqcgdps gsgsggpgys yadeltgeet yeagtlaman agpdtngsqf
      181 ffvfndspgl tpdynvfgsv dpaglklltk aakkgddgsh pagggvpnag piditgvtig
//
LOCUS       WP_010832992             151 aa            linear   BCT 01-JAN-2025
DEFINITION  Fur family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010832992
VERSION     WP_010832992.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..151
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16146
     Region          10..141
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 msllptvdpr erlkvaglrv tqprvavlha laaqphadad alatavrael gavstqavyd
       61 vlhaltdarl vrriepagsp aryelrvgdn hhhvvcrscg aiadvdcavg qrpcldasdh
      121 hgfvideaev tywgvcptca estrtplnee r
//
LOCUS       WP_010832990             124 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Nocardioides].
ACCESSION   WP_010832990
VERSION     WP_010832990.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..124
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13062
     Region          <13..>105
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(20..22,24..25,29,32,41,43,45,49..50,53..55,57..58,
                     62,65,74,76,78,82..83,86..88,90..91,95,98)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          43..74
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          76..105
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msltpeqtqr vltlaldlar ageteqlaef ldhglpidsv sesgdsllml aayhdrpetv
       61 smlldrgadp dqrnsrdqsi vagalfkgad dvvrrlvaag adldagtpta rqaaemfgrg
      121 glld
//
LOCUS       WP_010833077             287 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Nocardioides].
ACCESSION   WP_010833077
VERSION     WP_010833077.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..287
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30068
     Region          28..271
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mtasgstfts ptdatilaty swdnlfvpaa avqiahglae hsarydrlaq alngagylvh
       61 ahdhrghgks idgtpgdfgk ggfdaliadt aaygatlred rpdlplflia hsmgsfaaqs
      121 vllehsdlya gvvlsgstal dvlaaglaes edpagleafn agfehrtgye wlsrdeaevd
      181 ayvadplcgf dlpdetvpsl fgaaatladp kalagirsdl pilivsgsad plagggelvq
      241 llghryreag vkdvtvktyd garheifnet nraavtadvi dwlgrhr
//
LOCUS       WP_010833098             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Nocardioides].
ACCESSION   WP_010833098
VERSION     WP_010833098.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22304
     Region          13..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpeptstpst tgrrsellri aatlfaekgf rnttvrdiae aagilsgsly hhfdskesmv
       61 deilstfqde lfasydavla sdddartkld rvvrlsfeai dqhpaevaif qneadhlgtl
      121 erfgylaerg aqsrdiwvtl lregvetgvl rpdlnidlvh rfirdtvwva vrwyrpggdl
      181 shsdvadqyl tillegiara
//
LOCUS       WP_010833115             318 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Nocardioides].
ACCESSION   WP_010833115
VERSION     WP_010833115.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..318
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=33701
     Region          108..318
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvhaddlsls srvilingll faagtavlal spatvssrpv lselvvllvg ltvmivansm
       61 lvrrslrpld rlihhlaqae ssapatrvpv pssrlarrvs lavndlldri deaqrsnaaa
      121 alaaqesers riaqelhdgv gqsltavlle lklvsesvta ppldrvregv rasldevrsv
      181 artlrphvle dlglrsalaa lsqdlfgatr thvrrgimpg lpdlpddvel vvfrvaqeal
      241 tnvarhaead tvevslgivg qevelrvtdd grglpadadg tglrgmrera slvggrlslt
      301 rregggtvit lrvpvdpa
//
LOCUS       WP_010833132             214 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Nocardioides sp. CF8].
ACCESSION   WP_010833132
VERSION     WP_010833132.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..214
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23098
     Region          37..165
                     /region_name="Methyltransf_24"
                     /note="Methyltransferase domain; pfam13578"
                     /db_xref="CDD:433324"
ORIGIN      
        1 mtdwlehara aqgfmpedeg lllhrygrqq agqgallevg tycgksavyl gaaareaggt
       61 vftvdhhhgs eenqagwehh dtslvdprtg rmdtlpffrr tiedagledq vvavigtsat
      121 varhwrtpla llfidgghga eparadydgw vrwvqrggll vihdvfpdpa dggrppyeqi
      181 ylpalesgaf tevealgsmr vlertsgdag dpvg
//
LOCUS       WP_010833246             139 aa            linear   BCT 01-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Nocardioides sp.
            CF8].
ACCESSION   WP_010833246
VERSION     WP_010833246.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..139
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=14339
     Region          3..137
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mnrrdergsv tvwlalssfv miflvglavd lggqvhaher ahdvaaqaar aggeeveggs
       61 aiqghdlvin paaartaaqr yleaagvtgt vtitagttit vtvndsydpq flsliginrl
      121 dvtgtatarl vrtlggseq
//
LOCUS       WP_010833161             146 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PH domain-containing protein [Nocardioides].
ACCESSION   WP_010833161
VERSION     WP_010833161.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..146
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=15854
     Region          72..141
                     /region_name="bPH_6"
                     /note="Bacterial PH domain; pfam10756"
                     /db_xref="CDD:431475"
ORIGIN      
        1 mtapdalslp htwrpfgari aviffgamlv lmcvfawigf dpeirakftl fqrstivfig
       61 llyavagyal arsrvvasea gvvvvngykr rdyewaeiis ihlpvgapwa tidladgstt
      121 sllaiqgsdg drarsavrtl ralidr
//
LOCUS       WP_010833255             372 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Nocardioides sp. CF8].
ACCESSION   WP_010833255
VERSION     WP_010833255.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..372
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37724
     Region          <242..371
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mgikvlavsa taavllapga avlgvatlis paaagsgscm wdgqsteslg vsgpvpdsls
       61 atntngetvt lnqqqltraa tiiatgqsen ipargqmiav mtaltesslr vlsntgaypd
      121 sgnipndgdg sdhdsvglfq qrpaagwgsv enlmdpvwss rafyggpsgp nhgsprglld
      181 idgwasiepg aaaqavqvsa ypdryavnqp iaekvltsls gvslsselac aqpagdapln
      241 lppgfagdfi kaaasqlgkp yvwgggdfng ptaggfdcsg lvlyaayqas ggrirlphys
      301 gdqiragtgi pfgqkmpgdl iffsypgagg phhvaiyvgg drilhaprtg dvvrhgtige
      361 fagevmtvrr lg
//
LOCUS       WP_010833277             413 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Nocardioides sp. CF8].
ACCESSION   WP_010833277
VERSION     WP_010833277.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..413
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46276
     Region          75..401
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 marqrlmvgt ygeiscfrlk sgswqarary cdvdgvvrqy rkngetktka ranlkaffve
       61 htgtfgdgal apddtvqdll dlwfkkveqa dggpraetlg yyrshvrwil dpdktehplg
      121 ayqlrhvrpv iiqaaldsag vspdlrkrir svlvrafnma ifheaingnp atavpsvpvp
      181 rnkkkpvpvk dldavraair ewanaekrng pksvdlpdiv emliatgmri gellalrwsd
      241 ieltpperrd ddgwfpwlmv ngqitskgkr vdygkthaai rpialpdwaa allrrrkvaq
      301 tpndldavfi trngtwhfpt nvqgrlwhir hladyadlaa lqdvsphsfr rtvateidev
      361 ydaeaamnql ghtskvvter hyinrrlvvp dyraatdrla pgpetndgpt pgl
//
LOCUS       WP_010833278             382 aa            linear   BCT 01-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Nocardioides sp. CF8].
ACCESSION   WP_010833278
VERSION     WP_010833278.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..382
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=41501
     Region          18..375
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 msrharprke rgrsrvgerf eavvgpvahg ghcivrlpep esrvvftrhc lpgeqvvlei
       61 tegtdgdrfw rgdaisvldp spdrvqapcp vagpglcggc dfqhvslpaq ralkgavvse
      121 qlrrlagldl dvtvepvpgd eqglrwrtrm qwahtpdgqr glrahrsrrv vpvddcliat
      181 vdareptpgl tltesvldrh flveadgfwq vhpgapstlv ssvltmldpq pgervldlya
      241 gvglfarfla davgdgtrvi aveadraasr hskenlashq gavvecgpve kvlaaaydep
      301 idlvvldppr egakrvvveq vvdraprava yvacdpaala rdvaifaehg yrlerlrafd
      361 lfpmthhvec valltkigsd lr
//
LOCUS       WP_010833279             686 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Nocardioides].
ACCESSION   WP_010833279
VERSION     WP_010833279.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..686
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74547
     Region          19..488
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msvgdvskri llgrklrssq lgetllpkri alpvfasdal ssvayapdei fimlsvvgvs
       61 aytwswkigl vvalvmltvv tsyrqtvhay psgggdyeva tvnlgrnagi tvasallvdy
      121 vltvavsiss asqyaagaip llighealva sgavvvltal nlrgvresgs ffavptylfm
      181 vsilgmcayg lvqlllgdlp maesadlkie paegwdgplt qvamvfllar afssgcaalt
      241 gveaisngvp afkrpkskna attllllgli avsmmmsviv lakqmsiryv dpheierlrt
      301 aaggalpgdy eqhpvisqia ngvfqgfppg fyfvvtvtgi ilvlaantaf ngfpvlgsil
      361 aqdglaprsl gsrgdrlays ngivflaams ivlivvfeae ttkliqlyiv gvfvsfnlsq
      421 lgmirhwtrh lklthdpver rrmmrsrain tfglcmtavv lvivlvtkfl sgawitiiam
      481 vvfflvmkgi snhyamvete laadeqdkll ptrvhaivlv sklhkptlra lafakatrpn
      541 llegvyvsid aaatnklled wdernlgtpl kvlhspyrei vrpiveyaqe irrsnprgvv
      601 avyipeyvvg rwweqilhnq talrlkgrll ftpgvmvisv pyqlrsslia qergsredkr
      661 vqagdlrrgr vmrdtgdvdh drridp
//
LOCUS       WP_010833334             589 aa            linear   BCT 01-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Nocardioides sp. CF8].
ACCESSION   WP_010833334
VERSION     WP_010833334.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..589
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=65845
     Region          1..588
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 malpiedyal vgdrgtaali gkdgsidwlc lprfdspacf aallgspdng rwllapadld
       61 gvttsrtyvg nsailettft tptgvlvlrd vmpegdgrad lvrtircteg tvrvrhewvv
      121 rfdygrvrpw vmrqhvggqe vivatagpdk lmlrgprlph andgrhddef dvsagevmtf
      181 sttwvrswrd lpeplpfddr ieatraeheq walhcvedip haqlvrrsll tlrllthaet
      241 ggivaaptts lpedfggern wdyrfcwlrd aaltleslla agytdeardw rdwllravag
      301 dpedlqimyt vdggrqlper glphlagyed slpvrignaa vdqrqtdvlg evmialedar
      361 nagiaettqs walqrslven laehwdqpdn glweirgdlr hfthsrvmvw vafdravkav
      421 eqhgldgpve rwrtlrdqvc eeilekgyda ergtftqhyd treldaslln islvgflpgd
      481 dermlgtira ieedlmhhgf lrryrtqtgv dglsggehpf lacsfwlvsa yaragrreda
      541 halmdrlcal andvgllsee ydvdgdrmag nfpqafshlt lvqaalalr
//
LOCUS       WP_010832996             153 aa            linear   BCT 01-JAN-2025
DEFINITION  NfeD family protein [Nocardioides sp. CF8].
ACCESSION   WP_010832996
VERSION     WP_010832996.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..153
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15933
     Region          6..149
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mewlrdhawe twlgltivlg vaemfsldli limlaagalv gmvaalldlh iaiqilaasa
       61 aslaaiavvr psmvkrlhgg pelslghgkl vgkqgvvtee isalapgrik lagefwtaep
      121 ydetatiaag etvevlairg atalvhpvar les
//
LOCUS       WP_010833377             206 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SCO family protein [Nocardioides].
ACCESSION   WP_010833377
VERSION     WP_010833377.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..206
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21509
     Region          51..206
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 madrrrwfav vlasalaggl lsgcgatsda ggehqmtgtl ldppfavagd alvdgsrapy
       61 slvedtdkql tlvffgythc pdicgivmst masamtrlsd eeraevdvvf vttdptrdtp
      121 evtadyatnf dpgfigvtgp irtiidvakp lgisvdrgek lpsggfdvah gtqivaidaa
      181 ddgiaywsed vssaqlaadl qhllse
//
LOCUS       WP_010833455             312 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Nocardioides].
ACCESSION   WP_010833455
VERSION     WP_010833455.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33038
     Region          6..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msdlvietsg lrkeftgrrg trvavndldl avprggvhgf lgpngsgktt tirmllglar
       61 ptagtmslfg tpvpqrlpev igrvgavves pkfsptfsar qnlrllagsv gvergvvdda
      121 lvrvgladra ddrfksyslg mkqrlaiaat llkspdllil deptngldpa gireirelir
      181 glgeagvtvl lsshilaevq qvctsatiig ngrmlasglv edllgstsyr lrvgdpaaaa
      241 taleragmtv rtdvdsldvi tdepadritr vladaglyls eltpvradle tifleltadd
      301 rmgvtpmtee vr
//
LOCUS       WP_010833466             177 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PaaI family thioesterase [Nocardioides].
ACCESSION   WP_010833466
VERSION     WP_010833466.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..177
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=18764
     Region          36..155
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtsvdeilat wldkfkphed gahlpphhdh clacgpdnph ghhlvvhrrg eevhavhafd
       61 qrhvgapgia hggavatvld dlfgfllylt gppavtrqle vrydspvllg vayelvariv
      121 gaegrklfve aemsdtsggs vafasalflr vdgahfrqga snspplvapv esgqadp
//
LOCUS       WP_010833467             400 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nocardioides sp. CF8].
ACCESSION   WP_010833467
VERSION     WP_010833467.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..400
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43164
     Region          7..400
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtqgtalvvg ashagaqvva glrqqgwsgr vvligdeavl pyhrpplska ylsgksaige
       61 lairkphfya kqeielldar vesieraerr lvmadgdsls ydklalctgg rarllpvpga
      121 dlpgvhylrt fadveqires aqpgrhaviv gggyigleta asllalgldv tvleaaervl
      181 mrvtapevsa fyerihreag vtirtgalve amtgdarvre vqlaggerlr adlvvigvgi
      241 epntelaaaa gllvddgvvi ddhartndpd ivaagdctsh wmtrygrrir lesvpnaseq
      301 akaaaatmcg kektitalpw fwsdqydlkl qiaglstgyd eillsgdptq drdftcfylr
      361 eqkliaadcv nrprdfmrsk qkiteglead raellqiaad
//
LOCUS       WP_010833480             720 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MMPL family transporter [Actinomycetes].
ACCESSION   WP_010833480
VERSION     WP_010833480.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 720)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..720
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=74930
     Region          30..710
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mstttapskg apdftpgfrp gplgrlglwv sghaklvtgv wlllivglga fapqvehnls
       61 gagwqadgse svaarelaqe sfggnassai qvvvhstdgp vtegpgaevl aqvtrmleae
      121 priaeviapm pgatisqdgs taiilagaga dtnemvrvat dlkgdlqdls vegiqvnptg
      181 ssllwsdfne anleamlkse mvswpvtmai lvlafgalva aglpliltla glvasagslv
      241 linelvpvsi wamnfammfa lalgidyalf lvvryrasrm gsgnsarqav aetmdtagka
      301 vllsgatvli slsavmlvps psfrsmaggi mlsvvfvlaa tltllplvlf kldhkinkls
      361 lpwvktgehr spkfaawger lwkrplvwgl galivllala apiiglktam psikvlpeda
      421 sarvgydlvq esfgegapgt lqivmkasda daaktvlasd pgiagampsm paaddsglvl
      481 iqavptvdps dpalndtvdr lradlpssal vggaavenld lkaqldestp lvigvvlvlg
      541 fllllvalqa plisllgtla sllstaaafg varlvfqegi gadffgfesq gfldawapvf
      601 ffamifaiam dytvfllasa kehyehsgdp kdamvgslah sgrvifaaga vmvavfftfa
      661 lsgplppkem givlgvavll daflvrlvll pvmlrltgka awwspawlrr vlptitfshg
//
LOCUS       WP_010833496             188 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase family protein
            [Nocardioides].
ACCESSION   WP_010833496
VERSION     WP_010833496.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..188
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20550
     Region          2..157
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrklivtafv sldgvmeapg gepgyrntgw tfqdiefdpa ayeikgreqd eagalmmgrt
       61 syeafapvwp tmtedfagyn ampryvvstt leqedprwpa tilrstddva alketdgdpi
      121 ivhgsatlgr sladaglvdr yhllvfpvll gagkrlfsds dkdkdlldvv esesyangit
      181 kivadvrr
//
LOCUS       WP_010833505             142 aa            linear   BCT 01-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Nocardioides sp. CF8].
ACCESSION   WP_010833505
VERSION     WP_010833505.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..142
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15738
     Region          31..129
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mllrttdpfr dldrlaqqvl gttsrpavmp mdawregdrf viefdlpgva rdsidldver
       61 nvltvraerv apngdwesla serprglfsr qlvlgdnldl eqieaaygdg vlrlvvpiae
      121 rakprkieva ldgdqdrtai sa
//
LOCUS       WP_010833520             280 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TraR/DksA family transcriptional regulator
            [Nocardioides].
ACCESSION   WP_010833520
VERSION     WP_010833520.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..280
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28875
     Region          172..280
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 marstrksla gsaaaaakkv igrrgaattt dtvastskap akkaapaakk apakkaapaa
       61 kkapakkaap aakkapakka apaakkapak ktapaakkap aakapaktva kkvapakava
      121 tapvakkapa ktakksapaa kktaprkapi sslavkdged awtktdvkev laelhfqrdk
      181 lvhliedaeh dlqglmrdag dgaghdqadm gatsferdhe ltvvnnerdm vaqidralgr
      241 ihdgtygvce scgqpigkmr lmafpratlc msckqreerr
//
LOCUS       WP_010833646             108 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Nocardioides].
ACCESSION   WP_010833646
VERSION     WP_010833646.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..108
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=11507
     Region          3..101
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mdntqllkgv ldlavlavvd dedgygydvv rrlragglde vgdasvygtl rrlyaagalt
       61 syvvpsesgp hrkyygitps grdqlktqsd dwahfsttvt nllqgasa
//
LOCUS       WP_010833651             255 aa            linear   BCT 01-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Nocardioides
            sp. CF8].
ACCESSION   WP_010833651
VERSION     WP_010833651.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..255
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26232
     Region          1..255
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 myaeerqqam aqlinqhgrv svaelaadls vttetvrrdl salermglir rvhggavpas
       61 alaviesgis erdqanteak daiaaaaval lpppgsmivi dagsttarfa allprdhrlt
      121 vvthavpvaa rlaglpqidl fllpgrvrpt thaavgadtv aalsdiradv sflatnglsa
      181 thglttpdrd eaatkraiaa agrrsivlad stklgvessi rfaaldeidv litdsgmsda
      241 dasalaaadv evvia
//
LOCUS       WP_010833652             317 aa            linear   BCT 01-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase [Nocardioides sp. CF8].
ACCESSION   WP_010833652
VERSION     WP_010833652.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..317
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31739
     Region          2..304
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 miltltpnps idrtitlgge lvrgqvqrvv svtsqaggkg vnisrasvsa geptlavlpa
       61 akddpfvmel ltagidcrpv rpagevrvnv titepdgttt klnspgatvd addleamaat
      121 llarapgasw tvlagslpag apagfyaelv rrlraigarv avdtsdaplr alvealpgsa
      181 pdlmkpngae lasfaggdad dlerdpekaa taartlvvrg vgtvlatlgg ngavlvtaeg
      241 awhatppptt vvstvgagds slfgyllgdl rglpapdrla lavaygsaaa alpgttipep
      301 ahlrtdlvtv tvlggse
//
LOCUS       WP_010833667             143 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ferritin-like domain-containing protein
            [Nocardioides].
ACCESSION   WP_010833667
VERSION     WP_010833667.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..143
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14820
     Region          6..140
                     /region_name="DUF4439"
                     /note="Domain of unknown function (DUF4439); pfam14530"
                     /db_xref="CDD:434020"
ORIGIN      
        1 mstiealqat laaehaaifv ygdagahtsq saepdlfsti ttlyrthrar rdqlrlllad
       61 rgatpaaaaa tyeipsqlga pgavrrqalr teercagvya alvantagtd rawaisalse
      121 aaqarimlng spetfpgape lag
//
LOCUS       WP_010833715             444 aa            linear   BCT 01-JAN-2025
DEFINITION  ammonium transporter [Nocardioides sp. CF8].
ACCESSION   WP_010833715
VERSION     WP_010833715.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..444
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45507
     Region          4..415
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mtsldsgdta wllvsaalvl lmapglalfy ggmvrskgvl nmmmmtfgsl avitvvwvlv
       61 gyslafgddl ggglvgdprq yaglsslmse dsntgtvphi lfavfqglfc vitgalvsga
      121 iadrarfgaw mvfvtvwtll vyapvahwvf dfsagdhtgg wianrlgaid faggmaveic
      181 sgasalalal vlgprlgfgk dpmrphnltl vmlgagllwv gwfgfnagsa laanqsaaiv
      241 ftttlvagaa galgwlaler vrdghatslg aasglvaglv aitpscgsvt pigaivmglv
      301 agvvcalavg lkyrwrydds ldvvgvhlvg glvgtfgigl lasaaaptgv dgllygggad
      361 qlgkqlvggg avlvyafvvs giiglvvdkv mgfriheehe isgidliiha etaydlhata
      421 gsrsgssfld nltrhddneq rdrp
//
LOCUS       WP_010833732             735 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent DNA helicase RecG [Nocardioides sp. CF8].
ACCESSION   WP_010833732
VERSION     WP_010833732.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Singleton,M.R., Scaife,S. and Wigley,D.B.
  TITLE     Structural analysis of DNA replication fork reversal by RecG
  JOURNAL   Cell 107 (1), 79-89 (2001)
   PUBMED   11595187
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..735
                     /product="ATP-dependent DNA helicase RecG"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=79007
     Region          7..716
                     /region_name="RecG"
                     /note="RecG-like helicase [Replication, recombination and
                     repair]; COG1200"
                     /db_xref="CDD:440813"
ORIGIN      
        1 mvsitpespv asvfgrspkr klveeglgit tvgellrhfp rryvettels evgtpevgql
       61 lsvvgevtss avrpfqrgrk tqfrtevrir tngpsfslsf fspyagqans yaeemapgsr
      121 glftgkakif ngswqleqph qlmfgdgege detlskllpv ypltnklyvw dlikvirval
      181 dlvtdvpdml trelrerydv ldvmtalrlv hgpddyaqag aaqrrfrfee alvlqlvlar
      241 rraaqralga qarlggggll aafdarlpfe ltggqreiga vleaelaeph pmnrllqgev
      301 gsgktlvalr amlrvvdsgg qavllaptev laqqhhrsis amlgdlaqgg mlggaadgts
      361 valltgsmsk aakdqaldlm asgeaglvig thalledtva fadlglvvvd eqhrfgvkqr
      421 aaltdkagsp phvlvmtatp iprtvamtvf gdletsvlte lpagrapiqt nvvplvdqps
      481 wigrvwervr eevakghqvy vvcprisgdt leegesdqld vdedgevttk kvplaavedl
      541 heelaggalq glrtailhgk lppdekdrtm rafaagqidv listtvievg vdvhnattmv
      601 lldadrfgvs qlhqlrgrvg rgglpglcll vtraeadtpa rerldavast tdgfelskvd
      661 leqrregdvl gasqsgfrss lvtlrvlrde ktiirareaa dellaedadl apypvlaaav
      721 aavetsqqse fvdks
//
LOCUS       WP_010832432             843 aa            linear   BCT 01-JAN-2025
DEFINITION  MMPL family transporter [Nocardioides sp. CF8].
ACCESSION   WP_010832432
VERSION     WP_010832432.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..843
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=88958
     Region          12..813
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 masllyrlgl gaarrpiaiv iawllvlaav taamvsfqrp ltnefelpds efaavldelg
       61 eqipevaggt gtvvlhsedg ftpaqrrvid etmaqwrtlp hvtgtvdpfe tqrqldqssa
      121 dlaegeqkli dgrkkyekga rklsrlrwlv gegerdiarl qrtdpdnatl pyrisgqael
      181 damladgerk ldrartrler gqdkytdgat lrglgdgvrm vsedgttalv qvrfdesmqq
      241 ispddlalvp qageqledag vevdygqelv fvtqvggige iigvavaavv llvmlgsfvm
      301 aglplaiafa gvgaslmgam althwldiqq mapvlgamlg lavgidyalf ivnrhrrqla
      361 dvvrggavtt reeirhsial atgtagtavv vagatviial aallvsgipt liqmgllaaa
      421 tvtvtvlval tltpallsla grravprkav astaphrdgw pekwvgvvtr rapaaivavv
      481 ivmgalavpa lslrlglpdg gsesrdstaf qayervadaf gtgangpilv satletpiaa
      541 gelvgteari geeiaavegv rdvlpigvse drrtvafqvv seegpsaert valvdalrgp
      601 vteslagegv dlgvtgqava nievserlag alplyialvi glslvlltiv frsvlvpila
      661 tagfllsvva sfgvivavyq wgwlggvfdv hnpgavfsfm ptlligilfg lamdyqmflv
      721 sgmresyvhg qtagqavrng fasgarvvaa aalimvavfs gfvfshmtma rpiglglavg
      781 vlldaflirm tltpavmsll gdkiwwmpvw ldrllphldv egsalvdkqr pprrsasred
      841 vlv
//
LOCUS       WP_010833761             190 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010833761
VERSION     WP_010833761.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13273981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /calculated_mol_wt=20605
     Region          2..187
                     /region_name="PRK13756"
                     /note="TetR family transcriptional regulator"
                     /db_xref="CDD:172294"
     Region          5..>90
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mryhrddvla hahqlvatyg lgaltmrrlg aelgvqpsai yhhfankqtl laavaeeilr
       61 rgqrprtadd adwtgrvhev caelrdamla ctdgadvvat vwafgmgvqg ppleleailr
      121 eaglddqlal vgsrtllhyi fghafeeqta iqaisagave reldslpdfw tglevvvdgl
      181 rsrveaavra
//
LOCUS       WP_010833756             134 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Nocardioides sp. CF8].
ACCESSION   WP_010833756
VERSION     WP_010833756.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..134
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14713
     Region          8..116
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mtvemhnvtf dcadarklad fwaallgwsv fhdddpevvv apsfptrglg llfipvpegk
       61 kvknrlhldv aptdctrdeq veqaivlgaa ihedhrnedg tgwvtmtdpe gnefcierst
      121 vekggpqrgv frlg
//
LOCUS       WP_010833770             465 aa            linear   BCT 01-JAN-2025
DEFINITION  amidase [Nocardioides sp. CF8].
ACCESSION   WP_010833770
VERSION     WP_010833770.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..465
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48716
     Region          1..463
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mpplhdltal eqgelvrrgd vtpldlvehy leradtvgaf vtstpeqara harrlrdggr
       61 pegagplwgv ptaikdlhpt agvrttfgsa aydgfvpdes ddlvltveaa gmpslgktnt
      121 pefgspcyte pdvappavtp wdprrtaggs sggaaaavaa glvpvapgsd gggsiripas
      181 ccglvglkpt rgrisgapry gdpvglatpg plartvrdaa alldvlagrr vgdpswappp
      241 ldsfltacdr dpgrlrvarf itpvitdsev epvvrtawde asamlaglgh dvvdidvplp
      301 reavatfevc wavltamaev pegreheirp ltrwlsekgr avsapefgla igqlrryaad
      361 alaslapydl vltptvatlp plvgdlrdde dpaadfeaqk rftpwtsawn vtgmpavslp
      421 lhwtpdglpv gvmlaarpae eelllsvsaq veaaapwagr qppgw
//
LOCUS       WP_010833767             376 aa            linear   BCT 01-JAN-2025
DEFINITION  8-amino-7-oxononanoate synthase [Nocardioides sp. CF8].
ACCESSION   WP_010833767
VERSION     WP_010833767.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..376
                     /product="8-amino-7-oxononanoate synthase"
                     /EC_number="2.3.1.47"
                     /GO_function="GO:0008710 - 8-amino-7-oxononanoate synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_process="GO:0009102 - biotin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38249
     Region          3..371
                     /region_name="PRK05958"
                     /note="8-amino-7-oxononanoate synthase; Reviewed"
                     /db_xref="CDD:235655"
     Site            order(100..101,104,167,196,199,228,231)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:99747"
     Site            231
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99747"
ORIGIN      
        1 mgawetwltd eavrrdaagl trrlrprgsd ddvidlagnd ylglsrdpvv vaaaadaart
       61 wgagagasrl vtgtlslhat leqelavflg qpaalvmstg yhanlavvta ladrdtlivs
      121 dahihaslid aarlsraeia vtphgdvaav dqalagagsr raivlaesiy svlgdaaplt
      181 dlasvcarhd allvvdeahg lgvagtageg lvkalglasa phvvvtatls kslgaqggav
      241 lgspalvhhl vnrarpfifd talnpaatgg alaalrvlrs rpdlpgvvra rveslaarlg
      301 vdvpagavls vpmtsphvai aaqaeclehg vrvgcfrpps vpdgisrlri ttnagvpdda
      361 wakagdllak vveahr
//
LOCUS       WP_010833798             182 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Nocardioides].
ACCESSION   WP_010833798
VERSION     WP_010833798.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..182
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20010
     Region          7..87
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mgqglpvtsy allglltfgd altgyelkqr adatlrfywv spamsqvyse larlaehglv
       61 tpsgegrgtt ytisdagrea lttwmresap gfpvlkhpva lrlllghvvd rettvamlrd
      121 hvlalekeea alvevrdglr ghdgpgeifr hpslvadwgl dyfenerriv gdlirrlede
      181 gp
//
LOCUS       WP_010833792             137 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Nocardioides].
ACCESSION   WP_010833792
VERSION     WP_010833792.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..137
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14843
     Region          2..126
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 mdqrisfitl avrdlgesrk fyldglgwkp cldqpgevlm fdvgdklils lwdvdaftae
       61 vgqppgggvp pitiahnlat tdgvdrvleq arvagaaqvt davqrdwggy sgyfvdpdgf
      121 rweichnpse igqkvlp
//
LOCUS       WP_010833810             176 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SigE family RNA polymerase sigma factor
            [Nocardioides].
ACCESSION   WP_010833810
VERSION     WP_010833810.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..176
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19110
     Region          11..163
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 marppsgarh dgdftefvqa swpglyrtay lllgdrglae dlaqtalakt yaawsriddr
       61 aaapayarrt lvntasswfr kkgwrnelpt ssmpesayav dpstrpavid algqlpprqr
      121 avvvlryyed lsvvetadal gcstgtvksq tyeafaklrv llgdavipet lgahhd
//
LOCUS       WP_010833834             392 aa            linear   BCT 01-JAN-2025
DEFINITION  LCP family protein [Nocardioides sp. CF8].
ACCESSION   WP_010833834
VERSION     WP_010833834.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..392
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=42233
     Region          127..382
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 maerppgkgg peegtpeydw lygsrgtarp ddatrmvpqq dragerpdet rimpaqprat
       61 prtppaapap kpartrrrpr frfgfvklal llwlvfmvav pfwawsnidk vdaepsgarp
      121 ddqpgtnyli vgsdkaddlt aeqqkalgtg prggtntdti ivlhtgsgad trmsiprdtl
      181 aevpghgtqm inaafslgka pllvasvekl tgihidhyve lgfgsvintv dalggieicp
      241 ktdmddprar ldikkgcqev dgetalaysr sryvsalsdl drvgrqgevi galgaeaksp
      301 wtflnpvryw rltdasakai ridedmgpis lgrfalamtg dsrtctmpnm aapsdpnriv
      361 adpdrapavf kaiinddavp kslctptgra rq
//
LOCUS       WP_010833961             375 aa            linear   BCT 01-JAN-2025
DEFINITION  carbon-nitrogen hydrolase family protein [Nocardioides sp. CF8].
ACCESSION   WP_010833961
VERSION     WP_010833961.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163270
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..375
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41163
     Region          6..236
                     /region_name="nitrilase"
                     /note="Nitrilase superfamily, including nitrile- or
                     amide-hydrolyzing enzymes and amide-condensing enzymes;
                     cd07197"
                     /db_xref="CDD:143587"
     Site            order(42,115,119,123,148..149,151..152,173)
                     /site_type="active"
                     /db_xref="CDD:143587"
     Site            order(42,115,148)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143587"
     Site            order(116..119,122,129..131,149,151..155,158..159,
                     181..182,184..186,188..189,207)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143587"
ORIGIN      
        1 mslamatcqp tassdprang aevrrmlrva aaagarlahf pegflsgyav advaawedvd
       61 wsavrrelee vaalagelgi wvvlgsahpl tpphwphnsl yvisdqgelv drydkrkcsn
      121 teltrfytpg fepvvvdvdg frfglalcie vnfedlfaey rrlwvdcvll saypvdsife
      181 tkarahaaih nywlslsvpa qrthlfhsgl igphgevlad agseaglvig aldrddpalh
      241 valdlakpwr alaragdiye errvddersr vrtgtaeakv vtlcgstrfe aefaevnqrl
      301 tmdgcvvisl gmfgtvdgsd lkerlgalhf qkirmadevy vvdpggyvge strreiayae
      361 slgkpvryls rersa
//
LOCUS       WP_010833937             277 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Nocardioides].
ACCESSION   WP_010833937
VERSION     WP_010833937.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..277
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28387
     Region          78..270
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mgnhrahrgp rrdlsaapva grrkaskppa rhpflsalps apiivgvaal avsaggavsa
       61 adadlvgqvt sqtgsmaaag stglanvapi ahrdaivsrd srrdaladaa neelvaqaea
      121 qaeqqhaalk emaraaeqqs akikenqwvl plenyrisat fgassylwss vhtgldmsas
      181 igstirsvan gvvtetgydg sygnktvitl ddgteiwych qtsflvsvgd tvrggdaigt
      241 vgstgnstgp hlhievrpgg gdpvdpftal vehgiap
//
LOCUS       WP_010834191             424 aa            linear   BCT 01-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Nocardioides sp. CF8].
ACCESSION   WP_010834191
VERSION     WP_010834191.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..424
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42802
     Region          24..382
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mapqpgvgrl rrsaghpaar llrasllaqv alvvsgplvv rmlgvtdrgq lalvfavvll
       61 vsqvgvaglp aavtwfvasr rldaaaflar lqrqfvrqvv acsvlaaavv llldiadhpl
      121 prvwllalvv algvaavmaa mlgmaalqgq qrfgvlarlq plpavsyala talllvtggg
      181 tvalllainl agwavvavvs lrlvargvpg dgtefpapga vrsyarsamv ttaapidtlg
      241 ieqllvglig ghyllglfti gwafetgpvv vlvalasfvg prlstlpapq raafvrlwll
      301 vavgvgvaac laiqvvlapl lvlafgaeae pavplarvlv aagvvlglrr vtssclvglg
      361 rastatlaem aglalmlagf avmavasvgg typgwvllva gtvtlvgqla vlaraassge
      421 pasa
//
LOCUS       WP_010834205             331 aa            linear   BCT 01-JAN-2025
DEFINITION  inorganic phosphate transporter [Nocardioides sp. CF8].
ACCESSION   WP_010834205
VERSION     WP_010834205.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..331
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34032
     Region          14..330
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 meiaiiiavv vvalvfdytn gfhdaanaia tsvstgaltp kvalamaavm nfvgaflgqk
       61 vattvsdtid pgtgthglvi vmaglvgaia wnlttwyygl psssshalig glvgaavaag
      121 asanwglvle kvvipmllsp lvafglgfav mlaimwafrn ahparanrgf kiaqtisaga
      181 malghglqda qktmgvifla lltggyvaes dglplwviia aataislgtw sggwrimrtl
      241 grriihldpp rgfaaesvaa svlyttayvf eapistthti tsavmgvgat krlsavrwgv
      301 aksiltawvl tfpaaalaaa vtywiaalfl p
//
LOCUS       WP_010834226             164 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [Nocardioides].
ACCESSION   WP_010834226
VERSION     WP_010834226.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..164
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17636
     Region          1..164
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mpeqtfilng esvtvdvedd vrllwvlrdv lgvtgpkygc ginvckacts hingrafnpc
       61 avpvgdlqpg dkvttieglp eavpavkrgq nglhpmqeaw lardvpqcgy cqpgqimaav
      121 alvnktkreg rtitdadldt irnicrcgty trirsavrdg atkm
//
LOCUS       WP_010834263             455 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [Nocardioides].
ACCESSION   WP_010834263
VERSION     WP_010834263.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..455
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49147
     Region          1..455
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mstsidalre qvraqiitad dsayddarav hngmfdrkpl ailraeqvad vvagvnyard
       61 agvelavrgg ghsapgfgst dgglvidlsg mrgvhvdpra ltaragggat wgdynyatha
      121 yglastggiv sttgvggltl nggigyltrg qglsidclas aevvtadgqv rtasaeenpd
      181 lfwairgggg nfgvvtsfef nvqpvkdayv glffyeleha gdllrffrdw iqdapreyga
      241 fpafqvappl pfvpedrhgd tfcvavvhwt gpmdegekam qpfrdlaprv aemcdvwpyp
      301 qlngafdglf pkgirsywkg ayvmeltdea ieahlahgph apdasstmhl ypingaahdp
      361 spsdtafayr satyaavils awqdpaldve rrqwvrdyyd aisphsergg ylgfmaedda
      421 dkvednfagn yprltevkra ydpdnlfrln qnivp
//
LOCUS       WP_010834299             282 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Nocardioides sp. CF8].
ACCESSION   WP_010834299
VERSION     WP_010834299.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..282
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31000
     Region          11..275
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mtsvpslplh dgtsipqlgf gvyqvppaet aatvlmafev gyrhidtaqm yeneegvgaa
       61 ikdsglardd lyittklnng fhlpddarrs leeslsrlgl dqvdlflihw plptrydgdf
      121 vstwetlval qeegkarsig vsnfqpshld eivaktgvvp vvnqvevhpf fanedvraan
      181 arhgvvteaw spiaqgkvnd ddvmgelasl vgkspaqval rwhlqrgdiv fpksmhrerm
      241 qqnfdlfdws ladthmaaid eldagsagrl gpdpdlfdyi pr
//
LOCUS       WP_010834292             243 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: pentapeptide repeat-containing protein
            [Nocardioides].
ACCESSION   WP_010834292
VERSION     WP_010834292.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..243
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=25700
     Region          <62..>204
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
     Region          <152..230
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mnlpvlqadc sqcfalccvl lpfqkgesfp etkpsgvpch nlddrdrcgi hatlredgws
       61 gcvafdcfga gqqvaqvtyg gvswreggnl gemaavlsvm rqlhemlall deavrrsagp
      121 agpwlervvg lvggtpeell aldidqlrle vgavlgeasr gvrahwtdal dltgqdlagr
      181 dlreldlrga alrgavllga dlrgcdltda dllgadlrga dargaelsea lfltvaqrav
      241 lrv
//
LOCUS       WP_010834313             190 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Nocardioides].
ACCESSION   WP_010834313
VERSION     WP_010834313.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..190
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21082
     Region          2..172
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 matlvfearg gsqsawnqlv erllplvtsl irrhrvtgad addvnqtvwl rlvehldrid
       61 epralpgwls tvtrneclrm lekrgrvipt dpqtsptfer addapdvada llvserqnal
      121 vdallelpae rrelllllte dppltyaeis rrsgipvgsi gptraraiqq lrnttalrhl
      181 appapdgrnr
//
LOCUS       WP_010834345             869 aa            linear   BCT 01-JAN-2025
DEFINITION  (Fe-S)-binding protein, partial [Nocardioides sp. CF8].
ACCESSION   WP_010834345
VERSION     WP_010834345.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 869)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..869
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..>869
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
     Region          287..722
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mqifaivvsl altvaamall vpavrkmlgv irsgqpapgr adnpvgrglt mlketflhtr
       61 mlqwhwigim hwfvymaflf lstavlaayf qlfkadfawp iighwypyew fsefiglmst
      121 igilvlivyr qmhhpkregr ksrfygstmw qayfveylal legsailfvr gaewkldeha
      181 grshyplssw igdalyptsv tslenliyai atfkialami wlmviarnit mgvawhrfta
      241 wfniffkres dggtalgamk pltsggkait lddiddlded silgvgsied fswkgildft
      301 tctecgrcqs qcpawntekp lspkllimal rdhayekage ktaaasgtsd ttdgqvavae
      361 ksligsgmed nwfynpegad yvidedvlws ctscgacvqq cpvdiehvdh imdmrryqvl
      421 vesnfpaeln glfkglenkg npwnmsstar mdwakglefd vpvvgedles lesvdwlfwv
      481 gcagayedra kkttravael lnmagvtfgv lgngetctgd parragnefv fqglaaqnve
      541 tfkeykvkkv vstcahcfnt lkneykdfgi elevvhhtql lnrlvregkl tpikegagaa
      601 krsityhdpc ylgrhndvyt pprelleilp gaefkemern seksfccgag garmwmeeni
      661 gerinlnrtk eavgtgadqi avgcpfcrvm ladgltaeqa ggnareevev ldvaqmllas
      721 vkgesatrap aaapaaaaaa ggtatatata dvatkaepea gdvtitedtv tdtadagpaa
      781 kasggsslfd tpaseapaap assggslfdt papeapaapa ssggslfdtp apeapaapaa
      841 passeapass ggslfdltpe ptkaapaap
//
LOCUS       WP_010834349             279 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Nocardioides sp. CF8].
ACCESSION   WP_010834349
VERSION     WP_010834349.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..279
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29903
     Region          10..263
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtsatapatr lsasrltlgy adgpivtdld lqvpdgkvtv ivganacgks tllrglarll
       61 kpqsgvvlld gevihrqptk hvarilgllp qnpiapegvt vvdlvgrgrh phhgafqrwt
      121 svddeavaea leltdtlgla drvvdelsgg qrqrvwiama laqgtdllll depttyldva
      181 hqvemldlla dlnarrgtti vmvlhdlnls aryadhlval rdgavvaegt prqvvtedvv
      241 rtvfgldnrv iddpvshtpl vvpvsrhlrq aqpptqelp
//
LOCUS       WP_010834365             289 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Nocardioides sp. CF8].
ACCESSION   WP_010834365
VERSION     WP_010834365.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..289
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30239
     Region          6..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mttpairata lnktfrstdg tsvvavehvd ltvqpgeiva flgpngagkt ttvdmllglt
       61 sptsgtiely gatphhavvd grvsavlqtg glltdftvre tiqaiaalhg rpdrvdavie
      121 rtglaplasr lvkacsggeq qrlkfalalv pdpdliilde pttgmdvaar qafwdtmrad
      181 aetgrtivfa thylaeadaf adrtvlmadg rivadgptae iraeyggrtv tfrppshvvd
      241 gqgideawld avraavaplg vtelevasas leaaflalts tteaqealr
//
LOCUS       WP_010834368             214 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Nocardioides sp. CF8].
ACCESSION   WP_010834368
VERSION     WP_010834368.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..214
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=22428
     Region          18..214
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvwpimlggv lirvfgdkaq eatetrnrla lvaerervar dvhdvlghsl talsikaela
       61 srlievdpar akaelesiqe tarqalaevr atvgglrasn leaelatapr vladagirtq
      121 vlgsvaetdp rhrallawvl resvtnvvrh aratsvsvel gptglvvadd gagfeatggr
      181 egnglrgmre rvsaaggtlq vsggpgtrve vvlp
//
LOCUS       WP_010834379             170 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Nocardioides].
ACCESSION   WP_010834379
VERSION     WP_010834379.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..170
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18617
     Region          13..152
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mtiafrpvap ridaalihaw vteprarfwg mldrdldevr diytwiveqp hltasiasvd
       61 dvpvallqty dpfvdeigdf ydrrpgdlgl hlfladepar aghtttvvtt avrsllarpg
      121 verivlepda anersialli rlgaalgpvv elpgktaqfv fldeanlvsp
//
LOCUS       WP_010834382             177 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Nocardioides sp. CF8].
ACCESSION   WP_010834382
VERSION     WP_010834382.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..177
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19019
     Region          9..153
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mrltiepldl ardlatlqaw vthprsvfwg mqgatldevh aeyariaddp hheallgrad
       61 gspvflmery dpfhspladl pelaagdvgm hllvaptdtp vpgftgavmr rvveecfadp
      121 avarvvvepd vrndkiaaln aavgfrvvrp vrlpdktaaf stctradfva sqlggva
//
LOCUS       WP_010834395             181 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Nocardioides].
ACCESSION   WP_010834395
VERSION     WP_010834395.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..181
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19967
     Region          1..181
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtpddiddla rrardgdrda megllaavrp ralnvcrgvl pysgdsedac qeallnistk
       61 lgswngqgrf ttwmhvvaln sarttyrklk nqavptdfeg ghhdrpdprt tsviagtrld
      121 lleametiek dhpqyvepll lrdvygmayd diaqligvpl gtvkaqihhg rklarpllrg
      181 e
//
LOCUS       WP_010834416             422 aa            linear   BCT 01-JAN-2025
DEFINITION  anthranilate synthase component I family protein [Nocardioides sp.
            CF8].
ACCESSION   WP_010834416
VERSION     WP_010834416.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Kerbarh,O., Bulloch,E.M., Payne,R.J., Sahr,T., Rebeille,F. and
            Abell,C.
  TITLE     Mechanistic and inhibition studies of chorismate-utilizing enzymes
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 763-766 (2005)
   PUBMED   16042594
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Dosselaere,F. and Vanderleyden,J.
  TITLE     A metabolic node in action: chorismate-utilizing enzymes in
            microorganisms
  JOURNAL   Crit Rev Microbiol 27 (2), 75-131 (2001)
   PUBMED   11450855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..422
                     /product="anthranilate synthase component I family
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=45889
     Region          3..420
                     /region_name="TrpE"
                     /note="Anthranilate/para-aminobenzoate synthases component
                     I [Amino acid transport and metabolism, Coenzyme transport
                     and metabolism]; COG0147"
                     /db_xref="CDD:439917"
ORIGIN      
        1 msdpidffaq vaaehprcfw ldgggarews gqrsligwld eddvsltyaa ssglvtrhag
       61 arsevvgddv favleetmap geqwfgyfgy acrpdlparp dpalpdavwm rarnvrifeh
      121 gplqesppkr gllhglavat pkkretspts pprsyaagfa dvqeqlragn syevnltyrl
      181 arrdsvtpae aylrlrevnp apyagflqhd veghrawlls ssperyalit pdrtlqtkpi
      241 kgttprgsta aeddalrtsl atdpktraen lmivdllrnd latvcevgsv evpalmqves
      301 yesvhqlvst vsgrlrddvs tvgalralfp agsmtgapkl rtmeiideve etargvyaga
      361 fgwisgdgpa dlgvvirslm tagdgswtlg tgggitvrsn ledewaesrw kaerllsvfe
      421 sd
//
LOCUS       WP_010834445             199 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Nocardioides].
ACCESSION   WP_010834445
VERSION     WP_010834445.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..199
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21496
     Region          4..199
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mtttarvpqe qrsramrlrl leatveclve rgysgtsttl vstragvsrg aqlhhfptkn
       61 dlvvaavehl tvlrgaeiad avaglptgrr rtravltmlg dhfaspvfta alelwvaart
      121 deallaavgp leqrvgrevh rltvealgad esqpgvrelv qatldlvrgl glantisdda
      181 arrrrildhw advldrela
//
LOCUS       WP_010834447             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Nocardioides].
ACCESSION   WP_010834447
VERSION     WP_010834447.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..239
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24947
     Region          1..227
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msavvlhldn vtrvhgegpt evhalrgvsf racagelvav mgpsgsgkst lltiagglde
       61 ptsgtvsveg avlgslgnag rarmrrtsig yvfqdfnlip altaaenval preldgersk
      121 aarllalaal eevgivdlad rfpdemsggq qqrvaiarai vgerrlilad eptgaldtdt
      181 geeilrllrn rcdagaagvl vthearhaaw adrvvflrdg livdesgadv adellevtp
//
LOCUS       WP_010834448             208 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010834448
VERSION     WP_010834448.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 208)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..208
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23051
     Region          1..93
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          100..183
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 msvrqamlal lepgpmygyq lraefeqrtg atwplnvgqv yttlsrlerd gliehdehvd
       61 aagaadatdr aaqvmyritp sgrgevsawf ttpvprtqpp rdelaiklai avtlpgvdvt
      121 sliqqqrtat mtalqdytrl krtgrasrpd qpedlawslv ldslvfdaea eirwldhcea
      181 rlrraaaegh lhvparptrt adseevrp
//
LOCUS       WP_010834458             168 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Nocardioides].
ACCESSION   WP_010834458
VERSION     WP_010834458.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..168
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18536
     Region          7..146
                     /region_name="CatE"
                     /note="Catechol-2,3-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2514"
                     /db_xref="CDD:442004"
ORIGIN      
        1 mpipavrlnh avlfvadlqr sidfytsvfd mevaatepra haaflrlthg gnhhdlglfg
       61 igadqvkrpg iglyhlawqv dtieqlelar lslanhdayt gesshgatks vygkdpdgne
      121 fevmwmlpre dwgrfeheap verldlaaev rawagvrtaa dnipvvar
//
LOCUS       WP_010834465             176 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010834465
VERSION     WP_010834465.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..176
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=19837
     Region          1..87
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          93..174
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 malehallva lserpgsgle lagrfeksig ffwhathqqi yrvlgrmetn gwlsvetvaq
       61 sgrpdrkvya vsptgaqvla dwlveplpme afrsdlavkl raasygeraa llrrvretlg
      121 dhetrlahyr elekrdypvp adlagpdldq ylvlrggirl eefwigwlne yleaha
//
LOCUS       WP_010834479             524 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Nocardioides sp. CF8].
ACCESSION   WP_010834479
VERSION     WP_010834479.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..524
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=54045
     Region          65..524
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mteqiemhaq rwgdpaaats vpdearglie lafgindspa vsgatppapa igaealaale
       61 avvgadqviv ddavravrtr gkstpdllka ragdlsdapd vvvrpadqae ieallavava
      121 hnlavvpfgg gtsvtgglva araayagvvs ldlvrmksll svdkesmtat lepglrgpea
      181 eallaeqgvt lghypqsfef atiggfaatr ssgqssagyg rfdavvvamt vvtpsgtiav
      241 gsapanaagp dlrqlflgse gafgvissvt vrvrelpavk eyvgwrwpsf aagatamrtl
      301 aqagllptvi rlsdeaetai nladpssigg agdpgcmmit gfegtqsavd akraavtail
      361 telggtdlge epgqkwahgr fnapylrdsl ldlgvlvetl etatfwsnre rlyadvktal
      421 etslgegsiv lchishvyet gcslyftvat kekedplaqw aaaktaasda midagatith
      481 hhavgtdhkp wfereigpvg vqtlravkas ldpsgilnpg vlip
//
LOCUS       WP_010834495             142 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Nocardioides sp. CF8].
ACCESSION   WP_010834495
VERSION     WP_010834495.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..142
                     /product="VOC family protein"
                     /calculated_mol_wt=14731
     Region          5..134
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(5..10,27,59..60,63,80..85,87,93,122,132)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 maarlnpyvn vldgqareal efyqsvlgge ltvmtfgdmg tqgdlaiqvm hgqletpagf
       61 tlmvadappe mvqvtrgnnv sislsgtsed gealrgyfag lsdggqvvqa lepapwgdef
      121 galvdkfgin wlvniagdga pa
//
LOCUS       WP_010834510             133 aa            linear   BCT 01-JAN-2025
DEFINITION  YbaB/EbfC family nucleoid-associated protein [Nocardioides sp.
            CF8].
ACCESSION   WP_010834510
VERSION     WP_010834510.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Cordeiro,T.F.V.B., Gontijo,M.T.P., Jorge,G.P. and Brocchi,M.
  TITLE     EbfC/YbaB: A Widely Distributed Nucleoid-Associated Protein in
            Prokaryotes
  JOURNAL   Microorganisms 10 (10), 1945 (2022)
   PUBMED   36296221
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Cooley,A.E., Riley,S.P., Kral,K., Miller,M.C., DeMoll,E.,
            Fried,M.G. and Stevenson,B.
  TITLE     DNA-binding by Haemophilus influenzae and Escherichia coli YbaB,
            members of a widely-distributed bacterial protein family
  JOURNAL   BMC Microbiol 9, 137 (2009)
   PUBMED   19594923
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..133
                     /product="YbaB/EbfC family nucleoid-associated protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13927
     Region          11..108
                     /region_name="YbaB"
                     /note="DNA-binding nucleoid-associated protein YbaB/EfbC
                     [Transcription]; COG0718"
                     /db_xref="CDD:440482"
ORIGIN      
        1 mtqtppsepw lddlrretar hleqiarvqd elstlygeah taegrvrvrv naagrptalt
       61 lepsalslpp sdlaaailra vddatarage rlaelvgtlv paadldamla grptdadrva
      121 vraeldalsa dgg
//
LOCUS       WP_010834652             199 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010834652
VERSION     WP_010834652.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..199
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21386
     Region          3..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          <142..184
                     /region_name="TetR_C_32"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam19344"
                     /db_xref="CDD:437176"
ORIGIN      
        1 mtgaerreql iavartlfse rgfegaaiee vaaraqvskp vvyehfggke glyavvvdre
       61 vqtllaimrg sltagtsriv leqaalalls yveenpqgfr ilvrdspige asfqtilgdv
      121 asrvegllad tfkrtgldak napmyaqmlv gmvaslgqww ldtrkparev vaahvvnlaw
      181 nglsgldgdp vlysetpea
//
LOCUS       WP_010834665             177 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: dihydrofolate reductase family protein
            [Nocardioides].
ACCESSION   WP_010834665
VERSION     WP_010834665.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..177
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19369
     Region          1..166
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mttiyytgcs ldgfiatpdh sldwltsrdi deagpmhyag freqigacvm gattwqwild
       61 hddepwgdla tyvmthrdfe pvtsvtftad avedvhaqav eraagkdlwl vgggelvgqf
      121 hdaglldevw vqyapvtlga gtpvlprhve lkleevarnr dfvcarhtvv kpatias
//
LOCUS       WP_010834871             328 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Nocardioides sp. CF8].
ACCESSION   WP_010834871
VERSION     WP_010834871.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..328
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35162
     Region          8..214
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 msestrritq varheyraal rsrvlvilia ilvastigsv ligasdyaaq ladyntyraa
       61 aeaqgltria psplavlall rgaleyieil gaiiaitlgy lsvsrervnr tlpllrsrpl
      121 tgaelatgsy lgalgifatl ilatalvgvv slgvighdwi spiqvlrvtl aclaallyls
      181 afyclgaiat arakvpvngl tialgiwlvv vlvlpqigdt ldadnqlpgg lfqalgldhd
      241 gelavlthft gyervrtgie easlakhfer fafamtdvke ryrpyglswl lnetlnniaw
      301 llayaavlfa alrrtlsrqq pietggns
//
LOCUS       WP_010834942             156 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Nocardioides sp. CF8].
ACCESSION   WP_010834942
VERSION     WP_010834942.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..156
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16746
     Region          4..152
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 mtdhtyaial swtgntgrgt knlrsysrnh dvaadglpti aassdpafrg dpsrwnpeql
       61 ylasiaqchm lwhlglaaqa gvtvlgyedr ptglmieead gagqfdsvtl hpvvtiaads
      121 daqtaeelhh rvadycfiar svqtpihhva tiehas
//
LOCUS       WP_010834939             256 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Nocardioides sp. CF8].
ACCESSION   WP_010834939
VERSION     WP_010834939.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..256
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25986
     Region          13..>101
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mpdgpaeltl viaaiigvsa vlqtstgfgf ailsapllta lvggpmavtt ititgatvda
       61 lilggrrtlp rpdwrivvll alwsvpgmvl galalarmpq sglqllvaaa vllavahrvh
      121 adrcdlegsp qatrvrgrgw hapvagltsg algtsttlag ppvvmyltrr ladplttrdt
      181 lvalslvrlp lailvltrag awapptsglf vilaagvvgc vvgqgvharl dhrsyqratl
      241 gllavaaata tiaavi
//
LOCUS       WP_010835217             285 aa            linear   BCT 01-JAN-2025
DEFINITION  DNA adenine methylase [Salmonella enterica].
ACCESSION   WP_010835217
VERSION     WP_010835217.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Timinskas,A., Butkus,V. and Janulaitis,A.
  TITLE     Sequence motifs characteristic for DNA [cytosine-N4] and DNA
            [adenine-N6] methyltransferases. Classification of all DNA
            methyltransferases
  JOURNAL   Gene 157 (1-2), 3-11 (1995)
   PUBMED   7607512
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10015703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..285
                     /product="DNA adenine methylase"
                     /EC_number="2.1.1.72"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009007 - site-specific
                     DNA-methyltransferase (adenine-specific) activity
                     [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /GO_process="GO:0032775 - obsolete DNA methylation on
                     adenine [Evidence IEA]"
                     /calculated_mol_wt=31863
     Region          1..261
                     /region_name="dam"
                     /note="DNA adenine methylase (dam); TIGR00571"
                     /db_xref="CDD:273146"
ORIGIN      
        1 mstilkwagn ktaimpelik hlpagprlve pfagscavmm atdyphylva dinpdlisly
       61 naiksgpell isigkdlfak nksaedyydi rkefnhgrdw pvdcraamfi ylnrhcyrgl
      121 crynlsghfn vpygnyknpy fpeneirafa ekaqratfic asydetlall ktgdvvycdp
      181 pydgtftgyh tagfteddqy hlasilerrs seghpvivsn sdtslarsly rnftrhrita
      241 krsmgvaagd gksaveiiat skprywigfa pagghdccvk hevrv
//
LOCUS       WP_010835336             434 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Salmonella].
ACCESSION   WP_010835336
VERSION     WP_010835336.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47712
     Region          7..414
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(21..22,25..26,29,61,111..112,114..116,119,139,
                     142..143,146,239,242..243,246..248,251,279,283,341..342,
                     346,350,366,369..370,373..374,377)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mkmtklrwwi iglvcvgtiv nylsrsslsv aapammkelh fdeqqyswvv safqlcytia
       61 qpitgylmdv iglkigffif allwslinma halaggwisl aflrglmglt easaipagik
      121 asaewfptke rgiagglfni gtsigamlap plvvwamltf adsgigtema fvitggigvl
      181 faitwfliyn spnkhpwith kelryiedgq esylqddnkk pavkeivkkr nfwalvitrf
      241 ladpawgtls fwmplylinv mhlplkeiam fawlpflaad fgcvaggfla kffmekmhmt
      301 tinarrcsft igavlmisig fvsittnpyv aialmsiggf ahqtlstvvi tmsadlfkkn
      361 evatvaglag saawmgqlsf nlfmgalvai igygpffial slfdiigaii lwvlikdpek
      421 hhppmteqpl ashr
//
LOCUS       WP_010835425             290 aa            linear   BCT 01-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Salmonella enterica].
ACCESSION   WP_010835425
VERSION     WP_010835425.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..290
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32411
     Region          4..281
                     /region_name="HAD_YbiV-Like"
                     /note="Escherichia coli YbiV sugar
                     phosphatase/phosphotransferase and related proteins;
                     belongs to the haloacid dehalogenase-like superfamily;
                     cd07518"
                     /db_xref="CDD:319820"
     Site            order(9..13,44..46,67,148,150,205,213,235..237,239..240)
                     /site_type="active"
                     /db_xref="CDD:319820"
ORIGIN      
        1 mtvnvvvtdm dgtflddakq ydrvrfmaqy qelkkrnief vvasgnqyyq lisffpelkd
       61 eisfvaenga lvyehgkqlf hgeltrhesr ivigellkdk qlnfvacglk sayvsknape
      121 tfvalmakhy hrlqpvndyh diddilfkfs lnlpdeqipl vidklhvsld gimkpvtsgf
      181 gfidliyvsl agimtpvtsg fgfidliipg lhkangisrl lkrwnrspqn vvaigdsgnd
      241 aemlkmahys famgnaadni kalsryhtdd nnhqgalnvi qavldgtdpf
//
LOCUS       WP_010836087             187 aa            linear   BCT 01-JAN-2025
DEFINITION  potassium channel family protein [Rhodococcus rhodnii].
ACCESSION   WP_010836087
VERSION     WP_010836087.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..187
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=19517
     Region          98..>159
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mpddhdgasr hhdpvahdag arsavravaa rscltvvaat vvyftapvqd lsgvpgvlwl
       61 vagiaivgvl awlqlraitr srvpalrsle gaavvlpvyl lgfatayyvl aaavpgsfda
      121 vvtrigslyf tlsvfatvgf gdivavtdra ralvvvqmig nllllglgvr vvvalvrwsr
      181 dhrppts
//
LOCUS       WP_010836116             342 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010836116
VERSION     WP_010836116.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..342
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36908
     Region          10..144
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          181..310
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 marqdtensp qideidlrii nalqweprst wlalaralgl daatvarrwa rlteerlawv
       61 titpgprvld listallevd capslhaava drlcslphaa tvetlssras vlatvgapsy
      121 aalvrivdev raiegvhavr tgvvtewfaq ggdwrldala pderdrtrap arprqqpvpa
      181 ltdedrqvla ilardgrtpm ralaasvgaa pqvlarrldr llssdligmr cefarpaagf
      241 pilatlwcrv pavdvaaagr haarlpevrt cvavvgaddl vvqlwlhaps aladvetrlh
      301 sehpaltvtd ravdlrlhkl fgsllddggr rtgtiapdvw ap
//
LOCUS       WP_010836151             452 aa            linear   BCT 01-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Rhodococcus
            rhodnii].
ACCESSION   WP_010836151
VERSION     WP_010836151.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..452
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=46998
     Region          158..450
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 massrtkqyg piprarhvvr alviaflgiv aaltvggsal aqpadppppd pgsaveapaa
       61 ggvpvsgsln nggerltgvt vravdasgse vastesaegg rwelvvppga ytfeidtdtl
      121 pdgvsvqgav drqvaegrin avvfsfgevr tgnavplweq mlrllvdglr fglviaiagv
      181 glslifgttg ltnfahgelv tlgavfawvf nvtfgiqlip atilailvgi aigalanlgi
      241 wkplrkrrtg lipqlvvsig laialryiil iffsdrsqpy adyqgqvqhe wgpfaitsvn
      301 lativistvv ligvalllqk trigkamrav adnrdlaass gidvervilf vwglggglaa
      361 lggvlfglse lagrvqwemg fkllllmfag itlgglgtay gallgciivg vvvqmstlvl
      421 dpdlkyiggl lilililivr pqgilgsrqr ig
//
LOCUS       WP_010836237             538 aa            linear   BCT 01-JAN-2025
DEFINITION  amidohydrolase [Rhodococcus rhodnii].
ACCESSION   WP_010836237
VERSION     WP_010836237.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..538
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55889
     Region          1..538
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 msigeragtt lllgghiyss fapdatamai tgdtvvwvge drtgralhpd advvdlhgaf
       61 vapgfvdthv hvtalglnli gldltgarsr seclqwvray aatsaddivw ghgwddeswd
      121 dggppttael deaaggrpvy lsridvhsav cstalrrvva gldesagysp dgplrfdahh
      181 lgravardll tpaqraaart aaldlaasrg vvavhecggp disglddfre llahehavev
      241 rgywgeaard aghaqelldr tgahalggdl fldgsigsht ahlsqpytdr pdlvgesyld
      301 aervaahvaa ctevgvqagf hvigdaamsv avdgfsrvad rlggpavarl ghrlehaemm
      361 sagdaqalar lgviasvqpv fdalwggpdg myatrlgaer aaamnpfvma agagvslafg
      421 sdapvtpvdp wtmlraavhh htpgsavspr aafaaatrga wraggvrdgl agtlqpgapa
      481 syavwdtdel vvaapkdavq rwstdprsgv palprldada tlpvclssvh rgrtvytr
//
LOCUS       WP_010836247             310 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010836247
VERSION     WP_010836247.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..310
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32519
     Region          30..>195
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mstdvdvttl lplpgegeta grwdalisaa rrdlvaarfl eahndaaail helgadaprp
       61 gqwwgvwaae ppdpvlrava tdaghrlrgr kpwcsgahsc thalvtatre dgrvqlfavd
      121 lgqpsvrpvp dswhaigmaa sdsgavdfdd vpaqpigepg dylarpgfwh gaigvaacwf
      181 ggalavgdal rdsrrddpft lahlgavdaa eyaaraalea aaretdlapd dtdaarirar
      241 rvraivehva tatidrvgra lgpgpltanr rhaqlvadlg vylrqshaer dlaalgadar
      301 avgtdgegar
//
LOCUS       WP_010836382             277 aa            linear   BCT 01-JAN-2025
DEFINITION  TlyA family RNA methyltransferase [Rhodococcus rhodnii].
ACCESSION   WP_010836382
VERSION     WP_010836382.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..277
                     /product="TlyA family RNA methyltransferase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29094
     Region          6..257
                     /region_name="YqxC"
                     /note="Predicted rRNA methylase YqxC, contains S4 and FtsJ
                     domains [Translation, ribosomal structure and biogenesis];
                     COG1189"
                     /db_xref="CDD:440802"
ORIGIN      
        1 marrarvdae lvrrglarsr eharelidag rvlisgttat kpataieagt plrvvevsde
       61 iawasrgahk llgaldefvp rgltvsgrrc ldagastggf tdvllhrgaq evvavdvgyg
      121 qlvwrlrsdd rvrvhdrtnv rtldaetigg pvdlvvadls fislelvlpa fvaccapgad
      181 llpmvkpqfe vgkdrvgsgg vvrdpelrag avvavarsaa ahglvtkgav asplpgpsgn
      241 veyflwltvp erdaepvgad deavtqmihd aveagpr
//
LOCUS       WP_010836432             137 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Rhodococcus rhodnii].
ACCESSION   WP_010836432
VERSION     WP_010836432.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..137
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14973
     Region          6..117
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mlilgsivlg aadvpratrf wcdalglept eplsgneftg lrdadgrtvl siqhsdtepe
       61 peprlhldlf ardsadqaae verlvgigah rvdwprypad adfvvladte gnlfcvvdda
      121 rasepfrlfr erdaekg
//
LOCUS       WP_010836444             177 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010836444
VERSION     WP_010836444.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..177
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19082
     Region          19..173
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mevavtareq rtdvpgvapa eyrdalgrhp agvtvvtmss pdgpvgftat sfaslsldpp
       61 lvsfniarts ssyaaaqqad tmvvhllgeh qravatrfsr aaserfadta mwetldsgep
      121 hvlgaptwmr vridqridig dhtlviarvl sihaepdadd tapllyhrga yhrpeel
//
LOCUS       WP_010836451             212 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010836451
VERSION     WP_010836451.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..212
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23293
     Region          2..198
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mygdvkeril vgdlpggeli segevatrig vsrtpvreaf lrleaegwmr lypkrgalvv
       61 pipegeaani vdarrlvesh avttlagdpq lrahvlaqlh enlerqhela rhgdvaafsa
      121 adadfhtaiv ggsnpllraf yiglrerqrr mtarslardp eqlpriiddh trlftlveta
      181 dadgfddalr ihmeqvhalr ppargvqdgg ar
//
LOCUS       WP_010836614             178 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Rhodococcus rhodnii].
ACCESSION   WP_010836614
VERSION     WP_010836614.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..178
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18815
     Region          <13..138
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mstrflpvar gfyvtsgfga rwgtthwgtd fgrdggsggh pvfaaqggtv vmvgpasgfg
       61 qwvvvdhpta dgsgttvygh vipevrlgqr veagqriari npdsntnggv aphlhfevhr
      121 svwsqpgpnr ldpqpwlaga rwpgeaprpt tpvaapvded adeawlpile qltgprea
//
LOCUS       WP_010836884             109 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010836884
VERSION     WP_010836884.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..109
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12053
     Region          5..103
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 msrqmtemlk gtlegivlas laqapgygye itarlrekgl teiaegtvya llvrmdqrgl
       61 vasekrpsek gpprkvysls dagaeyldef wktwnflaer ldelrggea
//
LOCUS       WP_010836901             484 aa            linear   BCT 01-JAN-2025
DEFINITION  NCS2 family permease [Rhodococcus rhodnii].
ACCESSION   WP_010836901
VERSION     WP_010836901.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..484
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49571
     Region          5..479
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mavgtklldn yfkisergst vsaevrggvv tffamayivv lnplilgsfs pddavakvdv
       61 lgnilpvnqv aavtalvagl msivfgvvan ypfaiaaglg insllavtia pqvtwpeamg
      121 lvvidgiiiv vlaltgfrta vfnaippelk aaiaagigaf iafiglvdsg fvrripdaag
      181 ttvpvglgid gsiaswptav fvfglllmgv lvarkvkggl ligivvttiv aaiveafanv
      241 gpsqgtnpkg wnlstperpd sffglpdlsl vgdvsvfgaf trigviaasl lvftlvlanf
      301 fdamgtmtgl gkeanlvdek gnlpkigkal vvegagaiag ggasassntv fvesasgiae
      361 gartglanvv tgilflvamf ftplysvvpi eaaapalvvv galmiaqvld idlrrfeial
      421 pafltilamp ftysiangig vgfiswvvlq taagkvkqih pllwivaalf vayftidpit
      481 ealt
//
LOCUS       WP_010836931             162 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase [Rhodococcus rhodnii].
ACCESSION   WP_010836931
VERSION     WP_010836931.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..162
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17424
     Region          4..161
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(8,25,30,63,98,104,117)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(10,17,47..49,70,99..102)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mpgtvslvwa qanggvigdd naipwhvped mahfkrsttg rtvvmgrrtw eslppkvrpl
       61 pgrrnivvts hpesiegaet vasieealal cgddacivgg griysaampf atelvvthid
      121 ldvdgdchap aiddsfsvgt dsgwqhsekn gtpyrwvryt rd
//
LOCUS       WP_010836937             420 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein [Rhodococcus
            rhodnii].
ACCESSION   WP_010836937
VERSION     WP_010836937.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..420
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44859
     Region          21..331
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          321..382
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(347,349..351,353,369..370,374..375,378,382)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mfdsggggsg nelvdvaglv eskralarae yrqiraigaf haarvaaeqs asvsmpgesa
       61 anevslalgm segrvwfait lcedldtrlp ltdeafasge ldlaqvrtih nllqnlsdek
      121 ariveaalfa rgpidrlppa rlsgrlrrlv arydrdgfae rsarakeery isvkqcddgm
      181 aflsgelpsl daatiwnrlk emaigdvcag dersmsqrha dalvaladgs grltcgcgrd
      241 dcaaavpaag krgplvqivv sdgsvsaggm tagflpgvgp ldpetvreai aysatqrihv
      301 savdpvepap diaalryrip raladrirar dgvcrfphcp vpapscdidh tipfdhanpg
      361 qggrteeanl aclcrrhhrw ktqgrmavqq lgdgllrwtm pdgqvydtep dsptfwaaga
//
LOCUS       WP_010836940             487 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010836940
VERSION     WP_010836940.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..487
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=52734
     Region          2..481
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 msslqiavdg gvvsgrrigg lrtwrgvpya appagelrfr aphpvtpwqg vrpahrfaar
       61 paqprgggse dclhldvvap vapsgelrpv mvyihggaye sgassnamyh gtglvkrgdv
      121 vyvsvgyrlg algyldfsqf stpdrtfesn lglrdqiaal ewvqrniaaf ggdpanvtlf
      181 gesaganavt tlmtvprarg lftraiaqsp paastylper aarwarefve igatddpatw
      241 laaappeelv aagseltars ltaepgvrpy aptvdgdllp spaleafeag rshpvpflvg
      301 tnshegrvfp rfldilptsp erithlfsrf dadlfdrvvg aypgyphrha aadlggdvtf
      361 wepaircarg haahsptyvy rydyapallh aaglsathtl elyavfghhp wwtrvftagg
      421 ardaltrvte vvqghwlafa rdgepenswp ryeladpaty vidrqprvei gldeakrlaw
      481 lgyehlr
//
LOCUS       WP_010836957             389 aa            linear   BCT 01-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Rhodococcus rhodnii].
ACCESSION   WP_010836957
VERSION     WP_010836957.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..389
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42228
     Region          104..347
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 magdttpgvr rvlgglavaa gvaalaraaw sipvemgarr sairpfaaas phwrsgtfhn
       61 aepahpgpta ppwriaarfa trgrvgkppt pipvvapqfp dtvadlavtw lghasaliei
      121 dgatvladpv wservspstv vgparlhpvp sgldelprld avvishdhyd hldrrtllal
      181 rdlqevpfvv pvgvgahlrr wgiaeqrive ldwddsvelg girltctpar hfsgrgltrn
      241 ptlwsswvla gpqhrvffgg dtgytrqfae igdrygpfdv tvlpvgayde mwheihmdpe
      301 eavrahrdlr gglllpihwa tfdlafhpwv epatrlvsaa rdadvpvlip rpgerteidd
      361 arpvgivglr eqpdsvspww itvaagrad
//
LOCUS       WP_010837018             338 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Rhodococcus rhodnii].
ACCESSION   WP_010837018
VERSION     WP_010837018.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..338
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=36750
     Region          44..313
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 msdkflstst slrpgsgrsp rttltrtalg aagaaaagig yasliernaf alrevtmpvl
       61 epgaptlrvl hisdlhmlpg qrrkqnwlre lesldpdlvv ntgdnlshpk avpavvqslg
      121 nllarpglfv fgsndyfapr pknplkyfrt ehkrthgapl pwgdlraaft ergwldvthv
      181 rrelevagvr iaaggvddph lkrdryetia gkpnpmadls lgvthspepr vldrfaqdgy
      241 dlvlaghthg gqlclpfyga lvtnceldrs rvkgasawgs htklhvsagi gtspfaparf
      301 ccrpeatllt ltatkrddad sdvvrgrrrr srrtvlrg
//
LOCUS       WP_010837163             126 aa            linear   BCT 01-JAN-2025
DEFINITION  YidH family protein [Rhodococcus rhodnii].
ACCESSION   WP_010837163
VERSION     WP_010837163.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..126
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13282
     Region          1..122
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 mtvstpnhpg dpdlpepdyr ftlanertfl awqrtslgll aaavaiiqfl pdsagtftry
       61 glgglfgala tatsisgilr wrandrairr daplpqprvl tavsvvlavl gvvtltaalv
      121 taslnr
//
LOCUS       WP_010837135             440 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein [Rhodococcus
            rhodnii].
ACCESSION   WP_010837135
VERSION     WP_010837135.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..440
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46726
     Region          28..358
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          350..404
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(374,376..378,380,391..392,396..397,400,404)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mgsgdshtah gvdaacvepw qlgdpelsta vldvsrqiev lqarritlmg eladrglata
       61 agyrdagawl aahtmleige ardvaalgts lrtepeiaaa vaeqrisprh aamlcgffdt
      121 ppsllaalae ndpdehaavi aacrdallaa avpgpetatk svrtaietlr arldidtegp
      181 ttreredlnt ltvsntlngr vvlhgdfdal sgeilstals kssaprpsad gtrdprsagq
      241 rradglieic rrhldtgdsg feaaekphvt vlihqrdlek ppadkgdrvs vsvtalldgi
      301 glpwmpwggt ltpetarava cdahvtpvii ddhgvplsmg rttrlvtpaq rraltvrdrg
      361 cafpnctapa swceahhieh wadggatdld ntvllcgkhh rhvhhstwri vptprgrprf
      421 eppgepsssr ppgppppiva
//
LOCUS       WP_010837092             181 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010837092
VERSION     WP_010837092.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..181
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=19712
     Region          3..80
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mayvilglll lapqsqydlv knfeagvall ysasagsirr aldvlldkgw ievasvepgg
       61 rgrkvyrtte agrteferwm tgdlggpdle aaalprlffl glladtdrep vlrriqqrae
      121 adlaaleaqr krldalelpd gfadvvayqr atleygiamg rharewftdl anhggapgar
      181 s
//
LOCUS       WP_010837171             260 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhodococcus rhodnii].
ACCESSION   WP_010837171
VERSION     WP_010837171.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27561
     Region          5..248
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mkvllddltv arggravvrd vtltvpsgsv lgllgangsg kstllrtlyr aarpdrgriv
       61 vgdddvhact prvaarlvaa mtqdppgefe lsvldtvllg rtphtgrita panleiatra
      121 lacvdgeqwl grsvatlsgg erqrvllara iaqqtpvlvl deptnhldia hrhslldtvt
      181 elgvtaival hdldlaaryc davavlhdgr vyahgapddv ltptmlrtvf gvdgslvvhp
      241 etgrshlvid grhrketplp
//
LOCUS       WP_010837198             497 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Rhodococcus rhodnii].
ACCESSION   WP_010837198
VERSION     WP_010837198.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..497
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=52229
     Region          5..481
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(62,64,68,71,75,108,111..112,121..128,133,136,139,
                     232,236,239,242,244,417,419..420,422..423,426,429..430,
                     432,434..437,446,450,452,466,473..478,480..481)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(148..151,159,174,177,207,224..227,230,248..250,282,
                     382,384,410)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(151,248,279,282)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mtptvshwsd gkpfagtgdr tapitnpatg tvtgevalag vedvrvvvea aaaafpawrd
       61 tslaqrtavm frfrellnar kgelaeiitr ehgkvlsdal gevnrgqevv efacgaahll
      121 egrftenast kvdvysirqp lgpvgiispf nfpamvpmwf fpiaiaagnt vvvkpsekdp
      181 saslwlaelw aeaglpagvf nvvqgdkvav dellenpaik aisfvgstpi aqyvyangta
      241 kgkrvqalgg aknhavilpd adldlaadam vnagfgsage rcmaisvava vgdiadtlve
      301 kiaerarsvk tgdgtgdadm gplvtrehrd rvasyvgage esgativldg rtveadggtd
      361 gfwlgptiid hvtpdmsvyt deifgpvlsv vraasyeeal dlinanpygn gtaiftndgg
      421 aarrfqneve vgmvginvpi pvpmayysfg gwknslfgdt haygaegvhf ftrgkaitsr
      481 wldpshggvd lgfpqnv
//
LOCUS       WP_010837215             307 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010837215
VERSION     WP_010837215.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..307
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33044
     Region          27..270
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtvldvdqtv pesrgatadd aapqpprdap vsmvervtli ldsfdapttr ltleevscra
       61 glprstvhri ldqlvkldwi ehasfgyclg rrslgfgadp dgharireaa apvlhtlhmr
      121 tglvvhlsvl dggdgvyldk iggklaaalp srvggrvpah atacgkalla wldpesvddl
      181 yrheyprrat ertigdvsll hqelgrirrr hgvaferdea vrgvscvgva vrghdgpvas
      241 islagrtqev hlervapiva eaardvtgal fpetgrrrtr avpdavppsw tppaldrmls
      301 mpptgwl
//
LOCUS       WP_010837229             214 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Rhodococcus rhodnii].
ACCESSION   WP_010837229
VERSION     WP_010837229.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..214
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22542
     Region          100..214
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtahptangs rdgtvltspp adapidrata qarrlveall rtdrtrgdla avadelgria
       61 dqleahapdv sdrlidmwqg egvtrhdpvt gpenvlappl vihgradgsv datvtlglpy
      121 qgppghvhgg vsallldhvl gvanawaghs gmtaqlsvry rrptplfesl tvrarveevd
      181 grkirttgei ttangdacvt vdalfvtaml prpr
//
LOCUS       WP_010837258             191 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010837258
VERSION     WP_010837258.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21184
     Region          2..191
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mvrtnperrr alldaaievl aqrgargltf rgvdeeagvp vgtasnyftn rddlfvqvgh
       61 ryyerltpda qtiaaarepq treslvdvmt evvervasfr tgylailelr leatrrpelq
      121 alltervrad meynvdnyrs tglpggadsv tllhlalnwl ilerltlpgv vdadraaelv
      181 rlaveravpg e
//
LOCUS       WP_010837321             181 aa            linear   BCT 01-JAN-2025
DEFINITION  RNA polymerase sigma factor [Rhodococcus rhodnii].
ACCESSION   WP_010837321
VERSION     WP_010837321.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..181
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20380
     Region          4..156
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msadharftd iyvrcyprvl afarrrapds lareatdeaf lvawrrldev pmdplpwllt
       61 tarhtlselr rrgerhdalv deisrarrlv sasepgadda vvervtvlda laslrerdre
      121 tlmltvwdgl thqeaasvsg cttatftvrh hrarrrlaaa laqrdgrppd talhpnertp
      181 t
//
LOCUS       WP_010837278             405 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Rhodococcus rhodnii].
ACCESSION   WP_010837278
VERSION     WP_010837278.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41377
     Region          18..388
                     /region_name="MFS_MdtG_SLC18_like"
                     /note="bacterial MdtG-like and eukaryotic solute carrier
                     18 (SLC18) family of the Major Facilitator Superfamily of
                     transporters; cd17325"
                     /db_xref="CDD:340883"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,143,
                     146..147,150,222,226..227,230..232,235,263,267,316..317,
                     321,325,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340883"
ORIGIN      
        1 mteeveprar lpkeiwvlvs aaflialgfg lvapalpqfa rsfdvsvtaa svvissfafm
       61 rlvfapasgr lvqrlgerpi yitgvlvvaa stgacaiaan ygqllvfrgl ggigstmftv
      121 samglliria ppgmrgrvsg lyatsflmgn itgplfggll vgfglrvpfv iyaialliaa
      181 avvffalrgs hlaapdrgad vptltlrdgl aapsyraalv snfayggvif gvrvamvplf
      241 vvealnrdaa fagialmvfa vgnaavqsia grmsdrigrk pfvlgglivc gastvamgig
      301 enlvvflvas vtaglgsgam npaqqaavad vigskarggp vlatfqmmsd vggvlgpiig
      361 gllaetfsyg vafavtgsvm lvaalvwakv paepvpkdan edtqr
//
LOCUS       WP_010837456              82 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl carrier protein [Rhodococcus rhodnii].
ACCESSION   WP_010837456
VERSION     WP_010837456.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..82
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=8723
     Region          1..79
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mtapalddwl aekiagylsv tpesvdrdrs ladygldsvy avtlcgeied efglvveptl
       61 awdhptvnam sdhletllgs gv
//
LOCUS       WP_010837557             231 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010837557
VERSION     WP_010837557.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..231
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24286
     Region          14..231
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtseidgvlq tlhsarprvv ltssaeraae vvreritdga fhpgdrlpee piaealgisr
       61 ntlrealgtl vservlvrrp nrgvfvrtpt aadvrdiyra rrviepgclr aatspdgpaa
      121 arsllaavda gaaalaagdg ravasanqrf hravvalggs arldaemsrl laemrlvfsc
      181 agsaedfhgp yvamnraiae svrddgaaaa aplldeylva aerhllsaft s
//
LOCUS       WP_010837565             308 aa            linear   BCT 01-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Rhodococcus
            rhodnii].
ACCESSION   WP_010837565
VERSION     WP_010837565.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..308
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31921
     Region          27..297
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mghghghgvg ghaptdrdev trsrivrmsi algiiasflv levvvalaid slalladagh
       61 mltdvaglsm glialtlarr gstnaartfg whraevltai vnaalllgia tfilieaisr
      121 rgdppeipgv alvltaaagl tanlvvvaml rrdaggslav rgaylevlad avgsvgvlva
      181 gasmllfdwr wadivvavli slwvlpravl laasalrilt qaspahvdvp aveadlaalp
      241 gvcgvhdlhv wtlttgmdva tvhivtepdv ggvldraqrv ldghglshat vqvestergr
      301 tcerditw
//
LOCUS       WP_010837571             232 aa            linear   BCT 01-JAN-2025
DEFINITION  DedA family protein [Rhodococcus rhodnii].
ACCESSION   WP_010837571
VERSION     WP_010837571.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..232
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24219
     Region          25..183
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mtsvaldavh aagsfgplrt agpvlvwiiv vtfvflecav vlglflpgds mlltagivla
       61 shssgsahvw alslgamiaa iignqvgyai garaghrvvv rrggrylnek nllavqslle
      121 rhgfwsvlva rwipwvrtlc plvagaagmn rtkyvvassl gaiawapvll lvgfyaggll
      181 ervpwlvpav vgvllvvlvi gtivgvrqyr aemarpanvv diddvpadst aa
//
LOCUS       WP_010837656             407 aa            linear   BCT 01-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Rhodococcus rhodnii].
ACCESSION   WP_010837656
VERSION     WP_010837656.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 407)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..407
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42088
     Region          1..407
                     /region_name="PRK06205"
                     /note="acetyl-CoA C-acetyltransferase"
                     /db_xref="CDD:235741"
ORIGIN      
        1 mrdvvvcepv rtpigrygga vasltaaelg tialrglldr tglapeaied vilghcnats
       61 eapaigrvva ldaglpitvp gmhidrrcgs glqaviqaam qvgtgnddvv vaggtesmsn
      121 asfysvdmrw ggarsgiamh dslararsta ggkhhpvagg mietaenlrk qyeitreeqd
      181 elavashlra vraqkdgvla eeivpvavqt kggeqivdtd ehprpdvsld slarlkpima
      241 kadpaatvta gnasgqndaa amcivttpev aerhglrplv rlvswglagv ppstmgigpv
      301 pataaalgka gltladidvi elneafaaqa lavtrewgfg rfgeggdfdr tnvhgsgisl
      361 ghpvgatgvr mlaslareld rrearygret mcigggqgla avferva
//
LOCUS       WP_010837691             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010837691
VERSION     WP_010837691.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..262
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28307
     Region          1..101
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(49,52,56..57,66,83,87,93,97,100..101)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mrigqmaraa gttvravrhy hrlgllgeph rtsngyrdyt iadlarlmri rwlaaeglpl
       61 dsvatvlgaa ddadrdgdlr tdllaltadt rrqiallqrk ldslqrllda vdqgrrptal
      121 prdladafdk qsvaatdpsa alalarerdl vemlaisgea psdlftwfag aladpdsaat
      181 yrallrrwge legrnptert ddiellahdl aghldglipg hadvdtapsf pgftlpdvvp
      241 daaqravier aitilaageq ar
//
LOCUS       WP_010837716             443 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein [Rhodococcus
            rhodnii].
ACCESSION   WP_010837716
VERSION     WP_010837716.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..443
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46993
     Region          39..364
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          356..402
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mgsgdtshas riaashvagl hvaswpedse rlgdaalada ilemsaavaa leakriaflg
       61 dfdrrglage aghrdtaswl tertlleigp araavtlars ladepeiaaa vaesalspeh
      121 arllchffek pptalralen tdpeeydavr sacrdallaa aapspttstr tvrtakekle
      181 qrldceagag pttkerdein elsvgttlhg rvvihgnlda vagdivktal sklsaprpad
      241 ggtrddrtps krradalvev cnsflasgaa gfeggerphv tlivddrdlr spegpvaetv
      301 adtltrdlpw thwgttlspr tsralacdaq vtpvlvgdrg vplamgrthr lvtpaqrral
      361 tvrdkgcafp gcgapspwcd ahhvihwadg gstdldnlvl lcghhhrhlh hsewsitidp
      421 gapprfeppp rrtrsahgpl caa
//
LOCUS       WP_010837754             741 aa            linear   BCT 01-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Rhodococcus rhodnii].
ACCESSION   WP_010837754
VERSION     WP_010837754.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..741
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=77597
     Region          4..659
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 magkkpakkk srwrtvrrag yvvvalalvv pilgfmaayv vqdvprpgdl etnqvatiya
       61 adgtseiarv vppegnrqev disqipehvr navlaaedre fysnpgfsvt gfaraardnv
      121 lgresagggs titqqyvknt lvgdersmtr klkelvissk marewskddi laaylntiyf
      181 grgaygisaa anayfdkpve eltveegavl aasiqlpsvl dpevnpdraq qrwnyvldgm
      241 vasgwvdeat ratmqyppyr aladldaasq qstgpeghvk nqvlgelsaa gisenqlnte
      301 glqitttidp kaqqaavdga rnnldgepdn lrtavvsvdp rtggvvayyg gedgngydfa
      361 naglqtgssf kvfglaagld qgiplsamyd sspltvngis ignvegescg tctiaealkr
      421 slntsfyrlq adldggpqav admahlagip eeipgvgpsl tepngagpnn gvilgqyqsr
      481 pldmasayat laasgtyrap hfiekvvtad gnvlldrsqe qeqiqgeqri deavadntta
      541 amapiaaysr ghalaggrps asktgtaqlg dtgmnkdawm vgytpsmsta vwvgtpdgep
      601 lvnsyggsiy gsglpsdiwk samdaslrgt dvesfprpgs iggqagvpqy tgpapsttte
      661 aprstlqlpt eipdleitqr pveilpgvti pipglqqrpe peqppqtqqp pgagadpggq
      721 ggqnggenga pqdgdlvmpg g
//
LOCUS       WP_010837731             507 aa            linear   BCT 01-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Rhodococcus rhodnii].
ACCESSION   WP_010837731
VERSION     WP_010837731.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..507
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53950
     Region          5..483
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(62,64,68,71,75,108,111..112,121..128,133,136,139,
                     232,236,239,242,244,419,421..422,424..425,428,431..432,
                     434,436..439,448,452,454,468,475..480,482..483)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(148..151,159,174,177,207,224..227,230,248..250,282,
                     384,386,412)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(151,248,279,282)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mavelshfvg gkrvpgesgd fadvldpvgg tvaarvplan arevsaivsd aeraqqewaa
       61 fnpqrrarvl mrflqlvqde mdslarllss ehgktvadak gdiqrglevv efavgiphll
      121 kgeytesagp gidvysmrqp lgvvagitpf nfpamiplwq aapalacgns fvlkpserdp
      181 svplrlaelf veaglppgvf dvvngdktav dalladervr avgfvgstpi aqyiyetaar
      241 ngtraqcfgg aknhavvmpd adldevadav vgagygsage rcmaisvvvp vgeatadalv
      301 ekiaervrgl tigpgddaas dygplvgpda vdrvngyvdl gveegaelvv dgrgftlpgh
      361 engyfvgpsl fdrvtpemri hreeifgpvl lvaraanyee alrlpsehey gngvaiftrd
      421 gdtardftar vnvgmvgvnv pipvpiayht fggwkrsvfg dlnqhgpdsi rfytktktvt
      481 qrwpaglrea adgavdrgdh fviptmk
//
LOCUS       WP_010837718             444 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Rhodococcus rhodnii].
ACCESSION   WP_010837718
VERSION     WP_010837718.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..444
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47675
     Region          23..430
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(36..37,40..41,44,83,141..142,144..146,149,169,
                     172..173,176,260,263..264,267..269,272,300,304,357..358,
                     362,366,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msvttrstqp egeseyerrk rlrtvtaasl lgttvewydf flyataaalv fnqlffpdes
       61 sfvgtmlafa tfavgfvvrp iggvvfghig drigrkktla ltmflmgiat almgvlpthe
      121 qigvlaplll lilrvaqgfa iggewagavl lsvehspkgk rglfgsipqv glalglalgt
      181 lvfailqvvf ddeqflaygw riafllslvl vvvgfvvrlk vdetpafqev telskqssmp
      241 irdtfrkpnt rttvlgmlsr wgegaafntw gvfaityatg tlafdrvpvl lvvtlaalvm
      301 aalipvsgvl tdrfgarqmy lvgiaaygvl vfpvfalfgt enlawftvam vvvfgvvhsv
      361 fygaqgtlya slypaeiryt glsvvyqfsg vyasgltpmi ltaliaaggg spwfaclylv
      421 ltavvsvvat sairnedlhl ttgr
//
LOCUS       WP_010837825             185 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010837825
VERSION     WP_010837825.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..185
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19621
     Region          21..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mpdavtlddl dfalldalhs dpragalels rrlrvargtv qahlrkleeg gviashaphi
       61 gldaagfgvq afvtletsqg aldavtrelt aipgileaft ttgsgdvlcr vaarshldlq
      121 etlirvstca hvarstsvmv lsvivpfrtl pllhtlerpq tskapayrpe avqgvqqvsp
      181 ppsrr
//
LOCUS       WP_010837846             289 aa            linear   BCT 01-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010837846
VERSION     WP_010837846.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..289
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29827
     Region          66..278
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mrvlvssgra alavgggavd iaaasggrfs sdvqdiygvw gefcdwargf agpadldvrp
       61 gnvgcpvprp pqvfavglny rahavesglp ipeipvvftk fpaavtgpyd rvvlptgpvd
      121 feaevvavlg traenvaard awshvagltv gqdlsqravq wagdapqqfs lgksfagfap
      181 igpvvvtpde fdnpddveia cslngeqmqk srtsdlvfsi peliayisai vpmmpgdllf
      241 tgtpsgvgfs rdpkivlqpg delttsidgv gsmittfaar aagatgspt
//
LOCUS       WP_010837917             193 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010837917
VERSION     WP_010837917.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20243
     Region          14..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvstsnadsv dvgerildaa ascvvdfgve rvalaeiarr agvsrptvyr rwpdtnavla
       61 elltrritsa ladvpsrgpd rgalvqrivd vagvlrrdal igavlgsape famvyiarrl
      121 gtsqaivvda lpaeigrcqr dgtvrvgepr tlaamvllit qstvqsaqmv egildadala
      181 aelshslngy lap
//
LOCUS       WP_010837898             250 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010837898
VERSION     WP_010837898.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..250
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27087
     Region          15..246
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mrkyagtred aarwvrdvlr aqildggfgg lsaprpmlpp entlasdlgv srnaireald
       61 llraeglitr vqgagtfvtg aklrqrldrl eglaeslagh qlsvvnrvvs aredtanpfv
      121 aaklhvqegs piyfiervrs vggvalsldt tslrpeaidv vrgadldttd vftlletelg
      181 vrlgraentv eavaadrgsa rmlevrpgsp lllvhrltfl dddtpfdles vryrgdrlsl
      241 vtvnprltrg
//
LOCUS       WP_010837942             222 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010837942
VERSION     WP_010837942.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24025
     Region          3..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mlrsdarenl drilgaarqv faeqgldakl advaaragvg vgtvyrrfen kdaliaalfd
       61 srlevvveks raalefedpl eglvwfldvs tqlmaddral rdlavggpat phahlsqatl
      121 drveklryev hehvqrlvar gqaagvvrdd ldatdiglls stlqaavdpg adsepdvwrr
      181 vlglvvdglr tdgvrtplap rpltepqlsa vmrrvkspad pk
//
LOCUS       WP_010837945             375 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Rhodococcus rhodnii].
ACCESSION   WP_010837945
VERSION     WP_010837945.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..375
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38775
     Region          131..371
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflalrelwf artrfllmga vvalisilmv ilsglssglv gdgvsslqrs sidafafeeg
       61 tkadsafsrs vvteeqaqlw aerpdvadae lmgnaivnah tgsgtpvdlt lfgitpgsyl
      121 epepaqgerl vgdhdivvsa alaeeglsig dtvvldrlgt eltvvgftae krtfghvdva
      181 ylplptwqei hagtragetp dpriydeasv valrgvdgtp dlaagdaaag tsattleesf
      241 dsspgfsaem mtmsmieafl yaisalvvga ffsiwtvqrs relavlramg astgfllrdg
      301 vvqalvvlva svvvgvglgv glgsglegsg mpfalevgpv vngavllavl glagavvail
      361 ritrvdplaa lgenr
//
LOCUS       WP_010837946             236 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhodococcus rhodnii].
ACCESSION   WP_010837946
VERSION     WP_010837946.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24885
     Region          19..233
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnhpttdtrs dtprtatgls lrdvvltfgd gdqtvtaldh vdldvargei vaivgpsgag
       61 kssllavaga ltvptsgtvr vgetdlsgln rrrlaalrre qigfvfqsgn llpaltardq
      121 lrlvpritgr pgrdpdalld avgmshradk rpgrlsgger qrvgiaralv gepavllvde
      181 ptaaldrars qeivallare theagvatim vthdhdvlgh cdrvlemvdg alhphd
//
LOCUS       WP_010837953             342 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010837953
VERSION     WP_010837953.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..342
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37213
     Region          6..139
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          184..313
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mristdldet dleivncvqi aprvtwneig svlligpdaa arrwkrlagv gltwvtaypq
       61 lsswakyhcl afvgvdcelr arqsvvedle ripqvasvsq mssgrdlwli vlfddlqelg
      121 rflqghlasl pgvrrtrtya vsevysdgar wklgalprds hqrlvakshg shlegpvvla
      181 gglrelacel ardgrasasa laqrlgtsas tvrrrlarle dagvltfrce vaqvlsgyrv
      241 iatywarvpp gdlddaarai gampevrlaa tvtgtenlim tawhrtigdt kefearvvgr
      301 cptvdfvdsa ialqmnkrmg wildgdgrgv aavpiggyaa re
//
LOCUS       WP_010837984             378 aa            linear   BCT 01-JAN-2025
DEFINITION  alkaline phosphatase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010837984
VERSION     WP_010837984.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..378
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39410
     Region          42..374
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mptaldvysg ptlanvlpaa laglgasgeh dpwglprcsa wvvllvdglg wnllqdslse
       61 apalgeltgv ptpagfpttt atslttlgtg lpsglhgvtg yrsfvpeidd tvgwlswrsg
      121 rsgndlretv vpertqphpt vferavragi patavlpasf egsgltraal rgarfaprha
      181 hgdmiahtvv aaaegglvyc yisevdtlgh vygpgslawr selaevgaav dvllrelprg
      241 tgllvtadhg mvtvpesari dadhddtlrs gvhtlagepr crhvhtepgr tddvaarwrd
      301 rlgddwhilt raeaiasglf gptvapdvag rigdlvvvar ggggivrsra ephlselvgq
      361 hgaltddela vpvlhtvt
//
LOCUS       WP_010838018             251 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010838018
VERSION     WP_010838018.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..251
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27272
     Region          40..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mssdgatdet tsepstngdt pppakpdapa ksdgrkrrwr ehkiarreel vdgtisairl
       61 hgrdigmdei aseigvsktv lyryfsdksd lmnatmmryv qttlaprvya avssdmsefe
      121 lteatikayv etvasdpeiy lyvmsngqga dtsvvadser miaevlasvl geklraldmd
      181 sggsvpwayg vvgsvqlath wwisnrsmst edliayltmm lwggisgiae mkgsptrfra
      241 adhsfptgpe t
//
LOCUS       WP_010838042             195 aa            linear   BCT 01-JAN-2025
DEFINITION  dTDP-4-dehydrorhamnose 3,5-epimerase family protein [Rhodococcus
            rhodnii].
ACCESSION   WP_010838042
VERSION     WP_010838042.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..195
                     /product="dTDP-4-dehydrorhamnose 3,5-epimerase family
                     protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /calculated_mol_wt=21269
     Region          1..184
                     /region_name="RfbC"
                     /note="dTDP-4-dehydrorhamnose 3,5-epimerase or related
                     enzyme [Cell wall/membrane/envelope biogenesis]; COG1898"
                     /db_xref="CDD:441502"
ORIGIN      
        1 meyrelkvpg aweitprqfg ddrgvflewf repgfseatg rvldlqqanc svsaagvlrg
       61 ihfadvppgq akyvtcvsga vldvavdlrv gsptfgvwda vllddrerra iflseglgha
      121 flsledgstv vylcstgyap ereheispld peigiewpav dragaplelv lsdkdraapt
      181 lrearergll pahre
//
LOCUS       WP_010838028              95 aa            linear   BCT 01-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Rhodococcus rhodnii].
ACCESSION   WP_010838028
VERSION     WP_010838028.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..95
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10367
     Region          1..75
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mplyefhcqd cgpierhhpm atvpddepcp ecgesmrrrv gapalgrigs pamralddaa
       61 rsahepavvn slpgsprtrr tprsadprhr klprp
//
LOCUS       WP_010838077             143 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Rhodococcus rhodnii].
ACCESSION   WP_010838077
VERSION     WP_010838077.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..143
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15703
     Region          8..142
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mstirrfdvt fdcakpalla afwcevlgyv vppvpdgfss wedyhdslpp edeiyfsctd
       61 psgvgprvlf qrvpegkvak nrvhldvrvg kglvgderla vleaecarls algathvltq
      121 raddenesci tmqdiegnef cld
//
LOCUS       WP_010838130             438 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Rhodococcus rhodnii].
ACCESSION   WP_010838130
VERSION     WP_010838130.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..438
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45287
     Region          45..406
                     /region_name="MFS_YfmO_like"
                     /note="Bacillus subtilis multidrug efflux protein YfmO and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17474"
                     /db_xref="CDD:341027"
     Site            order(55..56,59..60,63,95,145..146,148..150,153,172,
                     175..176,179,247,250..251,254..256,259,283,287,338..339,
                     343,347,362,365..366,369..370,373)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341027"
ORIGIN      
        1 mtptnppptp pkevavssat qddstththd sggaqesllh qpkavwavaf asviafmgig
       61 lvdpilkpig eqldatpsqv sllftsymlv tgvamlvtgv vssrigpkrt llsglaiivv
      121 faalagmsdt igqiigfrag wgfgnalfia talaaivgaa sggvarsiil yeaalgigia
      181 igplvggvlg diswrapffg vavlmavafa livvllptse kpdhhtslaa pflalrhrgl
      241 ltvgitally nygfftllay tpfpldlgay pigfiffgwg valavssvfv aprlqrrfgt
      301 ihimmaslll favdlgvmal ftttkpvliv cvvlagvflg vnntlitevv misapverst
      361 asaaysfvrf vggaaapwva gtlgernvhl pfwvgaactv aaiavlstgr rilahvddhd
      421 paphsidear avtagdag
//
LOCUS       WP_010838147             431 aa            linear   BCT 01-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010838147
VERSION     WP_010838147.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..431
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46128
     Region          1..429
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mgtdsfwddv drhlvryips ftpriierga gsyvydedgn aildftsgqm savlghahpa
       61 iveavsesva tldhlfsgml srpvvtlgkr lsdslpenlt kmllvttgae sneaaikmak
      121 lytggyeivs fdrswhgmts gaaaatfsag rrgygpvlpg nltlptpnay rspfrnpdgs
      181 hdwkteleyg fsivdtqstg slaavliepv lssggiidlp lgylarlrel cdergmllil
      241 deaqtglgrt gtmyaferdg vapdiltlsk tlgaglpvaa vmtsdeienv caergflfyt
      301 thaadplaai vanavldvie rdglveraak lgdqlterlv gmqnrfdvvg dvrgrgllqg
      361 velvldkqtr epadelgavv tkgclerglh mnivqlpgmg gifriapplt iseddlhagv
      421 dileeslraa l
//
LOCUS       WP_010838220             448 aa            linear   BCT 01-JAN-2025
DEFINITION  hemolysin family protein [Rhodococcus rhodnii].
ACCESSION   WP_010838220
VERSION     WP_010838220.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..448
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48042
     Region          7..431
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mtanvedalp livlaivlvp lggifaavds alatlsparv delvkegrpg serlaqilre
       61 rpryiniavl lrivceitat vvlaaafmdl lepvwalvga avvmvivdfv vigvgprtlg
      121 rqhaysltla lalplravgv llvpisrlli gfgnavtpgr gfrngpfase velrelvdla
      181 rergvvaege grmiqsvfel gdtsarevmv prtemvwiea hktagqatsl avrsghsrip
      241 vigegvddvl gvvylkdlvq qtyysadggr gvtvgeimrp avfvpdsksl dellgdmqrt
      301 anhmailvde yggvaglvtm edlieeivge ivdeydhdep envedlgdge yrvstrlste
      361 dlgdlfgldi endevetvgg llalelgrvp lpgsevrshg lllrgeggkd qrgrvrvttv
      421 tarraddedd tgadetvhae tnegehtr
//
LOCUS       WP_010838163             233 aa            linear   BCT 01-JAN-2025
DEFINITION  PadR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010838163
VERSION     WP_010838163.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..233
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25813
     Region          27..108
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mgesddhdtr dgdavpsypp lpvtswavlg mlafgeelsg ndlkkwadws igffywspsv
       61 sqvygelkkl esmglvasrt isetgvrgrr vyaatsegmd avrawvrdap veipvlkhgv
      121 mlriwlghls dpehlkslvr ahienmeqlr araalhadhs trepgwafpr mslrwalryf
      181 eaeielsral fdeideaaeq faaarvdgtg llapqvpgsw rtvedvvsgl trg
//
LOCUS       WP_010838269             287 aa            linear   BCT 01-JAN-2025
DEFINITION  DegV family protein [Rhodococcus rhodnii].
ACCESSION   WP_010838269
VERSION     WP_010838269.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..287
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=29113
     Region          13..275
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mpvvvvtdss ssipadvaqr wgievvplhv lvdgrdvreg vddvpadlss attsgaspae
       61 lrevyaaale rsggdgvlav hlsqqlsgtw raattaadef agavrvldsr siayglgypv
      121 laaardaaag valgelaera athaaagccf vvverldqlr rggrigtaaa lvgtalaikp
      181 vlhlddgklv lrekartssk altrlvsvaa eaargahgrv elavqhvaap eraadiaqrl
      241 eqaldgedas apivadigav vgthlgpgav givvvpgesg fpphrar
//
LOCUS       WP_010838278             489 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Rhodococcus rhodnii].
ACCESSION   WP_010838278
VERSION     WP_010838278.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..489
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51934
     Region          46..459
                     /region_name="MFS_ProP"
                     /note="Proline/betaine transporter of the Major
                     Facilitator Superfamily of transporters; cd17366"
                     /db_xref="CDD:340924"
     Site            order(56..57,60..61,64,102,160..161,163..165,168,188,
                     191..192,195,284,287..288,291..293,296,324,328,380..381,
                     385,389,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340924"
ORIGIN      
        1 mnphdphatp edetsgdgrg rtltraeida apevtltdek avkravkatm lgnamewfdf
       61 gvyaylaati gkvffpeasg taqllstfai faaafvvrpl gglffgplgd rigrkqvlat
      121 tivlmaastf aiglvpsygs igiaapiilv llrllqgfst ggeysgastf vaeyapdrrr
      181 gsfasflefg tlagyvaaag lvttiqalvs eealvdwawr ipflvagplg liglylrlrl
      241 eetpafrhle aaedasraae sagagikrtl vdhwrplvlc illvaaynia hygllsympt
      301 ylnstlgyde shglilmivv mlvmmigitf vgrlsdrvgr kpllylgfag ffvlsvpayl
      361 ligmgsylsi fvglailggl lllfvgvfps vlpalfatgi rygglsigyn vavsvfggtt
      421 pfvltalgsv tdsqlaapay mmvasvvggi avfciretar kplagsppav stedearrvi
      481 lehrtyqpr
//
LOCUS       WP_010838298             207 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Rhodococcus rhodnii].
ACCESSION   WP_010838298
VERSION     WP_010838298.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18096355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..207
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22105
     Region          5..188
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          118..205
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mpplirsara devpavagll aeafesdpvm aamlpdsgtr drrltrlfat eigvhhlpgg
       61 avdvavgedg vmggaavwdp pgrwhqgigt qlrmlpglvr algpralaga rmsqaferah
      121 pttphwflsa igtgrsargg gfgsallrsr levvdrdamp aylessnvan isyyerfgfe
      181 aydeielvpa rgdaeavvay amwrdpr
//
LOCUS       WP_010838321            1605 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Rhodococcus rhodnii].
ACCESSION   WP_010838321
VERSION     WP_010838321.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 1605)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1605
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..1605
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=174481
     Region          14..1596
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mrsvtmsgtg nsidrlaaqa apeyfrtvdr gdstdpiags aeavvrahve lalnrptgri
       61 ltrvhrsdgi apslqivvdd mpllveslla llgrlgivvg elvhpvmqvr raqngtlvei
      121 gaaaqaspse rvvaeswihv hldphtardv ldvlaveivg vledvaavvh dgdamrriql
      181 dladdvadaa lpatvgeqer sdctdllrwm adgnftllgy hrlaradelg adghrpmvpv
      241 rdsglgllrs rvddgalaar davrdgdsrl lvltegsapa tvhraaypff agvavfgtdg
      301 avigehrflg vftvsalhrn vldipvvgrr araviegagf plesysgqam leiiedlpkt
      361 elfasspevl aetveavhsi grrrsvrlfv rgdrferfvs cliylprdry ttrvrvamqd
      421 alarefhagt veytarvtes alamvhvvlr daapghvlph riteadreri eaglieisrg
      481 wddrfddaam ragfsptmir walaalpeay kedfealrav rdvalldala vgdvdvrlah
      541 tradrwrvtv yvrgsalslg qilpilqslg yevhderpyt vsgpgrpdaw iydfslvdpr
      601 gvddgagadt rraervqdaf laawrgdaea drfnelvpra gltwrqaavl rtyakylrqe
      661 gfpysqhhie tvalahptva aglvalfeay fdpdtddatr eqrsadidae lnagiervvs
      721 ldedrvlrav hslvhatvrt nafvvgrnga rpalavkllp reidelplpr pqfeifvcsp
      781 dvegvhlrfg rvargglrws drredfrtei lglakaqqvk navivpvgak ggfvvkrppk
      841 ltgdantdrt atheagvaay rafvsamldv tddydrsegt sippqrvvrr dgdddylvva
      901 adkgtatfsd lansiaedyg ywlgdafasg gstgydhkel gitargawks verhfremgl
      961 dpatddftav gvgdmsgdvf gngmllsehi rlvaafdhrh vfldpdpdaa asfaersrmf
     1021 alprsswady daalisrggg vwersvksip vspqarrslg laddvtelsp pelvrailla
     1081 pvdllwnggi gtyvkarsea ngdvgdksnd lvrvdgaqvr arvigeggnl gvtqlgriey
     1141 araggrintd aidnsagvds sdhevnikil ldsavtdglv ppdernplla smsdevadlv
     1201 ladntaqnsl lglsratapa midvherlva qlerergldr sleslptpee faelaergag
     1261 lsspelatlt ahvklalead llatdlpdsd tfasllpgyf ptplrdrlqr tilrhplrrq
     1321 ivatmlvget idmggitysf rlaedtgaat tdtvrafaaa taifglrdvw srirsrglpv
     1381 avedamidet lrlldratrw llarrpqpla vgaeiaryte pvaelvaafp tlerdagrrw
     1441 rdrraawale hdaprdlade vyglvdrfaf ldvvdvadvt drpltsvada wlgleahlev
     1501 ptlfdaiaal drggrwhsla rlalrddvyg slrqltyevl sagepgeste dmiaeweatn
     1561 gqrvvrarta lgeiyasdtl dlatlsvaar qvrsmvrgga agagv
//
LOCUS       WP_010838360             465 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Rhodococcus rhodnii].
ACCESSION   WP_010838360
VERSION     WP_010838360.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..465
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49096
     Region          27..431
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(40..41,44..45,48,87,145..146,148..150,153,173,
                     176..177,180,261,264..265,268..270,273,300,304,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtiepsspet penqepprtp eerralrrva lssllgttie yydfllygtm aaivfghiff
       61 pssnpalgti aafgtlaagy varplggilf ghfgdrvgrk smlivtmttm giastligll
      121 ptyetvgmla pillvtlrvi qgiavggewg gaalmvveha darsrgrwag imqlgtpfgf
      181 llstgvvall tsyapdamlt wgwripflls avllliglyv rlqvvespif aeaaerheer
      241 rvpvlevlar pgrvllaiaa gvgpfaltal tsshiiayat sigyetsqvm ntliavvavs
      301 ivfiplfaal sdrlgrrrvm mfgavgtiaf afplyhlvgl gttvgllagl miaqmlqnam
      361 yapltpllse lfptkirysg vsisyqfasl igagftplva sslvagfggs svplsliagg
      421 talvsvlalv vtreatgral dweeqetvss gavetadpav aerrs
//
LOCUS       WP_010838383             344 aa            linear   BCT 01-JAN-2025
DEFINITION  AI-2E family transporter [Rhodococcus rhodnii].
ACCESSION   WP_010838383
VERSION     WP_010838383.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..344
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35344
     Region          11..321
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mvrvwaawtw rllivaagia lvgwlalrfd avvipvalal lasaflsplv grlhrigmpr
       61 aiavvltlla glavlgaivt fvveqfvagf prlvadaeqt vsdlqdrlrs grlpftedqv
      121 hsagdtlvhq lqehqsqits galstatalg dvlagvaltv fvtifflygg aqvwhyvtki
      181 vpeahrekar aagvagfasl tgwmrgttav aaidalafvp lvgafvaggl avivalvsng
      241 plaaaivlva ivaivqlegh vlqplllgra vqlhplavvl sittgivvhg iiggllavpl
      301 vsllnasias lraeeardpd epadagdapa aaddapaaad epeg
//
LOCUS       WP_010838385             420 aa            linear   BCT 01-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein [Rhodococcus
            rhodnii].
ACCESSION   WP_010838385
VERSION     WP_010838385.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..420
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44812
     Region          29..331
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          321..382
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(347,349..351,353,369..370,374..375,378,382)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mfdsggggsg nelvevsglv eskrmlacae yrqiraiggf haarvaaean gpvgipgesa
       61 anevalalgm segrvwfait lcedldtrlr ltntafsvge ldlaqvrtih nllqnlsdek
      121 ariveaalfa rgpidrlppa rlsgrlrrlv arydrdgfae rsarakgery isvkqcddgm
      181 aflsgelpsl daamiwnrlk emaigdvcag dersmpqrha dalvaladgs grltcgcgrn
      241 dcataipaag krgplvqivv sdgsvsaggm tagflpgvgp ldpetvreav ahsatqrihv
      301 savdpveaap diaglryrip raladrirar dgvcrfpqca vpaascdidh ttpfdhehpd
      361 qggrteeanl aclcrrhhrw ktqgrmavqq lgdgllrwtm pdgtvydtep dsptfwaaga
//
LOCUS       WP_010838444             259 aa            linear   BCT 01-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010838444
VERSION     WP_010838444.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..259
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26599
     Region          5..248
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 maefvtleve dgigtirlar ppmnalnrqv qeelraasra atvdaavkav ivyggekvfa
       61 agadikemse msfaemsava gdlqsalgav seipkptvaa itgyalgggl evalsadyri
      121 agdnaklgvp etllglipgg ggtqrlarli gpskakdmvf tgrhvradea laiglvdkvv
      181 apddvyeaar awagqftgaa sralaaakas idqgldvdlt tglrievaqf aslfatkdre
      241 igiasfieng pgkaefvge
//
LOCUS       WP_010838452             266 aa            linear   BCT 01-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Rhodococcus rhodnii].
ACCESSION   WP_010838452
VERSION     WP_010838452.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..266
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27857
     Region          3..266
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mtnivvlikq vpdtwserkl sdgdftldre aadavldein eraveealli keaqggeviv
       61 lsagpdratd airkalsmga dkavhvndpa lhgsdaiqtg wtlaaalgqi tfdngepaev
      121 iiagneatdg rvgavpaiia eylgipqlth irkltiadgk asgeretdeg vfgleaplpv
      181 ivsvnekine prfpsfkgim aakkkevtty tladlgvdpd tvgvanagtt vtastpkppr
      241 tageritdeg eggtkvaeyl vaqkii
//
LOCUS       WP_010838508             388 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhodococcus rhodnii].
ACCESSION   WP_010838508
VERSION     WP_010838508.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..388
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42029
     Region          1..386
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maeivldhvs kvfadganav hefdltigdg efvilvgpsg cgksttlnmi agledissge
       61 lridgkrvne vapkdrdiam vfqsyalyph mtvreniafp ltlakmskae idkkvddaak
      121 ildvtsyldr kpanlsggqr qrvamgraiv rspkaflmde plsnldaklr vqmrteiaql
      181 qqrlgtttvy vthdqteamt lgdrvvvmrt gliqqvgepq elydrpvnif vagfigspam
      241 nfvpgrltad gidtalgamr lseerratia rnesaqevvv girpehfeda alltdsvrgt
      301 gtvftaevdv lesmgsdkya yftlegaevs saeleelaad sessiggpql iarlstesav
      361 rqgkpielwf dpakvsvfdn htgrnvgl
//
LOCUS       WP_010838524             214 aa            linear   BCT 01-JAN-2025
DEFINITION  O-methyltransferase [Rhodococcus rhodnii].
ACCESSION   WP_010838524
VERSION     WP_010838524.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..214
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22412
     Region          39..211
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mhtnaerlld haeatvredd alaaardrav evgadpvspa vgaalsvfar mldaksvvev
       61 gtgagvssmw llrgmredgv lttidaepeh qrtaklsfrt sgiapartrl ingtaldvlp
      121 rladssydlv fvdcapvdhp hyvaegvrll ragglivfhn agnggrvadp tqrdrttval
      181 reaakalaad dsllqvfvpl gdgllcaski gead
//
LOCUS       WP_010838548             158 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Rhodococcus rhodnii].
ACCESSION   WP_010838548
VERSION     WP_010838548.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..158
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17130
     Region          9..150
                     /region_name="YdbS"
                     /note="Uncharacterized membrane protein YdbS, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3402"
                     /db_xref="CDD:442629"
ORIGIN      
        1 madprerpsp rarllwslaa allwvpllva aivlfvfspw ptwlhvllva vaavgcavdv
       61 gvvpqwryrv hrweisdtav ytltgwfdqe rriapisriq tvdtergple rllglatvtv
      121 ttassagavr ipaldlavad avtarlteit aaaredat
//
LOCUS       WP_010838650             154 aa            linear   BCT 01-JAN-2025
DEFINITION  peroxiredoxin [Rhodococcus rhodnii].
ACCESSION   WP_010838650
VERSION     WP_010838650.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..154
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16651
     Region          3..151
                     /region_name="PRX_AhpE_like"
                     /note="Peroxiredoxin (PRX) family, AhpE-like subfamily;
                     composed of proteins similar to Mycobacterium tuberculosis
                     AhpE. AhpE is described as a 1-cys PRX because of the
                     absence of a resolving cysteine. The structure and
                     sequence of AhpE, however, show greater...; cd03018"
                     /db_xref="CDD:239316"
     Site            order(25..26,28)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239316"
     Site            order(43,46,117)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239316"
ORIGIN      
        1 mplevgaiap dftlkdqnnq lvsladyrge knvllvffpl aftgtcqgel crvrdelpkf
       61 endesaivav svgaspthki wsaeqgytfp lladfwphga vaqaygvfne dlgfanrgtf
      121 vidkdgvvrf aemngpgear dpgtwekala ales
//
LOCUS       WP_010838658             477 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Rhodococcus rhodnii].
ACCESSION   WP_010838658
VERSION     WP_010838658.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..477
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49954
     Region          22..455
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtvlapeart asetdprdpl arlerlfdpg ttrllherdr sgmlaatgti dgvltvayas
       61 datvmggamg idgcrhvvaa idhaldndap ivglwhsgga rlaegvealh avgrvfeamv
      121 rasgripqis vvlgfaagga aygpaltdvv imapegrvfv tgpdvvqsvt geqvdmdtlg
      181 gprthytksg vahiaardes davhrarrlv smlceqgrfd lgaaehgdtd lrallpaspr
      241 raydvhpivd elldnveghs sfeelqggya rsivtgfgrl agrtvgvian nplhlggcln
      301 sesaekaarf vrmadafgvp lvvlvdvpgy lpgvsmeweg vvrrgakllh afaeatvprv
      361 tvvtrkiygg ayiamnsral gatavyawpd aevavmgaka avgilhrral aaapdderda
      421 lhdrlaeeha laaggvdrai eigvvdeeid partrstvaa alaaapprrg ahtnipl
//
LOCUS       WP_010838690             258 aa            linear   BCT 01-JAN-2025
DEFINITION  siderophore-interacting protein [Rhodococcus rhodnii].
ACCESSION   WP_010838690
VERSION     WP_010838690.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..258
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=27510
     Region          7..242
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 makptatvtv lrteriaphl vrvylggpgf defvpssftd myvkaefdvd getvlrtyti
       61 rsvdterrei aidfvvhgdi gvagpwataa rpgdtltlrg pggayapdps adwhllagde
      121 taipaigaal salpesavgd avievggtad eidlaapagv tvhwvhrgas sdeatderag
      181 dnaplvgavk slpwrageph vfvhgeaqav mhnlrpyirk ergvpaaras isgywrrgrt
      241 eegfrvwkre lsereavg
//
LOCUS       WP_010838754             171 aa            linear   BCT 01-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Rhodococcus
            rhodnii].
ACCESSION   WP_010838754
VERSION     WP_010838754.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Leiros,H.K., Tedesco,C. and McSweeney,S.M.
  TITLE     High-resolution structure of the antibiotic resistance protein NimA
            from Deinococcus radiodurans
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 64 (Pt 6), 442-447
            (2008)
   PUBMED   18540048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..171
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18497
     Region          29..163
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 mtettnepag qlhpdysdpd atpppwsvid gvlrdagiyw ltttrptgrp httpviavwd
       61 grsvwfctgp derkarnlgd rgpctvttgc ndyeagtdvv vegdaervre paelarfada
      121 lhagygddwr fdtvadgveh paggvaavyr vradvvfaft rgpaaqvryr p
//
LOCUS       WP_010838844             313 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Rhodococcus rhodnii].
ACCESSION   WP_010838844
VERSION     WP_010838844.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..313
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32340
     Region          3..273
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mqydvtvvgg gpaglsaaiv larslrsvlv vdageprnap spaahnvlgh egiaphdlla
       61 rgrseavgyg vefrndrvhe idrasgdfav tfadgesvrt rrivlatgvv delpdvpglr
      121 dewghrvlhc pychgwevrg trvgvlgtsp gsvhqtllfq qiagettlfr hdmdgldtdt
      181 aerlaalgvr ivdarvdrie tsgaaldlll gsgeavsvda lvvaphivpr aelftrlgga
      241 valhpsgmah iptgvmgatd vagvwavgnv tdpgatvaaa aaagvqagaa vnldlvtdaa
      301 dravqemrat prt
//
LOCUS       WP_010838979             362 aa            linear   BCT 01-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Rhodococcus rhodnii].
ACCESSION   WP_010838979
VERSION     WP_010838979.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..362
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38734
     Region          98..356
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 msqtrrgglg rglaaliptg paagpglgna aadvvigsas tavatpaqpk qdaetteqet
       61 taagftgntk dgftgnndda taaesgaeql vdpgavyrei plgdiernpk qprqvfddea
      121 laelihsire fglmqpivvr tiedgryqli mgerrwrask eaglekipai vrqtddgdll
      181 rdallenihr vqlnpleeaa ayqqlleefe vtheelatrl grsrsvitnm irllklpvpv
      241 qrrvaagvls agharallal dagadaqevm aarivaegms vrateeavtl anrgdatdpt
      301 pprrkpiqmp glqdvaerls dsfdtrvtvs lgkrkgkivv efgsvddlqr ivqmmetgkg
      361 es
//
LOCUS       WP_010838961             448 aa            linear   BCT 01-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010838961
VERSION     WP_010838961.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..448
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=47932
     Region          3..446
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mttaetdpli attteglvrg rrvdellafr gipyaappvg plrfrapeph epwdgvrdat
       61 eygtasfqpq qytrtglrtv hpigedaltl nvlakpggrd arrpvmvfvh ggayslgmsa
      121 tplyrglslv rradvvfvsi nyrlgvlgyl dfsefstptr cfdsnlglrd qvaalawaqr
      181 niaefggdpa nvtvfgesag gdavttllat paagglfara iaespapalt apadrarswa
      241 kqffefldvd adpataldta dpellgkaga rltravvtdt pglapfgpvv dgdylpeapl
      301 davrsgrahr vplvigtnan egtlfprfld alptsperie emfartdpea grrvtgaypg
      361 ypdddaaiai ggdltfwlps veiaeahsrf aptymyrydf aprllrllrl hathalelfa
      421 vfgegdsvvg rlltalggrr glravsss
//
LOCUS       WP_010839052             324 aa            linear   BCT 01-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010839052
VERSION     WP_010839052.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..324
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33226
     Region          1..321
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(45..46,126,130,151,154..156,175..176,180,195,215,
                     237..238,240..241,262..264,313,315,317)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mraavvsrla gpsaiavvdv pdvdvpdape atdrvvldva asgvcfpdll mtygkyqvrp
       61 dppfvpgaev agtvvsapes tgltpgsrvl afaslggyae rvavdpgava aipdslgfae
      121 aaslvinyqt vefalsrrar laegetvvvl gaaggvgtaa igvakahgar vvavvrregh
      181 ddllrelgad evvrlgdgwg ervrelggad vvldpvggdv fdeavrvlrp dgrlvvigfa
      241 aggipeikvn rvlfrnisiv gaawgeylrt hpgefgrihd dllglvaggl epvvtarygl
      301 pdaaraladl esgaivgkgv llre
//
LOCUS       WP_010839112             544 aa            linear   BCT 01-JAN-2025
DEFINITION  (2,3-dihydroxybenzoyl)adenylate synthase [Rhodococcus rhodnii].
ACCESSION   WP_010839112
VERSION     WP_010839112.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..544
                     /product="(2,3-dihydroxybenzoyl)adenylate synthase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0008668 -
                     2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
                     [Evidence IEA]"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57497
     Region          8..543
                     /region_name="EntE"
                     /note="2,3-dihydroxybenzoate-AMP synthase component of
                     non-ribosomal peptide synthetase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1021"
                     /db_xref="CDD:440644"
ORIGIN      
        1 mttddaaftp wpenlasryr daglwsgrtl gdvlrataaa rpghlavvde rtawtyadld
       61 aavdrlaagl vtlgvspgdr imlalpnrae yvqtffavfr agalpvfclp ahrraeltal
      121 aeasgaiali tvdthdgfdh aalarevaaa spamrdvvll pvtgepvrea vdfaaladgp
      181 tpetlpevaa ssvaflqlsg gstgipklip rthddylysv vrsneicgvt gdtvylatlp
      241 aahnfpmssp gilgtiaagg tvaltlspap saafamieka rvtttglvpp larlwtesae
      301 agtdadlssl dtvlvggarc pdelaarigp algarlqqvf gmaeglvcyt rlddpdeitl
      361 ttqgrpmseh devrvvdddd ndvpagaegn litqgpytir gyyrnaaana rsftadgwyr
      421 tgdvvrrdpd gnivvcgrav dhinrggekv saeeleehll ghpavrdvvi vgvpdpylgn
      481 rtcafvlpad pqappragtl rkflrergla twklpdtvtv ldtfpetgvg ktsrkdlrtl
      541 ltar
//
LOCUS       WP_010839134             284 aa            linear   BCT 01-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Rhodococcus rhodnii].
ACCESSION   WP_010839134
VERSION     WP_010839134.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..284
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30487
     Region          38..220
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(41,43,117)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(68,116..117)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            115..117
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mtapspidpp atatpdvpvv ppaavdsgng phrptvtvvi pamnearnlp fvaarmpdgv
       61 dqivfvdgns tddtmavare lwptatfvtq trrgkgnala cgfaaatsdi ivmidadgst
      121 dpgeiprfve alvggadlak gsrfvapggs sditvlrsvg nkglnglvnl vfrthfsdlc
      181 ygynafwrrh vpvlelappe ysraqwgdgf eietvinvrl atsgleivev gsfegprihg
      241 rsnlnaysdg mrvlrtigqe wrhwratrdi rkqsqradir elsa
//
LOCUS       WP_010839289             246 aa            linear   BCT 01-JAN-2025
DEFINITION  DUF427 domain-containing protein [Rhodococcus rhodnii].
ACCESSION   WP_010839289
VERSION     WP_010839289.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..246
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=27215
     Region          121..237
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 mamhmggmaa mreelrwqpi harvralarg drrvvadtta avlvwepghy vpsyaipgvd
       61 vavalvaaeq psdehtapgt efvaggdetr rgsvyrlsdp dlasyfvfth ddfewleedd
      121 evighprdpy hrvdvrrssr hvrivagrdv lvdttrarml fetgfpfarl yvpredvavp
      181 ltatdarsvc pykgeasywt aevggrlltd vawtydapld gaaaiaglvc fyherfetti
      241 dpapnt
//
LOCUS       WP_010839273             110 aa            linear   BCT 01-JAN-2025
DEFINITION  YbaB/EbfC family nucleoid-associated protein [Rhodococcus rhodnii].
ACCESSION   WP_010839273
VERSION     WP_010839273.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Cordeiro,T.F.V.B., Gontijo,M.T.P., Jorge,G.P. and Brocchi,M.
  TITLE     EbfC/YbaB: A Widely Distributed Nucleoid-Associated Protein in
            Prokaryotes
  JOURNAL   Microorganisms 10 (10), 1945 (2022)
   PUBMED   36296221
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..110
                     /product="YbaB/EbfC family nucleoid-associated protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11264
     Region          12..>78
                     /region_name="YbaB_DNA_bd"
                     /note="YbaB/EbfC DNA-binding family; cl46540"
                     /db_xref="CDD:480880"
ORIGIN      
        1 mttpqpapga pdidaiverv qnqvavldqa lgdlqgvrgr asspdglvta evdgngalvg
       61 lwiddavarh daahvamlvt qtasraaada sahreqlmat faddfadppr
//
LOCUS       WP_010839345             542 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-binding protein [Rhodococcus rhodnii].
ACCESSION   WP_010839345
VERSION     WP_010839345.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..542
                     /product="thiamine pyrophosphate-binding protein"
                     /GO_component="GO:0005948 - acetolactate synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0009097 - isoleucine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009099 - L-valine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57192
     Region          1..531
                     /region_name="IlvB"
                     /note="Acetolactate synthase large subunit or other
                     thiamine pyrophosphate-requiring enzyme [Amino acid
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0028"
                     /db_xref="CDD:439799"
ORIGIN      
        1 myvrdaigrt lhelgvrtaf gvvgsgnfhy tnaftaaggr fvaarhegga asmadgyarm
       61 sgevtvlslh qgcgytnslt gvaeaaksnt pllvvtaeat tpmsnffidq aaiaeglgar
      121 tvrvrsaasa vadvteayrl aaqgrtvvln vpidvqdell pddqvaprvv dvalprpsdg
      181 elaqlvellt taerpvfvag rgarsagake alaaladrtg allatsavsk gmfrehdwsi
      241 dvsggfstpl aaelisdadl ivgwgcalnm wtmrhgklig ddarvvqvdl dpaalgrtrp
      301 idlglwggia etahaattal ghisrtgyrt seiaerirtg lrwndvpytd asteteidpr
      361 iltseidtml paervvsvds gnflgfpsmf ldvpdeygfc ftqafqsvgl glataigaal
      421 aqptrlpvag csdggflmgi seldtavrlg lpllvivynd sqygaevhhf tgdedlttvt
      481 fpdtdiaaia kgfgcdsltv rrredlaavk twldaeparp lvvdaktvsn egswwlveaf
      541 gh
//
LOCUS       WP_010839383             383 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010839383
VERSION     WP_010839383.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..383
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41734
     Region          3..382
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtrlndeetf lvdtvrafvd rdvkptvqqv ehandypekw ieqmkqigiy glavpeqygg
       61 tpvsmpcyaq vteqlargwm slagamgght vvaklltlfg tdeqkqhylp rmatgemrat
      121 maltepgggs dlqamktvar adgddlvvng aktwisnarr sgliallckt dpaatprhrg
      181 isillvehgr gltvsrdlpk lgykgvesce lsfddfrvpa savlggtpgk gfsqmmkgle
      241 tgriqvacra lgvasaaled slayaqqres fgkpiwkhqs ignyladmat kltaarqltw
      301 haaerydrge rcdmeagmak lfaseiamei aldavrihgg ygystefdve ryfrdaplmi
      361 vgegtneiqr nvivgqlver ggv
//
LOCUS       WP_010839418             253 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010839418
VERSION     WP_010839418.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..253
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28974
     Region          3..104
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(51,54,58..59,68,79,83,89,93,96..97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          134..247
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mawtiadvar msgvtsrtlr hydeiglltp arvgsngyry yeeeellrlq qilvlrelrl
       61 glseiadvla khtdevealr ahhrrlvder drlatlvttv artiaelenr kdgsdmtnld
      121 epenlfegfd ttrydadarq kwpqewedsk rfsdslaped hermqretsa qmfrmaelme
      181 adtpvddpav qaeidvhyrg ickfwtptaa aykhlgetla sdaqwkatyd rvrpgladyh
      241 rdamaayada qld
//
LOCUS       WP_010839404             487 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Rhodococcus rhodnii].
ACCESSION   WP_010839404
VERSION     WP_010839404.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..487
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49285
     Region          20..451
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(27..28,31..32,35,67,117..118,120..122,125,145,
                     148..149,152,268,271..272,275..277,280,308,312,365..366,
                     370,374,390,393..394,397..398,401)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mttptialks trgrwivaat vlgsslamld gtivnvalph igssldaqms glqwvlsgyt
       61 lslaslilla gslgdrlgrr rmfvigtvwf avasvlcala ptiamlivar ilqgigaall
      121 tpgslaiina sidendrgaa iglwsglggv asaigpligg wlveavgwra vfllnlplav
      181 avvwvalrhv pesndpdapa kmdyvgsala iaglglltyg lielqplaai aglvamvffv
      241 vverrsphal vppslfrsrv ftaanivtla vyaalggvff lllmqlqiva gyspiaagaa
      301 tipvtllmlv lsaragrwaq qhgphllmti gpaiaalgll lmlrigpdas yvvdvlpgvv
      361 lfglglsalv apltaavlgs vpvvqsgias gvnnaiarta qllavaalpp laglsgigvg
      421 qpeefssgfr iamlicvgll vtgavvaavl irnpsspppa savttaprcd vtgpaiapap
      481 aardggt
//
LOCUS       WP_010839330             206 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010839330
VERSION     WP_010839330.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22025
     Region          29..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 martpdpent arrraailaa aaarfaadgy dgttvaaiar dagmssgnvf hyfpdkaavf
       61 rglvgdalpe rrelvadfva redalpavle fvdlhvaeal dplapglale mfrrvghdee
      121 ltrlcledaa ltidtlatll argqrdgsvd pdldpaetar wiaaivdaaf lntdadaphd
      181 vrpiarttvt rlleprtpqe shdhaa
//
LOCUS       WP_010839435             178 aa            linear   BCT 01-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase [Rhodococcus
            rhodnii].
ACCESSION   WP_010839435
VERSION     WP_010839435.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..178
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18500
     Region          2..169
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtvgyrlfdt avgtcaiawr tagvvalrla epspeeteaa itatlddeth daeppaevar
       61 vvdavrahlg gelddlrwia vdlegipdfd arvyeitrti gpgqtrtygd vaselgspga
      121 aqavgqalgr npiplivpch rvlaasgigg fsagagtvtk rellalerap gfddpvlf
//
LOCUS       WP_010839471             299 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter permease [Rhodococcus rhodnii].
ACCESSION   WP_010839471
VERSION     WP_010839471.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..299
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30492
     Region          24..278
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 msdrftdams rmfefsitgd llrydfvqqa lvagailgll agiigpliis rqmsfavhgt
       61 selsltgasa allvgigvgt gaiigsvvaa vlfgllgaka rdrdsvigvi msfglglsvl
      121 fiwsydgrtg tsfslligqi vapggqglal ltvcavfvvl vlaviyrpll fastdaevar
      181 argvpvrals ivfavvlgvt aalgvqvvga llvmallitp aaaasyvtan pltttilavv
      241 faeiaavggi llslapgvpv ssfvtaisfa iyvlcrifgr srrrsagrvt tghghahah
//
LOCUS       WP_010839470             291 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Rhodococcus rhodnii].
ACCESSION   WP_010839470
VERSION     WP_010839470.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..291
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30998
     Region          14..255
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mppnpsapdp esrsaavelr gaelsfgdrv lwqgldlsia pgefvailgp ngsgktsllr
       61 vllgeldlvs gsaeiagipa qranrnvgyv pqqksmdegl plrgrdlvgl gvdghmwgtg
      121 llrrrrrmqi vddairkvga eafadapvgl msggeqqrlr iaqalvgdps vllcdeplls
      181 ldlanqdlvs slidrrrheh dtavlfvthe inpilplvdr vlylvdgqfr igtptevmts
      241 evlselygtd vevlhvrgrl vvvgtgdaid algsagglrp gegvhhhdgd h
//
LOCUS       WP_010839494             214 aa            linear   BCT 01-JAN-2025
DEFINITION  DsbA family oxidoreductase [Rhodococcus rhodnii].
ACCESSION   WP_010839494
VERSION     WP_010839494.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..214
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23203
     Region          12..211
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(20,23)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 msnendtsri hveiwsdiac pwcyigkarf qsaleqfegr drvdvtwray qlmadtpvge
       61 grrevdalve skgmsreqvl smfdhvaktg advgltldfe kaiaantfda hrvvqlagdr
      121 agevvdglfr ahfaqglavd drdvlldvat eaglerdvva kqlasedgad avrsdlaaar
      181 elqiggvpff vgnrrvavsg aqpedvflql laqa
//
LOCUS       WP_010839495             145 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Rhodococcus rhodnii].
ACCESSION   WP_010839495
VERSION     WP_010839495.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..145
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14691
     Region          4..140
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mptrtartaw ngglqdgsgq velsssqlat fevsfptrsa dsadghtspe eliaaahssc
       61 yamqlsalig eaggtpqave vkadvslgpd dvgfkltgia ltvraevdgv daetfariaa
      121 dakrtcpvsk altgveitld aaleg
//
LOCUS       WP_010839499             193 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010839499
VERSION     WP_010839499.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20068
     Region          11..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 markqnpdag traamitgai asirengvaa tsfadvlars gasrgsiyhh fpggraqlve
       61 datrsaarwl dreidrilet rdvagalrai vdlwrttleq tdyrsgcpiv aaalgpdagt
      121 rdiaaasfta wraviastli ddgatperag slatlvvaal egalvlaqae rtsrpldvvv
      181 delvalcdcs psa
//
LOCUS       WP_010839576             186 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010839576
VERSION     WP_010839576.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..186
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20171
     Region          7..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mteaggrrtg ertrgailda agrafgsrpy aeitlkeiae dagvsaplii kyfgskeklf
       61 eavvdfrgaa dlvfsvprdr lgehivrlfa qprepykpls tsilymsats edsvaklrgn
      121 ysaqmidvla glldgddtrl raelvmsmvt glavmrrrml aehatgavde vvaryaplvq
      181 qlidtp
//
LOCUS       WP_010839598              63 aa            linear   BCT 01-JAN-2025
DEFINITION  ferredoxin [Rhodococcus rhodnii].
ACCESSION   WP_010839598
VERSION     WP_010839598.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..63
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=6642
     Region          1..61
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mrvavdatkc dgygtcfemc psvfrsdewg yastvgdgtv ppdqaavarr aislcaeqai
       61 rel
//
LOCUS       WP_010839618             224 aa            linear   BCT 01-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010839618
VERSION     WP_010839618.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..224
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24671
     Region          11..223
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mddvlaragi fqgvepsava altkqlqpvd fprghiifne gepgdrlyii vsgkvkigrr
       61 spdgrenllt imgpsdmfge lsifdpgprt stattvtevr avsmdrealk awieqrpeia
      121 eqllrvlarr lrrtnnnlad liftdvpgrv akallqlaqr fgtqeagalr vthdltqeei
      181 aqlvgasret vnkaladfah rgwlrlegks vlisdserla rrar
//
LOCUS       WP_010839658             188 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010839658
VERSION     WP_010839658.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20934
     Region          10..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpkvsedhla arrsqildga rrcfaeygyd gatvrrleea tglsrgaifh hfkdkdglfl
       61 alahedarrm advvaegglv qvmrdmlasp qdfdwlgtrl eiarrlrtdp efrrswsqrs
      121 aeltdatiar laaqkeadrl rddvptdvlv eyldlvldgl iarlaagnas sdlsavldlv
      181 ensvrrrd
//
LOCUS       WP_010839686             142 aa            linear   BCT 01-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Rhodococcus
            rhodnii].
ACCESSION   WP_010839686
VERSION     WP_010839686.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..142
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=15801
     Region          1..103
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 maglgelera vmdhlwesse pqtvrqvhea lsarrelayt tvmtvlqrla kkdlvvqrrd
       61 drahrylpvh rreelvaslm vdalqqadrs gsrqaalvhf veqvgadeaa alrealaale
      121 tretsrpsir avpdgdpsrr vs
//
LOCUS       WP_010839701             256 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Rhodococcus rhodnii].
ACCESSION   WP_010839701
VERSION     WP_010839701.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..256
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27002
     Region          128..226
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 msapaaaarr iivdldgtdr talayarlfa aepgsplgva tatvdvrqgg tgqggvghrv
       61 lfavedheaa trllhrrget vttdqwgsvl drfpylgvta eygatehgga edneksgdne
      121 gsgdivaldh vvltsrdrdg avalcsgvlg ldfrldseaf gmrqlffrap atvvevvltg
      181 ddglgglawr srdlaatrtr llaagcevse irtgrkpgtr vatvrdpell lptllleqre
      241 rhdpsastsa afgire
//
LOCUS       WP_010839742             600 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Rhodococcus rhodnii].
ACCESSION   WP_010839742
VERSION     WP_010839742.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..600
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65273
     Region          7..496
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          537..597
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 manlvnleqv sksfgvspll dsvslgvdeg erigvvglng ggkttmlevl tgieepdsgr
       61 vsrvgglrma vvtqrgvlpe gstvadvvlg pldvaehewa gdarirsvlt gigidelgld
      121 arvdalsgge rrrvalaaal vreldllvld eptnhldveg vqwlaehlvn rrtalvvvth
      181 drwfldtvat rtwevvggrv esyeggyndw ifaraerarq adaaeerrrn larkelawlr
      241 rgpqartskp ryrveaaeal iadvpaprdt tqlaafakrr lgrvvveled vrletpdgrv
      301 lvddltwrla pgervglvgv ngsgkttllr aiagdaplsa grriegqtvq igwlrqeldd
      361 lpvdmrvlda vkevaeriml gdkeisagql aerlgfspar qrtpvgdlsg gerrrlqltr
      421 vlmaepnvll ldeptndldi dtlqqledll dgwagtlvvi shdrylveri adstwalfgd
      481 grltnlpggi eeylrrraas gpsrtpsvaa tvgsgsprsq pepgrpalgg aeeraarkel
      541 arleravakl dekesalhva laeaatepdr lqeldaqlrg vvaekndaee rwmelaaeld
//
LOCUS       WP_010839762             238 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010839762
VERSION     WP_010839762.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..238
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25570
     Region          15..234
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 martaaraaq rrtlspidap qtavlianql rekvldgsfg pgeqlseasl agqlevsrgp
       61 vrealqrlsq egllvshrnr gvfvvelsad dvaeiyaard avetaaaqtv fgfpktrkra
      121 avatlskivd gmpaliasgd warvakqdla fhqalvdatg nsrlvriyst laaesrmcmv
      181 hlanaynrph vladehrhlv dlldsgalpe leaaihehmd tavrdltalm qqrdggvl
//
LOCUS       WP_010839776             258 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhodococcus rhodnii].
ACCESSION   WP_010839776
VERSION     WP_010839776.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..258
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28147
     Region          1..252
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtpsteflta rglhksfsgd hgtravlggv dfhvargefv aivgpsgcgk stlftllagl
       61 ddadsgeivl ggeritagvp rcaympqndl lfpwrsvlen aslglevqgv prararerag
      121 tlfaefgldg fedarpsqls ggmrqraalv rtvvqerpll lldeplgald sltrtdmqyw
      181 lqdvwsrfrw talmithdvr eallladrvl vlaprptrva reirvdlprp rtldttatde
      241 ftalerevla alvptvst
//
LOCUS       WP_010839795             140 aa            linear   BCT 01-JAN-2025
DEFINITION  HIT family protein [Rhodococcus rhodnii].
ACCESSION   WP_010839795
VERSION     WP_010839795.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..140
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14689
     Region          3..135
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mtdcpfcaiv hsgapatrvf edertvafld irplarghtl vvprahasgl heltgddaaa
       61 vfataqrlaa amrsgpiaad gvhlvvndgr aamqtvfhah mhvvprhrgd kislaagiat
      121 rrrhdaeqag advraglppe
//
LOCUS       WP_010839794             385 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Rhodococcus rhodnii].
ACCESSION   WP_010839794
VERSION     WP_010839794.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 385)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..385
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41218
     Region          35..330
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msrsistrar igagaaalal salaltgcst teteatgaas eggltpvtlq lqwfkqgqfa
       61 gflaakekgf yeqqgldvei ldggsdivpq tvlaqgqady aiawvpkala freagaaitd
      121 vaqvfqrsgt lqvsfadeni tgpadlrgkn vgnwgygney elfaamteag idpandvtlv
      181 qqqfdmngll agdidaaqam syneyaqlle avdpdtgely tpdkfrtidw ndegvamlqd
      241 aiwastdkle dpayreqtvk fvaaslegwa ycrdnveecr ditvaagstl gashqlwqin
      301 evnkliwpsp agvgtideaa wdrtveiase trnaegqtvl tqepdeaays neyvtealei
      361 lrdkgvdvtg enyapievtl eeggn
//
LOCUS       WP_010839805             342 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010839805
VERSION     WP_010839805.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..342
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36488
     Region          26..278
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(31,34..36,39,51,53,85,104..107,205,207,209..210,212,
                     224..225,228,243..244,247)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(31,35,39,51,53,85,104..107,205,209..210,212,
                     224..225)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(34..36,205,207,210,225,228,243..244,247)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mnavgideda vtgwiaslgv gavapltfer igngqsnlty avrdsggarw vlrrpplgkl
       61 lssahdvvre hrilsalqgs svpvpkvlgl tedpaitdap lvlmsyvdgv vvdsvntaes
      121 ltvdqrravg lalprtlvri hdvdlddagl tdlashkpya prqldrwsaq weksrtrdvp
      181 evdelatvla rnvpeqsevt lvhgdfhlnn vivdpaegkv lsvldwelct lgdpladvga
      241 llaywpeagd svagpfmast legfptrgel vaayaaksgr dvsavgywhv lalwkltiia
      301 egvlrrivdd prnragsggp teklidgivr raldtaeaeg ls
//
LOCUS       WP_010839865             366 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhodococcus rhodnii].
ACCESSION   WP_010839865
VERSION     WP_010839865.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..366
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39334
     Region          1..365
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masiayqqac cvypgaerla vdrldldihd gefvvlvgps gsgkstalrm lagledidsg
       61 aieiggrsmv gvapkdrdia mvfqnyalyp nktvaenmgf alkmrgigid errrkvedaa
      121 rlldlteyld rkparlsggq rqrvamgrai vrepqvfcmd eplsnldakl rvqtrtqiaa
      181 lqrrlgtttv yvthdqieam tmgdrvavlr ggelqqfaap telydrprna fvagfigsps
      241 mnlftapvtd gtlsvagspl eldaatrall sgrssvtagi rpehltvssd gtgidadvvl
      301 leelgnetlv hgevkdpdir tldgepvtfv arsphrapak lgdgirlkqs aptvhlfdpe
      361 sgdrvg
//
LOCUS       WP_010839858             465 aa            linear   BCT 01-JAN-2025
DEFINITION  xylulokinase [Rhodococcus rhodnii].
ACCESSION   WP_010839858
VERSION     WP_010839858.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..465
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46795
     Region          3..427
                     /region_name="ASKHA_NBD_FGGY_BaXK-like"
                     /note="nucleotide-binding domain (NBD) of Bifidobacterium
                     adolescentis xylulose kinase (XK) and similar proteins;
                     cd07809"
                     /db_xref="CDD:466809"
ORIGIN      
        1 mplvagidss tqsckvvvcd adsgeivrtg ahphppgtei dpaawwdalt qavasaggld
       61 dvaavsvggq qhgmiclaen gsvvrdallw ndtrsapaae alvtelgggk awaervgvvp
      121 vaaitvaklr wladheprna dataavclph dwltwqlgga asldtlatdr sdasgtgyfs
      181 aarggydtgl lttalrgrsp rlprvlgphe aagetdtgaa lgpgagdnaa aalglhaetg
      241 davvslgtsg vvaavtdapp cdasglvagf adatgrqlpl vctlngapvl aatarmlgvd
      301 legfsrlals arpgaeglvl vpyfagersp nlpaatgalq gittanltaa niaraavegl
      361 lcslvfaadc iraegtpldr ivlagggars eavariapav ferpvalpad geyvalgaar
      421 qaawtltgel pewsgqgpap rtfeanpepd vvtryreaaa ltfgq
//
LOCUS       WP_010839927             132 aa            linear   BCT 01-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Rhodococcus rhodnii].
ACCESSION   WP_010839927
VERSION     WP_010839927.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..132
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13834
     Region          14..121
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 mseppvpgdd vadvhaaaee feravvanda daisalvtpd wvlvdgdgvg grgtfldlva
       61 sgdlvhnama tvegteriri hgdtavrtar vtntaefggr rfdadewttd vyirtgtgwr
      121 cvashttpva ea
//
LOCUS       WP_010839958             213 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Rhodococcus rhodnii].
ACCESSION   WP_010839958
VERSION     WP_010839958.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..213
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=21877
     Region          7..213
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 msenptlavi ggtgyagghi treavargyg vtvvsrhdpa daapgvtyvr geisdedllr
       61 rlakdhdvva iavsaastdl lgampviaea vdagsarlav vggagslvap gggrlvdspd
      121 fpaafrpeal ahadvltwlq kngdgidwvy lspavgfgsf apgertgtyr tgddtpvfae
      181 dgssqisgad yalafvdela shrhvnrrft vgy
//
LOCUS       WP_010839952             252 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhodococcus rhodnii].
ACCESSION   WP_010839952
VERSION     WP_010839952.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..252
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27088
     Region          1..252
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 maeaspapgr qvlgfqgtdl vypggthald sidltvaage fvsvvgpsgc gkstllrias
       61 gletatagya qvganrigyv fqdatllpwr svrdnvalla eldgvgkaer yrradeaiel
      121 vglagfekhl phmlsggmrm rtsvarsltl dpelflfdep fgaldeitrq rlgdetsklf
      181 adrrfaglfv thsvseavym strvvvmsgr pgrivediav pfdhprepsl rftpeftaia
      241 eqisdalrea ha
//
LOCUS       WP_010839960             195 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010839960
VERSION     WP_010839960.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..195
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20816
     Region          12..149
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mrttfvpadm rpsrvyrlvt asvvprpiaw vstrsvdgvl nvapysfftv asseppilqf
       61 tsvgrkdshr niaetgefvi nigteslvde mnatsaslpp dvdefahvgl tpepsdriav
      121 prvaeapiaf ectlerlldv gncslvfgev vsvsvasdvl addglpdfaa lappsrlgrs
      181 ewgltpptvi rdrpa
//
LOCUS       WP_010840032             486 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Rhodococcus rhodnii].
ACCESSION   WP_010840032
VERSION     WP_010840032.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..486
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51044
     Region          8..462
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 maesetpghg palkrvigpg llllfivgdi lgagiyavtg qmtaqvggia wlpfvlafgv
       61 atltafsyle lvtkfpqaag aalythkafg lhivtflvaf avicsgvtsa stsssvvagn
      121 llagldetfg renglgwfdv pdggtaellv avgfivvlal inlrgvgesv kfnvvltlve
      181 ilalaivigi gfaaaargsg dgdirnlvif edpndkgwfl aitvattiaf famvgfedsv
      241 nmveetknpe rifprtmlsg lgiacltyvl vvvavvavlp vdydsgdegi llhvvrvgap
      301 slpideifpy ltvfavanta linmlmasrl lyglgrqgvl ppilgavlpr rrspwvaivf
      361 stalavgliv vvdrfaqssm vaalsgttgl lllvvfavvn iaclvlkrkp grgffvaptw
      421 ipvvgaavcl flvgpwarts eqmiqyriaa gmigigvvlw vityalrrra hestgftdve
      481 slgddr
//
LOCUS       WP_010840074              63 aa            linear   BCT 01-JAN-2025
DEFINITION  CsbD family protein [Rhodococcus rhodnii].
ACCESSION   WP_010840074
VERSION     WP_010840074.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..63
                     /product="CsbD family protein"
                     /calculated_mol_wt=6403
     Region          2..62
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mgigdkaenk addlggkake avgsatddkd lenegkgdqv kssvkdagek ikdaakdikd
       61 kls
//
LOCUS       WP_010840102             241 aa            linear   BCT 01-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Rhodococcus rhodnii].
ACCESSION   WP_010840102
VERSION     WP_010840102.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..241
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=26940
     Region          21..>224
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maycsvtlwr sssqrpklgy itigevgpdw lerkeadlkp sayrsletvw rvhveprwgr
       61 vrladvdlds vehwiadlgr tktvdgekvk grgpsvvira ygvlagildt avksgrlakn
      121 pargvenlpr kqpkarvyld hqqvealask agdrrtlvll laytglrwge avglrvkhld
      181 llrkrlhvvd navqvnmemh vgtpkshttr wvpvpeflvt elarecggqg trgsrvprpr
      241 r
//
LOCUS       WP_010840121             283 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Rhodococcus rhodnii].
ACCESSION   WP_010840121
VERSION     WP_010840121.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..283
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=30566
     Region          9..220
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mtdddrarnv lwllahpdhr slshalcadg vaylralghg vhlvdlhadg fdpvltdadt
       61 epgaatlsar qrdatehatl ppeilrhqda vraadilivq fplwwygmpa ilkgwfdrvf
      121 tngfafgird aagrvrkygd gglagrrllp ivtagdrata lgprgnsgdl edvlwpllhg
      181 tahytgmapl rphlvasvhh rgdalaetap elrarlngaf aeeplryrtl tggdygadha
      241 laehiapnat gfaihragcd plasrhardh dlrtrrprgd gvg
//
LOCUS       WP_010840172             163 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Rhodococcus rhodnii].
ACCESSION   WP_010840172
VERSION     WP_010840172.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..163
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17891
     Region          1..156
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mkpitpclwf dgdaeaaatf ytdlfddswi thvdrypsgt pggaegevmt vsfelrgspf
       61 iglnggpaft fseavsfeil cdgqaevdry wdaflagggv esqcgwlkdr wgvswqvvpe
      121 rlyelmrmpd rdavnrmtaa mmtmkrldqa alerafggea vps
//
LOCUS       WP_010840176             170 aa            linear   BCT 01-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Rhodococcus rhodnii].
ACCESSION   WP_010840176
VERSION     WP_010840176.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..170
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=19024
     Region          62..168
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mlikeaarra aedtlathwr grdfpvdpfe iaanmgvras eapledgtsg mvisrlrtqp
       61 vifveesetr prkrftcahe lghfvertet lgdlregfaf vdkrtsktda hefyanefaa
      121 nllmpedavr rledegctli rmagyfdvsv paievrlrrl girlvpaasc
//
LOCUS       WP_010840208             498 aa            linear   BCT 01-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Rhodococcus rhodnii].
ACCESSION   WP_010840208
VERSION     WP_010840208.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..498
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55294
     Region          1..482
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdaldvarwq fgittvyhfi fvpltiglap miavmqtmwv vtgkehwyrl tkffgkffli
       61 nfalgvatgi vqefqfgmnw seysrfvgdi fgaplalegl vafflestfi glwifgwgkl
      121 pklvhlatiw laaigvnasa yfiivansfm qhpvgavyne engraeldsi wtlltnptal
      181 aafphvvaga fltagtfvag iggwwmvrhm rkakatttap edaefsenea rqvfrpatrf
      241 allvmlvsgi alvvtgdiqg klmfqqqpmk masaeslcht etdpdfsilt igrhnncesv
      301 vhllevpyvl pylaegrftd velqgvedlq aqyeerfgpg dyrpnlfvty wsframigla
      361 vgslalglag lwvtrkgrvp eqswfgklai aaipfpflan iagwiftemg rqpwvvhpap
      421 ngvdmirltv dqgvsghpaw tvwislitft vvygalfvvw fflirryava gpqesdrpkp
      481 dpgddegpae hetlsfay
//
LOCUS       WP_010840212             224 aa            linear   BCT 01-JAN-2025
DEFINITION  MOSC domain-containing protein [Rhodococcus rhodnii].
ACCESSION   WP_010840212
VERSION     WP_010840212.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..224
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24277
     Region          5..178
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mtalgrvvav cvvhterdsg srraprtaid krpvdgdvqv gllglagdhv cdtefhggeh
       61 kavyayhdde aqrwagelgr dvapgwfgen lriagpvtat davvgerwri geqlvlevtg
      121 prvpcgtfgt wtgerrwvkr fteradtgay lrvvtagpvr agdavrrihv pdhgvtvrev
      181 ftgeqpdrle allaavpdls psateridhh lsraerarda egla
//
LOCUS       WP_010840240             210 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Rhodococcus rhodnii].
ACCESSION   WP_010840240
VERSION     WP_010840240.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..210
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22772
     Region          9..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtvpttrtdr prtgkrdail aaalevfgrd gyadasvaai arvagvakpt vynhfddknt
       61 lfgeamrwgm ahanertdgv igafdpsadd lrgelervge givgclrepv grnvmrlqwg
      121 ersrcpslae egrrnrdrti drlagklarl snagrlcevd peraarqflv lvvddlpais
      181 gfgehavpda qldafvregv dtflaafapr
//
LOCUS       WP_010840292             149 aa            linear   BCT 01-JAN-2025
DEFINITION  RidA family protein [Rhodococcus rhodnii].
ACCESSION   WP_010840292
VERSION     WP_010840292.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..149
                     /product="RidA family protein"
                     /calculated_mol_wt=15604
     Region          1..122
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mtrvgaetvp epprpgmfsn arvvgdrffl sgmhagspdg vvggddtylq aveafrrvre
       61 lteacgahvd divvlrlylt diadkgdvgr argevftgdf pcstlvevsa lvdpgltvei
      121 eaegivgasa rrlpfmhrsv gvgsdvtsg
//
LOCUS       WP_010840333             347 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010840333
VERSION     WP_010840333.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..347
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36096
     Region          3..333
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mgdehdalrs avrdlltkhs dsaavrkaia aehgfdpavw sllcgqigva alavpenhdg
       61 vgagmaeial vqeelgrrlt pspmlgsavl gvrtlvhsdd ddactrllpa vaagertlav
      121 cwadesgwdg ygvtasddvl dgtahyvlgg diadtllvlt dgglyevdpa aagvtrrrva
      181 tmdptrslse vtlsgvrgrp laspgdlaer vrtdavvala aeqvgaaagi leqtveytka
      241 rkqfgraigs fqalkhrmad myalvetars mayaaaesgt aedaaiakvy cseafehvaa
      301 eavqlhggia itwehdaqly fkrahgsahl fgapstylpa lataagl
//
LOCUS       WP_010840427             446 aa            linear   BCT 01-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Rhodococcus rhodnii].
ACCESSION   WP_010840427
VERSION     WP_010840427.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..446
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47639
     Region          23..442
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 msarstimdd nsfraehada ldpatralte rrekslggsy rlfyrrpvhl vrgegqylwd
       61 asgrryldmy nnvaslghch pavveavtrq astlnthtry lhetildytd dllttlpael
      121 dramymctgs eandlalrva kfvtggdgvi vtreayhgts eltssvspal gsgqpiapta
      181 rlvdapdayr vdtpdlgawf aqrvsdaidd meragtrfag llvdslfssd gvlpgpagyl
      241 reaadvvhra ggvviadevq pgfartgeaf wgfarhgivp dvvtmgkpmg ngipvsglva
      301 rtevldafsd ripyfntfgg npvsmaaara vldtirsegl qehsaaigae lltalrglat
      361 rheaigdvrg aglfvglelv sdrtaltpdr alaldvleel rergvltsva gphgnvlklr
      421 pplafasadi awvttaldea ltvlts
//
LOCUS       WP_010840441             370 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhodococcus rhodnii].
ACCESSION   WP_010840441
VERSION     WP_010840441.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..370
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38709
     Region          1..349
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msaitltsvg lrypdgtvgl agvdlhigdg efvalvgpsg sgkttllrti agfltpttat
       61 icidddivag drgtvppekr rlgmvfqqha iwphrsvgrn vgyplevtrt prreratrva
      121 atldlvglgg yenrdpatls ggqrqrvala ralvaqpral lldealsald eplrdrlrle
      181 lraltrahgl tvvhvthdra ealaladrvv vlgdgelrrv gtpeellttp gtpfvaeflw
      241 satllegrld atgfvdtdgs vvaargaitg sdaaeeagtl avlpadvelr apdapdawts
      301 givtsslfgr dasdvviacn gigvrcavrg prprvgdrvg vtvrrasfhp qhrgvlggsp
      361 aalpdtvatg
//
LOCUS       WP_010840492             397 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Gordonia].
ACCESSION   WP_010840492
VERSION     WP_010840492.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..397
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40696
     Region          18..395
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 msgssagvvv vgaglggirv aenlrnngft dpitlvgaea hppydrppls ksvllgkddr
       61 vdlkpaefyd eagitlrlge avtavspadq titlasgatv aydtlvlatg ldprpfpglt
      121 ekvrgvhvlr tyddavalrd eidsastavv igagfigcev aagltargva vslvepaptp
      181 lavalgeqig alvsrlhvan gvdlrtgvgv gnivvsdgrv haveltdgtt lpadivvvgi
      241 gstpvtgyld gsgielaprd vgggiacdat ghtsaeniya lgdvanwlde dgtphrvehw
      301 nhtveqasvi ahqitggdav tasvayfwsd qfdvkiqvlg apradddvhv vdddgkkfva
      361 yysrdgvltg vvgagkvgav mktrpklqtp tpvadll
//
LOCUS       WP_010840536             300 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Gordonia terrae].
ACCESSION   WP_010840536
VERSION     WP_010840536.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..300
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30285
     Region          13..288
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 msestptrtd pirlgyvglg niggpmagsl aawrggltvf dlsseaiakv vekgaaaags
       61 ladlaasadi igicvlddaq vrsvvagpdg llsearpgti itvhstiape taaelaeqca
      121 arevtlldap isggamgaas grlaimvggp reayeklkep faftadmlvh agpevgsgtr
      181 mklarnllhf isftatteaa rlaeaagidi aklgkvvrhs davtggpgai mlrdttapva
      241 addpwygilt gvrtlgekdl tlalalgeel gvdlplgqla lrnlaaglgv phlegegepa
//
LOCUS       WP_010840549             213 aa            linear   BCT 01-JAN-2025
DEFINITION  PaaI family thioesterase [Gordonia terrae].
ACCESSION   WP_010840549
VERSION     WP_010840549.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..213
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22791
     Region          95..202
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 meftledise devarrravy tpltdtvrdl vdavirteva dedldearrr iaevvadlrs
       61 rqmdgafgvr htrentgmaw gnavigvrna lappldvvhv ddgvrsaftl gaayegppgq
      121 vhggvcamvl dhvlgnaasv egpcytgtlt vrygrptplg alvarawvte rngrkrivrg
      181 tisdaqgvtc eaegvfivpr aaddvpsvrw sag
//
LOCUS       WP_010840540             259 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Gordonia terrae].
ACCESSION   WP_010840540
VERSION     WP_010840540.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..259
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27555
     Region          1..239
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msadhidgvr vtgaarefdg rrvldhvdlt idrgefvall gasgsgkstl lrgiggldrg
       61 ftgtieapsa kaivfqehrl mpwmpvwrnv alglrggdte aralraldev glaaksgawp
      121 stlsggeaqr talaralvre pdillldepf galdaltrin aqrlvarlwe ahrpatllvt
      181 hdveeallla dralilragr iaqeivvdlp rprrvtdpaf valrsqllag lgvsgsdaet
      241 dgptttptpa ptpqefthv
//
LOCUS       WP_010840556             232 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [Gordonia].
ACCESSION   WP_010840556
VERSION     WP_010840556.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..232
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24723
     Region          53..181
                     /region_name="Methyltransf_24"
                     /note="Methyltransferase domain; pfam13578"
                     /db_xref="CDD:433324"
ORIGIN      
        1 msqpaapspn apstdrlrva deapgfmpld eaqtlfeiag eylsqpdstk vgveigtycg
       61 kstvflgsag eahdavivtv dhhrgseehq pgweyhdesl vdahtgtldt sarfrrtmfd
      121 aglentvvgl lapsavaaki wgrpadfvfi dgghsmeaaq tdldgwapwv riggallihd
      181 vfpdpadggr ppyeiycqal etgqftevra egslrvlrrd sgevgaplap kv
//
LOCUS       WP_010840597             185 aa            linear   BCT 01-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Gordonia terrae].
ACCESSION   WP_010840597
VERSION     WP_010840597.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..185
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=20679
     Region          41..137
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mdttetptpp itaatpaeft aaeldeafaq fqrtvaeiav srdwdryael ftddadyieh
       61 algtmrgree irawiwrtmt sfpgshmtgf pslwhvvdap tgrvicevdn pmrdpgdsth
      121 itatnitilt yagegrwsce edvynpmefg raamrwceka relgtidesa aawmettgam
      181 fasrr
//
LOCUS       WP_010840635              64 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ferredoxin [Gordonia].
ACCESSION   WP_010840635
VERSION     WP_010840635.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..64
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=7001
     Region          1..63
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mrikadfdlc esnaicvgma pdffdlddnd ylvilqedip adrveelrqv aancpksala
       61 vved
//
LOCUS       WP_010840637             374 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Gordonia terrae].
ACCESSION   WP_010840637
VERSION     WP_010840637.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..374
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37875
     Region          1..374
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfslpesga dvrglardia tsistperva dleatraald adlwrelgga gllglelsse
       61 avgdaggdlg vvenalvate lgralarvpf gphaiaalpv isaqgsaqlr drvlaagatg
      121 davltvavee dlatdlrspt atlstegalt gvkvdvpyae aadmfvvtas gpdgvvavvv
      181 aadapgvvvt ptpstglips aqvefdstpv sgdavlggga dtaatlvara tlaccaeqtg
      241 iverglelta eyarereqfg raigsfqava qrladgyidt qglaltttqa awlldhstgh
      301 tpelqnavat akfwaaeagh rvahtavhvh ggvgldtshp vhryflrakh nefafgsata
      361 svrvigaela aapa
//
LOCUS       WP_010840691             465 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Gordonia terrae].
ACCESSION   WP_010840691
VERSION     WP_010840691.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..465
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=48215
     Region          11..285
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,65,70,75..78,90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,89..92,96,98,136,138,
                     140..141,143,165..166,169,188..191)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,89..92,96,138,140..141,
                     143,165..166)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,96,98,136,138,140,169,188..191)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(165..173,184..191)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mslepgtefa gytvvrkiga ggmgevylvr hprlprhdvi kvlaehvsnd ptfrarftre
       61 adlaaqldhp civsvydrge vdgrlwismq yvrgtdaaal lstvpgglpl advaavgdai
      121 gaaldhahrs gllhrdvkpa nilisaeepg prfpggsvqr rirladfgia rstdggvtsl
      181 tstdlvigsf pysspeqlsa qtldarsdvy slscsifell tgtvpfsart pammihhhls
      241 tpppevsalr pdvpravsdv vrsglaknra drppsagafa aelrsaidtt tfvprfdrtm
      301 raraplapts aptpaplppt vhastaaipt aaatppgsnp agpappsshl ratayselpg
      361 htvpqsdptp stvrasrdlp vldppaagag psrrttasla cgvvavplsv vggmglpvgv
      421 agwylagrgq sssagrlara lcalgivlsl gfiaftvgra vtmqf
//
LOCUS       WP_010840737             571 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-binding protein [Gordonia terrae].
ACCESSION   WP_010840737
VERSION     WP_010840737.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..571
                     /product="thiamine pyrophosphate-binding protein"
                     /GO_component="GO:0005948 - acetolactate synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0009097 - isoleucine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009099 - L-valine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58991
     Region          2..550
                     /region_name="IlvB"
                     /note="Acetolactate synthase large subunit or other
                     thiamine pyrophosphate-requiring enzyme [Amino acid
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0028"
                     /db_xref="CDD:439799"
ORIGIN      
        1 matvnggqll aralaqagtt evftlhgghl dafliacage girltdtrhe asaghaadaf
       61 arvtggfgvc vvtsgpgftn vytalanayl drsptlfvvg applretetn plqggfdqia
      121 aadpvtkway ritdaarvpe ivalairnat sgvpgpvlle lpidvmfgea dddqvrfptn
      181 yrvptrsgad pdavthaldl lhtasnpaiv igggvtfsra eealvtfaet vgvpvfypgk
      241 adgaipadhp lagggllsmg tipalgaptp dvvlmagtra gmftggrasm fpgakiiqid
      301 idaaeigriy dvevpivadc raaleqlaae aagrtwpdws ewaatvkaak gahaagfpda
      361 atdtgkmhpy faakaiveac ppdtifvldg aeapswaeff vavgrpgsvl rlgylgclgv
      421 gpgfaigaar arpgapvvli tgdgaagfhp qefdtmarhh lpvttvvfnn avwgmsihgq
      481 eavfgprgvv vseladsdye kiaeafggig mrvkhiddla pavdkalgag vpacinaeie
      541 pgivhpittm mlgdvtstde ivvpyyenlp r
//
LOCUS       WP_010840734             345 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator [Gordonia].
ACCESSION   WP_010840734
VERSION     WP_010840734.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..345
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37119
     Region          1..134
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          191..326
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mddidgtilr alqvspratf rqlgevagvs eqtaarryqa lrragvmkvv giikpsvrgq
       61 sewvarvrcr pdrmeplass larrrdvafa yvasggaeii cliraplgas gedaiaktfp
      121 arasvtdvsi dlilhafdpg hpasrwtgfg ghldgrdrdl lasaaagagd dtpedaeqdd
      181 sasdapaggg rltaddatli ealvqdgrrp hrelaricgw tvgrvrrrlr aleragalfy
      241 dveilpdrlg fdlsatlwlt vtpsaldqvg telaahdeva faaaisgern lmvsvicrdt
      301 ahfydylrtr vaaidgltgy svsirmrrlk qnaslvvqgr liqpv
//
LOCUS       WP_010840770             328 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator [Gordonia].
ACCESSION   WP_010840770
VERSION     WP_010840770.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..328
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35572
     Region          3..134
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          171..304
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mpddldyqiv halqvaprap wgvvgdvvgv saataarrwe rlvdsglawi vtypgaayln
       61 trcsafvevq assrreelve hlaadrhvat iqrtagdgdl lltvmvpdlg flgdwvqrla
      121 etegvartrt rvvmrvfges erwrvhtlsd adesvlgeyr pehrplvhgp demdlrliaa
      181 laedgrrsav dlaaasglsa ptvrrrltal vaervlsirc evahvisgwp vtanvwaras
      241 srsisalvga lddlpqvrvc cevtgtaniv mgvwlhtige lsefeqqles rvpglvvadr
      301 svtletpkrl gslldrsgcr tgsvpvvl
//
LOCUS       WP_010840776             435 aa            linear   BCT 01-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Gordonia terrae].
ACCESSION   WP_010840776
VERSION     WP_010840776.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..435
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44738
     Region          13..423
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mtasvdspir nsqtaslspa lkqatpvvvd taagswirgt dgrdyldftt gigvtstghc
       61 hphvvaaaqa qcakvihaqy ttvmhtplle ltarlgavlp agldsvfyan sgseaveaai
      121 rlarmatakp niivfqggfh grtvaaaslt tagtrfsagf splmsgvhma pfpyayrygw
      181 dtdtavdfal reldyllqsr vapndtaafl iepvlgdggy lptpprflqg lreradrhgi
      241 llvldevqag fgrtgrfwgh qhadglipdv litakglasg fpisaiaapt almskawpgs
      301 qggtyggnav aaaaaiatld vieseglven arvrgeqlla glrevcaafp gvgdvrglgl
      361 magiefvttd aagnttpdaa aalavqqatt aqgllsltcg psanvvrlip alvvtaeeid
      421 lgvarfaaal atalg
//
LOCUS       WP_010840797             201 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DNA-3-methyladenine glycosylase I [Gordonia].
ACCESSION   WP_010840797
VERSION     WP_010840797.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..201
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=22109
     Region          9..191
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mpddtitiad grarcswaar epettyhdte wgfpvagdta lfervclegf qsglswrtil
       61 mkrdnfraaf agfdieqvar ftdadvarll gdagiirhrg kieasinnar ravelidehg
      121 slesyfwgha psgdhvpgsm ttspesvals kdlkkrgwrf vgpttmfalm qatgmvndha
      181 ygcviraevd aalrdahpqk l
//
LOCUS       WP_010840821             235 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Gordonia terrae].
ACCESSION   WP_010840821
VERSION     WP_010840821.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..235
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25856
     Region          41..195
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpdavngrsd gaatsrspgq htrrydtsrr raaaaqtrsr ildtarglfl sqgyaattva
       61 aiargaavsp dtvytvvgrk pavfreliel alsgtdqpvp gaqrdyvarm laeddarrkl
      121 aiyahavtai qgrlaplflv lrdaaaldtd lrdlweeite rraenmrrla adlastgatr
      181 tdltveeiad ivwtmnssey ysmlvtdrgw tpdrfsnwlh dawcrlllsd pthpv
//
LOCUS       WP_010840834             346 aa            linear   BCT 01-JAN-2025
DEFINITION  TerC family protein [Gordonia terrae].
ACCESSION   WP_010840834
VERSION     WP_010840834.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..346
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=38183
     Region          4..322
                     /region_name="R_switched_Alx"
                     /note="integral membrane protein, TerC family; TIGR03718"
                     /db_xref="CDD:274743"
ORIGIN      
        1 mdvslsvwli tcavivglfv fdffthvrvp hapslkesgi wsavyisiai lfglfvwwqw
       61 gstyggeyfa gyvtekalsv dnlfvfviim akfavpkeyq qkvlllgilm alvmrgifia
      121 vgaaainays wvfylfgafl iftavkllre sddpveheed retrlerfvk rylrthdsyd
      181 rdklftrvng krlatpmlmv livigftdvl faldsipaiy gltsepylvf tanafalmgl
      241 rqlffliggl ldrlvylsig lsiilafigv klvlhalhen tlpfinggeh vavpeistgl
      301 slsvilgvlv ittvasliks rgaaktpqvd saddstdapa pkskdv
//
LOCUS       WP_010840867             310 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: hydrogen peroxide-inducible genes activator
            [Gordonia].
ACCESSION   WP_010840867
VERSION     WP_010840867.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Jo,I., Chung,I.Y., Bae,H.W., Kim,J.S., Song,S., Cho,Y.H. and
            Ha,N.C.
  TITLE     Structural details of the OxyR peroxide-sensing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 112 (20), 6443-6448 (2015)
   PUBMED   25931525
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..310
                     /product="hydrogen peroxide-inducible genes activator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32404
     Region          13..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..297
                     /region_name="PBP2_OxyR"
                     /note="The C-terminal substrate-binding domain of the
                     LysR-type transcriptional regulator OxyR, a member of the
                     type 2 periplasmic binding fold protein superfamily;
                     cd08411"
                     /db_xref="CDD:176103"
     Site            order(110,113..114,117,121,129..133,227,230..231,234,
                     237..238,240..241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176103"
ORIGIN      
        1 mpdrtyqptv aglrafvala hrrhfgtaat dlgvsqpsls qalsaleagl gvtlverttr
       61 rvqltadgve llpraiavte avdeftsaaa gagqplhgal rlgviptvap yvlptllrgl
      121 srrfpdlvpr vveeqtarlv eqlrtgvldv allalpvdmp givevpiyre dfvlalpsgh
      181 alagrrrvdp talaelplll ldeghclrdq alevcrlagv rpdlgqtraa slttavhcvv
      241 gglgvtlipq tavasetasg dlatatfaap rpgrriglvf rasarhdeay helasvigdl
      301 vgatgavtpl
//
LOCUS       WP_010840880             349 aa            linear   BCT 01-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Gordonia terrae].
ACCESSION   WP_010840880
VERSION     WP_010840880.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..349
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=36094
     Region          1..252
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mrtivliglv glaaqlvdgs lgmaygvttt tlllaigtnp aaasatvhla eigttlvsgv
       61 shwkfgnvdw rvvrriaipg aigaflgatv lsslstetaa pvmavillll glyilvrftf
      121 qgiprhnlgk plrkrflspl gfvagfvdat ggggwgpvgt pailasgrle prkvigsidt
      181 sefiiavaas lgflfslgsq ginfawvgai lvggviaapi aawlvrhipp rllgasvggl
      241 ivltntrsll ksdfidapas vrnvfyivia iawaaafays lreylrdren essdavthfr
      301 eeqeealvga egadrsdtat astsdipaae saaepdagat gthsptrts
//
LOCUS       WP_010840913             536 aa            linear   BCT 01-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Gordonia terrae].
ACCESSION   WP_010840913
VERSION     WP_010840913.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..536
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=57733
     Region          26..536
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 msapavdsst raltsaqtsk lgratigdql rrlarsqgst paivaydaqg grtstsyael
       61 damanrvahv lldlgvgrgd rvavmsrnrv etvatyygal kvgaaysgvs pmfregevaq
      121 qlrhleptvl vveeplsala gpiadglgis vlvvgddean swnsfdesva aaddsepdcd
      181 vdehdlamiv ytsgtestpk gveiahrnyl istspaytwg lrcrnddvwl yvmpfhtiag
      241 igsltsltll gatlvlpaav dpatalrmir dekisvlaqt ptffialanh pdfgpatvgs
      301 vrrcltyggq vsphavdawa aatpesvwgt ywgqseltql gsvgwfrrle dvpdqdptwi
      361 gkpvghlevr vvdadgndae egellcrtps vmlgyfkdpe rtaqvfeggw vhtgdivrid
      421 aegnlffrdr rkdmiktggf nvasqeverv lqahpdvera avvglpdpyw seavtgfvvl
      481 rpgaehtgad ireycrtdla sykvpkevyv vdalptdaqg kllkrelrka ygtgqg
//
LOCUS       WP_010841029             542 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Gordonia].
ACCESSION   WP_010841029
VERSION     WP_010841029.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..542
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58633
     Region          4..537
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mitatdlevr agartllsap gdalriqpgd riglvgrnga gktttlrila getepyagsi
       61 rrsgelgylp qdpkegdldv lakdrvlsar gldeilrdme kqqaamaeaa ddklrdkava
      121 rygrleerfs slggyvaese aaricnslgl pdrvlnqplr tlsggqrrri elarilfaas
      181 dgsgksdttl lldeptnhld adsiawlrgf lqnhegglvv ishdvdllad vvnrvwflda
      241 vrgeadiynm twkryldara tdeqrrrrer anaekkasal rtqaaklgak atkataaqnm
      301 lkraermida lddervadrt arirfpepaa cgktplmtsg lsksygslei ftgvdlaidk
      361 gsrvvvlgln gagkttllkm lagvekpdtg rlepgyglki gyfaqehdtl ddqatvweni
      421 rhaapdageq dlrsllgafm ftgpqldqpa gtlsggektr ltlaglvssa anvllldept
      481 nnldpisreq vldalrsytg avvlvthdpg aaaaldpqrv illpdgtedh wsdeyqelie
      541 la
//
LOCUS       WP_010841145             316 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: endonuclease/exonuclease/phosphatase family protein
            [Gordonia].
ACCESSION   WP_010841145
VERSION     WP_010841145.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..316
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34120
     Region          1..314
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mtrflwaaay vlgwamlagv vlgvflhfyp srgdvalylt sgvqfalipg liaivvfgvl
       61 rrwfmlalav vaagalaytq vplvvaepvp agerftvvss nllfgggdlg vlekivadad
      121 pdllslqevt pealerlrrs eigralphqf aipytyaagt alfskkplde rynipgtvlh
      181 nlqartdlpg aagtqvlaih paaplwgrnw dwladmdtla ehfeqlppgr viaigdynst
      241 wnhakyrnll tnglvdgtdl agagflpsyp tdkrignrpl vaidrvilrg fvatsmdthy
      301 lpgsdhrtlv vslvas
//
LOCUS       WP_010841176             217 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Gordonia].
ACCESSION   WP_010841176
VERSION     WP_010841176.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..217
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23831
     Region          19..191
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mgpsdsahrq sldlselgdd elagaaavgd teafdvlvrr vtpgllryml rmvdgqqtae
       61 dltqetllda wkglpdfafr ssfrtwmfti ahrkaadhhr rrrdvpfdde rfaeleaagp
      121 lpsdmaersl lidalraeld nlpatsraaw wlkevegltl eeigqvlrit tgsvrghlqr
      181 srkflltrla pwnpgkpttt ptattivgna eggeaga
//
LOCUS       WP_010841208             234 aa            linear   BCT 01-JAN-2025
DEFINITION  cysteine hydrolase family protein [Gordonia terrae].
ACCESSION   WP_010841208
VERSION     WP_010841208.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..234
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24633
     Region          22..207
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 msdtvtldaq pgpieldlah taliiidmqr dfllpggfge tlgndvsqlq rvvaplagll
       61 daaraagmri vhtreghlpd lsdcppakln rglpskrigd pgafgrilir geyghdivde
      121 lapldtevvi dkpgkgafya telaailadn ditqllvtgv ttevcvhttt reandrgfec
      181 vvvsdcvgsy fpefqrvgle miaaqggifg wtapsedvia lltsataedv vgsa
//
LOCUS       WP_010841239             245 aa            linear   BCT 01-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Gordonia terrae].
ACCESSION   WP_010841239
VERSION     WP_010841239.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..245
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=25564
     Region          1..233
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mtptlvlvah gsrdprfgat arrvrdavas slpgvevvls yldldeplvg dvlgqlggsh
       61 sthhgpvvvp mllsagyhhk idlpsiiasr rptarqtdvm gtrslagala drlieaglgp
      121 hdgvilsavg ssdpaadrsv rlraielstr lhrpvevvfa tklgphnrav vsavrrlrag
      181 garriavspy flsagllter vesaldalvd dtlvagplgt hpdvieaigs lyrtavgqra
      241 vpagr
//
LOCUS       WP_010841268             447 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Gordonia].
ACCESSION   WP_010841268
VERSION     WP_010841268.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..447
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47861
     Region          18..421
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(31..32,35..36,39,77,135..136,138..140,143,163,
                     166..167,170,252,254..255,258..260,263,290,294,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtndapstpd epdgrtpkra alasfmgsav eyydfflfgs aaalifphvf fpsddeaalv
       61 msfatfgfay varpvgafil ghfgdrigrq rvlmftlvlm glstfligcl psfetigwaa
      121 pallvicrlm qglsaageqa gassltlehs pddrraffts wtltgtqggl ilaslvlipf
      181 vslpdeakys wgwrvpfwls avvvvvayfi rrqlhetpqf aeakaagtia rvplvpllrd
      241 hwrdvlrvil cafiaavstv fgnlaiaygk evgldtdvtl wlvvvanvva lgtqpmfgil
      301 adrigrkpvf vygavssavl mpfymlsmsg dnnlltfala vatfscgyaa anavwpsfyg
      361 emfstrvrfs gmaigtqlgf lvagfapsiv talggvregg wvvisiftav vclisaaaal
      421 taretkdvpt tmlghkvpes akdlvhh
//
LOCUS       WP_010841182              65 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: CsbD family protein [Gordonia].
ACCESSION   WP_010841182
VERSION     WP_010841182.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..65
                     /product="CsbD family protein"
                     /calculated_mol_wt=6512
     Region          2..65
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mgfsdkvsnk aedlsgkake tagdvtgddq lksegkgdql saavkdgves vkdaasnikd
       61 klsgn
//
LOCUS       WP_010841269             249 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Gordonia terrae].
ACCESSION   WP_010841269
VERSION     WP_010841269.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..249
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26024
     Region          8..249
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 magntsvpga tvasrvlaii gafdeghral tltelaqrsn lvlptasrla gelvaggald
       61 rrgdgryvig rllweaglqa pvegrlkqva epflhdvyaa tlatvhlavl dgaqvlyler
      121 magrasvpiv stvgsrlplh ctgvgkvlla haskdverqa lanltrvtpy titapnilva
      181 qlekvrrdgv attveemslg acsmavpvir vsddtvaaai gvvvptlkrd rqrllgalqv
      241 aargigrll
//
LOCUS       WP_010841275             685 aa            linear   BCT 01-JAN-2025
DEFINITION  M3 family metallopeptidase [Gordonia terrae].
ACCESSION   WP_010841275
VERSION     WP_010841275.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..685
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=74942
     Region          7..685
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 mtaahdaanm npvleqsglp ydlpdfasis dddflpafta amashvaevd aiaadpaapt
       61 fvntiealel sgrdlarasg iffnlvgpdt npkrneisqe lstlltdhan tiamnpvlfe
      121 risdlhtrad elgltepqrr lldkryresv ragaglaage qqemreiasr layltttfsq
      181 kilddtndsa vlvadeseld glsagqiaaa rraaveaghe nghlitlelp tsqsvltelt
      241 nsdvrqrvfd asvnrcargn ehdtrelvle ivrlrarrae llgyrdhaef viaeqtapdp
      301 gavddmlrel nasamraggr eltrltefag datigpadlt ywldrekrth aavpldgfad
      361 yceldtvltr gvfhaankly glrfveltdl plyhpdvraw evrddagvgi glflgdfyar
      421 pskrggawmn nivdqssvlh tqpiivnvln ltkpdagqpc lltmdqlttl fhefghalhg
      481 llssveypsq sgtsvprdfv efpsqvnemw alhpevlgny arhhetgepi paelaeaare
      541 sagtesahgt ieylaassvd lawhrlsvse aeavsdveaf esqaltaagl htdlippryr
      601 ssyfnhifgg gysagyysyi wsevldaete qwflaegglq rengrrfaea tlsrgdsvdp
      661 lvahegligr rpridpllrr rglaa
//
LOCUS       WP_010841285             470 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Gordonia].
ACCESSION   WP_010841285
VERSION     WP_010841285.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..470
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50029
     Region          8..460
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtvehpgtdt gadtdegyqr gltartvqmi aiggaigtgl fygaggaiek agpalilaya
       61 laglaifivm ralgelliyr pvsggiseya deflgrfagf sqgwtywavw tttcmaeitv
      121 agkyinywwp svpvwvtali alivlfganl isvgvfgrae fwfsaikvta ilgmiivgig
      181 vllpiaglgp etgpsvtnlw ndggffatgf snallslqiv mfayvgvelv gvtageaqnp
      241 rvtlrkaint vpfrigifyv gslivilsvr swkdfqeges pfvsvfsyig ipgaagivnf
      301 illtaalssc nsgiystgrm lrslahtgda prqltwlssr kvpaagitls aavmaigvvv
      361 nvidpehafa yitavstvgi iviwstillc qmayrrkvar gelprsdyrv pgapvttwla
      421 lgflalvfvl lffdrdgria lvvgavwfta vgigylvwnr tageladrev
//
LOCUS       WP_010841314             192 aa            linear   BCT 01-JAN-2025
DEFINITION  HU family DNA-binding protein [Gordonia terrae].
ACCESSION   WP_010841314
VERSION     WP_010841314.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..192
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=19766
     Region          1..92
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mnkaelidel tkkldadrkt ateavelvvd tivravnkge svtitgfgvf ekrkraprva
       61 rnprtgetvk vratsvpafr pgaqfkavva gkqklsatgp avkrgsgttt taakkaapak
      121 ktaakkatta akkttaakka pakttaakkt ttaakkapak kaapakkata akkapakkap
      181 akktaakktt rr
//
LOCUS       WP_010841331             400 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Gordonia terrae].
ACCESSION   WP_010841331
VERSION     WP_010841331.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..400
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=41180
     Region          225..370
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mserdtsgts grdtpatspy deptgqipvp gtgggvpgag tgpgaarpea gpptppavtd
       61 rddfynrhar rspapysrvd dlddldpgdv etrpaaagpp ttsspaappp rsaapatgpa
      121 apadddfetv qfatppgpar vppaddavtt pepalppagt arydfldddd dassrtrard
      181 esaatevldd eprarrrfgr rrtdddtdvr pdaaadddle ealaksrrgt idlgllvlrv
      241 algglvgahg lqklfglwng prlsgfesml vdagftadya qilaivgals etigglmvil
      301 glltpigasa ilgtmlvaaa fkmsmadgfs ffaaaggvef elflavaaav viltgpglys
      361 ldyprgwarr pfvgsflwli vgaaaavavw vlangsnplv
//
LOCUS       WP_010841383             208 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Gordonia terrae].
ACCESSION   WP_010841383
VERSION     WP_010841383.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..208
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22334
     Region          21..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpngpdhspl hislnpsgte radaarnrrl llaaaknlid hhgaaavtme avareagvgk
       61 gtvfrrfgsr tglmlalldh seseiqqayl sgpeplgpga ppldrllayg rarlkltsdh
      121 ldvlleagag aedfmshpva rtstqhvqil lrqlgfddsl dflaltvqap msassvryll
      181 vdvgldleti trqwqemvta lvtghhrd
//
LOCUS       WP_010841317             244 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Gordonia].
ACCESSION   WP_010841317
VERSION     WP_010841317.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..244
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25593
     Region          10..224
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mgkdtasavs sgigvldksv avlhaiaeap cnlselcert glpratahrl avglethrfl
       61 trdvtgrwqp gpvlgelass ahdpitesal mvlprlrdit gesvqvyrre gaervcvaam
      121 epptglrdtv pvgtrfpmsa gsaakvllaw adpatqralv pdsifseral heirrrgwaq
      181 sageraagva svsapvrdgn gdvvaaisvs gpidrmgrrp garwaadlla aadaihkrlq
      241 aarp
//
LOCUS       WP_010841421             345 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Gordonia terrae].
ACCESSION   WP_010841421
VERSION     WP_010841421.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..345
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36365
     Region          3..343
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtsgnslevs dltvayggda vidglswrlg gegslvtail gpsgcgkstl iraiaglesp
       61 vrgtvrfggv dlagvevhrr dfgvvfqdgq lfggrsvasn igyglrmrrw srraiaervg
      121 emldvvglag ydtrlvdtls ggqaqrvala ralaprprll lldeplaald rrmrdelave
      181 iseivraagv ptmvvthdht eaatmadeia vmrdgvmiqt dapaalwrrp vdewtvrflg
      241 attvidaqvr sgvadtvlgg mpldlpdgsr rlglrpesvs vgplssreae daaatvvlva
      301 elpggprvri dtpigeidav tntsvaigdr vrmrlvperv avigp
//
LOCUS       WP_010841433             151 aa            linear   BCT 01-JAN-2025
DEFINITION  flavodoxin family protein [Gordonia terrae].
ACCESSION   WP_010841433
VERSION     WP_010841433.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..151
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=15784
     Region          3..148
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 msrllivhht pspacqemfe avvsgatdpe iegvevvrra alavtatdfl dadgyilgtp
       61 anlgyisgal khafdvsyyq ildstqgrpf glflhgnqgt egavravdsi taglgwtkaa
      121 ehvivsgapd keareacwel gatvaaqlme g
//
LOCUS       WP_010841467             168 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Gordonia].
ACCESSION   WP_010841467
VERSION     WP_010841467.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..168
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18449
     Region          17..164
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 misvprvhra qaddidaatl yrilrlrvev fvveqacpyp eldgrdlept trqfwitdga
       61 dppegageda tdgagtvlat lrlleepqtd ggqvfrigrv cternhrgrg lvatlmtaal
      121 devgdrpcri eaqtyltemy gkfgfardgd dyledgiphv smlragsr
//
LOCUS       WP_010841569             764 aa            linear   BCT 01-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Gordonia terrae].
ACCESSION   WP_010841569
VERSION     WP_010841569.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..764
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83472
     Region          351..671
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mevaialsli aapllvvlga vftmrtnkqr eydrdhrtiy kivfphdvpv draaamistl
       61 pasikpskgs lsvptmvfet intggvfsfr vrvpsahaey vvgqlrsaip giavepvgae
      121 ksslgefnag ydlgmtlpdr qievankpad favsllnsms pigdevlvyq wvvagtnklk
      181 lpeddervqs tdfswrkall gkteasrdek ssrrakvate pnflaalria arsqhpdrsk
      241 alchntimal kasdgvkvkf qyrevsaglt smmneawtpi sphlqlsvse lvprlgwalg
      301 sdfvegvara sfrhlpagpe vpedgivvgv ssltgrerrv alpagdgltk hlliagatgv
      361 gktflaqnil iqhisrggga iimerdgdlm sgtlsrihrs ffdrvvvvda tdlvnfvgin
      421 pfdfespmvi aakladlfer iykingvnlr kilfhgipal aetgdatlld liplvdpktp
      481 advrwsrdri srleskeliq ffkdwnaksa drrskdmepv lnrfweltld pqvsrmlnhs
      541 hstidlgaal rdnkivcinl kgvdsrlaev igsllaswiw gqaasnapae hdnllfldea
      601 hlfshletti ndmlatarkr klgvvmatqf veklpvsvqq elstnartki vmqsgpnsaq
      661 tlsrefasre vnaamiqnle kytaiarlvl pgggtstpit irtldappvi sdpnaavels
      721 nrkfarsaaq vdadqkarrh vaskgkqrpd igdepvlgdw kddf
//
LOCUS       WP_010841649            1574 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Gordonia terrae].
ACCESSION   WP_010841649
VERSION     WP_010841649.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 1574)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1574
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..1574
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=172408
     Region          3..1573
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mtslvpdavn hyfrsrtdgs aggaaadqvv rhldaarvrr rgqalvevta geggtveilv
       61 vnddmpmlve avlatveahd ltvdhmdhpv mpvrrdpdgt lvavdtgett feswivvngl
      121 arhpgidpep lrddlrevvs rvidvdadas emrsrmveca agladaslrr tgaadadrge
      181 yaallewfag nhfhplgysr vgvdgsaddt erlgvwrtds idrdfpsvtd qplvprvsrv
      241 fvatgiqrtn fpvllqvptf dssgehigeq rflgtltsag nhqavldvpv lrgkvhavla
      301 qagveedsya gqsmiellqn yplvemfsst edelerrvte mldavatrsl rlfvrtnfdg
      361 rtavaliylp rdrynthsrl aleralvaev ggtaleytar vsemplallq vlvcidpata
      421 telgsldtgs ptharmqaal vaairgwder vrelavadei pgldggpdvl lrhlsslsed
      481 ykelrepraa ladlirvvgl qpgeidvtld aaegdgqqdr wtftlylcga satltdvlpv
      541 lhslgldvle ehpyeihrld etvcwayefs vqlaagmtvd ldhsddlaqr fteafrriwl
      601 agadvdayne lviragldwr saamlraygq ylrqcgfsys pahvasvlgr hlaitrglvd
      661 lfvasfdpdt adeerreqvr dkldeeiglv lnldadrivs afaavltatd rtnyfvggrs
      721 agtdhspvis fklrprdipq tpkprpvhei fvysprvegv hlrfgsvarg glrwsdrred
      781 frteilglak aqavknaviv plgakggfvv krppppsgda akdreaqrde giacyrqfia
      841 glldvtdnid lttgevipar gvvrldsddt ylvvaadkgt asfsdianev sksygfwlgd
      901 afasggsagy dhkamgitar gawesvkrhf remgtdtqse dftvvgigdm sgdvfgngml
      961 lsehirlvaa fdhrhifvdp dpqaatsfae rsrlfglars swadydpeli sdgggvwerd
     1021 rksipisaqm aetlgiddgv delsppelir aillapvdll wnggigtyvk asteshgsvg
     1081 dksndpirvd gnevrakvig eggnlgvter griefdlagg rintdaldns agvdcsdhev
     1141 nikilldsav sageldpddr dpllesmtde vaelvladni sqnselgfcr sfeltrvevh
     1201 armlehlaak rgvdlrleal peprelrrrv dgelhrglts pefatlmahv klesksdlla
     1261 tdlpdndvfa priaryfpda vrarypdais ghrlrrqiva ttlvndvidh agmthlfrls
     1321 egssctteeg vrayvvsnkv fgmnevfegi rhapapveav demmlyarrl lfrasrwlla
     1381 frpqplamaa eitrygerva alsavagdwy gpssrrdvae raqtyvdhgv pedlahtvaa
     1441 slhrfclldi idaaeiadrd dnevgelyfa vmehfgleql ltavsgldyg drwhalarla
     1501 vrddmhgalr altlkilevs epeestaeki aewesshsnr lsrvrsvlre ieetgttsla
     1561 tlsvaarqlr svir
//
LOCUS       WP_010841654             137 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-binding protein [Gordonia terrae].
ACCESSION   WP_010841654
VERSION     WP_010841654.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..137
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15115
     Region          15..135
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mtentatrtl eeitsletmd hihalladll aecpiddmda mqfelavaei ganivehare
       61 gstvtlrlel evtsdriear ysddgnparv dldavslpdd faergrglai ainvldelay
      121 rradgknhwr lvrnrsa
//
LOCUS       WP_010841668             432 aa            linear   BCT 01-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Gordonia terrae].
ACCESSION   WP_010841668
VERSION     WP_010841668.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..432
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=45674
     Region          8..408
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkalkhpalq igfgaiagli fglvvgewaa nlkfigdmfi rliqmsivpl vlasvivata
       61 smsgagtgri afrtvkwmlg favvaavlaw glsvlirpga gmvfdgeldp tledeagqtt
      121 gwqdtllnfv sknvfeamst atmvpiiifa llfgvalrmq itksgddrvl tfidqiqqii
      181 ltmirlvmyi apigvfclla slagdvglsv vttavkylgt talgvailfv lfvvvvtart
      241 rlnparlpgk laeqttiait ttssavtfpt vlkntvekig vsqkianftl sigltmgsyg
      301 avlnymivvm flaqagnvel svgdialgmg laillnmgti tvpggfpvia tflatsldlp
      361 leavgiliav dwfagifrtf lnvngdtfva mlvanaddei drdvyndkkt vvseeidvse
      421 ysgafaradd ad
//
LOCUS       WP_010841701             209 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: rhomboid family intramembrane serine protease
            [Gordonia].
ACCESSION   WP_010841701
VERSION     WP_010841701.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..209
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22659
     Region          22..187
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mssytppvgq qptrrarplw lrsaiitvci vavlfvieai daatrydldq ngiqprqvdg
       61 ldgilwapml hgdwphlfan lmpgavlcfl vlmtrrfliv tgiiwavsgv gvwlfaapys
      121 vtvgasgivf gwltflivrg lfnrdlwqil gglvlflvyg silwgvlpsd pliswqahlf
      181 gaiagvfaaw alaardrrrp aagtpgvap
//
LOCUS       WP_010841874             224 aa            linear   BCT 01-JAN-2025
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Gordonia terrae].
ACCESSION   WP_010841874
VERSION     WP_010841874.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..224
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24438
     Region          2..224
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mieftdvsha ygdrvvlrev sltlaerrig ivgangsgks tlarminalv ipdsgtvtvd
       61 gltvaknkre irrrvgfifs dpdrqiimpt vredielslr rtglgkaara dralevlarf
      121 glgdhadhpa qrlsggqkql lalasifvtd paiivadept tlldlrntrm ltdvfatlde
      181 qlvvvshdld iladfdrviv vdegrvvadd eprpalaayr emms
//
LOCUS       WP_010841821             259 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Gordonia terrae].
ACCESSION   WP_010841821
VERSION     WP_010841821.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..259
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26484
     Region          2..207
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mkivvvgasg vlgsrvadll vergqevvra nrasgvdayt gtglaaafdg adavvdclsl
       61 ltlkaaeaid ffettathig raattagvkh vvvvsivnad vpavnakfgy yqgkaaqeaa
      121 yakvvdpaal tvlasvqwfe laeqmmsrmr fgpvaavprl rcapaavadv avavvdevta
      181 gpsgkrkvei ggpvemdlvd vakavaaqtg sprwvlgvrf ggpairgggl vpahpdvvtt
      241 ttldgwlagr eraraggrr
//
LOCUS       WP_010841892             154 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: tRNA (cytidine(34)-2'-O)-methyltransferase
            [Gordonia].
ACCESSION   WP_010841892
VERSION     WP_010841892.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..154
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=16995
     Region          1..154
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 mfrimfyqpc ippntgnair laantgcelh lieplgfsms daqvkragld yhemanvtvh
       61 pnlvtawttl kpervfafta haerfhtdvd yqpgdvllfg peptglpaev ldepevtdrv
      121 ripmlagrrs hnlanaasiv vyeawrqhgf dgav
//
LOCUS       WP_010841917             318 aa            linear   BCT 01-JAN-2025
DEFINITION  C40 family peptidase [Gordonia terrae].
ACCESSION   WP_010841917
VERSION     WP_010841917.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..318
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32849
     Region          143..317
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mipvelliep lrqlvaalgt gvlapgnpae rvradastle evrrrsmsat esvhtrwdga
       61 gsagadaatt airqqlaevt gcatefgrlv edasrtvhaa atgltglvds lerhvrglag
      121 glatpaglla ilpiavehlg rgveivtrar aelgsdteam aglarrttpa evtgvasgle
      181 qlstaptpgg ipitlpdgsv ayapnqraat avraalsqrg vpyvwggttp dgfdcsgftq
      241 wayrqaglel prlaqeqdta gvpvsqahlq pgdlavwsgh vamyigngqm veagdpvgvs
      301 pvrtsnldqa fegffrpr
//
LOCUS       WP_010841951             701 aa            linear   BCT 01-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Gordonia terrae].
ACCESSION   WP_010841951
VERSION     WP_010841951.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..701
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=74949
     Region          1..689
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtaigtshar idgadkvrgt apyayehltd avylwpvtat vargrmtgfd taaaestpgv
       61 llvlthenap rladtsngdl tilqspeiay rgqligavva espetareaa aavtvtyded
      121 dhdtefrvdh pgsyrpeqvn ggfeptsldg dpdrildraa vdpahtdlvt idewystpee
      181 hnnpmephtv vatwqpddst ltlydstqst qgvvstlapv lglepeqirv vaphvgggfg
      241 skgsphshdv laafaamslp grpvkfavtr qhmfvyvghr aptrsrlrla adrtghlial
      301 vheahthsah akefaeqaav tsrsmyaaen rrtdhhvvpl dvpvpfwmra pgeapgmfag
      361 evamdelaha tgidpielrv rnepsedpet gnpwssrrll dclregaarf gwdrraaepg
      421 arrdgrhlvg lgvasstyph mvqpgneasi ahrsgrysvr iaatdigtga wttllliaad
      481 alevstdvvd ieigdsalps atvaggssgt sswgsaivta ahqfrarfgd dppegaelsa
      541 eaadnpdlek ftvasfgahf vevrvdvdtg eiriprmlgv fsigrainpr tvrsqliggm
      601 tfgismalhe esvrdhrfgh vvtqdlaeyh ipvhadiadv daiclddrde hatpmgsrga
      661 geigivgsaa avvnaihnat gvrvrdlpvh lddlldglpd q
//
LOCUS       WP_010841954             436 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Gordonia terrae].
ACCESSION   WP_010841954
VERSION     WP_010841954.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..436
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=46743
     Region          5..406
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 matsrprvvv igagfagmhc vrrlknepvd vtivdrgtsh lfqpllyqca tgllsegais
       61 spvrhltrrh knldvvlgea sgidvdarel tvdridgssf hlsydylvva agmrtayrgn
      121 edfaahapgm ktlddalsir rkimaafema etitdpeeqr swltfavagg gptgvelagq
      181 irevatlale refdaidpaq arvlllhggd rvlpsfssrl sasaqrtldd lgvethlgvh
      241 vtgvgedfve ttrkadgskq tfparttlwt tgveavpfat tlaqalgveq drggripvep
      301 dlsvpghpdv fvcgdmssyr dlagvaevam qggrhagsvi aetvagqadr spfkyrdlgt
      361 aayiarrhai vqsgplqlsg flgwvawgvi hiaflagvrn rmgtvmtwga tlltdsrrer
      421 aitygdpeta rqpygg
//
LOCUS       WP_010841964             316 aa            linear   BCT 01-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Gordonia terrae].
ACCESSION   WP_010841964
VERSION     WP_010841964.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..316
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34233
     Region          9..218
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(50..51,53,67..69,75,77..78,118,218)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(50,52..53)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(75,78,81,87)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(110,114..117,119)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(115..116,139..141,192..193)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          234..315
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 maltdvvvsa ivqetpsikt fylsrpdgst mgeytpgahi dvvgptaitr qyslcsrpdg
       61 resfavavkr edqsrggsaa lhelrvgdrl qiseprnllg idpaathhvl vaagigitpm
      121 lsmarhmdvh gisfelhyfa rtaedaaflp llrercpekl hahvgvgrea hgailttale
      181 sapqqshvyv cgpdgfmtkv relaerfvpa davhfenfha tdqpdasent afdveldgqt
      241 yhvpadrsiv evleengcdv dtscqegicg tcimqvlage pehrdnvltk aeresgevia
      301 vcvsrtsgek ivldyy
//
LOCUS       WP_010841966             431 aa            linear   BCT 01-JAN-2025
DEFINITION  amidase [Gordonia terrae].
ACCESSION   WP_010841966
VERSION     WP_010841966.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..431
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44686
     Region          3..431
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mssaywkhpi seqatavhek vvsaevlaqq vreeiirtdt elhawvelsp tvvddarrqd
       61 ampgrrplrg vslgvkdlid vsglptrags pitssspass dapcvsrfrd lgavvqgktv
      121 ttefgyfspg ptrnphhheh tpggsssgsa aavgagvipv algtqtagsl trpaaycgaa
      181 gmvlahgstd lsgitglses ldslgiltrd iadlqyvysa fsgrspivpg rstvrtvvvw
      241 ggsdlhpide amtglinrlp elldgagvet raleyddhvr tladdhvtvm sheaagtldd
      301 avrehanalg pelralveag raisvtdhaa alirrdrsrd llaealgdht vivgpaapgp
      361 aphglaatgs pvlsrpwqll gcpvvvvpga ttdagmplgl qviglpgres alfevaavle
      421 telrshpvvp a
//
LOCUS       WP_010841968             390 aa            linear   BCT 01-JAN-2025
DEFINITION  flavin reductase family protein [Gordonia terrae].
ACCESSION   WP_010841968
VERSION     WP_010841968.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..390
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=42830
     Region          18..160
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 msdnvlsaid pgifrnvmgh yptgvvvvtg rgddgsvlam vvgtfssvsm dpplvsfmpm
       61 ktsrtfekmr gceslcinil ggeqedvvlt iaqrwenkld gidwfpspsg dpvladsvaw
      121 idtrirnvve agdhwialce vrdlavtnpv spliffqggy gsfvstslma rmdheilpti
      181 haahaarpqv ealatsarce vsvltavsrd emavvlsata pgvdreegla yripmvppig
      241 dtyvfdqdgd trerwlaklr daddevrqvh rdrldfvrqh gylvsflpda gstayeemra
      301 atksyergrl tpsqereice sigkspidyr lrdvrsdqty dvgsivlpir darggysmtl
      361 rlsqlplgvt gaqvqawieq aravvevlgr
//
LOCUS       WP_010842023             200 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: YdcF family protein [Gordonia].
ACCESSION   WP_010842023
VERSION     WP_010842023.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..200
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=21376
     Region          60..>185
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mrrrtlttaa aaaaiataas vavavapsep vanvqnaais tdfgsvdlgs selgtpnsnf
       61 lwqspptryi vvlgakfgvl gqtpdvlkrr ldvaanlgkk hpfnrmivsg gdthwlpvte
      121 aqfmnlglir rgipmwqmvn egaststvqn aqntvrmlkh mgangaiivt ngfhmeramk
      181 nfrdaarqqg ariefrsaya
//
LOCUS       WP_010842051             106 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Gordonia].
ACCESSION   WP_010842051
VERSION     WP_010842051.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..106
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11844
     Region          7..100
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 madvdalrid hspareryea ilvaestged evvgyldyvs epyqvvvtht vireqfsghg
       61 yaghlvrfvl edirssgkqv vpvcsyvqrf ierhpefadm avpvpq
//
LOCUS       WP_010842058             280 aa            linear   BCT 01-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Gordonia terrae].
ACCESSION   WP_010842058
VERSION     WP_010842058.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..280
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29864
     Region          15..249
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mtgtgsdgae tdarpvvtfs garlafgdri lwddlnltie pgefiavlgp ngsgktsflr
       61 vllrqyaldr gsvatidavg yipqqhaedd adpmairgrd lvgfgvdggr wgvglrgrar
      121 rrelvdrals avdalpyada plgvlsggeq qrlrvaqavv sdpglllcde plasldptnq
      181 qvvvelidrr rreagtavvf vtheinpilp yvdrvlylvd grfrigaphe vmttetlsel
      241 ygsdvevlrv ngrvvvigge yahhcaaetd sgiarsggpa
//
LOCUS       WP_010842120             322 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Gordonia terrae].
ACCESSION   WP_010842120
VERSION     WP_010842120.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..322
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32825
     Region          1..322
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfrlsdiht dlastvdaml gkadmptatr awaagdraav akvysqlada gisgllides
       61 hggssagave mvvaveqlgr hcapgpives vavlpillhd advsgplsdl aegrlatcai
      121 gplqplaadt asadvylvvd gvlsratvls tdasvdgtrt lsrvtagevl atgvdaadat
      181 dagalataaq llglgqamls iaseyaqsrk qfgrpigsfq avkhhladva iaiemarplv
      241 haaalgidgq vpegtdvsrd vsaakvaaae aadlsarrsl qvmgaigyta ehdislyitk
      301 trallnawgs pavhrqrile tl
//
LOCUS       WP_010842149             214 aa            linear   BCT 01-JAN-2025
DEFINITION  LysE family translocator [Gordonia terrae].
ACCESSION   WP_010842149
VERSION     WP_010842149.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..214
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21935
     Region          1..214
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mltalvsfvv tatlivllpg pdtlvvlrgv vrggrgeamr tsagvvcglm vwvtaavlgl
       61 sallqasqtg yeilkivgac ylvwmgissv rallraapdl aaaqeatapp adrragllfs
      121 gftaglltnm lnpkigilfi sllpgfvpdg ystgwttlgl gatyialtaa yftvlvgaag
      181 riagwlqsar irrrveaigg valiglgvrl aleg
//
LOCUS       WP_010842276             336 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Gordonia].
ACCESSION   WP_010842276
VERSION     WP_010842276.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..336
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35842
     Region          77..317
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mhtmstptpl pseastratl tahatrwglg tftgviplnp lgirlsrgli aaimrtlgrt
       61 psgttvlnve engisgewvl gpgvrrgraa iyyihgsaft icsarthrsl aarlslatdl
      121 pvfvvdyrla pehrfpaaad dvadgfdwll rqgftpgdiv vagdsagghl acdltlrrav
      181 adveqpsavi lfsplidltf glardqerir rdpaitaaaa arlvglytrd aaaddprlsl
      241 dftparhlpp flvqtggaem lsadarhlhd elrahggdsr leiwpgmmhv fqalprlgpe
      301 adaalrrvge fltdraadrh apapatsavr ivsdas
//
LOCUS       WP_010842274             230 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Gordonia].
ACCESSION   WP_010842274
VERSION     WP_010842274.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..230
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25206
     Region          10..223
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtdrlldqla etrtgnaran vleelrrlil sggappgtql ppgeiadafd vspipvreal
       61 ktlvgeglvv hrqgvgyrvs qlsteelrei yfvrgtleqa alarsvglid esslqtarar
      121 haellaavkf ndgkafhdis refhraltap camprllnmf eatwnltepf qvmrsvtadt
      181 qnalntdhad llaafadrdt asvldvarrh hqrlesavie taalldvrhd
//
LOCUS       WP_010842302             384 aa            linear   BCT 01-JAN-2025
DEFINITION  MlaD family protein [Gordonia terrae].
ACCESSION   WP_010842302
VERSION     WP_010842302.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..384
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39279
     Region          19..269
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mdsldragsa grpspapsrr gvrrggvlav llaalmgltg cgllpsltve qiplpapggi
       61 gdsitltanf dnalnlptra kvklngndvg qvtdlvakdy tavvtmevsk ktnlpvgtga
      121 elrqatplgd vfvallppie akdglmvdgd tltgptsaaa tvedllisms gvvdsgslns
      181 ltiiltelss avatnpsdln gairgmttgi rklnqssaav drslattrvl tgqladgraq
      241 imasinklgp aleslngqia tilttldktq qvtaatndfl dtdqdnlvem lghlstvlag
      301 lrqaagplgs ladnlhtltp kwvkstpgsa aavsskvywl spgvgfdsas rlpeiqdvde
      361 gsaalqqtlt rllaritgtr gccg
//
LOCUS       WP_010842375             339 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Gordonia].
ACCESSION   WP_010842375
VERSION     WP_010842375.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..339
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35971
     Region          19..335
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msapaldrpd agtddrvald vvdltvdlrt ptgtvravdh vsfrarrget lallgesgcg
       61 ksmtaqalvg lldpiasvsd gsitldsvdl vsaspskrrn iagtelaivf qdaltalnpv
      121 ypvgtqlaep frihrrmsrk karleaielm rhvgipepes rvdsyphqfs ggmrqrllia
      181 mavalspkvl ladepttald vtvqaqimal lsrlrtehdm avvlithdla lvaeqadrva
      241 imyagnvvet gpvaevfgsp khpytkglld svpvsaerga dlksiggtpp dlhsipagcv
      301 yqarcplara rcvqqrptlt atgadraaac hfseeigna
//
LOCUS       WP_010842377             239 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein [Gordonia].
ACCESSION   WP_010842377
VERSION     WP_010842377.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..239
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=24207
     Region          14..230
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 msvvacvvia vavflascmq asigfgmgml aapvvalvap tllpgmlias attvtllvvi
       61 rergsldlrg tgwaligrvp gtiagalllv wlptrglsll laavvlggva vasvgwrpap
      121 vrrnlataga asgllgtats iggppmalvy sgkenahvrs nmsafflvgs lmslgalaat
      181 gslraeilwa flaltpivvl gfvasrvvnr vldrnrlrtv sitvsaigaa lligqqiff
//
LOCUS       WP_010842387             380 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Gordonia].
ACCESSION   WP_010842387
VERSION     WP_010842387.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..380
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41761
     Region          9..380
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 maersswedd dltalrdlar sfcgkeikpn aekfieqhhv drdlwnkagd lgllcmsipe
       61 eygggggtfa heavlieeqa rvadsswgvs lhngivahyi leygseeqke twlpkmasge
      121 avgaiamtep gtgsdlqnvk tkaikqgdey vidgsktfit ngsqadliiv vaktdvsega
      181 kgislilvea eregfrrgrv ldkvgqrgqd tselffdgvr vpasnllgae egqgfiqlmq
      241 qlpqerliia vasvagmeka vsetiaytkd rtafgrpifs fqntkfklae aatetrigrv
      301 fvddcinkhi kgeldiptva makwwtsdra mvvadeclql fggygymney piarlwadnr
      361 vqkiyagtne imkeiiartl
//
LOCUS       WP_010842392             295 aa            linear   BCT 01-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Gordonia terrae].
ACCESSION   WP_010842392
VERSION     WP_010842392.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..295
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31121
     Region          65..277
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mrlinqsgrl midtgkgavd veqashgqfh sdpqavygrw adfvewasta tltpttevvd
       61 aklgapvprp gqvfavglny adhaaeadia hpdapviftk fpasiagpyd tiehpggsld
      121 fevelvavig tsardvapad gwqyvagltv gqdlserelq mrgptpqfgl sksfagfspi
      181 gpavvtldef adpsdiavss slsgeemqss strhlifsip vlvaylssfl elrpgdlift
      241 gtpsgvgftr dpkrlittdd elvstaegig emrhrfvssa hphpstalpn aghsa
//
LOCUS       WP_010842439             538 aa            linear   BCT 01-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Gordonia terrae].
ACCESSION   WP_010842439
VERSION     WP_010842439.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..538
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58197
     Region          <75..510
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mptllsagep gdssasgpva esvqawqrtl agdsatslpl aahaevdptg tamttaefar
       61 samrdclaae dalrdslras lrpyqirgva wlartaevtg gavlademgl gktvqaigll
      121 tlrahegpql vvcptslvtn wahemtrfap tldvhtgpld htpeapgsva visyarlrls
      181 ieairrypwa tvvfdeaqal knprtqvsra arsidarari altgtpiens lddlwailrv
      241 iapgvfphra vfrrrftrav ddgdtgalhr lrvavspvvl artksrvasa lppkisnpvl
      301 vdltdeqaql ydahlarved dgfgdgferh grilatltrl kqicnhpglv tgdtrvltgr
      361 sgkldvctei lgdnlrtdsp tlvftqyrdt gellvrhlae qfgvdvpffh gglppgrrde
      421 lvadfqagrg pgvmvmslka ggvgltltra cdvihfdrww npaveaqasd rvhrigqqrp
      481 vtittltsat sleehiddlh rrksalsaha ddssalaelt glsderlidv lrrnrevr
//
LOCUS       WP_010842466             377 aa            linear   BCT 01-JAN-2025
DEFINITION  sensor histidine kinase [Gordonia terrae].
ACCESSION   WP_010842466
VERSION     WP_010842466.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..377
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41477
     Region          122..377
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtwtgrlwrl avmlcisvga fatrasylwd earwwfitdl algvlsyivi wwrrshpvpv
       61 ttftnivtim sssslgpgil amvslstrrr wreiipqavl svgagiiale ffatpteasd
      121 pvivqytvtv vataamvawg lyigsrrell aswraralas eaeqqakvmq araleraria
      181 remhdilahr isamsmaaga layrsdlsge qiretaqtiq etshlaltel revlgvlreg
      241 pgdatpeepq gvpdlsalie earrlgmrve srcdidvtsl spaisrtlyr cvqealtnar
      301 rhspsapvtm hirggpdhgv dllvenplpl smgssrptpg fglvglaerv elhggrqsvt
      361 vsedkrfllh vwlpwqs
//
LOCUS       WP_010842512             158 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Gordonia].
ACCESSION   WP_010842512
VERSION     WP_010842512.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..158
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16815
     Region          3..137
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mlaltesarp wligvyrivv gflffchgtt tlfawpiepy ggstaefgaw pswwaaaiqv
       61 vggllimtgv gtrvaafvsa gsmavayfwk hqgdglvpiq ndgessalfc wallilvvig
      121 pgkltaqsil drlrgnatpa nqtdtesise ppetsmvr
//
LOCUS       WP_010842521             275 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Gordonia terrae].
ACCESSION   WP_010842521
VERSION     WP_010842521.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..275
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29522
     Region          6..111
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(6..8,22,40..42)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            43
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(54,57,61..62,71,84,88,94,98,101..102)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          118..263
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mgaqvsigdf avmtslsrka lrhyhdigil qpthidsrtg yrfydtsqvd hahiirrfrs
       61 lgmsipdika llstddaaar teiiathleq mevqlqqtrd tvgalrells pvhtptvvav
      121 rhepalavws igatlevsel dgwfaatlrt lrnavatvgg atsaivpggl ydralfvesr
      181 geatlfvpap esatppegir aevlpraefa vlahsggheg idrsygalgv yvnehlvsgp
      241 gpireryvgg tpsnptsitt teiywpifst tpppg
//
LOCUS       WP_010842527             304 aa            linear   BCT 01-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Gordonia terrae].
ACCESSION   WP_010842527
VERSION     WP_010842527.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..304
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33264
     Region          47..299
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          213..294
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mseratppgi adrftltgth rdrpdlsveh walgfdtylt llsydgiama slphreraar
       61 ghlrqvsvav laagdwwlri dgrsqligsd sptlvvvnhq rpldfrnnrr gsivalhtls
      121 arlmlsdnti draithlgps valyplavtq iqhlgmlart apallpelnv ptvalirsll
      181 lnaaasggsp sesnlvavie kyiddnirds smspatiaaa hhisvrqlnk iwpadnttvs
      241 syitrrrves acaalvseph lsiaalahrh gfvdpthfar rfreaygttp srfragdrrt
      301 qlpr
//
LOCUS       WP_010842567             154 aa            linear   BCT 01-JAN-2025
DEFINITION  DoxX family protein [Gordonia terrae].
ACCESSION   WP_010842567
VERSION     WP_010842567.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..154
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15832
     Region          7..135
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtnpivrsag illgrvalgv iflahglqkf qqngwtgpqt gfdmmgvpaa sfsafvvtwl
       61 eilggialii glltpiiaal ltlnmigalf iahvdngiwv sdggyelvla lgagaliltv
      121 igagrfsvda algskvswls addsrsrela gstr
//
LOCUS       WP_010842600             263 aa            linear   BCT 01-JAN-2025
DEFINITION  IclR family transcriptional regulator [Gordonia terrae].
ACCESSION   WP_010842600
VERSION     WP_010842600.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..263
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27611
     Region          12..262
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 matfadpetp ssrevvgavl kactllehfs adrpswtlne ltsasgmnkt tvhrlmatli
       61 hagwiertds gayrvglrvf evgsaalsdl dirsaakpfm telaadfgdt aylmvpaeqg
      121 avcidlvegn sslvvagisv gtvlpyhaaa gptvmlamsd tlraewisdr lpaftdrtlt
      181 daaaltrhld rireigysvs dsdyldgvaa vaapitdrsg dliasisigg riegfggeal
      241 aakvdrvcda aaristvlqs vpr
//
LOCUS       WP_010842624             228 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ZIP family metal transporter [Gordonia].
ACCESSION   WP_010842624
VERSION     WP_010842624.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..228
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22634
     Region          1..227
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mltavlygla tavpiavgaa iglrwnlpnp ilatlmafga gtmiaavste lfepaftqag
       61 tgvaamalfs gtavyvvadr lvetklgssa igpalmigvf ldgvpental gvsltaggsl
      121 vlvvaiavgn vpeavsgasl mrrehdasir salamwlfta vvlvavtvgg yavadaispt
      181 aisvvqafag gatlgvlans lmpeayregg wwvglatagg fllafvlg
//
LOCUS       WP_010842626             303 aa            linear   BCT 01-JAN-2025
DEFINITION  carbon-nitrogen hydrolase family protein [Gordonia terrae].
ACCESSION   WP_010842626
VERSION     WP_010842626.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163270
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..303
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32576
     Region          13..275
                     /region_name="nitrilase"
                     /note="Nitrilase superfamily, including nitrile- or
                     amide-hydrolyzing enzymes and amide-condensing enzymes;
                     cd07197"
                     /db_xref="CDD:143587"
     Site            order(41,120,124,127,152..153,155..156,177)
                     /site_type="active"
                     /db_xref="CDD:143587"
     Site            order(41,120,152)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143587"
     Site            order(121..124,126,133..135,153,155..159,162..163,
                     200..201,203..205,207..208,229..230,272..275)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143587"
ORIGIN      
        1 mttigtvaan ftrdleqnya tieqyvgear trgvdflvfp eaaiggylss lgnhgdtrkn
       61 sarslppais ldgpeiarvq sivgdlvvai gfcelgedge trynaaavld gnhiygsyrk
      121 vhqplgenms yssgdgygvf dtpvgriglq icydkafpea arimalkgae iiaslsawpa
      181 artataenlq ddrwtyrfnl fdtaralenq vfwvasnqsg tfgslryvgn akivdpggni
      241 ldttllgsgl avaevdiaes ftamragmfh lrdrrpevyg mlveadsdsd agadfawrdl
      301 aha
//
LOCUS       WP_010842631             282 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: carbon-nitrogen hydrolase family protein [Gordonia].
ACCESSION   WP_010842631
VERSION     WP_010842631.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163270
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..282
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29591
     Region          15..265
                     /region_name="nitrilase"
                     /note="Nitrilase superfamily, including nitrile- or
                     amide-hydrolyzing enzymes and amide-condensing enzymes;
                     cd07197"
                     /db_xref="CDD:143587"
     Site            order(43,114,118,121,146..147,149..150,171)
                     /site_type="active"
                     /db_xref="CDD:143587"
     Site            order(43,114,146)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143587"
     Site            order(115..118,120,127..129,147,149..153,156..157,
                     194..195,197..199,201..202,223..224)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143587"
ORIGIN      
        1 mrtvtlgala ahfgrdverg vakavgiies aardgvdllv fpdaslggyl gdlrhpdpae
       61 lppplhpdap elaaiaaaag dmtvcigyte avddqrfnta vcvngdgilg thrkvhqpag
      121 eelayaagdr fgafdtpvgr lgmlidydkt fpesartlal dgariiaals awpasvtdra
      181 arlpadrqsr lfdlydcara aenqvfvvss nqtgvmgslr flgqakvvgp ggdvlattrs
      241 kgglatatvd vdaevdrarr vlshlgelrp dtyrsttsad qr
//
LOCUS       WP_010842691             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SRPBCC family protein [Gordonia].
ACCESSION   WP_010842691
VERSION     WP_010842691.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167397
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..163
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=18161
     Region          17..145
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cd07812"
                     /db_xref="CDD:176854"
     Site            order(18,27..29,31..32,47,53,55,57,59,77,79,81,88,90,
                     101..102,104,106,112,114,116,118,126..130,132..133,
                     136..138,141)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176854"
ORIGIN      
        1 mttshddrta rfthaesiri datpqqvwdl vtdigrtgew spickacwwa epatgpevga
       61 yfhgrnetpe hvwetrslvl vaeeprefaw mvnenavrws ytitpdgdgt tlteswavqp
      121 ggfelfaqry gddadtqleq rrdaalsgip vtlaaikeia erg
//
LOCUS       WP_010842748             781 aa            linear   BCT 01-JAN-2025
DEFINITION  arylsulfatase [Gordonia terrae].
ACCESSION   WP_010842748
VERSION     WP_010842748.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..781
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=86351
     Region          43..549
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(53..54,91,149,151,244,354..355,418)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(53..54,91,149,151,244,355,418)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 madrnpptip enargyqgfg gvvgrttsqs epwwpeeksa ppgapnivvv liddmgysdi
       61 apfgaeidtp nldrlarngi rlsnyhttpv csparaallt glnphragyg svansdpgfp
      121 glrleladdv lalpeilres gyatyavgkw hlvrdanmgp grdrgswplq rgfdsyygsl
      181 eglnsffypn qliadnsvvd vetypedyyv tddltdraig qikslraqdp tkpfflyfah
      241 iamhgphqvk esdlakyrgr yadgwdvvrq qrferqkaeg lfdagtrmae rntepgydap
      301 pwadltveek rrfqryqevy aamvdsvdqs vgrvldtlde lgeldntivv ftsdnggtae
      361 ggpsgtrsyf sqfvhgpvpp dwerdvphde dligspelgv hyprgwgqas ntpfrfykgq
      421 tfaggvrvpf iiswpaglsr dprdngvrrq fsyvtdvvpt llelagvetp thrhgrpaqe
      481 rdgvsvvefl rnpsaespht eqyaefgghr gfyrdgwklv slhqdpaavd dpvwelydvt
      541 ndpaetrdla ashpdkvtel arawdeaawh ntvfplfdsp aaqsrrrpae erlsdpvril
      601 agtpaleryr ssrliayrdf dieaeldgwt pdaegvvvah gdpqggylly vesgsahfvf
      661 naygrrhrvs gpmpsgttrl vvhavatpsv rwgftieaaa gehssiiakl ddqvqlvgma
      721 pwtgisvgvd argpvdpdlr rrrgvfrfgp alravtyrpg tvrvpadvrr eidqaaessa
      781 d
//
LOCUS       WP_010842731             171 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Gordonia].
ACCESSION   WP_010842731
VERSION     WP_010842731.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..171
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16921
     Region          8..138
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 marlfttprp tsnhtaaqll lraaiggtmi ahgvkharsl agtagwfgsi gfkqpklqaq
       61 asavveigsg aavvagagtp lasaaivgtm avaarsvhqp ngffitsegw eyvanlsvaa
      121 ialaaigpgr fsvdralgid tkltsgqaaa vaagvgltaa gaqlalfhrp q
//
LOCUS       WP_010842758             371 aa            linear   BCT 01-JAN-2025
DEFINITION  ADP-ribosylglycohydrolase family protein [Gordonia terrae].
ACCESSION   WP_010842758
VERSION     WP_010842758.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..371
                     /product="ADP-ribosylglycohydrolase family protein"
                     /calculated_mol_wt=38433
     Region          21..334
                     /region_name="DraG"
                     /note="ADP-ribosylglycohydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG1397"
                     /db_xref="CDD:441007"
ORIGIN      
        1 mdrfsgclla gaagdalgga vefstrdsil drfgptgits yaeayggvgt itddtqmtlf
       61 taegllrawa hdcaggiscy aattaraylr wfitqgghpr hgvlatters swlaghrqlh
      121 srrapgttcl ealrvttrpg epadndsngc ggvmrvapvg lfaaraewsa ggafdlaaal
      181 aslthghpsg slpagvlavv irdlvagasl pealaeakgi lrvrtgheet lvaletaeal
      241 adsglsheaa ierlgggwtg eealaiavys alvaddleea viiavnhdgd sdstgaiagn
      301 llgardgvaa ipqrwleple lrdvivemag dlydfvdwdt aesdadagsa rwvekyrgsr
      361 pgttsdlrpv g
//
LOCUS       WP_010842727             247 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Gordonia].
ACCESSION   WP_010842727
VERSION     WP_010842727.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..247
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27140
     Region          7..245
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mgdagqsepa yktlanelrs qivagkyagg vrlptesels qeyalsrqtv rraflelvte
       61 gavyrvpgrg tfatenagqy lrqlgsiedl mnlstdtemq vlesparrvd leaagrlrld
      121 tdvvyrivfq rfhdgvpfvv ttvswpepva rlvidapeve qgaisdhtmi gllephlvdp
      181 ieecaqsita ttadattadr lgcpvghtvl rvdrlytdsr gravelavsh flpehytyrv
      241 tlrrsgi
//
LOCUS       WP_010842761             163 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [Gordonia].
ACCESSION   WP_010842761
VERSION     WP_010842761.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..163
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16822
     Region          1..136
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtttvvagnp kpgsrtldaa rqlakaltgt epdhvidvid fgagllgwgd aavrgavetv
       61 assdlvvvas ptfkatytgv lklfldqfat geglrdvtav plmlgagpah amapdlllkp
      121 vlvelgavcp apglylidst ystdsriady terwsstlvr lsp
//
LOCUS       WP_010842826             201 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Gordonia terrae].
ACCESSION   WP_010842826
VERSION     WP_010842826.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21326
     Region          21..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtqttregrg agrrdsasmp tretlltvae rlfladgydk vsvraicaaa eanpaavhyh
       61 fgtkedltia llqsrlgplw adplasldpa vtsiaqvvdv vvdpfvdlqa dpaghlhlrl
      121 larfvlahpt agwtsrwfdl dpfadmlada vpgltagqar rrwalafqli llrfggtetl
      181 staavtaltg fvtagltapa p
//
LOCUS       WP_010842835             574 aa            linear   BCT 01-JAN-2025
DEFINITION  thiamine pyrophosphate-binding protein [Gordonia terrae].
ACCESSION   WP_010842835
VERSION     WP_010842835.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..574
                     /product="thiamine pyrophosphate-binding protein"
                     /GO_component="GO:0005948 - acetolactate synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0009097 - isoleucine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009099 - L-valine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58453
     Region          38..561
                     /region_name="IlvB"
                     /note="Acetolactate synthase large subunit or other
                     thiamine pyrophosphate-requiring enzyme [Amino acid
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0028"
                     /db_xref="CDD:439799"
ORIGIN      
        1 mgapgrygpt vadvagrvla dlgvghvfgv vgsgnfvftn alrtggvpft aarheggaas
       61 madaysrmsg rvgvlsvhqg cgltnamtgi aeaaksrtpm ivltadspas alrsnfridq
      121 ealsasvgav ndrvhapstv vsdvtrafrt avtrrrtvvl hvaidiasaa sefdgpvels
      181 veppqvrpda rsaarladai raarrpvfva grgaraagpe vaalaetaga lvatsavang
      241 lfagnpfslg isggfssptt adliagadli vgwgcalnmw tmrhgrliga datvvqvddd
      301 idaigahrhv dlgvvgdcaa taadvldllt gagsaasgpn qpgagsaasg pvqsgyrtte
      361 vrqrisassr wqdvpvtgev tpgrvdpral tialdeilpa ervvsidsgn fmgypsthls
      421 vpdengfcft qafqsiglgl gtaigaafaq pgrlpvlgtg dggflmaiae letavrldlp
      481 lvvivyndsa ygaevhhfgd admttvtfpe vdiaaiargh gatgvtvtgl ddldevrewv
      541 gslsspepsg pliidakitd dggswwlaea fagh
//
LOCUS       WP_010842897             542 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Gordonia terrae].
ACCESSION   WP_010842897
VERSION     WP_010842897.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..542
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58169
     Region          16..540
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mttasrddaa apdihttagk ladlrnrlde tkhpvgeaav ekthakgklt arerithlld
       61 egsfveldal arhrstnfgl aerrplgdgv vsgygtidgr evcvfsqdst vfggslgevy
      121 gekivkvmdl aiktgrplig indgagariq egvvslglyg eifhrnvras gvipqislim
      181 gaaagghvys paltdfvvmv dktsqmfitg pdviktvtge evtmeelgga hthmsksgta
      241 hyvasdeeda leyvkellsy lpsnnradap rlpvaqpaag siedtlteed leldtlipds
      301 pnqpydmhev irrildddef levqaeyatn iivgygrvdg rsvgivanqp tqfagcldid
      361 asekaarfvr tcdafnipiv tlvdvpgflp gtdqeyrgii rrgakllyay geatvgkitv
      421 itrkayggay dvmgskhmga dvnlawptaq iavmgasgav gfvyrsqlkd aaakgedvda
      481 lrlqlqeeye dtlvnpyvaa argyvdavip pshtrgqiat alkllerkmv nlppkkhgni
      541 pl
//
LOCUS       WP_010842996             180 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Gordonia terrae].
ACCESSION   WP_010842996
VERSION     WP_010842996.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..180
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19629
     Region          2..176
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mgkihvhefi tldgsyedps ftmpygfadg mgellgsfms ectgillgrn tfemfapaws
       61 trtvdddpga pffndttkyv vsstlddtsa wqnstvigay dadrirelkq erdlyisgsg
      121 tlvrallrdk lidelhllvy pvvlgsgarl fdgladlplt lvgtdvfdng vvhlsysstd
//
LOCUS       WP_010843008             182 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Gordonia terrae].
ACCESSION   WP_010843008
VERSION     WP_010843008.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..182
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20241
     Region          2..179
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrtlaitqnm tldgsiemlt dwfdptvvap dlmaeshrqd aeadallvgr qtfedfrgfw
       61 phqtddatgi tdylntvdky vvsstmtdpe wqnstvlngd vieqvtalkn aagkdivvtg
      121 sislchtlir aglvdeyrlf vypavqgsgr rlfpdrleip tlrlvdtksf elgvsllryr
      181 tv
//
LOCUS       WP_010843045             433 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Gordonia terrae].
ACCESSION   WP_010843045
VERSION     WP_010843045.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..433
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=44446
     Region          9..247
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(9,33..34,63,68,73..76,88)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,71,87..90,94,96,132,134,
                     136..137,139,148..149,152,168..171)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,71,87..90,94,134,136..137,
                     139,148..149)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(20,94,96,132,134,136,152,168..171)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(148..156,164..171)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <173..403
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mdrdlldgry eirgvlgrgg mavvhdgwdr rlhrsvaikl lrsapetpvv arerfaaear
       61 aaaalnhpni vavhdfgehd gtpyivmerl sgttvgdlmv dgpmppdrva ailadvlaal
      121 haahaagvfh rdikpanllm agdrvkvadl giaktagtah tatgevvgti cylspgrvlg
      181 raatpaddly aaavvayeal tgrraydqdn paavahailh sppppltvvr pdvppalrdt
      241 idramrpgdv asfadaaaml aalsghgaep lshpatsrlt splsmtplsm tplsttplta
      301 tpgpvlptgg gsptaplfae rprprrrtwv alvggsaall aallvaitva atssdedaps
      361 ptnpapaslp aaepsipast ietpqptqte lpqtgvpqtg ptptendrng rgnsggnggn
      421 gnsgngkpkd dkn
//
LOCUS       WP_010843082             506 aa            linear   BCT 01-JAN-2025
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Gordonia terrae].
ACCESSION   WP_010843082
VERSION     WP_010843082.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..506
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=52890
     Region          38..506
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 matlsagtrr raldrlasge pldllviggg vtgvgvalda atrglrvalv ekddlaagts
       61 rwssklvhgg lrylargelr iaresaierh hlmtaiaphl iaplrqiipd rggrhssiir
      121 lglrtgdilr rnagtpdsll pppsrlsale tlgrcpavsp dglrggisaa dgqliddarl
      181 vvalartaag ygasictrvr adrvdgrgat ltdretgesf dvgarmvvna tgvwsggvdd
      241 aiavhpsrgt hlvidaarlg fpdaalmspl gtsvsrfvfa ipaqlgrvyv gitdvaapgp
      301 ipdvptpdes eidflldain palarpldrs divgtfaglr plvdtrggrd adaladvsrq
      361 hhvgvrgdgl vsvlggkltt yrrmaqdavd aalattdlsa gdcvttttpl vgalrspreh
      421 glptslvqrf ggeapavvda atldrpldpi vpgidvtrae iefamthega ldaddilhrr
      481 triglvrrda daarpeieri vgevlg
//
LOCUS       WP_010843116             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Gordonia].
ACCESSION   WP_010843116
VERSION     WP_010843116.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..233
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24155
     Region          31..>146
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgrapstpds rsaaasdstg tlrayggegg dtrvarrrsa lidagldllg addvgavtvr
       61 gvcrraglta ryfyesfesa dqlvgvmyde vieeiaqasl aafsegasmr akvagavtai
      121 vdvidadrrk grllfsqall spviaakrme stalfagltl qstsaildvh vgpaaavgva
      181 hyqvgglsrl laawlegdvd ldkaevvdls isllvspaem lekslsrrtg dae
//
LOCUS       WP_010843150             568 aa            linear   BCT 01-JAN-2025
DEFINITION  MDR family MFS transporter [Gordonia terrae].
ACCESSION   WP_010843150
VERSION     WP_010843150.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..568
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60052
     Region          34..436
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(41..42,45..46,49,80,130..131,133..135,138,158,
                     161..162,165,297,300..301,304..306,309,337,341,394..395,
                     399,403,419,422..423,426..427,430)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mtdspsgadt vahddevaga glthrqilti laglmmgmfl aaldqtivst airtiaddlq
       61 gydmqawvtt aylvtativt plygklsdly grkpffllai sifivgsllc tiatsmyela
      121 afrafqglga gglmtlaltt igdivpprer akyqgyflav fgtssvlgpv lgglfagqtt
      181 ilwvagwrwv flvnvpiglv alfvvykvln ydqqkgvggr tdywgatala vavaplliva
      241 eqgrqwgwss glsilcyvig vlgiaafiwi ehkmgddali plrvfqnrvf sqgiiisvvi
      301 gavmfggism lpqyfqvlrg sspmvaglqm lpmvlglmtg silsgqlisr tgrykiftiv
      361 gavlitaatf llhlvgtdtp vylvmlmaal lgfglgnlmq pitlamqnil pptdmglstg
      421 tatffrqigg tlgvavffsm lfsfmgpsiq demvaaaaqp eyraavveas qssdpqvsaf
      481 gqsliaaaqn pgaaagssds vmsdtsviek lptevaqpik egfadsmdrv flavsiisll
      541 aiigtitwke lplrqgrpig apestpas
//
LOCUS       WP_010843168             340 aa            linear   BCT 01-JAN-2025
DEFINITION  alpha/beta hydrolase [Gordonia terrae].
ACCESSION   WP_010843168
VERSION     WP_010843168.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12000796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..340
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36716
     Region          48..311
                     /region_name="Abhydrolase_1"
                     /note="alpha/beta hydrolase fold; pfam00561"
                     /db_xref="CDD:395444"
ORIGIN      
        1 mtqisaddsg hegtpdhddp vaatperitl elghitlhal awgpvagpvv vclhgfpdsa
       61 wtwrhlgpel aaaghrviap ftrgyapsei padndfhvaa laydaraihg avgagddavl
      121 ighdwgamta navahrddnp yarvvsmsvp pvpavrrsva ggidgarila rqalmswyia
      181 fnqlpwlper aldrlipllw rrwrlntgta aarpdhlldv dhalaalptr ahrtaalgyy
      241 ralrrprthp ryaslrddwl geprcptlyl hgaddgcmqs rltdhvrdvl paasaaavva
      301 gaghflhldr pdevnerila fvtsnargre ggtgparfvd
//
LOCUS       WP_010843173             144 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: SRPBCC family protein [Gordonia].
ACCESSION   WP_010843173
VERSION     WP_010843173.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..144
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=15743
     Region          4..140
                     /region_name="Polyketide_cyc2"
                     /note="Polyketide cyclase / dehydrase and lipid transport;
                     pfam10604"
                     /db_xref="CDD:431388"
ORIGIN      
        1 mnrverhtsa tpaqvwsvls ngwlyaswvv gasrirdvdq swpqagskih hsagvwpall
       61 ddetesvesk agllelsaag wpfgrarirm tvekdgngsl igmeefveta plkwippvvq
      121 eavmsprlne clrrlamlae nhag
//
LOCUS       WP_010843200             208 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Gordonia].
ACCESSION   WP_010843200
VERSION     WP_010843200.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..208
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21890
     Region          10..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mqkpacpirr rttpevreal lvaavaelde agpekaslra iarrvgithq svahhfadrr
       61 alftavavrg fdslhaehtr algelsddap lgeavatlgq vyvrfardnr ataalmmgsr
      121 lvdnkaaelv aararawelh tstvsdaadd gwgggvpgnl iaiatfamah glasletdfa
      181 dqlpdgtgie dllslvnaai itppqqds
//
LOCUS       WP_010843213             170 aa            linear   BCT 01-JAN-2025
DEFINITION  GtrA family protein [Gordonia terrae].
ACCESSION   WP_010843213
VERSION     WP_010843213.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..170
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19012
     Region          44..170
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 msrpdpgdhv rdddepshed fatrhapmpi elpfddeeas tnvglktqlv rfvitggfsg
       61 lldfgltill qygldmpfwp aksagfilgt tvayllnrrw tfraepsmar fvsvialylv
      121 tyfvnvgiyt alshawqetl lysfaayvia qgtatvinfv vqrmvifkir
//
LOCUS       WP_010843205             288 aa            linear   BCT 01-JAN-2025
DEFINITION  siderophore-interacting protein [Gordonia terrae].
ACCESSION   WP_010843205
VERSION     WP_010843205.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..288
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31941
     Region          1..283
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mtqsieaarp weysafpvkv awtqrisphf irvtltdprl tnfapwgldq riklvlpmdd
       61 gtepdfglle eptphpkqwy arwkelpadr rnelrtytps airpdageid vdvfvhepag
      121 pasrwaltca vgdrlvitgp dvrvgrtgyg ihfqpphaps qlllvgdesa mpaianilaa
      181 tppttsadvl leladplddi vgarrthgri qhvirghdtg rrledavrdw gtrragefrk
      241 glpaayawia geattttrir ryltnelgmd kdhvaflgyw klggplvg
//
LOCUS       WP_010843227             323 aa            linear   BCT 01-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Gordonia terrae].
ACCESSION   WP_010843227
VERSION     WP_010843227.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..323
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=32994
     Region          1..319
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(36..37,118,122,125,143,146..148,167..168,172,187,
                     208..209,230..231,233,255..257,308,313)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaivvesen lslsdvpdpt pasgevvidv vaagvnradi lqragnyppp pgasdtlgle
       61 vsgrisalgd gvsgwsegde vcallagggy aekvavpaeq llavpkgvdl vsaaalpeva
      121 ctvssnifdt ahlttgelll ihggssgigt hatqiahamg arvavtartq dklercrefg
      181 adilidyssq dfaevlkdag gadvildiig akylksnlka lrtdgrlvii gmqggtttei
      241 nlghllakrl svmgttlrar pvhgpggkae vvastltrtw plieagtvvp vvdrvfplad
      301 aaaahdhlns gdvigkvlls vgd
//
LOCUS       WP_010843246              69 aa            linear   BCT 01-JAN-2025
DEFINITION  CsbD family protein [Gordonia terrae].
ACCESSION   WP_010843246
VERSION     WP_010843246.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..69
                     /product="CsbD family protein"
                     /calculated_mol_wt=7124
     Region          2..66
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mgttddaknk aeelkgrgke aagsltddqd lknegkgdqa qaqgkqkvte aadavkgkid
       61 dvkdkltgh
//
LOCUS       WP_010843252             488 aa            linear   BCT 01-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Gordonia terrae].
ACCESSION   WP_010843252
VERSION     WP_010843252.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..488
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=51841
     Region          12..479
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtstyfawdl ihradapcvr ddsvaldyag farrvegaae qltrrgvrrg dvvatflpnr
       61 iellvtlmaa wrigavatpv npaftaeeve yqltdsgarv viatsaeevg sgrdhlvvde
      121 lattpssgrr gsyspaaadd alliytsgst grpkgvrlth gnlhymastm vthfgltdad
      181 hallvlplfh vnaicvsfla pmlaggqlsi tgkfspsrff ddvarlapty fsavptiyal
      241 lvsqdgltpe ataslrfavc gaapisrell drvegafgvp vvegyglteg tcasacnpvd
      301 gvrklgtvgp alpgqrisiv dehgaqvpag eigevvisgp nvmrgylnrp eatastivdg
      361 rlhtgdvgrl dedgyltlvd rikdmiirgg eniypkeien alathpdvle cavvgapdel
      421 ygelpvafvv ayphrevdae tlgahladrl akikqpsiih vvdelprnpv gkidkpalrs
      481 glrspqpi
//
LOCUS       WP_010843268             172 aa            linear   BCT 01-JAN-2025
DEFINITION  OsmC family protein [Gordonia terrae].
ACCESSION   WP_010843268
VERSION     WP_010843268.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..172
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17716
     Region          38..172
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mtetatrlnd vdiaavgqlv eaiqgdatka qttwaahvqw ngsfaseari rnfspvasde
       61 paalggsdta pnpveqllga lgnclavgya anatvagiel kdlridvkgd vdlhvflgla
      121 eghagfesit akvtidsdap rekldelhak vqasspvght lgnavpveiv ln
//
LOCUS       WP_010843302             677 aa            linear   BCT 01-JAN-2025
DEFINITION  M13 family metallopeptidase [Gordonia terrae].
ACCESSION   WP_010843302
VERSION     WP_010843302.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..677
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74791
     Region          5..677
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mervtasntd lnsgldlewv ddsvriqddl fahvngkwle shaipedrsv dgafhvlrdn
       61 seenvrdiit ecaasnpesg sdeqkigdly asfmdtdhie algigpitge lekiaaidsv
      121 ealarrigrl qrhgtgglfg yyvdtdakqs drylvhltqs glglpdesyy redkhadtrt
      181 ayvahvermf alagfddaaa raaaildlet aiagrhwdvv rrrdaeltyn lmsldeltat
      241 aagfpfaewf gglgtsgdat faevvvaqps fvsgvgelva erpldewktw ltwrllrsaa
      301 pylsspfvde nfdfygrtlt gaetnrdrwk rgvgfvegam gfavgklyva khfppeakar
      361 mdelianlve ayrrnisdlp wmtpetrera lvklgkfnpk igypakwrdy ssltvdrgdl
      421 ignvarassf eqdrefakig apvdrdewfm tpqtvnayyn pgmneivfpa ailqppffdp
      481 daddavnygg igavigheig hgfddqgaky dgdgnlvdww tdtdrtefss rtrklidqyg
      541 eftptgldpe hkvngdftig enigdlggls ialvayqiat egagseasgp dgsgagsepp
      601 vidgltgtqr vfyswaqiwr tktrdaeair rlsidphspp efrcngvvrn mdafydafdv
      661 epgdalyldp aervriw
//
LOCUS       WP_010843313             235 aa            linear   BCT 01-JAN-2025
DEFINITION  GntR family transcriptional regulator [Gordonia terrae].
ACCESSION   WP_010843313
VERSION     WP_010843313.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..235
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25683
     Region          26..235
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mrpeadttdp tpvltidept iadggptrpa trdaiatair ddvldgrlsp gdrlpepmla
       61 erfgvsrvpv realsqlqse gfvhlerykg atvsgasrtd alevmqvrrg levfgaqlaa
      121 errggefaeq lrmvtesgta akqmqqhdav pplvmqfhal vaeasgnrel artldrtlrr
      181 iawvfdreva tradgcwrdh taiagaildg spvqagylmd ehvrkdedlv rtllh
//
LOCUS       WP_010843330             848 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Gordonia terrae].
ACCESSION   WP_010843330
VERSION     WP_010843330.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 848)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 848)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 848)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 848)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 848)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..848
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87002
     Region          3..847
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mrrvslrnlr ahklrlfltl fsiilgtsfv agsmvftgsi skafndifds aapgvavevt
       61 padrqspgvp nsivdqlrdq raqfgidklv vnnnglvtva dsdgkaiqtg gapsvgstyi
      121 ppdealspee stilpggrgp enageialnt saaeaaglkv gsktkvvvgq gnatpldvtv
      181 vglvdapsst ggyvnvqfda atssrlftdg ehvgvvdmsa aagvtpeelq driiaglgad
      241 adlydvrtgd qvredqkaqv neflqifqyi llafaaiglv vgtfiiyntf smivaqrnre
      301 fallravgas qrqvsrsvlf eafvvgvlgg alglaigial aaglkaitsa tsglpdgela
      361 vgpdailagv lvgvvvtmis awvpaaraar vppveamras aaegsaslrn rtilgaiigv
      421 asiaaiviga mgegtgpavt vgagaagavl savlvgpala rpfvsvlgrv igapfgmigr
      481 lartnavrnp rrsaatafal tlglmlvaii gtlgqsfkgt vddavdagit adyivagtnq
      541 splppavtda idgvpgvgdv vsfgivqakv ddksetgfsa lggplnsvtv mdmqdgassd
      601 lpadgmlise rtgksngwkr gdvvtftsat gaqvqvpiag vyadnealqp wvvgpdvyek
      661 lvppfarvnv tlfvnaapgt dletlrtdle dataayltvq iqdrdqfkgq issqidqmlg
      721 tlyamlglal liavlgiint lalsvverkr eigmlraigm vraqvrrsiy lesvlisifg
      781 avlgvllgtv igvalvrtla ewglgapvvp wslivitlva savvgvlaal wpavraartg
      841 pleaiadi
//
LOCUS       WP_010843429             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Gordonia].
ACCESSION   WP_010843429
VERSION     WP_010843429.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..262
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28204
     Region          26..262
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtaiatrdle vplaeeraga vsyaaeveha slrygdnvvl rdvslrvgar eivaligrsg
       61 sgkstllrll aglsttesgs vrtaghpavs fqeprlfpwr tvlqnvafgl vrekvgktea
      121 rerarrtlde vglsdktgaw paqlsggqaq rvslaralva rpqlllldep fgaldaltrr
      181 tmhellirlw rdngfgallv thdvdealrl adrvvvlagg eivedlavpr prqtgdpdda
      241 dseiprlrar lltalgvadp ah
//
LOCUS       WP_010843443             125 aa            linear   BCT 01-JAN-2025
DEFINITION  VOC family protein [Gordonia terrae].
ACCESSION   WP_010843443
VERSION     WP_010843443.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..125
                     /product="VOC family protein"
                     /calculated_mol_wt=13430
     Region          1..118
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mitavhtliy cddpeaartf frdvlgfphv dtgggwlifk tgpsemgahp nawehegtag
       61 rtdqkfdvsf mcddlestmr elsargaefa gaptdegwgv tvglkvpgag eitlyepkyp
      121 apalr
//
LOCUS       WP_010843450             250 aa            linear   BCT 01-JAN-2025
DEFINITION  DsbA family protein [Gordonia terrae].
ACCESSION   WP_010843450
VERSION     WP_010843450.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..250
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25862
     Region          79..245
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mskkrkpgas vprtsnskyq psapsntmty vlggvailvi aglviggiww sgrgegetdq
       61 aalassstmi vgpetaplid vfedpmcpvc kafeqqsgpa itkavtegkl rvryhtlhfl
      121 nsrsatgdys sraagalacv adeqntdlfl rfhsalfaaq ppedgtgnit spelarmate
      181 qgatpatatc itdnakvaqa eenaqkstde lskatggqvg tptvlhdgkp vdgvlegnaw
      241 ldsilgggns
//
LOCUS       WP_010843473             260 aa            linear   BCT 01-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Gordonia terrae].
ACCESSION   WP_010843473
VERSION     WP_010843473.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..260
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25920
     Region          26..227
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mrsawrtldt atlravvvms lsvlvigtsy gvaahgagla lwqivlvatv vlagssefvf
       61 vgilaaggvp ilaalagllv ntrnfgygla vgkhlrgtpe illgahlind etaalataes
      121 dprraraafl lcglgvlvaw pagaalgatl ggvvadpakl gldaafpall aalaipalrd
      181 gatwaavtvg aavavastpf lpaglpiiga lggfaaletv rrsreaslra petagtgtda
      241 aeegasardm lghnnvrsrr
//
LOCUS       WP_010843504             100 aa            linear   BCT 01-JAN-2025
DEFINITION  GIY-YIG nuclease family protein [Gordonia terrae].
ACCESSION   WP_010843504
VERSION     WP_010843504.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Dunin-Horkawicz,S., Feder,M. and Bujnicki,J.M.
  TITLE     Phylogenomic analysis of the GIY-YIG nuclease superfamily
  JOURNAL   BMC Genomics 7, 98 (2006)
   PUBMED   16646971
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..100
                     /product="GIY-YIG nuclease family protein"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=11227
     Region          1..78
                     /region_name="YhbQ"
                     /note="Predicted endonuclease, GIY-YIG superfamily
                     [Replication, recombination and repair]; COG2827"
                     /db_xref="CDD:442075"
ORIGIN      
        1 mawvyileca dgkyyvgstr dldnrlrqhs saqvgftarr rpvslawsve lslddayaie
       61 rrihgwsrak kkalidgdid llrsrasrrs grprdpgvva
//
LOCUS       WP_010843512             202 aa            linear   BCT 01-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Gordonia
            terrae].
ACCESSION   WP_010843512
VERSION     WP_010843512.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..202
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=20537
     Region          1..201
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mlldvlnfag iavfaasgam lgvrkdfdmw givtvgvltg vgggvlrdvl lgitppasin
       61 gwgpivtatv aglivfffhp aftalhrsil vldafgmglf aatgasiald vgasafaatt
      121 vglltavggg vlrdvianev plllqpfdly avpavlgaai vavgatytsa phwtwlvvgs
      181 vlatglrlvs lryalrlpta rr
//
LOCUS       WP_010843551             580 aa            linear   BCT 01-JAN-2025
DEFINITION  BCCT family transporter [Gordonia terrae].
ACCESSION   WP_010843551
VERSION     WP_010843551.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..580
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=61481
     Region          3..512
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mnddisttst rpridltvfg vtaalviafl awglaapdnl savtadilsw itgslgwlfi
       61 lsatgfvvfa vclalskygk iplgkdgerp efrtiswiam mfsagmgigl mffgsyeply
      121 hfveappgmt agdvrtamat tmfhwgfhpw amyavvglal aystfrlgrn qlmsavfapi
      181 lgkqangagg kvidilaifa tlfgtvaslg lgalqigsgl snvgwvdnpg ttllvaviav
      241 ltaafvasav sgvakgiqrl sninmvlaiv lavfvfvvgp tvfilnllpt tlgayandit
      301 afsarssatv daegeswlag wtifywawwv swtpfvgmfl akisrgrtir efvigvmvvp
      361 ttvslvwfcv fggtaireqt dgvlgfdpat aasedtlfqm ldhlpltgia salamilvai
      421 ffvsgadsas lvmgtlserg ahepsrsvtv fwgvltgava alllamsggd glngikqmai
      481 iaalpfvvvm igmclslyld lrrdplivar sqlddqvdrh irkqaekigt geilvvdpaa
      541 idrktrgrrr irrradasad lpvsatgepa vavaeteprp
//
LOCUS       WP_010843597             249 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Gordonia].
ACCESSION   WP_010843597
VERSION     WP_010843597.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..249
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25044
     Region          <61..246
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mngvgdavvq igpalivvvv llavaavvvn rrsglatetm vavlravaql aalaavlaav
       61 iphlwasalf vllmasaaaw tsarrvnpdr sglvgiawca gpvavptivi vtallvigvl
      121 pargiavipt agiliggamv ttslagrrah delrvrrgev daalslglls rdarmeicgp
      181 aaasalipgl dqtksvgivt ipgafvgmvl ggasvwaaaa mqlfvlvall tvssiamlvt
      241 velvarerl
//
LOCUS       WP_010843608             389 aa            linear   BCT 01-JAN-2025
DEFINITION  M23 family metallopeptidase [Gordonia terrae].
ACCESSION   WP_010843608
VERSION     WP_010843608.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..389
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40749
     Region          200..379
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mddlaglgvs rgsgrvrsgg liddvtaeem ttiipivdtd eaagydlsey dfdfadsdat
       61 tressdagwt psswqgyyrp trseitqdil ipehefdqya hdepfdvdga eldlfdggel
      121 dlvtdddlda dtehrpfrtn pagqrvrrgg khriaappna lkggraalia maagaavaav
      181 aqvgtndeap apvnaaavnd asaqgaapve lgpgvaaatp qtdqmnvftn qlgvgakmaa
      241 dadrrealar rplftspipl gsydftsafa mrwgtmhggi dmaaplgtpi haatdgvvik
      301 aepasgyghw vqiqaadgtv tmyghmsssg vlvqegqrvt agdvialvgn egfsfgphlh
      361 fevwkngntk idpvpwlaak gvklsgytg
//
LOCUS       WP_010843629              92 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator [Gordonia].
ACCESSION   WP_010843629
VERSION     WP_010843629.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..92
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=9670
     Region          <2..75
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mitaivliqa dihhipetaq avadipgvee vyscagdvdl iakirvrdhe qiatvvtgei
       61 nrlpgvlksa thiafrsyss sdveggfsig es
//
LOCUS       WP_010843712             185 aa            linear   BCT 01-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Gordonia terrae].
ACCESSION   WP_010843712
VERSION     WP_010843712.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..185
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20448
     Region          1..178
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mlllsmgvsv dgfisdrdgd fnwtvpddgl fafhtervae lgafvcgrrl yeamvvwetd
       61 prmreneaha afadiwtalp kvvfsrtlta vegnarlarg pladeltavl dstdadveig
      121 gadlarqaie lgfvdefrif rypiivgggt pllppvtspv qlrlaetrty eqvvferylr
      181 vrdea
//
LOCUS       WP_010843695             197 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Gordonia terrae].
ACCESSION   WP_010843695
VERSION     WP_010843695.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20697
     Region          27..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msegktarqa qaersrtall eaaaeafvdv gvqapvrdia tragvgvgtv yrhfptrael
       61 vtavyrhqvd ecaalaeell aeqvppraal crwtsaftdf lvtkhglsda lssddpslad
      121 lhalifdtlv pafasllepa qatgevsedi caltflraig nlcivgpgyt dadaramvgl
      181 lligsgasse edenegr
//
LOCUS       WP_010843733             202 aa            linear   BCT 01-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Gordonia terrae].
ACCESSION   WP_010843733
VERSION     WP_010843733.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22365
     Region          2..194
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpklidrder raeiaealwr ivlregasgi svrevaaead isvgslrhvf adkeellefs
       61 mrliyervel rlrrherirn plrwaeavls ealpldderr vemhvnmami sesvahpgla
      121 taareahdgl rslcrtvlsv ldehgligsg rdldsqaial halvdglamh llladtdspa
      181 rvrrvlgdyl tglavesgev sq
//
LOCUS       WP_010843736             738 aa            linear   BCT 01-JAN-2025
DEFINITION  MMPL family transporter [Gordonia terrae].
ACCESSION   WP_010843736
VERSION     WP_010843736.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..738
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=78015
     Region          12..708
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 masylfalgr fsfrhkwvvi aawlvaliav aglvgtlqpk fakdfslpgt dsgiateqvq
       61 dyfpqvmqqq erastsilva aegglqnhta qlealaedlr tlpdvidpqt vanplavaaa
      121 qpalaptvvg dngrvgliqv rqniemldlt venkdelvki leensrdglq veatgslmqv
      181 mepggaaeli gfavafvvmi vafgaliaaf iplvtaivgv sitimllnls aevlsinesa
      241 taivtmlgia vsidyalfiv sryraelrrg gapedaagra vgtagsavvf agltviiavv
      301 alvvigipii tqmgagagva vliavlaalt lipallgafg rfafvpkipw ikhaeesesd
      361 dtlgirvgrt vvkwpipfiv lgllaltvaa ipatkmelgl sltseaeapa qellsrgfge
      421 gingpllvvv hdddgqikaa adetvrhiag lgdvanaaal twtgneggqn gntaliivtp
      481 esspssqath elmeqirafa ptveergael hvggqtaims dlsqklddal ipylivvvgl
      541 aflimigvfr slwvplvgtv gfifsvlatf gitvaifqeg wlglitqtqp iisflpifli
      601 gvvfglamdy qvflvtrmre eyihgmsake aivagyrhga rvvtsaaiim isvfaafmls
      661 pettakmmgf alaaavffda fvirmlvvpa viallgdraw glprwldrfv infdiegeav
      721 rhrgleepdd trtpvpan
//
LOCUS       WP_010843768             243 aa            linear   BCT 01-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Gordonia terrae].
ACCESSION   WP_010843768
VERSION     WP_010843768.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..243
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25869
     Region          21..209
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mhftsethlv dgvvernfvl gdipgilwtp attpspvpli mlghpgglqq myprlsarar
       61 ravtdgfaaa tietpgggdr ptsiavehar aelrrtlqag hevsadivdr lvlplveqsv
      121 pewqtamdql lalpdidgpv gysggvisvg vrlavtdprl aaavlfagsf ipraildear
      181 rvtiplhvll qwddehndrq aaldlfdafg stekslhanm gghtgvptya gdaaagffvr
      241 hls
//
LOCUS       WP_010843787             267 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter permease [Gordonia terrae].
ACCESSION   WP_010843787
VERSION     WP_010843787.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28107
     Region          67..264
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtalahtvsd srvmirrnvr rllrfpaltv mlvgipvvfl llfvfvfggq lgagmttqsg
       61 dsgraayldy vvpgivlvtv asavqgtaiv vamdmtagii nrfrtmdiar savltghvva
      121 sllqalfsiv vvlavavaig frptagpldw lgafgvtsvf aialiwlsvy fglaaksvet
      181 asntpmflti lpflstgfvp aeslpaglrq faeyqpftpv ievlrgtltd asvpagsvia
      241 alawsvaigg asyflalrty errripg
//
LOCUS       WP_010843882             256 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Gordonia terrae].
ACCESSION   WP_010843882
VERSION     WP_010843882.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27580
     Region          10..255
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mstattrrds asamrldlad irigygestv iegldlvvga geivvltgps gcgkstllra
       61 iagllpvrgg riladgdpvs ttsrdramvf qddalhpwrt vrgnimlalt lrgvprqqrr
      121 eqaeqwiaei gldgfgdhlp kslsggmrqr vqlarglags pravlmdepf galdaqtrts
      181 mqelllhtls ghpstvvfvt hdvdealllg drvvvlgrag epvravvdip hprdprrrgd
      241 datlrlrrti lealek
//
LOCUS       WP_010843884             243 aa            linear   BCT 01-JAN-2025
DEFINITION  SDR family oxidoreductase [Gordonia terrae].
ACCESSION   WP_010843884
VERSION     WP_010843884.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..243
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25046
     Region          1..238
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mtdpknivit gassgigaat aarlaadghr vflgarrtdr leqlvksiaa hggvasfrel
       61 dvtdasdvqg fvdtagaefg ridalinnag vmplsplaal kidewdrmid vnirgvlhgi
      121 aaalpvmqeq ggghivnias vgawevppts avysatkfav raitdglrie tdgtirvslv
      181 spgvtesela esisdadare smkayraval pasaiadaia yaisqppevd vnsivvrpag
      241 spq
//
LOCUS       WP_010843913             480 aa            linear   BCT 01-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Gordonia terrae].
ACCESSION   WP_010843913
VERSION     WP_010843913.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..480
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49186
     Region          23..480
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mpsrdhedlg ppgigsgprh padisgvlts lreivgdanv ltdadatagf ltdwtgryrg
       61 eadavvrprt tgevsrviae cdrsgiricv qggntglvgg svpppgdgtt dprivlstvr
      121 mtdidevdtv grcvgvqaga tvesidrrag esglsfgidl asrqsatagg vvatnaggtr
      181 mirrgnarsq ilgieavlad gsvlrrwtsl vkdnvgydlp sllagsegtl avitrvlfrl
      241 vtpptaatva vasvervena idligaassa gltveaaelm teagvalvsd hghrrptatp
      301 gpyyvlvels gtgdiesaaa ellaatpgii davlepapar alwaareght eaiarssstp
      361 vvkldisvpi ralpeafael srvgtdgafp crpilfghvg dgnihvnlld vppehatavt
      421 dsvfgivaan ggsisaehgi grakvawthl grdatdlatm raikaaldpr gllnpgvlfg
//
LOCUS       WP_010843927             262 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Gordonia].
ACCESSION   WP_010843927
VERSION     WP_010843927.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..262
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27973
     Region          2..252
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mtrilaianq kggvaktttv eslgaaladl dvsvlvvdld pqgcltfslg hepdqltssv
       61 hdvllgdeei advlldtedk vtllpatidl agaealllmr pgreyalkra laevsedfdv
      121 vivdcppslg vltlngltaa devivplqce tlahrgvgql lrtvrevqqi tnpnltmlga
      181 vatlfdartt hsrdvladvs drydlpvldp piprtvrfae ssasgtsvmr grknkgatay
      241 ralaenlwkh weagekvgtf ev
//
LOCUS       WP_010844005             223 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DedA family protein [Gordonia].
ACCESSION   WP_010844005
VERSION     WP_010844005.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..223
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24218
     Region          21..209
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mptqlaavla qtdpsqghsg figwildlmd tlgelgvgva illetflppi pseavlpgag
       61 flayegrmnv wlawvaatvg slvgawlwyw igaalgrdrt rrlvgrlpll dyddfdkaee
      121 yfvrwggmav llgrcvplvr sfvsipagie kmpfwrftay talgsgvwna lwigigfgfg
      181 paiapalerw sgalsnivia llvlmvawfv vkrvrrrras tag
//
LOCUS       WP_010844063             431 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Gordonia].
ACCESSION   WP_010844063
VERSION     WP_010844063.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..431
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=47153
     Region          23..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          237..395
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtsssfvrrr prdydgsspa elavfkatee lltstslqdl tvaqiletag lsranfyhyf
       61 ankydvlval lgqvfdesyg ndapwstdpg rdrarsmgss lehtlemwsr hgavicavie
      121 hmhskpavaa awqrmfeqfv savaeqikfl raegrapdga padmlaamlv ggserafyvs
      181 trglddrlpa aasvttslsa ineaaiyggr taqrakrkka grpvdtarel lpaaqdapae
      241 tetaqnilqa mrellltetl aqlsvakilk hsntsrasfy fyfrskedaf vvlfreaakd
      301 ivsaltavad vdrqdpsall eqvgqwlhld gyagavikna vhewprlpel raeylaamna
      361 mettlesiil tdrerglapd gppareytat llwtiertia gslageahlt didavtdmva
      421 rfmyaaiygt r
//
LOCUS       WP_010844112             159 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: Dps family protein [Gordonia].
ACCESSION   WP_010844112
VERSION     WP_010844112.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..159
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=17093
     Region          13..159
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mttttpitst ltdeqqsvag kalqdtlvdl idlsliakqa hwnvvgkqfr svhldldelv
       61 tvsreftdaa aerataigvs pdgraetvak tahtkgfgeg wtkdsdvvea ivanlkavva
      121 glrerigvte qadpvtqdll isfaskleql hwmwqaqia
//
LOCUS       WP_010844123             335 aa            linear   BCT 01-JAN-2025
DEFINITION  metallophosphoesterase [Gordonia terrae].
ACCESSION   WP_010844123
VERSION     WP_010844123.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..335
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=36253
     Region          40..313
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mqhseldfar lgiprlgtsg sgvparalag vaglaaaglf ystviernaf alrhttlsvl
       61 epgatplrvl hisdlhmmpg qrlkqawiae lealepdlvv ntgdnlahpq avpsviqalg
      121 gllsrpgffv fgsndyfgpk pknplkyfkk nhqrtqcepl pwqdlraaft ergwldatht
      181 vrelevsgvr vvaagvddph iqrdryetva grpnplahlr lglthspepr vldrfaadgy
      241 dlvmaghthg gqlclpffga lvtncqldrs rvkgpsnwgs smklhvsagl gtspyaparf
      301 ccrpeasllt ltpvshgdad ydadqslpql aretm
//
LOCUS       WP_010844161             555 aa            linear   BCT 01-JAN-2025
DEFINITION  serine/threonine-protein kinase [Gordonia terrae].
ACCESSION   WP_010844161
VERSION     WP_010844161.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..555
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=57839
     Region          11..276
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,65,70,75..78,90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,89..92,96,98,136,138,
                     140..141,143,157..158,161,179..182)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,89..92,96,138,140..141,
                     143,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,96,98,136,138,140,161,179..182)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,175..182)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mprnpgehfa gytiirlvgr ggmgeiylar hphlprneal kvlpadlsrd pmyrqrfvke
       61 aehassvvhp aivtifnsge ydghlwiame yidgidalkl lrqnpqgldt ptviaivrav
      121 gaaldrahat gllhrdvkpa nillqgvggp eprvlladfg iakseqdvsh ltstnvflgt
      181 vayaapeqll gdpvdpradq yalaatvfel ltgrppfqga stasiiahhl qsmpprpstl
      241 rpgisgsvda vfgralakep drrygscref aadleralta pqlskeptvr aparvpppvp
      301 vpgppashpp gpqpysnhlp ppgaypggyp sqagfapppp kkrsgllial gslaailvla
      361 iaagvvyvat qvssapsagg tstsrsttaa gpetttsaag tsaprtpdts tsavngpgdv
      421 qvgecigiat dsgsatsvna skvdcdsagl nfytaskias stscaspqns tltfpdstdk
      481 lcltpnfyed lcylvplsgg sladyreapc asaataqtvl arvttrsdas vtcsgdetkw
      541 vfyepesigy clvet
//
LOCUS       WP_010844215             846 aa            linear   BCT 01-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Gordonia terrae].
ACCESSION   WP_010844215
VERSION     WP_010844215.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..846
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=93616
     Region          1..807
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mferftdrar rvvvlaqeea rmlnhnyigt ehillglihe gegvaakale slgislegvr
       61 sqveeiigqg qqapsghipf tprakkvlel slrealqlgh nyigtehill gliregegva
      121 aqvlvklgad lnrvrqqviq llsgyqgkep qeagtggrss esgtpstslv ldqfgrnlta
      181 aasegkldpv igrekeierv mqvlsrrtkn npvligepgv gktavvegla qaivngkvpe
      241 tlkdkqlytl dlgslvagsr yrgdfeerlk kvlkeintrg diilfidelh tlvgagaaeg
      301 aidaasilkp klargelqti gattldeyrk yiekdaaler rfqpvqvgep svehtieilk
      361 glrdryeshh rvsitdgalv aaatladryi ndrflpdkai dlideagarm rirrmtappd
      421 lrefddriad arkekesaid aqdfekaasl rdkekqlvae raerekqwrs gdmdvvaevd
      481 deqiaevlgn wtgipvfklt eeettrllrm edelhkriig qedavkavsk airrtraglk
      541 dpkrpsgsfi fagpsgvgkt elskalanfl fgeddaliqi dmgefhdrft asrlfgappg
      601 yvgyeeggql tekvrrkpfs vvlfdeieka hseiyntllq vledgrltdg qgrtvdfknt
      661 vliftsnlgt sdiskavgmg fsssdgtksn ydrmkqkvnd elkkhfrpef lnriddivvf
      721 hqltreeiiq mvdlmltrve galknkdmal evtdraksll akrgfdpvlg arplrrtiqr
      781 eiedqlseki lfgdiapgqi vlvdvenwdg egegddarfv ftgsekprmv pdapveltka
      841 gesdas
//
LOCUS       WP_010844265             385 aa            linear   BCT 01-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Gordonia terrae].
ACCESSION   WP_010844265
VERSION     WP_010844265.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..385
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41661
     Region          6..384
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mqrriftedh esfrktvrdf iakevapvyh dwekqghppr efynrlgelg vlgieapeey
       61 ggggvsdfty smviaeetsa agvtfgsysv hsnlilpylv eyatdeqkqr wlpgfcsgel
      121 mfaiamtepg tgsdlanist taklsedgsh yvldgaktfi tggaladrvl vvartapfdp
      181 enrrsglsil vvdtksegfs vgrkiekigl kasdtaelsf ssvevpvsdr lgeegagfsy
      241 lahnlaqerl tiaigasata aaavqhaity tkerdvfgkp vaafqntkfv laecsaevea
      301 iraivdrale lhnegeltvp daaraklfat etagkvidkc lqlhggygyv leypiarlya
      361 dtrvtriygg tsevmktiia kdlgl
//
LOCUS       WP_010844315             494 aa            linear   BCT 01-JAN-2025
DEFINITION  APC family permease [Gordonia terrae].
ACCESSION   WP_010844315
VERSION     WP_010844315.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..494
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51279
     Region          17..480
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 maddliapss addelgtggy rpelrrtlgg favfaisfaf isvavgvfat ygevlatagp
       61 vgiwlwiiaa vgqtlialvv aqfaarials gssyqwasrl anprvgwlfg wlsfwylaia
      121 vvamdnalas qalmpllgma edesvarvit vavlvvqaal viastrllgl ftsgavavel
      181 aivailvval avvmvvtgsg hlgnlgsagi aagapdywai gggvmaamvm glttlvgfds
      241 aanlaeeakd pfrsvpraiv gsvvaaavvg lgflivltla iedvaavsrd gspvaaiird
      301 qlgsiaeril lvcivfamfg agmvvmaaca rqvfamardg rfpahrlmrr vnprtqtpvp
      361 atllilgvgv vlmlalpgsa lieliiasti lpaliyggiv vlylvvrkrl drkvggfslg
      421 rfefpiaiaa liwvvfalfv lvtpddatvp tlivlgliaa galyfawmmv rnrqvldsep
      481 gvdefaasst essd
//
LOCUS       WP_010844316             356 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphotransferase family protein [Gordonia terrae].
ACCESSION   WP_010844316
VERSION     WP_010844316.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..356
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=40023
     Region          40..296
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(45,48..50,53,64,66,98,117..120,219,221,223..224,226,
                     239..240,243,258..259,262)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(45,49,53,64,66,98,117..120,219,223..224,226,
                     239..240)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(48..50,219,221,224,240,243,258..259,262)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mtdevagage vrtedafdve vvakwleana sdpagldavp qvrqfgggas nltyllrypa
       61 rdlilrrapr gtkargahdm areyriqsel atairyiapm iafcdddsil gadfyvmgri
      121 dgviprtewp advpldveqa ralcsnfidt lvevhsvdps ttgladlgkg pgyvrrqvdg
      181 wttrfrnaht edvpdfeqtm vwlsenqpdd vatcvihndf kldnvvldkd dptrvigild
      241 wematlgdpl mdvagsmayw iqaddpdamq lmrrvpthlp gmisraefve kycermgfdm
      301 tperwrwyei fglfraavia qqiyyryyhg qtsnkaferl gyavgilaqr lddlll
//
LOCUS       WP_010844320             193 aa            linear   BCT 01-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Gordonia terrae].
ACCESSION   WP_010844320
VERSION     WP_010844320.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..193
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=21226
     Region          8..179
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(78,85,102..104,147,153,157)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mlispatide nilnwvvqnr sepwisiaev ltllgntvtm taltcvvvia lavthhrada
       61 vfvgagvlcg yavmqalkys fardrppved rllnidtfsy psghammtmv vfglfavaay
      121 rcstwvrshr wilaiapvls ilvgltriql avhwttdvis gwlfgaiwva lctwillrye
      181 arrgsgglvg drr
//
LOCUS       WP_010844333             148 aa            linear   BCT 01-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Gordonia terrae].
ACCESSION   WP_010844333
VERSION     WP_010844333.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..148
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=15508
     Region          9..147
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mtgdagtrvv htavvdepit ladheemvta aaegkagavv gfvgavrdhd ggrrvtalhy
       61 sghptatkvl advveevsav dgvravavsh rvgdlaigdi afvvavaadh rraafetcsr
      121 lvdevksrlp vwkhqffddg tdewvnsa
//
LOCUS       WP_010844351             364 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Gordonia].
ACCESSION   WP_010844351
VERSION     WP_010844351.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..364
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=38401
     Region          2..149
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
     Region          <180..>362
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
ORIGIN      
        1 milrriarpl lasafvasgv dairspkpia qsaepvvdka rsslppevag ripentetlv
       61 qinaaaqigg gillatgkfp rvasvvlagt lipttaagtd fwneadpvrk eaqrnafikn
      121 vgllggvlla avdtegkpsl awrgrqkasa vaaalpigaa agsstwehlv erthdgaeiv
      181 sersadaaak frehapeiae aaqkrslefa ekaadtasdv adrirdrapv ladaalvrss
      241 eladtalars sdlaetarkr gpklvkeaqk raekaqkqak kaqkqakkka pkiadsardr
      301 asdladtark rapefadvar drsaeladva rarsaelaet arqlaaaaed sadqgrkrlr
      361 karr
//
LOCUS       WP_010844433             204 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Gordonia].
ACCESSION   WP_010844433
VERSION     WP_010844433.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..204
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22221
     Region          15..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtsertyggr avsdraaerr qrfldaalve ftdtgyakss vtsicrvagl srrqfyaeft
       61 dreellvaly dtvqgaarva vaealaacas rdlrdlstaa mraymesvgt dprraavsfv
      121 qivgvssrve qhrldgreew adffvaamad fagrpaterq rhlaiafvga ltglvhrwse
      181 tadpaalddi vtvladilla farl
//
LOCUS       WP_010844405             708 aa            linear   BCT 01-JAN-2025
DEFINITION  cation:proton antiporter [Gordonia terrae].
ACCESSION   WP_010844405
VERSION     WP_010844405.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 708)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..708
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73565
     Region          5..409
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mekhtiafll ldvaiviaaa rvggmiarac rqpavvgeia agialgpsll gllpgnpdew
       61 lfpddvrpll galaqiglvl fmfivgleld mrltkgrera aasisafsia lpfglgaalg
      121 lllypshnmv ggmeierlgm vlfmgvamsi tafpvlaril tdrgmmrtvp gvfslaaaai
      181 ddilawtlla fiiaiiqggs plevakivgl tlvyaavmfg vvrpllakli vwrdaagrlt
      241 pdilavilig lflsaaatdv igihqifgaf vfgavmpkvg aeqlhreile rleqasvlll
      301 lpmffvvtgl nvdlteigla glgqlllvll vaiagkfvga yagarvsaip trqsaaiavl
      361 mntrgltelv ilaagrelgv lsdelfamlv vmalvttilt epllrvvypd kvvandiaaa
      421 erralatata prvlvlirdp vgtvadlrar hrrmldcatg fdvvlagmlt apdrsarple
      481 vgipvvpdfa aiasavekln elgssltgag svsvlcrfsa dpavdldams enanadiivv
      541 dsadlslggs lrsapvavid etadaavaps rstvtcvaad srsgrtavlm aaglalfgsr
      601 sltivasgsr rrwladlnav aeqgvsisiq dprrhrdesv sftvaaades gqgapvpvtv
      661 vdntgtsees lgdrvadlyr stpaaqptpa raapdtsspn igssserp
//
LOCUS       WP_010844511             407 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Gordonia].
ACCESSION   WP_010844511
VERSION     WP_010844511.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..407
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43891
     Region          16..399
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msinlelpkk lnvtvdqahq aaaeifrpis rkydlrehdy pveldtlasl ydglsetgqa
       61 gagadggrsq qkkekpksdg avvnggnmqs vvnvietswg dvglmlsipy qglgnsaiaa
      121 vatdeqlerf gkvwaamait epgfgsdsaa vsttatldgd eyvingekiy vtagsrathi
      181 vvwatvdksa graaiksfvv prthpgvtve rlehklgikv sdtaairfen cripkenllg
      241 spevdtkkgf ggvmqtfdnt rplvagmavg vtraaleelr rildeagiev dydrpaadqh
      301 aaaaeflrme adfeaaylht mraawmadnk qpnsteasms kakagrtatd vtnkvveltg
      361 tlgyserllv ekwardskil difegtqqiq nliiarrvln kssaelk
//
LOCUS       WP_010844550             179 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Gordonia].
ACCESSION   WP_010844550
VERSION     WP_010844550.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..179
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19644
     Region          9..179
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mqslidesps gadllerara gdqaafttlv eqhrdrlwai clritgnqhd aedamqdalv
       61 aawraignfr gdaqlstwly rigsnaalar irkrtdaddi adhdpmshld vaaqvvvsdr
      121 iaealsqvpd ayratfvlrv ygelsyseia eaqgiglqtv rsrisrarsi lselladlr
//
LOCUS       WP_010844577             675 aa            linear   BCT 01-JAN-2025
DEFINITION  CocE/NonD family hydrolase [Gordonia terrae].
ACCESSION   WP_010844577
VERSION     WP_010844577.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 675)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 675)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..675
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=73389
     Region          56..668
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mtyqldptqs rarvvpstrt rtsgaphfgt lplgdptgga dgirwreqvd gkqlyprvvi
       61 drnvsitmsd gvvlratvir panrfgqtil tpypavvnin pynraaidfi dqtlhapvlg
      121 kalhtasrsi datgtalegl ttltktlsgg vfdvfginrn lvrsgyvqvv vdvrgtgasl
      181 gkwqilgpre qqdsvevidw vteqewcdgs vgmagwsysa inslqaadkr paalqavfav
      241 egcddlvrdi yitggmpsaf ipvwlsavnm lkwvpnpanv irdlvrgdav rwaidrvksp
      301 ateipsllwg fltgrdprif ddpyfddrdp vvdrieaptf tvgawhdlfg rsatgvyerl
      361 qmepgrkqmi vgdgyhldvg sgyggqfapp rldvlerawf drwlkghrng ieyygpvtml
      421 qqggawtagq sfprpgvapt rlyltaesss tadhsvhdgs lsttpaqgvs slhvrpdsrg
      481 lrsrdmtqvt agatlvlgad yakdaryqer galsfttepv leatpisgam nlrlnvatta
      541 heaiwavtvn dvapdgtsvv ltngalsasn raldqsksty addgsllsah hylshkrklp
      601 vpadepirld vdlvptdavl qpghrlrvdv yaaslprylt lvpdlikarg rrhqrlvldp
      661 dhpshltlla gdglr
//
LOCUS       WP_010844585             213 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Gordonia].
ACCESSION   WP_010844585
VERSION     WP_010844585.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22626
     Region          19..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstssqpaag drtvvnsddp ravrtreklv dafariagsg pvtvaaltea agvhrsvfyk
       61 hfespddlav ymlrdlfaal sdadgvmrgr favdgleasr samtelvrfl garrsvyapl
      121 lgphapagag rqiaaafedl taaaitrmtt rpaevdtavl arflargvlg vierwlddaq
      181 prmsqaqvig qlvlcfpawl tagtnetpsk egr
//
LOCUS       WP_010844606             277 aa            linear   BCT 01-JAN-2025
DEFINITION  aldo/keto reductase [Gordonia terrae].
ACCESSION   WP_010844606
VERSION     WP_010844606.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..277
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30648
     Region          10..270
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mtvptitlnn gitipqlgfg vfqippedtr eatltalevg yrhidtaemy gnekgvgeav
       61 rdsgiprddi fitsklnngf hdhddalkal dgtladlgie qidlflihwp lpevgdyvqt
      121 wkalekayad gkaraigvsn fhqahlqrlf deadivpavn qievhpylsq nplrafnseh
      181 giateawspi aqgkvtddpv iteiaqakgr spaqvtlrwh iqrgdivfpk svtrarveen
      241 falfdfelsd aevaqidrln sddrigpdpd tfnyvpe
//
LOCUS       WP_010844620             176 aa            linear   BCT 01-JAN-2025
DEFINITION  PH domain-containing protein [Gordonia terrae].
ACCESSION   WP_010844620
VERSION     WP_010844620.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..176
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18849
     Region          26..168
                     /region_name="YdbS"
                     /note="Uncharacterized membrane protein YdbS, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3402"
                     /db_xref="CDD:442629"
ORIGIN      
        1 mdpssdpplp ahsevhptlr epanrvdpra ktlwrigplv lgalgvvaav vvavvvdear
       61 waavlvaili avlaviytav vpvwryrfhr wevsddavys qsgwfvrhrv iipiariqvv
      121 dteagpfeqf lglatltvtt assagtihia gldaevarat aadltirtqa ftddat
//
LOCUS       WP_010844742             556 aa            linear   BCT 01-JAN-2025
DEFINITION  (2,3-dihydroxybenzoyl)adenylate synthase [Gordonia terrae].
ACCESSION   WP_010844742
VERSION     WP_010844742.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..556
                     /product="(2,3-dihydroxybenzoyl)adenylate synthase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0008668 -
                     2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
                     [Evidence IEA]"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58779
     Region          12..551
                     /region_name="EntE"
                     /note="2,3-dihydroxybenzoate-AMP synthase component of
                     non-ribosomal peptide synthetase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1021"
                     /db_xref="CDD:440644"
ORIGIN      
        1 mpthldhvpd lldgftpyad aqaqkyrdag vfldrplfaa ldlaaerspd vpavtdastd
       61 gprtltyaef raatlrraag fvdaglqpaq rvvlqlnnsl dfavtlfgll ragvvpvmtl
      121 pahriteiah laagagavay igedgrrgfd frelaaelqs rvpevaqvfi sgdpgrfaal
      181 pdadpatvgl padpdpglpa lflvsggttg lpkliarthd dydlnarlsa dvagltaddt
      241 ylvalpaahn fplccpgilg vfgvgghvvf adnpspdntf dlierhrvtv talvpalaql
      301 wcaatewepa dvsslrllqv ggaklaqpda valdealgdv vqqvfgmaeg licytrpgep
      361 rdlvhqvqgs pmseldevrv vdedgadvpd gvegellvrg pytirgyyra aahneksftp
      421 dgfyrsgdkv trlpsghvav tgrikdtivr agenvaaddv eenllahdsv rqvavvglpd
      481 dalgekicaa vvlshehppa qplelatirt fltgrglasf klpdvirvvt tlpvtavgki
      541 dkkvlretll agppap
//
LOCUS       WP_010844704             254 aa            linear   BCT 01-JAN-2025
DEFINITION  MerR family transcriptional regulator [Gordonia terrae].
ACCESSION   WP_010844704
VERSION     WP_010844704.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..254
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28620
     Region          18..108
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(54,57,61..62,71,83,87,93,97,100..101)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          135..250
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mdareltvgv vagmvgvsir tlhhydqigl vepsgrtpag yrvyddtdve rlhqvltyre
       61 lgfsleqiat llddpdadpl shlqtqrell tdridrllrm vaaleemmsa knegislsas
      121 eqaeifgddw lgdeyaaeae erwgnteawt qsqkrsaqys kddwqrikde tddlerrlae
      181 amrrgvtpgn aeanslaeeh raqigrfydc dhdmqvclad myvadprfte hydaqapgla
      241 vylreviran agra
//
LOCUS       WP_010844748             324 aa            linear   BCT 01-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Gordonia terrae].
ACCESSION   WP_010844748
VERSION     WP_010844748.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..324
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34484
     Region          54..320
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mtsrlrlgal vasallfagl lagcsssdde aaggtvqlnl pdgrqvtipd tperivtlgd
       61 qwtdvvlsfg etpvgyydys ksatgemqpw ygekladatf idptkgddat tiakldpdli
      121 fapgfasdsp efqqisklap tvnaisdqei dpwqdmvtvm gtvlhdpdka ksiiddtnak
      181 iaavteeypg lkgktyafaf mygpdqlsvl gdendgaakl ftslgmkmap klvaeyrrtg
      241 qprfglsten ipmldadvlv vatatpeqae tlkslpgykn lkavkdnavt fmtqsqitgl
      301 naptpnsipy vldllkpsfa aass
//
LOCUS       WP_010844785             422 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Gordonia terrae].
ACCESSION   WP_010844785
VERSION     WP_010844785.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..422
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43524
     Region          16..409
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(26..27,30..31,34,66,121..122,124..126,129,149,
                     152..153,156,231,234..235,238..240,243,270,274,336..337,
                     341,345,361,364..365,368..369,372)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 marlladttp lrnqyfrrlw lanivtviga qlsvvavpaq iyevtgssay vgltgvfglv
       61 plvvfglwgg aladvvdrrt lliittigli vcsalfwaqa amggqnvwiv lvlfavqqaf
      121 favnqptrta vlprlldagd lpaalslnmt vmqagaiagp lvggslipvl gysllyfvdt
      181 lfllptlrav amlpslrpes daapkvaglr svleglryla ghkillasfl vdliamifgm
      241 pralfpqmah enfggpeggg iafallftai sagavvggif sgwvarverq glavivciii
      301 wglaitgtgi avsfadgtam pmlvvavvll miggaadmas aafrqtilla aatdevrgrl
      361 qgvfivvvag gpriadvahg aaaasigvaa atafggvavv iativaalmi pafvhyragq
      421 rt
//
LOCUS       WP_010844817             233 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Gordonia].
ACCESSION   WP_010844817
VERSION     WP_010844817.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..233
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25795
     Region          12..186
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(15,17,94)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(42,93..94)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            92..94
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 madpttnadv wlvvpvfneg qvirevatka retfpnivcv ddgssdnsad eiraagvhlv
       61 rhpvnlgqga aiqtgveyar rrpgarffvt fdadgqhqvd dvsamierlr repvdiivgt
      121 rfadgrsesv pllrrmalrt ivflsprtrr lglsdahngl rafnktvadq ldllmsgmsh
      181 asefialidh hrwrvaeqpv tilytdysra kgqslingvn ivadglfhtr mrk
//
LOCUS       WP_010844859             516 aa            linear   BCT 01-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA carboxylase subunit beta [Gordonia].
ACCESSION   WP_010844859
VERSION     WP_010844859.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..516
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55561
     Region          4..511
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtdttagkla dlrqkleaar epggekalak raakgicspr erlsmlfdpg tfveigalak
       61 mpgaaesgyg dgvvtghglv hgrpvaafsh dqsvfggtvg emfgrkvasl mewagkigcp
      121 mvgindsaga riqdavtsla wyaemgrrnd llsglapqvs vilgkcagga vytpantdil
      181 vavedksymf vtgpdvlkqv ngeeisaedl gsahnqarwg nihhvatdek aafdwvreyl
      241 qympssayer ppvinpglep eitesdlsln dfmpdndnag ydmhdiiikl fddgafhevg
      301 elfapniitg yarvdgrsvg vvanqpsvms gvldtdssek atrfvricna fsiplvflvd
      361 tpgilpglae eqkgtirrsg rflyayvead vpkvtvvlrk ayggayavmg skhlgadvnf
      421 awptakiavm gaesaaavlt rrqteglsaa eadkirrefi dfyntmmatp ylaaergyvd
      481 aviepaetrl qlrkalaqlr dkevlktprk hflmpi
//
LOCUS       WP_010844880             143 aa            linear   BCT 01-JAN-2025
DEFINITION  STAS domain-containing protein [Gordonia terrae].
ACCESSION   WP_010844880
VERSION     WP_010844880.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..143
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14395
     Region          30..122
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(41,43..45,51,74,76..78,80..82,85..86,107,111..112,
                     114)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            77
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mqaehpdavi vdesglsagr almtvvsaah eqlviltveg sidvltapql seavsealsg
       61 qpdgliidlt tteflasagm aalvaaheai aprgmfgvva agpattrplt vmgldqtmvl
      121 yptlddavta mtttegladr pag
//
LOCUS       WP_010844891             353 aa            linear   BCT 01-JAN-2025
DEFINITION  MlaD family protein [Gordonia terrae].
ACCESSION   WP_010844891
VERSION     WP_010844891.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..353
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=37155
     Region          13..238
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mltermrqhl ipiativtla vviaavginy atadddtrpl caefsdasgl yegnsvamlg
       61 kkvgrvvgih eegqrgvrvd mridktvplp advgatlvst sivterqief thpyrggehy
      121 esakciplnk trtplgisqt ldaistlsde lvkdggrntd ailqaltlvs knmegtqgdi
      181 sgilkdsatl indptrrdgq irrivanlat ltgvatensa evtqlfdnfv gaievivafg
      241 qtfgaateya gtfvpilsrl asdfgppifa igdaavplla qvgkqenila tvaartadli
      301 vkhpdaksil rafavsvplq tlrtacaspp vngvcrtgne vatianligg qsq
//
LOCUS       WP_010844948             115 aa            linear   BCT 01-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Gordonia terrae].
ACCESSION   WP_010844948
VERSION     WP_010844948.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..115
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12845
     Region          22..107
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mlrkhrhrpp qsaksilqqi sqvvhnpdrd rfelwvagdl vgvlgystet vdgqttitvl
       61 htvlydeysg hglatrltrt vvhhareqga rlrpvctftk ryldshpgiv tlapv
//
LOCUS       WP_010845053             156 aa            linear   BCT 01-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Xenorhabdus
            nematophila].
ACCESSION   WP_010845053
VERSION     WP_010845053.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus nematophila
  ORGANISM  Xenorhabdus nematophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Xenorhabdus nematophila"
                     /db_xref="taxon:628"
     Protein         1..156
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17695
     Region          1..140
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mldkidrkll ellqqdcsss lnslaeavnl tstpcwkrlk rledegyivg kvalingekl
       61 glgltaivmi ktqqhnsewy eqfvtfikkm pevltfyrma geydylmhve vvdmksydrf
      121 yksmvngvpg lidvtsnfam ekikyttalp ipdsva
//
LOCUS       WP_010845270             501 aa            linear   BCT 01-JAN-2025
DEFINITION  MFS transporter [Xenorhabdus nematophila].
ACCESSION   WP_010845270
VERSION     WP_010845270.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus nematophila
  ORGANISM  Xenorhabdus nematophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERE